|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5232 |
| Enzyme 1 Name |
Cytosolic 5'-nucleotidase 1B |
| Enzyme 1 Synonyms |
- Cytosolic 5'-nucleotidase IB
- cN1B
- cN-IB
- Autoimmune infertility-related protein
|
| Enzyme 1 Gene Name |
NT5C1B |
| Enzyme 1 Protein Sequence |
>Cytosolic 5'-nucleotidase 1B
MSQTSLKQKKNEPGMRSSKESLEAEKRKESDKTGVRLSNQMRRAVNPNHSLRCCPFQGHS
SCRRCLCAAEGTALGPCHTIRIYIHMCLLWEQGQQITMMRGSQESSLRKTDSRGYLVRSQ
WSRISRSPSTKAPSIDEPRSRNTSAKLPSSSTSSRTPSTSPSLHDSSPPPLSGQPSLQPP
ASPQLPRSLDSRPPTPPEPDPGSRRSTKMQENPEAWAQGIVREIRQTRDSQPLEYSRTSP
TEWKSSSQRRGIYPASTQLDRNSLSEQQQQQREDEDDYEAAYWASMRSFYEKNPSCSRPW
PPKPKNAITIALSSCALFNMVDGRKIYEQEGLEKYMEYQLTNENVILTPGPAFRFVKALQ
YVNARLRDLYPDEQDLFDIVLMTNNHAQVGVRLINSVNHYGLLIDRFCLTGGKDPIGYLK
AYLTNLYIAADSEKVQEAIQEGIASATMFDGAKDMAYCDTQLRVAFDGDAVLFSDESEHF
TKEHGLDKFFQYDTLCESKPLAQGPLKGFLEDLGRLQKKFYAKNERLLCPIRTYLVTARS
AASSGARVLKTLRRWGLEIDEALFLAGAPKSPILVKIRPHIFFDDHMFHIEGAQRLGSIA
AYGFNKKFSS
|
| Enzyme 1 Number of Residues |
610 |
| Enzyme 1 Molecular Weight |
68804 |
| Enzyme 1 Theoretical pI |
9.03 |
| Enzyme 1 GO Classification |
| Function |
- 5'-nucleotidase activity
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- magnesium ion binding
- metal ion binding
- nucleotidase activity
- nucleotide binding
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 1 General Function |
Not Available |
| Enzyme 1 Specific Function |
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Helps to regulate adenosine levels |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
13774961  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q96P26  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
5NT1B_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1699 bp
GGGCAAAAATGTGGATAACAACAAAAGAATTTCAACAGGTAAAAAAATGAGTCAAACATC
TCTCAAACAGAAAAAGAATGAGCCCGGAATGAGGTCCTCAAAAGAGAGTCTAGAAGCAGA
AAAAAGAAAGGAATCTGACAAAACAGGAGTTCGTCTGAGCAATCAGGGATCACAAGAATC
ATCACTGCGGAAGACAGACTCTCGAGGGTACCTTGTGCGCAGTCAATGGTCTAGAATATC
CCGGAGCCCATCCACCAAGGCTCCATCCATAGATGAGCCTAGAAGCAGGAACACCAGTGC
TAAGCTCCCCAGCAGCTCCACGAGCTCCCGGACTCCATCCACCTCCCCAAGCCTGCATGA
CTCCTCACCGCCGCCGCTGTCCGGGCAGCCCTCGCTCCAGCCACCCGCGTCGCCCCAGCT
GCCCCGGTCGCTGGACTCGCGGCCTCCCACGCCCCCAGAGCCCGATCCTGGCTCCCGGCG
CAGCACCAAAATGCAAGAAAATCCGGAGGCCTGGGCCCAAGGCATCGTGCGGGAAATCCG
CCAGACCCGGGACTCGCAGCCGCTGGAATATTCGCGCACGTCCCCCACCGAGTGGAAGTC
CTCCAGCCAGCGCAGGGGGATCTACCCCGCCTCCACCCAGCTGGACCGCAACTCTCTGTC
CGAGCAGCAGCAGCAGCAGCGGGAGGACGAAGACGACTACGAAGCTGCCTACTGGGCATC
CATGAAGTCGTTCTACGAAAAGAACCCGAGCTGCTGGCGCCCCTGGCCGCCCAAACCCAA
GAACGCCATCACCATTGCTCTCTCATCCTGCGCGCTCTTCAACATGGTGGACGGCAGGAA
AATCTACGAGCAAGAGGGTCTGGAAAAGTACATGGAGTATCAGCTCACCAATGAGAACGT
CATCCTGACCCCGGGCCCGGCGTTCCGTTTCGTCAAGGCACTACAGTATGTCAATGCTAG
ACTCCGTGATCTATATCCTGATGAACAGGACTTATTTGATATTGTACTGATGACTAATAA
CCATGCCCAAGTGGGAGTGCGGCTTATAAACAGCGTCAATCACTACGGCTTACTGATTGA
CCGCTTCTGTCTGACCGGGGGAAAAGACCCCATTGGCTATTTGAAGGCATATCTTACCAA
CTTGTATATTGCTGCAGATTCTGAAAAAGTGCAAGAGGCAATACAAGAAGGTATTGCCTC
TGCGACAATGTTTGATGGAGCCAAAGACATGGCTTACTGTGACACTCAGCTCCGTGTAGC
CTTTGATGGGGATGCTGTCCTCTTCTCTGATGAGTCTGAACATTTTACCAAGGAGCATGG
GCTGGACAAATTCTTCCAGTATGATACATTATGTGAAAGTAAGCCTCTTGCTCAGGGTCC
CCTAAAAGGCTTTCTGGAAGATTTAGGCAGACTGCAAAAGAAGTTCTATGCCAAAAATGA
ACGGTTACTTTGTCCTATCAGGACCTACCTGGTTACAGCTAGGAGTGCAGCCAGTTCAGG
CGCCCGTGTGCTGAAAACCTTCCGACGCTGGGGTCTAGAGATAGACGAAGCTCTTTTCCT
TGCTGGAGCCCCCAAAAGTCCCATCTTGGTGAAGATCCGGCCCCACATCTTCTTTGATGA
CCACATGTTCCACATTGAAGGGGCACAGAGGTTAGGTTCCATCGCAGCTTATGGCTTTAA
TAAAAAATTCAGTAGTTAG
|
| Enzyme 1 GenBank Gene ID |
AF356185  |
| Enzyme 1 GeneCard ID |
NT5C1B  |
| Enzyme 1 GenAtlas ID |
NT5C1B  |
| Enzyme 1 HGNC ID |
HGNC:17818  |
| Enzyme 1 Chromosome Location |
2 |
| Enzyme 1 Locus |
2p24.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Sala-Newby GB, Newby AC: Cloning of a mouse cytosolic 5'-nucleotidase-I identifies a new gene related to human autoimmune infertility-related protein. Biochim Biophys Acta. 2001 Oct 31;1521(1-3):12-8. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5233 |
| Enzyme 2 Name |
Cytosolic 5'-nucleotidase 1A |
| Enzyme 2 Synonyms |
- Cytosolic 5'-nucleotidase IA
- cN1A
- cN-IA
- cN-I
|
| Enzyme 2 Gene Name |
NT5C1A |
| Enzyme 2 Protein Sequence |
>Cytosolic 5'-nucleotidase 1A
MEPGQPREPQEPREPGPGAETAAAPVWEEAKIFYDNLAPKKKPKSPKPQNAVTIAVSSRA
LFRMDEEQQIYTEQGVEEYVRYQLEHENEPFSPGPAFPFVKALEAVNRRLRELYPDSEDV
FDIVLMTNNHAQVGVRLINSINHYDLFIERFCMTGGNSPICYLKAYHTNLYLSADAEKVR
EAIDEGIAAATIFSPSRDVVVSQSQLRVAFDGDAVLFSDESERIVKAHGLDRFFEHEKAH
ENKPLAQGPLKGFLEALGRLQKKFYSKGLRLECPIRTYLVTARSAASSGARALKTLRSWG
LETDEALFLAGAPKGPLLEKIRPHIFFDDQMFHVAGAQEMGTVAAHVPYGVAQTPRRTAP
AKQAPSAQ
|
| Enzyme 2 Number of Residues |
368 |
| Enzyme 2 Molecular Weight |
41021 |
| Enzyme 2 Theoretical pI |
6.52 |
| Enzyme 2 GO Classification |
| Function |
- 5'-nucleotidase activity
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- magnesium ion binding
- metal ion binding
- nucleotidase activity
- nucleotide binding
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides and has a broad substrate specificity. Helps to regulate adenosine levels in heart during ischemia and hypoxia |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
12659324  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q9BXI3  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
5NT1A_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1107 bp
ATGGAACCTGGGCAGCCCCGGGAGCCCCAGGAGCCCCGCGAGCCCGGGCCAGGAGCGGAG
ACCGCTGCGGCCCCGGTCTGGGAGGAAGCCAAGATTTTCTACGACAACCTCGCGCCCAAG
AAGAAACCCAAATCGCCCAAGCCTCAGAATGCAGTCACCATCGCTGTGTCCTCCCGAGCC
TTGTTTCGCATGGACGAGGAGCAGCAGATCTACACGGAGCAGGGCGTGGAGGAGTACGTG
CGCTACCAGCTGGAACATGAGAACGAACCCTTCAGTCCCGGGCCAGCCTTCCCTTTTGTG
AAGGCTCTGGAGGCCGTGAACAGGCGGCTGCGGGAGCTGTACCCTGATAGTGAGGACGTC
TTCGACATCGTCCTCATGACTAACAACCATGCTCAAGTGGGTGTCCGCCTCATCAACAGT
ATCAACCACTATGACCTGTTCATCGAGAGGTTCTGCATGACAGGTGGGAACAGCCCGATC
TGCTACCTCAAGGCCTATCACACCAACCTCTACTTGTCAGCCGATGCGGAAAAAGTGCGA
GAAGCCATTGATGAGGGGATCGCAGCTGCCACCATCTTCAGCCCCAGCAGGGATGTGGTT
GTGTCCCAGAGTCAGCTGCGCGTGGCCTTCGATGGGGACGCCGTGCTCTTCTCGGACGAG
TCGGAGCGCATCGTCAAGGCCCACGGGCTGGACCGATTCTTCGAGCATGAGAAGGCCCAC
GAGAACAAGCCTCTGGCTCAGGGCCCCTTAAAGGGCTTTCTGGAGGCACTGGGTAGGTTG
CAGAAGAAGTTCTACTCCAAAGGCCTGCGGCTGGAGTGCCCAATTCGTACCTACTTGGTG
ACAGCACGCAGTGCAGCCAGTTCCGGGGCCCGGGCTCTCAAGACCCTGCGCAGCTGGGGC
CTGGAGACAGATGAAGCCTTGTTCCTTGCTGGAGCGCCCAAGGGCCCTCTCCTTGAGAAG
ATCCGCCCACACATCTTCTTTGATGACCAGATGTTCCATGTGGCTGGGGCTCAGGAGATG
GGCACTGTGGCCGCCCATGTGCCTTATGGTGTGGCACAGACACCCCGGCGGACTGCACCT
GCAAAGCAGGCCCCATCTGCACAGTAG
|
| Enzyme 2 GenBank Gene ID |
AF331801  |
| Enzyme 2 GeneCard ID |
NT5C1A  |
| Enzyme 2 GenAtlas ID |
NT5C1A  |
| Enzyme 2 HGNC ID |
HGNC:17819  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1p34.3-p33 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Hunsucker SA, Spychala J, Mitchell BS: Human cytosolic 5'-nucleotidase I: characterization and role in nucleoside analog resistance. J Biol Chem. 2001 Mar 30;276(13):10498-504. Epub 2000 Dec 22. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5234 |
| Enzyme 3 Name |
5'(3')-deoxyribonucleotidase, cytosolic type |
| Enzyme 3 Synonyms |
- Cytosolic 5',3'-pyrimidine nucleotidase
- Deoxy-5'-nucleotidase 1
- dNT-1
|
| Enzyme 3 Gene Name |
NT5C |
| Enzyme 3 Protein Sequence |
>5'(3')-deoxyribonucleotidase, cytosolic type
MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADK
VASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHL
GPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFTCCHNRHLVLPPTRRRL
LSWSDNWREILDSKRGAAQRE
|
| Enzyme 3 Number of Residues |
201 |
| Enzyme 3 Molecular Weight |
23383 |
| Enzyme 3 Theoretical pI |
6.63 |
| Enzyme 3 GO Classification |
Not Available |
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 Specific Function |
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
7524492  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q8TCD5  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
NT5C_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>606 bp
ATGGCGCGGAGCGTGCGCGTGCTGGTGGACATGGACGGCGTCCTGGCCGACTTCGAGGCC
GGCCTCCTGCGGGGCTTCCGCCGCCGCTTCCCTGAGGAGCCGCACGTGCCGCTGGAGCAA
CGCCGCGGCTTCCTGGCCCGCGAGCAGTACCGCGCCCTGCGGCCCGACCTGGCGGATAAA
GTGGCCAGTGTGTACGAAGCCCCGGGCTTTTTCCTGGACCTGGAGCCCATCCCGGGAGCC
TTGGACGCTGTGCGGGAGATGAACGACCTACCGGACACGCAGGTCTTCATCTGCACCAGC
CCCCTGCTGAAGTACCACCACTGTGTGGGTGAGAAGTACCGCTGGGTGGAGCAGCACCTG
GGGCCCCAGTTCGTAGAACGAATTATCCTGACAAGGGACAAGACGGTGGTCTTGGGGGAC
CTGCTCATTGATGACAAGGACACAGTTCGAGGCCAGGAGGAGACCCCAAGCTGGGAGCAC
ATCTTGTTCACCTGCTGCCACAATCGGCACCTGGTCCTGCCCCCGACAAGGAGACGGCTG
CTCTCCTGGAGTGACAACTGGAGGGAGATCTTAGATAGCAAGCGCGGAGCTGCGCAGCGG
GAATGA
|
| Enzyme 3 GenBank Gene ID |
AF154829  |
| Enzyme 3 GeneCard ID |
NT5C  |
| Enzyme 3 GenAtlas ID |
NT5C  |
| Enzyme 3 HGNC ID |
HGNC:17144  |
| Enzyme 3 Chromosome Location |
17 |
| Enzyme 3 Locus |
17q25.1 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Rampazzo C, Johansson M, Gallinaro L, Ferraro P, Hellman U, Karlsson A, Reichard P, Bianchi V: Mammalian 5'(3')-deoxyribonucleotidase, cDNA cloning, and overexpression of the enzyme in Escherichia coli and mammalian cells. J Biol Chem. 2000 Feb 25;275(8):5409-15. [PubMed
]
- Rampazzo C, Kost-Alimova M, Ruzzenente B, Dumanski JP, Bianchi V: Mouse cytosolic and mitochondrial deoxyribonucleotidases: cDNA cloning of the mitochondrial enzyme, gene structures, chromosomal mapping and comparison with the human orthologs. Gene. 2002 Jul 10;294(1-2):109-17. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5236 |
| Enzyme 4 Name |
5'(3')-deoxyribonucleotidase, mitochondrial precursor |
| Enzyme 4 Synonyms |
- 5',3'-nucleotidase, mitochondrial
- Deoxy-5'-nucleotidase 2
- dNT-2
|
| Enzyme 4 Gene Name |
NT5M |
| Enzyme 4 Protein Sequence |
>5'(3')-deoxyribonucleotidase, mitochondrial precursor
MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRAR
FPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMAS
LQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDI
TGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC
|
| Enzyme 4 Number of Residues |
228 |
| Enzyme 4 Molecular Weight |
25862 |
| Enzyme 4 Theoretical pI |
8.12 |
| Enzyme 4 GO Classification |
Not Available |
| Enzyme 4 General Function |
Not Available |
| Enzyme 4 Specific Function |
Dephosphorylates specifically the 5' and 2'(3')- phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
Not Available |
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
9408106  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q9NPB1  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
NT5M_HUMAN  |
| Enzyme 4 PDB ID |
1Q92  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>687 bp
ATGATCCGGCTGGGCGGCTGGTGTGCGCGGCGGCTCTGCAGCGCGGCGGTTCCCGCGGGG
CGGCGCGGGGCGGCGGGCGGGCTGGGCCTGGCGGGAGGCCGCGCCCTACGGGTGCTGGTG
GACATGGACGGCGTGCTGGCTGACTTCGAGGGCGGATTCCTCAGGAAGTTCCGCGCGCGC
TTTCCCGACCAGCCCTTCATCGCGCTGGAGGACCGGCGCGGCTTCTGGGTGTCGGAGCAG
TACGGCCGCCTGCGGCCAGGGCTGAGCGAGAAGGCCATCAGCATTTGGGAGTCAAAGAAT
TTCTTTTTTGAACTTGAGCCTCTGCCAGGGGCCGTGGAAGCTGTCAAGGAGATGGCCAGC
CTACAAAACACTGACGTCTTCATCTGCACAAGCCCCATCAAGATGTTCAAGTACTGTCCC
TATGAGAAGTATGCCTGGGTGGAGAAGTACTTTGGCCCTGACTTTCTGGAGCAGATTGTG
CTGACCAGAGACAAGACCGTGGTCTCTGCTGACCTTCTCATAGACGACCGGCCGGACATC
ACAGGGGCCGAGCCAACCCCCAGCTGGGAGCATGTCCTCTTCACCGCCTGCCACAACCAG
CACCTGCAGCTGCAGCCCCCCCGCCGCAGGCTGCACTCGTGGGCGGACGACTGGAAGGCC
ATTCTGGACAGCAAGCGGCCCTGCTGA
|
| Enzyme 4 GenBank Gene ID |
AJ277557  |
| Enzyme 4 GeneCard ID |
NT5M  |
| Enzyme 4 GenAtlas ID |
NT5M  |
| Enzyme 4 HGNC ID |
HGNC:15769  |
| Enzyme 4 Chromosome Location |
17 |
| Enzyme 4 Locus |
17p11.2 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Rampazzo C, Gallinaro L, Milanesi E, Frigimelica E, Reichard P, Bianchi V: A deoxyribonucleotidase in mitochondria: involvement in regulation of dNTP pools and possible link to genetic disease. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8239-44. [PubMed
]
- Rinaldo-Matthis A, Rampazzo C, Reichard P, Bianchi V, Nordlund P: Crystal structure of a human mitochondrial deoxyribonucleotidase. Nat Struct Biol. 2002 Oct;9(10):779-87. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5239 |
| Enzyme 5 Name |
ATP-citrate synthase |
| Enzyme 5 Synonyms |
- ATP-citrate
- pro-S--lyase
- Citrate cleavage enzyme
|
| Enzyme 5 Gene Name |
ACLY |
| Enzyme 5 Protein Sequence |
>ATP-citrate synthase
MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPD
QLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFY
VCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEI
LASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPP
PFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNE
LANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRA
IRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALG
HRPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVP
SPRSLQGKSTTLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQK
FYWGHKEILIPVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEG
IPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYV
SRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIG
GTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALK
EAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASF
MTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADH
GPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFV
NKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPN
LILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQKRLK
QGLYRHPWDDISYVLPEHMSM
|
| Enzyme 5 Number of Residues |
1101 |
| Enzyme 5 Molecular Weight |
120841 |
| Enzyme 5 Theoretical pI |
7.34 |
| Enzyme 5 GO Classification |
| Function |
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Energy production and conversion |
| Enzyme 5 Specific Function |
ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
28935  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P53396  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
ACLY_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>3318 bp
ATGTCGGCCAAGGCAATTTCAGAGCAGACGGGCAAAGAACTCCTTTACAAGTTCATCTGT
ACCACCTCAGCCATCCAGAATCGGTTCAAGTATGCTCGGGTCACTCCTGACACAGACTGG
GCCCGCTTGCTGCAGGACCACCCCTGGCTGCTCAGCCAGAACTTGGTAGTCAAGCCAGAC
CAGCTGATCAAACGTCGTGGAAAACTTGGTCTCGTTGGGGTCGACCTCACTCTGGATGGG
GTCAAGTCCTGGCTGAAGCCACGGCTGGGACAGGAAGCCACAGTTGGCAAGGCCACAGGC
TTCCTCAAGAACTTTCTGATCGAGCCCTTCGCCCCCCACAGTCAGGCTGAGGAGTTCTAT
GTCTGCATCTATGCCACCCGAGAAGGGGACTACGTCCTGTTCCACCACGAGGGGGGTGTG
GACGTGGGTGATGTGGACGCCAAGGCCCAGAAGCTGCTTGTTGGCGTGGATGAGAAACTG
AATCCTGAGGACATCAAAAAACACCTGTTGGTCCACGCCCCTGACGACAAGAAAGAAATT
CTGGCCAGTTTTATCTCCGGCCTCTTCAATTTCTACGAGGACTTGTACTTCACCTACCTC
GAGATCAATCCCCTTGTAGTGACCAAAGATGGAGTCTATGTCCTTGACTTGGCGGCCAAG
GTGGACGCCACTGCCGACTACATCTGCAAAGTGAAGTGGGGTGACATCGAGTTCCCTCCC
CCCTTCGGGCGGGTGGCATATCCAGAGGAAGCCTACATTGCAGACCTCGATGCCAAAAGT
GGGGCAAGCCTGAAGCTGACCTTGCTGAACCCCAAAGGGAGGATCTGGACCATGGTGGCC
GGGGGTGGCGCCTCTGTCGTGTACAGCGATACCATCTGTGATCTAGGGGGTGTCAACGAG
CTGGCAAACTATGGGGAGTACTCAGGCGCCCCCAGCGAGCAGCAGACCTATGACTATGCC
AAGACTATCCTCTCCCTCATGACCCGAGAGAAGCACCCAGATGGCAAGATCCTCATCATT
GGAGGCAGCATCGCAAACTTCACCAACGTGGCTGCCACGTTCAAGGGCATCGTGAGAGCA
ATTCGAGATTACCAGGGCCCCCTGAAGGAGCACGAAGTCACAATCTTTGTCCGAAGAGGT
GGCCCCAACTATCAGGAGGGCTTACGGGTGATGGGAGAAGTCGGGAAGACCACTGGGATC
CCCATCCATGTCTTTGGCACAGAGACTCACATGACGGCCATTGTGGGCATGGCCTGGGCA
CCGGCCATCCCCAACCAGCCACCCACAGCGGCCCACACTGCAAACTTTCTCCTCAACGCC
CAGCGGGAGACATCGACTCCAGCCCCCAGCAGGACAGCATCTTTTTATGAGTCCATGGTC
GATGAGGTCAGGGCCGATGAGGTGGCGCCTGCAAAGAAGGCCAAGCCTGCCATGCCACAA
GATTCAGTCCCAAGTCCAAGATCCCTGCAAGGAAAGAGCACCACCCTCTTCAGCCGCCAC
ACCAAGGCCATTGTGTGGGGCATGCAGACCCGGGCCGTGCAAGGCATGCTGGACTTTGAC
TATGTCTGCTCCCGAGACGAGCCCTCAGTGGCTGCCATGGTCTATCCTTTCACTGGGGAC
CACAAGCAGAAGTTTTACTGGGGGCACAAAGAGATCCTGATCCCTGTCTTCAAGAACATG
GCTGATGCCATGAGGAAGCACCCGGAGGTAGATGTGCTCATCAACTTTGCCTCTCTCCGC
TCTGCCTATGACAGCACCATGGAGACCATGAACTATGCCCAGATCCGGACCATCGCCATC
ATAGCTGAAGGCATCCCTGAGGCCCTCACGAGAAAGCTGATCAAGAAGGCGGACCAGAAG
GGAGTGACCATCATCGGACCTGCCACTGTTGGAGGCATCAAGCCTGGGTGCTTTAAGATT
GGCAACACAGGTGGGATGCTGGACAACATCCTGGCCTCCAAACTGTACCCCCAGGCAGCT
GTGGCCTATGTCTCACGTTCCGGAGGCATGTCCAACGAGCTCAACAATATCATCTCTCGG
ACCACGGATGGCGTCTATGAGGGCGTGGCCATTGGTGGGGACAGGTACCCGGGCTCCACA
TTCATGGATCATGTGTTACGCTATCAGGACACTCCAGGAGTCAAAATGATTGTGGTTCTT
GGAGAGATTGGGGGCACTGAGGAATATAAGATTTCCCGGGGCATCAAGGAGGGCCGCCTC
ACTAAGCCCATCGTCTGCTGGTGCATCGGGACGTGTGCCACCATGTTCTCCTCTGAGGTC
CAGTTTGGCCATGCTGGAGCTTGTGCCAACCAGGCTTCTGAAACTGCAGTAGCCAAGAAC
CAGGCTTTGAAGGAAGCAGGAGTGTTTGTGCCCCGGAGCTTTGATGAGCTTGGAGAGATC
ATCCAGTCTGTATACGAAGATCTCGTGGCCAATGGAGTCATTGTACCTGCCCAGGAGGTG
CCGCCCCCAACCGTGCCCATGGACTACTCCTGGGCCAGGGAGCTTGGTTTGATCCGCAAA
CCTGCCTCGTTCATGACCAGCATCTGCGATGAGCGAGGACAGGAGCTCATCTACGCGGGC
ATGCCCATCACTGAGGTCTTCAAGGAAGAGATGGGCATTGGCGGGGCCCTCGGCCTCCTC
TGGTTCCAGAAAAGGTTGCCTAAGTACTCTTGCCAGTTCATTGAGATGTGTCTGATGGTG
ACAGCTGATCACGGGCCAGCCGTCTCTGGAGCCCACAACACCATCATTTGTGCGCGCACC
GCGGTGGAGCTGGTCTCCAGCCTCACCTCGGGGCTGCTCACCATCGGGGATCGGTTTGGG
GGTGCCTTGGATGCAGCAGCCAAGATGTTCAGTAAAGCCTTTGACAGTGGCATTATCCCC
ATGGAGTTTGTGAACAAGATGAAGAAGGAAGGGAAGCTGATCATGGGCATTGGTCACCGA
GTGAAGTCGATAAACAACCCAGACATGCGAGTGCAGATCCTCAAAGATTACGTCAGGCAG
CACTTCCCTGCCACTCCTCTGCTCGATTATGCACTGGAAGTAGAGAAGATTACCACCTCG
AAGAAGCCAAATCTTATCCTGAATGTAGATGGTCTCATCGGAGTCGCATTTGTAGACATG
CTTAGAAACTGTGGGTCCTTTACTCGGGAGGAAGCTGATGAATATATTGACATTGGAGCC
CTCAATGGCATCTTTGTGCTGGGAAGGAGTATGGGGTTCATTGGACACTATCTTGATCAG
AAGAGGCTGAAGCAGGGGCTGTATCGTCATCCGTGGGATGATATTTCATATGTTCTTCCG
GAACACATGAGCATGTAA
|
| Enzyme 5 GenBank Gene ID |
X64330  |
| Enzyme 5 GeneCard ID |
ACLY  |
| Enzyme 5 GenAtlas ID |
ACLY  |
| Enzyme 5 HGNC ID |
HGNC:115  |
| Enzyme 5 Chromosome Location |
17 |
| Enzyme 5 Locus |
17q12-q21 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Elshourbagy NA, Near JC, Kmetz PJ, Wells TN, Groot PH, Saxty BA, Hughes SA, Franklin M, Gloger IS: Cloning and expression of a human ATP-citrate lyase cDNA. Eur J Biochem. 1992 Mar 1;204(2):491-9. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5247 |
| Enzyme 6 Name |
Acetyl-CoA carboxylase 2 |
| Enzyme 6 Synonyms |
- ACC-beta[Includes: Biotin carboxylase
|
| Enzyme 6 Gene Name |
ACACB |
| Enzyme 6 Protein Sequence |
>Acetyl-CoA carboxylase 2
MVLLLCLSCLIFSCLTFSWLKIWGKMTDSKPITKSKSEANLIPSQEPFPASDNSGETPQR
NGEGHTLPKTPSQAEPASHKGPKDAGRRRNSLPPSHQKPPRNPLSSSDAAPSPELQANGT
GTQGLEATDTNGLSSSARPQGQQAGSPSKEDKKQANIKRQLMTNFILGSFDDYSSDEDSV
AGSSRESTRKGSRASLGALSLEAYLTTGEAETRVPTMRPSMSGLHLVKRGREHKKLDLHR
DFTVASPAEFVTRFGGDRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVT
PEDLKANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAKRIPVQAVWAGWGHASENPKL
PELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTVEWTEDDLQQGK
RISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQV
QSEIPGSPIFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAP
LAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNL
PAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPISFETPSNPPLARGHVIAARITSENPDE
GFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVA
LKELSIRGDFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDIMLGVVCGAL
NVADAMFRTCMTDFLHSLERGQVLPADSLLNLVDVELIYGGVKYILKVARQSLTMFVLIM
NGCHIEIDAHRLNDGGLLLSYNGNSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSP
SAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRPGAVLEAGCVVAR
LELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLPEPVFSIK
LKEWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKSVRRVMAQYASNITSVLCQFP
SQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSGIRGYMKTVVLDLLRRYLRV
EHHFQQAHYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGPDPSLSD
ELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGHQFCP
ENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRQLPDGTCV
VEFQFMLPSSHPNRMTVPISITNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEDFTR
NFDEVISCFANVPKDTPLFSEARTSLYSEDDCKSLREEPIHILNVSIQCADHLEDEALVP
ILRTFVQSKKNILVDYGLRRITFLIAQEKEFPKFFTFRARDEFAEDRIYRHLEPALAFQL
ELNRMRNFDLTAVPCANHKMHLYLGAAKVKEGVEVTDHRFFIRAIIRHSDLITKEASFEY
LQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPFKIEESVRYMVMRYGS
RLWKLRVLQAEVKINIRQTTTGSAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSF
GNKQGPQHGMLINTPYVTKDLLQAKRFQAQTLGTTYIYDFPEMFRQALFKLWGSPDKYPK
DILTYTELVLDSQGQLVEMNRLPGGNEVGMVAFKMRFKTQEYPEGRDVIVIGNDITFRIG
SFGPGEDLLYLRASEMARAEGIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGFK
YLYLTPQDYTRISSLNSVHCKHIEEGGESRYMITDIIGKDDGLGVENLRGSGMIAGESSL
AYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVENSHIILTGASALNKVLGREVYTSNNQL
GGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDPIDREIEFLPSR
APYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVE
TRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQAIKDFNREKLPLMIFANWRGF
SGGMKDMYDQVLKFGAYIVDGLRQYKQPILIYIPPYAELRGGSWVVIDATINPLCIEMYA
DKESRGGVLEPEGTVEIKFRKKDLIKSMRRIDPAYKKLMEQLGEPDLSDKDRKDLEGRLK
AREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARTFLYWRLRRLLLEDQVK
QEILQASGELSHVHIQSMLRRWFVETEGAVKAYLWDNNQVVVQWLEQHWQAGDGPRSTIR
ENITYLKHDSVLKTIRGLVEENPEVAVDCVIYLSQHISPAERAQVVHLLSTMDSPAST
|
| Enzyme 6 Number of Residues |
2458 |
| Enzyme 6 Molecular Weight |
276558 |
| Enzyme 6 Theoretical pI |
6.46 |
| Enzyme 6 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- ligase activity
- nucleotide binding
- purine nucleotide binding
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Lipid transport and metabolism |
| Enzyme 6 Specific Function |
ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions:biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
2138330  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
O00763  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
COA2_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>7452 bp
ATGGTCTTGCTTCTTTGTCTATCTTGTCTGATTTTCTCCTGTCTGACCTTTTCCTGGTTA
AAAATCTGGGAGAAAATGACGGACTCCAAGCCGATCACCAAGAGTAAATCAGAAGCAAAC
CTCATCCCGAGCCAGGAGCCCTTTCCAGCCTCTGATAACTCAGGGGAGACACCGCAGAGA
AATGGGGAGGGCCACACTCTGCACAAAGACACCCAGCCAGGCCGAGCCCAGCCTCCCACA
AAGGCCCAAAGATCCGGTCGGCGGAGAAACTCCCTACCACCCTCCCGCCAGAAGCCCCCA
AGAAACCCCCTTTCTTCCAGTGACGCAGCACCCTCCCCAGAGCTTCAAGCCAACGGGACT
GGGACACAAGGTCTGGAGGCCACAGATACCAATGGCCTGTCCTCCTCAGCCAGGCCCCAG
GGCAGCAAGCTGGTCCCCTCCAAAGAAGACAAGAAGCAGGCAAACATCAAGAGGCAGCTG
ATGACCAACTTCATCCTGGGCTCTTTTGATGACTACTCCTCCGACGAGGACTCTGTTGCT
GGCTCATCTCGTGAGTCTACCCGGAAGGGCAGCCGGGCCAGCTTGGGGGCCCTGTCCCTG
GAGGCTTATCTGACCACAGGTGAAGCTGAGACCCGCGTCCCCACTATGAGGCCGAGCATG
TCGGGACTCCACCTGGTGAAGAGGGGACGGGAACACAAGAAGCTGGACCTGCACAGAGAC
TTTACCGTGGCTTCTCCCGCTGAGTTTGTCACACGCTTTGGGGGGGATCGGGTCATCGAG
AAGGTGCTTATTGCCAACAACGGGATTGCCGCTGTGAAGTGCATGCGCTCCATCCGCAGG
TGGGCCTATGAGATGTTCCGCAACGAGCGGGCCATCCGGTTTGTTCGCATGGTGACCCCC
GAGGACCTTAAGGCCAACGCAGAGTACATCAAGATGGCGGATCATTACGGGCCCGCCCCA
GGAGGGCCCAATAACAACAACTATGCCAACGTGGAGCTGATTGTGGACATTGCCAAGAGA
ATCCCGTTGCAGGCGGTGTGGGCTGGCTGGGGCCATGCTTTAGAAAACCCTAAACTTCCG
GAGCTGCTGTGCAAGAATGGAGTTGCTTTCTTAGGCCCTCCCAGGTTGAGGCCAATGGTG
GGTCTAGGAGATAAGATCGCCTCCACCGTTGTCGCCCAGACGCTACAGGTCCCAACCCTG
CCCAGGAGTGGAAGCGCCCTGACAGTGGAGTGGACAGAAGATGATCTGCAGCAGGGAAAA
AGAATCAGTGTCCCAGAAGATGTTTATGACAAGGGTTGCGTGAAAGACGTAGATGAGGGC
TTGGAGGCAGCAGAAAGAATTGGTTTTCCATTGATGATCAAAGCTTCTGAAGGTGGCGGA
GGGAAGGGAATCCGGGAAACTGAGAGTGCGGAGGACTTCCCGATCCTTTTCAGACAAGTA
CAGAGTGAGATCCCAGGCTCGCCCATCTTTCTCATGAAGCTGGCCCAGCACGCCCGTCAC
CTGGAAGTTCAGATCCTCGCTGACCAGTATGGGAATGCTGTGTCTCTGTTTGGTCGCGAC
TGCTCCATCCAGCGGCGGCATCAGAAGATCGTTGAGGAAGCACCGGCCACCATCGCGCCG
CTGGCCATATTCGAGTTCATGGAGCAGTGTGCCATTCGCCTGGCCAAGACCGTGGGCTAT
GTGAGTGCAGGGACAGTGGAATACCTCTATAGTCAGGATGGTAGCTTCCACTTCTTGGAG
CTGAATCCTCGCTTGCAGGTGGAACATCCCTGCACAGAAATGATTGCTGACGTTAATCTG
CCGGCCGCCCAGCTACAGATCGCCATGGGTGCCCCACTGCACCGGCTGAAAGATATCCGG
CTTCTGTATGGAGAGTCACCCTGGGGAGACTCCCCAATTTCTTTTGAAAACTCAGCTCAT
CTCCCCTGCCCCCGAGGCCACGTCATTGCCACCAGAATCACCAGCGAAAACCCAGACGAG
GGTTTTAAGCCGAGCTCCGGGACTGTCCAGGAACTGAATTTCCGGAGCAGCAAGAACGTC
TGGGGTTACTTCACGGTGGCCGCTACTGGAGGCCTGCACGAGTTTGCGATTTCCCAGTTT
GGGCACTGCTTCTCCTGGGGAGAGAACCGGAAAGAGGCCATTTCGAACATGGTGGTGGCT
TTGAAGGAACTGTCCCTCCGAGGCGACTTTAGGACTACCGTGGAATACCTCATTAACCTC
CTGGAGACCGAGAGCTTCCAGAACAACTACATCGACACCGGGTGGTTGGACTACCTCATT
GCTGAGAAAGTGCAAAAGAAACCGAATATCATGCTTGGGGTGGTATGCGGGGCCCTTGAA
CGTGGAGATGCGATGTTCAGAACGTGCATGACAGATTTCTTACACTCCCTGGAAAGGGGC
CAGGTCCTCCCAGCGGATTCACTACTGAACCTCGTAGATGTGGAATTAATTTACGAGGGT
GTAAAGTACATTCTAAAGGTGACCCGGCAGTCTCTGACCATGTTCGTTCTCATCATGAAT
GGCTGCCACATCGAGATTGATGCCCACCGGCTGAATGATGGGGGGCTCCTGCTCTCCTAC
AATGGGAACAGCTACACCACCTACATGAAGGAAGAGGTTGACAGTTACCGTACCATCGGC
AATAAGACGTGTGTTTTTGAGAAGGAGAACGATCCTACAGTCCTGAGATCCCCCTCGGCT
GGGAAGCTGACACAGATCACAGTGGAGGATGGGGGCCACGTTGAGGCTGGGAGACGCTAC
GCTGAGATGGAGGTGATGAAGATGATCATGACCCTGAACGTTCAGGAAAGAGGCCGGGTG
AAGTACATCAAGCGTCCAGGTGCGGTGCTGGAAGCAGGCTGCGTGGTGGCCAGGCTGGAG
CTCGATGACCCTTCTAAAGTCCACCCGGCTGAACCGTTCACAGGAGAACTCCCTGCCCAG
CAGAACACTGCCGACCTCGGAAAGAAACTGCACAGGGTCTTCCACAGCGTCCTGGGAAGC
CTCACCAACGTCATGAGTGGCTTTTGTCTGCCAGAGCCGTTTTTTAGCATAAAGCTGAAG
GAGTGGGTGCAGAAGCTCATGATGACCCTCCGGCACCCGTCACTGCTGCTGGACGTGCAG
GAGATCATGACCAGTCGTGCAGGCCGCATCCCCCCCCCTGTTGAGAAGTCTGTCCGCAAG
GTGATGGCCCAGTATGCCAGCAACATCACCTCGGTGCTGTGCCAGTTCCCCAGCCAGCAG
ATAGCCACCATCCTGGACTGCCATGCAGCCACCCTGCAGCGGAAGGCTGATCGAGAGGTC
TTCTTCATCAACACCCAGAGCATGGTGCAGTTGGTCCAGAGGTACCGAAGTGGAATCCGC
GGTCATATGAAAACAGTGGTGATCGATCTCTTGAGAAGATACTTGCGTGTTGAGACCATT
TTCGGCAAGGCAAGAGATGCTGATGCCAACTCCAGTGGGATGGTGGGGGGCGTGAGGAGC
CTGAGCTTTACCTCTGTGTGGGTGGTTTTGTCTCCCCCAGCCCACTACGACAAGTGTGTG
ATAAACCTCAGGGAACAGTTCAAGCCAGACATGTCCCAGGTGCTGGACTGCATCTTCTCC
CACGCACAGGTGACCAAGAAGAACCAGCTGGTGATCATGTTGATCGATGAGCTGTGTGGC
CCAGACCCTTCCCTGTCGGACGAGCTGATCTCCATCCTCAACGAGCTCACTCAGCTGAGC
AAAAGCGAGCACTGCAAAGTGGCCCTCAGAGCCCGGCAGATCCTGATCGCCTCCCCCTCC
TACGAGCTGCGGCATAACCAGGTGGAGTCCATTTTCCTGTCTGCCATTGACATGTACGGC
CACCAGTTCTGCCCCGAGAACCTCCAGAAATTAATACTTTCGGAAACAACCATCTTCGAC
GTCCTGAATACTTTCTTCTATCACGCAAACAAAGTCGTGTGCATGGCGTCCTTGGAGGTT
TACGTGGGGGGGGCTTACATCGCCTATGTGTTAAACAGCCTGCAGCACCGGCAGCTCCCG
GACGGCACCTGCGTGGTAGAATTCCAGTTCATGCTGCCGTCCTCCCACCCAAACCGGATG
ACCGTGCCCATCAGCATCACCAACCCTGACCTGCTGAGGCACACGACAGAGCTCTTCATG
GACAGCGGCTTCTCCCCACTGTGCCAGCGCATGGGAGCCATGGTAGCCTTCAGGAGATTC
GAGGACTTCACCAGAAATTTTGATGAAGTCATCTCTTGCTTCGCCAACGTGCCGAAAGAC
CCCCCCCTCTTCAGCGAGGCCCGCACCTCCCTATACTCCGAGGATGACTGCAAGAGCCTC
AGAGAAGAGCCCATCCACATTCTGAATGTGTCCATCCAGTGTGCGGACCACCTGGAGGAT
GAGGCACTGGTGCCGATTTTACGTACATTCGTACAGTCCAAGAAAAATATCCTTGTGGAT
TATGGACTCCGACGAATCCCATTCTTGATTGCCCAAGAGAAAGAATTTCCCAAGTTTTTC
ACATTCAGAGCAAGAGATGAGTTTGCAGAAGATCGCATTTACCGTCACTTGGAACCTGCC
CTGGCTTTCCAGCTGGAACTCAACCGGATGCGTAACTTCGATCTGACCGCCGTGCCCTGT
GCCAACCACAAGATGCACCTTTACCTGGGTGCTGCCAAGGTGGAAGGAAGGTATGAAGTG
ACGGACCATAGGTTCTTCATCCGTGCCATCATCAGGCACTCTGACCTGATCACAAAGGAA
GCCTCCTTCGAATACCTGCAGAACGAGGGTGAGCGGCTGCTCCTGGAGGCCATGGACGAG
CTGGAGGTGGCGTTCAATAACACCAACGTGCGCACCGACTGCAACCACATCTTCCTCAAC
TTCGTGCCCACTGTCATCATGGACCCCAACAAGATCGAGGAGTCCGTGCGCTACATGGTT
ATGCGCTACGGCAGCCGGCTGTGGAAACTCCGTGTGCTACAGGCTGAGGTCAAGATCAAC
ATCCGCCAGACCACCACCGGCAGTGCCGTTCCCATCCGCCTGTTCATCACCAATGAGTCG
GGCTACTACCTGGACATCAGCCTCTACAAAGAAGTGACTGACTCCAGATCTGGAAATATC
ATGTTTCACTCCTTCGGCAACAAGCAAGGGCCCCAGCACGGGATGCTGATCAATACTCCC
TACGTCACCAAGGATCTGCTCCAGGCCAAGCGATTCCAGGCCCAGACCCTGGGAACCACC
TACATCTATGACTTCCCGGAAATGTTCAGGCAGGCTCTCTTTAAACTGTGGGGCTCCCCA
GACAAGTATCCCAAAGACATCCTGACATACACTGAATTAGTGTTGGACTCTCAGGGCCAG
CTGGTGGAGATGAACCGACTTCCTGGTGGAAATGAGGTGGGCATGGTGGCCTTCAAAATG
AGGTTTAAGACCCAGGAGTACCCGGAAGGACGGGATGTGATCGTCATCGGCAATGACATC
ACCTTTCGCATTGGATCCTTTGGCCCTGGAGAGGACCTTCTGTACCTGCGGGCATCCGAG
ATGGCCCGGGCAGAGGCGATTCCCAAAATTTACGTGGCAGCCAACAGTGGCGCCCGTATT
GGCATGGCAGAGGAGATCAAACACATGTTCCACGTGGCTTGGGTGGACCCAGAAGACCCC
CACAAAGGATTTAAATACCTGTACCTGACTCCCCAAGACTACACCAGAATCAGCTCCCTG
AACTCCGTCCACTGTAAACACATCGAGGAAGGAGGAGAGTCCAGATACATGATCACGGAT
ATCATCGGGAAGGATGATGGCTTGGGCGTGGAGAATCTGAGGGGCTCAGGCATGATTGCT
GGGGAGTCCTCTCTGGCTTACGAAGAGATCGTCACCATTAGCTTGGTGACCTGCCGAGCC
ATTGGGATTGGGGCCTACTTGGTGAGGCTGGGCCAGCGAGTGATCCAGGTGGAGAATTCC
CACATCATCCTCACAGGAGCAAGTGCTCTCAACAAGGTCCTGGGAAGAGAGGTCTACACA
TCCAACAACCAGCTGGGTGGCGTTCAGATCATGCATTACAATGGTGTCTCCCACATCACC
GTGCCAGATGACTTTGAGGGGGTTTATACCATCCTGGAGTGGCTGTCCTATATGCCAAAG
GATAATCACAGCCCTGTCCCTATCATCACACCCACTGACCCCATTGACAGAGAAATTGAA
TTCCTCCCATCCAGAGCTCCCTACGACCCCCGGTGGATGCTTGCAGGAAGGCCTCACCCA
ACTCTGAAGGGAACGTGGCAGAGCGGATTCTTTGACCACGGCAGTTTCAAGGAAATCATG
GCACCCTGGGCGCAGACCGTGGTGACAGGACGAGCAAGGCTTGGGGGGATTCCCGTGGGA
GTGATTGCTGTGGAGACACGGACTGTGGAGGTGGCAGTCCCTGCAGACCCTGCCAACCTG
GATTCTGAGGCCAAGATAATTCAGCAGGCAGGACAGGTGTGGTTCCCAGACTCAGCCTAC
AAAACCGCCCAGGCCATCAAGGACTTCAACCGGGAGAAGTTGCCCCTGATGATCTTTGCC
AACTGGAGGGGGTTCTCCGGTGGCATGAAAGACATGTATGACCAGGTGCTGAAGTTTGGA
GCCTACATCGTGGACGGCCTTAGACAATACAAACAGCCCATCCTGATCTATATCCGCCCT
ATGCGGGAGCTCCGGGGAGGCTCCTGGGTGGTCATAGATGCCACCATCAACCCGCTGTGC
ATAGAAATGTATGCAGACAAAGAGAGCAGGGGTGGTGTTCTGGAACCAGAGGGGACAGTG
GAGATTAAGTTCCGAAAGGAAGATCTGATAAAGTCCATGAGAAGGATCGATCCAGCTTAC
AAGAAGCTCATGGAACAGCTAGGGGAACCTGATCTCTCCGACAAGGACCGAAAGGACCTG
GAGGGCCGGCTAAAGGCTCGCGAGGACCTGCTGCTCCCCATCTACCACCAGGTGGCGGTG
CAGTTCGCCGACTTCCATGACACACCCGGCCGGATGCTGGAGAAGGGCGTCATATCTGAC
ATCCTGGAGTGGAAGACCGCACGCACCTTCCTGTATTGGCGTCTGCGCCGCCTCCTCCTG
GAGGACCAGGTCAAGCAGGAGATCCTGCAGGCCAGCGGGGAGCTGAGTCACGTGCATATC
CAGTCCATGCTGCGTCGCTGGTTCGTGGAGACGGAGGGGGCTGTCAAGGCCTACTTGTGG
GACAACAACCAGGTGGTTGTGCAGTGGCTGGAACAGCACTGGCAGGCAGGGGATGGCCCG
CGCTCCACCATCCGTGAGAACATCACGTACCTGAAGCACGACTCTGTCCTCAAGACCATC
CGAGGCCTGGTTGAAGAAAACCCCGAGGTGGCCGTGGACTGTGTGATATACCTGAGCCAG
CACATCAGCCCAGCTGAGCGGGCGCAGGTCGTTCACCTGCTGTCTACCATGGACAGCCCG
GCCTCCACCTGA
|
| Enzyme 6 GenBank Gene ID |
U89344  |
| Enzyme 6 GeneCard ID |
ACACB  |
| Enzyme 6 GenAtlas ID |
ACACB  |
| Enzyme 6 HGNC ID |
HGNC:85  |
| Enzyme 6 Chromosome Location |
12 |
| Enzyme 6 Locus |
12q24.11 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Abu-Elheiga L, Almarza-Ortega DB, Baldini A, Wakil SJ: Human acetyl-CoA carboxylase 2. Molecular cloning, characterization, chromosomal mapping, and evidence for two isoforms. J Biol Chem. 1997 Apr 18;272(16):10669-77. [PubMed
]
- Widmer J, Fassihi KS, Schlichter SC, Wheeler KS, Crute BE, King N, Nutile-McMenemy N, Noll WW, Daniel S, Ha J, Kim KH, Witters LA: Identification of a second human acetyl-CoA carboxylase gene. Biochem J. 1996 Jun 15;316 ( Pt 3):915-22. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5248 |
| Enzyme 7 Name |
Pyruvate carboxylase, mitochondrial precursor |
| Enzyme 7 Synonyms |
- Pyruvic carboxylase
- PCB
|
| Enzyme 7 Gene Name |
PC |
| Enzyme 7 Protein Sequence |
>Pyruvate carboxylase, mitochondrial precursor
MLKFRTVHGGLRLLGIRRTSTAPAASPNVRRLEYKPIKKVMVANRGEIAIRVFRACTELG
IRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVDAVHPGYGF
LSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEA
HEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIE
KPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPAAHLDPQLRTRLTSDSVKLAK
QVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRSLPDL
GLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISP
HYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQF
IDENPELFQLRPAQNRAQKLLHYLGHVMVNGPTTPIPVKASPSPTDPVVPAVPIGPPPAG
FRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFSK
LFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVF
KFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSL
QYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPDLPLHIHTHDTSGAGV
AAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEG
ARGLYAAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQM
LGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFP
EPFRSKVLKDLPRVEGRPGASLPPLDLQALEKELVDRHGEEVTPEDVLSAAMYPDVFAHF
KDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFEL
NGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVL
SAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE
|
| Enzyme 7 Number of Residues |
1178 |
| Enzyme 7 Molecular Weight |
129635 |
| Enzyme 7 Theoretical pI |
6.83 |
| Enzyme 7 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- biotin binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-carbon bonds
- nucleotide binding
- purine nucleotide binding
- pyruvate carboxylase activity
- vitamin binding
|
| Process |
- alcohol metabolism
- cellular metabolism
- gluconeogenesis
- glucose metabolism
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 7 General Function |
Not Available |
| Enzyme 7 Specific Function |
Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
Not Available |
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
458236  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P11498  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
PYC_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>3537 bp
ATGCTGAAGTTCCGAACAGTCCATGGGGGCCTGAGGCTCCTGGGAATCCGCCGAACCTCC
ACCGCCCCCGCTGCCTCCCCAAATGTCCGGCGCCTGGAGTATAAGCCCATCAAGAAAGTC
ATGGTGGCCAACAGAGGTGAGATTGCCATCCGTGTGTTCCGGGCCTGCACGGAGCTGGGC
ATCCGCACCGTAGCCATCTACTCTGAGCAGGACACGGGCCAGATGCACCGGCAGAAAGCA
GATGAAGCCTATCTCATCGGCCGCGGCCTGGCCCCCGTGCAGGCCTACCTGCACATCCCA
GACATCATCAAGGTGGCCAAGGAGAACAACGTAGATGCAGTGCACCCTGGCTACGGGTTC
CTCTCTGAGCGAGCGGACTTCGCCCAGGCCTGCCAGGATGCAGGGGTCCGGTTTATTGGG
CCAAGCCCAGAAGTGGTCCGCAAGATGGGAGACAAGGTGGAGGCCCGGGCCATCGCCATT
GCTGCGGGTGTTCCCGTTGTCCCTGGCACAGATGCCCCCATCACGTCCCTGCATGAGGCC
CACGAGTTCTCCAACACCTACGGCTTCCCCATCATCTTCAAGGCGGCCTATGGGGGTGGA
GGGCGTGGCATGAGGGTGGTGCACAGCTACGAGGAGCTGGAGGAGAATTACACCCGGGCC
TACTCAGAGGCTCTGGCCGCCTTTGGGAATGGGGCGCTGTTTGTGGAGAAGTTCATCGAG
AAGCCACGGCACATCGAGGTGCAGATCTTGGGGGACCAGTATGGGAACATCCTGCACCTG
TACGAGCGAGACTGCTCCATCCAGCGGCGGCACCAGAAGGTGGTCGAGATTGCCCCCGCC
GCCCACCTGGACCCGCAGCTTCGGACTCGGCTCACCAGCGACTCTGTGAAACTCGCTAAA
CAGGTGGGCTACGAGAACGCAGGCACCGTGGAGTTCCTGGTGGACAGGCACGGCAAGCAC
TACTTCATCGAGGTCAACTCCCGCCTGCAGGTGGAGCACACGGTCACAGAGGAGATCACC
GACGTAGACCTGGTCCATGCTCAGATCCACGTGGCTGAGGGCAGGAGCCTACCCGACCTG
GGCCTGCGGCAGGAGAACATCCGCATCAACGGGTGTGCCATCCAGTGCCGGGTCACCACC
GAGGACCCCGCGCGCAGCTTCCAGCCGGACACCGGCCGCATTGAGGTGTTCCGGAGCGGA
GAGGGCATGGGCATCCGCCTGGATAATGCTTCCGCCTTCCAAGGAGCCGTCATCTCGCCC
CACTACGACTCCCTGCTGGTCAAAGTCATTGCCCACGGCAAAGACCACCCCACGGCCGCC
ACCAAGATGAGCAGGGCCCTTGCGGAGTTCCGCGTCCGAGGTGTGAAGACCAACATCGCC
TTCCTGCAGAATGTGCTCAACAACCAGCAGTTCCTGGCAGGCACTGTGGACACCCAGTTC
ATCGACGAGAACCCAGAGCTGTTCCAGCTGCGGCCTGCACAGAACCGGGCCCAAAAGCTG
TTGCACTACCTCGGCCATGTCATGGTAAACGGTCCAACCACCCCGATTCCCGTCAAGGCC
AGCCCCAGCCCCACGGACCCCGTTGTCCCTGCAGTGCCCATAGGCCCGCCCCCGGCTGGT
TTCAGAGACATCCTGCTGCGAGAGGGGCCTGAGGGCTTTGCTCGAGCTGTGCGGAACCAC
CCGGGGCTGCTGCTGATGGACACGACCTTCAGGGACGCCCACCAGTCACTGCTGGCCACT
CGTGTGCGCACCCACGATCTCAAAAAGATCGCCCCCTATGTTGCCCACAACTTCAGCAAG
CTCTTCAGCATGGAGAACTGGGGAGGAGCCACGTTTGACGTCGCCATGCGCTTCCTGTAT
GAGTGCCCCTGGCGGCGGCTGCAGGAGCTCCGGGAGCTCATCCCCAACATCCCTTTCCAG
ATGCTGCTGCGGGGGGCCAATGCTGTGGGCTACACCAACTACCCAGACAACGTGGTCTTC
AAGTTCTGTGAAGTGGCCAAAGAGAATGGCATGGATGTCTTCCGTGTGTTTGACTCCCTC
AACTACTTGCCCAACATGCTGCTGGGCATGGAGGCGGCAGGAAGTGCCGGAGGCGTGGTG
GAGGCTGCCATCTCATACACGGGCGACGTGGCCGACCCCAGCCGCACCAAGTACTCACTG
CAGTACTACATGGGCTTGGCCGAAGAGCTGGTGCGAGCTGGCACCCACATCCTGTGCATC
AAGGACATGGCCGGGCTGCTGAAGCCCACGGCCTGCACCATGCTGGTCAGCTCCCTCCGG
GACCGCTTCCCCGACCTCCCACTGCACATCCACACCCACGACACGTCAGGGGCAGGCGTG
GCAGCCATGCTGGCCTGTGCCCAGGCTGGAGCTGATGTGGTGGATGTGGCAGCTGATTCC
ATGTCTGGGATGACTTCACAGCCCAGCATGGGGGCCCTGGTGGCCTGTACCAGAGGGACT
CCCCTGGACACAGAGGTGCCCATGGAGCGCGTGTTTGACTACAGTGAGTACTGGGAGGGG
GCTCGGGGACTGTACGCGGCCTTCGACTGCACGGCCACCATGAAGTCTGGCAACTCGGAC
GTGTATGAAAATGAGATCCCAGGGGGCCAGTACACCAACCTGCACTTCCAGGCCCACAGC
ATGGGGCTTGGCTCCAAGTTCAAGGAGGTCAAGAAGGCCTATGTGGAGGCCAACCAGATG
CTGGGCGATCTCATCAAGGTGACGCCCTCCTCCAAGATCGTGGGGGACCTGGCCCAGTTT
ATGGTGCAGAATGGATTGAGCCGGGCAGAGGCCGAAGCTCAGGCGGAAGAGCTGTCCTTT
CCCCGCTCCGTGGTGGAGTTCCTGCAGGGCTACATCGGTGTCCCCCATGGGGGGTTCCCC
GAACCCTTTCGCTCTAAGGTACTGAAGGACCTGCCAAGGGTGGAGGGGCGGCCTGGAGCC
TCCCTCCCTCCCCTGGATCTGCAGGCACTGGAGAAGGAGCTGGTAGACCGGCATGGGGAG
GAGGTGACGCCGGAAGATGTGCTCTCAGCAGCTATGTACCCCGATGTGTTTGCCCACTTC
AAGGACTTCACTGCCACCTTTGGCCCCCTGGATAGCCTGAATACTCGCCTCTTCCTGCAG
GGACCCAAGATCGCAGAGGAGTTTGAGGTGGAGCTGGAGCGGGGCAAGACGCTGCACATC
AAAGCCCTGGCCGTGAGCGACCTGAACCGGGCCGGCCAGAGGCAGGTCTTCTTTGAGCTC
AATGGGCAGCTGCGGTCCATCTTGGTCAAGGACACCCAGGCCATGAAGGAGATGCACTTC
CACCCCAAGGCCCTAAAGGACGTGAAGGGCCAGATCGGGGCGCCCATGCCTGGGAAGGTG
ATAGACATCAAAGTGGTGGCAGGGGCCAAGGTGGCCAAGGGCCAGCCCCTGTGTGTGCTC
AGTGCCATGAAGATGGAGACTGTGGTGACCTCACCCATGGAGGGTACTGTCCGCAAGGTT
CATGTGACCAAGGACATGACACTGGAAGGTGACGACCTCATCCTGGAGATCGAGTGA
|
| Enzyme 7 GenBank Gene ID |
U04641  |
| Enzyme 7 GeneCard ID |
PC  |
| Enzyme 7 GenAtlas ID |
PC  |
| Enzyme 7 HGNC ID |
HGNC:8636  |
| Enzyme 7 Chromosome Location |
Not Available |
| Enzyme 7 Locus |
Not Available |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Wexler ID, Du Y, Lisgaris MV, Mandal SK, Freytag SO, Yang BS, Liu TC, Kwon M, Patel MS, Kerr DS: Primary amino acid sequence and structure of human pyruvate carboxylase. Biochim Biophys Acta. 1994 Oct 21;1227(1-2):46-52. [PubMed
]
- MacKay N, Rigat B, Douglas C, Chen HS, Robinson BH: cDNA cloning of human kidney pyruvate carboxylase. Biochem Biophys Res Commun. 1994 Jul 29;202(2):1009-14. [PubMed
]
- Lamhonwah AM, Quan F, Gravel RA: Sequence homology around the biotin-binding site of human propionyl-CoA carboxylase and pyruvate carboxylase. Arch Biochem Biophys. 1987 May 1;254(2):631-6. [PubMed
]
- Freytag SO, Collier KJ: Molecular cloning of a cDNA for human pyruvate carboxylase. Structural relationship to other biotin-containing carboxylases and regulation of mRNA content in differentiating preadipocytes. J Biol Chem. 1984 Oct 25;259(20):12831-7. [PubMed
]
- Carbone MA, MacKay N, Ling M, Cole DE, Douglas C, Rigat B, Feigenbaum A, Clarke JT, Haworth JC, Greenberg CR, Seargeant L, Robinson BH: Amerindian pyruvate carboxylase deficiency is associated with two distinct missense mutations. Am J Hum Genet. 1998 Jun;62(6):1312-9. [PubMed
]
- Wexler ID, Kerr DS, Du Y, Kaung MM, Stephenson W, Lusk MM, Wappner RS, Higgins JJ: Molecular characterization of pyruvate carboxylase deficiency in two consanguineous families. Pediatr Res. 1998 May;43(5):579-84. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5276 |
| Enzyme 8 Name |
Acetyl-CoA carboxylase 1 |
| Enzyme 8 Synonyms |
- ACC-alpha[Includes: Biotin carboxylase
|
| Enzyme 8 Gene Name |
ACACA |
| Enzyme 8 Protein Sequence |
>Acetyl-CoA carboxylase 1
MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLDLLEEKEGSLSPASVGSDTLS
DLGISSLQDGLALHIRSSMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEK
VLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPG
GPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWAL
GDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQELYEKGYVKDVDDGLQA
AEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEV
QILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSA
GTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMMY
GVSPWGDSPIDFEDSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGY
FSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLET
ESFQMNRIDTGWLDRLIAEKVQAERPDTMLGVVCGALHVADVSLRNSVSNFLHSLERGQV
LPAHTLLNTVDVELIYEGVKYVLKVTRQSPNSYVVIMNGSCVEVDVHRLSDGGLLLSYDG
SSYTTYMKEEVDRYRITIGNKTCVFEKENDPSVMRSPSAGKLIQYIVEDGGHVFAGQCYA
EIEVMKMVMTLTAVESGCIHYVKRPGAALDPGCVLAKMQLDNPSKVQQAELHTGSLPRIQ
STALRGEKLHRVFHYVLDNLVNVMNGYCLPDPFFSSKVKDWVERLMKTLRDPSLPLLELQ
DIMTSVSGRIPPNVEKSIKKEMAQYASNITSVLCQFPSQQIANILDSHAATLNRKSEREV
FFMNTQSIVQLVQRYRSGIRGHMKAVVMDLLRQYLRVETQFQNGHYDKCVFALREENKSD
MNTVLNYIFSHAQVTKKNLLVTMLIDQLCGRDPTLTDELLNILTELTQLSKTTNAKVALR
ARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCIENLQKLILSETSIFDVLPNFFYH
SNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRM
SFSSNLNHYGMTHVASVSDVLLDNSFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFSDSP
PQSPTFPEAGHTSLYDEDKVPRDEPIHILNVAIKTDCDIEDDRLAAMFREFTQQNKATLV
DHGIRRLTFLVAQKDFRKQVNYEVDRRFHREFPKFFTFRARDKFEEDRIYRHLEPALAFQ
LELNRMRNFDLTAIPCANHKMHLYLGAAKVEVGTEVTDYRFFVRAIIRHSDLVTKEASFE
YLQNEGERLLLEAMDELEVAFNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYG
SRLWKLRVLQAELKINIRLTPTGKAIPIRLFLTNESGYYLDISLYKEVTDSRTAQIMFQA
YGDKQGPLHGMLINTPYVTKDLLQSKRFQAQSLGTTYIYDIPEMFRQSLIKLWESMSTQA
FLPSPPLPSDMLTYTELVLDDQGQLVHMNRLPGGNEIGMVAWKMTFKSPEYPEGRDIIVI
GNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVSANSGARIGLAEEIRHMFHVAWVD
PEDPYKGYRYLYLTPQDYKRVSALNSVHCEHVEDEGESRYKITDIIGKEEGIGPENLRGS
GMIAGESSLAYNEIITISLVTCRAIGIGAYLVRLGQRTIQVENSHLILTGAGALNKVLGR
EVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDPID
RIIEFVPTKTPYDPRWMLAGRPHPTQKGQWLSGFFDYGSFSEIMQPWAQTVVVGRARLGG
IPVGVVAVETRTVELSIPADPANLDSEAKIIQQAGQVWFPDSAFKTYQAIKDFNREGLPL
MVFANWRGFSGGMKDMYDQVLKFGAYIVDGLRECCQPVLVYIPPQAELRGGSWVVIDSSI
NPRHMEMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRRVDPVYIHLAERLGTPELSTAE
RKELENKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVISDILDWKTSRTFFYWRLR
RLLLEDLVKKKIHNANPELTDGQIQAMLRRWFVEVEGTVKAYVWDNNKDLAEWLEKQLTE
EDGVHSVIEENIKCISRDYVLKQIRSLVQANPEVAMDSIIHMTQHISPTQRAEVIRILST
MDSPST
|
| Enzyme 8 Number of Residues |
2346 |
| Enzyme 8 Molecular Weight |
265557 |
| Enzyme 8 Theoretical pI |
6.32 |
| Enzyme 8 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- biotin binding
- catalytic activity
- ligase activity
- nucleotide binding
- purine nucleotide binding
- vitamin binding
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Lipid transport and metabolism |
| Enzyme 8 Specific Function |
Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions:biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
849083  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q13085  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
COA1_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>7041 bp
ATGGATGAACCATCTCCCTTGGCCCAACCTCTGGAGCTGAACCAGCACTCTCGATTCATA
ATAGGTTCTGTGTCAGAAGATAACTCAGAGGATGAGATCAGCAACCTGGTGAAGCTGGAC
CTACTGGAGGAGAAGGAGGGCTCCTTGTCACCTGCTTCTGTTGGCTCAGATACACTCTCT
GATTTGGGGATCTCTGCCCTACAGGATGGCTTGGCCTTGCACATAAGGTCCAGCTGGTCT
GGCTTGCACCTAGTAAAGCAGGGCGGAGACAGAAAGAAAATAGATTCTCAACGAGATTTC
ACTGTGGCTTCTCCAGCAGAATTTGTTACTCGCTTTGGGGGAAATAAAGTGATTGAGAAG
GTTCTCATCGCTAACAATGGCATTGCAGCAGTGAAATGCATGCGGTCTATCCGTAGGTGG
TCTTATGAAATGTTTCGAAATGAACGTGCAATTAGATTCGTTGTCATGGTCACACCTGAA
GACCTTAAAGCCAATGCAGAATACATTAAGATGGCAGATCACTATGTGCCGGTGCCTGGA
GGAGCAAACAACAACAACTATGCAAATGTGGAATTAATTCTTGATATTGCTAAAAGGATC
CCAGTGCAAGCAGTGTGGGCTGGCTGGGGTCATGCTTCTGAGAATCCCAAACTACCGGAA
CTTCTCTTGAAAAATGGCATTGCCTTCATGGGTCCTCCAAACCAGGCCATGTGGGCTTTA
GGGGATAAGATTGCATCTTCCATAGTGGCTCAAACTGCAGGTATCCCAACTCTTCCCTGG
AGCGGCAGTGGTCTTCGTGTGGACTGGCAGGAAAATGATTTTTCAAAACGTATCTTAAAT
GTTCCCCAGGAGCTATATGAAAAAGGTTATGTGAAAGATGTGGATGATGGGCTAAAGGCA
GCTGAGAAGGTTGGATATCCAGTAATGATCAAGGCCTCAGAGGGAGGAGGAGGGAAGGGA
ATTAGAAAAGTTAACAATGCAGATGACTTCCCTAATCTCTTCAGACAGGTTCAAGCTGAA
GTTCCTGGATCTCCCATATTTGTGATGAGACTAGCCAAACAATCTCGTCATCTGGAGGTG
CAGATCTTAGCGGACCAATATGGCAATGCTATCTCTTTGTTTGGTCGTGATTGCTCTGTA
CAACGCAGGCATCAGAAGATTATTGAAGAAGCACCTGCTACTATTGCTACTCCAGCAGTA
TTTGAACACATGGAACAGTGTGCGGTGAAACTTGCCAAAATGGTGGGTTATGTGAGTGCT
GGGACTGTGGAATACCTGTACAGCCAGGATGGCAGCTTCTACTTTCTAGAATTGAACCCT
CGGCTACAGGTTGAACAACCTTGTACAGAGATGGTGGCTGATGTCAATCTCCCCGCAGCA
CAGCTCCAGATTGCCATGGGGATTCCTCTATATAGAATCAAGGATATCCGTATGATGTAT
GGGGTATCTCCTTGGGGTGATTCTCCCATTGATTTTGAAAATTCTGCTCACGTTCCTTGT
CCAAGGGGCCATGTTATTGCTGCTCGGATCACTAGTGAAAATCCAGATGAGGGTTTTAAG
CCCAGCTCAGGAACAGTTCAGGAGCTAAATTTCCGCAGCAATAAGAATGTTTGGGGATAT
TTCAGTGTTGCTGCTGCAGGGGGACTTCATGAATTTGCTGGTTCTCAGTTTGGTCACTGC
TTTTCTTGGGGAGAAAACAGAGAAGAAGCAATTTCAAACATGGTGGTGGCATTGAAGGAG
CTGTCTATTCGGGGTGACTTTCGAACTACAGTTGAATACCTGATCAAATTGTTAGAGACT
GAAAGCTTTCAAATGAACAGAATTGATACTGGCTGGCTGGACAGACTGATAGCAGAAAAA
GTACGGGCTGAGCGTCCTGACACCATGTTGGGGGTTGTGTGTGGTGCCCTCCACGTCGGA
GATGTGAGCCTGCGAAATAGCGTCTCTAACTTCCTTCACTCCTTAGAAAGGGGTCAAGTC
CTTCCGGCTCATACACTTCTGAATACAGTAGATGTTGAACTTATCTATGAGGGAGTCAAG
TATGTACTTAAGGTGACTCGACAGTCCCCCAACTCCTATGTGGTGATCATGAATGGCTCA
TGTGTAGAAGTAGATGTACATCGGCTGAGTGACGGTGGACTGCTCTTGTCCTATGATGGC
AGCAGTTACACCACGTATATGAAGGAGGAAGTAGACAGATATCGCATCACAATTGGCAAT
AAAACCTGTGTGTTTGAGAAGGAAAATGACCCATCGGTGATGCGCTCACCTTCTGCTGGG
AAGTTAATCCAGTACATTGTAGAAGATGGAGGTCATGTGTTTGCCGGCCAGTGCTATGCA
GAGATTGAGGTAATGAAGATGGTAATGACTTTGACAGCTGTGGAGTCTGGCTGTATCCAT
TACGTCAAGCGTCCTGGAGCAGCTCTTGACCCTGGCTGTGTACTCGCCAAAATGCAACTG
GACAACCCCAGCAAGGTTCAGCAGGCTGAACTTCACACAGGTAGTCTGCCACGGATCCAG
AGCACCGCTCTCCGAGGCGAGAAGCTCCATCGAGTGTTCCACTATGTCCTGGATAATCTG
GTCAATGTAATGAATGGATACTGCCTTCCAGATCCTTTCTTTAGCAGCAAGGTAAAAGAC
TGGGTAGAACGATTGATGAAAACCCTCAGAGATCCCTCCCTGCCTCTCCTAGAATTGCAA
GATATTATGACCAGTGTGTCTGGCCGCATTCCCCCCAATGTGGAGAAGTCTATCAAGAAG
GAAATGGCTCAGTATGCTAGCAACATCACATCAGTCCTCTGTCAGTTTCCCAGCCAGCAG
ATTGCAAACATCCTAGATAGCCATGCAGCTACATTGAACCGGAAATCTGAACGGGAAGTC
TTCTTTATGAATACTCAGAGCATTGTCCAGCTGGTACAGAGGTACCGAAGTGGCATCCGA
GGCCACATGAAGGCTGTGGTGATGGATCTGCTCCGGCAGTACCTGCGAGTAGAGACACAA
TTCCAGAATGGTCACTATGACAAATGTGTATTCGCCCTTCGAGAAGAGAATAAGAGTGAC
ATGAACACTGTACTGAACTACATCTTCTCTCACGCTCAAGTCACCAAGAAGAATCTTCTG
GTCACAATGCTTATTGATCAGTTGTGTGGCCGGGACCCTACTCTAACTGATGAGCTGCTG
AGTATTCTCACAGAGCTAACTCAACTCAGTAAGACCACCAATGCCAAAGTAGCACTTCGA
GCACGCCAGGTTCTTATTGCCTCCCATTTGCCATCATATGACGTTCGCCATAACCAAGTA
GAGTCTATCTTCCTATCAGCTATTGACATGTATGGACATCAATTTTGCATTGAGAACCTG
CAGAAACTCATCCTATCAGAAACATCTATTTTTGATGTCCTACCAAACTTCTTCTATCAC
AGCAACCAAGTAGTGAGGATGGCAGCTCTGGAGGTGTACGTTCGAAGGGCTTATATTGCC
TATGAACTTAACAGCGTACAACACCGCCAGCTTAAGGACAACACCTGCGTGGTGGAATTC
CAGTTCATGCTGCCCACATCTCATCCAAACAGAGGGAACATCCCTACGCTAAACAGAATG
TCCTTCTCCTCCAACCTCAACCACTATGGCATGACCCATGTAGCTAGTGTCAGCGATGTT
CTGTTGGACAACGCCTTCACACCACCTTGTCAACGCATGGGCGGAATGGTCTCTTTTCGG
ACTTTTGAAGATTTTGTCAGGATCTTTGATGAAGTAATGGGCTGCTTCTGTGACTCCCCA
CCCCAGAGTCCCACATTCCCTGAGGCAGGTCACACGTCTCTTTATGATGAGGATAAGGTT
CCCAGGGATGAACCAATTCACATTCTCAATGTGGCTATCAAGACTGACGGTGATATTGAG
GATGACAGGCTGGCAGCTATGTTCAGAGAATTCACCCAGCAAAATAAAGCTACCCTGGCT
GACCATGGGATCCGGCGCCTGACTTTCCTGGTTGCACAAAAGGATTTCAGAAAGCAGGTC
AACTATGAGGTGGATCGGAGATTTCATAGAGAATTCCCTAAATTTTTTACATTCCGAGCA
AGGGATAAGTTTGAGGAGGATCGTATCTATCGTCATCTGGAGCCTGCTCTGGCTTTCCAG
TTAGAGCTGAACCGGATGAGAAATTTTGACCTCACTGCCATTCCATGTGCTAATCACAAG
ATGCACCTGTATCTCGGGGCAGCCAAGGTGGAAGTGGGCACAGAAGTGACAGACTACAGG
TTCTTTGTTCGTGCAATCATCAGGCATTCTGATCTGGTCACCAAGGAAGCTTCTTTTGAA
TATCTGCAAAGTGAAGGGGAGCGGCTACTCCTGGAAGCCATGGATGAGTTGGAAGTTGCT
TTTAACAATACAAATGTCCGCACTGACTGTAACCACATCCTCCTCAACTTTGTGCCCACG
GTTATCATGGACCCATCAAAGATTGAGGAATCCGTGCGGAGCATGGTAATGCGGTATGGA
AGTCGCCTGTGGAAATTGCGCGTCCTCCAGGCAGAACTGAAAATCAACATTCGCCTGACG
CCAACTGGAAAAGCAATTCCCATCCGCCTTTTCCTGACAAACGAGTCTGGCTATTACTTG
GATATCAGCCTATACAAGGAAGTGACTGACTCCAGGACAGCACAGATCATGTTTCAGGCA
TATGGAGACAAGCAGGGACCACTGCATGGAATGTTAATCAATACTCCATATGTGACCAAA
GACCTGCTGCAATCAAAGAGGTTCCAGGCACAATCCTTAGGGACAACGTACATATATGAT
ATCCCAGAGATGTTTCGGCAGTCCCTGATCAAACTCTGGGAGTCTATGTCAACTCAAGCA
TTTCTTCCATCTCCCCCTCTGCCTTCTGACATGCTGACTTACACTGAACTGGTACTGGAT
GATCAAGGTCAGCTGGTCCACATGAACAGGCTTCCAGGAGGAAATGAGATTGGCATGGTA
GCTTGGAAAATGAGCCTTAAAAGTCCTGAATATCCAGAAGGCCGAGATGTTATTGTTATT
GGCAATGACATTACATACCGAATTGGGTCCTTTGGGCCTCAAGAAGATTTGTTATTTCTC
AGAGCTTCCGAACTTGCTAGGGCCGAAGGCATTCCACGCATCTATGTATCAGCCAACAGT
GGAGCAAGAATCGGACTGGCAGAAGAAATTCGCCATATGTTTCATGTGGCCTGGGTAGAT
TCTGAGGATCCTTACAAGGGATACAGGTATTTATATCTGACTCCTCAAGATTATAAGAGA
GTCGGTGCTCTCAACTCTGTCCATTGTGAACACGTGGAAGATGAAGGAGAATCCAGGTAC
AAGATAACAGATATTATTGGGAAAGAAGAGGGAATTGGACCCGAGAACCTTCGAGGTTCT
GGAATGATCGCTGGAGAATCCTCATTGGCCTATAATGAGATCATTACCATCAGCCTGGTG
ACGTCCCGGGCCATTGGGATTGGGGCTTACCTTGTCCGGCTGGGACAGAGAACCATCCAG
GTTGAGAATTCTCACTTGATTCTAACAGGAGCTGGAGCCCTCAACAAAGTCCTCGGGCGG
GAAGTGTACACCTCCAATAACCAGCTGGGGGGCATCCAGATTACGCACAACAATGGGGTG
ACCCACTGCACTGTGTGTGACGGCTTTGAAGGGGTTTTCACTGTCCTGCACTGGCTGTCT
TACATGCCCAAGAGCGTACACAGTTCAGTTCCTCTTCTGAACTCAAAGGATCCTATAGAC
AGAATCATCGAGTTTGTTCCCACAAAGACCCCATATGATCCTCGATGGATGCTAGCAGGC
CGCCCTCACCCAACCCAAAAAGGTCAGTGGTTGAGTGGCTTTTTTGACTATGGATCTTTC
TCAGAGATTATGCAGCCCTGGGCACAGACGGTGGTGGTTGGTAGAGCCAGGTTAGGGGGA
ATACCTGTGGGAGTTGTTGCTGTAGAAACCCGGACAGTAGAACTAAGTGTACCAGCTGAT
CCAGCAAACCTGGATTCTGAAGCCAAGATAATCCAGCACGCCGGCCAAGTTTGGTTTCCG
GATTCTGCGTTTAAGACGTATCAGGCCATCAAGGACTTCAACCGGGAAGGGCTACCTCTA
ATGGTCTTTGCCAACTGGAGAGGCTTCTCTGGTGGAATGAAAGATATGTATCACCAAGTG
CTGAAGTTTGGTGCTTACATTGTGGATGGCTTGCGGGAATGTTCCCAGCCTGTGCTGGTC
TACATTCCTCCCCAGGCTGAGCTGCGGGGTGGCTCCTGGGTGGTGATCGACCCAACCATC
AATCCTCGGCACATGGAGATGTATGCTGACCGAGAAAGCAGGGGATCTGTTCTGGAGCCA
GAAGGGACGGTAGAAATCAAATTCCGCAGAAAGGATCTGGTGAAAACCATGCGTCGGGTG
GACCCAGTCTACATCCACTTGGCTGAGCGATTGGGGACCCCAGAGCTGAGCCCAACTGAG
CGGAAGGAGTTGGAGAGCAAGTTGAAGGAGCGGGAGGAATTCCTAATTCCAATTTACCAT
CAGGTAGCCGTGCAGTTTGCTGACTTGCACGACACTCCAGGCCGGATGCAGGAGAAGGGT
GTTATTAGCGATATCCTGGATTGGAAAACATCCCGTACCTTCTTCTACTGGCGACTGAGG
CGTCTTCTGCTGGAGGACCTGGTCAAGAAGAAAATCCACAGTGCCAACCCTGAGCTGACT
GATGGCCAGATTCAAGCCATGTTAAGACGCTGGTTTGTGGAAGTGGAAGGAACAGTGAAG
GCTTATGTTTGGGACAATAATAAGGATCTGGCGGAGTGGCTAGAGAAACAGCTGACAGAG
GAGGATGGTGTTCACTCGGTAATAGAGGAAAACATCAAATGCATCAGCAGAGACTACGTC
CTCAAGCAAATCCGCAGCTTGGTCCAGGCCAATCCAGAGGTTGCCATGGATTCCATCATC
CATATGACGCAGCACATATCACCCACTCAGCGGGCAGAAGTCATAAGGATCCTTTCCACT
ATGGACTCCCCTTCTACGTAG
|
| Enzyme 8 GenBank Gene ID |
U19822  |
| Enzyme 8 GeneCard ID |
ACACA  |
| Enzyme 8 GenAtlas ID |
ACACA  |
| Enzyme 8 HGNC ID |
HGNC:84  |
| Enzyme 8 Chromosome Location |
17 |
| Enzyme 8 Locus |
17q21 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Abu-Elheiga L, Jayakumar A, Baldini A, Chirala SS, Wakil SJ: Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms. Proc Natl Acad Sci U S A. 1995 Apr 25;92(9):4011-5. [PubMed
]
- Mao J, Chirala SS, Wakil SJ: Human acetyl-CoA carboxylase 1 gene: presence of three promoters and heterogeneity at the 5'-untranslated mRNA region. Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7515-20. Epub 2003 Jun 16. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5313 |
| Enzyme 9 Name |
Ectonucleoside triphosphate diphosphohydrolase 1 |
| Enzyme 9 Synonyms |
- NTPDase 1
- Ecto-ATP diphosphohydrolase
- ATPDase
- Lymphoid cell activation antigen
- Ecto-apyrase
- CD39 antigen
|
| Enzyme 9 Gene Name |
ENTPD1 |
| Enzyme 9 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
|
| Enzyme 9 Number of Residues |
510 |
| Enzyme 9 Molecular Weight |
57965 |
| Enzyme 9 Theoretical pI |
6.29 |
| Enzyme 9 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 9 General Function |
Not Available |
| Enzyme 9 Specific Function |
In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation. Hydrolyzes ATP and ADP equally well |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- ATP + 2 H2O = AMP + 2 phosphate
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
765256  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P49961  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
ENTP1_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1533 bp
ATGGAAGATACAAAGGAGTCTAACGTGAAGACATTTTGCTCCAAGAATATCCTAGCCATC
CTTGGCTTCTCCTCTATCATAGCTGTGATAGCTTTGCTTGCTGTGGGGTTGACCCAGAAC
AAAGCATTGCCAGAAAACGTTAAGTATGGGATTGTGCTGGATGCGGGTTCTTCTCACACA
AGTTTATACATCTATAAGTGGCCAGCAGAAAAGGAGAATGACACAGGCGTGGTGCATCAA
GTAGAAGAATGCAGGGTTAAAGGTCCTGGAATCTCAAAATTTGTTCAGAAAGTAAATGAA
ATAGGCATTTACCTGACTGATTGCATGGAAAGAGCTAGGGAAGTGATTCCAAGGTCCCAG
CACCAAGAGACACCCGTTTACCTGGGAGCCACGGCAGGCATGCGGTTGCTCAGGATGGAA
AGTGAAGAGTTGGCAGACAGGGTTCTGGATGTGGTGGAGAGGAGCCTCAGCAACTACCCC
TTTGACTTCCAGGGTGCCAGGATCATTACTGGCCAAGAGGAAGGTGCCTATGGCTGGATT
ACTATCAACTATCTGCTGGGCAAATTCAGTCAGAAAACAAGGTGGTTCAGCATAGTCCCA
TATGAAACCAATAATCAGGAAACCTTTGGAGCTTTGGACCTTGGGGGAGCCTCTACACAA
GTCACTTTTGTACCCCAAAACCAGACTATCGAGTCCCCAGATAATGCTCTGCAATTTCGC
CTCTATGGCAAGGACTACAATGTCTACACACATAGCTTCTTGTGCTATGGGAAGGATCAG
GCACTCTGGCAGAAACTGGCCAAGGACATTCAGGTTGCAAGTAATGAAATTCTCAGGGAC
CCATGCTTTCATCCTGGATATAAGAAGGTAGTGAACGTAAGTGACCTTTACAAGACCCCC
TGCACCAAGAGATTTGAGATGACTCTTCCATTCCAGCAGTTTGAAATCCAGGGTATTGGA
AACTATCAACAATGCCATCAAAGCATCCTGGAGCTCTTCAACACCAGTTACTGCCCTTAC
TCCCAGTGTGCCTTCAATGGGATTTTCTTGCCACCACTCCAGGGGGATTTTGGGGCATTT
TCAGCTTTTTACTTTGTGATGAAGTTTTTAAACTTGACATCAGAGAAAGTCTCTCAGGAA
AAGGTGACTGAGATGATGAAAAAGTTCTGTGCTCAGCCTTGGGAGGAGATAAAAACATCT
TACGCTGGAGTAAAGGAGAAGTACCTGAGTGAATACTGCTTTTCTGGTACCTACATTCTC
TCCCTCCTTCTGCAAGGCTATCATTTCACAGCTGATTCCTGGGAGCACATCCATTTCATT
GGCAAGATCCAGGGCAGCGACGCCGGCTGGACTTTGGGCTACATGCTGAACCTGACCAAC
ATGATCCCAGCTGAGCAACCATTGTCCACACCTCTCTCCCACTCCACCTATGTCTTCCTC
ATGGTTCTATTCTCCCTGGTCCTTTTCACAGTGGCCATCATAGGCTTGCTTATCTTTCAC
AAGCCTTCATATTTCTGGAAAGATATGGTATAG
|
| Enzyme 9 GenBank Gene ID |
S73813  |
| Enzyme 9 GeneCard ID |
ENTPD1  |
| Enzyme 9 GenAtlas ID |
ENTPD1  |
| Enzyme 9 HGNC ID |
HGNC:3363  |
| Enzyme 9 Chromosome Location |
10 |
| Enzyme 9 Locus |
10q24 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed
]
- Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed
]
- Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [PubMed
]
- Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed
]
- Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed
]
- Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed
]
- Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed
]
- Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5314 |
| Enzyme 10 Name |
Soluble calcium-activated nucleotidase 1 |
| Enzyme 10 Synonyms |
- SCAN-1
- Apyrase homolog
- Putative NF-kappa-B-activating protein 107
- Putative MAPK-activating protein PM09
|
| Enzyme 10 Gene Name |
CANT1 |
| Enzyme 10 Protein Sequence |
>Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
|
| Enzyme 10 Number of Residues |
401 |
| Enzyme 10 Molecular Weight |
44840 |
| Enzyme 10 Theoretical pI |
5.98 |
| Enzyme 10 GO Classification |
Not Available |
| Enzyme 10 General Function |
Not Available |
| Enzyme 10 Specific Function |
Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- A nucleoside diphosphate + H2O = a nucleotide + phosphate
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
22218108  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q8WVQ1  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
CANT1_HUMAN  |
| Enzyme 10 PDB ID |
1S1D  |
| Enzyme 10 PDB File |
Show |
| Enzyme 10 3D Structure |
|
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1116 bp
ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA
|
| Enzyme 10 GenBank Gene ID |
AF328554  |
| Enzyme 10 GeneCard ID |
CANT1  |
| Enzyme 10 GenAtlas ID |
CANT1  |
| Enzyme 10 HGNC ID |
HGNC:19721  |
| Enzyme 10 Chromosome Location |
17 |
| Enzyme 10 Locus |
17q25.3 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [PubMed
]
- Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed
]
- Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5322 |
| Enzyme 11 Name |
Alkaline phosphatase, placental type precursor |
| Enzyme 11 Synonyms |
- PLAP-1
- Alkaline phosphatase Regan isozyme
|
| Enzyme 11 Gene Name |
ALPP |
| Enzyme 11 Protein Sequence |
>Alkaline phosphatase, placental type precursor
MLGPCMLLLLLLLGLRLQLSLGIIPVEEENPDFWNREAAEALGAAKKLQPAQTAAKNLII
FLGDGMGVSTVTAARILKGQKKDKLGPEIPLAMDRFPYVALSKTYNVDKHVPDSGATATA
YLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAG
TYAHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFRMGTPDPEYP
DDYSQGGTRLDGKNLVQEWLAKRQGARYVWNRTELMQASLDPSVTHLMGLFEPGDMKYEI
HRDSTLDPSLMEMTEAALRLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAI
ERAGQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPG
YVLKDGARPDVTESESGSPEYRQQSAVPLDEETHAGEDVAVFARGPQAHLVHGVQEQTFI
AHVMAFAACLEPYTACDLAPPAGTTDAAHPGRSVVPALLPLLAGTLLLLETATAP
|
| Enzyme 11 Number of Residues |
535 |
| Enzyme 11 Molecular Weight |
57954 |
| Enzyme 11 Theoretical pI |
6.24 |
| Enzyme 11 GO Classification |
| Function |
| — |
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 11 General Function |
Inorganic ion transport and metabolism |
| Enzyme 11 Specific Function |
A phosphate monoester + H(2)O = an alcohol + phosphate |
| Enzyme 11 Pathways |
- Folate and Pterine Biosynthesis (map00790
)
- gamma-Hexachlorocyclohexane Degradation (map00361
)
|
| Enzyme 11 Reactions |
- A phosphate monoester + H2O = an alcohol + phosphate
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
178474  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
P05187  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
PPB1_HUMAN  |
| Enzyme 11 PDB ID |
1EW2  |
| Enzyme 11 PDB File |
Show |
| Enzyme 11 3D Structure |
|
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1608 bp
ATGCTGGGGCCCTGCATGCTGCTGCTGCTGCTGCTGCTGGGCCTGAGGCTACAGCTCTCC
CTGGGCATCATCCCAGTTGAGGAGGAGAACCCGGACTTCTGGAACCGCGAGGCAGCCGAG
GCCCTGGGTGCCGCCAAGAAGCTGCAGCCTGCACAGACAGCCGCCAAGAACCTCATCATC
TTCCTGGGCGATGGGATGGGGGTGTCTACGGTGACAGCTGCCAGGATCCTAAAAGGGCAG
AAGAAGGACAAACTGGGGCCTGAGATACCCCTGGCCATGGACCGCTTCCCATATGTGGCT
CTGTCCAAGACATACAATGTAGACAAACATGTGCCAGACAGTGGAGCCACAGCCACGGCC
TACCTGTGCGGGGTCAAGGGCAACTTCCAGACCATTGGCTTGAGTGCAGCCGCCCGCTTT
AACCAGTGCAACACGACACGCGGCAACGAGGTCATCTCCGTGATGAATCGGGCCAAGAAA
GCAGGGAAGTCAGTGGGAGTGGTAACCACCACACGAGTGCAGCACGCCTCGCCAGCCGGC
ACCTACGCCCACACGGTGAACCGCAACTGGTACTCGGACGCCGACGTGCCTGCCTCGGCC
CGCCAGGAGGGGTGCCAGGACATCGCTACGCAGCTCATCTCCAACATGGACATTGACGTG
ATCCTAGGTGGAGGCCGAAAGTACATGTTTCCCATGGGAACCCCAGACCCTGAGTACCCA
GATGACTACAGCCAAGGTGGGACCAGGCTGGACGGGAAGAATCTGGTGCAGGAATGGCTG
GCGAAGCGCCAGGGTGCCCGGTATGTGTGGAACCGCACTGAGCTCATGCAGGCTTCCCTG
GACCCGTCTGTGACCCATCTCATGGGTCTCTTTGAGCCTGGAGACATGAAATACGAGATC
CACCGAGACTCCACACTGGACCCCTCCCTGATGGAGATGACAGAGGCTGCCCTGCGCCTG
CTGAGCAGGAACCCCCGCGGCTTCTTCCTCTTCGTGGAGGGTGGTCGCATCGACCATGGT
CATCATGAAAGCAGGGCTTACCGGGCACTGACTGAGACGATCATGTTCGACGACGCCATT
GAGAGGGCGGGCCAGCTCACCAGCGAGGAGGACACGCTGAGCCTCGTCACTGCCGACCAC
TCCCACGTCTTCTCCTTCGGAGGCTACCCCCTGCGAGGGAGCTCCATCTTCGGGCTGGCC
CCTGGCAAGGCCCGGGACAGGAAGGCCTACACGGTCCTCCTATACGGAAACGGTCCAGGC
TATGTGCTCAAGGACGGCGCCCGGCCGGATGTTACCGAGAGCGAGAGCGGGAGCCCCGAG
TATCGGCAGCAGTCAGCAGTGCCCCTGGACGAAGAGACCCACGCAGGCGAGGACGTGGCG
GTGTTCGCGCGCGGCCCGCAGGCGCACCTGGTTCACGGCGTGCAGGAGCAGACCTTCATA
GCGCACGTCATGGCCTTCGCCGCCTGCCTGGAGCCCTACACCGCCTGCGACCTGGCGCCC
CCCGCCGGCACCACCGACGCCGCGCACCCGGGGCGGTCCGTGGTCCCCGCGTTGCTTCCT
CTGCTGGCCGGGACCCTGCTGCTGCTGGAGACGGCCACTGCTCCCTGA
|
| Enzyme 11 GenBank Gene ID |
M13077  |
| Enzyme 11 GeneCard ID |
ALPP  |
| Enzyme 11 GenAtlas ID |
ALPP  |
| Enzyme 11 HGNC ID |
HGNC:439  |
| Enzyme 11 Chromosome Location |
2 |
| Enzyme 11 Locus |
2q37 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Knoll BJ, Rothblum KN, Longley M: Nucleotide sequence of the human placental alkaline phosphatase gene. Evolution of the 5' flanking region by deletion/substitution. J Biol Chem. 1988 Aug 25;263(24):12020-7. [PubMed
]
- Millan JL: Molecular cloning and sequence analysis of human placental alkaline phosphatase. J Biol Chem. 1986 Mar 5;261(7):3112-5. [PubMed
]
- Henthorn PS, Knoll BJ, Raducha M, Rothblum KN, Slaughter C, Weiss M, Lafferty MA, Fischer T, Harris H: Products of two common alleles at the locus for human placental alkaline phosphatase differ by seven amino acids. Proc Natl Acad Sci U S A. 1986 Aug;83(15):5597-601. [PubMed
]
- Kam W, Clauser E, Kim YS, Kan YW, Rutter WJ: Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8715-9. [PubMed
]
- Ezra E, Blacher R, Udenfriend S: Purification and partial sequencing of human placental alkaline phosphatase. Biochem Biophys Res Commun. 1983 Nov 15;116(3):1076-83. [PubMed
]
- Knoll BJ, Rothblum KN, Longley M: Two gene duplication events in the evolution of the human heat-stable alkaline phosphatases. Gene. 1987;60(2-3):267-76. [PubMed
]
- Ovitt CE, Strauss AW, Alpers DH, Chou JY, Boime I: Expression of different-sized placental alkaline phosphatase mRNAs in placenta and choriocarcinoma cells. Proc Natl Acad Sci U S A. 1986 Jun;83(11):3781-5. [PubMed
]
- Micanovic R, Bailey CA, Brink L, Gerber L, Pan YC, Hulmes JD, Udenfriend S: Aspartic acid-484 of nascent placental alkaline phosphatase condenses with a phosphatidylinositol glycan to become the carboxyl terminus of the mature enzyme. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1398-402. [PubMed
]
- Micanovic R, Gerber LD, Berger J, Kodukula K, Udenfriend S: Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase. Proc Natl Acad Sci U S A. 1990 Jan;87(1):157-61. [PubMed
]
- Kozlenkov A, Manes T, Hoylaerts MF, Millan JL: Function assignment to conserved residues in mammalian alkaline phosphatases. J Biol Chem. 2002 Jun 21;277(25):22992-9. Epub 2002 Apr 5. [PubMed
]
- Lowe ME: Site-specific mutations in the COOH-terminus of placental alkaline phosphatase: a single amino acid change converts a phosphatidylinositol-glycan-anchored protein to a secreted protein. J Cell Biol. 1992 Feb;116(3):799-807. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5325 |
| Enzyme 12 Name |
Intestinal alkaline phosphatase precursor |
| Enzyme 12 Synonyms |
- IAP
|
| Enzyme 12 Gene Name |
ALPI |
| Enzyme 12 Protein Sequence |
>Intestinal alkaline phosphatase precursor
MQGPWVLLLLGLRLQLSLGVIPAEEENPAFWNRQAAEALDAAKKLQPIQKVAKNLILFLG
DGLGVPTVTATRILKGQKNGKLGPETPLAMDRFPYLALSKTYNVDRQVPDSAATATAYLC
GVKANFQTIGLSAAARFNQCNTTRGNEVISVMNRAKQAGKSVGVVTTTRVQHASPAGTYA
HTVNRNWYSDADMPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPADA
SQNGIRLDGKNLVQEWLAKHQGAWYVWNRTELMQASLDQSVTHLMGLFEPGDTKYEIHRD
PTLDPSLMEMTEAALRLLSRNPRGFYLFVEGGRIDHGHHEGVAYQALTEAVMFDDAIERA
GQLTSEEDTLTLVTADHSHVFSFGGYTLRGSSIFGLAPSKAQDSKAYTSILYGNGPGYVF
NSGVRPDVNESESGSPDYQQQAAVPLSSETHGGEDVAVFARGPQAHLVHGVQEQSFVAHV
MAFAACLEPYTACDLAPPACTTDAAHPVAASLPLLAGTLLLLGASAAP
|
| Enzyme 12 Number of Residues |
528 |
| Enzyme 12 Molecular Weight |
56813 |
| Enzyme 12 Theoretical pI |
5.70 |
| Enzyme 12 GO Classification |
| Function |
| — |
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Inorganic ion transport and metabolism |
| Enzyme 12 Specific Function |
A phosphate monoester + H(2)O = an alcohol + phosphate |
| Enzyme 12 Pathways |
- Folate and Pterine Biosynthesis (map00790
)
- gamma-Hexachlorocyclohexane Degradation (map00361
)
|
| Enzyme 12 Reactions |
- A phosphate monoester + H2O = an alcohol + phosphate
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
Not Available |
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
178432  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P09923  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
PPBI_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1587 bp
ATGCAGGGGCCCTGGGTGCTGCTGCTGCTGGGCCTGAGGCTACAGCTCTCCCTGGGCGTC
ATCCCAGCTGAGGAGGAGAACCCGGCCTTCTGGAACCGCCAGGCAGCTGAGGCCCTGGAT
GCTGCCAAGAAGCTGCAGCCCATCCAGAAGGTCGCCAAGAACCTCATCCTCTTCCTGGGC
GATGGGTTGGGGGTGCCCACGGTGACAGCCACCAGGATCCTAAAGGGGCAGAAGAATGGC
AAACTGGGGCCTGAGACGCCCCTGGCCATGGACCGCTTCCCATACCTGGCTCTGTCCAAG
ACATACAATGTGGACAGACAGGTGCCAGACAGCGCAGCCACAGCCACGGCCTACCTGTGC
GGGGTCAAGGCCAACTTCCAGACCATCGGCTTGAGTGCAGCCGCCCGCTTTAACCAGTGC
AACACGACACGCGGCAATGAGGTCATCTCCGTGATGAACCGGGCCAAGCAAGCAGGAAAG
TCAGTAGGAGTGGTGACCACCACACGGGTGCAGCACGCCTCGCCAGCCGGCACCTACGCA
CACACAGTGAACCGCAACTGGTACTCAGATGCTGACATGCCTGCCTCAGCCCGCCAGGAG
GGGTGCCAGGACATCGCCACTCAGCTCATCTCCAACATGGACATTGACGTGATCCTTGGC
GGAGGCCGCAAGTACATGTTTCCCATGGGGACCCCAGACCCTGAGTACCCAGCTGATGCC
AGCCAGAATGGAATCAGGCTGGACGGGAAGAACCTGGTGCAGGAATGGCTGGCAAAGCAC
CAGGGTGCCTGGTATGTGTGGAACCGCACTGAGCTCATGCAGGCGTCCCTGGACCAGTCT
GTGACCCATCTCATGGGCCTCTTTGAGCCCGGAGACACGAAATATGAGATCCTCCGAGAC
CCCACACTGGACCCCTCCCTGATGGAGATGACAGAGGCTGCCCTGCGCCTGCTGAGCAGG
AACCCCCGCGGCTTCTACCTCTTTGTGGAGGGCGGCCGCATCGACCATGGTCATCATGAG
GGTGTGGCTTACCAGGCAGTCACTGAGGCGGTCATGTTCGACGACGCCATTGAGAGGGCG
GGCCAGCTCACCAGCGAGGAGGACACGCTGACCCTCGTCACCGCTGACCACTCCCATGTC
TTCTCCTTTGGTGGCTACACCTTGCGAGGGAGCTCCATCTTCGGGTTGGCCCCCAGCAAG
GCTCAGGACAGCAAAGCCTACACGTCCATCCTGTACGGCAATGGCCCGGGCTACGTGTTC
AACTCAGGCGTGCGACCAGACGTGAATGAGAGCGAGAGCGGGAGCCCCGATTACCAGCAG
CAGGCGGCGGTGCCCCTGTCGTCCGAGACCCACGGAGGCGAAGACGTGGCGGTGTTTGCG
CGCGGCCCGCAGGCGCACCTGGTGCATGGTGTGCAGGAGCAGAGCTTCGTAGCGCATGTC
ATGGCCTTCGCTGCCTGTCTGGAGCCCTACACGGCCTGCGACCTGGCGCTCCCCGCCTGC
ACCACCGACGCCGCGCACCCAGTTGCCGCGTCGCTGCCACTGCTGGCCGGGACCCTGCTG
CTGCTGGGGGCGTCCGCTGCTCCCTGA
|
| Enzyme 12 GenBank Gene ID |
M15694  |
| Enzyme 12 GeneCard ID |
ALPI  |
| Enzyme 12 GenAtlas ID |
ALPI  |
| Enzyme 12 HGNC ID |
HGNC:437  |
| Enzyme 12 Chromosome Location |
2 |
| Enzyme 12 Locus |
2q37.1 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Berger J, Garattini E, Hua JC, Udenfriend S: Cloning and sequencing of human intestinal alkaline phosphatase cDNA. Proc Natl Acad Sci U S A. 1987 Feb;84(3):695-8. [PubMed
]
- Henthorn PS, Raducha M, Edwards YH, Weiss MJ, Slaughter C, Lafferty MA, Harris H: Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase. Proc Natl Acad Sci U S A. 1987 Mar;84(5):1234-8. [PubMed
]
- Henthorn PS, Raducha M, Kadesch T, Weiss MJ, Harris H: Sequence and characterization of the human intestinal alkaline phosphatase gene. J Biol Chem. 1988 Aug 25;263(24):12011-9. [PubMed
]
- Millan JL: Promoter structure of the human intestinal alkaline phosphatase gene. Nucleic Acids Res. 1987 Dec 23;15(24):10599. [PubMed
]
- Knoll BJ, Rothblum KN, Longley M: Two gene duplication events in the evolution of the human heat-stable alkaline phosphatases. Gene. 1987;60(2-3):267-76. [PubMed
]
- Hua JC, Berger J, Pan YC, Hulmes JD, Udenfriend S: Partial sequencing of human adult, human fetal, and bovine intestinal alkaline phosphatases: comparison with the human placental and liver isozymes. Proc Natl Acad Sci U S A. 1986 Apr;83(8):2368-72. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5326 |
| Enzyme 13 Name |
Lysosomal acid phosphatase precursor |
| Enzyme 13 Synonyms |
- LAP
|
| Enzyme 13 Gene Name |
ACP2 |
| Enzyme 13 Protein Sequence |
>Lysosomal acid phosphatase precursor
MAGKRSGWSRAALLQLLLGVNLVVMPPTRARSLRFVTLLYRHGDRSPVKTYPKDPYQEEE
WPQGFGQLTKEGMLQHWELGQALRQRYHGFLNTSYHRQEVYVRSTDFDRTLMSAEANLAG
LFPPNGMQRFNPNISWQPIPVHTVPITEDRLLKFPLGPCPRYEQLQNETRQTPEYQNESS
RNAQFLDMVANETGLTDLTLETVWNVYDTLFCEQTHGLRLPPWASPQTMQRLSRLKDFSF
RFLFGIYQQAEKARLQGGVLLAQIRKNLTLMATTSQLPKLLVYSAHDTTLVALQMALDVY
NGEQAPYASCHIFELYQEDSGNFSVEMYFRNESDKAPWPLSLPGCPHRCPLQDFLRLTEP
VVPKDWQQECQLASGPADTEVIVALAVCGSILFLLIVLLLTVLFRMQAQPPGYRHVADGE
DHA
|
| Enzyme 13 Number of Residues |
423 |
| Enzyme 13 Molecular Weight |
48345 |
| Enzyme 13 Theoretical pI |
6.73 |
| Enzyme 13 GO Classification |
| Function |
- acid phosphatase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 13 General Function |
Not Available |
| Enzyme 13 Specific Function |
A phosphate monoester + H(2)O = an alcohol + phosphate |
| Enzyme 13 Pathways |
- gamma-Hexachlorocyclohexane Degradation (map00361
)
- Riboflavin Metabolism (map00740
)
|
| Enzyme 13 Reactions |
- A phosphate monoester + H2O = an alcohol + phosphate
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
34263  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
P11117  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
PPAL_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1272 bp
ATGGCGGGCAAGCGGTCCGGCTGGAGCCGGGCGGCTCTCCTCCAGCTCCTTCTCGGCGTG
AACCTGGTGGTGATGCCGCCCACCCGGGCCCGGAGTCTGCGCTTCGTTACCTTGCTGTAC
CGCCATGGAGACCGTTCACCAGTGAAGACATATCCCAAGGACCCCTATCAGGAAGAAGAA
TGGCCCCAGGGGTTTGGTCAGTTAACCAAGGAGGGGATGCTACAGCACTGGGAACTGGGC
CAGGCCCTGCGGCAGCGCTATCACGGCTTCCTAAACACCTCTTATCACCGGCAAGAGGTT
TATGTGCGAAGCACAGACTTTGACCGGACTCTCATGAGTGCTGAGGCCAACCTGGCTGGA
CTCTTCCCTCCCAACGGGATGCAGCGCTTCAACCCGAACATCTCGTGGCAGCCTATTCCT
GTGCACACTGTGCCCATCACTGAGGACAGGCTGCTGAAGTTCCCGTTGGGCCCATGTCCC
CGTTATGAGCAGCTGCAGAACGAGACCCGGCAGACACCAGAGTATCAGAATGAGAGTTCT
CGGAATGCACAATTTCTGGACATGGTGGCCAACGAGACAGGGCTTACAGACCTGACACTG
GAGACCGTCTGGAATGTCTATGACACACTCTTCTGTGAGCAAACGCACGGGCTGCGCCTG
CCGCCCTGGGCCTCACCCCAAACCATGCAGCGTCTCAGCCGGCTAAAGGACTTCAGCTTC
CGCTTCCTCTTCGGAATCTACCAGCAGGCGGAGAAGGCCCGGCTTCAGGGGGGAGTCCTG
CTGGCTCAGATAAGGAAGAACCTGACCCTAATGGCGACCACCTCCCAGCTCCCCAAGCTG
CTGGTTTACTCTGCGCACGACACTACCCTGGTTGCCCTGCAAATGGCACTGGATGTCTAC
AATGGTGAACAAGCCCCCTACGCCTCCTGCCACATATTTGAACTGTACCAGGAAGATTCT
GGGAATTTCTCAGTGGAGATGTACTTTCGGAACGAGAGTGACAAGGCCCCCTGGCCGCTC
AGCCTGCCTGGCTGCCCTCACCGCTGCCCACTGCAGGACTTCCTTCGCCTCACAGAGCCC
GTCGTGCCCAAGGATTGGCAGCAGGAGTGCCAGCTGGCAAGCGGTCCTGCAGACACAGAG
GTGATTGTGGCCTTGGCTGTATGTGGCTCCATCCTCTTCCTCCTCATAGTGCTGCTCCTC
ACCGTCCTCTTCCGGATGCAGGCCCAGCCTCCTGGCTACCGCCACGTCGCAGATGGGGAG
GACCACGCCTGA
|
| Enzyme 13 GenBank Gene ID |
X12548  |
| Enzyme 13 GeneCard ID |
ACP2  |
| Enzyme 13 GenAtlas ID |
ACP2  |
| Enzyme 13 HGNC ID |
HGNC:123  |
| Enzyme 13 Chromosome Location |
11 |
| Enzyme 13 Locus |
11p11.2-p11.11|11p12-p11 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Pohlmann R, Krentler C, Schmidt B, Schroder W, Lorkowski G, Culley J, Mersmann G, Geier C, Waheed A, Gottschalk S, et al.: Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment. EMBO J. 1988 Aug;7(8):2343-50. [PubMed
]
- Geier C, von Figura K, Pohlmann R: Structure of the human lysosomal acid phosphatase gene. Eur J Biochem. 1989 Aug 15;183(3):611-6. [PubMed
]
- Nadler HL, Egan TJ: Deficiency of lysosomal acid phosphatase. A new familial metabolic disorder. N Engl J Med. 1970 Feb 5;282(6):302-7. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
5327 |
| Enzyme 14 Name |
Low molecular weight phosphotyrosine protein phosphatase |
| Enzyme 14 Synonyms |
- LMW-PTPase
- LMW-PTP
- Low molecular weight cytosolic acid phosphatase
- Red cell acid phosphatase 1
- Adipocyte acid phosphatase
|
| Enzyme 14 Gene Name |
ACP1 |
| Enzyme 14 Protein Sequence |
>Low molecular weight phosphotyrosine protein phosphatase
MAEQATKSVLFVCLGNICRSPIAEAVFRKLVTDQNISENWRVDSAATSGYEIGNPPDYRG
QSCMKRHGIPMSHVARQITKEDFATFDYILCMDESNLRDLNRKSNQVKTCKAKIELLGSY
DPQKQLIIEDPYYGNDSDFETVYQQCVRCCRAFLEKAH
|
| Enzyme 14 Number of Residues |
158 |
| Enzyme 14 Molecular Weight |
18043 |
| Enzyme 14 Theoretical pI |
6.73 |
| Enzyme 14 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- non-membrane spanning protein tyrosine phosphatase activity
- phosphoprotein phosphatase activity
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
- protein tyrosine phosphatase activity
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid dephosphorylation
- protein modification
|
| Component |
| — |
|
| Enzyme 14 General Function |
Signal transduction mechanisms |
| Enzyme 14 Specific Function |
Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Isoform 3 does not possess phosphatase activity |
| Enzyme 14 Pathways |
- gamma-Hexachlorocyclohexane Degradation (map00361
)
- Riboflavin Metabolism (map00740
)
|
| Enzyme 14 Reactions |
- protein tyrosine phosphate + H2O = protein tyrosine + phosphate
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
Not Available |
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
179636  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P24666  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
PPAC_HUMAN  |
| Enzyme 14 PDB ID |
5PNT  |
| Enzyme 14 PDB File |
Show |
| Enzyme 14 3D Structure |
|
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>477 bp
ATGGCGGAACAGGCTACCAAGTCCGTGCTGTTTGTGTGTCTGGGTAACATTTGTCGATCA
CCCATTGCAGAAGCAGTTTTCAGGAAACTTGTAACCGATCAAAACATCTCAGAGAATTGG
AGGGTAGACAGCGCGGCAACTTCCGGGTATGAGATAGGGAACCCCCCTGACTACCGAGGG
CAGAGCTGCATGAAGAGGCACGGCATTCCCATGAGCCACGTTGCCCGGCAGATTACCAAA
GAAGATTTTGCCACATTTGATTATATACTATGTATGGATGAAAGCAATCTGAGAGATTTG
AATAGAAAAAGTAATCAAGTTAAAACCTGCAAAGCTAAAATTGAACTACTTGGGAGCTAT
GATCCACAAAAACAACTTATTATTGAAGATCCCTATTATGGGAATGACTCTGACTTTGAG
ACGGTGTACCAGCAGTGTGTCAGGTGCTGCAGAGCGTTCTTGGAGAAGGCCCACTGA
|
| Enzyme 14 GenBank Gene ID |
M83653  |
| Enzyme 14 GeneCard ID |
ACP1  |
| Enzyme 14 GenAtlas ID |
ACP1  |
| Enzyme 14 HGNC ID |
HGNC:122  |
| Enzyme 14 Chromosome Location |
2 |
| Enzyme 14 Locus |
2p25 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Dissing J, Johnsen AH, Sensabaugh GF: Human red cell acid phosphatase (ACP1). The amino acid sequence of the two isozymes Bf and Bs encoded by the ACP1*B allele. J Biol Chem. 1991 Nov 5;266(31):20619-25. [PubMed
]
- Dissing J, Johnsen AH: Human red cell acid phosphatase (ACP1): the primary structure of the two pairs of isozymes encoded by the ACP1*A and ACP1*C alleles. Biochim Biophys Acta. 1992 Jun 24;1121(3):261-8. [PubMed
]
- Wo YY, McCormack AL, Shabanowitz J, Hunt DF, Davis JP, Mitchell GL, Van Etten RL: Sequencing, cloning, and expression of human red cell-type acid phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase. J Biol Chem. 1992 May 25;267(15):10856-65. [PubMed
]
- Bryson GL, Massa H, Trask BJ, Van Etten RL: Gene structure, sequence, and chromosomal localization of the human red cell-type low-molecular-weight acid phosphotyrosyl phosphatase gene, ACP1. Genomics. 1995 Nov 20;30(2):133-40. [PubMed
]
- Shekels LL, Smith AJ, Van Etten RL, Bernlohr DA: Identification of the adipocyte acid phosphatase as a PAO-sensitive tyrosyl phosphatase. Protein Sci. 1992 Jun;1(6):710-21. [PubMed
]
- Sensabaugh GF, Lazaruk KA: A TaqI site identifies the *A allele at the ACP1 locus. Hum Mol Genet. 1993 Jul;2(7):1079. [PubMed
]
- Nicolas G, Fournier CM, Galand C, Malbert-Colas L, Bournier O, Kroviarski Y, Bourgeois M, Camonis JH, Dhermy D, Grandchamp B, Lecomte MC: Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain. Mol Cell Biol. 2002 May;22(10):3527-36. [PubMed
]
- Zhang M, Stauffacher CV, Lin D, Van Etten RL: Crystal structure of a human low molecular weight phosphotyrosyl phosphatase. Implications for substrate specificity. J Biol Chem. 1998 Aug 21;273(34):21714-20. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
5328 |
| Enzyme 15 Name |
Alkaline phosphatase, tissue-nonspecific isozyme precursor |
| Enzyme 15 Synonyms |
- AP-TNAP
- TNSALP
- Alkaline phosphatase liver/bone/kidney isozyme
|
| Enzyme 15 Gene Name |
ALPL |
| Enzyme 15 Protein Sequence |
>Alkaline phosphatase, tissue-nonspecific isozyme precursor
MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGD
GMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCG
VKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAH
SADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDE
KARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELN
RNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIG
QAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPG
YKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYV
PHVMAYAACIGANLGHCAPASSAGSLAAGPLLLALALYPLSVLF
|
| Enzyme 15 Number of Residues |
524 |
| Enzyme 15 Molecular Weight |
57305 |
| Enzyme 15 Theoretical pI |
6.66 |
| Enzyme 15 GO Classification |
| Function |
| — |
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Inorganic ion transport and metabolism |
| Enzyme 15 Specific Function |
This isozyme may play a role in skeletal mineralization |
| Enzyme 15 Pathways |
- Folate and Pterine Biosynthesis (map00790
)
- gamma-Hexachlorocyclohexane Degradation (map00361
)
|
| Enzyme 15 Reactions |
- A phosphate monoester + H2O = an alcohol + phosphate
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
Not Available |
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
28738  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P05186  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
PPBT_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1575 bp
ATGATTTCACCATTCTTAGTACTGGCCATTGGCACCTGCCTTACTAACTCCTTAGTGCCA
GAGAAAGAGAAAGACCCCAAGTACTGGCGAGACCAAGCGCAAGAGACACTGAAATATGCC
CTGGAGCTTCAGAAGCTCAACACCAACGTGGCTAAGAATGTCATCATGTTCCTGGGAGAT
GGGATGGGTGTCTCCACAGTGACGGCTGCCCGCATCCTCAAGGGTCAGCTCCACCACAAC
CCTGGGGAGGAGACCAGGCTGGAGATGGACAAGTTCCCCTTCGTGGCCCTCTCCAAGACG
TACAACACCAAAGCCCAGGTCCCTGACAGCGCCGGCACCGCCACCGCCTACCTGTGTGGG
GTGAAGGCCAATGAGGGCACCGTGGGGGTAAGCGCAGCCACTGAGCGTTCCCGGTGCAAC
ACCACCCAGGGGAACGAGGTCACCTCCATCCTGCGCTGGGCCAAGGACGCTGGGAAATCT
GTGGGCATTGTGACCACCACGAGAGTGAACCATGCCACCCCCAGCGCCGCCTACGCCCAC
TCGGCTGACCGGGACTGGTACTCAGACAACGAGATGCCCCCTGAGGCCTTGAGCCAGGGC
TGTAAGGACATCGCCTACCAGCTCATGCATAACATCAGGGACATTGACGTGATCATGGGG
GGTGGCCGGAAATACATGTACCCCAAGAATAAAACTGATGTGGAGTATGAGAGTGACGAG
AAAGCCAGGGGCACGAGGCTGGACGGCCTGGACCTCGTTGACACCTGGAAGAGCTTCAAA
CCGAGACACAAGCACTCCCACTTCATCTGGAACCGCACGGAACTCCTGACCCTTGACCCC
CACAATGTGGACTACCTATTGGGTCTCTTCGAGCCGGGGGACATGCAGTACGAGCTGAAC
AGGAACAACGTGACGGACCCGTCACTCTCCGAGATGGTGGTGGTGGCCATCCAGATCCTG
CGGAAGAACCCCAAAGGCTTCTTCTTGCTGGTGGAAGGAGGCAGAATTGACCACGGGCAC
CATGAAGGAAAAGCCAAGCAGGCCCTGCATGAGGCGGTGGAGATGGACCGGGCCATCGGG
CAGGCAGGCAGCTTGACCTCCTCGGAAGACACTCTGACCGTGGTCACTGCGGACCATTCC
CACGTCTTCACATTTGGTGGATACACCCCCCGTGGCAACTCTATCTTTGGTCTGGCCCCC
ATGCTGAGTGACACAGACAAGAAGCCCTTCACTGCCATCCTGTATGGCAATGGGCCTGGC
TACAAGGTGGTGGGCGGTGAACGAGAGAATGTCTCCATGGTGGACTATGCTCACAACAAC
TACCAGGCGCAGTCTGCTGTGCCCCTGCGCCACGAGACCCACGGCGGGGAGGACGTGGCC
GTCTTCTCCAAGGGCCCCATGGCGCACCTGCTGCACGGCGTCCACGAGCAGAACTACGTC
CCCCACGTGATGGCGTATGCAGCCTGCATCGGGGCCAACCTCGGCCACTGTGCTCCTGCC
AGCTCGGCAGGCAGCCTTGCTGCAGGCCCCCTGCTGCTCGCGCTGGCCCTCTACCCCCTG
AGCGTCCTGTTCTGA
|
| Enzyme 15 GenBank Gene ID |
X14174  |
| Enzyme 15 GeneCard ID |
ALPL  |
| Enzyme 15 GenAtlas ID |
ALPL  |
| Enzyme 15 HGNC ID |
HGNC:438  |
| Enzyme 15 Chromosome Location |
1 |
| Enzyme 15 Locus |
1p36.1-p34 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Kishi F, Matsuura S, Kajii T: Nucleotide sequence of the human liver-type alkaline phosphatase cDNA. Nucleic Acids Res. 1989 Mar 11;17(5):2129. [PubMed
]
- Weiss MJ, Henthorn PS, Lafferty MA, Slaughter C, Raducha M, Harris H: Isolation and characterization of a cDNA encoding a human liver/bone/kidney-type alkaline phosphatase. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7182-6. [PubMed
]
- Weiss MJ, Ray K, Henthorn PS, Lamb B, Kadesch T, Harris H: Structure of the human liver/bone/kidney alkaline phosphatase gene. J Biol Chem. 1988 Aug 25;263(24):12002-10. [PubMed
]
- Garattini E, Hua JC, Pan YC, Udenfriend S: Human liver alkaline phosphatase, purification and partial sequencing: homology with the placental isozyme. Arch Biochem Biophys. 1986 Mar;245(2):331-7. [PubMed
]
- Weiss MJ, Cole DE, Ray K, Whyte MP, Lafferty MA, Mulivor RA, Harris H: A missense mutation in the human liver/bone/kidney alkaline phosphatase gene causing a lethal form of hypophosphatasia. Proc Natl Acad Sci U S A. 1988 Oct;85(20):7666-9. [PubMed
]
- Henthorn PS, Raducha M, Fedde KN, Lafferty MA, Whyte MP: Different missense mutations at the tissue-nonspecific alkaline phosphatase gene locus in autosomal recessively inherited forms of mild and severe hypophosphatasia. Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9924-8. [PubMed
]
- Greenberg CR, Taylor CL, Haworth JC, Seargeant LE, Philipps S, Triggs-Raine B, Chodirker BN: A homoallelic Gly317-->Asp mutation in ALPL causes the perinatal (lethal) form of hypophosphatasia in Canadian mennonites. Genomics. 1993 Jul;17(1):215-7. [PubMed
]
- Ozono K, Yamagata M, Michigami T, Nakajima S, Sakai N, Cai G, Satomura K, Yasui N, Okada S, Nakayama M: Identification of novel missense mutations (Phe310Leu and Gly439Arg) in a neonatal case of hypophosphatasia. J Clin Endocrinol Metab. 1996 Dec;81(12):4458-61. [PubMed
]
- Goseki-Sone M, Orimo H, Iimura T, Takagi Y, Watanabe H, Taketa K, Sato S, Mayanagi H, Shimada T, Oida S: Hypophosphatasia: identification of five novel missense mutations (G507A, G705A, A748G, T1155C, G1320A) in the tissue-nonspecific alkaline phosphatase gene among Japanese patients. Hum Mutat. 1998;Suppl 1:S263-7. [PubMed
]
- Sugimoto N, Iwamoto S, Hoshino Y, Kajii E: A novel missense mutation of the tissue-nonspecific alkaline phosphatase gene detected in a patient with hypophosphatasia. J Hum Genet. 1998;43(3):160-4. [PubMed
]
- Zurutuza L, Muller F, Gibrat JF, Taillandier A, Simon-Bouy B, Serre JL, Mornet E: Correlations of genotype and phenotype in hypophosphatasia. Hum Mol Genet. 1999 Jun;8(6):1039-46. [PubMed
]
- Taillandier A, Zurutuza L, Muller F, Simon-Bouy B, Serre JL, Bird L, Brenner R, Boute O, Cousin J, Gaillard D, Heidemann PH, Steinmann B, Wallot M, Mornet E: Characterization of eleven novel mutations (M45L, R119H, 544delG, G145V, H154Y, C184Y, D289V, 862+5A, 1172delC, R411X, E459K) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with severe hypophosphatasia. Mutations in brief no. 217. Online. Hum Mutat. 1999;13(2):171-2. [PubMed
]
- Mochizuki H, Saito M, Michigami T, Ohashi H, Koda N, Yamaguchi S, Ozono K: Severe hypercalcaemia and respiratory insufficiency associated with infantile hypophosphatasia caused by two novel mutations of the tissue-nonspecific alkaline phosphatase gene. Eur J Pediatr. 2000 May;159(5):375-9. [PubMed
]
- Taillandier A, Cozien E, Muller F, Merrien Y, Bonnin E, Fribourg C, Simon-Bouy B, Serre JL, Bieth E, Brenner R, Cordier MP, De Bie S, Fellmann F, Freisinger P, Hesse V, Hennekam RC, Josifova D, Kerzin-Storrar L, Leporrier N, Zabot MT, Mornet E: Fifteen new mutations (-195C>T, L-12X, 298-2A>G, T117N, A159T, R229S, 997+2T>A, E274X, A331T, H364R, D389G, 1256delC, R433H, N461I, C472S) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with hypophosphatasia. Hum Mutat. 2000 Mar;15(3):293. [PubMed
]
- Muller HL, Yamazaki M, Michigami T, Kageyama T, Schonau E, Schneider P, Ozono K: Asp361Val Mutant of alkaline phosphatase found in patients with dominantly inherited hypophosphatasia inhibits the activity of the wild-type enzyme. J Clin Endocrinol Metab. 2000 Feb;85(2):743-7. [PubMed
]
- Lia-Baldini AS, Muller F, Taillandier A, Gibrat JF, Mouchard M, Robin B, Simon-Bouy B, Serre JL, Aylsworth AS, Bieth E, Delanote S, Freisinger P, Hu JC, Krohn HP, Nunes ME, Mornet E: A molecular approach to dominance in hypophosphatasia. Hum Genet. 2001 Jul;109(1):99-108. [PubMed
]
- Taillandier A, Lia-Baldini AS, Mouchard M, Robin B, Muller F, Simon-Bouy B, Serre JL, Bera-Louville A, Bonduelle M, Eckhardt J, Gaillard D, Myhre AG, Kortge-Jung S, Larget-Piet L, Malou E, Sillence D, Temple IK, Viot G, Mornet E: Twelve novel mutations in the tissue-nonspecific alkaline phosphatase gene (ALPL) in patients with various forms of hypophosphatasia. Hum Mutat. 2001;18(1):83-4. [PubMed
]
- Watanabe H, Hashimoto-Uoshima M, Goseki-Sone M, Orimo H, Ishikawa I: A novel point mutation (C571T) in the tissue-non-specific alkaline phosphatase gene in a case of adult-type hypophosphatasia. Oral Dis. 2001 Nov;7(6):331-5. [PubMed
]
- Litmanovitz, Reish O, Dolfin T, Arnon S, Regev R, Grinshpan G, Yamazaki M, Ozono K: Glu274Lys/Gly309Arg mutation of the tissue-nonspecific alkaline phosphatase gene in neonatal hypophosphatasia associated with convulsions. J Inherit Metab Dis. 2002 Feb;25(1):35-40. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
5329 |
| Enzyme 16 Name |
Tartrate-resistant acid phosphatase type 5 precursor |
| Enzyme 16 Synonyms |
- TR- AP
- Tartrate-resistant acid ATPase
- TrATPase
- Acid phosphatase 5, tartrate resistant
|
| Enzyme 16 Gene Name |
ACP5 |
| Enzyme 16 Protein Sequence |
>Tartrate-resistant acid phosphatase type 5 precursor
MDMWTALLILQALLLPSLADGATPALRFVAVGDWGGVPNAPFHTAREMANAKEIARTVQI
LGADFILSLGDNFYFTGVQDINDKRFQETFEDVFSDRSLRKVPWYVLAGNHDHLGNVSAQ
IAYSKISKRWNFPSPFYRLHFKIPQTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKL
ARTQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYGVTAYLCGH
DHNLQYLQDENGVGYVLSGAGNFMDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSK
EMTVTYIEASGKSLFKTRLPRRARP
|
| Enzyme 16 Number of Residues |
325 |
| Enzyme 16 Molecular Weight |
36599 |
| Enzyme 16 Theoretical pI |
8.95 |
| Enzyme 16 GO Classification |
| Function |
- acid phosphatase activity
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- iron ion binding
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
- transition metal ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 16 General Function |
Not Available |
| Enzyme 16 Specific Function |
A phosphate monoester + H(2)O = an alcohol + phosphate |
| Enzyme 16 Pathways |
- gamma-Hexachlorocyclohexane Degradation (map00361
)
- Riboflavin Metabolism (map00740
)
|
| Enzyme 16 Reactions |
- A phosphate monoester + H2O = an alcohol + phosphate
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
Not Available |
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
178006  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P13686  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
PPA5_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>972 bp
ATGGACATGTGGACGGCGCTGCTCATCCTGCAAGCCTTGTTGCTACCCTCCCTGGCTGAT
GGTGCCACCCCTGCCCTGCGCTTTGTAGCCGTGGGTGACTGGGGAGGGGTCCCCAATGCC
CCATTCCACACGGGCCCGGAAATGGCCAATGCCAAGGAGATCGCTCGGACTGTGCAGATC
CTGGGTGCAGACTTCATCCTGTCTCTAGGGGACAATTTTTACTTCACTGGTGTGCAAGAC
ATCAATGACAAGAGGTTCCAGGAGACCTTTGAGGACGTATTCTCTGACCGCTCCCTTCGC
AAAGTGCCCTGGTACGTGCTAGCCGGAAACCATGACCACCTTGGCAATGTCTCTGCCCAG
ATTGCATACTCTAAGATCTCCAAGCGCTGGAACTTCCCCAGCCCTTTCTACCGCCTGCAC
TTCAAGATCCCACAGACCAATGTGTCTGTGGCCATTTTTATGCTGGACACAGTGACACTA
TGTGGCAACTCAGATGACTTCCTCAGCCAGCAGCCTGAGAGGCCCCGACTAACTGCCCGC
ACACAGCTGTCCTGGCTCAAGAAACAGCTGGCGGCGGCCAGGGAGGACTACGTGCTGGTG
GCTGGCCACTACCCCGTGTGGTCCATAGCCGAGCACGGGCCTACCCACTGCCTGGTCAAG
CAGCTACGGCCACTGCTGGCCACATACGGGGTCACTGCCTACCTGTGCGGCCACGATCAC
AATCTGCAGTACCTGCAAGATGAGAATGGCGTGGGCTACGTGCTGAGTGGGGCTGGGAAT
TTCATGGACCCCTCAAAGCGGCACCAGCGCAAGGTCCCCAACGGCTATCTGCGCTTCCAC
TATGGGACTGAAGACTCACTGGGTGGCTTTGCCTATGTGGAGATCAGCTCCAAAGAGATG
ACTGTCACTTACATCGAGGCCTCGGGCAAGTCCCTCTTTAAGACCAGGCTGCCGAGGCGA
GCCAGGCCCTGA
|
| Enzyme 16 GenBank Gene ID |
J04430  |
| Enzyme 16 GeneCard ID |
ACP5  |
| Enzyme 16 GenAtlas ID |
ACP5  |
| Enzyme 16 HGNC ID |
HGNC:124  |
| Enzyme 16 Chromosome Location |
19 |
| Enzyme 16 Locus |
19p13.3-p13.2 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Ketcham CM, Roberts RM, Simmen RC, Nick HS: Molecular cloning of the type 5, iron-containing, tartrate-resistant acid phosphatase from human placenta. J Biol Chem. 1989 Jan 5;264(1):557-63. [PubMed
]
- Lord DK, Cross NC, Bevilacqua MA, Rider SH, Gorman PA, Groves AV, Moss DW, Sheer D, Cox TM: Type 5 acid phosphatase. Sequence, expression and chromosomal localization of a differentiation-associated protein of the human macrophage. Eur J Biochem. 1990 Apr 30;189(2):287-93. [PubMed
]
- Cassady AI, King AG, Cross NC, Hume DA: Isolation and characterization of the genes encoding mouse and human type-5 acid phosphatase. Gene. 1993 Aug 25;130(2):201-7. [PubMed
]
- Stepan JJ, Lau KH, Mohan S, Kraenzlin M, Baylink DJ: Purification and N-terminal sequence of two tartrate-resistant acid phosphatases type-5 from the hairy cell leukemia spleen. Biochem Biophys Res Commun. 1989 Dec 29;165(3):1027-34. [PubMed
]
- Stepan JJ, Lau KH, Mohan S, Singer FR, Baylink DJ: Purification and N-terminal amino acid sequence of the tartrate-resistant acid phosphatase from human osteoclastoma: evidence for a single structure. Biochem Biophys Res Commun. 1990 Apr 30;168(2):792-800. [PubMed
]
- Hayman AR, Warburton MJ, Pringle JA, Coles B, Chambers TJ: Purification and characterization of a tartrate-resistant acid phosphatase from human osteoclastomas. Biochem J. 1989 Jul 15;261(2):601-9. [PubMed
]
- Hayman AR, Dryden AJ, Chambers TJ, Warburton MJ: Tartrate-resistant acid phosphatase from human osteoclastomas is translated as a single polypeptide. Biochem J. 1991 Aug 1;277 ( Pt 3):631-4. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
5330 |
| Enzyme 17 Name |
Prostatic acid phosphatase precursor |
| Enzyme 17 Synonyms |
Not Available |
| Enzyme 17 Gene Name |
ACPP |
| Enzyme 17 Protein Sequence |
>Prostatic acid phosphatase precursor
MRAAPLLLARAASLSLGFLFLLFFWLDRSVLAKELKFVTLVFRHGDRSPIDTFPTDPIKE
SSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNL
AALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKR
LHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSE
LSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMAL
DVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELV
GPVIPQDWSTECMTTNSHQGTEDSTD
|
| Enzyme 17 Number of Residues |
386 |
| Enzyme 17 Molecular Weight |
44567 |
| Enzyme 17 Theoretical pI |
6.19 |
| Enzyme 17 GO Classification |
| Function |
- acid phosphatase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 17 General Function |
Not Available |
| Enzyme 17 Specific Function |
A phosphate monoester + H(2)O = an alcohol + phosphate |
| Enzyme 17 Pathways |
- gamma-Hexachlorocyclohexane Degradation (map00361
)
- Riboflavin Metabolism (map00740
)
|
| Enzyme 17 Reactions |
- A phosphate monoester + H2O = an alcohol + phosphate
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
Not Available |
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
189613  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
P15309  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
PPAP_HUMAN  |
| Enzyme 17 PDB ID |
1ND6  |
| Enzyme 17 PDB File |
Show |
| Enzyme 17 3D Structure |
|
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>1161 bp
ATGAGAGCTGCACCCCTCCTCCTGGCCAGGGCAGCAAGCCTTAGCCTTGGCTTCTTGTTT
CTGCTTTTTTTCTGGCTAGACCGAAGTGTACTAGCCAAGGAGTTGAAGTTTGTGACTTTG
GTGTTTCGGCATGGAGACCGAAGTCCCATTGACACCTTTCCCACTGACCCCATAAAGGAA
TCCTCATGGCCACAAGGATTTGGCCAACTCACCCAGCTGGGCATGGAGCAGCATTATGAA
CTTGGAGAGTATATAAGAAAGAGATATAGAAAATTCTTGAATGAGTCCTATAAACATGAA
CAGGTTTATATTCGAAGCACAGACGTTGACCGGACTTTGATGAGTGCTATGACAAACCTG
GCAGCCCTGTTTCCCCCAGAAGGTGTCAGCATCTGGAATCCTATCCTACTCTGGCAGCCC
ATCCCGGTGCACACAGTTCCTCTTTCTGAAGATCAGTTGCTATACCTGCCTTTCAGGAAC
TGCCCTCGTTTTCAAGAACTTGAGAGTGAGACTTTGAAATCAGAGGAATTCCAGAAGAGG
CTGCACCCTTATAAGGATTTTATAGCTACCTTGGGAAAACTTTCAGGATTACATGGCCAG
GACCTTTTTGGAATTTGGAGTAAAGTCTACGACCCTTTATATTGTGAGAGTGTTCACAAT
TTCACTTTACCCTCCTGGGCCACTGAGGACACCATGACTAAGTTGAGAGAATTGTCAGAA
TTGTCCCTCCTGTCCCTCTATGGAATTCACAAGCAGAAAGAGAAATCTAGGCTCCAAGGG
GGTGTCCTGGTCAATGAAATCCTCAATCACATGAAGAGAGCAACTCAGATACCAAGCTAC
AAAAAACTTATCATGTATTCTGCGCATGACACTACTGTGAGTGGCCTACAGATGGCGCTA
GATGTTTACAACGGACTCCTTCCTCCCTATGCTTCTTGCCACTTGACGGAATTGTACTTT
GAGAAGGGGGAGTACTTTGTGGAGATGTACTACCGGAATGAGACGCAGCACGAGCCGTAT
CCCCTCATGCTACCTGGCTGCAGCCCCAGCTGTCCTCTGGAGAGGTTTGCTGAGCTGGTT
GGCCCTGTGATCCCTCAAGACTGGTCCACGGAGTGTATGACCACAAACAGCCATCAAGGT
ACTGAGGACAGTACAGATTAG
|
| Enzyme 17 GenBank Gene ID |
M97589  |
| Enzyme 17 GeneCard ID |
ACPP  |
| Enzyme 17 GenAtlas ID |
ACPP  |
| Enzyme 17 HGNC ID |
HGNC:125  |
| Enzyme 17 Chromosome Location |
3 |
| Enzyme 17 Locus |
3q21-q23 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Sharief FS, Li SS: Structure of human prostatic acid phosphatase gene. Biochem Biophys Res Commun. 1992 May 15;184(3):1468-76. [PubMed
]
- Van Etten RL, Davidson R, Stevis PE, MacArthur H, Moore DL: Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase. J Biol Chem. 1991 Feb 5;266(4):2313-9. [PubMed
]
- Sharief FS, Lee H, Leuderman MM, Lundwall A, Deaven LL, Lee CL, Li SS: Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein sequence homology with lysosomal acid phosphatase. Biochem Biophys Res Commun. 1989 Apr 14;160(1):79-86. [PubMed
]
- Vihko P, Virkkunen P, Henttu P, Roiko K, Solin T, Huhtala ML: Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase. FEBS Lett. 1988 Aug 29;236(2):275-81. [PubMed
]
- Tailor PG, Govindan MV, Patel PC: Nucleotide sequence of human prostatic acid phosphatase determined from a full-length cDNA clone. Nucleic Acids Res. 1990 Aug 25;18(16):4928. [PubMed
]
- Sharief FS, Li SS: Nucleotide sequence of human prostatic acid phosphatase ACPP gene, including seven Alu repeats. Biochem Mol Biol Int. 1994 Jun;33(3):561-5. [PubMed
]
- LaCount MW, Handy G, Lebioda L: Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase. J Biol Chem. 1998 Nov 13;273(46):30406-9. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
5331 |
| Enzyme 18 Name |
Alkaline phosphatase, placental-like precursor |
| Enzyme 18 Synonyms |
- Alkaline phosphatase Nagao isozyme
- Germ-cell alkaline phosphatase
- GCAP
- PLAP-like
- ALP-1
|
| Enzyme 18 Gene Name |
ALPPL2 |
| Enzyme 18 Protein Sequence |
>Alkaline phosphatase, placental-like precursor
MQGPWVLLLLGLRLQLSLGIIPVEEENPDFWNRQAAEALGAAKKLQPAQTAAKNLIIFLG
DGMGVSTVTAARILKGQKKDKLGPETFLAMDRFPYVALSKTYSVDKHVPDSGATATAYLC
GVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGAYA
HTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPDDY
SQGGTRLDGKNLVQEWLAKHQGARYVWNRTELLQASLDPSVTHLMGLFEPGDMKYEIHRD
STLDPSLMEMTEAALLLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAIERA
GQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYVL
KDGARPDVTESESGSPEYRQQSAVPLDGETHAGEDVAVFARGPQAHLVHGVQEQTFIAHV
MAFAACLEPYTACDLAPRAGTTDAAHPGPSVVPALLPLLAGTLLLLGTATAP
|
| Enzyme 18 Number of Residues |
532 |
| Enzyme 18 Molecular Weight |
57378 |
| Enzyme 18 Theoretical pI |
6.31 |
| Enzyme 18 GO Classification |
| Function |
| — |
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 18 General Function |
Inorganic ion transport and metabolism |
| Enzyme 18 Specific Function |
A phosphate monoester + H(2)O = an alcohol + phosphate |
| Enzyme 18 Pathways |
- Folate and Pterine Biosynthesis (map00790
)
- gamma-Hexachlorocyclohexane Degradation (map00361
)
|
| Enzyme 18 Reactions |
- A phosphate monoester + H2O = an alcohol + phosphate
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
Not Available |
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
178428  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
P10696  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
PPBN_HUMAN  |
| Enzyme 18 PDB ID |
1EW2  |
| Enzyme 18 PDB File |
Show |
| Enzyme 18 3D Structure |
|
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>1599 bp
ATGCAGGGGCCCTGGGTGCTGCTCCTGCTGGGCCTGAGGCTACAGCTCTCCCTGGGCATC
ATCCCAGTTGAGGAGGAGAACCCGGACTTCTGGAACCGCCAGGCAGCCGAGGCCCTGGGT
GCCGCCAAGAAGCTGCAGCCTGCACAGACAGCCGCCAAGAACCTCATCATGTTCCTGGGT
GACGGGATGGGGGTGTCTACGGTGACAGCTGCCAGGATCCTAAAAGGGCAGAAGAAGGAC
AAACTGGGGCCTGAGACCTTCCTGGCCATGGACCGCTTCCCGTACGTGGCTCTGTCCAAG
ACATACAGTGTAGACAAGCATGTGCCAGACAGTGGAGCCACAGCCACGGCCTACCTGTGC
GGGGTCAAGGGCAACTTCCAGACCATTGGCTTGAGTGCAGCCGCCCGCTTTAACCAGTGC
AACACGACACGCGGCAACGAGGTCATCTCCGTGGTGAATCGGGCCAAGAAAGCAGGAAAG
TCAGTGGGAGTGGTAACCACCACACGGGTGCAGCATGCCTCGCCAGCCGGCACCTACGCC
CACACGGTGAACCGCAACTGGTACTCGGATGCCGACGTGCCTGCCTCGGCCCGCCAGGAG
GGGTGCCAGGACATCGCCACGCAGCTCATCTCCAACATGGACATTGATGTGATCCTAGGT
GGAGGCCGAAAGTACATGTTTCCCATGGGGACCCCAGACCCTGAGTACCCAGATGACTAC
AGCCAAGGTGGGACCAGGCTGGACGGGAAGAATCTGGTGCAGGAATGGCTGGCGAAGCAC
CAGGGTGCCCGGTACGTGTGGAACCGCACTGAGCTCCTGCAGGCTTCCCTGGACCCGTCT
GTGACCCATCTCATGGGTCTCTTTGAGCCTGGAGACATGAAATACGAGATCCACCGAGAC
TCCACACTGGACCCCTCCCTGATGGAGATGACAGAGGCTGCCCTGCTCCTGCTGAGCAGG
AACCCCCGCGGCTTCTTCCTCTTCGTGGAGGGTGGTCGCATCGACCATGGTCATCATGAA
AGCAGGGCTTACCGGGCACTGACTGAGACGATCATGTTCGACGACGCCATTGAGAGGGCG
GGCCAGCTCACCAGCGAGGAGGACACGCTGAGCCTCGTCACTGCCGACCACTCCCACGTC
TTCTCCTTCGGAGGCTACCCCCTGCGAGGGAGCTCCATCTTCGGGCTGGCCCCTGGCAAG
GCCCGGGACAGGAAGGCCTACACGGTCCTCCTATACGGAAACGGTCCAGGCTATGTGCTC
AAGGACGGCGCCCGGCCGGATGTTACGGAGAGCGAGAGCGGGAGCCCCGAGTATCGGCAG
CAGTCAGCAGTGCCCCTGGACGGAGAGACCCACGCAGGCGAGGACGTGGCGGTGTTCGCG
CGCGGCCCGCAGGCGCACCTGGTTCACGGCGTGCAGGAGCAGACCTTCATAGCGCACGTC
ATGGCCTTCGCCGCCTGCCTGGAGCCCTACACCGCCTGCGACCTGGCGCCCCCCGCCGGC
ACCACCGACGCCGCGCACCCGGGGCCGTCCGTGGTCCCCGCGTTGCTTCCTCTGCTGGCA
GGGACCTTGCTGCTGCTGGGGACGGCCACTGCTCCCTGA
|
| Enzyme 18 GenBank Gene ID |
J03252  |
| Enzyme 18 GeneCard ID |
ALPPL2  |
| Enzyme 18 GenAtlas ID |
ALPPL2  |
| Enzyme 18 HGNC ID |
HGNC:441  |
| Enzyme 18 Chromosome Location |
2 |
| Enzyme 18 Locus |
2q37 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Millan JL, Manes T: Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline phosphatase gene. Proc Natl Acad Sci U S A. 1988 May;85(9):3024-8. [PubMed
]
- Watanabe S, Watanabe T, Li WB, Soong BW, Chou JY: Expression of the germ cell alkaline phosphatase gene in human choriocarcinoma cells. J Biol Chem. 1989 Jul 25;264(21):12611-9. [PubMed
]
- Gum JR, Hicks JW, Sack TL, Kim YS: Molecular cloning of complementary DNAs encoding alkaline phosphatase in human colon cancer cells. Cancer Res. 1990 Feb 15;50(4):1085-91. [PubMed
]
- Lowe ME, Strauss AW: Expression of a Nagao-type, phosphatidylinositol-glycan anchored alkaline phosphatase in human choriocarcinomas. Cancer Res. 1990 Jul 1;50(13):3956-62. [PubMed
]
- Shen LP, Liu H, Kan YW, Kam W: 5' nucleotide sequence of a putative human placental alkaline phosphatase-like gene. Nucleic Acids Res. 1988 Jun 24;16(12):5694. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
5463 |
| Enzyme 19 Name |
Lipid phosphate phosphohydrolase 2 |
| Enzyme 19 Synonyms |
- Phosphatidic acid phosphatase 2c
- Phosphatidate phosphohydrolase type 2c
- PAP2c
- PAP- 2c
- PAP2-gamma
- PAP2-G
|
| Enzyme 19 Gene Name |
PPAP2C |
| Enzyme 19 Protein Sequence |
>Lipid phosphate phosphohydrolase 2
MQRRWVFVLLDVLCLLVASLPFAILTLVNAPYKRGFYCGDDSIRYPYRPDTITHGLMAGV
TITATVILVSAGEAYLVYTDRLYSRSDFNNYVAAVYKVLGTFLFGAAVSQSLTDLAKYMI
GRLRPNFLAVCDPDWSRVNCSVYVQLEKVCRGNPADVTEARLSFYSGHSSFGMYCMVFLA
LYVQARLCWKWARLLRPTVQFFLVAFALYVGYTRVSDYKHHWSDVLVGLLQGALVAALTV
CYISDFFKARPPQHCLKEEELERKPSLSLTLTLGEADHNHYGYPHSSS
|
| Enzyme 19 Number of Residues |
288 |
| Enzyme 19 Molecular Weight |
32574 |
| Enzyme 19 Theoretical pI |
8.44 |
| Enzyme 19 GO Classification |
Not Available |
| Enzyme 19 General Function |
Lipid transport and metabolism |
| Enzyme 19 Specific Function |
Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1- phosphate (S-1-P). The relative catalytic efficiency is PA > C-1-P > LPA > S-1-P |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
Not Available |
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
3123896  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
O43688  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
LPP2_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>867 bp
ATGCAGCGGAGGTGGGTCTTCGTGCTGCTCGACGTGCTGTGCTTACTGGTCGCCTCCCTG
CCCTTCGCTATCCTGACGCTGGTGAACGCCCCGTACAAGCGAGGATTTTACTGCGGGGAT
GACTCCATCCGGTACCCCTACCGTCCAGATACCATCACCCACGGGCTCATGGCTGGGGTC
ACCATCACGGCCACCGTCATCCTTGTCTCGGCCGGGGAAGCCTACCTGGTGTACACAGAC
CGGCTCTATTCTCGCTCGGACTTCAACAACTACGTGGCTGCTGTATACAAGGTGCTGGGG
ACCTTCCTGTTTGGGGCTGCCGTGAGCCAGTCTCTGACAGACCTGGCCAAGTACATGATT
GGGCGTCTGAGGCCCAACTTCCTAGCCGTCTGCGACCCCGACTGGAGCCGGGTCAACTGC
TCGGTCTATGTGCAGCTGGAGAAGGTGTGCAGGGGAAACCCTGCTGATGTCACCGAGGCC
AGGTTGTCTTTCTACTCGGGACACTCTTCCTTTGGGATGTACTGCATGGTGTTCTTGGCG
CTGTATGTGCAGGCACGACTCTGTTGGAAGTGGGCACGGCTGCTGCGACCCACAGTCCAG
TTCTTCCTGGTGGCCTTTGCCCTCTACGTGGGCTACACCCGCGTGTCTGATTACAAACAC
CACTGGAGCGATGTCCTTGTTGGCCTCCTGCAGGGGGCACTGGTGGCTGCCCTCACTGTC
TGCTACATCTCAGACTTCTTCAAAGCCCGACCCCCACAGCACTGTCTGAAGGAGGAGGAG
CTGGAACGGAAGCCCAGCCTGTCACTGACGTTGACCCTGGGCGAGGCTGACCACAACCAC
TATGGATACCCGCACTCCTCCTCCTGA
|
| Enzyme 19 GenBank Gene ID |
AF035959  |
| Enzyme 19 GeneCard ID |
PPAP2C  |
| Enzyme 19 GenAtlas ID |
PPAP2C  |
| Enzyme 19 HGNC ID |
HGNC:9230  |
| Enzyme 19 Chromosome Location |
19 |
| Enzyme 19 Locus |
19p13 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Leung DW, Tompkins CK, White T: Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. DNA Cell Biol. 1998 Apr;17(4):377-85. [PubMed
]
- Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
5469 |
| Enzyme 20 Name |
Lipid phosphate phosphohydrolase 1 |
| Enzyme 20 Synonyms |
- Phosphatidic acid phosphatase 2a
- Phosphatidate phosphohydrolase type 2a
- PAP2a
- PAP- 2a
- PAP2-alpha
|
| Enzyme 20 Gene Name |
PPAP2A |
| Enzyme 20 Protein Sequence |
>Lipid phosphate phosphohydrolase 1
MFDKTRLPYVALDVLCVLLAGLPFAILTSRHTPFQRGVFCNDESIKYPYKEDTIPYALLG
GIIIPFSIIVIILGETLSVYCNLLHSNSFIRNNYIATIYKAIGTFLFGAAASQSLTDIAK
YSIGRLRPHFLDVCDPDWSKINCSDGYIEYYICRGNAERVKEGRLSFYSGHSSFSMYCML
FVALYLQARMKGDWARLLRPTLQFGLVAVSIYVGLSRVSDYKHHWSDVLTGLIQGALVAI
LVAVYVSDFFKERTSFKERKEEDSHTTLHETPTTGNHYPSNHQP
|
| Enzyme 20 Number of Residues |
284 |
| Enzyme 20 Molecular Weight |
32156 |
| Enzyme 20 Theoretical pI |
8.06 |
| Enzyme 20 GO Classification |
Not Available |
| Enzyme 20 General Function |
Lipid transport and metabolism |
| Enzyme 20 Specific Function |
Broad-specificity phosphohydrolase that dephosphorylates exogenous bioactive glycerolipids and sphingolipids. Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). Pivotal regulator of lysophosphatidic acid (LPA) signaling in the cardiovascular system. Major enzyme responsible of dephosphorylating LPA in platelets, which terminates signaling actions of LPA. May control circulating, and possibly also regulate localized, LPA levels resulting from platelet activation. It has little activity towards ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA > PA > S-1-P > C-1-P. It's down-regulation may contribute to the development of colon adenocarcinoma |
| Enzyme 20 Pathways |
|
| Enzyme 20 Reactions |
- A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
Not Available |
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
2467298  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
O14494  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
LPP1_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>855 bp
ATGTTCGACAAGACGCGGCTGCCGTACGTGGCCCTCGATGTGCTCTGCGTGTTGCTGGCT
GGATTGCCTTTTGCAATTCTTACTTCAAGGCATACCCCCTTCCAACGAGGAGTATTCTGT
AATGATGAGTCCATCAAGTACCCTTACAAAGAAGACACCATACCTTATGCGTTATTAGGT
GGAATAATCATTCCATTCAGTATTATCGTTATTATTCTTGGAGAAACCCTGTCTGTTTAC
TGTAACCTTTTGCACTCAAATTCCTTTATCAGGAATAACTACATAGCCACTATTTACAAA
GCCATTGGAACCTTTTTATTTGGTGCAGCTGCTAGTCAGTCCCTGACTGACATTGCCAAG
TATTCAATAGGCAGACTGCGGCCTCACTTCTTGGATGTTTGTGATCCAGATTGGTCAAAA
ATCAACTGCAGCGATGGTTACATTGAATACTACATATGTCGAGGGAATGCAGAAAGAGTT
AAGGAAGGCAGGTTGTCCTTCTATTCAGGCCACTCTTCGTTTTCCATGTACTGCATGCTG
TTTGTGGCACTTTATCTTCAAGCCAGGATGAAGGGAGACTGGGCAAGACTCTTACGCCCC
ACACTGCAATTTGGTCTTGTTGCCGTATCCATTTATGTGGGCCTTTCTCGAGTTTCTGAT
TATAAACACCACTGGAGCGATGTGTTGACTGGACTCATTCAGGGAGCTCTGGTTGCAATA
TTAGTTGCTGTATATGTATCGGATTTCTTCAAAGAAAGAACTTCTTTTAAAGAAAGAAAA
GAGGAGGACTCTCATACAACTCTGCATGAAACACCAACAACTGGGAATCACTATCCGAGC
AATCACCAGCCTTGA
|
| Enzyme 20 GenBank Gene ID |
AB000888  |
| Enzyme 20 GeneCard ID |
PPAP2A  |
| Enzyme 20 GenAtlas ID |
PPAP2A  |
| Enzyme 20 HGNC ID |
HGNC:9228  |
| Enzyme 20 Chromosome Location |
5 |
| Enzyme 20 Locus |
5q11 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Kai M, Wada I, Imai S, Sakane F, Kanoh H: Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. J Biol Chem. 1997 Sep 26;272(39):24572-8. [PubMed
]
- Leung DW, Tompkins CK, White T: Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. DNA Cell Biol. 1998 Apr;17(4):377-85. [PubMed
]
- Ulrix W, Swinnen JV, Heyns W, Verhoeven G: Identification of the phosphatidic acid phosphatase type 2a isozyme as an androgen-regulated gene in the human prostatic adenocarcinoma cell line LNCaP. J Biol Chem. 1998 Feb 20;273(8):4660-5. [PubMed
]
- Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
5474 |
| Enzyme 21 Name |
Lipid phosphate phosphohydrolase 3 |
| Enzyme 21 Synonyms |
- Phosphatidic acid phosphatase 2b
- Phosphatidate phosphohydrolase type 2b
- PAP2b
- PAP- 2b
- PAP2-beta
- Vascular endothelial growth factor and type I collagen-inducible protein
- VCIP
|
| Enzyme 21 Gene Name |
PPAP2B |
| Enzyme 21 Protein Sequence |
>Lipid phosphate phosphohydrolase 3
MQNYKYDKAIVPESKNGGSPALNNNPRRSGSKRVLLICLDLFCLFMAGLPFLIIETSTIK
PYHRGFYCNDESIKYPLKTGETINDAVLCAVGIVIAILAIITGEFYRIYYLKKSRSTIQN
PYVAALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLSVCNPDFSQINCSEGYIQNYR
CRGDDSKVQEARKSFFSGHASFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFY
TGLSRVSDHKHHPSDVLAGFAQGALVACCIVFFVSDLFKTKTTLSLPAPAIRKEILSPVD
IIDRNNHHNMM
|
| Enzyme 21 Number of Residues |
311 |
| Enzyme 21 Molecular Weight |
35116 |
| Enzyme 21 Theoretical pI |
9.40 |
| Enzyme 21 GO Classification |
Not Available |
| Enzyme 21 General Function |
Lipid transport and metabolism |
| Enzyme 21 Specific Function |
Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1- phosphate (S-1-P). The relative catalytic efficiency is LPA = PA > C-1-P > S-1-P. May be involved in cell adhesion and in cell-cell interactions |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
- 34-54
86-106
123-143
194-214
228-248
258-278
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
2467300  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
O14495  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
LPP3_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>936 bp
ATGCAAAACTACAAGTACGACAAAGCGATCGTCCCGGAGAGCAAGAACGGCGGCAGCCCG
GCGCTCAACAACAACCCGAGGAGGAGCGGCAGCAAGCGGGTGCTGCTCATCTGCCTCGAC
CTCTTCTGCCTCTTCATGGCGGGCCTCCCCTTCCTCATCATCGAGACAAGCACCATCAAG
CCTTACCACCGAGGGTTTTACTGCAATGATGAGAGCATCAAGTACCCACTGAAAACTGGT
GAGACAATAAATGACGCTGTGCTCTGTGCCGTGGGGATCGTCATTGCCATCCTCGCGATC
ATCACGGGGGAATTCTACCGGATCTATTACCTGAAGAAGTCGCGGTCGACGATTCAGAAC
CCCTACGTGGCAGCACTCTATAAGCAAGTGGGCTGCTTCCTCTTTGGCTGTGCCATCAGC
CAGTCTTTCACAGACATTGCCAAAGTGTCCATAGGGCGCCTGCGTCCTCACTTCTTGAGT
GTCTGCAACCCTGATTTCAGCCAGATCAACTGCTCTGAAGGCTACATTCAGAACTACAGA
TGCAGAGGTGATGACAGCAAAGTCCAGGAAGCCAGGAAGTCCTTCTTCTCTGGCCATGCC
TCCTTCTCCATGTACACTATGCTGTATTTGGTGCTATACCTGCAGGCCCGCTTCACTTGG
CGAGGAGCCCGCCTGCTCCGGCCCCTCCTGCAGTTCACCTTGATCATGATGGCCTTCTAC
ACGGGACTGTCTCGCGTATCAGACCACAAGCACCATCCCAGTGATGTTCTGGCAGGATTT
GCTCAAGGAGCCCTGGTGGCCTGCTGCATAGTTTTCTTCGTGTCTGACCTCTTCAAGACT
AAGACGACGCTCTCCCTGCCTGCCCCTGCTATCCGGAAGGAAATCCTTTCACCTGTGGAC
ATTATTGACAGGAACAATCACCACAACATGATGTAG
|
| Enzyme 21 GenBank Gene ID |
AB000889  |
| Enzyme 21 GeneCard ID |
PPAP2B  |
| Enzyme 21 GenAtlas ID |
PPAP2B  |
| Enzyme 21 HGNC ID |
HGNC:9229  |
| Enzyme 21 Chromosome Location |
1 |
| Enzyme 21 Locus |
1pter-p22.1 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Kai M, Wada I, Imai S, Sakane F, Kanoh H: Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. J Biol Chem. 1997 Sep 26;272(39):24572-8. [PubMed
]
- Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed
]
- Humtsoe JO, Feng S, Thakker GD, Yang J, Hong J, Wary KK: Regulation of cell-cell interactions by phosphatidic acid phosphatase 2b/VCIP. EMBO J. 2003 Apr 1;22(7):1539-54. [PubMed
]
- Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
5490 |
| Enzyme 22 Name |
Propionyl-CoA carboxylase beta chain, mitochondrial precursor |
| Enzyme 22 Synonyms |
- PCCase subunit beta
- Propanoyl-CoA:carbon dioxide ligase subunit beta
|
| Enzyme 22 Gene Name |
PCCB |
| Enzyme 22 Protein Sequence |
>Propionyl-CoA carboxylase beta chain, mitochondrial precursor
MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHK
RGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVY
VFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIF
LRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVT
QEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVP
ELDTIVPLESTKAYNMVDIIHSVVDEREFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPK
VASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFA
EATVPKVTVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVE
AAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL
|
| Enzyme 22 Number of Residues |
539 |
| Enzyme 22 Molecular Weight |
58216 |
| Enzyme 22 Theoretical pI |
7.69 |
| Enzyme 22 GO Classification |
| Function |
- catalytic activity
- ligase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 22 General Function |
Not Available |
| Enzyme 22 Specific Function |
ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl-CoA |
| Enzyme 22 Pathways |
- Propanoate Metabolism (map00640
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 22 Reactions |
- ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
Not Available |
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
312812  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
P05166  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
PCCB_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>1620 bp
ATGGCGGCGGCATTACGGGTGGCGGCGGTCGGGGCAAGGCTCAGCGTTCTGGCGAGCGGT
CTCCGCGCCGCGGTCCGCAGCCTTTGCAGCCAGGCCACCTCTGTTAACGAACGCATCGAA
AACAAGCGCCGGACCGCGCTGCTGGGAGGGGGCCAACGCCGTATTGACGCGCAGCACAAG
CGAGGAAAGCTAACAGCCAGGGAGAGGATCAGTCTCTTGCTGGACCCTGGCAGCTTTGTT
GAGAGCGACATGTTTGTGGAACACAGATGTGCAGATTTTGGAATGGCTGCTGACAAGAAT
AAGTTTCCTGGAGACAGCGTGGTCACTGGACGAGGCCGAATCAATGGAAGATTGGTTTAT
GTCTTCAGTCAGGATTTTACAGTTTTTGGAGGCAGTCTGTCAGGAGCACATGCCCAAAAG
ATCTGCAAAATCATGGACCAGGCCATAACGGTGGGGGCTCCAGTGATTGGGCTGAATGAC
TCTGGGGGAGCACGGATCCAAGAAGGAGTGGAGTCTTTGGCTGGCTATGCAGACATCTTT
CTGAGGAATGTTACGGCATCCGGAGTCATCCCTCAGATTTCTCTGATCATGGGCCCATGT
GCTGGTGGGGCCGTCTACTCCCCAGCCCTAACAGACTTCACGTTCATGGTAAAGGACACC
TCCTACCTGTTCATCACTGGCCCTGATGTTGTGAAGTCTGTCACCAATGAGGATGTTACC
CAGGAGGAGCTCGGTGGTGCCAAGACCCACACCACCATGTCAGGTGTGGCCCACAGAGCT
TTTGAAAATGATGTTGATGCCTTGTGTAATCTCCGGGATTTCTTCAACTACCTGCCCCTG
AGCAGTCAGGACCCGGCTTCCGTCCGTGAGTGCCACGATCCCAGTGACCGTCTGGTTCCT
GAGCTTGACACAATTGTCCCTTTGGAATCAACCAAAGCCTACAACATGGTGGACATCATA
CACTCTGTTGTTGATGAGCGTGAATTTTTTGAGATCATGCCCAATTATGCCAAGAACATC
ATTGTTGGTTTTGCAAGAATGAATGGGAGGACTGTTGGAATTGTTGGCAACCAACCTAAG
GTGGCCTCAGGATGCTTGGATATTAATTCATCTGTGAAAGGGGCTCGTTTTGTCAGATTC
TGTGATGCATTCAATATTCCACTCATCACTTTTGTTGATGTCCCTGGCTTTCTACCTGGC
ACAGCACAGGAATACGGGGGCATCATCCGGCATGGTGCCAAGCTTCTCTACGCATTTGCT
GAGGCAACTGTACCCAAAGTCACAGTCATCACCAGGAAGGCCTATGGAGGTGCCTATGAT
GTCATGAGCTCTAAGCACCTTTGTGGTGATACCAACTATGCCTGGCCCACCGCAGAGATT
GCAGTCATGGGAGCAAAGGGCGCTGTGGAGATCATCTTCAAAGGGCATGAGAATGTGGAA
GCTGCTCAGGCAGAGTACATCGAGAAGTTTGCCAACCCTTTCCCTGCAGCAGTGCGAGGG
TTTGTGGATGACATCATCCAACCTTCTTCCACACGTGCCCGAATCTGCTGTGACCTGGAT
GTCTTGGCCAGCAAGAAGGTACAACGTCCTTGGAGAAAACATGCAAATATTCCATTGTAA
|
| Enzyme 22 GenBank Gene ID |
X73424  |
| Enzyme 22 GeneCard ID |
PCCB  |
| Enzyme 22 GenAtlas ID |
PCCB  |
| Enzyme 22 HGNC ID |
HGNC:8654  |
| Enzyme 22 Chromosome Location |
3 |
| Enzyme 22 Locus |
3q21-q22 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Lamhonwah AM, Leclerc D, Loyer M, Clarizio R, Gravel RA: Correction of the metabolic defect in propionic acidemia fibroblasts by microinjection of a full-length cDNA or RNA transcript encoding the propionyl-CoA carboxylase beta subunit. Genomics. 1994 Feb;19(3):500-5. [PubMed
]
- Ohura T, Ogasawara M, Ikeda H, Narisawa K, Tada K: The molecular defect in propionic acidemia: exon skipping caused by an 8-bp deletion from an intron in the PCCB allele. Hum Genet. 1993 Oct;92(4):397-402. [PubMed
]
- Rodriguez-Pombo P, Hoenicka J, Muro S, Perez B, Perez-Cerda C, Richard E, Desviat LR, Ugarte M: Human propionyl-CoA carboxylase beta subunit gene: exon-intron definition and mutation spectrum in Spanish and Latin American propionic acidemia patients. Am J Hum Genet. 1998 Aug;63(2):360-9. [PubMed
]
- Lamhonwah AM, Barankiewicz TJ, Willard HF, Mahuran DJ, Quan F, Gravel RA: Isolation of cDNA clones coding for the alpha and beta chains of human propionyl-CoA carboxylase: chromosomal assignments and DNA polymorphisms associated with PCCA and PCCB genes. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4864-8. [PubMed
]
- Tahara T, Kraus JP, Rosenberg LE: An unusual insertion/deletion in the gene encoding the beta-subunit of propionyl-CoA carboxylase is a frequent mutation in Caucasian propionic acidemia. Proc Natl Acad Sci U S A. 1990 Feb;87(4):1372-6. [PubMed
]
- Tahara T, Kraus JP, Ohura T, Rosenberg LE, Fenton WA: Three independent mutations in the same exon of the PCCB gene: differences between Caucasian and Japanese propionic acidaemia. J Inherit Metab Dis. 1993;16(2):353-60. [PubMed
]
- Muro S, Rodriguez-Pombo P, Perez B, Perez-Cerda C, Desviat LR, Sperl W, Skladal D, Sass JO, Ugarte M: Identification of novel mutations in the PCCB gene in European propionic acidemia patients. Mutation in brief no. 253. Online. Hum Mutat. 1999;14(1):89-90. [PubMed
]
- Ugarte M, Perez-Cerda C, Rodriguez-Pombo P, Desviat LR, Perez B, Richard E, Muro S, Campeau E, Ohura T, Gravel RA: Overview of mutations in the PCCA and PCCB genes causing propionic acidemia. Hum Mutat. 1999;14(4):275-82. [PubMed
]
- Perez B, Desviat LR, Rodriguez-Pombo P, Clavero S, Navarrete R, Perez-Cerda C, Ugarte M: Propionic acidemia: identification of twenty-four novel mutations in Europe and North America. Mol Genet Metab. 2003 Jan;78(1):59-67. [PubMed
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
5595 |
| Enzyme 23 Name |
Carbamoyl-phosphate synthase [ammonia], mitochondrial precursor |
| Enzyme 23 Synonyms |
- Carbamoyl-phosphate synthetase I
- CPSase I
|
| Enzyme 23 Gene Name |
CPS1 |
| Enzyme 23 Protein Sequence |
>Carbamoyl-phosphate synthase [ammonia], mitochondrial precursor
MTRILTAFKVVRTLKTGFGFTNVTAHQKWKFSRPGIRLLSVKAQTAHIVLEDGTKMKGYS
FGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTTALDELGLSKY
LESNGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTML
GKIEFEGQPVDFVDPNKQNLIAEVSTKDVKVYGKGNPTKVVAVDCGIKNNVIRLLVKRGA
EVHLVPWNHDFTKMEYDGILIAGGPGNPALAEPLIQNVRKILESDRKEPLFGISTGNLIT
GLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALDNTLPAGWKPLFVNVNDQT
NEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKKGKATTITSVLPKPALVASRV
EVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEVGLKQAD
TVYFLPITPQFVTEVIKAEQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVES
IMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMIRSAYALGGLGSGIC
PNRETLMDLSTKAFAMTNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHT
GDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLS
RSSALASKATGYPLAFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDR
FHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSIEGFTPRLPMNKEWPSNLDLR
KELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNSESMT
EETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYV
TYNGQEHDVNFDDHGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETV
STDFDECDKLYFEELSLERILDIYHQEACGGCIISVGGQIPNNLAVPLYKNGVKIMGTSP
LQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMN
VVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVGKDGRVISHAISEHVEDAG
VHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRA
SRSFPFVSKTLGVDFIDVATKVMIGENVDEKHLPTLDHPIIPADYVAIKAPMFSWPRLRD
ADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKGILIGIQQSFRPRFLGVAEQ
LHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPN
NNTKFVHDNYVIRRTAVDSGIPLLTNFQVTKLFAEAVQKSRKVDSKSLFHYRQYSAGKAA
|
| Enzyme 23 Number of Residues |
1500 |
| Enzyme 23 Molecular Weight |
164941 |
| Enzyme 23 Theoretical pI |
6.71 |
| Enzyme 23 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- carbamoyl-phosphate synthase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleotide binding
- purine nucleotide binding
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- arginine biosynthesis
- arginine metabolism
- cellular metabolism
- glutamine family amino acid metabolism
- glutamine metabolism
- metabolism
- nitrogen compound metabolism
- nucleobase metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- pyrimidine base biosynthesis
- pyrimidine base metabolism
- urea cycle intermediate metabolism
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 23 General Function |
Amino acid transport and metabolism |
| Enzyme 23 Specific Function |
Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell |
| Enzyme 23 Pathways |
|
| Enzyme 23 Reactions |
- 2 ATP + NH3 + CO2 + H2O = 2 ADP + phosphate + carbamoyl phosphate
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
Not Available |
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
219553  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
P31327  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
CPSM_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>4503 bp
ATGACGAGGATTTTGACAGCTTTCAAAGTGGTGAGGACACTGAAGACTGGTTTTGGCTTT
ACCAATGTGACTGCACACCAAAAATGGAAATTTTCAAGACCTGGCATCAGGCTCCTTTCT
GTCAAGGCACAGACAGCACACATTGTCCTGGAAGATGGAACTAAGATGAAAGGTTACTCC
TTTGGCCATCCATCCTCTGTTGCTGGTGAAGTGGTTTTTAATACTGGCCTGGGAGGGTAC
CCAGAAGCTATTACTGACCCTGCCTACAAAGGACAGATTCTCACAATGGCCAACCCTATT
ATTGGGAATGGTGGAGCTCCTGATACTACTTCTCTGGATGAACTGGGACTTAGCAAATAT
TTGGAGTCTAATGGAATCAAGGTTTCAGGTTTGCTGGTGCTGGATTATAGTAAAGACTAC
AACCACTGGCTGGCTACCAAGAGTTTAGGGCAATGGCTACAGGAAGAAAAGGTTCCTGCA
ATTTATGGAGTGGACACAAGAATGCTGACTAAAATAATTCGGGATAAGGGTACCATGCTT
GGGAAGATTGAATTTGAAGGTCAGCCTGTGGATTTTGTGGATCCAAATAAACAGAATTTG
ATTGCTGAGGTTTCAACCAAGGATGTCAAAGTGTACGGCAAAGGAAACCCCACAAAAGTG
GTAGCTGTAGACTGTGGGATTAAAAACAATGTAATCCGCCTGCTAGTAAAGCGAGGAGCT
GAAGTGCACTTAGTTCCCTGGAACCATGATTTCACCAAGATGGAGTATGATGGGATTTTG
ATCGCGGGAGGACCGGGGAACCCAGCTCTTGCAGAACCACTAATTCAGAATGTTCAGAAG
ATTTTGGAGAGTGATCGCAAGGAGCCATTGTTTGGAATCAGTACAGGAAACTTAATAACA
GGATTGGCTGCTGGTGCCAAAACCTACAAGATGTCCATGGCCAACAGAGGGCAGAATCAG
CCTGTTTTGAATATCACAAACAAACAGGCTTTCATTACTGCTCAGAATCATTGCTATGCC
TTGGACAACACCCTCCCTGCTGGCTGGAAACCACTTTTTGTGAATGTCAACGATCAAACA
AATGAGGGGATTATGCATGAGAGCAAACCCTTCTTCGCTGTGCAGTTCCACCCAGAGGTC
ACCCCGGGGCCAATAGACACTGAGTACCTGTTTGATTCCTTTTTCTCACTGATAAAGAAA
GGAAAAGCTACCACCATTACATCAGTCTTACCGAAGCCAGCACTAGTTGCATCTCGGGTT
GAGGTTTCCAAAGTCCTTATTCTAGGATCAGGAGGTCTGTCCATTGGTCAGGCTGGAGAA
TTTGATTACTCAGGATCTCAAGCTGTAAAAGCCATGAAGGAAGAAAATGTCAAAACTGTT
CTGATGAACCCAAACATTGCATCAGTCCAGACCAATGAGGTGGGCTTAAAGCAAGCGGAT
ACTGTCTACTTTCTTCCCATCACCCCTCAGTTTGTCACAGAGGTCATCAAGGCAGAACAG
CCAGATGGGTTAATTCTGGGCATGGGTGGCCAGACAGCTCTGAACTGTGGAGTAGAACTA
TTCAAGAGAGGTGTGCTCAAGGAATATGGTGTGAAAGTCCTGGGAACTTCAGTTGAGTCC
ATTATGGCTACGGAAGACAGGCAGCTGTTTTCAGATAAACTAAATGAGATCAATGAAAAG
ATTGCTCCAAGTTTTGCAGTGGAATCGATTGAGGATGCACTGAAGGCAGCAGACACCATT
GGCTACCCAGTGATGATCCGTTCCGCCTATGCACTGGGTGGGTTAGGCTCAGGCATCTGT
CCCAACAGAGAGACTTTGATGGACCTCAGCACAAAGGCCTTTGCTATGACCAACCAAATT
CTGGTGGAGAAGTCAGTGACAGGTTGGAAAGAAATAGAATATGAAGTGGTTCGAGATGCT
GATGACAATTGTGTCACTGTCTGTAACATGGAAAATGTTGATGCCATGGGTGTTCACACA
GGTGACTCAGTTGTTGTGGCTCCTGCCCAGACACTCTCCAATGCCGAGTTTCAGATGTTG
AGACGTACTTCAATCAATGTTGTTCGCCACTTGGGCATTGTGGGTGAATGCAACATTCAG
TTTGCCCTTCATCCTACCTCAATGGAATACTGCATCATTGAAGTGAATGCCAAGATGTCC
CCGAACTCTGCTCTGGCCTCCAAAACGACTGGCTACCCATTGGCATTCATTGCTGCAAAG
ATTGCCCTAGGAATCCCACTTCCAGGAATTAAGAACGTCGTATCCGGGAAGACATCAGCC
TGTTTTGAACCTAGCCTGGATTACATGGTCACCAAGATTCCCCGCTGGGATCTTGACCGT
TTTCATGGAACATCTAGCCGAATTGGTAGCTCTATGAAAAGTGTAGGAGAGGTCATGGCT
ATTGGTCGTACCTTTGAGGAGAGTTTCCAGAAAGCTTTACGGATGTGCCACCCATCTATA
GAGGGTTTCACTCCCCGTCTCCCAATGAACAAAGAATGGCCATCGAATTTAGATCTTAGA
AAAGAGTTGTCTGAACCAAGCAGCACGCGTATCTATGCCATTGCCAAGGCCATTGATGAC
AACATGTCCCTTGATGAGATTGAGAAGCTCACATACATTGACAAGTGGTTTTTGTATAAG
ATGCGTGATATTTTAAACATGGAAAAGACACTGAAAGGCCTCAACAGTGAGTCCATGACA
GAAGAAACCCTGAAAAGGGCAAAGGAGATTGGGTTCTCAGATAAGCAGATTTCAAAATGC
CTTGGGCTCACTGAGGCCCAGACAAGGGAGCTGAGGTTAAAGAAAAACATCCACCCTTGG
GTTAAACAGATTGATACACTGGCTGCAGAATACCCATCAGTAACAAACTATCTCTATGTT
ACCTACAATGGTCAGGAGCATGATGTCAATTTTGATGACCATGGAATGATGGTGCTAGGC
TGTGGTCCATATCACATTGGCAGCAGTGTGGAATTTGATTGGTGTGCTGTCTCTAGTATC
CGCACACTGCGTCAACTTGGCAAGAAGACGGTGGTGGTGAATTGCAATCCTGAGACTGTG
AGCACAGACTTTGATGAGTGTGACAAACTGTACTTTGAAGAGTTGTCCTTGGAGAGAATC
CTAGACATCTACCATCAGGAGGCATGTGGTGGCTGCATCATATCAGTTGGAGGCCAGATT
CCAAACAACCTGGCAGTTCCTCTATACAAGAATGGTGTCAAGATCATGGGCACAAGCCCC
CTGCAGATCGACAGGGCTGAGGATCGCTCCATCTTCTCAGCTGTCTTGGATGAGCTGAAG
GTGGCTCAGGCACCTTGGAAAGCTGTTAATACTTTGAATGAAGCACTGGAATTTGCAAAG
TCTGTGGACTACCCCTGCTTGTTGAGGCCTTCCTATGTTTTGAGTGGGTCTGCTATGAAT
GTGGTATTCTCTGAGGATGAGATGAAAAAATTCCTAGAAGAGGCGACTAGAGTTTCTCAG
GCCACGCCAGTGGTGCTGACAAAATTTGTTGAAGGGGCCCGAGAAGTAGAAATGGACGCT
GTTGGCAAAGATGGAAGGGTTATCTCTCATGCCATCTCTGAACATGTTGAAGATGCAGGT
GTCCACTCGGAGAATGCCACTCTGATGCTGCCCACACAAACCATCAGCCAAGGGGCCATT
GAAAAGGTGAAGGATGCTACCCGGAAGATTGCAAAGGCTTTTGCCATCTCTGGTCCATTC
AACGTCCAATTTCTTGTCAAAGGAAATGATGTCTTGGTGAATGAGTGTAACTTGAGAGCT
TCTCGATCCTTCCCCTCTGTTTCCAAGACTCTTGGGGTTGACTTCATTGATGTGGCCACC
AAGGTGTTGATTGGAGAGAATGTTGATGAGAAACATCTTCCAACATTGGACCATCCCATA
ATTCCTGTTGACTATGTTGCAATTAAGGCTCCCATGTTTTCCTGGCCCCGGTTGAGGGAT
GCTGACCCCATTCTGAGATGTGAGATGGCTTCCACTGGAGAGGTGGCTTGCTTTGGTGAA
GGTATTCATACAGCCTTCCTAAAGGCAATGCTTTCCACAGGATTTAAGATACCCCAGAAA
GGCATCCTGATAGGCATCCAGCAATCATTCCGGCCAAGATTCCTTGGTGTGGCTGAACAA
TTACACAATGAAGGTTTCAAGCTGTTTGCCACGGAAGCCACATCAGACTGGCTCAACGCC
AACAATGTCCCTGCCAACCCAGTGGCATGGCCGTCTCAAGAAGGACAGAATCCCAGCCTC
TCTTCCATCAGAAAATTGATTAGAGATGGCAGCATTGACCTAGTGATTAACCTTCCCAAC
AACAACACTAAATTTGTCCATGATAATTATGTGATTCGGAGGACAGCTGTTGATAGTGGA
ATCCCTCTCCTCACTAATTTTCAGGTGACCAAACTTTTTGCTGAAGCTGTGCAGAAATCT
CGCAAGGTGGACTCCAAGAGTCTTTTCCACTACAGGCAGTACAGTGCTGGAAAAGCAGCA
TAG
|
| Enzyme 23 GenBank Gene ID |
D90282  |
| Enzyme 23 GeneCard ID |
CPS1  |
| Enzyme 23 GenAtlas ID |
CPS1  |
| Enzyme 23 HGNC ID |
HGNC:2323  |
| Enzyme 23 Chromosome Location |
2 |
| Enzyme 23 Locus |
2q35 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Haraguchi Y, Uchino T, Takiguchi M, Endo F, Mori M, Matsuda I: Cloning and sequence of a cDNA encoding human carbamyl phosphate synthetase I: molecular analysis of hyperammonemia. Gene. 1991 Nov 15;107(2):335-40. [PubMed
]
- Finckh U, Kohlschutter A, Schafer H, Sperhake K, Colombo JP, Gal A: Prenatal diagnosis of carbamoyl phosphate synthetase I deficiency by identification of a missense mutation in CPS1. Hum Mutat. 1998;12(3):206-11. [PubMed
]
- Funghini S, Donati MA, Pasquini E, Zammarchi E, Morrone A: Structural organization of the human carbamyl phosphate synthetase I gene (CPS1) and identification of two novel genetic lesions. Hum Mutat. 2003 Oct;22(4):340-1. [PubMed
]
- Aoshima T, Kajita M, Sekido Y, Kikuchi S, Yasuda I, Saheki T, Watanabe K, Shimokata K, Niwa T: Novel mutations (H337R and 238-362del) in the CPS1 gene cause carbamoyl phosphate synthetase I deficiency. Hum Hered. 2001;52(2):99-101. [PubMed
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
5597 |
| Enzyme 24 Name |
Type I inositol-1,4,5-trisphosphate 5-phosphatase |
| Enzyme 24 Synonyms |
- 5PTase
|
| Enzyme 24 Gene Name |
INPP5A |
| Enzyme 24 Protein Sequence |
>Type I inositol-1,4,5-trisphosphate 5-phosphatase
MAGKAAAPGTAVLLVTANVGSLFDDPENLQKNWLREFYQVVHTHKPHFMALHCQEFGGKN
YEASMSHVDKFVKELLSSDAMKEYNRARVYLDENYKSQEHFTALGSFYFLHESLKNIYQF
DFKAKKYRKVAGKEIYSDTLESTPMLEKEKFPQDYFPECKWSRKGFIRTRWCIADCAFDL
VNIHLFHDASNLVAWETSPSVYSGIRHKALGYVLDRIIDQRFEKVSYFVFGDFNFRLDSK
SVVETLCTKATMQTVRAADTNEVVKLIFRESDNDRKVMLQLEKKLFDYFNQEVFRDNNGT
ALLEFDKELSVFKDRLYELDISFPPSYPYSEDARQGEQYMNTRCPAWCDRILMSPSAKEL
VLRSESEEKVVTYDHIGPNVCMGDHKPVFLAFRIMPGAGKPHAHVHKCCVVQ
|
| Enzyme 24 Number of Residues |
412 |
| Enzyme 24 Molecular Weight |
47820 |
| Enzyme 24 Theoretical pI |
7.04 |
| Enzyme 24 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 24 General Function |
Not Available |
| Enzyme 24 Specific Function |
Major isoenzyme hydrolyzing the calcium-mobilizing second messenger Ins(1,4,5)P3, this is a signal-terminating reaction |
| Enzyme 24 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 24 Reactions |
- (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate
- (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
Not Available |
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
556769  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q14642  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
I5P1_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>1239 bp
ATGGCGGGGAAGGCGGCCGCCCCGGGCACCGCGGTGCTGCTGGTCACGGCCAACGTGGGC
TCGCTCTTCGACGACCCAGAAAACCTGCAGAAGAACTGGCTTCGGGAATTTTACCAGGTC
GTGCACACACACAAGCCGCACTTCATGGCCTTGCACTGTCAGGAGTTTGGAGGGAAGAAC
TACGAGGCCTCCATGTCCCACGTGGACAAGTTCGTCAAAGAACTATTGTCGAGTGATGCG
ATGAAAGAATATAACAGGGCTCGAGTCTACCTGGATGAAAACTACAAATCCCAGGAGCAC
TTCACGGCACTAGGAAGCTTTTATTTTCTTCATGAGTCCTTAAAAAACATCTACCAGTTT
GACTTTAAAGCTAAGAAGTATAGAAAGGTCGCTGGCAAAGAGATCTACTCGGATACCTTA
GAGAGCACGCCCATGCTGGAGAAGGAGAAGTTTCCGCAGGACTACTTCCCCGAGTGCAAA
TGGTCAAGAAAAGGCTTCATCCGGACGAGGTGGTGCATTGCAGACTGTGCCTTTGACTTG
GTGAATATCCATCTTTTCCATGATGCTTCCAATCTGGTCGCCTGGGAAACAAGCCCTTCC
GTGTACTCGGGAATCCGGCACAAGGCACTGGGCTACGTGCTGGACAGAATCATTGATCAG
CGATTCGAGAAGGTTTCCTACTTTGTATTTGGTGATTTCAACTTCCGGCTGGATTCCAAG
TCCGTCGTGGAGACGCTCTGCACAAAAGCCACCATGCAGACGGTCCGGGCCGCCGACACC
AATGAAGTGGTGAAGCTCATATTTCGTGAGTCGGACAACGACCGGAAGGTTATGCTCCAG
TTAGAAAAGAAACTCTTCGACTACTTCAACCAGGAGGTTTTCCGAGACAACAACGGCACC
GCGCTCTTGGAGTTTGACAAGGAGTTGTCTGTCTTTAAGGACAGACTGTATGAACTGGAC
ATCTCGTTCCCTCCCAGCTACCCGTACAGTGAGGACGCCCGCCAGGGTGAGCAGTACATG
AACACCCGGTGCCCAGCCTGGTGTGACCGCATCCTCATGTCCCCGTCTGCCAAGGAGCTG
GTGCTGCGGTCGGAGAGCGAGGAGAAGGTTGTCACCTATGACCACATTGGGCCCAACGTC
TGCATGGGAGACCACAAGCCCGTGTTCCTGGCCTTCCGAATCATGCCCGGGGCAGGTAAA
CCTCATGCCCATGTGCACAAGTGTTGTGTCGTGCAGTGA
|
| Enzyme 24 GenBank Gene ID |
X77567  |
| Enzyme 24 GeneCard ID |
INPP5A  |
| Enzyme 24 GenAtlas ID |
INPP5A  |
| Enzyme 24 HGNC ID |
HGNC:6076  |
| Enzyme 24 Chromosome Location |
10 |
| Enzyme 24 Locus |
10q26.3 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- De Smedt F, Verjans B, Mailleux P, Erneux C: Cloning and expression of human brain type I inositol 1,4,5-trisphosphate 5-phosphatase. High levels of mRNA in cerebellar Purkinje cells. FEBS Lett. 1994 Jun 20;347(1):69-72. [PubMed
]
- Laxminarayan KM, Chan BK, Tetaz T, Bird PI, Mitchell CA: Characterization of a cDNA encoding the 43-kDa membrane-associated inositol-polyphosphate 5-phosphatase. J Biol Chem. 1994 Jun 24;269(25):17305-10. [PubMed
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
5598 |
| Enzyme 25 Name |
Inositol polyphosphate 1-phosphatase |
| Enzyme 25 Synonyms |
- IPPase
- IPP
|
| Enzyme 25 Gene Name |
INPP1 |
| Enzyme 25 Protein Sequence |
>Inositol polyphosphate 1-phosphatase
MSDILRELLCVSEKAANIARACRQQEALFQLLIEEKKEGEKNKKFAVDFKTLADVLVQEV
IKQNMENKFPGLEKNIFGEESNEFTNDWGEKITLRLCSTEEETAELLSKVLNGNKVASEA
LARVVHQDVAFTDPTLDSTEINVPQDILGIWVDPIDSTYQYIKGSADIKSNQGIFPCGLQ
CVTILIGVYDIQTGVPLMGVINQPFVSRDPNTLRWKGQCYWGLSYMGTNMHSLQLTISRR
NGSETHTGNTGSEAAFSPSFSAVISTSEKETIKAALSRVCGDRIFGAAGAGYKSLCVVQG
LVDIYIFSEDTTFKWDSCAAHAILRAMGGGIVDLKECLERNPETGLDLPQLVYHVENEGA
AGVDRWANKGGLIAYRSRKRLETFLSLLVQNLAPAETHT
|
| Enzyme 25 Number of Residues |
399 |
| Enzyme 25 Molecular Weight |
43998 |
| Enzyme 25 Theoretical pI |
4.91 |
| Enzyme 25 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 25 General Function |
Inorganic ion transport and metabolism |
| Enzyme 25 Specific Function |
1D-myo-inositol 1,4-bisphosphate + H(2)O = 1D- myo-inositol 4-phosphate + phosphate |
| Enzyme 25 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 25 Reactions |
- 1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
186426  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
P49441  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
INPP_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>1200 bp
ATGTCAGATATCCTCCGGGAGCTGCTCTGTGTCTCTGAGAAGGCTGCTAACATTGCCCGG
GCGTGCAGACAGCAGGAAGCCCTCTTCCAGCTGCTGATCGAAGAAAAGAAAGAGGGAGAA
AAGAACAAGAAGTTTGCAGTTGACTTCAAGACTCTGGCTGATGTACTGGTACAGGAAGTT
ATAAAACAGAATATGGAGAACAAGTTTCCAGGCTTGGAAAAAAATATTTTTGGAGAAGAA
TCCAATGAGTTTACTAATGACTGGGGGGAAAAGATTACCTTGAGGTTGTGTTCAACAGAG
GAAGAAACAGCAGAGCTTCTTAGCAAAGTCCTCAATGGTAACAAGGTAGCATCTGAAGCA
TTAGCCAGGGTTGTTCATCAGGATGTTGCCTTTACTGACCCAACTCTGGATTCCACAGAG
ATCAATGTTCCACAGGACATTTTGGGAATTTGGGTGGACCCCATAGATTCAACTTATCAG
TATATAAAAGGTTCTGCTGACATTAAATCCAACCAGGGAATCTTCCCCTGTGGACTTCAG
TGTGTCACCATTTTAATTGGTGTCTATGACATACAGACAGGGGTTCCCCTGATGGGAGTC
ATCAATCAACCTTTTGTGTCACGAGATCCAAACACCCTCAGGTGGAAAGGACAGTGCTAT
TGGGGCCTTTCTTACATGGGGACCAACATGCATTCACTACAGCTCACCATCTCTAGAAGA
AACGGCAGTGAAACACACACTGGAAACACCGGCTCTGAGGCAGCATTCTCCCCCAGTTTT
TCAGCCGTAATTAGTACAAGTGAAAAGGAGACTATCAAAGCTGCATTGTCACGTGTGTGT
GGAGATCGCATATTTGGGGCAGCTGGGGCTGGTTATAAGAGCCTATGTGTTGTCCAAGGC
CTCGTTGACATTTACATCTTTTCAGAAGATACCACATTCAAATGGGACTCTTGTGCTGCT
CATGCCATACTGCGGGCCATGGGTGGGGGAATAGTAGACTTGAAAGAATGCTTAGAAAGA
AATCCAGAAACAGGGCTTGATTTGCCACAGTTGGTGTACCACGTGGAAAATGAGGGTGCT
GCTGGGGTGGATCGGTGGGCCAACAAGGGAGGACTCATTGCATACAGATCCAGGAAGCGG
CTGGAGACATTCCTGAGCCTCCTGGTCCAAAACCTGGCACCTGCAGAGACGCATACCTAG
|
| Enzyme 25 GenBank Gene ID |
L08488  |
| Enzyme 25 GeneCard ID |
INPP1  |
| Enzyme 25 GenAtlas ID |
INPP1  |
| Enzyme 25 HGNC ID |
HGNC:6071  |
| Enzyme 25 Chromosome Location |
2 |
| Enzyme 25 Locus |
2q32 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- York JD, Veile RA, Donis-Keller H, Majerus PW: Cloning, heterologous expression, and chromosomal localization of human inositol polyphosphate 1-phosphatase. Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5833-7. [PubMed
]
- Lovlie R, Gulbrandsen AK, Molven A, Steen VM: Genomic structure and sequence analysis of a human inositol polyphosphate 1-phosphatase gene (INPP1). Pharmacogenetics. 1999 Aug;9(4):517-28. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
5600 |
| Enzyme 26 Name |
Skeletal muscle and kidney-enriched inositol phosphatase |
| Enzyme 26 Synonyms |
Not Available |
| Enzyme 26 Gene Name |
SKIP |
| Enzyme 26 Protein Sequence |
>Skeletal muscle and kidney-enriched inositol phosphatase
MSSRKLSGPKGRRLSIHVVTWNVASAAPPLDLSDLLQLNNRNLNLDIYVIGLQELNSGII
SLLSDAAFNDSWSSFLMDVLSPLSFIKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPT
GLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHFDRILEMQNCEGRDIPN
ILDHDLIIWFGDMNFRIEDFGLHFVRESIKNRCYGGLWEKDQLSIAKKHDPLLREFQEGR
LLFPPTYKFDRNSNDYDTSEKKRKPAWTDRILWRLKRQPCAGPDTPIPPASHFSLSLRGY
SSHMTYGISDHKPVSGTFDLELKPLVSAPLIVLMPEDLWTVENDMMVSYSSTSDFPSSPW
DWIGLYKVGLRDVNDYVSYAWVGDSKVSCSDNLNQVYIDISNIPTTEDEFLLCYYSNSLR
SVVGISRPFQIPPGSLREDPLGEAQPQI
|
| Enzyme 26 Number of Residues |
448 |
| Enzyme 26 Molecular Weight |
51091 |
| Enzyme 26 Theoretical pI |
6.51 |
| Enzyme 26 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 26 General Function |
Not Available |
| Enzyme 26 Specific Function |
Inositol 5-phosphatase which acts on inositol 1,4,5- trisphosphate, inositol 1,3,4,5-tetrakisphosphate, phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-triphosphate. Has 6-fold higher affinity for phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5- trisphosphate. May negatively regulate assembly of the actin cytoskeleton |
| Enzyme 26 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 26 Reactions |
- (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate
- (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
Not Available |
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
7209855  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
Q9BT40  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
SKIP_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>1347 bp
ATGAGCTCGCGGAAGCTGAGCGGGCCGAAAGGCAGGAGGCTCAGCATACACGTCGTGACT
TGGAACGTGGCTTCGGCAGCGCCCCCTCTAGATCTCAGTGACCTGCTTCAGCTGAACAAC
CGGAACCTCAATCTTGACATATATGTTATTGGTTTGCAGGAATTGAACTCTGGGATCATA
AGCCTCCTTTCCGATGCTGCCTTTAATGACTCGTGGAGCAGTTTCCTCATGGATGTGCTT
TCCCCTCTGAGCTTCATCAAGGTCTCCCATGTCCGTATGCAGGGGATCCTCTTACTGGTC
TTTGCCAAGTATCAGCATTTGCCCTATATCCAGATTCTGTCTACTAAATCCACCCCCACT
GGCCTGTTTGGGTACTGGGGGAACAAAGGTGGAGTCAACATCTGCCTGAAGCTTTATGGC
TACTATGTCAGCATCATCAACTGCCACCTGCCTCCCCACATTTCCAACAATTACCAGCGG
CTGGAGCACTTTGACCGGATCCTGGAGATGCAGAATTGTGAGGGGCGAGACATCCCAAAC
ATCCTGGACCACGACCTCATTATCTGGTTTGGAGACATGAACTTTCGGATCGAGGACTTT
GGGTTGCACTTTGTTCGGGAATCCATTAAAAATCGGTGCTACGGTGGCCTGTGGGAGAAG
GACCAGCTCAGCATTGCCAAGAAACATGACCCGCTGCTCCGGGAGTTCCAGGAGGGCCGC
CTACTCTTCCCGCCCACCTACAAGTTTGATAGGAACTCCAACGACTATGACACCAGTGAG
AAAAAACGCAAGCCTGCATGGACCGATCGCATCCTGTGGAGGCTGAAGCGGCAGCCCTGT
GCTGGCCCCGACACTCCCATACCGCCGGCGTCACACTTCTCCTTGTCTCTGAGGGGCTAC
AGCAGCCACATGACGTACGGCATCAGCGACCACAAGCCTGTCTCCGGCACGTTCGACTTG
GAGCTGAAGCCATTGGTGTCTGCTCCGCTGATCGTCCTGATGCCCGAGGACCTGTGGACC
GTGGAAAATGACATGATGGTCAGCTACTCTTCAACCTCGGACTTCCCCAGCAGCCCGTGG
GACTGGATTGGACTGTACAAGGTGGGGCTGCGGGACGTTAATGACTACGTGTCCTATGCC
TGGGTCGGGGACAGCAAGGTCTCCTGCAGCGACAACCTGAACCAGGTTTACATCGACATC
AGCAATATCCCTACCACTGAAGATGAGTTTCTCCTCTGTTACTACAGAAACAGTCTGCGT
TCTGTGGTGGGGATAAGAAGACCCTTCCAGATCCCGCCTGGCTCCTTGAGGGAGGACCCA
CTGGGTGAAGCACAGCCACAGATCTGA
|
| Enzyme 26 GenBank Gene ID |
AB036829  |
| Enzyme 26 GeneCard ID |
Not Available |
| Enzyme 26 GenAtlas ID |
Not Available |
| Enzyme 26 HGNC ID |
Not Available |
| Enzyme 26 Chromosome Location |
17 |
| Enzyme 26 Locus |
17p13.3 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- Ijuin T, Mochizuki Y, Fukami K, Funaki M, Asano T, Takenawa T: Identification and characterization of a novel inositol polyphosphate 5-phosphatase. J Biol Chem. 2000 Apr 14;275(15):10870-5. [PubMed
]
- Gurung R, Tan A, Ooms LM, McGrath MJ, Huysmans RD, Munday AD, Prescott M, Whisstock JC, Mitchell CA: Identification of a novel domain in two mammalian inositol-polyphosphate 5-phosphatases that mediates membrane ruffle localization. The inositol 5-phosphatase skip localizes to the endoplasmic reticulum and translocates to membrane ruffles following epidermal growth factor stimulation. J Biol Chem. 2003 Mar 28;278(13):11376-85. Epub 2003 Jan 20. [PubMed
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
5601 |
| Enzyme 27 Name |
Lactase-phlorizin hydrolase precursor |
| Enzyme 27 Synonyms |
- Lactase-glycosylceramidase[Includes: Lactase
|
| Enzyme 27 Gene Name |
LCT |
| Enzyme 27 Protein Sequence |
>Lactase-phlorizin hydrolase precursor
MELSWHVVFIALLSFSCWGSDWESDRNFISTAGPLTNDLLHNLSGLLGDQSSNFVAGDKD
MYVCHQPLPTFLPEYFSSLHASQITHYKVFLSWAQLLPAGSTQNPDEKTVQCYRRLLKAL
KTARLQPMVILHHQTLPASTLRRTEAFADLFADYATFAFHSFGDLVGIWFTFSDLEEVIK
ELPHQESRASQLQTLSDAHRKAYEIYHESYAFQGGKLSVVLRAEDIPELLLEPPISALAQ
DTVDFLSLDLSYECQNEASLRQKLSKLQTIEPKVKVFIFNLKLPDCPSTMKNPASLLFSL
FEAINKDQVLTIGFDINEFLSCSSSSKKSMSCSLTGSLALQPDQQQDHETTDSSPASAYQ
RVWEAFANQSRAERDAFLQDTFPEGFLWGASTGAFNVEGGWAEGGRGVSIWDPRRPLNTT
EGQATLEVASDSYHKVASDVALLCGLRAQVYKFSISWSRIFPMGHGSSPSLPGVAYYNKL
IDRLQDAGIEPMATLFHWDLPQALQDHGGWQNESVVDAFLDYAAFCFSTFGDRVKLWVTF
HEPWVMSYAGYGTGQHPPGISDPGVASFKVAHLVLKAHARTWHHYNSHHRPQQQGHVGIV
LNSDWAEPLSPERPEDLRASERFLHFMLGWFAHPVFVDGDYPATLRTQIQQMNRQCSHPV
AQLPEFTEAEKQLLKGSADFLGLSHYTSRLISNAPQNTCIPSYDTIGGFSQHVNHVWPQT
SSSWIRVVPWGIRRLLQFVSLEYTRGKVPIYLAGNGMPIGESENLFDDSLRVDYFNQYIN
EVLKAIKEDSVDVRSYIARSLIDGFEGPSGYSQRFGLHHVNFSDSSKSRTPRKSAYFFTS
IIEKNGFLTKGAKRLLPPNTVNLPSKVRAFTFPSEVPSKAKVVWEKFSSQPKFERDLFYH
GTFRDDFLWGVSSSAYQIEGAWDADGKGPSIWDNFTHTPGSNVKDNATGDIACDSYHQLD
ADLNMLRALKVKAYRFSISWSRIFPTGRNSSINSHGVDYYNRLINGLVASNIFPMVTLFH
WDLPQALQDIGGWENPALIDLFDSYADFCFQTFGDRVKFWMTFNEPMYLAWLGYGSGEFP
PGVKDPGWAPYRIAHTVIKAHARVYHTYDEKYRQEQKGVISLSLSTHWAEPKSPGVPRDV
EAADRMLQFSLGWFAHPIFRNGDYPDTMKWKVGNRSELQHLATSRLPSFTEEEKRFIRAT
ADVFCLNTYYSRIVQHKTPRLNPPSYEDDQEMAEEEDPSWPSTAMNRAAPWGTRRLLNWI
KEEYGDIPIYITENGVGLTNPNTEDTDRIFYHKTYINEALKAYRLDGIDLRGYVAWSLMD
NFEWLNGYTVKFGLYHVDFNNTNRPRTARASARYYTEVITNNGMPLAREDEFLYGRFPEG
FIWSAASAAYQIEGAWRADGKGLSIWDTFSHTPLRVENDAIGDVACDSYHKIAEDLVTLQ
NLGVSHYRFSISWSRILPDGTTRYINEAGLNYYVRLIDTLLAASIQPQVTIYHWDLPQTL
QDVGGWENETIVQRFKEYADVLFQRLGDKVKFWITLNEPFVIAYQGYGYGTAAPGVSNRP
GTAPYIVGHNLIKAHAEAWHLYNDVYRASQGGVISITISSDWAEPRDPSNQEDVEAARRY
VQFMGGWFAHPIFKNGDYNEVMKTRIRDRSLAAGLNKSRLPEFTESEKRRINGTYDFFGF
NHYTTVLAYNLNYATAISSFDADRGVASIADRSWPDSGSFWLKMTPFGFRRILNWLKEEY
NDPPIYVTENGVSQREETDLNDTARIYYLRTYINEALKAVQDKVDLRGYTVWSAMDNFEW
ATGFSERFGLHFVNYSDPSLPRIPKASAKFYASVVRCNGFPDPATGPHACLHQPDAGPTI
SPVRQEEVQFLGLMLGTTEAQTALYVLFSLVLLGVCGLAFLSYKYCKRSKQGKTQRSQQE
LSPVSSF
|
| Enzyme 27 Number of Residues |
1927 |
| Enzyme 27 Molecular Weight |
218604 |
| Enzyme 27 Theoretical pI |
6.30 |
| Enzyme 27 GO Classification |
| Function |
- catalytic activity
- glucosidase activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
|
| Process |
- carbohydrate metabolism
- macromolecule metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 27 General Function |
Carbohydrate transport and metabolism |
| Enzyme 27 Specific Function |
LPH splits lactose in the small intestine |
| Enzyme 27 Pathways |
|
| Enzyme 27 Reactions |
- lactose + H2O = D-galactose + D-glucose
|
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
34400  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
P09848  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
LPH_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>5784 bp
ATGGAGCTGTCTTGGCATGTAGTCTTTATTGCCCTGCTAAGTTTTTCATGCTGGGGGTCA
GACTGGGAGTCTGATAGAAATTTCATTTCCACCGCTGGTCCTCTAACCAATGACTTGCTG
CACAACCTGAGTGGTCTCCTGGGAGACCAGAGTTCTAACTTTGTAGCAGGGGACAAAGAC
ATGTATGTTTGTCACCAGCCACTGCCCACTTTCCTGCCAGAATACTTCAGCAGTCTCCAT
GCCAGTCAGATCACCCATTATAAGGTATTTCTGTCATGGGCACAGCTCCTCCCAGCAGGA
AGCACCCAGAATCCAGACGAGAAAACAGTGCAGTGCTACCGGCGACTCCTCAAGGCCCTC
AAGACTGCACGGCTTCAGCCCATGGTCATCCTGCACCACCAGACCCTCCCTGCCAGCACC
CTCCGGAGAACCGAAGCCTTTGCTGACCTCTTCGCCGACTATGCCACATTCGCCTTCCAC
TCCTTCGGGGACCTAGTTGGGATCTGGTTCACCTTCAGTGACTTGGAGGAAGTGATCAAG
GAGCTTCCCCACCAGGAATCAAGAGCGTCACAACTCCAGACCCTCAGTGATGCCCACAGA
AAAGCCTATGAGATTTACCACGAAAGCTATGCTTTTCAGGGCGGAAAACTCTCTGTTGTC
CTGCGAGCTGAAGATATCCCGGAGCTCCTGCTAGAACCACCCATATCTGCGCTTGCCCAG
GACACGGTCGATTTCCTCTCTCTTGATTTGTCTTATGAATGCCAAAATGAGGCAAGTCTG
CGGCAGAAGCTGAGTAAATTGCAGACCATTGAGCCAAAAGTGAAAGTTTTCATCTTCAAC
CTAAAACTCCCAGACTGCCCCTCCACCATGAAGAACCCAGCCAGTCTGCTCTTCAGCCTT
TTTGAAGCCATAAATAAAGACCAAGTGCTCACCATTGGGTTTGATATTAATGAGTTTCTG
AGTTGTTCATCAAGTTCCAAGAAAAGCATGTCTTGTTCTCTGACTGGCAGCCTGGCCCTT
CAGCCTGACCAGCAGCAGGACCACGAGACCACGGACTCCTCTCCTGCCTCTGCCTATCAG
AGAGTCTGGGAAGCATTTGCCAATCAGTCCAGAGCGGAAAGGGATGCCTTCCTGCAGGAT
ACTTTCCCTGAAGGCTTCCTCTGGGGTGCCTCCACAGGAGCCTTTAACGTGGAAGGAGGC
TGGGCCGAGGGTGGGAGAGGGGTGAGCATCTGGGATCCACGCAGGCCCCTGAACACCACT
GAGGGCCAAGCGACGCTGGAGGTGGCCAGCGACAGTTACCACAAGGTAGCCTCTGACGTC
GCCCTGCTTTGCGGCCTCCGGGCTCAGGTGTACAAGTTCTCCATCTCCTGGTCCCGGATC
TTCCCCATGGGGCACGGGAGCAGCCCCAGCCTCCCAGGCGTTGCCTACTACAACAAGCTG
ATTGACAGGCTACAGGATGCGGGCATCGAGCCCATGGCCACGCTGTTCCACTGGGACCTG
CCTCAGGCCCTGCAGGATCATGGTGGATGGCAGAATGAGAGCGTGGTGGATGCCTTCCTG
GACTATGCGGCCTTCTGCTTCTCCACATTTGGGGACCGTGTGAAGCTGTGGGTGACCTTC
CATGAGCCGTGGGTGATGAGCTACGCAGGCTATGGCACCGGCCAGCACCCTCCCGGCATC
TCTGACCCAGGAGTGGCCTCTTTTAAGGTGGCTCACTTGGTCCTCAAGGCTCATGCCAGA
ACTTGGCACCACTACAACAGCCATCATCGCCCACAGCAGCAGGGGCACGTGGGCATTGTG
CTGAACTCAGACTGGGCAGAACCCCTGTCTCCAGAGAGGCCTGAGGACCTGAGAGCCTCT
GAGCGCTTCTTGCACTTCATGCTGGGCTGGTTTGCACACCCCGTCTTTGTGGATGGAGAC
TACCCAGCCACCCTGAGGACCCAGATCCAACAGATGAACAGACAGTGCTCCCATCCTGTG
GCTCAACTCCCCGAGTTCACAGAGGCAGAGAAGCAGCTCCTGAAAGGCTCTGCTGATTTT
CTGGGTCTGTCGCATTACACCTCCCGCCTCATCAGCAACGCCCCACAAAACACCTGCATC
CCTAGCTATGATACCATTGGAGGCTTCTCCCAACACGTGAACCATGTGTGGCCCCAGACC
TCATCCTCTTGGATTCGTGTGGTGCCCTGGGGGATAAGGAGGCTGTTGCAGTTTGTATCC
CTGGAATACACAAGAGGAAAAGTTCCAATATACCTTGCCGGGAATGGCATGCCCATAGGG
GAAAGTGAAAATCTCTTTGATGATTCCTTAAGAGTAGACTACTTCAATCAATATATCAAT
GAGGTGCTCAAGGCTATCAAGGAAGACTCTGTGGATGTTCGTTCCTACATTGCTCGTTCC
CTCATTGATGGCTTCGAAGGCCCTTCTGGTTACAGCCAGCGGTTTGGCCTGCACCACGTC
AACTTCAGCGACAGCAGCAAGTCAAGGACTCCCAGGAAATCTGCCTACTTTTTCACTAGC
ATCATAGAAAAGAACGGTTTCCTCACCAAGGGGGCAAAAAGACTGCTACCACCTAATACA
GTAAACCTCCCCTCCAAAGTCAGAGCCTTCACTTTTCCATCTGAGGTGCCCTCCAAGGCT
AAAGTCGTTTGGGAAAAGTTCTCCAGCCAACCCAAGTTCGAAAGAGATTTGTTCTACCAC
GGGACGTTTCGGGATGACTTTCTGTGGGGCGTGTCCTCTTCCGCTTATCAGATTGAAGGC
GCGTGGGATGCCGATGGCAAAGGCCCCAGCATCTGGGATAACTTTACCCACACACCAGGG
AGCAATGTGAAAGACAATGCCACTGGAGACATCGCCTGTGACAGCTATCACCAGCTGGAT
GCCGATCTGAATATGCTCCGAGCTTTGAAGGTGAAGGCCTACCGCTTCTCTATCTCCTGG
TCTCGGATTTTCCCAACTGGGAGAAACAGCTCTATCAACAGTCATGGGGTTGATTATTAC
AACAGGCTGATCAATGGCTTGGTGGCAAGCAACATCTTTCCCATGGTGACATTGTTCCAT
TGGGACCTGCCCCAGGCCCTCCAGGATATCGGAGGCTGGGAGAATCCTGCCTTGATTGAC
TTGTTTGACAGCTACGCAGACTTTTGTTTCCAGACCTTTGGTGATAGAGTCAAGTTTTGG
ATGACTTTTAATGAGCCCATGTACCTGGCATGGCTAGGTTATGGCTCAGGGGAATTTCCC
CCAGGGGTGAAGGACCCAGGCTGGGCACCATATAGGATAGCCCACACCGTCATCAAAGCC
CATGCCAGAGTCTATCACACGTACGATGAGAAATACAGGCAGGAGCAGAAGGGGGTCATC
TCGCTGAGCCTCAGTACACACTGGGCAGAGCCCAAGTCACCAGGGGTCCCCAGAGATGTG
GAAGCCGCTGACCGAATGCTGCAGTTCTCCCTGGGCTGGTTTGCTCACCCCATTTTTAGA
AACGGAGACTATCCTGACACCATGAAGTGGAAAGTGGGGAACAGGAGTGAACTGCAGCAC
TTAGCCACCTCCCGCCTGCCAAGCTTCACTGAGGAAGAGAAGAGGTTCATCAGGGCGACG
GCCGACGTCTTCTGCCTCAACACGTACTACTCCAGAATCGTGCAGCACAAAACACCCAGG
CTAAACCCACCCTCCTACGAAGACGACCAGGAGATGGCTGAGGAGGAGGACCCTTCGTGG
CCTTCCACGGCAATGAACAGAGCTGCGCCCTGGGGGACGCGAAGGCTGCTGAACTGGATC
AAGGAAGAGTATGGTGACATCCCCATTTACATCACCGAAAACGGAGTGGGGCTGACCAAT
CCGAACACGGAGGATACTGATAGGATATTTTACCACAAAACCTACATCAATGAGGCTTTG
AAAGCCTACAGGCTCGATGGTATAGACCTTCGAGGGTATGTCGCCTGGTCTCTGATGGAC
AACTTTGAGTGGCTAAATGGCTACACGGTCAAGTTTGGACTGTACCATGTTGATTTCAAC
AACACGAACAGGCCTCGCACAGCAAGAGCCTCCGCCAGGTACTACACAGAGGTCATTACC
AACAACGGCATGCCACTGGCCAGGGAGGATGAGTTTCTGTACGGACGGTTTCCTGAGGGC
TTCATCTGGAGTGCAGCTTCTGCTGCATATCAGATTGAAGGTGCGTGGAGAGCAGATGGC
AAAGGACTCAGCATTTGGGACACGTTTTCTCACACACCACTGAGGGTTGAGAACGATGCC
ATTGGAGACGTGGCCTGTGACAGTTATCACAAGATTGCTGAGGATCTGGTCACCCTGCAG
AACCTGGGTGTGTCCCACTACCGTTTTTCCATCTCCTGGTCTCGCATCCTCCCTGATGGA
ACCACCAGGTACATCAATGAAGCGGGCCTGAACTACTACGTGAGGCTCATCGATACACTG
CTGGCCGCCAGCATCCAGCCCCAGGTGACCATTTACCACTGGGACCTACCACAGACGCTC
CAAGATGTAGGAGGCTGGGAGAATGAGACCATCGTGCAGCGGTTTAAGGAGTATGCAGAT
GTGCTCTTCCAGAGGCTGGGAGACAAGGTGAAGTTTTGGATCACGTTGAATGAGCCCTTT
GTCATTGCTTACCAGGGCTATGGCTACGGAACAGCAGCTCCAGGAGTCTCCAATAGGCCT
GGCACTGCCCCCTACATTGTTGGCCACAATCTAATAAAGGCTCATGCTGAGGCCTGGCAT
CTGTACAACGATGTGTACCGCGCCAGTCAAGGTGGCGTGATTTCCATCACCATCAGCAGT
GACTGGGCTGAACCCAGAGATCCCTCTAACCAGGAGGATGTGGAGGCAGCCAGGAGATAT
GTTCAGTTCATGGGAGGCTGGTTTGCACATCCTATTTTCAAGAATGGAGATTACAATGAG
GTGATGAAGACGCGGATCCGTGACAGGAGCTTGGCTGCAGGCCTCAACAAGTCTCGGCTG
CCAGAATTTACAGAGAGTGAGAAGAGGAGGATCAACGGCACCTATGACTTTTTTGGGTTC
AATCACTACACCACTGTCCTCGCCTACAACCTCAACTATGCCACTGCCATCTCTTCTTTT
GATGCAGACAGAGGAGTTGCTTCCATCGCAGATCGCTCGTGGCCAGACTCTGGCTCCTTC
TGGCTGAAGATGACGCCTTTTGGCTTCAGGAGGATCCTGAACTGGTTAAAGGAGGAATAC
AATGACCCTCCAATTTATGTCACAGAGAATGGAGTGTCCCAGCGGGAAGAAACAGACCTC
AATGACACTGCAAGGATCTACTACCTTCGGACTTACATCAATGAGGCCCTCAAAGCTGTG
CAGGACAAGGTGGACCTTCGAGGATACACAGTTTGGAGTGCGATGGACAATTTTGAGTGG
GCCACAGGCTTTTCAGAGAGATTTGGTCTGCATTTTGTGAACTACAGTGACCCTTCTCTG
CCAAGGATCCCCAAAGCATCAGCGAAGTTCTACGCCTCTGTGGTCCGATGCAATGGCTTC
CCTGACCCCGCTACAGGGCCTCACGCTTGTCTCCACCAGCCAGATGCTGGACCCACCATC
AGCCCCGTGAGACAGGAGGAGGTGCAGTTCCTGGGGCTAATGCTCGGCACCACAGAAGCA
CAGACAGCTTTGTACGTTCTCTTTTCTCTTGTGCTTCTTGGAGTCTGTGGCTTGGCATTT
CTGTCATACAAGTACTGCAAGCGCTCTAAGCAAGGGAAAACACAACGAAGCCAACAGGAA
TTGAGCCCGGTGTCTTCATTCTGA
|
| Enzyme 27 GenBank Gene ID |
X07994  |
| Enzyme 27 GeneCard ID |
LCT  |
| Enzyme 27 GenAtlas ID |
LCT  |
| Enzyme 27 HGNC ID |
HGNC:6530  |
| Enzyme 27 Chromosome Location |
Not Available |
| Enzyme 27 Locus |
Not Available |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Mantei N, Villa M, Enzler T, Wacker H, Boll W, James P, Hunziker W, Semenza G: Complete primary structure of human and rabbit lactase-phlorizin hydrolase: implications for biosynthesis, membrane anchoring and evolution of the enzyme. EMBO J. 1988 Sep;7(9):2705-13. [PubMed
]
- Boll W, Wagner P, Mantei N: Structure of the chromosomal gene and cDNAs coding for lactase-phlorizin hydrolase in humans with adult-type hypolactasia or persistence of lactase. Am J Hum Genet. 1991 May;48(5):889-902. [PubMed
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
5606 |
| Enzyme 28 Name |
Glycogen phosphorylase, liver form |
| Enzyme 28 Synonyms |
Not Available |
| Enzyme 28 Gene Name |
PYGL |
| Enzyme 28 Protein Sequence |
>Glycogen phosphorylase, liver form
MAKPLTDQEKRRQISIRGIVGVENVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTV
RDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDI
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIRDGWQVEEA
DDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQVVLALPYDTPVPGYMNNTVN
TMRLWSARAPNDFNLRDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKASKFGSTRGAGTVFDAFPDQVAIQLNDTHPALAIPELMRIFVDIEKL
PWSKAWELTQKTFAYTNHTVLPEALERWPVDLVEKLLPRHLEIIYEINQKHLDRIVALFP
KDVDRLRRMSLIEEEGSKRINMAHLCIVGSHAVNGVAKIHSDIVKTKVFKDFSELEPDKF
QNKTNGITPRRWLLLCNPGLAELIAEKIGEDYVKDLSQLTKLHSFLGDDVFLRELAKVKQ
ENKLKFSQFLETEYKVKINPSSMFDVQVKRIHEYKRQLLNCLHVITMYNRIKKDPKKLFV
PRTVIIGGKAAPGYHMAKMIIKLITSVADVVNNDPMVGSKLKVIFLENYRVSLAEKVIPA
TDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRIDDVA
ALDKKGYEAKEYYEALPELKLVIDQIDNGFFSPKQPDLFKDIINMLFYHDRFKVFADYEA
YVKCQDKVSQLYMNPKAWNTMVLKNIAASGKFSSDRTIKEYAQNIWNVEPSDLKISLSNE
SNKVNGN
|
| Enzyme 28 Number of Residues |
847 |
| Enzyme 28 Molecular Weight |
97150 |
| Enzyme 28 Theoretical pI |
7.17 |
| Enzyme 28 GO Classification |
| Function |
- binding
- catalytic activity
- phosphorylase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
- vitamin binding
|
| Process |
- carbohydrate metabolism
- macromolecule metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 28 General Function |
Carbohydrate transport and metabolism |
| Enzyme 28 Specific Function |
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties |
| Enzyme 28 Pathways |
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 28 Reactions |
- (1,4-alpha-D-glucosyl)n + phosphate = (1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
|
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
183353  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
P06737  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
PYGL_HUMAN  |
| Enzyme 28 PDB ID |
1L7X  |
| Enzyme 28 PDB File |
Show |
| Enzyme 28 3D Structure |
|
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>2544 bp
ATGGGCGAACCGCTGACAGACCAGGAGAAGCGGCGGCAGATCAGCATCCGCGGCATCGTG
GGCGTGGAGAACGTGGCAGAGCTGAAGAAGAGTTTCAACCGGCACCTGCACTTCACGCTG
GTCAAGGACCGCAACGTGGCCACCACCCGCGACTACTACTTCGCGCTGGCGCACACGGTG
CGGGACCACCTGGTGGGGCGCTGGATCCGCACGCAGCAGCACTACTACGACAAGTGCCCC
AAGAGGGAATATTACCTCTCTCTGGAATTTTACATGGGCCGAACATTACAGAACACCATG
ATCAACCTCGGTCTGCAAAATGCCTGTGATGAGGCCATTTACCAGCTTGGATTGGATATA
GAAGAGTTAGAAGAAATTGAAGAAGATGCTGGACTTGGCAATGGTGGTCTTGGGAGACTT
GCTGCCTGCTTCTTGGATTCCATGGCAACCCTGGGACTTGCAGCCTATGGATACGGCATT
CGGTATGAATATGGGATTTTCAATCAGAAGATCCGAGATGGATGGCAGGTAGAAGAAGCA
GATGATTGGCTCAGATATGGAAACCCTTGGGAGAAGTCCCGCCCAGAATTCATGCTGCCT
GTGCACTTCTATGGAAAAGTAGAACACACCAACACCGGGACCAAGTGGATTGACACTCAA
GTGGTCCTGGCTCTGCCATATGACACCCCCGAGCCCGGCTACATGAATAACACTGTCAAC
ACCATGCGCCTCTGGTCTGCTCGGGCACCAAATGACTTTAACCTCAGAGACTTTAATGTT
GGAGACTACATTCAGGCTGTGCTGGACCGAAACCTGGCCGAGAACATCTCCCGGGTCCTC
TATCCCAATGACAATTTTTTTGAAGGGAAGGAGCTAAGATTGAAGCAGGAATACTTTGTG
GTGGCTGCAACCTTGCAAGATATCATCCGCCGTTTCAAAGCCTCCAAGTTTGGCTCCACC
CGTGGTCAAGGAACTGTGTTTGATGCCTTCCCGGATCAGGTGGCCATCCAGCTGAATGAT
ACTCACCCTCGCATCGCGATCCCTGAGCTGATGAGGATTTTTGTGGATATTGAAAAACTG
CCCTGGTCCAAGGCATGGGAGCTCAACCAGAAGACCTTCGCCTACACCAACCACACAGTG
CTCCCGGAAGCCCTGGAGCGCTGGCCCGTGGACCTGGTGGAGAAGCTGCTCCCTCGACAT
TTGGAAATCATTTATGAGATAAATCAGAAGCATTTAGATAGAATTGTGGCCTTGTTTCCT
AAAGATGTGGACCCTCTGAGAAGGATGTCTCTGATAGAAGAGGAAGGAAGCAAAAGGATC
AACATGGCCCATCTCTGCATTGTCGGTTCCCATGCTGTGAATGGCGTGGCTAAAATCCAC
TCAGACATCGTGAAGACTAAAGTATTCAAGGACTTCAGTGAGCTAGAACCTGACAAGTTT
CAGAATAAAACCAATGGGATCACTCCAAGGCGCTGGCTCCTACTCTGCAACCCAGGACTT
GCAGAGCTCATAGCAGAGAAAATTGGAGAAGACTATGTGAAAGACCTGAGCCAGCTGACG
AAGCTCCACAGCTTCCTGGGTGATGATGTCTTCCTCCGGGAACTCGCCAAGGTGAAGCAG
GAGAATAAGCTGAAGTTTTCTCAGTTCCTGGAGACGGAGTACAAAGTGAAGATCAACCCA
TCCTCCATGTTTGATGTCCAGGTGAAGAGGATACATGAGTACAAGCGACAGCTCTTGAAC
TGTCTGCATGTGATCACGATGTACAACCGCATTAAGAAAGACCCTAAGAAGTTATTCGTG
CCAAGGACAGTTATCATTGGTGGTAAAGCTGCCCCAGGATATCACATGGCCAAAATGATC
ATAAAGCTGATCACTTCAGTGGCAGATGTGGTGAACAATGACCCTATGGTTGGAAGCAAG
TTGAAAGTCATCTTCTTGGAGAACTACAGAGTATCTCTTGCTGAAAAAGTCATTCCAGCC
ACAGATCTGTCAGAGCAGATTTCCACTGCAGGCACCGAAGCCTCGGGGACAGGCAATATG
AAGTTCATGCTAAATGGGGCCCTAACTATCGGGACCATGGATGGGGCCAATGTGGAAATG
GCAGAAGAAGCTGGGGAAGAGAACCTGTTCATCTTTGGCATGAGCATAGATGATGTGGCT
GCTTTGGACAAGAAAGGGTACGAGGCAAAAGAATACTATGAGGCACTTCCAGAGCTGAAG
CTGGTCATTGATCAAATTGACAATGGCTTTTTTTCTCCCAAGCAGCCTGACCTCTTCAAA
GATATCATCAACATGCTATTTTATCATGACAGGTTTAAAGTCTTTGCAGACTACGAAGCC
TATGTCAAGTGTCAAGATAAAGTGAGTCAGCTGTACATGAATCCAAAGGCCTGGAACACA
ATGGTACTCAAAAACATAGCTGCCTCGGGGAAATTCTCCAGTGACCGAACAATTAAAGAA
TATGCCCAAAACATCTGGAACGTGGAACCTTCAGATCTAAAGATTTCTCTATCCAATGAA
TCTAACAAAGTCAATGGAAATTGA
|
| Enzyme 28 GenBank Gene ID |
M14636  |
| Enzyme 28 GeneCard ID |
PYGL  |
| Enzyme 28 GenAtlas ID |
PYGL  |
| Enzyme 28 HGNC ID |
HGNC:9725  |
| Enzyme 28 Chromosome Location |
14 |
| Enzyme 28 Locus |
14q21-q22 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- Newgard CB, Nakano K, Hwang PK, Fletterick RJ: Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8132-6. [PubMed
]
- Chang S, Rosenberg MJ, Morton H, Francomano CA, Biesecker LG: Identification of a mutation in liver glycogen phosphorylase in glycogen storage disease type VI. Hum Mol Genet. 1998 May;7(5):865-70. [PubMed
]
- Burwinkel B, Bakker HD, Herschkovitz E, Moses SW, Shin YS, Kilimann MW: Mutations in the liver glycogen phosphorylase gene (PYGL) underlying glycogenosis type VI. Am J Hum Genet. 1998 Apr;62(4):785-91. [PubMed
]
- Gorin FA, Mullinax RL, Ignacio PC, Neve RL, Kurnit DM: McArdle's & Hers' diseases: glycogen phosphorylase transcriptional expression in human tissues. J Neurogenet. 1987 Dec;4(6):293-308. [PubMed
]
- Rath VL, Ammirati M, Danley DE, Ekstrom JL, Gibbs EM, Hynes TR, Mathiowetz AM, McPherson RK, Olson TV, Treadway JL, Hoover DJ: Human liver glycogen phosphorylase inhibitors bind at a new allosteric site. Chem Biol. 2000 Sep;7(9):677-82. [PubMed
]
- Rath VL, Ammirati M, LeMotte PK, Fennell KF, Mansour MN, Danley DE, Hynes TR, Schulte GK, Wasilko DJ, Pandit J: Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core. Mol Cell. 2000 Jul;6(1):139-48. [PubMed
]
- Ekstrom JL, Pauly TA, Carty MD, Soeller WC, Culp J, Danley DE, Hoover DJ, Treadway JL, Gibbs EM, Fletterick RJ, Day YS, Myszka DG, Rath VL: Structure-activity analysis of the purine binding site of human liver glycogen phosphorylase. Chem Biol. 2002 Aug;9(8):915-24. [PubMed
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
5610 |
| Enzyme 29 Name |
Glycogen phosphorylase, muscle form |
| Enzyme 29 Synonyms |
- Myophosphorylase
|
| Enzyme 29 Gene Name |
PYGM |
| Enzyme 29 Protein Sequence |
>Glycogen phosphorylase, muscle form
MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTV
RDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDM
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKISGGWQMEEA
DDWLRYGNPWEKARPEFTLPVHFYGHVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVN
TMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRILVDLERM
DWDKAWDVTVRTCAYTNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFP
GDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKF
QNKTNGITPRRWLVLCNPGLAEVIAERIGEDFISDLDQLRKLLSFVDDEAFIRDVAKVKQ
ENKLKFAAYLEREYKVHINPNSLFDIQVKRIHEYKRQLLNCLHVITLYNRIKREPNKFFV
PRTVMIGGKAAPGYHMAKMIIRLVTAIGDVVNHDPAVGDRLRVIFLENYRVSLAEKVIPA
ADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVD
KLDQRGYNAQEYYDRIPELRQVIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYED
YIKCQEKVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDE
AI
|
| Enzyme 29 Number of Residues |
842 |
| Enzyme 29 Molecular Weight |
97093 |
| Enzyme 29 Theoretical pI |
7.03 |
| Enzyme 29 GO Classification |
| Function |
- binding
- catalytic activity
- phosphorylase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
- vitamin binding
|
| Process |
- carbohydrate metabolism
- macromolecule metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 29 General Function |
Carbohydrate transport and metabolism |
| Enzyme 29 Specific Function |
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties |
| Enzyme 29 Pathways |
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 29 Reactions |
- (1,4-alpha-D-glucosyl)n + phosphate = (1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
|
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
190784  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
P11217  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
PYGM_HUMAN  |
| Enzyme 29 PDB ID |
1XL1  |
| Enzyme 29 PDB File |
Show |
| Enzyme 29 3D Structure |
|
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>2529 bp
ATGTCCCGGCCCCTGTCAGACCAAGAGAAAAGAAAGCAAATCAGTGTGCGTGGCCTGGCC
GGCGTGGAGAACGTGACTGAGCTGAAAAAGAACTTCAACCGGCACCTGCATTTCACACTC
GTAAAGGACCGCAATGTGGCCACCCCACGAGACTACTACTTTGCTCTGGCCCATACCGTG
CGCGACCACCTCGTGGGGCGGTGGATCCGCACGCAGCAGCACTACTATGAGAAGGACCCC
AAGAGGATCTACTACCTGTCTTTAGAGTTCTATATGGGACGGACGCTACAGAACACCATG
GTGAACCTGGCCTTAGAGAATGCCTGTGACGAGGCCACCTACCAGCTGGGCCTGGACATG
GAGGAGCTGGAGGAAATTGAGGAGGATGCGGGGCTGGGCAACGGGGGCCTGGGCCGGCTG
GCAGCCTGCTTTCTTGACTCCATGGCAACACTGGGCCTGGCTGCCTATGGCTACGGGATT
CGCTATGAGTTTGGGATTTTTAACCAGAAGATCTCCGGGGGCTGGCAGATGGAGGAGGCC
GATGACTGGCTTCGCTACGGCAACCCCTGGGAGAAGGCCCGGCCCGAGTTCACGCTACCT
GTGCACTTCTACGGCCATGTGGAGCACACCAGCCAGGGTGCCAAGTGGGTGGACACACAG
GTGGTACTGGCCATGCCCTACGATACCCCGGTGCCTGGCTATCGCAACAATGTTGTCAAC
ACCATGCGCCTCTGGTCTGCCAAGGCTCCCAATGACTTCAACCTCAAGGACTTCAATGTC
GGTGGCTACATCCAGGCTGTGTTGGACCGAAACCTGGCGGAGAACATCTCTCGTGTCCTG
TACCCCAATGATAATTTCTTCGAAGGGAAGGAGCTGCGGCTGAAGCAGGAGTATTTCGTG
GTGGCTGCCACCCTCCAGGACATCATCCGTCGCTTCAAGTCTTCCAAGTTCGGCTGCCGT
GATCCCGTGCGCACGAACTTCGATGCCTTCCCAGATAAGGTGGCCATCCAGCTCAATGAC
ACCCACCCCTCCCTGGCCATCCCCGAGCTGATGAGGATCCTGGTGGACCTGGAACGGATG
GACTGGGACAAGGCGTGGGATGTGACAGTGAGGACCTGTGCCTACACCAACCACACGGTG
CTGCCCGAGGCCCTGGAGCGCTGGCCGGTGCACCTCTTGGAGACGCTGCTGCCGCGGCAC
CTCCAGATCATCTACGAGATCAACCAGCGCTTCCTCAACCGGGTGGCGGCCGCATTCCCA
GGGGACGTAGACCGGCTGCGGCGCATGTCGCTGGTGGAGGAGGGCGCAGTGAAGCGCATC
AACATGGCACACCTGTGCATCGCGGGGTCGCACGCCGTCAACGGTGTGGCCCGCATCCAC
TCGGAGATCCTCAAGAAGACCATCTTCAAAGACTTCTATGAGCTGGAGCCTCATAAGTTC
CAGAATAAGACCAACGGCATCACCCCTCGGCGCTGGCTGGTTCTGTGTAACCCCGGGCTG
GCAGAGGTCATTGCTGAGCGCATCGGGGAGGACTTCATCTCTGACCTGGACCAGCTGCGC
AAACTGCTCTCCTTTGTGGATGATGAAGCTTTCATTCGGGATGTGGCCAAAGTGAAGCAG
GAAAACAAGTTGAAGTTTGCTGCCTACCTAGAGAGGGAATACAAAGTCCACATCAACCCC
AACTCACTCTTCGACATCCAGGTGAAGCGGATTCACGAATATAAACGACAGCTCCTCAAC
TGCCTCCATGTCATCACCCTGTACAACCGCATCAAGAGGGAGCCCAATAAGTTTTTTGTG
CCTCGGACTGTGATGATTGGAGGGAAGGCTGCACCTGGGTACCACATGGCCAAGATGATC
ATCAGACTCGTCACAGCCATCGGGGATGTGGTCAACCATGACCCGGCAGTGGGTGACCGC
CTCCGTGTCATCTTCCTGGAGAACTACCGAGTCTCACTGGCCGAGAAAGTGATCCCAGCT
GCAGACCTCTCTGAGCAGATCTCCACTGCGGGCACTGAAGCCTCAGGCACCGGCAACATG
AAGTTCATGCTCAACGGGGCTCTGACCATTGGCACCATGGACGGGGCCAATGTGGAGATG
GCAGAAGAGGCGGGAGAGGAAAACTTCTTCATCTTTGGCATGCGGGTGGAGGATGTGGAT
AAGCTTGACCAAAGAGGGTACAATGCCCAGGAGTACTACGATCGCATTCCTGAGCTTCGG
CAGGTCATTGAGCAGCTGAGCAGTGGCTTCTTCTCCCCCAAACAACCCGACCTGTTCAAG
GACATTGTCAATATGCTCATGCACCATGACCGGTTTAAAGTCTTCGCAGATTATGAAGAC
TACATTAAATGCCAGGAGAAAGTCAGCGCCTGGTACAAGAACCCAAGAGAGTGGACGCGG
ATGGTGATCCGGAACATAGCCACTTCTGGCAAGTTCTCCAGTGACCGCACCATTGCCCAG
TATGCCCGGGAGATCTGGGGTGTGGAGCCTTCCCGCCAGCGCCTGCCAGCCCCGGATGAG
GCCATCTGA
|
| Enzyme 29 GenBank Gene ID |
M32598  |
| Enzyme 29 GeneCard ID |
PYGM  |
| Enzyme 29 GenAtlas ID |
PYGM  |
| Enzyme 29 HGNC ID |
HGNC:9726  |
| Enzyme 29 Chromosome Location |
11 |
| Enzyme 29 Locus |
11q12-q13.2 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- Burke J, Hwang P, Anderson L, Lebo R, Gorin F, Fletterick R: Intron/exon structure of the human gene for the muscle isozyme of glycogen phosphorylase. Proteins. 1987;2(3):177-87. [PubMed
]
- Hwang PK, See YP, Vincentini AM, Powers MA, Fletterick RJ, Crerar MM: Comparative sequence analysis of rat, rabbit, and human muscle glycogen phosphorylase cDNAs. Eur J Biochem. 1985 Oct 15;152(2):267-74. [PubMed
]
- Gautron S, Daegelen D, Mennecier F, Dubocq D, Kahn A, Dreyfus JC: Molecular mechanisms of McArdle's disease (muscle glycogen phosphorylase deficiency). RNA and DNA analysis. J Clin Invest. 1987 Jan;79(1):275-81. [PubMed
]
- Tsujino S, Shanske S, DiMauro S: Molecular genetic heterogeneity of myophosphorylase deficiency (McArdle's disease). N Engl J Med. 1993 Jul 22;329(4):241-5. [PubMed
]
- Tsujino S, Shanske S, Martinuzzi A, Heiman-Patterson T, DiMauro S: Two novel missense mutations (E654K, L396P) in Caucasian patients with myophosphorylase deficiency (McArdle's disease). Hum Mutat. 1995;6(3):276-7. [PubMed
]
- Tsujino S, Shanske S, Nonaka I, DiMauro S: The molecular genetic basis of myophosphorylase deficiency (McArdle's disease). Muscle Nerve. 1995;3:S23-7. [PubMed
]
- Vorgerd M, Kubisch C, Burwinkel B, Reichmann H, Mortier W, Tettenborn B, Pongratz D, Lindemuth R, Tegenthoff M, Malin JP, Kilimann MW: Mutation analysis in myophosphorylase deficiency (McArdle's disease). Ann Neurol. 1998 Mar;43(3):326-31. [PubMed
]
- Gamez J, Fernandez R, Bruno C, Andreu AL, Cervera C, Navarro C, Schwartz S, Dimauro S: A new mutation in the regulatory domain of the myophosphorylase gene affecting protein dimer contact. Muscle Nerve. 1999 Aug;22(8):1136-8. [PubMed
]
- Andreu AL, Bruno C, Tamburino L, Gamez J, Shanske S, Cervera C, Navarro C, DiMauro S: A new mutation in the myophosphorylase gene (Asn684Tyr) in a Spanish patient with McArdle's disease. Neuromuscul Disord. 1999 May;9(3):171-3. [PubMed
]
- Rubio JC, Martin MA, Garcia A, Campos Y, Cabello A, Culebras JM, Arenas J: McArdle's disease associated with homozygosity for the missense mutation Gly204Ser of the myophosphorylase gene in a Spanish patient. Neuromuscul Disord. 1999 May;9(3):174-5. [PubMed
]
- Fernandez R, Navarro C, Andreu AL, Bruno C, Shanske S, Gamez J, Teijeira S, Hernandez I, Teijeiro A, Fernandez JM, Musumeci O, DiMauro S: A novel missense mutation (W797R) in the myophosphorylase gene in Spanish patients with McArdle disease. Arch Neurol. 2000 Feb;57(2):217-9. [PubMed
]
- Rubio JC, Martin MA, Campos Y, Auciello R, Cabello A, Arenas J: A missense mutation W797R in the myophosphorylase gene in a Spanish patient with McArdle's disease. Muscle Nerve. 2000 Jan;23(1):129-31. [PubMed
]
- Rubio JC, Martin MA, Campos Y, Cabello A, Arenas J: A missense mutation T487N in the myophosphorylase gene in a Spanish patient with McArdle's disease. Neuromuscul Disord. 2000 Feb;10(2):138-40. [PubMed
]
- Martin MA, Rubio JC, Campos Y, Ricoy JR, Cabello A, Arenas J: A homozygous missense mutation (A659D) in the myophosphorylase gene in a Spanish patient with McArdle's disease. Neuromuscul Disord. 2000 Aug;10(6):447-9. [PubMed
]
- Martin MA, Rubio JC, Buchbinder J, Fernandez-Hojas R, del Hoyo P, Teijeira S, Gamez J, Navarro C, Fernandez JM, Cabello A, Campos Y, Cervera C, Culebras JM, Andreu AL, Fletterick R, Arenas J: Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study. Ann Neurol. 2001 Nov;50(5):574-81. [PubMed
]
- Bruno C, Lanzillo R, Biedi C, Iadicicco L, Minetti C, Santoro L: Two new mutations in the myophosphorylase gene in Italian patients with McArdle's disease. Neuromuscul Disord. 2002 Jun;12(5):498-500. [PubMed
]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
5612 |
| Enzyme 30 Name |
Glycogen phosphorylase, brain form |
| Enzyme 30 Synonyms |
Not Available |
| Enzyme 30 Gene Name |
PYGB |
| Enzyme 30 Protein Sequence |
>Glycogen phosphorylase, brain form
MAKPLTDSEKRKQISVRGLAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTV
RDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQNACDEAIYQLGLDL
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEA
DDWLRYGNPWEKARPEYMLPVHFYGRVEHTPDGVKWLDTQVVLAMPYDTPVPGYKNNTVN
TMRLWSAKAPNDFKLQDFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKSSKFGCRDPVRTCFETFPDKVAIQLNDTHPALSIPELMRILVDVEKV
DWDKAWEITKKTCAYTNHTVLPEALERWPVSMFEKLLPRHLEIIYAINQRHLDHVAALFP
GDVDRLRRMSVIEEGDCKRINMAHLCVIGSHAVNGVARIHSEIVKQSVFKDFYELEPEKF
QNKTNGITPRRWLLLCNPGLADTIVEKIGEEFLTDLSQLKKLLPLVSDEVFIRDVAKVKQ
ENKLKFSAFLEKEYKVKINPSSMFDVHVKRIHEYKRQLLNCLHVVTLYNRIKRDPAKAFV
PRTVMIGGKAAPGYHMAKLIIKLVTSIGDVVNHDPVVGDRLKVIFLENYRVSLAEKVIPA
ADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGAENLFIFGLRVEDVE
ALDRKGYNAREYYDHLPELKQAVDQISSGFFSPKEPDCFKDIVNMLMHHDRFKVFADYEA
YMQCQAQVDQLYRNPKEWTKKVIRNIACSGKFSSDRTITEYAREIWGVEPSDLQIPPPNI
PRD
|
| Enzyme 30 Number of Residues |
843 |
| Enzyme 30 Molecular Weight |
96697 |
| Enzyme 30 Theoretical pI |
6.85 |
| Enzyme 30 GO Classification |
| Function |
- binding
- catalytic activity
- phosphorylase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
- vitamin binding
|
| Process |
- carbohydrate metabolism
- macromolecule metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 30 General Function |
Carbohydrate transport and metabolism |
| Enzyme 30 Specific Function |
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties |
| Enzyme 30 Pathways |
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 30 Reactions |
- (1,4-alpha-D-glucosyl)n + phosphate = (1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
|
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
307200  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
P11216  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
PYGB_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>2592 bp
ATGGGCGAACCGCTGACGGACAGCGAGAAGCGGAAGCAGATCAGCGTGCGCGGCCTGGCG
GGGCTAGGCGACGTGGCCGAGGTGCGGAAGAGCTTCAACCGGCACTTGCACTTCACGCTG
GTCAAGGACCGCAATGTGGCCACGCCCCGCGACTACTTCTTCGCGCTGGCGCACACGGTG
CGCGACCACCTCGTGGGCCGCTGGATCCGCACGCAGCAGCACTACTACGAGCGCGACCCC
AAGCGAATTTATTATCTTTCCCTGGAATTCTACATGGGTCGCACGCTGCAGAACACGATG
GTGAACCTGGGCCTTCAGAATGCCTGCGATGAAGCCATCTATCAGTTGGGGTTAGACTTG
GAGGAACTCGAGGAGATAGAAGAAGATGCTGGCCTTGGGAATGGAGGCCTGGGGAGGCTG
GCAGCGTGTTTCCTTGACTCAATGGCTACCTTGGGCCTGGCAGCATACGGCTATGGAATC
CGCTATGAATTTGGGATTTTTAACCAGAAGATTGTCAATGGCTGGCAGGTAGAGGAGGCC
GATGACTGGCTGCGCTACGGCAACCCCTGGGAGAAAGCGCGGCCTGAGTATATGCTTCCC
GTGCACTTCTACGGACGCGTGGAGCACACCCCCGACGGCGTGAAGTGGCTGGACACACAG
GTGGTGCTGGCCATGCCCTACGACACCCCAGTGCCCGGCTACAAGAACAACACCGTCAAC
ACCATGCGGCTGTGGTCCGCAAGGGCTCCCAACGACTTCAAGCTGCAGGACTTCAACGTG
GGAGACTACATCGAGGCGGTCCTGGACCGGAACTTGGCTGAGAACATCTCCAGGGTCCTG
TATCCAAATGATAACTTCTTTGAGGGGAAGGAGCTGCGGCTGAAGCAGGAGTACTTCGTG
GTGGGCGCCACGCTCCAGGACATCATCCGCCGCTTCAAGTCGTCCAAGTTCGGCTGCCGG
GACCCTGTGAGAACCTGTTTCGAGACGTTCCCAGACAAGGTGGCCATCCAGCTGAACGAC
ACCCACCCCGCCCTCTCCATCCCTGAGCTCATGCGGATCCTGGTGGACGTGGAGAAGGTG
GACTGGGACAAGGCCTGGGAAATCACGAAGAAGACCTGTGCATACACCAACCACACTGTG
CTGCCTGAGGCCTTGGAGCGCTGGCCCGTGTCCATGTTTGAGAAGCTGCTGCCGCGGCAC
CTGGAGATAATCTATGCCATCAACCAGCGGCACCTGGACCACGTGGCCGCGCTGTTTCCC
GGCGATGTGGACCGCCTGCGCAGGATGTCTGTGATCGAGGAGGGGGACTGCAAGCGGATC
AACATGGCCCACCTGTGTGTGATTGGGTCCCATGCTGTCAATGGTGTGGCGAGGATCCAC
TCGGAGATCGTGAAACAGTCGGTCTTTAAGGATTTTTATGAACTGGAGCCAGAGAAGTTC
CAGAATAAGACCAATGGCATCACCCCCCGCCGGTGGCTGCTGCTGTGCAACCCGGGGCTG
GCCGATACCATCGTGGAGAAAATTGGGGAGGAGTTCCTGACTGACCTGAGCCAGCTGAAG
AAGCTGCTGCCGCTGGTCAGTGACGAGGTGTTCATCAGGGACGTGGCCAAGGTCAAACAG
GAGAACAAGCTCAAGTTCTCGGCCTTCCTGGAGAAGGAGTACAAGGTGAAGATCAACCCC
TCCTCCATGTTCGATGTGCATGTGAAGAGGATCCACGAGTACAAGCGGCAGCTGCTCAAC
TGCCTGCACGTCGTCACCCTGTACAATCGAATCAAGAGAGACCCGGCCAAGGCTTTTGTG
CCCAGGACTGTTATGATTGGGGGCAAGGCAGCGCCCGGTTACCACATGGCCAAGCTGATC
ATCAAGTTGGTCACCTCCATCGGCGACGTCGTCAATCATGACCCAGTTGTGGGTGACAGG
TTGAAAGTGATCTTCCTGGAGAACTACCGTGTGTCCTTGGCTGAGAAAGTGATCCCGGCC
GCTGATCTGTCGCAGCAGATCTCCACTGCAGGCACCGAGGCCTCAGGCACAGGCAACATG
AAGTTCATGCTCAACGGGGCCCTCACCATCGGCACCATGGACGGCGCCAACGTGGAGATG
GCCGAGGAGGCCGGGGCCGAGAACCTCTTCATCTTCGGCCTGCGGGTGGAGGATGTCGAG
GCCTTGGACCGGAAAGGGTACAATGCCAGGGAGTACTACGACCACCTGCCCGAGCTGAAG
CAGGCCGTGGACCAGATCAGCAGTGGCTTTTTTTCTCCCAAGGAGCCAGACTGCTTCAAG
GACATCGTGAACATGCTGATGCACCATGACAGGTTCAAGGTGTTTGCAGACTATGAAGCC
TACATGCAGTGCCAGGCACAGGTGGACCAGCTGTACCGGAACCCCAAGGAGTGGACCAAG
AAGGTCATCAGGAACATCGCCTGCTCGGGCAAGTTCTCCAGTGACCGGACCATCACGGAG
TATGCACGGGAGATCTGGGGTGTGGAGCCCTCCGACCTGCAGCTTCAGCACCTGCCCCAC
CCAGAGTGGGAGTCAGGTGGAGCCACCTGCTGGGCTCCCCCAGAACTTTGCACACATCTT
GCTATGTATTAG
|
| Enzyme 30 GenBank Gene ID |
J03544  |
| Enzyme 30 GeneCard ID |
PYGB  |
| Enzyme 30 GenAtlas ID |
PYGB  |
| Enzyme 30 HGNC ID |
HGNC:9723  |
| Enzyme 30 Chromosome Location |
20 |
| Enzyme 30 Locus |
20p11.2-p11.1 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Newgard CB, Littman DR, van Genderen C, Smith M, Fletterick RJ: Human brain glycogen phosphorylase. Cloning, sequence analysis, chromosomal mapping, tissue expression, and comparison with the human liver and muscle isozymes. J Biol Chem. 1988 Mar 15;263(8):3850-7. [PubMed
]
- Gelinas RP, Froman BE, McElroy F, Tait RC, Gorin FA: Human brain glycogen phosphorylase: characterization of fetal cDNA and genomic sequences. Brain Res Mol Brain Res. 1989 Nov;6(2-3):177-85. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
5613 |
| Enzyme 31 Name |
Glucose-6-phosphatase |
| Enzyme 31 Synonyms |
- G6Pase
- G-6-Pase
|
| Enzyme 31 Gene Name |
G6PC |
| Enzyme 31 Protein Sequence |
>Glucose-6-phosphatase
MEEGMNVLHDFGIQSTHYLQVNYQDSQDWFILVSVIADLRNAFYVLFPIWFHLQEAVGIK
LLWVAVIGDWLNLVFKWILFGQRPYWWVLDTDYYSNTSVPLIKQFPVTCETGPGSPSGHA
MGTAGVYYVMVTSTLSIFQGKIKPTYRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQ
VVAGVLSGIAVTETFSHIHSIYNASLKKYFLITFFLFSFAIGFYLLLKGLGVDLLWTLEK
AQRWCEQPEWVHIDTTPFASLLKNLGTLFGLGLALNSSMYRESCKGKLSKWLPFRLSSIV
ASLVLLHVFDSLKPPSQVELVFYVLSFCKSAVVPLASVSVIPYCLAQVLGQPHKKSL
|
| Enzyme 31 Number of Residues |
357 |
| Enzyme 31 Molecular Weight |
40514 |
| Enzyme 31 Theoretical pI |
8.61 |
| Enzyme 31 GO Classification |
Not Available |
| Enzyme 31 General Function |
Not Available |
| Enzyme 31 Specific Function |
May be a single membrane channel protein acting both as a hydrolase and a translocase. It is the key enzyme in homeostatic regulation of blood glucose levels |
| Enzyme 31 Pathways |
|
| Enzyme 31 Reactions |
- D-glucose 6-phosphate + H2O = D-glucose + phosphate
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
- 30-46
59-75
153-169
211-227
296-312
320-336
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
452444  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
P35575  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
G6PT_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>1074 bp
ATGGAGGAAGGAATGAATGTTCTCCATGACTTTGGGATCCAGTCAACACATTACCTCCAG
GTGAATTACCAAGACTCCCAGGACTGGTTCATCTTGGTGTCCGTGATCGCAGACCTCAGG
AATGCCTTCTACGTCCTCTTCCCCATCTGGTTCCATCTTCAGGAAGCTGTGGGCATTAAA
CTCCTTTGGGTAGCTGTGATTGGAGACTGGCTCAACCTCGTCTTTAAGTGGATTCTCTTT
GGACAGCGTCCATACTGGTGGGTTTTGGATACTGACTACTACAGCAACACTTCCGTGCCC
CTGATAAAGCAGTTCCCTGTAACCTGTGAGACTGGACCAGGGAGCCCCTCTGGCCATGCC
ATGGGCACAGCAGGTGTATACTACGTGATGGTCACATCTACTCTTTCCATCTTTCAGGGA
AAGATAAAGCCGACCTACAGATTTCGGTGCTTGAATGTCATTTTGTGGTTGGGATTCTGG
GCTGTGCAGCTGAATGTCTGTCTGTCACGAATCTACCTTGCTGCTCATTTTCCTCATCAA
GTTGTTGCTGGAGTCCTGTCAGGCATTGCTGTTACAGAAACTTTCAGCCACATCCACAGC
ATCTATAATGCCAGCCTCAAGAAATATTTTCTCATTACCTTCTTCCTGTTCAGCTTCGCC
ATCGGATTTTATCTGCTGCTCAAGGGACTGGGTGTAGACCTCCTGTGGACTCTGGAGAAA
GCCCAGAGGTGGTGCGAGCAGCCAGAATGGGTCCACATTGACACCACACCCTTTGCCAGC
CTCCTCAAGAACCTGGGCACGCTCTTTGGCCTGGGGCTGGCTCTCAACTCCAGCATGTAC
AGGGAGAGCTGCAAGGGGAAACTCAGCAAGTGGCTCCCATTCCGCCTCAGCTCTATTGTA
GCCTCCCTCGTCCTCCTGCACGTCTTTGACTCCTTGAAACCCCCATCCCAAGTCGAGCTG
GTCTTCTACGTCTTGTCCTTCTGCAAGAGTGCGGTAGTGCCCCTGGCATCCGTCAGTGTC
ATCCCCTACTGCCTCGCCCAGGTCCTGGGCCAGCCGCACAAGAAGTCGTTGTAA
|
| Enzyme 31 GenBank Gene ID |
U01120  |
| Enzyme 31 GeneCard ID |
G6PC  |
| Enzyme 31 GenAtlas ID |
G6PC  |
| Enzyme 31 HGNC ID |
HGNC:4056  |
| Enzyme 31 Chromosome Location |
17 |
| Enzyme 31 Locus |
17q21 |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
- Lei KJ, Shelly LL, Pan CJ, Sidbury JB, Chou JY: Mutations in the glucose-6-phosphatase gene that cause glycogen storage disease type 1a. Science. 1993 Oct 22;262(5133):580-3. [PubMed
]
- Pan CJ, Lei KJ, Chou JY: Asparagine-linked oligosaccharides are localized to a luminal hydrophilic loop in human glucose-6-phosphatase. J Biol Chem. 1998 Aug 21;273(34):21658-62. [PubMed
]
- Lei KJ, Chen YT, Chen H, Wong LJ, Liu JL, McConkie-Rosell A, Van Hove JL, Ou HC, Yeh NJ, Pan LY, et al.: Genetic basis of glycogen storage disease type 1a: prevalent mutations at the glucose-6-phosphatase locus. Am J Hum Genet. 1995 Oct;57(4):766-71. [PubMed
]
- Parvari R, Moses S, Hershkovitz E, Carmi R, Bashan N: Characterization of the mutations in the glucose-6-phosphatase gene in Israeli patients with glycogen storage disease type 1a: R83C in six Jews and a novel V166G mutation in a Muslim Arab. J Inherit Metab Dis. 1995;18(1):21-7. [PubMed
]
- Hwu WL, Chuang SC, Tsai LP, Chang MH, Chuang SM, Wang TR: Glucose-6-phosphatase gene G327A mutation is common in Chinese patients with glycogen storage disease type Ia. Hum Mol Genet. 1995 Jun;4(6):1095-6. [PubMed
]
- Lee WJ, Lee HM, Chi CS, Shu SG, Lin LY, Lin WH: Genetic analysis of the glucose-6-phosphatase mutation of type 1a glycogen storage disease in a Chinese family. Clin Genet. 1996 Oct;50(4):206-11. [PubMed
]
- Chevalier-Porst F, Bozon D, Bonardot AM, Bruni N, Mithieux G, Mathieu M, Maire I: Mutation analysis in 24 French patients with glycogen storage disease type 1a. J Med Genet. 1996 May;33(5):358-60. [PubMed
]
- Rake JP, ten Berge AM, Verlind E, Visser G, Niezen-Koning KE, Buys CH, Smit GP, Scheffer H: Glycogen storage disease type Ia: four novel mutations (175delGG, R170X, G266V and V338F) identified. Mutations in brief no. 220. Online. Hum Mutat. 1999;13(2):173. [PubMed
]
- Trioche P, Francoual J, Chalas J, Capel L, Bernard O, Labrune P: Identification of three novel mutations (Q54P, W70X and T108I) in the glucose-6-phosphatase gene of patients with glycogen storage disease type Ia. Mutation in brief no. 256. Online. Hum Mutat. 1999;14(1):91. [PubMed
]
- Seydewitz HH, Matern D: Molecular genetic analysis of 40 patients with glycogen storage disease type Ia: 100% mutation detection rate and 5 novel mutations. Hum Mutat. 2000 Jan;15(1):115-6. [PubMed
]
|
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
5634 |
| Enzyme 32 Name |
S-methyl-5-thioadenosine phosphorylase |
| Enzyme 32 Synonyms |
- 5'- methylthioadenosine phosphorylase
- MTA phosphorylase
- MTAPase
|
| Enzyme 32 Gene Name |
MTAP |
| Enzyme 32 Protein Sequence |
>S-methyl-5-thioadenosine phosphorylase
MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLAR
HGRQHTIMPSKVNYQANIWALKEEGCTHVIVTTACGSLREEIQPGDIVIIDQFIDRTTMR
PQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSR
AESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTL
KENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH
|
| Enzyme 32 Number of Residues |
283 |
| Enzyme 32 Molecular Weight |
31236 |
| Enzyme 32 Theoretical pI |
7.21 |
| Enzyme 32 GO Classification |
Not Available |
| Enzyme 32 General Function |
Nucleotide transport and metabolism |
| Enzyme 32 Specific Function |
Plays a major role in polyamine metabolism and is important for the salvage of both adenine and methionine |
| Enzyme 32 Pathways |
Not Available |
| Enzyme 32 Reactions |
- S-methyl-5-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
|
| Enzyme 32 Pfam Domain Function |
Not Available |
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
847724  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
Q13126  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
MTAP_HUMAN  |
| Enzyme 32 PDB ID |
1SD2  |
| Enzyme 32 PDB File |
Show |
| Enzyme 32 3D Structure |
|
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>852 bp
ATGGCCTCTGGCACCACCACCACCGCCGTGAAGATTGGAATAATTGGTGGAACAGGCCTG
GATGATCCAGAAATTTTAGAAGGAAGAACTGAAAAATATGTGGATACTCCATTTGGCAAG
CCATCTGATGCCTTAATTTTGGGGAAGATAAAAAATGTTGATTGCATCCTCCTTGCAAGG
CATGGAAGGCAGCACACCATCATGCCTTCAAAGGTCAACTACCAGGCGAACATCTGGGCT
TTGAAGGAAGAGGGCTGTACACATGTCATAGTGACCACAGCTTGTGGCTCCTTGAGGGAG
GAGATTCAGCCCGGCGATATTGTCATTATTGATCAGTTCATTGACAGGACCACTATGAGA
CCTCAGTCCTTCTATGATGGAAGTCATTCTTGTGCCAGAGGAGTGTGCCATATTCCAATG
GCTGAGCCGTTTTGCCCCAAAACGAGAGAGGTTCTTATAGAGACTGCTAAGAAGCTAGGA
CTCCGGTGCCACTCAAAGGGGACAATGGTCACAATCGAGGGACCTCGTTTTAGCTCCCGG
GCAGAAAGCTTCATGTTCCGCACCTGGGGGGCGGATGTTATCAACATGACCACAGTTCCA
GAGGTGGTTCTTGCTAAGGAGGCTGGAATTTGTTACGCAAGTATCGCCATGGCGACAGAT
TATGACTGCTGGAAGGAGCACGAGGAAGCAGTTTCGGTGGACCGGGTCTTAAAGACCCTG
AAAGAAAACGCTAATAAAGCCAAAAGCTTACTGCTCACTACCATACCTCAGATAGGGTCC
ACAGAATGGTCAGAAACCCTCCATAACCTGAAGAATATGGCCCAGTTTTCTGTTTTATTA
CCAAGACATTAA
|
| Enzyme 32 GenBank Gene ID |
U22233  |
| Enzyme 32 GeneCard ID |
MTAP  |
| Enzyme 32 GenAtlas ID |
MTAP  |
| Enzyme 32 HGNC ID |
HGNC:7413  |
| Enzyme 32 Chromosome Location |
Not Available |
| Enzyme 32 Locus |
Not Available |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
- Olopade OI, Pomykala HM, Hagos F, Sveen LW, Espinosa R 3rd, Dreyling MH, Gursky S, Stadler WM, Le Beau MM, Bohlander SK: Construction of a 2.8-megabase yeast artificial chromosome contig and cloning of the human methylthioadenosine phosphorylase gene from the tumor suppressor region on 9p21. Proc Natl Acad Sci U S A. 1995 Jul 3;92(14):6489-93. [PubMed
]
- Nobori T, Takabayashi K, Tran P, Orvis L, Batova A, Yu AL, Carson DA: Genomic cloning of methylthioadenosine phosphorylase: a purine metabolic enzyme deficient in multiple different cancers. Proc Natl Acad Sci U S A. 1996 Jun 11;93(12):6203-8. [PubMed
]
- Della Ragione F, Takabayashi K, Mastropietro S, Mercurio C, Oliva A, Russo GL, Della Pietra V, Borriello A, Nobori T, Carson DA, Zappia V: Purification and characterization of recombinant human 5'-methylthioadenosine phosphorylase: definite identification of coding cDNA. Biochem Biophys Res Commun. 1996 Jun 25;223(3):514-9. [PubMed
]
- Appleby TC, Erion MD, Ealick SE: The structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase at 1.7 A resolution provides insights into substrate binding and catalysis. Structure. 1999 Jun 15;7(6):629-41. [PubMed
]
|
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
5655 |
| Enzyme 33 Name |
S-adenosylmethionine synthetase isoform type-1 |
| Enzyme 33 Synonyms |
- Methionine adenosyltransferase 1
- AdoMet synthetase 1
- Methionine adenosyltransferase I/III
- MAT-I/III
|
| Enzyme 33 Gene Name |
MAT1A |
| Enzyme 33 Protein Sequence |
>S-adenosylmethionine synthetase isoform type-1
MNGPVDGLCDHSLSEGVFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVC
KTGMVLLCGEITSMAMVDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQC
VHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIILAHKLNARMADLRRSGLLPWLRPDS
KTQVTVQYMQDNGAVIPVRIHTIVISVQHNEDITLEEMRRALKEQVIRAVVPAKYLDEDT
VYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARW
VAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSQKTERELLDVVHKNFDLRPGVI
VRDLDLKKPIYQKTACYGHFGRSEFPWEVPRKLVF
|
| Enzyme 33 Number of Residues |
395 |
| Enzyme 33 Molecular Weight |
43648 |
| Enzyme 33 Theoretical pI |
6.24 |
| Enzyme 33 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- methionine adenosyltransferase activity
- nucleotide binding
- purine nucleotide binding
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- cellular metabolism
- metabolism
- one-carbon compound metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 33 General Function |
Coenzyme transport and metabolism |
| Enzyme 33 Specific Function |
Catalyzes the formation of S-adenosylmethionine from methionine and ATP |
| Enzyme 33 Pathways |
|
| Enzyme 33 Reactions |
- ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine
|
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
220066  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
Q00266  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
METK1_HUMAN  |
| Enzyme 33 PDB ID |
1O9T  |
| Enzyme 33 PDB File |
Show |
| Enzyme 33 3D Structure |
|
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>1188 bp
ATGAATGGACCGGTGGATGGCTTGTGTGACCACTCTCTAAGTGAAGGAGTCTTCATGTTC
ACATCGGAGTCTGTGGGAGAGGGACACCCGGATAAGATCTGTGACCAGATCAGTGATGCA
GTGCTGGATGCCCATCTCAAGCAAGACCCCAATGCCAAGGTGGCCTGTGAGACAGTGTGC
AAGACCGGCATGGTGCTGCTGTGTGGTGAGATCACCTCAATGGCCATGGTGGACTACCAG
CGGGTGGTGAGGGACACCATCAAGCACATCGGCTACGATGACTCAGCCAAGGGCTTTGAC
TTCAAGACTTGCAACGTGCTGGTGGCTTTGGAGCAGCAATCCCCAGATATTGCCCAGTGC
GTCCATCTGGACAGAAATGAGGAGGATGTGGGGGCAGGAGATCAGGGTTTGATGTTCGGC
TATGCCACCGACGAGACAGAGGAGTGCATGCCCCTCACCATCATCCTTGCTCACAAGCTC
AACGCCCGGATGGCAGACCTCAGGCGCTCCGGCCTCCTCCCCTGGCTGCGGCCTGACTCT
AAGACTCAGGTGACAGTTCAGTACATGCAGGACAATGGCGCAGTCATCCCTGTGCGCATC
CACACCATCGTCATCTCTGTGCAGCACAACGAAGACATCACGCTGGAGGAGATGCGCAGG
GCCCTGAAGGAGCAAGTCATCAGGGCCGTGGTGCCGGCCAAGTACCTGGACGAAGACACC
GTCTACCACCTGCAGCCCAGTGGGCGGTTTGTCATCGGAGGTCCCCAGGGGGATGCGGGT
GTCACTGGCCGTAAGATTATTGTGGACACCTATGCGGCCTGGGGGGCTCATGGTGGTGGG
GCCTTCTCTGGGAAGGACTACACCAAGGTGGACCGCTCAGCCGCATATGCTGCCCGCTGG
GTGGCCAAGTCTCTGGTGAAAGCAGGGCTCTGCCGGAGAGTGCTTGTCCAGGTTTCCTAT
GCCATTGGTGTGGCCGAGCCGCTGTCCATTTCCATCTTCACCTACGGAACCTCTCAGAAG
ACAGAGCGAGAGCTGCTGGATGTGGTGCATAAGAACTTCGACCTCCGGCCGGGCGTCATT
GTCAGGGACTTGGATTTGAAGAAGCCCATCTACCAGAAGACAGCATGCTACGGCCATTTC
GGAAGAAGCGAGTTCCCATGGGAGGTTCCCAGGAAGCTTGTATTTTAG
|
| Enzyme 33 GenBank Gene ID |
D49357  |
| Enzyme 33 GeneCard ID |
MAT1A  |
| Enzyme 33 GenAtlas ID |
MAT1A  |
| Enzyme 33 HGNC ID |
HGNC:6903  |
| Enzyme 33 Chromosome Location |
Not Available |
| Enzyme 33 Locus |
Not Available |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
- Alvarez L, Corrales F, Martin-Duce A, Mato JM: Characterization of a full-length cDNA encoding human liver S-adenosylmethionine synthetase: tissue-specific gene expression and mRNA levels in hepatopathies. Biochem J. 1993 Jul 15;293 ( Pt 2):481-6. [PubMed
]
- Horikawa S, Tsukada K: Molecular cloning and nucleotide sequence of cDNA encoding the human liver S-adenosylmethionine synthetase. Biochem Int. 1991 Sep;25(1):81-90. [PubMed
]
- Ubagai T, Lei KJ, Huang S, Mudd SH, Levy HL, Chou JY: Molecular mechanisms of an inborn error of methionine pathway. Methionine adenosyltransferase deficiency. J Clin Invest. 1995 Oct;96(4):1943-7. [PubMed
]
- Chamberlin ME, Ubagai T, Mudd SH, Wilson WG, Leonard JV, Chou JY: Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency. J Clin Invest. 1996 Aug 15;98(4):1021-7. [PubMed
]
- Chamberlin ME, Ubagai T, Mudd SH, Levy HL, Chou JY: Dominant inheritance of isolated hypermethioninemia is associated with a mutation in the human methionine adenosyltransferase 1A gene. Am J Hum Genet. 1997 Mar;60(3):540-6. [PubMed
]
- Chamberlin ME, Ubagai T, Mudd SH, Thomas J, Pao VY, Nguyen TK, Levy HL, Greene C, Freehauf C, Chou JY: Methionine adenosyltransferase I/III deficiency: novel mutations and clinical variations. Am J Hum Genet. 2000 Feb;66(2):347-55. [PubMed
]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
5755 |
| Enzyme 34 Name |
Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial precursor |
| Enzyme 34 Synonyms |
- 3-methylcrotonyl-CoA carboxylase 2
- MCCase subunit beta
- 3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta
- 3- methylcrotonyl-CoA carboxylase non-biotin-containing subunit
|
| Enzyme 34 Gene Name |
MCCC2 |
| Enzyme 34 Protein Sequence |
>Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial precursor
MWAVLRLALRPCARASPAGPRAYHGDSVASLGTQPDLGSALYQENYKQMKALVNQLHERV
EHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSPFLELSQFAGYQLYDNEEVPGGGII
TGIGRVSGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPR
QADVFPDRDHFGRTFYNQAIMSSKNIAQIAVVMGSCTAGGAYVPAMADENIIVRKQGTIF
LAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVVRNLNYQKKL
DVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTGFA
RIFGYPVGIVGNNGVLFSESAKKGTHFVQLCCQRNIPLLFLQNITGFMVGREYEAEGIAK
DGAKMVAAVACAQVPKITLIIGGSYGAGNYGMCGRAYSPRFLYIWPNARISVMGGEQAAN
VLATITKDQRAREGKQFSSADEAALKEPIIKKFEEEGNPYYSSARVWDDGIIDPADTRLV
LGLSFSAALNAPIEKTDFGIFRM
|
| Enzyme 34 Number of Residues |
563 |
| Enzyme 34 Molecular Weight |
61334 |
| Enzyme 34 Theoretical pI |
7.75 |
| Enzyme 34 GO Classification |
| Function |
- catalytic activity
- ligase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 34 General Function |
Not Available |
| Enzyme 34 Specific Function |
ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-methylglutaconyl-CoA |
| Enzyme 34 Pathways |
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 34 Reactions |
- ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA
|
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
Not Available |
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
10934059  |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
Q9HCC0  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
MCCC2_HUMAN  |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>1692 bp
ATGTGGGCCGTCCTGAGGTTAGCCCTGCGGCCGTGTGCCCGCGCCTCTCCCGCCGGGCCG
CGCGCCTATCACGGGGACTCGGTGGCCTCGCTGGGCACCCAGCCGGACTTGGGCTCTGCC
CTCTACCAGGAGAACTACAAGCAGATGAAAGCACTAGTAAATCAGCTCCATGAACGAGTG
GAGCATATAAAACTAGGAGGTGGTGAGAAAGCCCGAGCACTTCACATATCAAGAGGAAAA
CTATTGCCCAGAGAAAGAATTGACAATCTCATAGACCCAGGGTCTCCATTTCTGGAATTA
TCCCAGTTTGCAGGTTACCAGTTATATGACAATGAGGAGGTGCCAGGAGGTGGCATTATT
ACAGGCATTGGAAGAGTATCAGGAGTAGAATGCATGATTATTGCCAATGATGCCACCGTC
AAAGGAGGTGCCTACTACCCAGTGACTGTGAAAAAACAATTACGGGCCCAAGAAATTGCC
ATGCAAAACAGGCTCCCCTGCATCTACTTAGTTGATTCGGGAGGAGCATACTTACCTCGA
CAAGCAGATGTGTTTCCAGATCGAGACCACTTTGGCCGTACATTCTATAATCAGGCAATT
ATGTCTTCTAAAAATATTGCACAGATCGCAGTGGTCATGGGCTCCTGCACCGCAGGAGGA
GCCTATGTGCCTGCCATGGCTGATGAAAACATCATTGTACGCAAGCAGGGTACCATTTTC
TTGGCAGGACCCCCCTTGGTTAAAGCGGCAACTGGGGAAGAAGTATCTGCTGAGGATCTT
GGAGGTGCTGATCTTCATTGCAGAAAGTCTGGAGTAAGTGACCACTGGGCTTTGGATGAT
CATCATGCCCTTCACTTAACTAGGAAGGTTGTGAGGAATCTAAATTATCAGAAGAAATTG
GATGTCACCATTGAACCTTCTGAAGAGCCTTTATTTCCTGCTGATGAATTGTATGGAATA
GTTGGTGCTAACCTTAAGAGGAGCTTTGATGTCCGAGAGGTCATTGCTAGAATCGTGGAT
GGAAGCAGATTCACTGAGTTCAAAGCCTTTTATGGAGACACATTAGTTACAGGATTTGCT
CGAATATTTGGGTACCCAGTAGGTATCGTTGGAAACAACGGAGTTCTCTTTTCTGAATCT
GCAAAAAAGGGTACTCACTTTGTCCAGTTATGCTGCCAAAGAAATATTCCTCTGCTGTTC
CTTCAAAACATTACTGGATTTATGGTTGGTAGAGAGTATGAAGCTGAAGGAATTGCCAAG
GATGGTGCCAAGATGGTGGCCGCTGTGGCCTGTGCCCAAGTGCCTAAGATAACCCTCATC
ATTGGGGGCTCCTATGGAGCCGGAAACTATGGGATGTGTGGCAGAGCGTATAGCCCAAGA
TTTCTCTACATTTGGCCAAATGCTCGTATCTCAGTGATGGGAGGAGAGCAGGCAGCCAAT
GTGTTGGCCACGATAACAAAGGACCAAAGAGCCCGGGAAGGAAAGCAGTTCTCCAGTGCT
GATGAAGCGGCTTTAAAAGAGCCCATCATTAAGAAGTTTGAAGAGGAAGGAAACCCTTAC
TATTCCAGCGCAAGGGTATGGGATGATGGGATCATTGATCCAGCAGACACCAGACTGGTC
TTGGGTCTCAGTTTTAGTGCAGCCCTCAACGCACCAATAGAGAAGACTGACTTCGGTATC
TTCAGGATGTAA
|
| Enzyme 34 GenBank Gene ID |
AB050049  |
| Enzyme 34 GeneCard ID |
MCCC2  |
| Enzyme 34 GenAtlas ID |
MCCC2  |
| Enzyme 34 HGNC ID |
HGNC:6937  |
| Enzyme 34 Chromosome Location |
Not Available |
| Enzyme 34 Locus |
Not Available |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
- Holzinger A, Roschinger W, Lagler F, Mayerhofer PU, Lichtner P, Kattenfeld T, Thuy LP, Nyhan WL, Koch HG, Muntau AC, Roscher AA: Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency. Hum Mol Genet. 2001 Jun 1;10(12):1299-306. [PubMed
]
- Baumgartner MR, Almashanu S, Suormala T, Obie C, Cole RN, Packman S, Baumgartner ER, Valle D: The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency. J Clin Invest. 2001 Feb;107(4):495-504. [PubMed
]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
5757 |
| Enzyme 35 Name |
Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial precursor |
| Enzyme 35 Synonyms |
- 3-methylcrotonyl-CoA carboxylase 1
- MCCase subunit alpha
- 3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha
- 3- methylcrotonyl-CoA carboxylase biotin-containing subunit
|
| Enzyme 35 Gene Name |
MCCC1 |
| Enzyme 35 Protein Sequence |
>Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial precursor
MAAASAVSVLLVAAERNRWHRLPSLLLPPRTWVWRQRTMKYTTATGRNITKVLIANRGEI
ACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTS
AAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEG
YHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFN
DDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRK
KLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQL
RIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRADPSTRIETGV
RQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFE
AGNVHTDFIPQHHKQLLLSRKAAAKESLCQAALGLILKEKAMTDTFTLQAHDQFSPFSSS
SGRRLNISYTRNMTLKDGKNNVAIAVTYNHDGSYSMQIEDKTFQVLGNLYSEGDCTYLKC
SVNGVASKAKLIILENTIYLFSKEGSIEIDIPVPKYLSSVSSQETQGGPLAPMTGTIEKV
FVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEESD
KRESE
|
| Enzyme 35 Number of Residues |
725 |
| Enzyme 35 Molecular Weight |
80474 |
| Enzyme 35 Theoretical pI |
7.86 |
| Enzyme 35 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- biotin binding
- catalytic activity
- ligase activity
- nucleotide binding
- purine nucleotide binding
- vitamin binding
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 35 General Function |
Not Available |
| Enzyme 35 Specific Function |
ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-methylglutaconyl-CoA |
| Enzyme 35 Pathways |
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 35 Reactions |
- ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA
|
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
Not Available |
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
12382296  |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
Q96RQ3  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
MCCA_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>2178 bp
ATGGCGGCGGCCTCTGCGGTGTCGGTGCTGCTGGTGGCGGCGGAGAGGAACCGGTGGCAT
CGTCTCCCGAGCCTGCTCCTGCCGCCGAGGACATGGGTGTGGAGGCAAAGAACCATGAAG
TACACAACAGCCACAGGAAGAAACATTACCAAGGTCCTCATTGCAAACAGAGGAGAAATT
GCCTGCAGGGTGATGCGCACAGCCAAAAAACTGGGTGTACAGACTGTGGCGGTTTATAGT
GAGGCTGACAGAAATTCCATGCATGTAGATATGGCAGATGAAGCATATTCCATCGGCCCC
GCTCCCTCCCAGCAGAGCTACCTATCTATGGAGAAAATCATTCAAGTGGCCAAGACCTCT
GCTGCACAGGCTATCCATCCAGGATGCGGTTTTCTTTCAGAAAACATGGAATTTGCTGAA
CTTTGTAAGCAAGAAGGAATTATTTTTATAGGCCCTCCTCCATCTGCAATTAGAGACATG
GGTATAAAGAGCACATCCAAATCCATAATGGCTGCTGCTGGAGTACCTGTTGTGGAGGGT
TATCATGGTGAGGACCAATCAGACCAGTGCCTGAAGGAACACGCCAGGAGAATTGGCTAT
CCTGTCATGATTAAAGCCGTCCGGGGTGGAGGAGGAAAAGGAATGAGGATTGTTAGATCA
GAACAAGAATTTCAAGAACAGTTAGAGTCAGCACGGAGAGAAGCTAAGAAGTCTTTCAAT
GATGATGCTATGCTGATCGAGAAGTTTGTAGACACACCGAGGCATGTAGAAGTCCAGGTG
TTTGGTGATCACCATGGCAATGCTGTGTACTTGTTTGAAAGAGACTGTAGTGTGCAGAGG
CGACATCAGAAGATCATTGAGGAGGCCCCAGCGCCTGGTATTAAATCTGAAGTAAGAAAA
AAGCTGGGAGAAGCTGCAGTCAGAGCTGCTAAAGCTGTAAATTATGTTGGAGCAGGGACT
GTGGAGTTTATTATGGACTCAAAACATAATTTCTGTTTCATGGAGATGAATACAAGGCTG
CAAGTGGAACATCCTGTTACTGAGATGATCACAGGAACTGACTTGGTGGAGTGGCAGCTT
AGAATTGCAGCAGGAGAGAAGATTCCTTTGAGCCAGGAAGAAATAACTCTGCAGGGCCAT
GCCTTCGAAGCTAGAATATATGCAGAAGATCCTAGCAATAACTTCATGCCTGTGGCAGGC
CCATTAGTGCACCTCTCTACTCCTCGAGCAGACCCTTCCACCAGGATTGAAACTGGAGTA
CGGCAAGGAGACGAAGTTTCCGTGCATTATGACCCCATGATTGCGAAGCTGGTCGTGTGG
GCAGCAGATCGCCAGGCGGCATTGACAAAACTGAGGTACAGCCTTCGTCAGTACAATATT
GTTGGACTGCACACCAACATTGACTTCTTACTCAACCTGTCTGGCCACCCAGAGTTTGAA
GCTGGGAACGTGCACACTGATTTCATCCCTCAACACCACAAACAGTTGTTGCTCAGTCGG
AAGGCTGCAGCCAAAGAGTCTTTATGCCAGGCAGCCCTGGGTCTCATCCTCAAGGAGAAA
GCCATGACCGACACTTTCACTCTTCAGGCACATGATCAATTCTCTCCATTTTCGTCTAGC
AGTGGAAGAAGACTGAATATCTCGTATACCAGAAACATGACTCTTAAAGATGGTAAAAAC
AATGTAGCCATAGCTGTAACGTATAACCATGATGGGTCTTATAGCATGCAGATTGAAGAT
AAAACTTTCCAAGTCCTTGGTAATCTTTACAGCGAGGGAGACTGCACTTACCTGAAATGT
TCTGTTAATGGAGTTGCTAGTAAAGCGAAGCTGATTATCCTGGAAAACACTATTTACCTA
TTTTCCAAGGAAGGAAGTATTGAGATTGACATTCCAGTCCCCAAATACTTATCTTCTGTG
AGCTCACAAGAAACTCAGGGCGGCCCCTTAGCTCCTATGACTGGAACCATTGAAAAGGTG
TTTGTCAAAGCTGGAGACAAAGTGAAAGCGGGAGATTCCCTCATGGTTATGATCGCCATG
AAGATGGAGCATACCATAAAGTCTCCAAAGGATGGCACAGTAAAGAAAGTGTTCTACAGA
GAAGGTGCTCAGGCCAACAGACACACTCCTTTAGTCGAGTTTGAGGAGGAAGAATCAGAC
AAAAGGGAATCGGAATAA
|
| Enzyme 35 GenBank Gene ID |
AF310972  |
| Enzyme 35 GeneCard ID |
MCCC1  |
| Enzyme 35 GenAtlas ID |
MCCC1  |
| Enzyme 35 HGNC ID |
HGNC:6936  |
| Enzyme 35 Chromosome Location |
3 |
| Enzyme 35 Locus |
3q27 |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 General References |
- Obata K, Fukuda T, Morishita R, Abe S, Asakawa S, Yamaguchi S, Yoshino M, Ihara K, Murayama K, Shigemoto K, Shimizu N, Kondo I: Human biotin-containing subunit of 3-methylcrotonyl-CoA carboxylase gene (MCCA): cDNA sequence, genomic organization, localization to chromosomal band 3q27, and expression. Genomics. 2001 Mar 1;72(2):145-52. [PubMed
]
- Holzinger A, Roschinger W, Lagler F, Mayerhofer PU, Lichtner P, Kattenfeld T, Thuy LP, Nyhan WL, Koch HG, Muntau AC, Roscher AA: Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency. Hum Mol Genet. 2001 Jun 1;10(12):1299-306. [PubMed
]
- Baumgartner MR, Almashanu S, Suormala T, Obie C, Cole RN, Packman S, Baumgartner ER, Valle D: The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency. J Clin Invest. 2001 Feb;107(4):495-504. [PubMed
]
|
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
5759 |
| Enzyme 36 Name |
Glutamate--cysteine ligase catalytic subunit |
| Enzyme 36 Synonyms |
- Gamma- glutamylcysteine synthetase
- Gamma-ECS
- GCS heavy chain
|
| Enzyme 36 Gene Name |
GCLC |
| Enzyme 36 Protein Sequence |
>Glutamate--cysteine ligase catalytic subunit
MGLLSQGSPLSWEETKRHADHVRRHGILQFLHIYHAVKDRHKDVLKWGDEVEYMLVSFDH
ENKKVRLVLSGEKVLETLQEKGERTNPNHPTLWRPEYGSYMIEGTPGQPYGGTMSEFNTV
EANMRKRRKEATSILEENQALCTITSFPRLGCPGFTLPEVKPNPVEGGASKSLFFPDEAI
NKHPRFSTLTRNIRHRRGEKVVINVPIFKDKNTPSPFIETFTEDDEASRASKPDHIYMDA
MGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVI
SASVDDRTREERGLEPLKNNNYRISKSRYDSIDSYLSKCGEKYNDIDLTIDKEIYEQLLQ
EGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDANESDHFENIQSTNWQTMRFKPPPPNSDI
GWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMKVAQKRDAVL
QGMFYFRKDICKGGNAVVDGCGKAQNSTELAAEEYTLMSIDTIINGKEGVFPGLIPILNS
YLENMEVDVDTRCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYS
LILKCNQIANELCECPELLGSAFRKVKYSGSKTDSSN
|
| Enzyme 36 Number of Residues |
637 |
| Enzyme 36 Molecular Weight |
72767 |
| Enzyme 36 Theoretical pI |
5.98 |
| Enzyme 36 GO Classification |
| Function |
- acid-amino acid ligase activity
- catalytic activity
- glutamate-cysteine ligase activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
|
| Process |
- cellular metabolism
- coenzyme metabolism
- cofactor metabolism
- glutathione biosynthesis
- glutathione metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 36 General Function |
Not Available |
| Enzyme 36 Specific Function |
ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine |
| Enzyme 36 Pathways |
|
| Enzyme 36 Reactions |
- ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
|
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
183039  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
P48506  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
GSH1_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>1914 bp
ATGGGGCTGCTGTCCCAGGGCTCGCCGCTGAGCTGGGAGGAAACCAAGCGCCATGCCGAC
CACGTGCGGCGGCACGGGATCCTCCAGTTCCTGCACATCTACCACGCCGTCAAGGACCGG
CACAAGGACGTTCTCAAGTGGGGCGATGAGGTGGAATACATGTTGGTATCTTTTGATCAT
GAAAATAAAAAAGTCCGGTTGGTCCTGTCTGGGGAGAAAGTTCTTGAAACTCTGCAAGAG
AAGGGGGAAAGGACAAACCCAAACCATCCTACCCTTTGGAGACCAGAGTATGGGAGTTAC
ATGATTGAAGGGACACCAGGACAGCCCTACGGAGGAACAATGTCCGAGTTCAATACAGTT
GAGGCCAACATGCGAAAACGCCGGAAGGAGGCTACTTCTATATTAGAAGAAAATCAGGCT
CTTTGCACAATAACTTCATTTCCCAGATTAGGCTGTCCTGGGTTCACACTGCCCGAGGTC
AAACCCAACCCAGTGGAAGGAGGAGCTTCCAAGTCCCTCTTCTTTCCAGATGAAGCAATA
AACAAGCACCCTCGCTTCAGTACCTTAACAAGAAATATCCGACATAGGAGAGGAGAAAAG
GTTGTCATCAATGTACCAATATTTAAGGACAAGAATACACCATCTCCATTTATAGAAACA
TTTACTGAGGATGATGAAGCTTCAAGGGCTTCTAAGCCGGATCATATTTACATGGATGCC
ATGGGATTTGGAATGGGCAATTGCTGTCTCCAGGTGACATTCCAAGCCTGCAGTATATCT
GAGGCCAGATACCTTTATGATCAGTTGGCTACTATCTGTCCAATTGTTATGGCTTTGAGT
GCTGCATCTCCCTTTTACCGAGGCTATGTGTCAGACATTGATTGTCGCTGGGGAGTGATT
TCTGCATCTGTAGATGATAGAACTCGGGAGGAGCGAGGACTGGAGCCATTGAAGAACAAT
AACTATAGGATCAGTAAATCCCGATATGACTCAATAGACAGCTATTTATCTAAGTGTGGT
GAGAAATATAATGACATCGACTTGACGATAGATAAAGAGATCTACGAACAGCTGTTGCAG
GAAGGCATTGATCATCTCCTGGCCCAGCATGTTGCTCATCTCTTTATTAGAGACCCACTG
ACACTGTTTGAAGAGAAAATACACCTGGATGATGCTAATGAGTCTGACCATTTTGAGAAT
ATTCAGTCCACAAATTGGCAGACAATGAGATTTAAGCCCCCTCCTCCAAACTCAGACATT
GGATGGAGAGTAGAATTTCGACCCATGGAGGTGCAATTAACAGACTTTGAGAACTCTGCC
TATGTGGTGTTTGTGGTACTGCTCACCAGAGTGATCCTTTCCTACAAATTGGATTTTCTC
ATTCCACTGTCAAAGGTTGATGAGAACATGAAGGTAGCACAGAAAAGAGATGCTGTCTTG
CAGGGAATGTTTTATTTCAGGAAAGATATTTGCAAAGGTGGCAATGCAGTGGTGGATGGT
TGTGGCAAGGCCCAGAACAGCACGGAGCTCGCTGCAGAGGAGTACACCCTCATGAGCATA
GACACCATCATCAATGGGAAGGAAGGTGTGTTTCCTGGACTGATCCCAATTCTGAACTCT
TACCTTGAAAACATGGAAGTGGATGTGGACACCAGATGTAGTATTCTGAACTACCTAAAG
CTAATTAAGAAGAGAGCATCTGGAGAACTAATGACAGTTGCCAGATGGATGAGGGAGTTT
ATCGCAAACCATCCTGACTACAAGCAAGACAGTGTCATAACTGATGAAATGAATTATAGC
CTTATTTTGAAGTGTAACCAAATTGCAAATGAATTATGTGAATGCCCAGAGTTACTTGGA
TCAGCATTTAGGAAAGTAAAATATAGTGGAAGTAAAACTGACTCATCCAACTAG
|
| Enzyme 36 GenBank Gene ID |
M90656  |
| Enzyme 36 GeneCard ID |
GCLC  |
| Enzyme 36 GenAtlas ID |
GCLC  |
| Enzyme 36 HGNC ID |
HGNC:4311  |
| Enzyme 36 Chromosome Location |
6 |
| Enzyme 36 Locus |
6p12 |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
- Gipp JJ, Chang C, Mulcahy RT: Cloning and nucleotide sequence of a full-length cDNA for human liver gamma-glutamylcysteine synthetase. Biochem Biophys Res Commun. 1992 May 29;185(1):29-35. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Mulcahy RT, Gipp JJ: Identification of a putative antioxidant response element in the 5'-flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene. Biochem Biophys Res Commun. 1995 Apr 6;209(1):227-33. [PubMed
]
- Beutler E, Gelbart T, Kondo T, Matsunaga AT: The molecular basis of a case of gamma-glutamylcysteine synthetase deficiency. Blood. 1999 Oct 15;94(8):2890-4. [PubMed
]
- Ristoff E, Augustson C, Geissler J, de Rijk T, Carlsson K, Luo JL, Andersson K, Weening RS, van Zwieten R, Larsson A, Roos D: A missense mutation in the heavy subunit of gamma-glutamylcysteine synthetase gene causes hemolytic anemia. Blood. 2000 Apr 1;95(7):2193-6. [PubMed
]
|
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
5801 |
| Enzyme 37 Name |
Uridine phosphorylase 1 |
| Enzyme 37 Synonyms |
- UrdPase 1
- UPase 1
|
| Enzyme 37 Gene Name |
UPP1 |
| Enzyme 37 Protein Sequence |
>Uridine phosphorylase 1
MAATGANAEKAESHNDCPVRLLNPNIAKMKEDILYHFNLTTSRHNFPALFGDVKFVCVGG
SPSRMKAFIRCVGAELGLDCPGRDYPNICAGTDRYAMYKVGPVLSVSHGMGIPSISIMLH
ELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKT
DLNKKLVQELLLCSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAY
AAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDQISSPRNVLSEYQQRPQRLVS
YFIKKKLSKA
|
| Enzyme 37 Number of Residues |
310 |
| Enzyme 37 Molecular Weight |
33935 |
| Enzyme 37 Theoretical pI |
7.95 |
| Enzyme 37 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring pentosyl groups
- uridine phosphorylase activity
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleoside metabolism
- nucleotide catabolism
- nucleotide metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 37 General Function |
Nucleotide transport and metabolism |
| Enzyme 37 Specific Function |
Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1- phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis |
| Enzyme 37 Pathways |
|
| Enzyme 37 Reactions |
- uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
|
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
1050525  |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
Q16831  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
UPP1_HUMAN  |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
>933 bp
ATGGCGGCCACGGGAGCCAATGCAGAGAAAGCTGAAAGTCACAATGATTGCCCCGTCAGA
CTTTTAAATCCAAACATAGCAAAAATGAAAGAAGATATTCTCTATCATTTCAATCTCACC
ACTAGCAGACACAATTTCCCAGCCTTGTTTGGAGATGTGAAGTTTGTGTGTGTTGGTGGA
AGCCCCTCCCGGATGAAAGCCTTCATCAGGTGCGTTGGTGCAGAGCTGGGCCTTGACTGC
CCAGGTAGAGACTATCCCAACATCTGTGCGGGAACTGACCGCTATGCCATGTATAAAGTA
GGACCGGTGCTGTCTGTCAGTCATGGTATGGGCATTCCTTCTATCTCAATCATGTTGCAT
GAGCTCATAAAGCTGCTGTACTATGCCCGGTGCTCCAACGTCACTATCATCCGCATTGGC
ACTTCTGGTGGGATAGGTCTGGAGCCCGGCACTGTGGTCATAACAGAGCAGGCAGTGGAT
ACCTGCTTCAAGGCAGAGTTTGAGCAGATTGTCCTGGGGAAGCGGGTCATCCGGAAAACG
GACCTTAACAAGAAGCTGGTGCAGGAGCTGTTGCTGTGTTCTGCAGAGCTGAGCGAGTTC
ACCACAGTGGTGGGGAACACCATGTGCACCTTGGACTTCTATGAAGGGCAAGGCCGTCTG
GATGGGGCTCTCTGCTCCTACACGGAGAAGGACAAGCAGGCGTATCTGGAGGCAGCCTAT
GCAGCCGGCGTCCGCAATATCGAGATGGAGTCCTCGGTGTTTGCCGCCATGTGCAGCGCC
TGCGGCCTCCAAGCGGCCGTGGTGTGTGTCACCCTCCTGAACCGCCTGGAAGGGGACCAG
ATCAGCAGCCCTCGCAATGTGCTCAGCGAGTACCAGCAGAGGCCGCAGCGGCTGGTGAGC
TACTTCATCAAGAAGAAACTGAGCAAGGCCTGA
|
| Enzyme 37 GenBank Gene ID |
X90858  |
| Enzyme 37 GeneCard ID |
UPP1  |
| Enzyme 37 GenAtlas ID |
UPP1  |
| Enzyme 37 HGNC ID |
HGNC:12576  |
| Enzyme 37 Chromosome Location |
7 |
| Enzyme 37 Locus |
7p12.3 |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
- Watanabe S, Uchida T: Cloning and expression of human uridine phosphorylase. Biochem Biophys Res Commun. 1995 Nov 2;216(1):265-72. [PubMed
]
|
| Enzyme 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
5805 |
| Enzyme 38 Name |
Purine nucleoside phosphorylase |
| Enzyme 38 Synonyms |
- Inosine phosphorylase
- PNP
|
| Enzyme 38 Gene Name |
NP |
| Enzyme 38 Protein Sequence |
>Purine nucleoside phosphorylase
MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRST
VPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGL
NPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQ
MGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSL
ITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS
|
| Enzyme 38 Number of Residues |
289 |
| Enzyme 38 Molecular Weight |
32118 |
| Enzyme 38 Theoretical pI |
6.95 |
| Enzyme 38 GO Classification |
| Function |
- catalytic activity
- purine-nucleoside phosphorylase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring pentosyl groups
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 38 General Function |
Nucleotide transport and metabolism |
| Enzyme 38 Specific Function |
Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate |
| Enzyme 38 Pathways |
|
| Enzyme 38 Reactions |
- purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
|
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
35565  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
P00491  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
PNPH_HUMAN  |
| Enzyme 38 PDB ID |
1RT9  |
| Enzyme 38 PDB File |
Show |
| Enzyme 38 3D Structure |
|
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>870 bp
ATGGAGAACGGATACACCTATGAAGATTATAAGAACACTGCAGAATGGCTTCTGTCTCAT
ACTAAGCACCGACCTCAAGTTGCAATAATCTGTGGTTCTGGATTAGGAGGTCTGACTGAT
AAATTAACTCAGGCCCAGATCTTTGACTACAGTGAAATCCCCAACTTTCCTCGAAGTACA
GTGCCAGGTCATGCTGGCCGACTGGTGTTTGGGTTCCTGAATGGCAGGGCCTGTGTGATG
ATGCAGGGCAGGTTCCACATGTATGAAGGGTACCCACTCTGGAAGGTGACATTCCCAGTG
AGGGTTTTCCACCTTCTGGGTGTGGACACCCTGGTAGTCACCAATGCAGCAGGAGGGCTG
AACCCCAAGTTTGAGGTTGGAGATATCATGCTGATCCGTGACCATATCAACCTACCTGGT
TTCAGTGGTCAGAACCCTCTCAGAGGGCCCAATGATGAAAGGTTTGGAGATCGTTTCCCT
GCCATGTCTGATGCCTACGACCGGACTATGAGGCAGAGGGCTCTCAGTACCTGGAAACAA
ATGGGGGAGCAACGTGAGCTACAGGAAGGCACCTATGTGATGGTGGCAGGCCCCAGCTTT
GAGACTGTGGCAGAATGTCGTGTGCTGCAGAAGCTGGGAGCAGACGCTGTTGGCATGAGT
ACAGTACCAGAAGTTATCGTTGCACGGCACTGTGGACTTCGAGTCTTTGGCTTCTCACTC
ATCACTAACAAGGTCATCATGGATTATGAAAGCCTGGAGAAGGCCAACCATGAAGAAGTC
TTAGCAGCTGGCAAACAAGCTGCACAGAAATTGGAACAGTTTGTCTCCATTCTTATGGCC
AGCATTCCACTCCCTGACAAAGCCAGTTGA
|
| Enzyme 38 GenBank Gene ID |
X00737  |
| Enzyme 38 GeneCard ID |
NP  |
| Enzyme 38 GenAtlas ID |
NP  |
| Enzyme 38 HGNC ID |
HGNC:7892  |
| Enzyme 38 Chromosome Location |
14 |
| Enzyme 38 Locus |
14q13.1 |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 General References |
- Williams SR, Goddard JM, Martin DW Jr: Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization. Nucleic Acids Res. 1984 Jul 25;12(14):5779-87. [PubMed
]
- Williams SR, Gekeler V, McIvor RS, Martin DW Jr: A human purine nucleoside phosphorylase deficiency caused by a single base change. J Biol Chem. 1987 Feb 15;262(5):2332-8. [PubMed
]
- Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. [PubMed
]
- Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE Jr, et al.: Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. J Biol Chem. 1990 Jan 25;265(3):1812-20. [PubMed
]
- Aust MR, Andrews LG, Barrett MJ, Norby-Slycord CJ, Markert ML: Molecular analysis of mutations in a patient with purine nucleoside phosphorylase deficiency. Am J Hum Genet. 1992 Oct;51(4):763-72. [PubMed
]
- Pannicke U, Tuchschmid P, Friedrich W, Bartram CR, Schwarz K: Two novel missense and frameshift mutations in exons 5 and 6 of the purine nucleoside phosphorylase (PNP) gene in a severe combined immunodeficiency (SCID) patient. Hum Genet. 1996 Dec;98(6):706-9. [PubMed
]
|
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
5824 |
| Enzyme 39 Name |
Acylphosphatase-2 |
| Enzyme 39 Synonyms |
- Acylphosphate phosphohydrolase 2
- Acylphosphatase, muscle type isozyme
|
| Enzyme 39 Gene Name |
ACYP2 |
| Enzyme 39 Protein Sequence |
>Acylphosphatase-2
MSTAQSLKSVDYEVFGRVQGVCFRMYTEDEARKIGVVGWVKNTSKGTVTGQVQGPEDKVN
SMKSWLSKVGSPSSRIDRTNFSNEKTISKLEYSNFSIRY
|
| Enzyme 39 Number of Residues |
99 |
| Enzyme 39 Molecular Weight |
11140 |
| Enzyme 39 Theoretical pI |
10.01 |
| Enzyme 39 GO Classification |
| Function |
- acylphosphatase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 39 General Function |
Energy production and conversion |
| Enzyme 39 Specific Function |
Its physiological role is not yet clear |
| Enzyme 39 Pathways |
|
| Enzyme 39 Reactions |
- An acylphosphate + H2O = a carboxylate + phosphate
|
| Enzyme 39 Pfam Domain Function |
|
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
15341747  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
P14621  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
ACYP2_HUMAN  |
| Enzyme 39 PDB ID |
1APS  |
| Enzyme 39 PDB File |
Show |
| Enzyme 39 3D Structure |
|
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>300 bp
ATGTCTACCGCCCAGTCACTCAAATCCGTGGACTACGAGGTGTTCGGAAGAGTGCAGGGT
GTTTGCTTCAGAATGTATACAGAAGATGAAGCTAGGAAAATAGGAGTGGTTGGCTGGGTG
AAGAATACCAGCAAAGGCACCGTGACAGGCCAAGTGCAGGGGCCAGAAGACAAAGTCAAT
TCCATGAAGTCCTGGCTGAGCAAGGTTGGAAGCCCTAGTTCTCGCATTGACCGCACAAAC
TTTTCTAATGAAAAAACCATCTCTAAGCTTGAATACTCTAATTTTAGTATTAGATACTAA
|
| Enzyme 39 GenBank Gene ID |
BC012290  |
| Enzyme 39 GeneCard ID |
ACYP2  |
| Enzyme 39 GenAtlas ID |
ACYP2  |
| Enzyme 39 HGNC ID |
HGNC:180  |
| Enzyme 39 Chromosome Location |
2 |
| Enzyme 39 Locus |
2p16.2 |
| Enzyme 39 SNPs |
SNPJam Report  |
| Enzyme 39 General References |
- Manao G, Camici G, Modesti A, Liguri G, Berti A, Stefani M, Cappugi G, Ramponi G: Human skeletal muscle acylphosphatase: the primary structure. Mol Biol Med. 1984 Dec;2(6):369-78. [PubMed
]
- Chiarugi P, Raugei G, Marzocchini R, Fiaschi T, Ciccarelli C, Berti A, Ramponi G: Differential modulation of expression of the two acylphosphatase isoenzymes by thyroid hormone. Biochem J. 1995 Oct 15;311 ( Pt 2):567-73. [PubMed
]
|
| Enzyme 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
5925 |
| Enzyme 40 Name |
Selenide, water dikinase 1 |
| Enzyme 40 Synonyms |
- Selenophosphate synthetase 1
- Selenium donor protein 1
|
| Enzyme 40 Gene Name |
SEPHS1 |
| Enzyme 40 Protein Sequence |
>Selenide, water dikinase 1
MSTRESFNPESYELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAV
MPRLGIGMDTCVIPLRHGGLSLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECD
NMLMLLGVSNKMTDRERDKVMPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTVC
QPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEA
MMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMA
AVSKACGNMFGLMHGTCPETSGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKG
NRTARIIDKPRIIEVAPQVATQNVNPTPGATS
|
| Enzyme 40 Number of Residues |
392 |
| Enzyme 40 Molecular Weight |
42911 |
| Enzyme 40 Theoretical pI |
5.84 |
| Enzyme 40 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleotide binding
- purine nucleotide binding
- selenide, water dikinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 40 General Function |
Amino acid transport and metabolism |
| Enzyme 40 Specific Function |
Synthesizes selenophosphate from selenide and ATP |
| Enzyme 40 Pathways |
|
| Enzyme 40 Reactions |
- ATP + selenide + H2O = AMP + selenophosphate + phosphate
|
| Enzyme 40 Pfam Domain Function |
|
| Enzyme 40 Signals |
|
| Enzyme 40 Transmembrane Regions |
|
| Enzyme 40 Essentiality |
Not Available |
| Enzyme 40 GenBank ID Protein |
1000284  |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
P49903  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
SPS1_HUMAN  |
| Enzyme 40 PDB ID |
Not Available |
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
>1152 bp
ATGTCTACGCGGGAGTCCTTTAACCCGGAAAGTTACGAATTGGACAAAAGCTTCCGGCTA
ACCAGATTCACTGAACTGAAGGGCACAGGCTGCAAAGTGCCCCAAGATGTCCTGCAAAAA
TTGCTGGAATCTTTACAGGAGAACCACTTCCAAGAAGATGAGCAGTTTCTGGGAGCCGTT
ATGCCAAGGCTTGGCATTGGAATGGATACTTGTGTCATTCCTTTGAGGCACGGTGGGCTT
TCCTTGGTTCAAACCACAGATTACATTTACCCGATCGTAGACGACCCTTACATGATGGGC
AGGATAGCGTGTGCCAATGTCCTCAGTGACCTCTATGCAATGGGGGTCACGGAATGTGAC
AATATGCTGATGCTCCTTGGAGTCAGTAATAAAATGACCGACAGGGAAAGGGATAAAGTG
ATGCCTCTGATTATCCAAGGTTTTAAAGACGCAGCTGAGGAAGCAGGAACGTCTGTAACA
GGCGGCCAAACAGTACTAAACCCCTGGATTGTCCTGGGAGGAGTGGCTACCACTGTCTGC
CAACCCAATGAATTTATCATGCCAGACAATGCAGTGCCAGGGGACGTGCTGGTGCTGACA
AAACCCCTGGGGACACAGGTGGCAGTGGCTGTGCACCAGTGGCTGGATATCCCTGAGAAA
TGGAATAAGATTAAACTAGTGGTCACCCAAGAAGATGTAGAGCTGGCCTACCAGGAGGCG
ATGATGAACATGGCGAGGCTCAACAGGACAGCTGCAGGACTCATGCACACGTTCAATACC
CACGCCGCCACTGACATCACGGGCTTCGGGATTTTGGGCCATGCGCAGAACCTGGCCAAG
CAGCAGAGGAACGAGGTGTCGTTTGTAATTCACAACCTCCCGGTGCTGGCCAAGATGGCT
GCGGTGAGCAAGGCCTGCGGAAACATGTTCGGCCTCATGCACGGGACCTGCCCGGAGACT
TCAGGCGGCCTTCTGATCTGTTTACCACGTGAGCAAGCAGCTCGGTTCTGTGCAGAGATA
AAGTCCCCCAAATATGGTGAAGGCCACCAAGCATGGATTATTGGGATTGTAGAGAAGGGC
AACCGCACAGCCAGAATCATAGACAAACCCCGGATCATCGAGGTCGCACACAAGTGGCCA
CTCAAAACGTGA
|
| Enzyme 40 GenBank Gene ID |
U34044  |
| Enzyme 40 GeneCard ID |
SEPHS1  |
| Enzyme 40 GenAtlas ID |
SEPHS1  |
| Enzyme 40 HGNC ID |
HGNC:19685  |
| Enzyme 40 Chromosome Location |
10 |
| Enzyme 40 Locus |
10p14 |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 General References |
- Low SC, Harney JW, Berry MJ: Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis. J Biol Chem. 1995 Sep 15;270(37):21659-64. [PubMed
]
|
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
5930 |
| Enzyme 41 Name |
Selenide, water dikinase 2 |
| Enzyme 41 Synonyms |
- Selenophosphate synthetase 2
- Selenium donor protein 2
|
| Enzyme 41 Gene Name |
SEPHS2 |
| Enzyme 41 Protein Sequence |
>Selenide, water dikinase 2
MAEASATGACGEAMAAAEGSSGPAGLTLGRSFSNYRPFEPQALGLSPSWRLTGFSGMKGC
GCKVPQEALLKLLAGLTRPDVRPPLGRGLVGGQEEASQEAGLPAGAGPSPTFPALGIGMD
SCVIPLRHGGLSLVQTTDFFYPLVEDPYMMGRIACANVLSDLYAMGITECDNMLMLLSVS
QSMSEEEREKVTPLMVKGFRDAAEEGGTAVTGGQTVVNPWIIIGGVATVVCQPNEFIMPD
SAVVGDVLVLTKPLGTQVAVNAHQWLDNPERWNKVKMVVSREEVELAYQEAMFNMATLNR
TAAGLMHTFNAHAATDITGFGILGHSQNLAKQQRNEVSFVIHNLPIIAKMAAVSKASGRF
GLLQGTSAETSGGLLICLPREQAARFCSEIKSSKYGEGHQAWIVGIVEKGNRTARIIDKP
RVIEVLPRGATAAVLAPDSSNASSEPSS
|
| Enzyme 41 Number of Residues |
448 |
| Enzyme 41 Molecular Weight |
47259 |
| Enzyme 41 Theoretical pI |
5.69 |
| Enzyme 41 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleotide binding
- purine nucleotide binding
- selenide, water dikinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 41 General Function |
Amino acid transport and metabolism |
| Enzyme 41 Specific Function |
Synthesizes selenophosphate from selenide and ATP |
| Enzyme 41 Pathways |
|
| Enzyme 41 Reactions |
- ATP + selenide + H2O = AMP + selenophosphate + phosphate
|
| Enzyme 41 Pfam Domain Function |
|
| Enzyme 41 Signals |
|
| Enzyme 41 Transmembrane Regions |
|
| Enzyme 41 Essentiality |
Not Available |
| Enzyme 41 GenBank ID Protein |
14717790  |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
Q99611  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
SPS2_HUMAN  |
| Enzyme 41 PDB ID |
Not Available |
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
>1347 bp
ATGGCGGAAGCCTCGGCGACGGGCGCCTGCGGAGAGGCGATGGCAGCGGCGGAAGGCTCC
TCGGGCCCGGCGGGCTTGACTCTGGGCCGGAGCTTCTCGAACTACCGGCCCTTCGAGCCC
CAGGCGTTGGGCCTCAGCCCGAGCTGGCGGCTGACGGGCTTCTCCGGCATGAAGGGCTGA
GGCTGCAAGGTCCCGCAGGAGGCGCTGCTCAAACTCCTGGCGGGACTGACGCGGCCGGAC
GTGCGGCCCCCGCTGGGCCGGGGCCTGGTGGGTGGCCAGGAAGAGGCGTCCCAGGAAGCC
GGCCTGCCGGCAGGAGCGGGCCCCAGCCCCACCTTTCCAGCCCTGGGCATCGGGATGGAC
TCCTGCGTCATCCCCCTGAGGCACGGGGGCCTGTCACTGGTGCAGACCACGGACTTCTTT
TACCCCTTGGTAGAAGATCCCTACATGATGGGGCGCATAGCTTGTGCCAACGTGCTGAGT
GACCTCTACGCCATGGGGATTACTGAGTGTGACAACATGTTGATGTTACTCAGCGTCAGC
CAGAGTATGAGTGAGGAGGAACGCGAAAAGGTAACGCCACTCATGGTCAAAGGCTTTCGG
GATGCGGCTGAGGAAGGAGGGACGGCAGTGACCGGTGGGCAAACGGTGGTCAACCCTTGG
ATTATAATCGGTGGAGTTGCCACTGTAGTATGCCAACCAAATGAGTTCATAATGCCGGAC
AGCGCCGTCGTTGGGGACGTGCTGGTGTTAACCAAACCGTTAGGAACCCAGGTTGCTGTC
AATGCCCACCAATGGCTGGATAATCCTGAAAGATGGAATAAAGTAAAGATGGTGGTCTCC
AGAGAAGAGGTGGAGCTGGCCTATCAGGAAGCCATGTTCAATATGGCTACCCTCAACAGA
ACTGCTGCAGGTTTAATGCACACATTTAATGCCCATGCGGCCACAGATATCACAGGCTTT
GGCATTCTAGGACACTCCCAGAACCTTGCAAAACAACAAAGAAATGAAGTGTCCTTTGTT
ATTCATAATCTGCCAATAATTGCCAAGATGGCTGCCGTCAGCAAGGCCAGTGGACGGTTT
GGGCTTCTTCAAGGAACCTCAGCTGAAACCTCTGGGGGATTACTGATTTGTCTGCCAAGA
GAACAGGCGGCTCGCTTTTGTTCTGAAATCAAATCCTCCAAGTACGGAGAGGGTCACCAA
GCGTGGATCGTTGGCATTGTGGAAAAGGGAAACCGAACGGCCCGGATCATTGACAAGCCG
CGAGTTATTGAAGTCCTGCCTCGTGGGGCCACAGCTGCTGTTCTTGCTCCTGACAGTTCA
AATGCCTCCTCTGAGCCTAGCTCGTGA
|
| Enzyme 41 GenBank Gene ID |
U43286  |
| Enzyme 41 GeneCard ID |
SEPHS2  |
| Enzyme 41 GenAtlas ID |
SEPHS2  |
| Enzyme 41 HGNC ID |
HGNC:19686  |
| Enzyme 41 Chromosome Location |
16 |
| Enzyme 41 Locus |
16p11.2 |
| Enzyme 41 SNPs |
SNPJam Report  |
| Enzyme 41 General References |
- Guimaraes MJ, Bazan JF, Zlotnik A, Wiles MV, Grimaldi JC, Lee F, McClanahan T: A new approach to the study of haematopoietic development in the yolk sac and embryoid bodies. Development. 1995 Oct;121(10):3335-46. [PubMed
]
- Guimaraes MJ, Peterson D, Vicari A, Cocks BG, Copeland NG, Gilbert DJ, Jenkins NA, Ferrick DA, Kastelein RA, Bazan JF, Zlotnik A: Identification of a novel selD homolog from eukaryotes, bacteria, and archaea: is there an autoregulatory mechanism in selenocysteine metabolism? Proc Natl Acad Sci U S A. 1996 Dec 24;93(26):15086-91. [PubMed
]
|
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
5949 |
| Enzyme 42 Name |
CTP synthase 1 |
| Enzyme 42 Synonyms |
- UTP--ammonia ligase 1
- CTP synthetase 1
|
| Enzyme 42 Gene Name |
CTPS |
| Enzyme 42 Protein Sequence |
>CTP synthase 1
MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFV
LDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDA
IQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHV
SLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ
VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCS
IALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQK
LCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDAN
STEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRH
RFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPY
FGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD
|
| Enzyme 42 Number of Residues |
591 |
| Enzyme 42 Molecular Weight |
66691 |
| Enzyme 42 Theoretical pI |
6.42 |
| Enzyme 42 GO Classification |
| Function |
- CTP synthase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
- pyrimidine nucleotide biosynthesis
- pyrimidine nucleotide metabolism
|
| Component |
| — |
|
| Enzyme 42 General Function |
Nucleotide transport and metabolism |
| Enzyme 42 Specific Function |
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen |
| Enzyme 42 Pathways |
|
| Enzyme 42 Reactions |
- ATP + UTP + NH3 = ADP + phosphate + CTP
|
| Enzyme 42 Pfam Domain Function |
|
| Enzyme 42 Signals |
|
| Enzyme 42 Transmembrane Regions |
|
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
30293  |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
P17812  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
PYRG1_HUMAN  |
| Enzyme 42 PDB ID |
Not Available |
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
>1776 bp
ATGAAGTACATTCTGGTTACTGGTGGTGTTATATCAGGAATTGGAAAAGGAATCATTGCC
AGCAGTGTGGGCACAATACTCAAGTCATGTGGTTTACATGTAACTTCAATCAAAATTGAC
CCCTACATTAACATTGATGCAGGAACATTCTCTCCTTATGAGCATGGTGAGGTTTTTGTG
CTGGATGATGGTGGGGAAGTAGACCTTGACCTGGGTAACTATGAGCGGTTCCTTGACATC
CGCCTCACCAAGGACAATAATCTGACCACTGGAAAGATATACCAGTATGTCATTAACAAG
GAACGGAAAGGAGATTACTTGGGGAAAACTGTCCAAGTTGTCCCTCATATCACAGATGCA
ATCCAGGAGTGGGTGATGAGACAGGCGTTAATACCTGTAGATGAAGATGGCCTGGAACCT
CAAGTGTGTGTTATTGAGCTTGGTGGAACCGTGGGGGACATAGAAAGCATGCCCTTTATT
GAGGCCTTCCGTCAGTTCCAATTCAAGGTCAAAAGAGAGAACTTTTGTAACATCCACGTC
AGTCTAGTTCCCCAGCCAAGTTCAACAGGGGAACAGAAGACTAAACCTACCCAGAATAGT
GTTCGGGAACTTAGAGGACTTGGGCTTTCCCCAGATCTGGTTGTATGCAGGTGCTCAAAT
CCACTTGACACATCAGTGAAGGAGAAAATATCAATGTTCTGCCATGTTGAGCCTGAACAA
GTGATCTGTGTCCACGATGTCTCATCCATCTACCGAGTCCCCTTGTTGTTAGAGGAGCAA
GGGGTTGTAGATTATTTTCTTCGAAGACTTGACCTTCCTATTGAGAGGCAGCCAAGAAAA
ATGCTGATGAAATGGAAAGAGATGGCTGACAGATATGATCGCTTGCTGGAGACCTGCTCT
ATTGCCCTTGTGGCGAAATACACCGAGTTCTCAGACTCCTATGCCTCTGTCATTAAGGCT
CTGGAGCATTCTGCACTGGCCATCAACCACAAATTGGAAATCAAGTACATAGATTCTGCG
GACTTGGAGCCCATCACCTCGCAAGAAGAGCCCGTGCGCTACCACGAAGCTTGGCAGAAG
CTCTGTAGTGCTCATGGAGTGCTGGTTCCAGGAGGATTTGGTGTTCGAGGAACAGAAGGA
AAAATCCAAGCAATTGCCTGGGCTCGGAATCAGAAAAAGCCTTTTTTGGGCGTGTGCTTA
GGGATGCAGTTGGCAGTGGTTGAATTCTCAAGAAACGTGCTGGGATGGCAAGATGCCAAT
TCTACAGAGTTTGACCCTACGACCAGTCATCCCGTGGTCGTAGACATGCCAGAACACAAC
CCAGGGCAGATGGGCGGAACCATGAGGCTGGGCAAGAGGAGAACCCTGTTCCAGACCAAG
AACTCAGTCATGAGGAAACTCTATGGAGACGCAGACTACTTGGAAGAGAGGCACCGCCAC
CGATTTGAGGTGAATCCAGTCTGGAAAAAGTGTTTGGAAGAACAAGGCTTGAAGTTTGTT
GGCCAAGATGTTGAAGGAGAGAGAATGGAAATTGTGGAGTTAGAAGATCATCCCTTTTTT
GTTGGGGTTCAGTACCACCCTGAGTTCCTGTCCAGGCCTATCAAGCCCTCCCCACCATAC
TTTGGCCTCCTCCTGGCCTCTGTGGGGCGGCTCTCACATTACCTCCAGAAAGGCTGCAGG
CTCTCACCCAGGGACACCTATAGTGACAGGAGTGGAAGCAGCTCCCCTGACTCTGAAATC
ACCGAACTGAAGTTTCCATCAATAAATCATGACTGA
|
| Enzyme 42 GenBank Gene ID |
X52142  |
| Enzyme 42 GeneCard ID |
CTPS  |
| Enzyme 42 GenAtlas ID |
CTPS  |
| Enzyme 42 HGNC ID |
HGNC:2519  |
| Enzyme 42 Chromosome Location |
1 |
| Enzyme 42 Locus |
1p34.1 |
| Enzyme 42 SNPs |
SNPJam Report  |
| Enzyme 42 General References |
- Yamauchi M, Yamauchi N, Meuth M: Molecular cloning of the human CTP synthetase gene by functional complementation with purified human metaphase chromosomes. EMBO J. 1990 Jul;9(7):2095-9. [PubMed
]
|
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
5962 |
| Enzyme 43 Name |
Glyceraldehyde-3-phosphate dehydrogenase, testis-specific |
| Enzyme 43 Synonyms |
- Spermatogenic glyceraldehyde-3-phosphate dehydrogenase
- Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2
- GAPDH-2
|
| Enzyme 43 Gene Name |
GAPDHS |
| Enzyme 43 Protein Sequence |
>Glyceraldehyde-3-phosphate dehydrogenase, testis-specific
MSKRDIVLTNVTVVQLLRQPCPVTRAPPPPEPKAEVEPQPQPEPTPVREEIKPPPPPLPP
HPATPPPKMVSVARELTVGINGFGRIGRLVLRACMEKGVKVVAVNDPFIDPEYMVYMFKY
DSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQIPWRAVGSPYVVESTGVYLSIQAAS
DHISAGAQRVVISAPSPDAPMFVMGVNENDYNPGSMNIVSNASCTTNCLAPLAKVIHERF
GIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKL
TGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLG
DTHSSIFDAKAGIALNDNFVKLISWYDNEYGYSHRVVDLLRYMFSRDK
|
| Enzyme 43 Number of Residues |
408 |
| Enzyme 43 Molecular Weight |
44502 |
| Enzyme 43 Theoretical pI |
8.34 |
| Enzyme 43 GO Classification |
| Function |
- NAD binding
- binding
- catalytic activity
- coenzyme binding
- cofactor binding
- glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity
- glyceraldehyde-3-phosphate dehydrogenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on the aldehyde or oxo group of donors
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
|
| Process |
- alcohol metabolism
- cellular metabolism
- glucose catabolism
- glucose metabolism
- glycolysis
- hexose metabolism
- metabolism
- monosaccharide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 43 General Function |
Carbohydrate transport and metabolism |
| Enzyme 43 Specific Function |
May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility |
| Enzyme 43 Pathways |
|
| Enzyme |