|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5901 |
| Enzyme 1 Name |
Seryl-tRNA synthetase, mitochondrial precursor |
| Enzyme 1 Synonyms |
- Seryl- tRNA(Ser/Secsynthetase
- Serine--tRNA ligase
- SerRSmt
|
| Enzyme 1 Gene Name |
SARS2 |
| Enzyme 1 Protein Sequence |
>Seryl-tRNA synthetase, mitochondrial precursor
MAASMARRLWPLLTRRGFRPRGGCISNDSPRRSFTTEKRNRNLLYEYAREGYSALPQLDI
ERFCACPEEAAHALELRKGELRSADLPAIISTWQELRQLQEQIRSLEEEKAAVTEAVRAL
LANQDSGEVQQDPKYQGLRARGREIRKELVHLYPREAQLEEQFYLQALKLPNQTHPDVPV
GDESQARVLHMVGDKPVFSFQPRGHLEIGEKLDIIRQKRLSHVSGHRSYYLRGAGALLQH
GLVNFTFNKLLRRGFTPMTVPDLLRGAVFEGCGMTPNANPSQIYNIDPARFKDLNLAGTA
EVGLAGYFMDHTVAFRDLPVRMVCSSTCYRAETNTGQEPRGLYRVHHFTKVEMFGVTGPG
LEQSSQLLEEFLSLQMEILTELGLHFRVLDMPTQELGLPAYRKFDIEAWMPGRGRFGEVT
SASNCTDFQSRRLHIMFQTEAGELQFAHTVNATACAVPRLLIALLESNQQKDGSVLVPPA
LQSYLGTDRITAPTHVPLQYIGPNQPRKPGLPGQPAVS
|
| Enzyme 1 Number of Residues |
518 |
| Enzyme 1 Molecular Weight |
58283 |
| Enzyme 1 Theoretical pI |
8.22 |
| Enzyme 1 GO Classification |
| Function |
- ATP binding
- RNA ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming phosphoric ester bonds
- nucleotide binding
- purine nucleotide binding
- serine-tRNA ligase activity
- tRNA ligase activity
|
| Process |
- RNA metabolism
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- seryl-tRNA aminoacylation
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolism
|
| Component |
| — |
|
| Enzyme 1 General Function |
Translation, ribosomal structure and biogenesis |
| Enzyme 1 Specific Function |
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) |
| Enzyme 1 Pathways |
- Aminoacyl-tRNA biosynthesis (map00970
)
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 1 Reactions |
- ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser)
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
Not Available |
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
9188535  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q9NP81  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
SYSM_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1557 bp
ATGGCTGCGTCCATGGCGCGGCGCTTGTGGCCTTTGCTGACTCGTCGGGGGTTCCGGCCC
CGGGGAGGCTGCATCTCCAACGATAGTCCAAGGAGAAGTTTCACTACAGAGAAACGAAAC
CGGAACCTCCTGTACGAGTATGCGCGCGAGGGCTACAGCGCACTCCCTCAGCTGGACATA
GAGCGGTTCTGCGCATGCCCAGAAGAGGCCGCACACGCCCTGGAGCTCCGCAAGGGGGAG
CTGCGCTCGGCGGACCTGCCCGCGATCATCTCGACATGGCAGGAGCTGAGGCAGCTGCAG
GAGCAGATCCGGAGCCTGGAGGAAGAGAAGGCAGCTGTGACTGAGGCAGTGCGGGCCCTG
CTGGCAAACCAGGACAGTGGTGAAGTGCAGCAGGACCCCAAGTACCAGGGTCTGCGGGCA
CGTGGCCGGGAGATCCGGAAGGAGCTTGTTCACCTGTACCCCAGGGAGGCCCAGCTTGAG
GAGCAGTTCTACCTGCAGGCGCTGAAGCTGCCCAACCAGACCCACCCAGACGTGCCCGTC
GGGGATGAGAGCCAGGCTCGAGTGCTCCACATGGTCGGAGACAAGCCAGTTTTCTCCTTC
CAACCTCGGGGCCACCTGGAAATTGGCGAGAAACTCGACATCATCCGTCAGAAGCGCCTG
TCCCACGTGTCTGGCCACCGGTCCTATTACCTGCGCGGGGCTGGAGCCCTCCTGCAGCAC
GGCCTGGTCAACTTCACATTCAACAAGCTTCTCCGCCGGGGCTTCACCCCCATGACGGTG
CCAGACCTTCTCCGCGGAGCAGTGTTTGAAGGCTGTGGGATGACACCAAATGCCAACCCA
TCCCAAATTTACAACATCGACCCTGCCCGCTTCAAAGATCTCAACCTGGCTGGAACAGCG
GAGGTGGGGCTTGCAGGCTACTTCATGGACCACACCGTGGCCTTCAGGGACCTGCCAGTC
AGGATGGTTTGCTCCAGCACCTGCTACCGGGCAGAGACAAACACGGGACAGGAACCCCGG
GGGCTGTATCGAGTACACCACTTCACCAAGGTGGAGATGTTTGGGGTGACAGGCCCTGGG
CTGGAGCAGAGCTCACAGCTGCTGGAGGAGTTCCTGTCCCTTCAGATGGAGATCTTGACA
GAGCTGGGCTTGCACTTCCGGGTCCTGGATATGCCCACCCAAGAACTGGGCCTCCCCGCC
TACCGCAAGTTTGACATTGAGGCCTGGATGCCAGGCCGAGGCCGCTTTGGAGAGGTCACC
AGTGCTTCCAACTGCACAGACTTCCAGAGCCGCCGCCTCCACATCATGTTCCAGACCGAG
GCTGGGGAGCTGCAGTTTGCCCACACGGTGAACGCCACCGCCTGTGCTGTCCCCCGCCTT
CTCATCGCGCTCCTGGAGAGTAACCAGCAGAAGGACGGCTCAGTGCTCGTGCCCCCTGCC
CTCCAGTCCTACCTCGGCACTGATCGGATCACAGCCCCTACCCACGTGCCTCTCCAGTAC
ATCGGCCCCAACCAGCCCCGGAAGCCTGGGCTGCCTGGCCAGCCTGCTGTAAGCTAA
|
| Enzyme 1 GenBank Gene ID |
AB029948  |
| Enzyme 1 GeneCard ID |
SARS2  |
| Enzyme 1 GenAtlas ID |
SARS2  |
| Enzyme 1 HGNC ID |
HGNC:17697  |
| Enzyme 1 Chromosome Location |
Not Available |
| Enzyme 1 Locus |
Not Available |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Yokogawa T, Shimada N, Takeuchi N, Benkowski L, Suzuki T, Omori A, Ueda T, Nishikawa K, Spremulli LL, Watanabe K: Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase. J Biol Chem. 2000 Jun 30;275(26):19913-20. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5918 |
| Enzyme 2 Name |
Seryl-tRNA synthetase, cytoplasmic |
| Enzyme 2 Synonyms |
- Seryl-tRNA(Ser/Secsynthetase
- Serine--tRNA ligase
- SerRS
|
| Enzyme 2 Gene Name |
SARS |
| Enzyme 2 Protein Sequence |
>Seryl-tRNA synthetase, cytoplasmic
MVLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLC
SKTIGEKMKKKEPVGDDESVPENVLSFDDLTADALANLKVSQIKKVRLLIDEAILKCDAE
RIKLEAERFENLREIGNLLHPSVPISNDEDVDNKVERIWGDCTVRKKYSHVDLVVMVDGF
EGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQL
SQFDEELYKVIGKGSEKSDDNSYDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTC
FRQEVGSHGRDTRGIFRVHQFEKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYH
IVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYGQTKKMMDKV
EFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEFMPPGLQELIPFVKPAPIEQEP
SKKQKKQHEGSKKKAAARDVTLENRLQNMEVTDA
|
| Enzyme 2 Number of Residues |
514 |
| Enzyme 2 Molecular Weight |
58778 |
| Enzyme 2 Theoretical pI |
6.38 |
| Enzyme 2 GO Classification |
| Function |
- ATP binding
- RNA ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming phosphoric ester bonds
- nucleotide binding
- purine nucleotide binding
- serine-tRNA ligase activity
- tRNA ligase activity
|
| Process |
- RNA metabolism
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- seryl-tRNA aminoacylation
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolism
|
| Component |
| — |
|
| Enzyme 2 General Function |
Translation, ribosomal structure and biogenesis |
| Enzyme 2 Specific Function |
Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) |
| Enzyme 2 Pathways |
- Aminoacyl-tRNA biosynthesis (map00970
)
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 2 Reactions |
- ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser)
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
1050527  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P49591  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
SYSC_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1545 bp
ATGGTGCTGGATCTGGATTTGTTTCGGGTGGATAAAGGAGGGGACCCAGCCCTCATCCGA
GAGACGCAGGAGAAGCGCTTCAAGGACCCGGGACTAGTGGACCAGCTGGTGAAGGCAGAC
AGCGAGTGGCGACGATGTAGATTTCGGGCAGACAACTTGAGCAAGCTGAAGAACCTATGC
AGCAAGACAATCGGAGAGAAAATGAAGAAAAAAGAGCCAGTGGGAGATGATGAGTCTGTC
CCAGAGAATGTGCTGAGTTTCGATGACCTTACTGCAGACGCTTTAGCTAACCTGAAAGTC
TCACAAATCAAAAAAGTCCGACTCCTCATTGATGAAGCCATCCTGAAGTGTGACGCGGAG
CGGATAAAGTTGGAAGCAGAGCGGTTTGAGAACCTCCGAGAGATTGGGAACCTTCTGCAC
CCTTCTGTACCCATCAGTAACGATGAGGATGTGGACAACAAAGTAGAGAGGATTTGGGGC
GATTGTACAGTCAGGAAGAAGTACTCTCATGTGGACCTGGTGGTGATGGTAGATGGCTTT
GAAGGCGAAAAGGGGGCCGTGGTGGCTGGGAGTCGAGGGTACTTCTTGAAGGGGGTCCTG
GTGTTCCTGGAACAGGCTCTCATCCAGTATGCCCTTCGCACCTTGGGAAGTCGGGGCTAC
ATTCCCATTTATACCCCCTTTTTCATGAGGAAGGAGGTCATGCAGGAGGTGGCACAGCTC
AGCCAGTTTGATGAAGAACTTTATAAGGTGATTGGCAAAGGCAGTGAAAAGTCTGATGAC
AACTCCTATGATGAGAAGTACCTGATTGCCACCTCAGAGCAGCCCATTGCTGCCCTGCAC
CGGGATGAGTGGCTCCGGCCGGAGGACCTGCCCATCAAGTATGCTGGCCTGTCTACCTGC
TTCCGTCAGGAGGTGGGCTCCCATGGCCGTGACACCCGTGGCATCTTCCGAGTCCATCAG
TTTGAGAAGATTGAACAGTTTGTGTACTCATCACCCCATGACAACAAGTCATGGGAGATG
TTTGAAGAGATGATTACCACCGCAGAGGAGTTCTACCAGTCCCTGGGGATTCCTTACCAC
ATTGTGAATATTGTCTCAGGTTCTTTGAATCATGCTGCCAGTAAGAAGCTTGACCTGGAG
GCCTGGTTTCCGGGCTCAGGAGCCTTCCGTGAGTTGGTCTCCTGTTCTAATTGCACGGAT
TACCAGGCTCGCCGGCTTCGAATCCGATATGGGCAAACCAAGAAGATGATGGACAAGGTG
GAGTTTGTCCATATGCTCAATGCTACCATGTGCGCCACTACCCGTACCATCTGCGCCATC
CTGGAGAACTACCAGACAGAGAAGGGCATCACTGTGCCTGAGAAATTGAAGGAGTTCATG
CCGCCAGGACTGCAAGAACTGATCCCCTTTGTGAAGCCTGCGCCCATTGAGCAGGAGCCA
TCAAAGAAGCAGAAGAAGCAACATGAGGGCAGCAAAAAGAAAGCAGCAGCAAGAGACGTC
ACCCTAGAAAACAGGCTGCAGAACATGGAGGTCACCGATGCTTGA
|
| Enzyme 2 GenBank Gene ID |
X91257  |
| Enzyme 2 GeneCard ID |
SARS  |
| Enzyme 2 GenAtlas ID |
SARS  |
| Enzyme 2 HGNC ID |
HGNC:10537  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1p13.3-p13.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Vincent C, Tarbouriech N, Hartlein M: Genomic organization, cDNA sequence, bacterial expression, and purification of human seryl-tRNA synthase. Eur J Biochem. 1997 Nov 15;250(1):77-84. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5944 |
| Enzyme 3 Name |
L-serine dehydratase |
| Enzyme 3 Synonyms |
- L-serine deaminase
|
| Enzyme 3 Gene Name |
SDS |
| Enzyme 3 Protein Sequence |
>L-serine dehydratase
MMSGEPLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHF
VCSSAGNAGMAAAYAARQLGVPATIVVPGTTPALTIERLKNEGATCKVVGELLDEAFELA
KALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIALSVGGGGLLCGVVQGL
QECGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGSQALKLFQEHP
IFSEVISDQEAVAAIEKFVDDEKILVEPAWGAALAAVYSHVIQKLQLEGNLRTPLPSLVV
IVCGGSNISLAQLRALKEQLGMTNRLPK
|
| Enzyme 3 Number of Residues |
328 |
| Enzyme 3 Molecular Weight |
34703 |
| Enzyme 3 Theoretical pI |
8.07 |
| Enzyme 3 GO Classification |
| Function |
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Amino acid transport and metabolism |
| Enzyme 3 Specific Function |
L-serine = pyruvate + NH(3) |
| Enzyme 3 Pathways |
- Cysteine Metabolism (map00272
)
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 3 Reactions |
- L-serine = pyruvate + NH3
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
338030  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P20132  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
SDHL_HUMAN  |
| Enzyme 3 PDB ID |
1P5J  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>987 bp
ATGATGTCTGGAGAACCCCTGCACGTGAAGACCCCCATCCGTGACAGCATGGCCCTGTCC
AAAATGGCCGGCACCAGCGTCTACCTCAAGATGGACAGTGCCCAGCCCTCCGGCTCCTTC
AAGATCCGGGGCATTGGGCACTTCTGCAAGAGGTGGGCCAAGCAAGGCTGTGCACATTTT
GTCTGCTCCTCGGCGGGCAACGCAGGCATGGCGGCTGCATATGCGGCCAGGCAACTCGGC
GTCCCCGCCACCATCGTAGTGCCCGGCACCACACCTGCTCTCACCATTGAGCGCCTCAAG
AATGAAGGTGCCACATGCAAGGTGGTGGGTGAGTTATTGGATGAAGCCTTCGAGCTGGCC
AAGGCCCTAGCGAAGAACAACCCGGGTTGGGTCTACATTCCCCCCTTTGATGACCCCCTC
ATCTGGGAAGGCCACGCTTCCATCGTGAAAGAGCTGAAGGAGACACTGTGGGAAAAGCCG
GGGGCCATCGCGCTGTCAGTGGGCGGCGGGGGCCTGCTGTGTGGAGTGGTCCAGGGGCTG
CAGGAGTGTGGCTGGGGGGACGTGCCTGTCATCGCCATGGAGACTTTTGGTGCCCACAGC
TTCCACGCTGCCACCACCGCAGGCAAACTTGTCTCCCTGCCCAAGATCACCAGTGTTGCC
AAGGCCCTGGGCGTGAAGACTGTGGGGTCTCAGGCCCTGAAGCTGTTTCAGGAACACCCC
ATTTTCTCTGAAGTTATCTCGGACCAGGAGGCTGTGGCCGCCATTGAGAAGTTCGTGGAT
GATGAGAAGATCCTGGTGGAGCCCGCCTGGGGCGCAGCCCTGGCCGCTGTCTATAGCCAC
GTGATCCAGAAGCTCCAACTGGAGGGGAATCTCCGAACCCCGCTGCCATCCCTCGTGGTC
ATCGTCTGCGGGGGCAGCAACATCAGCCTGGCCCAGCTGCGGGCGCTCAAGGAACAGCTG
GGCATGACAAATAGGTTGCCCAAGTGA
|
| Enzyme 3 GenBank Gene ID |
J05037  |
| Enzyme 3 GeneCard ID |
SDS  |
| Enzyme 3 GenAtlas ID |
SDS  |
| Enzyme 3 HGNC ID |
HGNC:10691  |
| Enzyme 3 Chromosome Location |
12 |
| Enzyme 3 Locus |
12q24.13 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Ogawa H, Gomi T, Konishi K, Date T, Nakashima H, Nose K, Matsuda Y, Peraino C, Pitot HC, Fujioka M: Human liver serine dehydratase. cDNA cloning and sequence homology with hydroxyamino acid dehydratases from other sources. J Biol Chem. 1989 Sep 25;264(27):15818-23. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6059 |
| Enzyme 4 Name |
Cystathionine beta-synthase |
| Enzyme 4 Synonyms |
- Serine sulfhydrase
- Beta- thionase
|
| Enzyme 4 Gene Name |
CBS |
| Enzyme 4 Protein Sequence |
>Cystathionine beta-synthase
MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPA
SESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKD
RISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDV
LRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEI
LQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTT
YEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKA
AQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLS
APLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVG
KVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLL
NFVAAQERDQK
|
| Enzyme 4 Number of Residues |
551 |
| Enzyme 4 Molecular Weight |
60587 |
| Enzyme 4 Theoretical pI |
6.63 |
| Enzyme 4 GO Classification |
| Function |
- carbon-oxygen lyase activity
- catalytic activity
- cystathionine beta-synthase activity
- hydro-lyase activity
- lyase activity
|
| Process |
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- cysteine biosynthesis
- cysteine biosynthesis from serine
- cysteine biosynthesis via cystathione
- metabolism
- physiological process
- serine family amino acid metabolism
- sulfur amino acid biosynthesis
- sulfur amino acid metabolism
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 4 General Function |
Amino acid transport and metabolism |
| Enzyme 4 Specific Function |
L-serine + L-homocysteine = L-cystathionine + H(2)O |
| Enzyme 4 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
- Methionine Metabolism (map00271
)
- Selenoamino Acid Metabolism (map00450
)
|
| Enzyme 4 Reactions |
- L-serine + L-homocysteine = cystathionine + H2O
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
388716  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P35520  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
CBS_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1656 bp
ATGCCTTCTGAGACCCCCCAGGCAGAAGTGGGGCCCACAGGCTGCCCCCACCGCTCAGGG
CCACACTCGGCGAAGGGGAGCCTGGAGAAGGGGTCCCCAGAGGATAAGGAAGCCAAGGAG
CCCCTGTGGATCCGGCCCGATGCTCCGAGCAGGTGCACCTGGCAGCTGGGCCGGCCTGCC
TCCGAGTCCCCACATCACCACACTGCCCCGGCAAAATCTCCAAAAATCTTGCCAGATATT
CTGAAGAAAATCGGGGACACCCCTATGGTCAGAATCAACAAGATTGGGAAGAAGTTCGGC
CTGAAGTGTGAGCTCTTGGCCAAGTGTGAGTTCTTCAACGCGGGCGGGAGCGTGAAGGAC
CGCATCAGCCTGCGGATGATTGAGGATGCTGAGCGCGACGGGACGCTGAAGCCCGGGGAC
ACGATTATCGAGCCGACATCCGGGAACACCGGGATCGGGCTGGCCCTGGCTGCGGCAGTG
AGGGGCTATCGCTGCATCATCGTGATGCCAGAGAAGATGAGCTCCGAGAAGGTGGACGTG
CTGCGGGCACTGGGGGCTGAGATTGTGAGGACGCCCACCAATGCCAGGTTCGACTCCCCG
GAGTCACACGTGGGGGTGGCCTGGCGGCTGAAGAACGAAATCCCCAATTCTCACATCCTA
GACCAGTACCGCAACGCCAGCAACCCCCTGGCTCACTACGACACCACCGCTGATGAGATC
CTGCAGCAGTGTGATGGGAAGCTGGACATGCTGGTGGCTTCAGTGGGCACGGGCGGCACC
ATCACGGGCATTGCCAGGAAGCTGAAGGAGAAGTGTCCTGGATGCAGGATCATTGGGGTG
GATCCCGAAGGGTCCATCCTCGCAGAGCCGGAGGAGCTGAACCAGACGGAGCAGACAACC
TACGAGGTGGAAGGGATCGGCTACGACTTCATCCCCACGGTGCTGGACAGGACGGTGGTG
GACAAGTGGTTCAAGAGCAACGATGAGGAGGCGTTCACCTTTGCCCGCATGCTGATCGCG
CAAGAGGGGCTGCTGTGCGGTGGCAGTGCTGGCAGCACGGTGGCGGTGGCCGTGAAGGCT
GCGCAGGAGCTGCAGGAGGGCCAGCGCTGCGTGGTCATTCTGCCCGACTCAGTGCGGAAC
TACATGACCAAGTTCCTGAGCGACAGGTGGATGCTGCAGAAGGGCTTTCTGAAGGAGGAG
GACCTCACGGAGAAGAAGCCCTGGTGGTGGCACCTCCGTGTTCAGGAGCTGGGCCTGTCA
GCCCCGCTGACCGTGCTCCCGACCATCACCTGTGGGCACACCATCGAGATCCTCCGGGAG
AAGGGCTTCGACCAGGCGCCCGTGGTGGATGAGGCGGGGGTAATCCTGGGAATGGTGACG
CTTGGGAACATGCTCTCGTCCCTGCTTGCCGGGAAGGTGCAGCCGTCAGACCAAGTTGGC
AAAGTCATCTACAAGCAGTTCAAACAGATCCGCCTCACGGACACGCTGGGCAGGCTCTCG
CACATCCTGGAGATGGACCACTTCGCCCTGGTGGTGCACGAGCAGATCCAGTACCACAGC
ACCGGGAAGTCCAGTCAGCGGCAGATGGTGTTCGGGGTGGTCACCGCCATTGACTTGCTG
AACTTCGTGGCCGCCCAGGAGCGGGACCAGAAGTGA
|
| Enzyme 4 GenBank Gene ID |
L19501  |
| Enzyme 4 GeneCard ID |
CBS  |
| Enzyme 4 GenAtlas ID |
CBS  |
| Enzyme 4 HGNC ID |
HGNC:1550  |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Kraus JP, Le K, Swaroop M, Ohura T, Tahara T, Rosenberg LE, Roper MD, Kozich V: Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells. Hum Mol Genet. 1993 Oct;2(10):1633-8. [PubMed
]
- Chasse JF, Paly E, Paris D, Paul V, Sinet PM, Kamoun P, London J: Genomic organization of the human cystathionine beta-synthase gene: evidence for various cDNAs. Biochem Biophys Res Commun. 1995 Jun 26;211(3):826-32. [PubMed
]
- Kruger WD, Cox DR: A yeast system for expression of human cystathionine beta-synthase: structural and functional conservation of the human and yeast genes. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6614-8. [PubMed
]
- Chasse JF, Paul V, Escanez R, Kamoun P, London J: Human cystathionine beta-synthase: gene organization and expression of different 5' alternative splicing. Mamm Genome. 1997 Dec;8(12):917-21. [PubMed
]
- Kraus JP, Oliveriusova J, Sokolova J, Kraus E, Vlcek C, de Franchis R, Maclean KN, Bao L, Bukovsk, Patterson D, Paces V, Ansorge W, Kozich V: The human cystathionine beta-synthase (CBS) gene: complete sequence, alternative splicing, and polymorphisms. Genomics. 1998 Sep 15;52(3):312-24. [PubMed
]
- Kraus J, Packman S, Fowler B, Rosenberg LE: Purification and properties of cystathionine beta-synthase from human liver. Evidence for identical subunits. J Biol Chem. 1978 Sep 25;253(18):6523-8. [PubMed
]
- Meier M, Janosik M, Kery V, Kraus JP, Burkhard P: Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. EMBO J. 2001 Aug 1;20(15):3910-6. [PubMed
]
- Taoka S, Lepore BW, Kabil O, Ojha S, Ringe D, Banerjee R: Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme. Biochemistry. 2002 Aug 20;41(33):10454-61. [PubMed
]
- Kraus JP, Janosik M, Kozich V, Mandell R, Shih V, Sperandeo MP, Sebastio G, de Franchis R, Andria G, Kluijtmans LA, Blom H, Boers GH, Gordon RB, Kamoun P, Tsai MY, Kruger WD, Koch HG, Ohura T, Gaustadnes M: Cystathionine beta-synthase mutations in homocystinuria. Hum Mutat. 1999;13(5):362-75. [PubMed
]
- Kozich V, Kraus JP: Screening for mutations by expressing patient cDNA segments in E. coli: homocystinuria due to cystathionine beta-synthase deficiency. Hum Mutat. 1992;1(2):113-23. [PubMed
]
- Kozich V, de Franchis R, Kraus JP: Molecular defect in a patient with pyridoxine-responsive homocystinuria. Hum Mol Genet. 1993 Jun;2(6):815-6. [PubMed
]
- Hu FL, Gu Z, Kozich V, Kraus JP, Ramesh V, Shih VE: Molecular basis of cystathionine beta-synthase deficiency in pyridoxine responsive and nonresponsive homocystinuria. Hum Mol Genet. 1993 Nov;2(11):1857-60. [PubMed
]
- de Franchis R, Kozich V, McInnes RR, Kraus JP: Identical genotypes in siblings with different homocystinuric phenotypes: identification of three mutations in cystathionine beta-synthase using an improved bacterial expression system. Hum Mol Genet. 1994 Jul;3(7):1103-8. [PubMed
]
- Marble M, Geraghty MT, de Franchis R, Kraus JP, Valle D: Characterization of a cystathionine beta-synthase allele with three mutations in cis in a patient with B6 nonresponsive homocystinuria. Hum Mol Genet. 1994 Oct;3(10):1883-6. [PubMed
]
- Kraus JP: Komrower Lecture. Molecular basis of phenotype expression in homocystinuria. J Inherit Metab Dis. 1994;17(4):383-90. [PubMed
]
- Shih VE, Fringer JM, Mandell R, Kraus JP, Berry GT, Heidenreich RA, Korson MS, Levy HL, Ramesh V: A missense mutation (I278T) in the cystathionine beta-synthase gene prevalent in pyridoxine-responsive homocystinuria and associated with mild clinical phenotype. Am J Hum Genet. 1995 Jul;57(1):34-9. [PubMed
]
- Sebastio G, Sperandeo MP, Panico M, de Franchis R, Kraus JP, Andria G: The molecular basis of homocystinuria due to cystathionine beta-synthase deficiency in Italian families, and report of four novel mutations. Am J Hum Genet. 1995 Jun;56(6):1324-33. [PubMed
]
- Kluijtmans LA, Blom HJ, Boers GH, van Oost BA, Trijbels FJ, van den Heuvel LP: Two novel missense mutations in the cystathionine beta-synthase gene in homocystinuric patients. Hum Genet. 1995 Aug;96(2):249-50. [PubMed
]
- Kruger WD, Cox DR: A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene. Hum Mol Genet. 1995 Jul;4(7):1155-61. [PubMed
]
- Sperandeo MP, Panico M, Pepe A, Candito M, de Franchis R, Kraus JP, Andria G, Sebastio G: Molecular analysis of patients affected by homocystinuria due to cystathionine beta-synthase deficiency: report of a new mutation in exon 8 and a deletion in intron 11. J Inherit Metab Dis. 1995;18(2):211-4. [PubMed
]
- Kluijtmans LA, Boers GH, Stevens EM, Renier WO, Kraus JP, Trijbels FJ, van den Heuvel LP, Blom HJ: Defective cystathionine beta-synthase regulation by S-adenosylmethionine in a partially pyridoxine responsive homocystinuria patient. J Clin Invest. 1996 Jul 15;98(2):285-9. [PubMed
]
- Sperandeo MP, Candito M, Sebastio G, Rolland MO, Turc-Carel C, Giudicelli H, Dellamonica P, Andria G: Homocysteine response to methionine challenge in four obligate heterozygotes for homocystinuria and relationship with cystathionine beta-synthase mutations. J Inherit Metab Dis. 1996;19(3):351-6. [PubMed
]
- Dawson PA, Cox AJ, Emmerson BT, Dudman NP, Kraus JP, Gordon RB: Characterisation of five missense mutations in the cystathionine beta-synthase gene from three patients with B6-nonresponsive homocystinuria. Eur J Hum Genet. 1997 Jan-Feb;5(1):15-21. [PubMed
]
- Kim CE, Gallagher PM, Guttormsen AB, Refsum H, Ueland PM, Ose L, Folling I, Whitehead AS, Tsai MY, Kruger WD: Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria. Hum Mol Genet. 1997 Dec;6(13):2213-21. [PubMed
]
- Aral B, Coude M, London J, Aupetit J, Chasse JF, Zabot MT, Chadefaux-Vekemans B, Kamoun P: Two novel mutations (K384E and L539S) in the C-terminal moiety of the cystathionine beta-synthase protein in two French pyridoxine-responsive homocystinuria patients. Hum Mutat. 1997;9(1):81-2. [PubMed
]
- Kozich V, Janosik M, Sokolova J, Oliveriusova J, Orendac M, Kraus JP, Elleder D: Analysis of CBS alleles in Czech and Slovak patients with homocystinuria: report on three novel mutations E176K, W409X and 1223 + 37 del99. J Inherit Metab Dis. 1997 Jul;20(3):363-6. [PubMed
]
- de Franchis R, Kraus E, Kozich V, Sebastio G, Kraus JP: Four novel mutations in the cystathionine beta-synthase gene: effect of a second linked mutation on the severity of the homocystinuric phenotype. Hum Mutat. 1999;13(6):453-7. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6069 |
| Enzyme 5 Name |
Serine--pyruvate aminotransferase |
| Enzyme 5 Synonyms |
- SPT
- Alanine-- glyoxylate aminotransferase
- AGT
|
| Enzyme 5 Gene Name |
AGXT |
| Enzyme 5 Protein Sequence |
>Serine--pyruvate aminotransferase
MASHKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEI
KEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVDIGERIG
ARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLL
LVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSF
YLDIKWLANFWGCDDQPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHG
RLQALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPSTGKVLR
IGLLGCNATRENVDRVTEALRAALQHCPKKKL
|
| Enzyme 5 Number of Residues |
392 |
| Enzyme 5 Molecular Weight |
43011 |
| Enzyme 5 Theoretical pI |
8.55 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Amino acid transport and metabolism |
| Enzyme 5 Specific Function |
L-serine + pyruvate = 3-hydroxypyruvate + L- alanine |
| Enzyme 5 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 5 Reactions |
- L-serine + pyruvate = 3-hydroxypyruvate + L-alanine
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
36582  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P21549  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
SPYA_HUMAN  |
| Enzyme 5 PDB ID |
1H0C  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1179 bp
ATGGCCTCTCACAAGCTGCTGGTGACCCCCCCCAAGGCCCTGCTCAAGCCCCTCTCCATC
CCCAACCAGCTCCTGCTGGGGCCTGGTCCTTCCAACCTGCCTCCTCGCATCATGGCAGCC
GGGGGGCTGCAGATGATCGGGTCCATGAGCAAGGATATGTACCAGATCATGGACGAGATC
AAGGAAGGCATCCAGTACGTGTTCCAGACCAGGAACCCACTCACACTGGTCATCTCTGGC
TCGGGACACTGTGCCCTGGAGGCCGCCCTGGTCAATGTGCTGGAGCCTGGGGACTCCTTC
CTGGTTGGGGCCAATGGCATTTGGGGGCAGCGAGCCGTGGACATCGGGGAGCGCATAGGA
GCCCGAGTGCACCCGATGACCAAGGACCCTGGAGGCCACTACACACTGCAGGAGGTGGAG
GAGGGCCTGGCCCAGCACAAGCCAGTGCTGCTGTTCTTAACCCACGGGGAGTCGTCCACC
GGCGTGCTGCAGCCCCTTGATGGCTTCGGGGAACTCTGCCACAGGTACAAGTGCCTGCTC
CTGGTGGATTCGGTGGCATCCCTGGGCGGGACCCCCCTTTACATGGACCGGCAAGGCATC
GACATCCTGTACTCGGGCTCCCAGAAGGCCCTGAACGCCCCTCCAGGGACCTCGCTCATC
TCCTTCAGTGACAAGGCCAAAAAGAAGATGTACTCCCGCAAGACGAAGCCCTTCTCCTTC
TACCTGGACATCAAGTGGCTGGCCAACTTCTGGGGCTGTGACGACCAGCCCAGGATGTAC
CATCACACAATCCCCGTCATCAGCCTGTACAGCCTGAGAGAGAGCCTGGCCCTCATTGCG
GAACAGGGCCTGGAGAACAGCTGGCGCCAGCACCGCGAGGCCGCGGCGTATCTGCATGGG
CGCCTGCAGGCACTGGGGCTGCAGCTCTTCGTGAAGGACCCGGCGCTCCGGCTTCCCACA
GTCACCACTGTGGCTGTACCCGCTGGCTATGACTGGAGAGACATCGTCAGCTACGTCATA
GACCACTTCGACATTGAGATCATGGGTGGCCTTGGGCCCTCCACGGGGAAGGTGCTGCGG
ATCGGCCTGCTGGGCTGCAATGCCACCCGCGAGAATGTGGACCGCGTGACGGAGGCCCTG
AGGGCGGCCCTGCAGCACTGCCCCAAGAAGAAGCTGTGA
|
| Enzyme 5 GenBank Gene ID |
X56092  |
| Enzyme 5 GeneCard ID |
AGXT  |
| Enzyme 5 GenAtlas ID |
AGXT  |
| Enzyme 5 HGNC ID |
HGNC:341  |
| Enzyme 5 Chromosome Location |
2 |
| Enzyme 5 Locus |
2q36-q37 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Nishiyama K, Berstein G, Oda T, Ichiyama A: Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase. Eur J Biochem. 1990 Nov 26;194(1):9-18. [PubMed
]
- Purdue PE, Takada Y, Danpure CJ: Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1. J Cell Biol. 1990 Dec;111(6 Pt 1):2341-51. [PubMed
]
- Takada Y, Kaneko N, Esumi H, Purdue PE, Danpure CJ: Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon. Biochem J. 1990 Jun 1;268(2):517-20. [PubMed
]
- Purdue PE, Lumb MJ, Fox M, Griffo G, Hamon-Benais C, Povey S, Danpure CJ: Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase. Genomics. 1991 May;10(1):34-42. [PubMed
]
- Nishiyama K, Funai T, Katafuchi R, Hattori F, Onoyama K, Ichiyama A: Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene. Biochem Biophys Res Commun. 1991 May 15;176(3):1093-9. [PubMed
]
- Purdue PE, Lumb MJ, Allsop J, Minatogawa Y, Danpure CJ: A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1. Genomics. 1992 May;13(1):215-8. [PubMed
]
- Minatogawa Y, Tone S, Allsop J, Purdue PE, Takada Y, Danpur CJ, Kido R: A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1. Hum Mol Genet. 1992 Nov;1(8):643-4. [PubMed
]
- Danpure CJ, Purdue PE, Fryer P, Griffiths S, Allsop J, Lumb MJ, Guttridge KM, Jennings PR, Scheinman JI, Mauer SM, et al.: Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation. Am J Hum Genet. 1993 Aug;53(2):417-32. [PubMed
]
- Danpure CJ: Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase. Biochimie. 1993;75(3-4):309-15. [PubMed
]
- von Schnakenburg C, Rumsby G: Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene. J Med Genet. 1997 Jun;34(6):489-92. [PubMed
]
- Amoroso A, Pirulli D, Puzzer D, Ferri L, Crovella S, Ferrettini C, Marangella M, Mazzola G, Florian F: Gene symbol: AGXT. Disease: primary hyperoxaluria type I. Hum Genet. 1999 May;104(5):441. [PubMed
]
- Basmaison O, Rolland MO, Cochat P, Bozon D: Identification of 5 novel mutations in the AGXT gene. Hum Mutat. 2000 Jun;15(6):577. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6072 |
| Enzyme 6 Name |
Serine hydroxymethyltransferase, mitochondrial precursor |
| Enzyme 6 Synonyms |
- Serine methylase
- Glycine hydroxymethyltransferase
- SHMT
|
| Enzyme 6 Gene Name |
SHMT2 |
| Enzyme 6 Protein Sequence |
>Serine hydroxymethyltransferase, mitochondrial precursor
MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELL
QREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQ
RRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
KRISATSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREV
CDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVD
PKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARA
MADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAIT
PGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQ
RLANLRQRVEQFARAFPMPGFDEH
|
| Enzyme 6 Number of Residues |
504 |
| Enzyme 6 Molecular Weight |
55994 |
| Enzyme 6 Theoretical pI |
8.67 |
| Enzyme 6 GO Classification |
| Function |
- catalytic activity
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- glycine metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
| — |
|
| Enzyme 6 General Function |
Amino acid transport and metabolism |
| Enzyme 6 Specific Function |
Interconversion of serine and glycine |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
746436  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P34897  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
GLYM_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1452 bp
ATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGGGGAAGCAAACAGG
GGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTGGGAGTTGCTGCAG
AGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGAGAACTTCTGCAGC
CGAGCTGCGCTGGAGGCCCTGGGGTCCTGTCTGAACAACAAGTACTCGGAGGGTTATCCT
GGCAAGAGATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAGCGC
CGGGCCTTGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCCTAC
TCCGGGTCCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGGATC
ATGGGGCTGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTCAAG
CGGATATCAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCCCAAAACT
GGCCTCATTGACTACAACCAGCTGGCACTGACTGCTCGACTTTTCCGGCCACGGCTCATC
ATAGCTGGCACCAGCGCCTATGCTCGCCTCATTGACTACGCCCGCATGAGAGAGGTGTGT
GATGAAGTCAAAGCACACCTGCTGGCAGACATGGCCCACATCAGTGGCCTGGTGGCTGCC
AAGGTGATTCCCTCGCCTTTCAAGCACGCGGACATCGTCACCACCACTACTCACAAGACT
CTTCGAGGGGCCAGGTCAGGGCTCATCTTCTACCGGAAAGGGGTGAAGGCTGTGGACCCC
AAGACTGGCCGGGAGATCCCTTACACATTTGAGGACCGAATCAACTTTGCCGTGTTCCCA
TCCCTGCAGGGGGGCCCCCACAATCATGCCATTGCTGCAGTAGCTGTGGCCCTAAAGCAG
GCCTGCACCCCCATGTTCCGGGAGTACTCCCTGCAGGTTCTGAAGAATGCTCGGGCCATG
GCAGATGCCCTGCTAGAGCGAGGCTACTCACTGGTATCAGGTGGTACTGACAACCACCTG
GTGCTGGTGGACCTGCGGCCCAAGGGCCTGGATGGAGCTCGGGCTGAGCGGGTGCTAGAG
CTTGTATCCATCACTGCCAACAAGAACACCTGTCCTGGAGACCGAAGTGCCATCACACCG
GGCGGCCTGCGGCTTGGGGCCCCAGCCTTAACTTCTCGACAGTTCCGTGAGGATGACTTC
CGGAGAGTTGTGGACTTTATAGATGAAGGGGTCAACATTGGCTTAGAGGTGAAGAGCAAG
ACTGCCAAGCTCCAGGATTTCAAATCCTTCCTGCTTAAGGACTCAGAAACAAGTCAGCGT
CTGGCCAACCTCAGGCAACGGGTGGAGCAGTTTGCCAGGGCCTTCCCCATGCCTGGTTTT
GATGAGCATTGA
|
| Enzyme 6 GenBank Gene ID |
U23143  |
| Enzyme 6 GeneCard ID |
SHMT2  |
| Enzyme 6 GenAtlas ID |
SHMT2  |
| Enzyme 6 HGNC ID |
HGNC:10852  |
| Enzyme 6 Chromosome Location |
12 |
| Enzyme 6 Locus |
12q12-q14 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Stover PJ, Chen LH, Suh JR, Stover DM, Keyomarsi K, Shane B: Molecular cloning, characterization, and regulation of the human mitochondrial serine hydroxymethyltransferase gene. J Biol Chem. 1997 Jan 17;272(3):1842-8. [PubMed
]
- Garrow TA, Brenner AA, Whitehead VM, Chen XN, Duncan RG, Korenberg JR, Shane B: Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization. J Biol Chem. 1993 Jun 5;268(16):11910-6. [PubMed
]
- Snell K, Baumann U, Byrne PC, Chave KJ, Renwick SB, Sanders PG, Whitehouse SK: The genetic organization and protein crystallographic structure of human serine hydroxymethyltransferase. Adv Enzyme Regul. 2000;40:353-403. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6074 |
| Enzyme 7 Name |
Serine hydroxymethyltransferase, cytosolic |
| Enzyme 7 Synonyms |
- Serine methylase
- Glycine hydroxymethyltransferase
- SHMT
|
| Enzyme 7 Gene Name |
SHMT1 |
| Enzyme 7 Protein Sequence |
>Serine hydroxymethyltransferase, cytosolic
MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRA
VLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSG
SPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGY
INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGV
VPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGL
QGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL
VDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQK
VAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL
PDF
|
| Enzyme 7 Number of Residues |
483 |
| Enzyme 7 Molecular Weight |
53083 |
| Enzyme 7 Theoretical pI |
7.77 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- glycine metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
| — |
|
| Enzyme 7 General Function |
Amino acid transport and metabolism |
| Enzyme 7 Specific Function |
Interconversion of serine and glycine |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
307422  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P34896  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
GLYC_HUMAN  |
| Enzyme 7 PDB ID |
1BJ4  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1452 bp
ATGACGATGCCAGTCAACGGGGCCCACAAGGATGCTGACCTGTGGTCCTCACATGACAAG
ATGCTGGCACAACCCCTCAAAGACAGTGATGTTGAGGTTTACAACATCATTAAGAAGGAG
AGTAACCGGCAGAGGGTTGGATTGGAGCTGATTGCCTCGGAGAATTTCGCCAGCCGAGCA
GTTTTGGAGGCCCTAGGCTCTTGCTTAAATAACAAATACTCTGAGGGGTACCCGGGCCAG
AGATACTATGGCGGGACTGAGTTTATTGATGAACTGGAGACCCTCTGTCAGAAGCGAGCC
CTGCAGGCCTATAAGCTGGACCCACAGTGCTGGGGGGTCAACGTCCAGCCCTACTCAGGC
TCCCCTGCAAACTTTGCTGTGTACACTGCCCTGGTGGAACCCCATGGGCGCATCATGGGC
CTGGACCTTCCGGATGGGGGCCACCTGACCCATGGGTTCATGACAGACAAGAAGAAAATC
TCTGCCACGTCCATCTTCTTTGAATCTATGCCCTACAAGGTGAACCCAGATACTGGCTAC
ATCAACTATGACCAGCTGGAGGAGAACGCACGCCTCTTCCACCCGAAGCTGATCATCGCA
GGAACCAGCTGCTACTCCCGAAACCTGGAATATGCCCGGCTACGGAAGATTGCAGATGAG
AACGGGGCGTATCTCATGGCGGACATGGCTCACATCAGCGGGCTGGTGGCGGCTGGCGTG
GTGCCCTCCCCATTTGAACACTGCCATGTGGTGACCACCACCACTCACAAGACCCTGCGA
GGCTGCCGAGCTGGCATGATCTTCTACAGGAAAGGAGTGAAAAGTGTGGATCCCAAGACT
GGCAAAGAGATTCTGTACAACCTGGAGTCTCTTATCAATTCTGCTGTGTTCCCTGGCCTG
CAGGGAGGTCCCCACAACCACGCCATTGCTGGGGTTGCTGTGGCACTGAAGCAAGCTATG
ACTCTGGAATTTAAAGTTTATCAACACCAGGTGGTGGCCAACTGCAGGGCTCTGTCTGAG
GCCCTGACGGAGCTGGGCTACAAAATAGTCACAGGTGGTTCTGACAACCATTTGATCCTT
GTGGATCTCCGTTCCAAAGGCACAGATGGTGGAAGGGCTGAGAAGGTGCTAGAAGCCTGT
TCTATTGCCTGCAACAAGAACACCTGTCCAGGTGACAGAAGCGCTCTGCGGCCCAGTGGA
CTGCGGCTGGGGACCCCAGCACTGACGTCCCGTGGACTTTTGGAAAAAGACTTCCAAAAA
GTAGCCCACTTTATTCACAGAGGGATAGAGCTGACCCTGCAGATCCAGAGCGACACTGGT
GTCAGAGCCACCCTGAAAGAGTTCAAGGAGAGACTGGCAGGGGATAAGTACCAGGCGGCC
GTGCAGGCTCTCCGGGAGGAGGTTGAGAGCTTCGCCTCTCTCTTCCCTCTGCCTGGCCTG
CCTGACTTCTAA
|
| Enzyme 7 GenBank Gene ID |
L11931  |
| Enzyme 7 GeneCard ID |
SHMT1  |
| Enzyme 7 GenAtlas ID |
SHMT1  |
| Enzyme 7 HGNC ID |
HGNC:10850  |
| Enzyme 7 Chromosome Location |
17 |
| Enzyme 7 Locus |
17p11.2 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Garrow TA, Brenner AA, Whitehead VM, Chen XN, Duncan RG, Korenberg JR, Shane B: Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization. J Biol Chem. 1993 Jun 5;268(16):11910-6. [PubMed
]
- Chave KJ, Snell K, Sanders PG: Isolation and characterisation of human genomic sequences encoding cytosolic serine hydroxymethyltransferase. Biochem Soc Trans. 1997 Feb;25(1):53S. [PubMed
]
- Renwick SB, Snell K, Baumann U: The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy. Structure. 1998 Sep 15;6(9):1105-16. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6168 |
| Enzyme 8 Name |
Serine palmitoyltransferase 1 |
| Enzyme 8 Synonyms |
- Long chain base biosynthesis protein 1
- LCB 1
- Serine-palmitoyl-CoA transferase 1
- SPT 1
- SPT1
|
| Enzyme 8 Gene Name |
SPTLC1 |
| Enzyme 8 Protein Sequence |
>Serine palmitoyltransferase 1
MATATEQWVLVEMVQALYEAPAYHLILEGILILWIIRLLFSKTYKLQERSDLTVKEKEEL
IEEWQPEPLVPPVPKDHPALNYNIVSGPPSHKTVVNGKECINFASFNFLGLLDNPRVKAA
ALASLKKYGVGTCGPRGFYGTFDVHLDLEDRLAKFMKTEEAIIYSYGFATIASAIPAYSK
RGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDQKNPRKARVTRR
FIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDI
DLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENP
GIFAVLKEKCGQIHKALQGISGLKVVGESLSPAFHLQLEESTGSREQDVRLLQEIVDQCM
NRSIALTQARYLEKEEKCLPPPSIRVVVTVEQTEEELERAASTIKEVAQAVLL
|
| Enzyme 8 Number of Residues |
473 |
| Enzyme 8 Molecular Weight |
52745 |
| Enzyme 8 Theoretical pI |
5.87 |
| Enzyme 8 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Coenzyme transport and metabolism |
| Enzyme 8 Specific Function |
Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D- sphinganine + CO(2) |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
2564247  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
O15269  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
LCB1_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1422 bp
ATGGCGACCGCCACGGAGCAGTGGGTTCTGGTGGAGATGGTACAGGCGCTTTACGAGGCT
CCTGCTTACCATCTTATTTTGGAAGGGATTCTGATCCTCTGGATAATCAGACTTCTTTTC
TCTAAGACTTACAAATTACAAGAACGATCTGATCTTACAGTCAAGGAAAAAGAAGAACTG
ATTGAAGAGTGGCAACCAGAACCTCTTGTTCCTCCTGTCCCAAAAGACCATCCTGCTCTC
AACTACAACATCGTTTCAGGCCCTCCAAGCCACAAAACTGTGGTGAATGGAAAAGAATGT
ATAAACTTCGCCTCATTTAATTTTCTTGGATTGTTGGATAACCCTAGGGTTAAGGCAGCA
GCTTTAGCATCTCTAAAGAAGTATGGCGTGGGGACTTGTGGACCCAGAGGATTTTATGGC
ACATTTGATGTTCATTTGGATTTGGAAGACCGCCTGGCAAAATTTATGAAGACAGAAGAA
GCCATTATATACTCATATGGATTTGCCACCATAGCCAGTGCTATTCCTGCTTACTCTAAA
AGAGGGGACATTGTTTTTGTAGATAGAGCTGCCTGCTTTGCTATTCAGAAAGGATTACAG
GCATCCCGTAGTGACATTAAGTTATTTAAGCATAATGACATGGCTGACCTCGAGCGACTA
CTAAAAGAACAAGAGATCGAAGATCAAAAGAATCCTCGCAAGGCTCGTGTAACTCGGCGT
TTCATTGTAGTAGAAGGATTGTATATGAATACTGGAACTATTTGTCCTCTTCCAGAATTG
GTTAAGTTAAAATACAAATACAAAGCAAGAATCTTCCTGGAGGAAAGCCTTTCATTTGGA
GTCCTAGGAGAGCATGGCCGAGGAGTCACTGAACACTATGGAATCAATATTGATGATATT
GATCTTATCAGTGCCAACATGGAGAATGCACTTGCTTCTATTGGAGGTTTCTGCTGTGGC
AGGTCTTTTGTAATTGACCATCAGCGACTTTCCGGCCAGGGATACTGCTTTTCAGCTTCG
TTACCTCCCCTGTTAGCTGCTGCAGCAATTGAGGCCCTCAACATCATGGAAGAGAATCCA
GGTATTTTTGCAGTGTTGAAGGAAAAGTGCGGACAAATTCATAAAGCTTTACAAGGCATT
TCTGGATTAAAAGTGGTGGGGGAGTCCCTTTCTCCAGCCTTTCACCTACAACTGGAAGAG
AGCACTGGGTCTCGCGAGCAAGATGTCAGACTGCTTCAGGAAATTGTAGATCAATGCATG
AACAGAAGTATTGCATTAACTCAGGCGCGCTACTTGGAGAAAGAAGAGAAGTGTCTCCCT
CCTCCCAGCATTCGGGTTGTGGTCACGGTGGAACAAACAGAGGAAGAACTGGAGAGAGCT
GCGTCCACCATCAAGGAGGTAGCCCAGGCCGTCCTGCTCTAG
|
| Enzyme 8 GenBank Gene ID |
Y08685  |
| Enzyme 8 GeneCard ID |
SPTLC1  |
| Enzyme 8 GenAtlas ID |
SPTLC1  |
| Enzyme 8 HGNC ID |
HGNC:11277  |
| Enzyme 8 Chromosome Location |
9 |
| Enzyme 8 Locus |
9q22.2 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Weiss B, Stoffel W: Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis. Eur J Biochem. 1997 Oct 1;249(1):239-47. [PubMed
]
- Dawkins JL, Hulme DJ, Brahmbhatt SB, Auer-Grumbach M, Nicholson GA: Mutations in SPTLC1, encoding serine palmitoyltransferase, long chain base subunit-1, cause hereditary sensory neuropathy type I. Nat Genet. 2001 Mar;27(3):309-12. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
6169 |
| Enzyme 9 Name |
Phosphoserine phosphatase |
| Enzyme 9 Synonyms |
- PSP
- O-phosphoserine phosphohydrolase
- PSPase
- L-3-phosphoserine phosphatase
|
| Enzyme 9 Gene Name |
PSPH |
| Enzyme 9 Protein Sequence |
>Phosphoserine phosphatase
MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKA
ALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVA
SKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKIIMIGDG
ATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE
|
| Enzyme 9 Number of Residues |
225 |
| Enzyme 9 Molecular Weight |
25008 |
| Enzyme 9 Theoretical pI |
5.42 |
| Enzyme 9 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
- phosphoserine phosphatase activity
|
| Process |
- L-serine biosynthesis
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
| — |
|
| Enzyme 9 General Function |
Amino acid transport and metabolism |
| Enzyme 9 Specific Function |
Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates |
| Enzyme 9 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 9 Reactions |
- L(or D)-O-phosphoserine + H2O = L(or D)-serine + phosphate
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
1890331  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P78330  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
SERB_HUMAN  |
| Enzyme 9 PDB ID |
1NNL  |
| Enzyme 9 PDB File |
Show |
| Enzyme 9 3D Structure |
|
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>678 bp
ATGGTCTCCCACTCAGAGCTGAGGAAGCTTTTCTACTCAGCAGATGCTGTGTGTTTTGAT
GTTGACAGCACGGTCATCAGAGAAGAAGGAATCGATGAGCTAGCCAAAATCTGTGGCGTT
GAGGACGCGGTGTCAGAAATGACACGGCGAGCCATGGGCGGGGCAGTGCCTTTCAAAGCT
GCTCTCACAGAGCGCTTAGCCCTCATCCAGCCCTCCAGGGAGCAGGTGCAGAGACTCATA
GCAGAGCAACCCCCACACCTGACCCCCGGCATAAGGGAGCTGGTAAGTCGCCTACAGGAG
CGAAATGTTCAGGTTTTCCTAATATCTGGTGGCTTTAGGAGTATTGTAGAGCATGTTGCT
TCAAAGCTCAATATCCCAGCAACCAATGTATTTGCCAATAGGCTGAAATTCTACTTTAAC
GGTGAATATGCAGGTTTTGATGAGACGCAGCCAACAGCTGAATCTGGTGGAAAAGGAAAA
GTGATTAAACTTTTAAAGGAAAAATTTCATTTTAAGAAAATAATCATGATTGGAGATGGT
GCCACAGATATGGAAGCCTGTCCTCCTGCTGATGCTTTCATTGGATTTGGAGGAAATGTG
ATCAGGCAACAAGTCAAGGATAACGCCAAATGGTATATCACTGATTTTGTAGAGCTGCTG
GGAGAACTGGAAGAATAA
|
| Enzyme 9 GenBank Gene ID |
Y10275  |
| Enzyme 9 GeneCard ID |
PSPH  |
| Enzyme 9 GenAtlas ID |
PSPH  |
| Enzyme 9 HGNC ID |
HGNC:9577  |
| Enzyme 9 Chromosome Location |
7 |
| Enzyme 9 Locus |
7p15.2-p15.1 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Collet JF, Gerin I, Rider MH, Veiga-da-Cunha M, Van Schaftingen E: Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate. FEBS Lett. 1997 May 26;408(3):281-4. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6170 |
| Enzyme 10 Name |
Serine palmitoyltransferase 2 |
| Enzyme 10 Synonyms |
- Long chain base biosynthesis protein 2
- LCB 2
- Serine-palmitoyl-CoA transferase 2
- SPT 2
|
| Enzyme 10 Gene Name |
SPTLC2 |
| Enzyme 10 Protein Sequence |
>Serine palmitoyltransferase 2
MRPEPGGCCCRRTVRANGCVANGEVRNGYVRSSAAAAAAAAAGQIHHVTQNGGLYKRPFN
EAFEETPMLVAVLTYVGYGVLTLFGYLRDFLRYWRIEKCHHATEREEQKDFVSLYQDFEN
FYTRNLYMRIRDNWNRPICSVPGARVDIMERQSHDYNWSFKYTGNIIKGVINMGSYNYLG
FARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFA
TNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQ
PRTRRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVV
EYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSLSPPVVEQII
TSMKCIMGQDGTSLGKECVQQLAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIG
AFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYS
RHRLVPLLDRPFDETTYEETED
|
| Enzyme 10 Number of Residues |
562 |
| Enzyme 10 Molecular Weight |
62925 |
| Enzyme 10 Theoretical pI |
7.85 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 10 General Function |
Coenzyme transport and metabolism |
| Enzyme 10 Specific Function |
Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D- sphinganine + CO(2) |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
2564249  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
O15270  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
LCB2_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1689 bp
ATGCGGCCGGAGCCCGGAGGCTGCTGCTGCCGCCGCACGGTGCGGGCGAATGGCTGCGTG
GCGAACGGGGAAGTACGGAACGGGTACGTGAGGAGCAGCGCTGCAGCCGCAGCCGCAGCC
GCCGCCGGCCAGATCCATCATGTTACACAAAATGGAGGACTATATAAAAGACCGTTTAAT
GAAGCTTTTGAAGAAACACCAATGCTGGTTGCTGTGCTCACGTATGTGGGGTATGGCGTA
CTCACCCTCTTTGGATATCTTCGAGATTTCTTGAGGTATTGGAGAATTGAAAAGTGTCAC
CATGCAACAGAAAGAGAAGAACAAAAGGACTTTGTGTCATTGTATCAAGATTTTGAAAAC
TTTTATACAAGGAATCTGTACATGAGGATAAGAGACAACTGGAATCGGCCAATCTGTAGT
GTGCCTGGAGCCAGGGTGGACATCATGGAGAGACAGTCTCATGATTATAACTGGTCCTTC
AAGTATACAGGGAATATAATAAAGGGTGTTATAAACATGGGTTCCTACAACTATCTTGGA
TTTGCACGGAATACTGGATCATGTCAAGAAGCAGCCGCCAAAGTCCTTGAGGAGTATGGA
GCTGGAGTGTGCAGTACTCGGCAGGAAATTGGAAACCTGGACAAGCATGAAGAACTAGAG
GAGCTTGTAGCAAGGTTCTTAGGAGTAGAAGCTGCTATGGCGTATGGCATGGGATTTGCA
ACGAATTCAATGAACATTCCTGCTCTTGTTGGCAAAGGTTGCCTGATTCTGAGTGATGAA
CTGAACCATGCATCACTGGTTCTGGGAGCCAGACTGTCAGGAGCAACCATTAGAATCTTC
AAACACAACAATATGCAAAGCCTAGAGAAGCTATTGAAAGATGCCATTGTTTATGGTCAG
CCTCGGACACGAAGGCCCTGGAAGAAAATTCTCATCCTTGTGGAAGGAATATATAGCATG
GAGGGATCTATTGTTCGTCTTCCTGAAGTGATTGCCCTCAAGAAGAAATACAAGGCATAC
TTGTATCTGGATGAGGCTCACAGCATTGGCGCCCTGGGCCCCACAGGCCGGGGTGTGGTG
GAGTACTTTGGCCTGGATCCCGAGGATGTGGATGTTATGATGGGAACGTTCACAAAGAGT
TTTGGTGCTTCTGGAGGATATATTGGAGGCAAGAAGGAGCTGATAGACTACCTGCGAACA
CATTCTCATAGTGCAGTGTATGCCACGTCATTGTCACCTCCTGTAGTGGAGCAGATCATC
ACCTCCATGAAGTGCATCATGGGGCAGGATGGCACCAGCCTTGGTAAAGAGTGTGTACAA
CAGTTAGCTGAAAACACCAGGTATTTCAGGAGACGCCTGAAAGAGATGGGCTTCATCATC
TATGGAAATGAAGACTCTCCAGTAGTGCCTTTGATGCTCTACATGCCTGCCAAAATTGGC
GCCTTTGGACGGGAGATGCTGAAGCGGAACATCGGTGTCGTTGTGGTTGGATTTCCTGCC
ACCCCAATTATTGAGTCCAGAGCCAGGTTTTGCCTGTCAGCAGCTCATACCAAAGAAATA
CTTGATACTGCTTTAAAGGAGATAGATGAAGTTGGGGACCTATTGCAGCTGAAGTATTCC
CGTCATCGGTTGGTACCTCTACTGGACAGGCCCTTTGACGAGACGACGTATGAAGAAACA
GAAGACTGA
|
| Enzyme 10 GenBank Gene ID |
Y08686  |
| Enzyme 10 GeneCard ID |
SPTLC2  |
| Enzyme 10 GenAtlas ID |
SPTLC2  |
| Enzyme 10 HGNC ID |
HGNC:11278  |
| Enzyme 10 Chromosome Location |
14 |
| Enzyme 10 Locus |
14q24.3-q31 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Weiss B, Stoffel W: Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis. Eur J Biochem. 1997 Oct 1;249(1):239-47. [PubMed
]
- Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed
]
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed
]
- Nagiec MM, Lester RL, Dickson RC: Sphingolipid synthesis: identification and characterization of mammalian cDNAs encoding the Lcb2 subunit of serine palmitoyltransferase. Gene. 1996 Oct 24;177(1-2):237-41. [PubMed
]
- Takeda J, Yano H, Eng S, Zeng Y, Bell GI: A molecular inventory of human pancreatic islets: sequence analysis of 1000 cDNA clones. Hum Mol Genet. 1993 Nov;2(11):1793-8. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
8650 |
| Enzyme 11 Name |
Neutral amino acid transporter A |
| Enzyme 11 Synonyms |
- SATT
- Solute carrier family 1 member 4
- Alanine/serine/cysteine/ threonine transporter
- ASCT1
|
| Enzyme 11 Gene Name |
SLC1A4 |
| Enzyme 11 Protein Sequence |
>Neutral amino acid transporter A
MEKSNETNGYLDSAQAGPAAGPGAPGTAAGRARRCAGFLRRQALVLLTVSGVLAGAGLGA
ALRGLSLSRTQVTYLAFPGEMLLRMLRMIILPLVVCSLVSGAASLDASCLGRLGGIAVAY
FGLTTLSASALAVALAFIIKPGSGAQTLQSSDLGLEDSGPPPVPKETVDSFLDLARNLFP
SNLVVAAFRTYATDYKVVTQNSSSGNVTHEKIPIGTEIEGMNILGLVLFALVLGVALKKL
GSEGEDLIRFFNSLNEATMVLVSWIMWYVPVGIMFLVGSKIVEMKDIIVLVTSLGKYIFA
SILGHVIHGGIVLPLIYFVFTRKNPFRFLLGLLAPFATAFATCSSSATLPSMMKCIEENN
GVDKRISRFILPIGATVNMDGAAIFQCVAAVFIAQLNNVELNAGQIFTILVTATASSVGA
AGVPAGGVLTIAIILEAIGLPTHDLPLILAVDWIVDRTTTVVNVEGDALGAGILHHLNQK
ATKKGEQELAEVKVEAIPNCKSEEETSPLVTHQNPAGPVASAPELESKESVL
|
| Enzyme 11 Number of Residues |
532 |
| Enzyme 11 Molecular Weight |
55724 |
| Enzyme 11 Theoretical pI |
6.18 |
| Enzyme 11 GO Classification |
| Function |
- carboxylic acid transporter activity
- dicarboxylic acid transporter activity
- organic acid transporter activity
- sodium:dicarboxylate symporter activity
- transporter activity
|
| Process |
- carboxylic acid transport
- cellular physiological process
- dicarboxylic acid transport
- organic acid transport
- physiological process
- transport
|
| Component |
|
|
| Enzyme 11 General Function |
Energy production and conversion |
| Enzyme 11 Specific Function |
Transporter for alanine, serine, cysteine, and threonine. Exhibits sodium dependence |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
- 42-62
88-108
119-139
217-237
257-277
298-318
328-348
373-393
418-438
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
348012  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
P43007  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
SATT_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1599 bp
ATGGAGAAGAGCAACGAGACCAACGGCTACCTTGACAGCGCTCAGGCGGGGCCTGCGGCC
GGGCCCGGAGCTCCGGGGACCGCGGCGGGACGCGCACGGCGTTGCGCGCGCTTCCTGCGG
CGCCAAGCGCTGGTGCTGCTCACCGTGTCCGGGGTGCTGGCGGGCGCGGGCCTGGGCGCG
GCGTTGCGCGGGCTCAGCCTGAGCCGCACGCAGGTCACCTACCTGGCCTTCCCCGGCGAG
ATGCTGCTCCGCATGCTGCGCATGATCATCCTGCCGCTGGTGGTCTGCAGCCTGGTGTCG
GGCGCCGCCTCGCTCGATGCCAGCTGCCTCGGGCGTCTGGGCGGCATCCGTGTCGCCTAC
TTTGGCCTCACCACACTGAGTGCCTCGGCGCTCGCCGTGGCCTTGGCGTTCATCATCAAG
CCAGGATCCGGTGCGCAGACCCTTCAGTCCAGCGACCTGGGGCTGGAGGACTCGGGGCCT
CCTCCTGTCCCCAAAGAGACGGTGGACTCTTTCCTCGACCTGGCCAGAAACCTGTTTCCC
TCCAATCTTGTGGTTGCAGCTTTCCGTACGTATGCAACCGATTATAAAGTCGTGACCCAG
AACAGCAGCTCTGGAAATGTAACCCATGAAAAGATCCCCATAGGCACTGAGATAGAAGGG
ATGAACATTTTAGGATTGGTCCTGTTTGCTCTGGTGTTAGGAGTGGCCTTAAAGAAACTA
GGCTCCGAAGGAGAAGACCTCATCCGTTTCTTCAATTCCCTCAACGAGGCGACGATGGTG
CTGGTGTCCTGGATTATGTGGTACGTACCTGTGGGCATCATGTTCCTTGTTGGAAGCAAG
ATCGTGGAAATGAAAGACATCATCGTGCTGGTGACCAGCCTGGGGAAATACATCTTCGCA
TCTATATTGGGCCATGTTATTCATGGAGGAATTGTTCTGCCACTTATTTATTTTGTTTTC
ACACGAAAAAACCCATTCAGATTCCTCCTGGGCCTCCTCGCCCCATTTGCGACAGCATTT
GCTACCTGCTCCAGCTCAGCGACCCTTCCCTCTATGATGAAGTGCATTGAAGAGAACAAT
GGTGTGGACAAGAGGATCAGCAGGTTTATTCTCCCCATCGGGGCCACCGTGAACATGGAC
GGAGCAGCCATCTTCCAGTGTGTGGCCGCGGTGTTCATTGCGCAACTCAACAACATAGAG
CTCAACGCAGGACAGATTTTCACCATTCTAGTGACTGCCACAGCGTCCAGTGTTGGAGCA
GCAGGCGTGCCAGCTGGAGGGGTCCTCACCATTGCCATTATCCTGGAGGCCATTGGGCTG
CCTACTCATGACCTGCCTCTGATCCTGGCTGTGGACTGGATTGTGGACCGGACCACCACG
GTGGTGAATGTGGAAGGGGATGCCCTGGGTGCAGGCATTCTCCACCACCTGAATCAGAAG
GCAACAAAGAAAGGCGAGCAGGAACTTGCTGAGGTGAAAGTGGAAGCCATCCCCAACTGC
AAGTCTGAGGAGGAGACATCGCCCCTGGTGACACACCAGAACCCCGCTGGCCCCGTGGCC
AGTGCCCCAGAACTGGAATCCAAGGAGTCGGTTCTGTGA
|
| Enzyme 11 GenBank Gene ID |
L14595  |
| Enzyme 11 GeneCard ID |
SLC1A4  |
| Enzyme 11 GenAtlas ID |
SLC1A4  |
| Enzyme 11 HGNC ID |
HGNC:10942  |
| Enzyme 11 Chromosome Location |
2 |
| Enzyme 11 Locus |
2p15-p13 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Arriza JL, Kavanaugh MP, Fairman WA, Wu YN, Murdoch GH, North RA, Amara SG: Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family. J Biol Chem. 1993 Jul 25;268(21):15329-32. [PubMed
]
- Shafqat S, Tamarappoo BK, Kilberg MS, Puranam RS, McNamara JO, Guadano-Ferraz A, Fremeau RT Jr: Cloning and expression of a novel Na(+)-dependent neutral amino acid transporter structurally related to mammalian Na+/glutamate cotransporters. J Biol Chem. 1993 Jul 25;268(21):15351-5. [PubMed
]
- Hofmann K, Duker M, Fink T, Lichter P, Stoffel W: Human neutral amino acid transporter ASCT1: structure of the gene (SLC1A4) and localization to chromosome 2p13-p15. Genomics. 1994 Nov 1;24(1):20-6. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
13019 |
| Enzyme 12 Name |
cDNA FLJ75824, highly similar to Homo sapiens serine dehydratase |
| Enzyme 12 Synonyms |
- SDS, mRNA
- Serine dehydratase, isoform CRA_a
|
| Enzyme 12 Gene Name |
SDS |
| Enzyme 12 Protein Sequence |
>cDNA FLJ75824, highly similar to Homo sapiens serine dehydratase
MMSGEPLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHF
VCSSAGNAGMAAAYAARQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELA
KALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIALSVGGGGLLCGVVQGL
QEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHP
IFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQLEGNLRTPLPSLVV
IVCGGSNISLAQLRALKEQLGMTNRLPK
|
| Enzyme 12 Number of Residues |
328 |
| Enzyme 12 Molecular Weight |
34626 |
| Enzyme 12 Theoretical pI |
8.14 |
| Enzyme 12 GO Classification |
Not Available |
| Enzyme 12 General Function |
Amino acid transport and metabolism |
| Enzyme 12 Specific Function |
Not Available |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
Not Available |
| Enzyme 12 Pfam Domain Function |
Not Available |
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
158258957  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
A8K9P5  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
A8K9P5_HUMAN  |
| Enzyme 12 PDB ID |
1P5J  |
| Enzyme 12 PDB File |
Show |
| Enzyme 12 3D Structure |
|
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
Not Available |
| Enzyme 12 GenBank Gene ID |
AK292760  |
| Enzyme 12 GeneCard ID |
A8K9P5  |
| Enzyme 12 GenAtlas ID |
Not Available |
| Enzyme 12 HGNC ID |
Not Available |
| Enzyme 12 Chromosome Location |
Not Available |
| Enzyme 12 Locus |
Not Available |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
Not Available |
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
13103 |
| Enzyme 13 Name |
cDNA FLJ75707, highly similar to Homo sapiens serine palmitoyltransferase, long chain base subunit 1 |
| Enzyme 13 Synonyms |
- SPTLC1, transcript variant 1, mRNA
- Serine palmitoyltransferase, long chain base subunit 1, isoform CRA_a
|
| Enzyme 13 Gene Name |
SPTLC1 |
| Enzyme 13 Protein Sequence |
>cDNA FLJ75707, highly similar to Homo sapiens serine palmitoyltransferase, long chain base subunit 1
MATATEQWVLVEMVQALYEAPAYHLILEGILILWIIRLLFSKTYKLQERSDLTVKEKEEL
IEEWQPEPLVPPVPKDHPALNYNIVSGPPSHKTVVNGKECINFASFNFLGLLDNPRVKAA
ALASLKKYGVGTCGPRGFYGTFDVHLDLEDRLAKFMKTEEAIIYSYGFATIASAIPAYSK
RGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDQKNPRKARVTRR
FIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDI
DLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENP
GIFAVLKEKCGQIHKALQGISGLKVVGESLSPAFHLQLEESTGSREQDVRLLQEIVDQCM
NRSIALTQARYLEKEEKCLPPPSIRVVVTVEQTEEELERAASTIKEVAQAVLL
|
| Enzyme 13 Number of Residues |
473 |
| Enzyme 13 Molecular Weight |
52745 |
| Enzyme 13 Theoretical pI |
5.87 |
| Enzyme 13 GO Classification |
Not Available |
| Enzyme 13 General Function |
Coenzyme transport and metabolism |
| Enzyme 13 Specific Function |
Not Available |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
Not Available |
| Enzyme 13 Pfam Domain Function |
Not Available |
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
158256524  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
A8K681  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
A8K681_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
Not Available |
| Enzyme 13 GenBank Gene ID |
AK291546  |
| Enzyme 13 GeneCard ID |
A8K681  |
| Enzyme 13 GenAtlas ID |
Not Available |
| Enzyme 13 HGNC ID |
Not Available |
| Enzyme 13 Chromosome Location |
Not Available |
| Enzyme 13 Locus |
Not Available |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
Not Available |
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
14708 |
| Enzyme 14 Name |
Serine palmitoyltransferase 3 |
| Enzyme 14 Synonyms |
- Long chain base biosynthesis protein 3
- LCB 3
- Serine-palmitoyl-CoA transferase 3
- SPT 3
|
| Enzyme 14 Gene Name |
SPTLC3 |
| Enzyme 14 Protein Sequence |
>Serine palmitoyltransferase 3
MANPGGGAVCNGKLHNHKKQSNGSQSRNCTKNGIVKEAQQNGKPHFYDKLIVESFEEAPL
HVMVFTYMGYGIGTLFGYLRDFLRNWGIEKCNAAVERKEQKDFVPLYQDFENFYTRNLYM
RIRDNWNRPICSAPGPLFDLMERVSDDYNWTFRFTGRVIKDVINMGSYNFLGLAAKYDES
MRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPA
LVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAVIYGQPRTRRAWK
KILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPH
EVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMG
LDGTTQGLQRVQQLAKNTRYFRQRLQEMGFIIYGNENASVVPLLLYMPGKVAAFARHMLE
KKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQLKYSRHKKSARP
ELYDETSFELED
|
| Enzyme 14 Number of Residues |
552 |
| Enzyme 14 Molecular Weight |
62050 |
| Enzyme 14 Theoretical pI |
9.05 |
| Enzyme 14 GO Classification |
Not Available |
| Enzyme 14 General Function |
Coenzyme transport and metabolism |
| Enzyme 14 Specific Function |
Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D- sphinganine + CO(2) |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 [RN:R01281] ALL_REAC R01281
|
| Enzyme 14 Pfam Domain Function |
Not Available |
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
7023574  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q9NUV7  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
SPTC3_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>528 bp
ATGGCTAACCCTGGAGGTGGTGCTGTTTGCAACGGGAAACTTCACAATCACAAGAAACAG
AGCAATGGCTCACAAAGCAGAAACTGCACAAAGAATGGAATAGTGAAGGAAGCCCAGCAA
AATGGGAAGCCACATTTTTATGATAAGCTCATTGTTGAATCGTTTGAGGAAGCACCCCTT
CATGTTATGGTTTTCACTTACATGGGATATGGAATTGGAACCCTGTTTGGCTATCTCAGA
GACTTTTTAAGAAACTGGGGAATAGAAAAATGCAACGCAGCTGTGGAACGAAAAGAACAA
AAAGTACGTATGCGCACCTCCCTGGATCTTTGTCAATGCCTACTCCTCTCTAAAGTGTTC
TCAGAAGTGGTGATGCAGGTGCAGATTCTAGAAAGCATGAGGTGCTCAGGAACTATTCAG
GGCAAATTTCATTCATCTCCACCTGCTAAACCCCATTACCCATGGGCTTATGGACCTGTT
TTTACAAACATCTCATGGGCAACTACTATTTGCCACATACCAAACTAA
|
| Enzyme 14 GenBank Gene ID |
AK001974  |
| Enzyme 14 GeneCard ID |
Q9NUV7  |
| Enzyme 14 GenAtlas ID |
SPTLC3  |
| Enzyme 14 HGNC ID |
HGNC:16253  |
| Enzyme 14 Chromosome Location |
20 |
| Enzyme 14 Locus |
20p12.1 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- 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
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
14709 |
| Enzyme 15 Name |
Serine racemase |
| Enzyme 15 Synonyms |
Not Available |
| Enzyme 15 Gene Name |
SRR |
| Enzyme 15 Protein Sequence |
>Serine racemase
MCAQYCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGA
LNAVRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQA
YGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDAL
VVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNLYPPETIADGV
KSSIGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQT
VSPEVKNICIVLSGGNVDLTSSITWVKQAERPASYQSVSV
|
| Enzyme 15 Number of Residues |
340 |
| Enzyme 15 Molecular Weight |
36567 |
| Enzyme 15 Theoretical pI |
6.51 |
| Enzyme 15 GO Classification |
| Function |
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Amino acid transport and metabolism |
| Enzyme 15 Specific Function |
Catalyzes the synthesis of D-serine from L-serine |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
Not Available |
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
11034785  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q9GZT4  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
SRR_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1023 bp
ATGTGTGCTCAGTATTGCATCTCCTTTGCTGATGTTGAAAAAGCTCATATCAACATTCGA
GATTCTATCCACCTCACACCAGTGCTAACAAGCTCCATTTTGAATCAACTAACAGGGCGC
AATCTTTTCTTCAAATGTGAACTCTTCCAGAAAACAGGATCTTTTAAGATTCGTGGTGCT
CTCAATGCCGTCAGAAGCTTGGTTCCTGATGCTTTAGAAAGGAAGCCGAAAGCTGTTGTT
ACTCACAGCAGTGGAAACCATGGCCAGGCTCTCACCTATGCTGCCAAATTGGAAGGAATT
CCTGCTTATATTGTGGTGCCCCAGACAGCTCCAGACTGTAAAAAACTTGCAATACAAGCC
TACGGAGCGTCAATTGTATACTGTGAACCTAGTGATGAGTCCAGAGAAAATGTTGCAAAA
AGAGTTACAGAAGAAACAGAAGGCATCATGGTACATCCCAACCAGGAGCCTGCAGTGATA
GCTGGACAAGGGACAATTGCCCTGGAAGTGCTGAACCAGGTTCCTTTGGTGGATGCACTG
GTGGTACCTGTAGGTGGAGGAGGAATGCTTGCTGGAATAGCAATTACAGTTAAGGCTCTG
AAACCTAGTGTGAAGGTATATGCTGCTGAACCCTCAAATGCAGATGACTGCTACCAGTCC
AAGCTGAAGGGGAAACTGATGCCCAATCTTTATCCTCCAGAAACCATAGCAGATGGTGTC
AAATCCAGCATTGGCTTGAACACCTGGCCTATTATCAGGGACCTTGTGGATGATATCTTC
ACTGTCACAGAGGATGAAATTAAGTGTGCAACCCAGCTGGTGTGGGAGAGGATGAAACTA
CTCATTGAACCTACAGCTGGTGTTGGAGTGGCTGCTGTGCTGTCTCAACATTTTCAAACT
GTTTCCCCAGAAGTAAAGAACATTTGTATTGTGCTCAGTGGTGGAAATGTAGACTTAACC
TCCTCCATAACTTGGGTGAAGCAGGCTGAAAGGCCAGCTTCTTATCAGTCTGTTTCTGTT
TAA
|
| Enzyme 15 GenBank Gene ID |
AF169974  |
| Enzyme 15 GeneCard ID |
Q9GZT4  |
| Enzyme 15 GenAtlas ID |
SRR  |
| Enzyme 15 HGNC ID |
HGNC:14398  |
| Enzyme 15 Chromosome Location |
17 |
| Enzyme 15 Locus |
17p13 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- De Miranda J, Santoro A, Engelender S, Wolosker H: Human serine racemase: moleular cloning, genomic organization and functional analysis. Gene. 2000 Oct 3;256(1-2):183-8. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
14721 |
| Enzyme 16 Name |
Uncharacterized protein SHMT1 |
| Enzyme 16 Synonyms |
Not Available |
| Enzyme 16 Gene Name |
SHMT1 |
| Enzyme 16 Protein Sequence |
>Uncharacterized protein SHMT1
MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRA
VLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSG
SPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGY
INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGV
VPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGL
QGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL
VDLRSKGTDGGRAEKVLEACSIACNKNTCPGIELTLQIQSDTGVRATLKEFKERLAGDKY
QAAVQALREEVESFASLFPLPGLPDF
|
| Enzyme 16 Number of Residues |
446 |
| Enzyme 16 Molecular Weight |
48999 |
| Enzyme 16 Theoretical pI |
7.01 |
| Enzyme 16 GO Classification |
Not Available |
| Enzyme 16 General Function |
Amino acid transport and metabolism |
| Enzyme 16 Specific Function |
Not Available |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
Not Available |
| Enzyme 16 Pfam Domain Function |
Not Available |
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
Not Available |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
A8MYA6  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
A8MYA6_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
Not Available |
| Enzyme 16 GenBank Gene ID |
AL353997  |
| Enzyme 16 GeneCard ID |
A8MYA6  |
| Enzyme 16 GenAtlas ID |
SHMT1  |
| Enzyme 16 HGNC ID |
HGNC:10850  |
| Enzyme 16 Chromosome Location |
17 |
| Enzyme 16 Locus |
17p11.2 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
Not Available |
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
14728 |
| Enzyme 17 Name |
Serine hydroxymethyltransferase |
| Enzyme 17 Synonyms |
Not Available |
| Enzyme 17 Gene Name |
SHMT2 |
| Enzyme 17 Protein Sequence |
>Serine hydroxymethyltransferase
ELRCCTSLCFGRLGLCRDVGSWSGWPFGLSTATQPRLRLGKQTGAGQARRACRTVILRCG
SCCRGRRTGSVVAWSSLPQRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPYSGS
PANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKTGLI
DYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVI
PSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYTFEDRINFAVFPSLQ
GGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGYSLVSGGTDNHLVLV
DLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV
VDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPMPGFDEH
|
| Enzyme 17 Number of Residues |
480 |
| Enzyme 17 Molecular Weight |
52910 |
| Enzyme 17 Theoretical pI |
9.66 |
| Enzyme 17 GO Classification |
| Function |
- catalytic activity
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- glycine metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
| — |
|
| Enzyme 17 General Function |
Amino acid transport and metabolism |
| Enzyme 17 Specific Function |
Interconversion of serine and glycine |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945] ALL_REAC R00945
- (other) R03284
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
60552225  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q5BJF5  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
Q5BJF5_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>1445 bp
CCGAGTTGCGATGCTGTACTTCTCTTTGTTTTGGGCGGCTCGGCCTCTGCAGAGATGTGG
GCAGCTGGTCAGGATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGG
GGAAGCAAACAGGGGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTG
GGAGTTGCTGCAGAGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGA
GATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAGCGCCGGGCCT
TGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCCTACTCCGGGT
CCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGGATCATGGGGC
TGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTCAAGCGGATAT
CAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCCCAAAACTGGCCTCA
TTGACTACAACCAGCTGGCACTGACTGCTCGACTTTTCCGGCCACGGCTCATCATAGCTG
GCACCAGCGCCTATGCTCGCCTCATTGACTACGCCCGCATGAGAGAGGTGTGTGATGAAG
TCAAAGCACACCTGCTGGCAGACATGGCCCACATCAGTGGCCTGGTGGCTGCCAAGGTGA
TTCCCTCGCCTTTCAAGCACGCGGACATCGTCACCACCACTACTCACAAGACTCTTCGAG
GGGCCAGGTCAGGGCTCATCTTCTACCGGAAAGGGGTGAAGGCTGTGGACCCCAAGACTG
GCCGGGAGATCCCTTACACATTTGAGGACCGAATCAACTTTGCCGTGTTCCCATCCCTGC
AGGGGGGCCCCCACAATCATGCCATTGCTGCAGTAGCTGTGGCCCTAAAGCAGGCCTGCA
CCCCCATGTTCCGGGAGTACTCCCTGCAGGTTCTGAAGAATGCTCGGGCCATGGCAGATG
CCCTGCTAGAGCGAGGCTACTCACTGGTATCAGGTGGTACTGACAACCACCTGGTGCTGG
TGGACCTGCGGCCCAAGGGCCTGGATGGAGCTCGGGCTGAGCGGGTGCTAGAGCTTGTAT
CCATCACTGCCAACAAGAACACCTGTCCTGGAGACCGAAGTGCCATCACACCGGGCGGCC
TGCGGCTTGGGGCCCCAGCCTTAACTTCTCGACAGTTCCGTGAGGATGACTTCCGGAGAG
TTGTGGACTTTATAGATGAAGGGGTCAACATTGGCTTAGAGGTGAAGAGCAAGACTGCCA
AGCTCCAGGATTTCAAATCCTTCCTGCTTAAGGACTCAGAAACAAGTCAGCGTCTGGCCA
ACCTCAGGCAACGGGTGGAGCAGTTTGCCAGGGCCTTCCCCATGCCTGGTTTTGATGAGC
ATTGA
|
| Enzyme 17 GenBank Gene ID |
BC091501  |
| Enzyme 17 GeneCard ID |
Q5BJF5  |
| Enzyme 17 GenAtlas ID |
SHMT2  |
| Enzyme 17 HGNC ID |
HGNC:10852  |
| Enzyme 17 Chromosome Location |
12 |
| Enzyme 17 Locus |
12q12-q14 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
14741 |
| Enzyme 18 Name |
Serine hydroxymethyltransferase |
| Enzyme 18 Synonyms |
Not Available |
| Enzyme 18 Gene Name |
SHMT2 |
| Enzyme 18 Protein Sequence |
>Serine hydroxymethyltransferase
MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELL
QREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQ
RRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
KRISATSIFFESMPYKLNLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLA
DMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYT
FEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGY
SLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPA
LTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVE
QFARAFPMPGFDEH
|
| Enzyme 18 Number of Residues |
494 |
| Enzyme 18 Molecular Weight |
54863 |
| Enzyme 18 Theoretical pI |
8.68 |
| Enzyme 18 GO Classification |
| Function |
- catalytic activity
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- glycine metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
| — |
|
| Enzyme 18 General Function |
Amino acid transport and metabolism |
| Enzyme 18 Specific Function |
Interconversion of serine and glycine |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945] ALL_REAC R00945
- (other) R03284
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
21619733  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q8N1A5  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
Q8N1A5_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>1485 bp
ATGCTGTACTTCTCTTTGTTTTGGGCGGCTCGGCCTCTGCAGAGATGTGGGCAGCTGGTC
AGGATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGGGGAAGCAAAC
AGGGGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTGGGAGTTGCTG
CAGAGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGAGAACTTCTGC
AGCCGAGCTGCGCTGGAGGCCCTGGGGTCCTGTCTGAACAACAAGTACTCGGAGGGTTAT
CCTGGCAAGAGATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAG
CGCCGGGCCTTGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCC
TACTCCGGGTCCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGG
ATCATGGGGCTGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTC
AAGCGGATATCAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCTGGCA
CTGACTGCTCGACTTTTCCGGCCACGGCTCATCATAGCTGGCACCAGCGCCTATGCTCGC
CTCATTGACTACGCCCGCATGAGAGAGGTGTGTGATGAAGTCAAAGCACACCTGCTGGCA
GACATGGCCCACATCAGTGGCCTGGTGGCTGCCAAGGTGATTCCCTCGCCTTTCAAGCAC
GCGGACATCGTCACCACCACTACTCACAAGACTCTTCGAGGGGCCAGGTCAGGGCTCATC
TTCTACCGGAAAGGGGTGAAGGCTGTGGACCCCAAGACTGGCCGGGAGATCCCTTACACA
TTTGAGGACCGAATCAACTTTGCCGTGTTCCCATCCCTGCAGGGGGGCCCCCACAATCAT
GCCATTGCTGCAGTAGCTGTGGCCCTAAAGCAGGCCTGCACCCCCATGTTCCGGGAGTAC
TCCCTGCAGGTTCTGAAGAATGCTCGGGCCATGGCAGATGCCCTGCTAGAGCGAGGCTAC
TCACTGGTATCAGGTGGTACTGACAACCACCTGGTGCTGGTGGACCTGCGGCCCAAGGGC
CTGGATGGAGCTCGGGCTGAGCGGGTGCTAGAGCTTGTATCCATCACTGCCAACAAGAAC
ACCTGTCCTGGAGACCGAAGTGCCATCACACCGGGCGGCCTGCGGCTTGGGGCCCCAGCC
TTAACTTCTCGACAGTTCCGTGAGGATGACTTCCGGAGAGTTGTGGACTTTATAGATGAA
GGGGTCAACATTGGCTTAGAGGTGAAGAGCAAGACTGCCAAGCTCCAGGATTTCAAATCC
TTCCTGCTTAAGGACTCAGAAACAAGTCAGCGTCTGGCCAACCTCAGGCAACGGGTGGAG
CAGTTTGCCAGGGCCTTCCCCATGCCTGGTTTTGATGAGCATTGA
|
| Enzyme 18 GenBank Gene ID |
BC032584  |
| Enzyme 18 GeneCard ID |
Q8N1A5  |
| Enzyme 18 GenAtlas ID |
SHMT2  |
| Enzyme 18 HGNC ID |
HGNC:10852  |
| Enzyme 18 Chromosome Location |
12 |
| Enzyme 18 Locus |
12q12-q14 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
14744 |
| Enzyme 19 Name |
Serine hydroxymethyltransferase |
| Enzyme 19 Synonyms |
Not Available |
| Enzyme 19 Gene Name |
SHMT1 |
| Enzyme 19 Protein Sequence |
>Serine hydroxymethyltransferase
MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRA
VLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSG
SPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGY
INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGV
VPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGL
QGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL
VDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQK
VAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASFFPLPGL
PDF
|
| Enzyme 19 Number of Residues |
483 |
| Enzyme 19 Molecular Weight |
53117 |
| Enzyme 19 Theoretical pI |
7.77 |
| Enzyme 19 GO Classification |
| Function |
- catalytic activity
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- glycine metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
| — |
|
| Enzyme 19 General Function |
Amino acid transport and metabolism |
| Enzyme 19 Specific Function |
Interconversion of serine and glycine |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945] ALL_REAC R00945
- (other) R03284
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
14124914  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q96HY0  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
Q96HY0_HUMAN  |
| Enzyme 19 PDB ID |
1BJ4  |
| Enzyme 19 PDB File |
Show |
| Enzyme 19 3D Structure |
|
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>1452 bp
ATGACGATGCCAGTCAACGGGGCCCACAAGGATGCTGACCTGTGGTCCTCACATGACAAG
ATGCTGGCACAACCCCTCAAAGACAGTGATGTTGAGGTTTACAACATCATTAAGAAGGAG
AGTAACCGGCAGAGGGTTGGATTGGAGCTGATTGCCTCGGAGAATTTCGCCAGCCGAGCA
GTTTTGGAGGCCCTAGGCTCTTGCTTAAATAACAAATACTCTGAGGGGTACCCGGGCCAG
AGATACTATGGCGGGACTGAGTTTATTGATGAACTGGAGACCCTCTGTCAGAAGCGAGCC
CTGCAGGCCTATAAGCTGGACCCACAGTGCTGGGGGGTCAACGTCCAGCCCTACTCAGGC
TCCCCTGCAAACTTTGCTGTGTACACTGCCCTGGTGGAACCCCATGGGCGCATCATGGGC
CTGGACCTTCCGGATGGGGGCCACCTGACCCATGGGTTCATGACAGACAAGAAGAAAATC
TCTGCCACGTCCATCTTCTTTGAATCTATGCCCTACAAGGTGAACCCAGATACTGGCTAC
ATCAACTATGACCAGCTGGAGGAGAACGCACGCCTCTTCCACCCGAAGCTGATCATCGCA
GGAACCAGCTGCTACTCCCGAAACCTGGAATATGCCCGGCTACGGAAGATTGCAGATGAG
AACGGGGCGTATCTCATGGCGGACATGGCTCACATCAGCGGGCTGGTGGCGGCTGGCGTG
GTGCCCTCCCCATTTGAACACTGCCATGTGGTGACCACCACCACTCACAAGACCCTGCGA
GGCTGCCGAGCTGGCATGATCTTCTACAGGAAAGGAGTGAAAAGTGTGGATCCCAAGACT
GGCAAAGAGATTCTGTACAACCTGGAGTCTCTTATCAATTCTGCTGTGTTCCCTGGCCTG
CAGGGAGGTCCCCACAACCACGCCATTGCTGGGGTTGCTGTGGCACTGAAGCAAGCTATG
ACTCTGGAATTTAAAGTTTATCAACACCAGGTGGTGGCCAACTGCAGGGCTCTGTCTGAG
GCCCTGACGGAGCTGGGCTACAAAATAGTCACAGGTGGTTCTGACAACCATTTGATCCTT
GTGGATCTCCGTTCCAAAGGCACAGATGGTGGAAGGGCTGAGAAGGTGCTAGAAGCCTGT
TCTATTGCCTGCAACAAGAACACCTGTCCAGGTGACAGAAGCGCTCTGCGGCCCAGTGGA
CTGCGGCTGGGGACCCCAGCACTGACGTCCCGTGGACTTTTGGAAAAAGACTTCCAAAAA
GTAGCCCACTTTATTCACAGAGGGATAGAGCTGACCCTGCAGATCCAGAGCGACACTGGT
GTCAGAGCCACCCTGAAAGAGTTCAAGGAGAGACTGGCAGGGGATAAGTACCAGGCGGCC
GTGCAGGCTCTCCGGGAGGAGGTTGAGAGCTTCGCCTCTTTCTTCCCTCTGCCTGGCCTG
CCTGACTTCTAA
|
| Enzyme 19 GenBank Gene ID |
BC007979  |
| Enzyme 19 GeneCard ID |
Q96HY0  |
| Enzyme 19 GenAtlas ID |
SHMT1  |
| Enzyme 19 HGNC ID |
HGNC:10850  |
| Enzyme 19 Chromosome Location |
17 |
| Enzyme 19 Locus |
17p11.2 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
16443 |
| Enzyme 20 Name |
cDNA, FLJ93186, Homo sapiens seryl-tRNA synthetase (SARS), mRNA (Seryl-tRNA synthetase, isoform CRA_e) |
| Enzyme 20 Synonyms |
Not Available |
| Enzyme 20 Gene Name |
SARS |
| Enzyme 20 Protein Sequence |
>cDNA, FLJ93186, Homo sapiens seryl-tRNA synthetase (SARS), mRNA (Seryl-tRNA synthetase, isoform CRA_e)
MVLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLC
SKTIGEKMKKKEPVGDDESVPENVLSFDDLTADALANLKVSQIKKVRLLIDEAILKCDAE
RIKLEAERFENLREIGNLLHPSVPISNDEDVDNKVERIWGDCTVRKKYSHVDLVVMVDGF
EGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQL
SQFDEELYKVIGKGSEKSDDNSYDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTC
FRQEVGSHGRDTRGIFRVHQFEKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYH
IVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYGQTKKMMDKV
EFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEFMPPGLQELIPFVKPAPIEQEP
SKKQKKQHEGSKKKAAARDVTLENRLQNMEVTDA
|
| Enzyme 20 Number of Residues |
514 |
| Enzyme 20 Molecular Weight |
58778 |
| Enzyme 20 Theoretical pI |
6.38 |
| Enzyme 20 GO Classification |
| Function |
- ATP binding
- RNA ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming phosphoric ester bonds
- nucleotide binding
- purine nucleotide binding
- serine-tRNA ligase activity
- tRNA ligase activity
|
| Process |
- RNA metabolism
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- seryl-tRNA aminoacylation
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolism
|
| Component |
| — |
|
| Enzyme 20 General Function |
Translation, ribosomal structure and biogenesis |
| Enzyme 20 Specific Function |
Not Available |
| Enzyme 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
Not Available |
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
Not Available |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
B2R6Y9  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
B2R6Y9_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
Not Available |
| Enzyme 20 GenBank Gene ID |
AK312771  |
| Enzyme 20 GeneCard ID |
B2R6Y9  |
| Enzyme 20 GenAtlas ID |
Not Available |
| Enzyme 20 HGNC ID |
Not Available |
| Enzyme 20 Chromosome Location |
Not Available |
| Enzyme 20 Locus |
Not Available |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
Not Available |
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
16487 |
| Enzyme 21 Name |
cDNA, FLJ94281, Homo sapiens cystathionine-beta-synthase (CBS), mRNA (Cystathionine-beta-synthase, isoform CRA_b) |
| Enzyme 21 Synonyms |
Not Available |
| Enzyme 21 Gene Name |
CBS |
| Enzyme 21 Protein Sequence |
>cDNA, FLJ94281, Homo sapiens cystathionine-beta-synthase (CBS), mRNA (Cystathionine-beta-synthase, isoform CRA_b)
MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPA
SESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKD
RISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDV
LRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEI
LQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTT
YEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKA
AQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLS
APLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVG
KVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLL
NFVAAQERDQK
|
| Enzyme 21 Number of Residues |
551 |
| Enzyme 21 Molecular Weight |
60587 |
| Enzyme 21 Theoretical pI |
6.63 |
| Enzyme 21 GO Classification |
| Function |
- carbon-oxygen lyase activity
- catalytic activity
- cystathionine beta-synthase activity
- hydro-lyase activity
- lyase activity
|
| Process |
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- cysteine biosynthesis
- cysteine biosynthesis from serine
- cysteine biosynthesis via cystathione
- metabolism
- physiological process
- serine family amino acid metabolism
- sulfur amino acid biosynthesis
- sulfur amino acid metabolism
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 21 General Function |
Amino acid transport and metabolism |
| Enzyme 21 Specific Function |
Not Available |
| Enzyme 21 Pathways |
Not Available |
| Enzyme 21 Reactions |
Not Available |
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
Not Available |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
B2R993  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
B2R993_HUMAN  |
| Enzyme 21 PDB ID |
1JBQ  |
| Enzyme 21 PDB File |
Show |
| Enzyme 21 3D Structure |
|
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
Not Available |
| Enzyme 21 GenBank Gene ID |
AK313691  |
| Enzyme 21 GeneCard ID |
B2R993  |
| Enzyme 21 GenAtlas ID |
Not Available |
| Enzyme 21 HGNC ID |
Not Available |
| Enzyme 21 Chromosome Location |
21 |
| Enzyme 21 Locus |
21q22.3 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
Not Available |
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
16507 |
| Enzyme 22 Name |
cDNA, FLJ96235, Homo sapiens phosphoserine phosphatase (PSPH), mRNA (Phosphoserine phosphatase, isoform CRA_a) |
| Enzyme 22 Synonyms |
Not Available |
| Enzyme 22 Gene Name |
PSPH |
| Enzyme 22 Protein Sequence |
>cDNA, FLJ96235, Homo sapiens phosphoserine phosphatase (PSPH), mRNA (Phosphoserine phosphatase, isoform CRA_a)
MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKA
ALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVA
SKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKIIMIGDG
ATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE
|
| Enzyme 22 Number of Residues |
225 |
| Enzyme 22 Molecular Weight |
25008 |
| Enzyme 22 Theoretical pI |
5.42 |
| Enzyme 22 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
- phosphoserine phosphatase activity
|
| Process |
- L-serine biosynthesis
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
| — |
|
| Enzyme 22 General Function |
Amino acid transport and metabolism |
| Enzyme 22 Specific Function |
Not Available |
| Enzyme 22 Pathways |
Not Available |
| Enzyme 22 Reactions |
Not Available |
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
Not Available |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
B2RCR5  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
B2RCR5_HUMAN  |
| Enzyme 22 PDB ID |
1NNL  |
| Enzyme 22 PDB File |
Show |
| Enzyme 22 3D Structure |
|
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
Not Available |
| Enzyme 22 GenBank Gene ID |
AK315235  |
| Enzyme 22 GeneCard ID |
B2RCR5  |
| Enzyme 22 GenAtlas ID |
Not Available |
| Enzyme 22 HGNC ID |
Not Available |
| Enzyme 22 Chromosome Location |
Not Available |
| Enzyme 22 Locus |
Not Available |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
Not Available |
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
17005 |
| Enzyme 23 Name |
Serine incorporator 1 |
| Enzyme 23 Synonyms |
- Tumor differentially expressed protein 2
- Tumor differentially expressed 1 protein-like
|
| Enzyme 23 Gene Name |
SERINC1 |
| Enzyme 23 Protein Sequence |
>Serine incorporator 1
MGSVLGLCSMASWIPCLCGSAPCLLCRCCPSGNNSTVTRLIYALFLLVGVCVACVMLIPG
MEEQLNKIPGFCENEKGVVPCNILVGYKAVYRLCFGLAMFYLLLSLLMIKVKSSSDPRAA
VHNGFWFFKFAAAIAIIIGAFFIPEGTFTTVWFYVGMAGAFCFILIQLVLLIDFAHSWNE
SWVEKMEEGNSRCWYAALLSATALNYLLSLVAIVLFFVYYTHPASCSENKAFISVNMLLC
VGASVMSILPKIQESQPRSGLLQSSVITVYTMYLTWSAMTNEPETNCNPSLLSIIGYNTT
STVPKEGQSVQWWHAQGIIGLILFLLCVFYSSIRTSNNSQVNKLTLTSDESTLIEDGGAR
SDGSLEDGDDVHRAVDNERDGVTYSYSFFHFMLFLASLYIMMTLTNWYRYEPSREMKSQW
TAVWVKISSSWIGIVLYVWTLVAPLVLTNRDFD
|
| Enzyme 23 Number of Residues |
453 |
| Enzyme 23 Molecular Weight |
50495 |
| Enzyme 23 Theoretical pI |
5.65 |
| Enzyme 23 GO Classification |
| Function |
| — |
| Process |
| — |
| Component |
|
|
| Enzyme 23 General Function |
Not Available |
| Enzyme 23 Specific Function |
Enhances the incorporation of serine into phosphatidylserine and sphingolipids |
| Enzyme 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
Not Available |
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
- 89-109
124-144
152-172
198-218
232-252
260-280
310-330
388-408
427-447
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
Not Available |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q9NRX5  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
SERC1_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
Not Available |
| Enzyme 23 GenBank Gene ID |
AF087902  |
| Enzyme 23 GeneCard ID |
Q9NRX5  |
| Enzyme 23 GenAtlas ID |
SERINC1  |
| Enzyme 23 HGNC ID |
HGNC:13464  |
| Enzyme 23 Chromosome Location |
Not Available |
| Enzyme 23 Locus |
Not Available |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [PubMed
]
- Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
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| Enzyme 23 Metabolite References |
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