|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5329 |
| Enzyme 1 Name |
Tartrate-resistant acid phosphatase type 5 precursor |
| Enzyme 1 Synonyms |
- TR- AP
- Tartrate-resistant acid ATPase
- TrATPase
- Acid phosphatase 5, tartrate resistant
|
| Enzyme 1 Gene Name |
ACP5 |
| Enzyme 1 Protein Sequence |
>Tartrate-resistant acid phosphatase type 5 precursor
MDMWTALLILQALLLPSLADGATPALRFVAVGDWGGVPNAPFHTAREMANAKEIARTVQI
LGADFILSLGDNFYFTGVQDINDKRFQETFEDVFSDRSLRKVPWYVLAGNHDHLGNVSAQ
IAYSKISKRWNFPSPFYRLHFKIPQTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKL
ARTQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYGVTAYLCGH
DHNLQYLQDENGVGYVLSGAGNFMDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSK
EMTVTYIEASGKSLFKTRLPRRARP
|
| Enzyme 1 Number of Residues |
325 |
| Enzyme 1 Molecular Weight |
36599 |
| Enzyme 1 Theoretical pI |
8.95 |
| Enzyme 1 GO Classification |
| Function |
- acid phosphatase activity
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- iron ion binding
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
- transition metal ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 1 General Function |
Not Available |
| Enzyme 1 Specific Function |
A phosphate monoester + H(2)O = an alcohol + phosphate |
| Enzyme 1 Pathways |
- gamma-Hexachlorocyclohexane Degradation (map00361
)
- Riboflavin Metabolism (map00740
)
|
| Enzyme 1 Reactions |
- A phosphate monoester + H2O = an alcohol + phosphate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
Not Available |
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
178006  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P13686  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
PPA5_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>972 bp
ATGGACATGTGGACGGCGCTGCTCATCCTGCAAGCCTTGTTGCTACCCTCCCTGGCTGAT
GGTGCCACCCCTGCCCTGCGCTTTGTAGCCGTGGGTGACTGGGGAGGGGTCCCCAATGCC
CCATTCCACACGGGCCCGGAAATGGCCAATGCCAAGGAGATCGCTCGGACTGTGCAGATC
CTGGGTGCAGACTTCATCCTGTCTCTAGGGGACAATTTTTACTTCACTGGTGTGCAAGAC
ATCAATGACAAGAGGTTCCAGGAGACCTTTGAGGACGTATTCTCTGACCGCTCCCTTCGC
AAAGTGCCCTGGTACGTGCTAGCCGGAAACCATGACCACCTTGGCAATGTCTCTGCCCAG
ATTGCATACTCTAAGATCTCCAAGCGCTGGAACTTCCCCAGCCCTTTCTACCGCCTGCAC
TTCAAGATCCCACAGACCAATGTGTCTGTGGCCATTTTTATGCTGGACACAGTGACACTA
TGTGGCAACTCAGATGACTTCCTCAGCCAGCAGCCTGAGAGGCCCCGACTAACTGCCCGC
ACACAGCTGTCCTGGCTCAAGAAACAGCTGGCGGCGGCCAGGGAGGACTACGTGCTGGTG
GCTGGCCACTACCCCGTGTGGTCCATAGCCGAGCACGGGCCTACCCACTGCCTGGTCAAG
CAGCTACGGCCACTGCTGGCCACATACGGGGTCACTGCCTACCTGTGCGGCCACGATCAC
AATCTGCAGTACCTGCAAGATGAGAATGGCGTGGGCTACGTGCTGAGTGGGGCTGGGAAT
TTCATGGACCCCTCAAAGCGGCACCAGCGCAAGGTCCCCAACGGCTATCTGCGCTTCCAC
TATGGGACTGAAGACTCACTGGGTGGCTTTGCCTATGTGGAGATCAGCTCCAAAGAGATG
ACTGTCACTTACATCGAGGCCTCGGGCAAGTCCCTCTTTAAGACCAGGCTGCCGAGGCGA
GCCAGGCCCTGA
|
| Enzyme 1 GenBank Gene ID |
J04430  |
| Enzyme 1 GeneCard ID |
ACP5  |
| Enzyme 1 GenAtlas ID |
ACP5  |
| Enzyme 1 HGNC ID |
HGNC:124  |
| Enzyme 1 Chromosome Location |
19 |
| Enzyme 1 Locus |
19p13.3-p13.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Ketcham CM, Roberts RM, Simmen RC, Nick HS: Molecular cloning of the type 5, iron-containing, tartrate-resistant acid phosphatase from human placenta. J Biol Chem. 1989 Jan 5;264(1):557-63. [PubMed
]
- Lord DK, Cross NC, Bevilacqua MA, Rider SH, Gorman PA, Groves AV, Moss DW, Sheer D, Cox TM: Type 5 acid phosphatase. Sequence, expression and chromosomal localization of a differentiation-associated protein of the human macrophage. Eur J Biochem. 1990 Apr 30;189(2):287-93. [PubMed
]
- Cassady AI, King AG, Cross NC, Hume DA: Isolation and characterization of the genes encoding mouse and human type-5 acid phosphatase. Gene. 1993 Aug 25;130(2):201-7. [PubMed
]
- Stepan JJ, Lau KH, Mohan S, Kraenzlin M, Baylink DJ: Purification and N-terminal sequence of two tartrate-resistant acid phosphatases type-5 from the hairy cell leukemia spleen. Biochem Biophys Res Commun. 1989 Dec 29;165(3):1027-34. [PubMed
]
- Stepan JJ, Lau KH, Mohan S, Singer FR, Baylink DJ: Purification and N-terminal amino acid sequence of the tartrate-resistant acid phosphatase from human osteoclastoma: evidence for a single structure. Biochem Biophys Res Commun. 1990 Apr 30;168(2):792-800. [PubMed
]
- Hayman AR, Warburton MJ, Pringle JA, Coles B, Chambers TJ: Purification and characterization of a tartrate-resistant acid phosphatase from human osteoclastomas. Biochem J. 1989 Jul 15;261(2):601-9. [PubMed
]
- Hayman AR, Dryden AJ, Chambers TJ, Warburton MJ: Tartrate-resistant acid phosphatase from human osteoclastomas is translated as a single polypeptide. Biochem J. 1991 Aug 1;277 ( Pt 3):631-4. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5330 |
| Enzyme 2 Name |
Prostatic acid phosphatase precursor |
| Enzyme 2 Synonyms |
Not Available |
| Enzyme 2 Gene Name |
ACPP |
| Enzyme 2 Protein Sequence |
>Prostatic acid phosphatase precursor
MRAAPLLLARAASLSLGFLFLLFFWLDRSVLAKELKFVTLVFRHGDRSPIDTFPTDPIKE
SSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNL
AALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKR
LHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSE
LSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMAL
DVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELV
GPVIPQDWSTECMTTNSHQGTEDSTD
|
| Enzyme 2 Number of Residues |
386 |
| Enzyme 2 Molecular Weight |
44567 |
| Enzyme 2 Theoretical pI |
6.19 |
| Enzyme 2 GO Classification |
| Function |
- acid phosphatase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
A phosphate monoester + H(2)O = an alcohol + phosphate |
| Enzyme 2 Pathways |
- gamma-Hexachlorocyclohexane Degradation (map00361
)
- Riboflavin Metabolism (map00740
)
|
| Enzyme 2 Reactions |
- A phosphate monoester + H2O = an alcohol + phosphate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
Not Available |
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
189613  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P15309  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PPAP_HUMAN  |
| Enzyme 2 PDB ID |
1ND6  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1161 bp
ATGAGAGCTGCACCCCTCCTCCTGGCCAGGGCAGCAAGCCTTAGCCTTGGCTTCTTGTTT
CTGCTTTTTTTCTGGCTAGACCGAAGTGTACTAGCCAAGGAGTTGAAGTTTGTGACTTTG
GTGTTTCGGCATGGAGACCGAAGTCCCATTGACACCTTTCCCACTGACCCCATAAAGGAA
TCCTCATGGCCACAAGGATTTGGCCAACTCACCCAGCTGGGCATGGAGCAGCATTATGAA
CTTGGAGAGTATATAAGAAAGAGATATAGAAAATTCTTGAATGAGTCCTATAAACATGAA
CAGGTTTATATTCGAAGCACAGACGTTGACCGGACTTTGATGAGTGCTATGACAAACCTG
GCAGCCCTGTTTCCCCCAGAAGGTGTCAGCATCTGGAATCCTATCCTACTCTGGCAGCCC
ATCCCGGTGCACACAGTTCCTCTTTCTGAAGATCAGTTGCTATACCTGCCTTTCAGGAAC
TGCCCTCGTTTTCAAGAACTTGAGAGTGAGACTTTGAAATCAGAGGAATTCCAGAAGAGG
CTGCACCCTTATAAGGATTTTATAGCTACCTTGGGAAAACTTTCAGGATTACATGGCCAG
GACCTTTTTGGAATTTGGAGTAAAGTCTACGACCCTTTATATTGTGAGAGTGTTCACAAT
TTCACTTTACCCTCCTGGGCCACTGAGGACACCATGACTAAGTTGAGAGAATTGTCAGAA
TTGTCCCTCCTGTCCCTCTATGGAATTCACAAGCAGAAAGAGAAATCTAGGCTCCAAGGG
GGTGTCCTGGTCAATGAAATCCTCAATCACATGAAGAGAGCAACTCAGATACCAAGCTAC
AAAAAACTTATCATGTATTCTGCGCATGACACTACTGTGAGTGGCCTACAGATGGCGCTA
GATGTTTACAACGGACTCCTTCCTCCCTATGCTTCTTGCCACTTGACGGAATTGTACTTT
GAGAAGGGGGAGTACTTTGTGGAGATGTACTACCGGAATGAGACGCAGCACGAGCCGTAT
CCCCTCATGCTACCTGGCTGCAGCCCCAGCTGTCCTCTGGAGAGGTTTGCTGAGCTGGTT
GGCCCTGTGATCCCTCAAGACTGGTCCACGGAGTGTATGACCACAAACAGCCATCAAGGT
ACTGAGGACAGTACAGATTAG
|
| Enzyme 2 GenBank Gene ID |
M97589  |
| Enzyme 2 GeneCard ID |
ACPP  |
| Enzyme 2 GenAtlas ID |
ACPP  |
| Enzyme 2 HGNC ID |
HGNC:125  |
| Enzyme 2 Chromosome Location |
3 |
| Enzyme 2 Locus |
3q21-q23 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Sharief FS, Li SS: Structure of human prostatic acid phosphatase gene. Biochem Biophys Res Commun. 1992 May 15;184(3):1468-76. [PubMed
]
- Van Etten RL, Davidson R, Stevis PE, MacArthur H, Moore DL: Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase. J Biol Chem. 1991 Feb 5;266(4):2313-9. [PubMed
]
- Sharief FS, Lee H, Leuderman MM, Lundwall A, Deaven LL, Lee CL, Li SS: Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein sequence homology with lysosomal acid phosphatase. Biochem Biophys Res Commun. 1989 Apr 14;160(1):79-86. [PubMed
]
- Vihko P, Virkkunen P, Henttu P, Roiko K, Solin T, Huhtala ML: Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase. FEBS Lett. 1988 Aug 29;236(2):275-81. [PubMed
]
- Tailor PG, Govindan MV, Patel PC: Nucleotide sequence of human prostatic acid phosphatase determined from a full-length cDNA clone. Nucleic Acids Res. 1990 Aug 25;18(16):4928. [PubMed
]
- Sharief FS, Li SS: Nucleotide sequence of human prostatic acid phosphatase ACPP gene, including seven Alu repeats. Biochem Mol Biol Int. 1994 Jun;33(3):561-5. [PubMed
]
- LaCount MW, Handy G, Lebioda L: Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase. J Biol Chem. 1998 Nov 13;273(46):30406-9. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5351 |
| Enzyme 3 Name |
Ectonucleotide pyrophosphatase/phosphodiesterase family member 1 |
| Enzyme 3 Synonyms |
- E- NPP 1
- Phosphodiesterase I/nucleotide pyrophosphatase 1
- Plasma-cell membrane glycoprotein PC-1[Includes: Alkaline phosphodiesterase I
- NPPase]
|
| Enzyme 3 Gene Name |
ENPP1 |
| Enzyme 3 Protein Sequence |
>Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED
|
| Enzyme 3 Number of Residues |
925 |
| Enzyme 3 Molecular Weight |
104925 |
| Enzyme 3 Theoretical pI |
7.14 |
| Enzyme 3 GO Classification |
| Function |
- binding
- catalytic activity
- endonuclease activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- nuclease activity
- nucleic acid binding
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 Specific Function |
Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity |
| Enzyme 3 Pathways |
- Nicotinate and Nicotinamide Metabolism (map00760
)
- Pantothenate and CoA Biosynthesis (map00770
)
- Purine Metabolism (map00230
)
- Riboflavin Metabolism (map00740
)
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 3 Reactions |
- A dinucleotide + H2O = 2 mononucleotides
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
189650  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P22413  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
ENPP1_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>2622 bp
ATGGACGTGGGGGAGGAGCCGCTGGAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCC
AACACCTATAAAGTACTCTCGCTGGTATTGTCAGTATGTGTGTTAACAACAATACTTGGT
TGTATATTTGGGTTGAAACCAAGCTGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGT
TTCGAGAGAACATTTGGGAACTGTCGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGC
TGTTTAGATTACCAGGAGACGTGCATAGAACCAGAACATATATGGACTTGCAACAAATTC
AGGTGTGGTGAGAAAAGGTTGACCAGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGAC
AAGGGCGACTGCTGCATCAACTACAGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAA
GAACCATGTGAGAGCATTAATGAGCCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACC
CTCTTATTTTCTTTGGATGGATTCAGGGCAGAATATTTACACACTTGGGGTGGACTTCTT
CCTGTTATTAGCAAACTAAAAAAATGTGGAACATATACTAAAAACATGAGACCGGTATAT
CCAACAAAAACTTTCCCCAATCACTACAGCATTGTCACCGGATTGTATCCAGAATCTCAT
GGCATAATCGACAATAAAATGTATGATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGT
AAAGAGAAATTTAATCCTGAGTGGTACAAAGGAGAACCAATTTGGGTCACAGCTAAGTAT
CAAGGCCTCAAGTCTGGCACATTTTTCTGGCCAGGATCAGATGTGGAAATTAACGGAATT
TTCCCAGACATCTATAAAATGTATAATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCT
GTTCTTCAGTGGCTACAGCTTCCTAAAGATGAAAGACCACACTTTTACACTCTGTATTTA
GAAGAACCAGATTCTTCAGGTCATTCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCC
TTGCAGAGGGTTGATGGTATGGTTGGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTG
CACAGATGCCTGAACCTCATCCTTATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAG
AAATACATATATCTGAATAAATATTTGGGGGATGTTAAAAATATTAAAGTTATCTATGGA
CCTGCAGCTCGATTGAGACCCTCTGATGTCCCAGATAAATACTATTCATTTAACTATGAA
GGCATTGCCCGAAATCTTTCTTGCCGGGAACCAAACCAGCACTTCAAACCTTACCTGAAA
CATTTCTTACCTAAGCGTTTGCACTTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTC
TATTTGGACCCTCAGTGGCAACTTGCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGT
GGATTTCATGGCTCTGACAATGTATTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGA
CCTGGATTCAAGCATGGCATTGAGGCTGACACCTTTGAAAACATTGAAGTCTATAACTTA
ATGTGTGATTTACTGAATTTGACACCGGCTCCTAATAACGGAACTCATGGAAGTCTTAAC
CACCTTCTAAAGAATCCTGTTTATACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTA
CAGTGCCCCTTCACAAGAAACCCCAGAGATAACCTTGGCTGCTCATGTAACCCTTCGATT
TTGCCGATTGAGGATTTTCAAACACAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATT
AAGCATGAAACTTTACCCTATGGAAGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGT
CTTCTTTCCCAGCACCAGTTTATGAGTGGATACAGCCAAGACATCTTAATGCCCCTTTGG
ACATCCTATACCGTGGACAGAAATGACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTG
TACCAGGACTTTAGAATTCCTCTTAGTCCTGTCCATAAATGTTCATTTTATAAAAATAAC
ACCAAAGTGAGTTACGGGTTCCTCTCCCCACCACAACTAAATAAAAATTCAAGTGGAATA
TATTCTGAAGCTTTGCTTACTACAAATATAGTGCCAATGTACCAGAGTTTTCAAGTTATA
TGGCGCTACTTTCATGACACCCTACTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAAT
GTCGTCAGTGGTCCTGTGTTTGACTTTGATTATGATGGACGTTGTGATTCCTTAGAGAAT
CTGAGGCAAAAAAGAAGAGTCATCCGTAACCAAGAAATTTTGATTCCAACTCACTTCTTT
ATTGTGCTAACAAGCTGTAAAGATACATCTCAGACGCCTTTGCACTGTGAAAACCTAGAC
ACCTTAGCTTTCATTTTGCCTCACAGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAG
CATGACTCCTCATGGGTTGAAGAATTGTTAATGTTACACAGAGCACGGATCACAGATGTT
GAGCACATCACTGGACTCAGCTTCTATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTA
AAGTTGAAAACACATTTGCCAACCTTTAGCCAAGAAGACTGA
|
| Enzyme 3 GenBank Gene ID |
M57736  |
| Enzyme 3 GeneCard ID |
ENPP1  |
| Enzyme 3 GenAtlas ID |
ENPP1  |
| Enzyme 3 HGNC ID |
HGNC:3356  |
| Enzyme 3 Chromosome Location |
6 |
| Enzyme 3 Locus |
6q22-q23 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed
]
- Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed
]
- Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed
]
- Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed
]
- Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed
]
- Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5367 |
| Enzyme 4 Name |
Lathosterol oxidase |
| Enzyme 4 Synonyms |
- Lathosterol 5-desaturase
- Delta(7-sterol 5-desaturase
- C-5 sterol desaturase
- Sterol-C5- desaturase
|
| Enzyme 4 Gene Name |
SC5DL |
| Enzyme 4 Protein Sequence |
>Lathosterol oxidase
MDLVLRVADYYFFTPYVYPATWPEDDIFRQAISLLIVTNVGAYILYFFCATLSYYFVFDH
ALMKHPQFLKNQVRREIKFTVQALPWISILTVALFLLEIRGYSKLHDDLGEFPYGLFELV
VSIISFLFFTDMFIYWIHRGLHHRLVYKRLHKPHHIWKIPTPFASHAFHPIDGFLQSLPY
HIYPFIFPLHKVVYLSLYILVNIWTISIHDGDFRVPQILQPFINGSAHHTDHHMFFDYNY
GQYFTLWDRIGGSFKNPSSFEGKGPLSYVKEMTEGKRSSHSGNGCKNEKLFNGEFTKTE
|
| Enzyme 4 Number of Residues |
299 |
| Enzyme 4 Molecular Weight |
35301 |
| Enzyme 4 Theoretical pI |
8.24 |
| Enzyme 4 GO Classification |
| Function |
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Lipid transport and metabolism |
| Enzyme 4 Specific Function |
Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
- 32-52
79-99
117-137
186-206
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
1906796  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
O75845  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
SC5D_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>711 bp
ATGGATCTTGTACTCCGTGTTGCAGATTACTATTTTTTTACACCATACGTGTATCCAGCC
ACATGGCCAGAAGATGACATCTTCCGACAAGCTATTAGTCTTCTGATTGTAACAAATGTT
GGTGCTTACATCCTTTATTTCTTCTGTGCAACACTGAGCTATTATTTTGTCTTCGATCAT
GCATTAATGAAACATCCACAATTTTTAAAGAATCAAGTCCGTCGAGAGATTAAGTTTACT
GTCCAGGCATTGCCATGGATAAGTATTCTTACTGTTGCACTGTTCTTGCTGGAGATAAGA
GGTTACAGCAAATTACATGATGACCTAGGAGAGTTTCCATATGGATTGTTTGAACTTGTC
GTTAGTATAATATCTTTCCTCTTTTTCACTGACATGTTCATCTACTGGATTCACAGAGGC
CTTCATCATAGACTGGTATATAAGCGCCTACATAAACCTCACCATATTTGGAAGATTCCT
ACTCCATTTGCAAGTCATGCTTTTCACCCTATTGATGGCTTTCTTCAGAGTCTACCTTAC
CATATATACCCTTTTATCTTTCCATTACACAAGGTGGTTTATTTAAGTCTGTACATCTTG
GTTAATATCTGGACAATTTCCATTCATGACGGTGATTTTCGTGTAAGAATGAAAAATTAT
TCAATGGAGAGTTTACAAAGACTGAATAGATTATTGCCCAGTTATTCTTAA
|
| Enzyme 4 GenBank Gene ID |
D85181  |
| Enzyme 4 GeneCard ID |
SC5DL  |
| Enzyme 4 GenAtlas ID |
SC5DL  |
| Enzyme 4 HGNC ID |
HGNC:10547  |
| Enzyme 4 Chromosome Location |
11 |
| Enzyme 4 Locus |
11q23.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Matsushima M, Inazawa J, Takahashi E, Suzumori K, Nakamura Y: Molecular cloning and mapping of a human cDNA (SC5DL) encoding a protein homologous to fungal sterol-C5-desaturase. Cytogenet Cell Genet. 1996;74(4):252-4. [PubMed
]
- Husselstein T, Schaller H, Gachotte D, Benveniste P: Delta7-sterol-C5-desaturase: molecular characterization and functional expression of wild-type and mutant alleles. Plant Mol Biol. 1999 Mar;39(5):891-906. [PubMed
]
- Nishi S, Nishino H, Ishibashi T: cDNA cloning of the mammalian sterol C5-desaturase and the expression in yeast mutant. Biochim Biophys Acta. 2000 Jan 31;1490(1-2):106-8. [PubMed
]
- Brunetti-Pierri N, Corso G, Rossi M, Ferrari P, Balli F, Rivasi F, Annunziata I, Ballabio A, Russo AD, Andria G, Parenti G: Lathosterolosis, a novel multiple-malformation/mental retardation syndrome due to deficiency of 3beta-hydroxysteroid-delta5-desaturase. Am J Hum Genet. 2002 Oct;71(4):952-8. Epub 2002 Aug 20. [PubMed
]
- Krakowiak PA, Wassif CA, Kratz L, Cozma D, Kovarova M, Harris G, Grinberg A, Yang Y, Hunter AG, Tsokos M, Kelley RI, Porter FD: Lathosterolosis: an inborn error of human and murine cholesterol synthesis due to lathosterol 5-desaturase deficiency. Hum Mol Genet. 2003 Jul 1;12(13):1631-41. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5415 |
| Enzyme 5 Name |
NADPH--cytochrome P450 reductase |
| Enzyme 5 Synonyms |
- CPR
- P450R
|
| Enzyme 5 Gene Name |
POR |
| Enzyme 5 Protein Sequence |
>NADPH--cytochrome P450 reductase
MGDSHVDTSSTVSEAVAEEVSLFSMTDMILFSLIVGLLTYWFLFRKKKEEVPEFTKIQTL
TSSVRESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLA
DLSSLPEIDNALVVFCMATYGEGDPTDNAQDFYDWLQETDVDLSGVKFAVFGLGNKTYEH
FNAMGKYVDKRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEHFGVEATGEES
SIRQYELVVHTDIDAAKVYMGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHL
MHLELDISDSKIRYESGDHVAVYPANDSALVNQLGKILGADLDVVMSLNNLDEESNKKHP
FPCPTSYRTALTYYLDITNPPRTNVLYELAQYASEPSEQELLRKMASSSGEGKELYLSWV
VEARRHILAILQDCPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVVVEYET
KAGRINKGVATNWLRAKEPAGENGGRALVPMFVRKSQFRLPFKATTPVIMVGPGTGVAPF
IGFIQERAWLRQQGKEVGETLLYYGCRRSDEDYLYREELAQFHRDGALTQLNVAFSREQS
HKVYVQHLLKQDREHLWKLIEGGAHIYVCGDARNMARDVQNTFYDIVAELGAMEHAQAVD
YIKKLMTKGRYSLDVWS
|
| Enzyme 5 Number of Residues |
677 |
| Enzyme 5 Molecular Weight |
76691 |
| Enzyme 5 Theoretical pI |
5.28 |
| Enzyme 5 GO Classification |
| Function |
- FMN binding
- binding
- catalytic activity
- electron transporter activity
- nucleotide binding
- oxidoreductase activity
- transporter activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Inorganic ion transport and metabolism |
| Enzyme 5 Specific Function |
This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5 |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
- NADPH + H+ + n oxidized hemoprotein = NADP+ + n reduced hemoprotein
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
Not Available |
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
247307  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P16435  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
NCPR_HUMAN  |
| Enzyme 5 PDB ID |
1AMO  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>2031 bp
GGAGACTCCCACGTGGACACCAGCTCCACCGTGTCCGAGGCGGTGGCCGAAGAAGTATCT
CTTTTCAGCATGACGGACATGATTCTGTTTTCGCTCATCGTGGGTCTCCTAACCTACTGG
TTCCTCTTCAGAAAGAAAAAAGAAGAAGTCCCCGAGTTCACCAAAATTCAGACATTGACC
TCCTCTGTCAGAGAGAGCAGCTTTGTGGAAAAGATGAAGAAAACGGGGAGGAACATCATC
GTGTTCTACGGCTCCCAGACGGGGACTGCAGAGGAGTTTGCCAACCGCCTGTCCAAGGAC
GCCCACCGCTACGGGATGCGAGGCATGTCAGCGGACCCTGAGGAGTATGACCTGGCCGAC
CTGAGCAGCCTGCCAGAGATCGACAACGCCCTGGTGGTTTTCTGCATGGCCACCTACGGT
GAGGGAGACCCCACCGACAATGCCCAGGACTTCTACGACTGGCTGCAGGAGACAGACGTG
GATCTCTCTGGGGTCAAGTTCGCGGTGTTTGGTCTTGGGAACAAGACCTACGAGCACTTC
AATGCCATGGGCAAGTACGTGGACAAGCGGCTGGAGCAGCTCGGCGCCCAGCGCATCTTT
GAGCTGGGGTTGGGCGACGACGATGGGAACTTGGAGGAGGACTTCATCACCTGGCGAGAG
CAGTTCTGGCCGGCCGTGTGTGAACACTTTGGGGTGGAAGCCACTGGCGAGGAGTCCAGC
ATTCGCCAGTACGAGCTTGTGGTCCACACCGACATAGATGCGGCCAAGGTGTACATGGGG
GAGATGGGCCGGCTGAAGAGCTACGAGAACCAGAAGCCCCCCTTTGATGCCAAGAATCCG
TTCCTGGCTGCAGTCACCACCAACCGGAAGCTGAACCAGGGAACCGAGCGCCACCTCATG
CACCTGGAATTGGACATCTCGGACTCCAAAATCAGGTATGAATCTGGGGACCACGTGGCT
GTGTACCCAGCCAACGACTCTGCTCTCGTCAACCAGCTGGGCAAAATCCTGGGTGCCGAC
CTGGACGTCGTCATGTCCCTGAACAACCTGGATGAGGAGTCCAACAAGAAGCACCCATTC
CCGTGCCCTACGTCCTACCGCACGGCCCTCACCTACTACCTGGACATCACCAACCCGCCG
CGTACCAACGTGCTGTACGAGCTGGCGCAGTACGCCTCGGAGCCCTCGGAGCAGGAGCTG
CTGCGCAAGATGGCCTCCTCCTCCGGCGAGGGCAAGGAGCTGTACCTGAGCTGGGTGGTG
GAGGCCCGGAGGCACATCCTGGCCATCCTGCAGGACTGCCCGTCCCTGCGGCCCCCCATC
GACCACCTGTGTGAGCTGCTGCCGCGCCTGCAGGCCCGCTACTACTCCATCGCCTCATCC
TCCAAGGTCCACCCCAACTCTGTGCACATCTGTGCGGTGGTTGTGGAGTACGAGACCAAG
GCCGGCCGCATCAACAAGGGCGTGGCCACCAACTGGCTGCGGGCCAAGGAGCCTGTCGGG
GAGAACGGCGGCCGTGCGCTGGTGCCCATGTTCGTGCGCAAGTCCCAGTTACGCCTGCCC
TTCAAGGCCACCACGCCTGTCATCATGGTGGGCCCCGGCACCGGGTGGCACCCTTTCATA
GGCTTCATCCAGGAGCGGGCCTGGCTGCGACAGCAGGGCAAGGAGGTGGGGGAGACGCTG
CTGTACTACGGCTGCCGCCGCTCGGATGAGGACTACCTGTACCGGGAGGAGCTGGCGCAG
TTCCACAGGGACGGTGCGCTCACCCAGCTCAACGTGGCCTTCTCCCGGGAGCAGTCCCAC
AAGGTCTACGTCCAGCACCTGCTAAAGCAAGACCGAGAGCACCTGTGGAAGTTGATCGAA
GGCGGTGCCCACATCTACGTCTGTGGGGATGCACGGAACATGGCCAGGGATGTGCAGAAC
ACCTTCTACGACATCGTGGCTGAGCTCGGGGCCATGGAGCACGCGCAGGCGGTGGACTAC
ATCAAGAAACTGATGACCAAGGGCCGCTACTCCCTGGACGTGTGGAGCTAG
|
| Enzyme 5 GenBank Gene ID |
S90469  |
| Enzyme 5 GeneCard ID |
POR  |
| Enzyme 5 GenAtlas ID |
POR  |
| Enzyme 5 HGNC ID |
HGNC:9208  |
| Enzyme 5 Chromosome Location |
7 |
| Enzyme 5 Locus |
7q11.2 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Shephard EA, Palmer CN, Segall HJ, Phillips IR: Quantification of cytochrome P450 reductase gene expression in human tissues. Arch Biochem Biophys. 1992 Apr;294(1):168-72. [PubMed
]
- Haniu M, McManus ME, Birkett DJ, Lee TD, Shively JE: Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: complete sequence of human enzyme and NADPH-binding sites. Biochemistry. 1989 Oct 17;28(21):8639-45. [PubMed
]
- Zhao Q, Modi S, Smith G, Paine M, McDonagh PD, Wolf CR, Tew D, Lian LY, Roberts GC, Driessen HP: Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution. Protein Sci. 1999 Feb;8(2):298-306. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5416 |
| Enzyme 6 Name |
Dihydroorotate dehydrogenase, mitochondrial precursor |
| Enzyme 6 Synonyms |
- Dihydroorotate oxidase
- DHOdehase
|
| Enzyme 6 Gene Name |
DHODH |
| Enzyme 6 Protein Sequence |
>Dihydroorotate dehydrogenase, mitochondrial precursor
MAWRHLKKRAQDAVIILGGGGLLFASYLMATGDERFYAEHLMPTLQGLLDPESAHRLAVR
FTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSV
TPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVN
LGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQER
DGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSET
GGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTF
WGPPVVGKVKRELEALLKEQGFGGVTDAIGADHRR
|
| Enzyme 6 Number of Residues |
395 |
| Enzyme 6 Molecular Weight |
42868 |
| Enzyme 6 Theoretical pI |
10.23 |
| Enzyme 6 GO Classification |
| Function |
- catalytic activity
- dihydroorotate dehydrogenase activity
- dihydroorotate oxidase activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
|
| Process |
- 'de novo' pyrimidine base biosynthesis
- UMP biosynthesis
- cellular metabolism
- metabolism
- nucleobase metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
- pyrimidine base biosynthesis
- pyrimidine base metabolism
- pyrimidine nucleoside monophosphate biosynthesis
- pyrimidine nucleotide biosynthesis
- pyrimidine nucleotide metabolism
- pyrimidine ribonucleoside monophosphate biosynthesis
|
| Component |
|
|
| Enzyme 6 General Function |
Nucleotide transport and metabolism |
| Enzyme 6 Specific Function |
(S)-dihydroorotate + O(2) = orotate + H(2)O(2) |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- (S)-dihydroorotate + O2 = orotate + H2O2
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
Not Available |
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
555594  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q02127  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
PYRD_HUMAN  |
| Enzyme 6 PDB ID |
1D3H  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1191 bp
AAATTACCGTGGAGACACCTGCAAAAGCGGGCCCAGGATGCTGTGATCATCCTGGGGGGA
GGAGGACTTCTCTTCGCCTCCTACCTGATGGCCACGGGAGATGAGCGTTTCTATGCTGAA
CACCTGATGCCGACTCTGCAGGGGCTGCTGGACCCGGAGTCAGCCCACAGACTGGCTGTT
CGCTTCACCTCCCTGGGGCTCCTTCCACGGGCCAGATTTCAAGACTCTGACATGCTGGAA
GTGAGAGTTCTGGGCCATAAATTCCGAAATCCAGTAGGAATTGCTGCAGGATTTGACAAG
CATGGGGAAGCCGTGGACGGACTTTATAAGATGGGCTTTGGTTTTGTTGAGATAGGAAGT
GTGACTCCAAAACCTCAGGAAGGAAACCCTAGACCCAGAGTCTTCCGCCTCCCTGAGGAC
CAAGCTGTCATTAACAGGTATGGATTTAACAGTCACGGGCTTTCAGTGGTGGAACACAGG
TTACGGGCCAGACAGCAGAAGCAGGCCAAGCTCACAGAAGATGGACTGCCTCTGGGGGTC
AACTTGGGGAAGAACAAGACCTCAGTGGACGCCGCGGAGGACTACGCAGAAGGGGTGCGC
GTACTGGGCCCCCTGGCCGACTACCTGGTGGTGAATGTGTCCAGCCCCAACACTGCCGGG
CTGCGGAGCCTTCAGGGAAAGGCCGAGCTGCGCCGCCTGCTGACCAAGGTGCTGCAGGAG
AGGGATGGCTTGCGGAGAGTGCACAGGCCGGCAGTCCTGGTGAAGATCGCTCCTGACCTC
ACCAGCCAGGATAAGGAGGACATTGCCAGTGTGGTCAAAGAGTTGGGCATCGATGGGCTG
ATTGTTACGAACACCACCGTGAGTCGCCCTGCGGGCCTCCAGGGTGCCCTGCGCTCTGAA
ACAGGAGGGCTGAGTGGGAAGCCCCTCCGGGATTTATCAACTCAAACCATTCGGGAGATG
TATGCACTCACCCAAGGCCGAGTTCCCATAATTGGGGTTGGTGGTGTGAGCAGCGGGCAG
GACGCGCTGGAGAAGATCCGGGCAGGGGCCTCCCTGGTGCAGCTGTACACGGCCCTCACC
TTCTGGGGGCCACCCGTTGTGGGCAAAGTCAAGCGGGAACTGGAGGCCCTTCTGAAAGAG
CAGGGCTTTGGCGGAGTCACAGATGCCATTGGAGCAGATCATCGGAGGTGA
|
| Enzyme 6 GenBank Gene ID |
M94065  |
| Enzyme 6 GeneCard ID |
DHODH  |
| Enzyme 6 GenAtlas ID |
DHODH  |
| Enzyme 6 HGNC ID |
HGNC:2867  |
| Enzyme 6 Chromosome Location |
16 |
| Enzyme 6 Locus |
16q22 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Minet M, Dufour ME, Lacroute F: Cloning and sequencing of a human cDNA coding for dihydroorotate dehydrogenase by complementation of the corresponding yeast mutant. Gene. 1992 Nov 16;121(2):393-6. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5418 |
| Enzyme 7 Name |
NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial precursor |
| Enzyme 7 Synonyms |
- NADH-ubiquinone oxidoreductase 51 kDa subunit
- Complex I-51kD
- CI-51kD
- NADH dehydrogenase flavoprotein 1
|
| Enzyme 7 Gene Name |
NDUFV1 |
| Enzyme 7 Protein Sequence |
>NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial precursor
MLATRRLLGWSLPARVSVRFSGDTTAPKKTSFGSLKDEDRIFTNLYGRHDWRLKGSLSRG
DWYKTKEILLKGPDWILGEIKTSGLRGRGGAGFPTGLKWSFMNKPSDGRPKYLVVNADEG
EPGTCKDREILRHDPHKLLEGCLVGGRAMGARAAYIYIRGEFYNEASNLQVAIREAYEAG
LIGKNACGSGYDFDVFVVRGAGAYICGEETALIESIEGKQGKPRLKPPFPADVGVFGCPT
TVANVETVAVSPTICRRGGTWFAGFGRERNSGTKLFNISGHVNHPCTVEEEMSVPLKELI
EKHAGGVTGGWDNLLAVIPGGSSTPLIPKSVCETVLMDFDALVQAQTGLGTAAVIVMDRS
TDIVKAIARLIEFYKHESCGQCTPCREGVDWMNKVMARFVRGDARPAEIDSLWEISKQIE
GHTICALGDGAAWPVQGLIRHFRPELEERMQRFAQQHQARQAAS
|
| Enzyme 7 Number of Residues |
464 |
| Enzyme 7 Molecular Weight |
50818 |
| Enzyme 7 Theoretical pI |
8.29 |
| Enzyme 7 GO Classification |
| Function |
- FMN binding
- NAD binding
- NADH dehydrogenase (ubiquinone) activity
- binding
- catalytic activity
- cation binding
- cation transporter activity
- coenzyme binding
- cofactor binding
- hydrogen ion transporter activity
- ion binding
- ion transporter activity
- iron ion binding
- monovalent inorganic cation transporter activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on NADH or NADPH
- transition metal ion binding
- transporter activity
|
| Process |
- ATP synthesis coupled electron transport
- ATP synthesis coupled electron transport (sensu Eukaryota)
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- mitochondrial electron transport, NADH to ubiquinone
- physiological process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Energy production and conversion |
| Enzyme 7 Specific Function |
Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- NADH + H+ + acceptor = NAD+ + reduced acceptor
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
Not Available |
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
3184148  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P49821  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
NDUV1_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>72 bp
ATGCTGGCAACACGGCGGCTGCTCGGCTGGTCGCTTCCCGCGCGGGTATCTGTGCGTTTC
AGCGGCGACACG
|
| Enzyme 7 GenBank Gene ID |
Y17379  |
| Enzyme 7 GeneCard ID |
NDUFV1  |
| Enzyme 7 GenAtlas ID |
NDUFV1  |
| Enzyme 7 HGNC ID |
HGNC:7716  |
| Enzyme 7 Chromosome Location |
11 |
| Enzyme 7 Locus |
11q13 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Schuelke M, Loeffen J, Mariman E, Smeitink J, van den Heuvel L: Cloning of the human mitochondrial 51 kDa subunit (NDUFV1) reveals a 100% antisense homology of its 3'UTR with the 5'UTR of the gamma-interferon inducible protein (IP-30) precursor: is this a link between mitochondrial myopathy and inflammation? Biochem Biophys Res Commun. 1998 Apr 17;245(2):599-606. [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
]
- Spencer SR, Taylor JB, Cowell IG, Xia CL, Pemble SE, Ketterer B: The human mitochondrial NADH: ubiquinone oxidoreductase 51-kDa subunit maps adjacent to the glutathione S-transferase P1-1 gene on chromosome 11q13. Genomics. 1992 Dec;14(4):1116-8. [PubMed
]
- Ali ST, Duncan AM, Schappert K, Heng HH, Tsui LC, Chow W, Robinson BH: Chromosomal localization of the human gene encoding the 51-kDa subunit of mitochondrial complex I (NDUFV1) to 11q13. Genomics. 1993 Nov;18(2):435-9. [PubMed
]
- Schuelke M, Smeitink J, Mariman E, Loeffen J, Plecko B, Trijbels F, Stockler-Ipsiroglu S, van den Heuvel L: Mutant NDUFV1 subunit of mitochondrial complex I causes leukodystrophy and myoclonic epilepsy. Nat Genet. 1999 Mar;21(3):260-1. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5426 |
| Enzyme 8 Name |
Ectonucleotide pyrophosphatase/phosphodiesterase family member 3 |
| Enzyme 8 Synonyms |
- E- NPP 3
- Phosphodiesterase I/nucleotide pyrophosphatase 3
- Phosphodiesterase I beta
- PD-Ibeta
- CD203c antigen[Includes: Alkaline phosphodiesterase I
- NPPase]
|
| Enzyme 8 Gene Name |
ENPP3 |
| Enzyme 8 Protein Sequence |
>Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
MESTLTLATEQPVKKNTLKKYKIACIVLLALLVIMSLGLGLGLGLRKLEKQGSCRKKCFD
ASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNKFRCGETRLEASLCSCSDDCL
QKKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLYTWDTL
MPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVNLNKNFSLS
SKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEVAINGSFPSIYMPYNGSVPFEERIS
TLLKWLDLPKAERPRFYTMYFEEPDSSGHAGGPVSARVIKALQVVDHAFGMLMEGLKQRN
LHNCVNIILLADHGMDQTYCNKMEYMTDYFPRINFFYMYEGPAPRIRAHNIPHDFFSFNS
EEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDQQWLAVRSKSNTNCGG
GNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLN
HLLKVPFYEPSHAEEVSKFSVCGFANPLPTESLDCFCPHLQNSTQLEQVNQMLNLTQEEI
TATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPT
VPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEE
FRKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHY
FVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNVESCPEGKPEALWVEERFTAHIARVR
DVELLTGLDFYQDKVQPVSEILQLKTYLPTFETTI
|
| Enzyme 8 Number of Residues |
875 |
| Enzyme 8 Molecular Weight |
100097 |
| Enzyme 8 Theoretical pI |
6.55 |
| Enzyme 8 GO Classification |
| Function |
- binding
- catalytic activity
- endonuclease activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- nuclease activity
- nucleic acid binding
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Not Available |
| Enzyme 8 Specific Function |
Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD |
| Enzyme 8 Pathways |
- Nicotinate and Nicotinamide Metabolism (map00760
)
- Pantothenate and CoA Biosynthesis (map00770
)
- Purine Metabolism (map00230
)
- Riboflavin Metabolism (map00740
)
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 8 Reactions |
- A dinucleotide + H2O = 2 mononucleotides
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
Not Available |
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
2465540  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
O14638  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
ENPP3_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>2628 bp
ATGGAATCTACGTTGACTTTAGCAACGGAACAACCTGTTAAGAAGAACACTCTTAAGAAA
TATAAAATAGCTTGCATTGTTCTTCTTGCTTTGCTGGTGATCATGTCACTTGGATTAGGC
CTGGGGCTTGGACTCAGGAAACTGGAAAAGCAAGGCAGCTGCAGGAAGAAGTGCTTTGAT
GCATCATTTAGAGGACTGGAGAACTGCCGGTGTGATGTGGCATGTAAAGACCGAGGTGAT
TGCTGCTGGGATTTTGAAGACACCTGTGTGGAATCAACTCGAATATGGATGTGCAATAAA
TTTCGTTGTGGAGAGACCAGATTAGAGGCCAGCCTTTGCTCTTGTTCAGATGACTGTTTG
CAGAAGAAAGATTGCTGTGCTGACTATAAGAGTGTTTGCCAAGGAGAAACCTCATGGCTG
GAAGAAAACTGTGACACAGCCCAGCAGTCTCAGTGCCCAGAAGGGTTTGACCTGCCACCA
GTTATCTTGTTTTCTATGGATGGATTTAGAGCTGAATATTTATACACATGGGATACTTTA
ATGCCAAATATCAATAAACTGAAAACATGTGGAATTCATTCAAAATACATGAGAGCTATG
TATCCTACCAAAACCTTCCCAAATCATTACACCATTGTCACGGGCTTGTATCCAGAGTCA
CATGGCATCATTGACAATAATATGTATGATGTAAATCTCAACAAGAATTTTTCACTTTCT
TCAAAGGAACAAAATAATCCAGCCTGGTGGCATGGGCAACCAATGTGGCTGACAGCAATG
TATCAAGGTTTAAAAGCCGCTACCTACTTTTGGCCCGGATCAGAAGTGGCTATAAATGGC
TCCTTTCCTTCCATATACATGCCTTACAACGGAAGTGTCCCATTTGAAGAGAGGATTTCT
ACACTGTTAAAATGGCTGGACCTGCCCAAAGCTGAAAGACCCAGGTTTTATACCATGTAT
TTTGAAGAACCTGATTCCTCTGGACATGCAGGTGGACCAGTCAGTGCCAGAGTAATTAAA
GCCTTACAGGTAGTAGATCATGCTTTTGGGATGTTGATGGAAGGCCTGAAGCAGCGGAAT
TTGCACAACTGTGTCAATATCATCCTTCTGGCTGACCATGGAATGGACCAGACTTATTGT
AACAAGATGGAATACATGACTGATTATTTTCCCAGAATAAACTTCTTCTACATGTACGAA
GGGCCTGCCCCCCGCATCCGAGCTCATAATATACCTCATGACTTTTTTAGTTTTAATTCT
GAGGAAATTGTTAGAAACCTCAGTTGCCGAAAACCTGATCAGCATTTCAAGCCCTATTTG
ACTCCTGATTTGCCAAAGCGACTGCACTATGCCAAGAACGTCAGAATCGACAAAGTTCAT
CTCTTTGTGGATCAACAGTGGCTGGCTGTTAGGAGTAAATCAAATACAAATTGTGGAGGA
GGCAACCATGGTTATAACAATGAGTTTAGGAGCATGGAGGCTATCTTTCTGGCACATGGA
CCCAGTTTTAAAGAGAAGACTGAAGTTGAACCATTTGAAAATATTGAAGTCTATAACCTA
ATGTGTGATCTTCTACGCATTCAACCAGCACCAAACAATGGAACCCATGGTAGTTTAAAC
CATCTTCTGAAGGTGCCTTTTTATGAGCCATCCCATGCAGAGGAGGTGTCAAAGTTTTCT
GTTTGTGGCTTTGCTAATCCATTGCCCACAGAGTCTCTTGACTGTTTCTGCCCTCACCTA
CAAAATAGTACTCAGCTGGAACAAGTGAATCAGATGCTAAATCTCACCCAAGAAGAAATA
ACAGCAACAGTGAAAGTAAATTTGCCATTTGGGAGGCCTAGGGTACTGCAGAAGAACGTG
GACCACTGTCTCCTTTACCACAGGGAATATGTCAGTGGATTTGGAAAAGCTATGAGGATG
CCCATGTGGAGTTCATACACAGTCCCCCAGTTGGGAGACACATCGCCTCTGCCTCCCACT
GTCCCAGACTGTCTGCGGGCTGATGTCAGGGTTCCTCCTTCTGAGAGCCAAAAATGTTCC
TTCTATTTAGCAGACAAGAATATCACCCACGGCTTCCTCTATCCTCCTGCCAGCAATAGA
ACATCAGATAGCCAATATGATGCTTTAATTACTAGCAATTTGGTACCTATGTATGAAGAA
TTCAGAAAAATGTGGGACTACTTCCACAGTGTTCTTCTTATAAAACATGCCACAGAAAGA
AATGGAGTAAATGTGGTTAGTGGACCAATATTTGATTATAATTATGATGGCCATTTTGAT
GCTCCAGATGAAATTACCAAACATTTAGCCAACACTGATGTTCCCATCCCAACACACTAC
TTTGTGGTGCTGACCAGTTGTAAAAACAAGAGCCACACACCGGAAAACTGCCCTGGGTGG
CTGGATGTCCTACCCTTTATCATCCCTCACCGACCTACCAACGTGGAGAGCTGTCCTGAA
GGTAAACCAGAAGCTCTTTGGGTTGAAGAAAGATTTACAGCTCACATTGCCCGGGTCCGT
GATGTAGAACTTCTCACTGGGCTTGACTTCTATCAGGATAAAGTGCAGCCTGTCTCTGAA
ATTTTGCAACTAAAGACATATTTACCAACATTTGAAACCACTATTTAA
|
| Enzyme 8 GenBank Gene ID |
AF005632  |
| Enzyme 8 GeneCard ID |
ENPP3  |
| Enzyme 8 GenAtlas ID |
ENPP3  |
| Enzyme 8 HGNC ID |
HGNC:3358  |
| Enzyme 8 Chromosome Location |
6 |
| Enzyme 8 Locus |
6q22 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5658 |
| Enzyme 9 Name |
Methionine synthase reductase, mitochondrial precursor |
| Enzyme 9 Synonyms |
- MSR
|
| Enzyme 9 Gene Name |
MTRR |
| Enzyme 9 Protein Sequence |
>Methionine synthase reductase, mitochondrial precursor
MGAASVRAGARLVEVALCSFTVTCLEVMRRFLLLYATQQGQAKAIAEEICEQAVVHGFSA
DLHCISESDKYDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQTLPVDFFAHLRYGL
LGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDCVGLELVVEPWIAGLWPALRKH
FRSSRGQEEISGALPVASPASLRTDLVKSELLHIESQVELLRFDDSGRKDSEVLKQNAVN
SNQSNVVIEDFESSLTRSVPPLSQASLNIPGLPPEYLQVHLQESLGQEESQVSVTSADPV
FQVPISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQL
EDKREHCVLLKIKADTKKKGATLPQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTS
DSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPY
SCASSSLFHPGKLHFVFNIVEFLSTATTEVLRKGVCTGWLALLVASVLQPNIHASHEDSG
KALAPKISISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGA
MWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDAPVGEEEAPAKYVQDNIQLHG
QQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYL
QDIWS
|
| Enzyme 9 Number of Residues |
725 |
| Enzyme 9 Molecular Weight |
80437 |
| Enzyme 9 Theoretical pI |
6.47 |
| Enzyme 9 GO Classification |
| Function |
- FMN binding
- binding
- catalytic activity
- electron transporter activity
- nucleotide binding
- oxidoreductase activity
- transporter activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 9 General Function |
Inorganic ion transport and metabolism |
| Enzyme 9 Specific Function |
Involved in the reductive regeneration of cob(I)alamin cofactor required for the maintenance of methionine synthase in a functional state |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
- 2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+ = 2 [methionine synthase]-cob(I)alamin + NADPH + H+ + 2 S-adenosylLmethionine
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
Not Available |
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
6572540  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q9UBK8  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
MTRR_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>2178 bp
ATGGGCGCTGCGTCAGTGCGCGCTGGCGCAAGGTTGGTGGAAGTCGCGTTGTGCAGTTTC
ACTGTTACATGCCTTGAAGTGATGAGGAGGTTTCTGTTACTATATGCTACACAGCAGGGA
CAGGCAAAGGCCATCGCAGAAGAAATGTGTGAGCAAGCTGTGGTACATGGATTTTCTGCA
GATCTTCACTGTATTAGTGAATCCGATAAGTATGACCTAAAAACCGAAACAGCTCCTCTT
GTTGTTGTGGTTTCTACCACGGGCACCGGAGACCCACCCGACACAGCCCGCAAGTTTGTT
AAGGAAATACAGAACCAAACACTGCCGGTTGATTTCTTTGCTCACCTGCGGTATGGGTTA
CTGGGTCTCGGTGATTCAGAATACACCTACTTTTGCAATGGGGGGAAGATAATTGATAAA
CGACTTCAAGAGCTTGGAGCCCGGCATTTCTATGACACTGGACATGCAGATGACTGTGTA
GGTTTAGAACTTGTGGTTGAGCCGTGGATTGCTGGACTCTGGCCAGCCCTCAGAAAGCAT
TTTAGGTCAAGCAGAGGACAAGAGGAGATAAGTGGCGCACTCCCGGTGGCATCACCTGCA
TCCTTGAGGACAGACCTTGTGAAGTCAGAGCTGCTACACATTGAATCTCAAGTCGAGCTT
CTGAGATTCGATGATTCAGGAAGAAAGGATTCTGAGGTTTTGAAGCAAAATGCAGTGAAC
AGCAACCAATCCAATGTTGTAATTGAAGACTTTGAGTCCTCACTTACCCGTTCGGTACCC
CCACTCTCACAAGCCTCTCTGAATATTCCTGGTTTACCCCCAGAATATTTACAGGTACAT
CTGCAGGAGTCTCTTGGCCAGGAGGAAAGCCAAGTATCTGTGACTTCAGCAGATCCAGTT
TTTCAAGTGCCAATTTCAAAGGCAGTTCAACTTACTACGAATGATGCCATAAAAACCACT
CTGCTGGTAGAATTGGACATTTCAAATACAGACTTTTCCTATCAGCCTGGAGATGCCTTC
AGCGTGATCTGCCCTAACAGTGATTCTGAGGTACAAAGCCTACTCCAAAGACTGCAGCTT
GAAGATAAAAGAGAGCACTGCGTCCTTTTGAAAATAAAGGCAGACACAAAGAAGAAAGGA
GCTACCTTACCCCAGCATATACCTGCGGGATGTTCTCTCCAGTTCATTTTTACCTGGTGT
CTTGAAATCCGAGCAATTCCTAAAAAGGCATTTTTGCGAGCCCTTGTGGACTATACCAGT
GACAGTGCTGAAAAGCGCAGGCTACAGGAGCTGTGCAGTAAACAAGGGGCAGCCGATTAT
AGCCGCTTTGTACGAGATGCCTGTGCCTGCTTGTTGGATCTCCTCCTCGCTTTCCCTTCT
TGCCAGCCACCACTCAGTCTCCTGCTCGAACATCTTCCTAAACTTCAACCCAGACCATAT
TCGTGTGCAAGCTCAAGTTTATTTCACCCAGGAAAGCTCCATTTTGTCTTCAACATTGTG
GAATTTCTGTCTACTGCCACAACAGAGGTTCTGCGGAAGGGAGTATGTACAGGCTGGCTG
GCCTTGTTGGTTGCTTCAGTTCTTCAGCCAAACATACATGCATCCCATGAAGACAGCGGG
AAAGCCCTGGCTCCTAAGATATCCATCTCTCCTCGAACAACAAATTCTTTCCACTTACCA
GATGACCCCTCAATCCCCATCATAATGGTGGGTCCAGGAACCGGCATAGCCCCGTTTATT
GGGTTCCTACAACATAGAGAGAAACTCCAAGAACAACACCCAGATGGAAATTTTGGAGCA
ATGTGGTTGTTTTTTGGCTGCAGGCATAAGGATAGGGATTATCTATTCAGAAAAGAGCTC
AGACATTTCCTTAAGCATGGGATCTTAACTCATCTAAAGGTTTCCTTCTCAAGAGATGCT
CCTGTTGGGGAGGAGGAAGCCCCAGCAAAGTATGTACAAGACAACATCCAGCTTCATGGC
CAGCAGGTGGCGAGAATCCTCCTCCAGGAGAACGGCCATATTTATGTGTGTGGAGATGCA
AAGAATATGGCCAAGGATGTACATGATGCCCTTGTGCAAATAATAAGCAAAGAGGTTGGA
GTTGAAAAACTAGAAGCAATGAAAACCCTGGCCACTTTAAAAGAAGAAAAACGCTACCTT
CAGGATATTTGGTCATAA
|
| Enzyme 9 GenBank Gene ID |
AF121213  |
| Enzyme 9 GeneCard ID |
MTRR  |
| Enzyme 9 GenAtlas ID |
MTRR  |
| Enzyme 9 HGNC ID |
HGNC:7473  |
| Enzyme 9 Chromosome Location |
5 |
| Enzyme 9 Locus |
5p15.3-p15.2 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Leclerc D, Odievre M, Wu Q, Wilson A, Huizenga JJ, Rozen R, Scherer SW, Gravel RA: Molecular cloning, expression and physical mapping of the human methionine synthase reductase gene. Gene. 1999 Nov 15;240(1):75-88. [PubMed
]
- Leclerc D, Wilson A, Dumas R, Gafuik C, Song D, Watkins D, Heng HH, Rommens JM, Scherer SW, Rosenblatt DS, Gravel RA: Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria. Proc Natl Acad Sci U S A. 1998 Mar 17;95(6):3059-64. [PubMed
]
- Wilson A, Leclerc D, Rosenblatt DS, Gravel RA: Molecular basis for methionine synthase reductase deficiency in patients belonging to the cblE complementation group of disorders in folate/cobalamin metabolism. Hum Mol Genet. 1999 Oct;8(11):2009-16. [PubMed
]
- Wilson A, Platt R, Wu Q, Leclerc D, Christensen B, Yang H, Gravel RA, Rozen R: A common variant in methionine synthase reductase combined with low cobalamin (vitamin B12) increases risk for spina bifida. Mol Genet Metab. 1999 Aug;67(4):317-23. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5947 |
| Enzyme 10 Name |
Pyridoxine-5'-phosphate oxidase |
| Enzyme 10 Synonyms |
- Pyridoxamine-phosphate oxidase
|
| Enzyme 10 Gene Name |
PNPO |
| Enzyme 10 Protein Sequence |
>Pyridoxine-5'-phosphate oxidase
MTCWLRGVTATFGRPAEWPGYLSHLCGRSAAMDLGPMRKSYRGDREAFEETHLTSLDPVK
QFAAWFEEAVQCPDIGEANAMCLATCTRDGKPSARMLLLKGFGKDGFRFFTNFESRKGKE
LDSNPFASLVFYWEPLNRQVRVEGPVKKLPEEEAECYFHSRPKSSQIGAVVSHQSSVIPD
REYLRKKNEELEQLYQDQEVPKPKSWGGYVLYPQVMEFWQGQTNRLHDRIVFRRGLPTGD
SPLGPMTHRGEEDWLYERLAP
|
| Enzyme 10 Number of Residues |
261 |
| Enzyme 10 Molecular Weight |
29988 |
| Enzyme 10 Theoretical pI |
7.09 |
| Enzyme 10 GO Classification |
| Function |
- FMN binding
- binding
- catalytic activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-NH2 group of donors
- oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
- pyridoxamine-phosphate oxidase activity
|
| Process |
- cellular metabolism
- metabolism
- physiological process
- pyridoxine biosynthesis
- pyridoxine metabolism
- vitamin B6 metabolism
- vitamin metabolism
- water-soluble vitamin metabolism
|
| Component |
| — |
|
| Enzyme 10 General Function |
Coenzyme transport and metabolism |
| Enzyme 10 Specific Function |
Oxidizes PNP and PMP into pyridoxal 5'-phosphate (PLP) |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + ammonia + H2O2
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
21728336  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q9NVS9  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
PNPO_HUMAN  |
| Enzyme 10 PDB ID |
1NRG  |
| Enzyme 10 PDB File |
Show |
| Enzyme 10 3D Structure |
|
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>786 bp
ATGACGTGCTGGCTGCGGGGCGTCACGGCGACGTTCGGGCGACCTGCCGAGTGGCCAGGC
TACCTCAGTCACCTGTGTGGTCGCAGTGCTGCCATGGACCTGGGACCCATGCGCAAGAGT
TACCGCGGGGACCGAGAGGCATTTGAGGAGACTCATCTGACCTCCCTTGACCCAGTGAAA
CAGTTTGCTGCCTGGTTTGAGGAGGCTGTTCAGTGTCCTGACATAGGGGAAGCCAATGCC
ATGTGTCTGGCTACCTGCACCAGAGATGGAAAACCCTCTGCTCGCATGTTGCTGCTGAAG
GGCTTCGGGAAAGATGGCTTCCGCTTCTTCACTAACTTCGAGAGTCGAAAAGGAAAAGAG
CTGGACTCTAATCCCTTTGCTTCCCTTGTCTTCTACTGGGAGCCACTTAACCGTCAGGTG
CGTGTGGAAGGCCCTGTGAAGAAACTGCCTGAGGAGGAGGCTGAGTGCTACTTCCACTCC
CGCCCCAAGAGCAGCCAGATTGGGGCTGTGGTCAGCCACCAGAGTTCTGTGATCCCTGAT
CGGGAGTATCTGAGAAAGAAAAATGAGGAACTGGAACAGCTCTACCAGGATCAAGAGGTG
CCCAAGCCAAAATCCTGGGGTGGCTATGTCCTGTACCCTCAGGTGATGGAGTTCTGGCAA
GGTCAAACCAACCGCCTGCATGACCGGATAGTCTTTCGGCGGGGCCTACCCACAGGAGAT
TCCCCTTTGGGGCCCATGACCCACCGCGGGGAGGAAGACTGGCTCTATGAGAGACTTGCA
CCTTAA
|
| Enzyme 10 GenBank Gene ID |
AF468030  |
| Enzyme 10 GeneCard ID |
PNPO  |
| Enzyme 10 GenAtlas ID |
PNPO  |
| Enzyme 10 HGNC ID |
HGNC:30260  |
| Enzyme 10 Chromosome Location |
17 |
| Enzyme 10 Locus |
17q21.32 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Musayev FN, Di Salvo ML, Ko TP, Schirch V, Safo MK: Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase. Protein Sci. 2003 Jul;12(7):1455-63. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6002 |
| Enzyme 11 Name |
Dihydropyrimidine dehydrogenase [NADP+] precursor |
| Enzyme 11 Synonyms |
- DPD
- DHPDHase
- Dihydrouracil dehydrogenase
- Dihydrothymine dehydrogenase
|
| Enzyme 11 Gene Name |
DPYD |
| Enzyme 11 Protein Sequence |
>Dihydropyrimidine dehydrogenase [NADP+] precursor
MAPVLSKDSADIESILALNPRTQTHATLCSTSAKKLDKKHWKRNPDKNCFNCEKLENNFD
DIKHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDN
PLGLTCGMVCPTSDLCVGGCNLYATEEGPINIGGLQQFATEVFKAMSIPQIRNPSLPPPE
KMSEAYSAKIALFGAGPASISCASFLARLGYSDITIFEKQEYVGGLSTSEIPQFRLPYDV
VNFEIELMKDLGVKIICGKSLSVNEMTLSTLKEKGYKAAFIGIGLPEPNKDAIFQGLTQD
QGFYTSKDFLPLVAKGSKAGMCACHSPLPSIRGVVIVLGAGDTAFDCATSALRCGARRVF
IVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEQDETGKWN
EDEDQMVHLKADVVISAFGSVLSDPKVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGG
DVVGLANTTVESVNDGKQASWYIHKYVQSQYGASVSAKPELPLFYTPIDLVDISVEMAGL
KFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRGTTSGPMY
GPGQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDS
GADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSI
ARAAKEGGANGVTATNTVSGLMGLKSDGTPWPAVGIAKRTTYGGVSGTAIRPIALRAVTS
IARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYL
KSIEELQDWDGQSPATVSHQKGKPVPRIAELMDKKLPSFGPYLEQRKKIIAENKIRLKEQ
NVAFSPLKRSCFIPKRPIPTIKDVIGKALQYLGTFGELSNVEQVVAMIDEEMCINCGKCY
MTCNDSGYQAIQFDPETHLPTITDTCTGCTLCLSVCPIVDCIKMVSRTTPYEPKRGVPLS
VNPVC
|
| Enzyme 11 Number of Residues |
1025 |
| Enzyme 11 Molecular Weight |
111375 |
| Enzyme 11 Theoretical pI |
7.05 |
| Enzyme 11 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- dihydroorotate dehydrogenase activity
- dihydroorotate oxidase activity
- disulfide oxidoreductase activity
- electron transporter activity
- ion binding
- iron ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
- transition metal ion binding
- transporter activity
|
| Process |
- 'de novo' pyrimidine base biosynthesis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- nucleobase metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- physiological process
- pyrimidine base biosynthesis
- pyrimidine base metabolism
|
| Component |
- cell
- cytoplasm
- intracellular
- membrane
|
|
| Enzyme 11 General Function |
Amino acid transport and metabolism |
| Enzyme 11 Specific Function |
Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- 5,6-dihydrouracil + NADP+ = uracil + NADPH + H+
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
558305  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q12882  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
DPYD_HUMAN  |
| Enzyme 11 PDB ID |
1GTE  |
| Enzyme 11 PDB File |
Show |
| Enzyme 11 3D Structure |
|
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>3078 bp
ATGGCCCCTGTGCTCAGTAAGGACTCGGCGGACATCGAGAGTATCCTGGCTTTAAATCCT
CGAACACAAACTCATGCAACTCTGTGTTCCACTTCGGCCAAGAAATTAGACAAGAAACAT
TGGAAAAGAAATCCTGATAAGAACTGCTTTAATTGTGAGAAGCTGGAGAATAATTTTGAT
GACATCAAGCACACGACTCTTGGTGAGCGAGGAGCTCTCCGAGAAGCAATGAGATGCCTG
AAATGTGCAGATGCCCCGTGTCAGAAGAGCTGTCCAACTAATCTTGATATTAAATCATTC
ATCACAAGTATTGCAAACAAGAACTATTATGGAGCTGCTAAGATGATATTTTCTGACAAC
CCACTTGGTCTGACTTGTGGAATGGTATGTCCAACCTCTGATCTATGTGTAGGTGGATGC
AATTTATATGCCACTGAAGAGGGACCCATTAATATTGGTGGATTGCAGCAATTTGCTACT
GAGGTATTCAAAGCAATGAGTATCCCACAGATCAGAAATCCTTCGCTGCCTCCCCCAGAA
AAAATGTCTGAAGCCTATTCTGCAAAGATTGCTCTTTTTGGTGCTGGGCCTGCAAGTATA
AGTTGTGCTTCCTTTTTGGCTCGATTGGGGTACTCTGACATCACTATATTTGAAAAACAA
GAATATGTTGGTGGTTTAAGTACTTCTGAAATTCCTCAGTTCCGGCTGCCGTATGATGTA
GTGAATTTTGAGATTGAGCTAATGAAGGACCTTGGTGTAAAGATAATTTGCGGTAAAAGC
CTTTCAGTGAATGAAATGACTCTTAGCACTTTGAAAGAAAAAGGCTACAAAGCTGCTTTC
ATTGGAATAGGTTTGCCAGAACCCAATAAAGATGCCATCTTCCAAGGCCTGACGCAGGAC
CAGGGGTTTTATACATCCAAAGACTTTTTGCCACTTGTAGCCAAAGGCAGTAAAGCAGGA
ATGTGCGCCTGTCACTCTCCATTGCCATCGATACGGGGAGTCGTGATTGTACTTGGAGCT
GGAGACACTGCCTTCGACTGTGCAACATCTGCTCTACGTTGTGGAGCTCGCCGAGTGTTC
ATCGTCTTCAGAAAAGGCTTTGTTAATATAAGAGCTGTCCCTGAGGAGATGGAGCTTGCT
AAGGAAGAAAAGTGTGAATTTCTGCCATTCCTGTCCCCACGGAAGGTTATAGTAAAAGGT
GGGAGAATTGTTGCTATGCAGTTTGTTCGGACAGAGCAAGATGAAACTGGAAAATGGAAT
GAAGATGAAGATCAGATGGTCCATCTGAAAGCCGATGTGGTCATCAGTGCCTTTGGTTCA
GTTCTGAGTGATCCTAAAGTAAAAGAAGCCTTGAGCCCTATAAAATTTAACAGATGGGGT
CTCCCAGAAGTAGATCCAGAAACTATGCAAACTAGTGAAGCATGGGTATTTGCAGGTGGT
GATGTCGTTGGTTTGGCTAACACTACAGTGGAATCGGTGAATGATGGAAAGCAAGCTTCT
TGGTACATTCACAAATACGTACAGTCACAATATGGAGCTTCCGTTTCTGCCAAGCCTGAA
CTACCCCTCTTTTACACTCCTATTGATCTGGTGGACATTAGTGTAGAAATGGCCGGATTG
AAGTTTATAAATCCTTTTGGTCTTGCTAGCGCAACTCCAGCCACCAGCACATCAATGATT
CGAAGAGCTTTTGAAGCTGGATGGGGTTTTGCCCTCACCAAAACTTTCTCTCTTGATAAG
GACATTGTGACAAATGTTTCCCCCAGAATCATCCGGGGAACCACCTCTGGCCCCATGTAT
GGCCCTGGACAAAGCTCCTTTCTGAATATTGAGCTCATCAGTGAGAAAACGGCTGCATAT
TGGTGTCAAAGTGTCACTGAACTAAAGGCTGACTTCCCAGACAACATTGTGATTGCTAGC
ATTATGTGCAGTTACAATAAAAATGACTGGACGGAACTTGCCAAGAAGTCTGAGGATTCT
GGAGCAGATGCCCTGGAGTTAAATTTATCATGTCCACATGGCATGGGAGAAAGAGGAATG
GGCCTGGCCTGTGGGCAGGATCCAGAGCTGGTGCGGAACATCTGCCGCTGGGTTAGGCAA
GCTGTTCAGATTCCTTTTTTTGCCAAGCTGACCCCAAATGTCACTGATATTGTGAGCATC
GCAAGAGCTGCAAAGGAAGGTGGTGCCAATGGCGTTACAGCCACCAACACTGTCTCAGGT
CTGATGGGATTAAAATCTGATGGCACACCTTGGCCAGCAGTGGGGATTGCAAAGCGAACT
ACATATGGAGGAGTGTCTGGGACAGCAATCAGACCTATTGCTTTGAGAGCTGTGACCTCC
ATTGCTCGTGCTCTGCCTGGATTTCCCATTTTGGCTACTGGTGGAATTGACTCTGCTGAA
AGTGGTCTTCAGTTTCTCCATAGTGGTGCTTCCGTCCTCCAGGTATGCAGTGCCATTCAG
AATCAGGATTTCACTGTGATCGAAGACTACTGCACTGGCCTCAAAGCCCTGCTTTATCTG
AAAAGCATTGAAGAACTACAAGACTGGGATGGACAGAGTCCAGCTACTGTGAGTCACCAG
AAAGGGAAACCAGTTCCACGTATAGCTGAACTCATGGACAAGAAACTGCCAAGTTTTGGA
CCTTATCTGGAACAGCGCAAGAAAATCATAGCAGAAAACAAGATTAGACTGAAAGAACAA
AATGTAGCTTTTTCACCACTTAAGAGAAGCTGTTTTATCCCCAAAAGGCCTATTCCTACC
ATCAAGGATGTAATAGGAAAAGCACTGCAGTACCTTGGAACATTTGGTGAATTGAGCAAC
GTAGAGCAAGTTGTGGCTATGATTGATGAAGAAATGTGTATCAACTGTGGTAAATGCTAC
ATGACCTGTAATGATTCTGGCTACCAGGCTATACAGTTTGATCCAGAAACCCACCTGCCC
ACCATAACCGACACTTGTACAGGCTGTACTCTGTGTCTCAGTGTTTGCCCTATTGTCGAC
TGCATCAAAATGGTTTCCAGGACAACACCTTATGAACCAAAGAGAGGCGTACCCTTATCT
GTGAATCCGGTGTGTTAA
|
| Enzyme 11 GenBank Gene ID |
U09178  |
| Enzyme 11 GeneCard ID |
DPYD  |
| Enzyme 11 GenAtlas ID |
DPYD  |
| Enzyme 11 HGNC ID |
HGNC:3012  |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
1p22 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Yokota H, Fernandez-Salguero P, Furuya H, Lin K, McBride OW, Podschun B, Schnackerz KD, Gonzalez FJ: cDNA cloning and chromosome mapping of human dihydropyrimidine dehydrogenase, an enzyme associated with 5-fluorouracil toxicity and congenital thymine uraciluria. J Biol Chem. 1994 Sep 16;269(37):23192-6. [PubMed
]
- Johnson MR, Wang K, Tillmanns S, Albin N, Diasio RB: Structural organization of the human dihydropyrimidine dehydrogenase gene. Cancer Res. 1997 May 1;57(9):1660-3. [PubMed
]
- Ogura K, Nishiyama T, Takubo H, Kato A, Okuda H, Arakawa K, Fukushima M, Nagayama S, Kawaguchi Y, Watabe T: Suicidal inactivation of human dihydropyrimidine dehydrogenase by (E)-5-(2-bromovinyl)uracil derived from the antiviral, sorivudine. Cancer Lett. 1998 Jan 9;122(1-2):107-13. [PubMed
]
- Vreken P, Van Kuilenburg AB, Meinsma R, Smit GP, Bakker HD, De Abreu RA, van Gennip AH: A point mutation in an invariant splice donor site leads to exon skipping in two unrelated Dutch patients with dihydropyrimidine dehydrogenase deficiency. J Inherit Metab Dis. 1996;19(5):645-54. [PubMed
]
- Fernandez-Salguero PM, Sapone A, Wei X, Holt JR, Jones S, Idle JR, Gonzalez FJ: Lack of correlation between phenotype and genotype for the polymorphically expressed dihydropyrimidine dehydrogenase in a family of Pakistani origin. Pharmacogenetics. 1997 Apr;7(2):161-3. [PubMed
]
- Lu ZH, Zhang R, Diasio RB: Purification and characterization of dihydropyrimidine dehydrogenase from human liver. J Biol Chem. 1992 Aug 25;267(24):17102-9. [PubMed
]
- Vreken P, Van Kuilenburg AB, Meinsma R, van Gennip AH: Dihydropyrimidine dehydrogenase (DPD) deficiency: identification and expression of missense mutations C29R, R886H and R235W. Hum Genet. 1997 Dec;101(3):333-8. [PubMed
]
- Vreken P, Van Kuilenburg AB, Meinsma R, van Gennip AH: Identification of novel point mutations in the dihydropyrimidine dehydrogenase gene. J Inherit Metab Dis. 1997 Jul;20(3):335-8. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6067 |
| Enzyme 12 Name |
Hydroxyacid oxidase 1 |
| Enzyme 12 Synonyms |
- HAOX1
- Glycolate oxidase
- GOX
|
| Enzyme 12 Gene Name |
HAO1 |
| Enzyme 12 Protein Sequence |
>Hydroxyacid oxidase 1
MLPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAET
DLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAE
AGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLDDVRNRFKLPPQ
LRMKNFETSTLSFSPEENFGDDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILR
GDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDV
LKALALGAKAVFVGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLV
RKNPLAVSKI
|
| Enzyme 12 Number of Residues |
370 |
| Enzyme 12 Molecular Weight |
40925 |
| Enzyme 12 Theoretical pI |
8.29 |
| Enzyme 12 GO Classification |
| Function |
- FMN binding
- binding
- catalytic activity
- nucleotide binding
- oxidoreductase activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Energy production and conversion |
| Enzyme 12 Specific Function |
Has 2-hydroxyacid oxidase activity. Most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids |
| Enzyme 12 Pathways |
- Glyoxylate and Dicarboxylate Metabolism (map00630
)
|
| Enzyme 12 Reactions |
- (S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
7530485  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q9UJM8  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
HAOX1_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1113 bp
ATGCTCCCCCGGCTAATTTGTATCAATGATTATGAACAACATGCTAAATCAGTACTTCCA
AAGTCTATATATGACTATTACAGGTCTGGGGCAAATGATGAAGAAACTTTGGCTGATAAT
ATTGCAGCATTTTCCAGATGGAAGCTGTATCCAAGGATGCTCCGGAATGTTGCTGAAACA
GATCTGTCGACTTCTGTTTTAGGACAGAGGGTCAGCATGCCAATATGTGTGGGGGCTACG
GCCATGCAGCGCATGGCTCATGTGGACGGCGAGCTTGCCACTGTGAGAGCCTGTCAGTCC
CTGGGAACGGGCATGATGTTGAGTTCCTGGGCCACCTCCTCAATTGAAGAAGTGGCGGAA
GCTGGTCCTGAGGCACTTCGTTGGCTGCAACTGTATATCTACAAGGACCGAGAAGTCACC
AAGAAGCTAGTGCGGCAGGCAGAGAAGATGGGCTACAAGGCCATATTTGTGACAGTGGAC
ACACCTTACCTGGGCAACCGTCTGGATGATGTGCGTAACAGATTCAAACTGCCGCCACAA
CTCAGGATGAAAAATTTTGAAACCAGTACTTTATCATTTTCTCCTGAGGAAAATTTTGGA
GACGACAGTGGACTTGCTGCATATGTGGCTAAAGCAATAGACCCATCTATCAGCTGGGAA
GATATCAAATGGCTGAGAAGACTGACATCATTGCCAATTGTTGCAAAGGGCATTTTGAGA
GGTGATGATGCCAGGGAGGCTGTTAAACATGGCTTGAATGGGATCTTGGTGTCGAATCAT
GGGGCTCGACAACTCGATGGGGTGCCAGCCACTATTGATGTTCTGCCAGAAATTGTGGAG
GCTGTGGAAGGGAAGGTGGAAGTCTTCCTGGACGGGGGTGTGCGGAAAGGCACTGATGTT
CTGAAAGCTCTGGCTCTTGGCGCCAAGGCTGTGTTTGTGGGGAGACCAATCGTTTGGGGC
TTAGCTTTCCAGGGGGAGAAAGGTGTTCAAGATGTCCTCGAGATACTAAAGGAAGAATTC
CGGTTGGCCATGGCTCTGAGTGGGTGCCAGAATGTGAAAGTCATCGACAAGACATTGGTG
AGGAAAAATCCTTTGGCCGTTTCCAAGATCTGA
|
| Enzyme 12 GenBank Gene ID |
AF244134  |
| Enzyme 12 GeneCard ID |
HAO1  |
| Enzyme 12 GenAtlas ID |
HAO1  |
| Enzyme 12 HGNC ID |
HGNC:4809  |
| Enzyme 12 Chromosome Location |
20 |
| Enzyme 12 Locus |
20p12 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Williams E, Cregeen D, Rumsby G: Identification and expression of a cDNA for human glycolate oxidase. Biochim Biophys Acta. 2000 Sep 7;1493(1-2):246-8. [PubMed
]
- Jones JM, Morrell JC, Gould SJ: Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases. J Biol Chem. 2000 Apr 28;275(17):12590-7. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6068 |
| Enzyme 13 Name |
Hydroxyacid oxidase 2 |
| Enzyme 13 Synonyms |
- HAOX2
- (S-2-hydroxy-acid oxidase, peroxisomal
- Long chain alpha-hydroxy acid oxidase
- Long- chain L-2-hydroxy acid oxidase
|
| Enzyme 13 Gene Name |
HAO2 |
| Enzyme 13 Protein Sequence |
>Hydroxyacid oxidase 2
MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDT
RTTIQGEEISAPICIAPTGFHCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAA
PEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRNQLRRNLTLT
DLQSPKKGNAIPYFQMTPISTSLCWNDLSWFQSITRLPIILKGILTKEDAELAVKHNVQG
IIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLG
RPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINRNLVQFSRL
|
| Enzyme 13 Number of Residues |
351 |
| Enzyme 13 Molecular Weight |
38839 |
| Enzyme 13 Theoretical pI |
7.69 |
| Enzyme 13 GO Classification |
| Function |
- FMN binding
- binding
- catalytic activity
- nucleotide binding
- oxidoreductase activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 13 General Function |
Energy production and conversion |
| Enzyme 13 Specific Function |
Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids |
| Enzyme 13 Pathways |
- Glyoxylate and Dicarboxylate Metabolism (map00630
)
|
| Enzyme 13 Reactions |
- (S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
7208438  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q9NYQ3  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
HAOX2_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1056 bp
ATGTCCTTGGTGTGTTTGACAGACTTTCAGGCCCATGCGCGAGAGCAGCTGTCTAAGTCA
ACTCGGGATTTTATTGAAGGTGGAGCAGATGACAGCATCACGCGGGATGACAACATTGCA
GCATTTAAAAGAATTCGCCTCCGTCCGCGGTACCTGAGAGATGTGTCTGAGGTGGACACC
AGAACCACAATCCAAGGGGAGGAGATCAGTGCCCCTATTTGTATCGCACCCACAGGGTTC
CACTGCCTTGTCTGGCCTGATGGGGAAATGAGCACAGCAAGAGCTGCCCAAGCGGCTGGT
ATCTGCTACATCACCAGCACATTTGCCAGCTGTAGCCTTGAAGACATTGTCATTGCAGCT
CCCGAAGGCCTCCGATGGTTCCAACTCTATGTGCATCCAGACCTGCAGCTGAACAAACAG
TTGATCCAGAGGGTAGAATCCCTAGGTTTCAAAGCTTTGGTAATAACTTTGGATACACCT
GTATGTGGCAACAGGCGACATGACATTCGAAACCAGTTGAGGAGGAACTTAACACTAACA
GATCTTCAATCACCTAAAAAGGGAAATGCAATACCTTATTTCCAGATGACTCCTATCAGC
ACTTCTCTCTGCTGGAATGATCTCTCCTGGTTTCAGAGCATAACTCGATTGCCCATCATC
CTGAAAGGGATTTTGACAAAAGAGGATGCAGAGTTAGCTGTGAAGCACAATGTCCAGGGT
ATCATTGTTTCCAACCATGGTGGGAGGCAGCTTGATGAGGTTCTTGCTTCAATTGATGCT
TTGACAGAAGTGGTGGCTGCTGTAAAGGGGAAAATTGAAGTCTACCTGGATGGCGGGGTC
CGAACTGGCAATGATGTGCTGAAGGCTCTGGCCCTTGGAGCTAAGTGCATTTTTCTTGGG
AGACCAATCCTATGGGGCCTTGCCTGCAAGGGTGAACATGGTGTTAAGGAAGTTTTGAAC
ATTTTAACAAATGAGTTCCACACTTCCATGGCCCTTACAGGCTGCCGGTCGGTCGCTGAG
ATCAATCGAAACTTGGTCCAGTTTTCCAGGCTGTAA
|
| Enzyme 13 GenBank Gene ID |
AF231917  |
| Enzyme 13 GeneCard ID |
HAO2  |
| Enzyme 13 GenAtlas ID |
HAO2  |
| Enzyme 13 HGNC ID |
HGNC:4810  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
1p13.3-p13.1 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Jones JM, Morrell JC, Gould SJ: Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases. J Biol Chem. 2000 Apr 28;275(17):12590-7. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
6214 |
| Enzyme 14 Name |
Nitric oxide synthase, inducible |
| Enzyme 14 Synonyms |
- NOS type II
- Inducible NO synthase
- Inducible NOS
- iNOS
- Hepatocyte NOS
- HEP- NOS
|
| Enzyme 14 Gene Name |
NOS2A |
| Enzyme 14 Protein Sequence |
>Nitric oxide synthase, inducible
MACPWKFLFKTKFHQYAMNGEKDINNNVEKAPCATSSPVTQDDLQYHNLSKQQNESPQPL
VETGKKSPESLVKLDATPLSSPRHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIM
TPKSLTRGPRDKPTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQ
LTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNI
RSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYG
RFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVG
GLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINI
AVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEM
LNYVLSPFYYYQVEAWKTHVWQDEKRRPKRREIPLKVLVKAVLFACMLMRKTMASRVRVT
ILFATETGKSEALAWDLGALFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPG
NGEKLKKSLFMLKELNNKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGD
ELSGQEDAFRSWAVQTFKAACETFDVRGKQHIQIPKLYTSNVTWDPHHYRLVQDSQPLDL
SKALSSMHAKNVFTMRLKSRQNLQSPTSSRATILVELSCEDGQGLNYLPGEHLGVCPGNQ
PALVQGILERVVDGPTPHQTVRLEALDESGSYWVSDKRLPPCSLSQALTYFLDITTPPTQ
LLLQKLAQVATEEPERQRLEALCQPSEYSKWKFTNSPTFLEVLEEFPSLRVSAGFLLSQL
PILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPLHHGVCSTWLNSLKPQDPVPCF
VRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDSQHKGVRGGRMTLVFGCRRPD
EDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKPKVYVQDILRQQLASEVLRVLHKEPGHLY
VCGDVRMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIFGAVFPYEAKKDR
VAVQPSSLEMSAL
|
| Enzyme 14 Number of Residues |
1153 |
| Enzyme 14 Molecular Weight |
131119 |
| Enzyme 14 Theoretical pI |
8.01 |
| Enzyme 14 GO Classification |
| Function |
- FAD binding
- FMN binding
- NADP binding
- adenyl nucleotide binding
- binding
- calmodulin binding
- catalytic activity
- cation binding
- coenzyme binding
- cofactor binding
- electron transporter activity
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- nitric-oxide synthase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
- protein binding
- purine nucleotide binding
- tetrapyrrole binding
- transition metal ion binding
- transporter activity
|
| Process |
- biosynthesis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- nitric oxide biosynthesis
- physiological process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Inorganic ion transport and metabolism |
| Enzyme 14 Specific Function |
Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions |
| Enzyme 14 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 14 Reactions |
- L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
292242  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P35228  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
NOS2A_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>3462 bp
ATGGCCTGTCCTTGGAAATTTCTGTTCAAGACCAAATTCCACCAGTATGCAATGAATGGG
GAAAAAGACATCAACAACAATGTGGAGAAAGCCCCCTGTGCCACCTCCAGTCCAGTGACA
CAGGATGACCTTCAGTATCACAACCTCAGCAAGCAGCAGAATGAGTCCCCGCAGCCCCTC
GTGGAGACGGGAAAGAAGTCTCCAGAATCTCTGGTCAAGCTGGATGCAACCCCATTGTCC
TCCCCACGGCATGTGAGGATCAAAAACTGGGGCAGCGGGATGACTTTCCAAGACACACTT
CACCATAAGGCCAAAGGGATTTTAACTTGCAGGTCCAAATCTTGCCTGGGGTCCATTATG
ACTCCCAAAAGTTTGACCAGAGGACCCAGGGACAAGCCTACCCCTCCAGATGAGCTTCTA
CCTCAAGCTATCGAATTTGTCAACCAATATTACGGCTCCTTCAAAGAGGCAAAAATAGAG
GAACATCTGGCCAGGGTGGAAGCGGTAACAAAGGAGATAGAAACAACAGGAACCTACCAA
CTGACGGGAGATGAGCTCATCTTCGCCACCAAGCAGGCCTGGCGCAATGCCCCACGCTGC
ATTGGGAGGATCCAGTGGTCCAACCTGCAGGTCTTCGATGCCCGCAGCTGTTCCACTGCC
CGGGAAATGTTTGAACACATCTGCAGACACGTGCGTTACTCCACCAACAATGGCAACATC
AGGTCGGCCATCACCGTGTTCCCCCAGCGGAGTGATGGCAAGCACGACTTCCGGGTGTGG
AATGCTCAGCTCATCCGCTATGCTGGCTACCAGATGCCAGATGGCAGCATCAGAGGGGAC
CCTGCCAACGTGGAATTCACTCAGCTGTGCATCGACCTGGGCTGGAAGCCCAAGTACGGC
CGCTTCGATGTGGTCCCCCTGGTCCTGCAGGCCAATGGCCGTGACCCTGAGCTCTTCGAA
ATCCCACCTGACCTTGTGCTTGAGGTGGCCATGGAACATCCCAAATACGAGTGGTTTCGG
GAACTGGAGCTAAAGTGGTACGCCCTGCCTGCAGTGGCCAACATGCTGCTTGAGGTGGGC
GGCCTGGAGTTCCCAGGGTGCCCCTTCAATGGCTGGTACATGGGCACAGAGATCGGAGTC
CGGGACTTCTGTGACGTCCAGCGCTACAACATCCTGGAGGAAGTGGGCAGGAGAATGGGC
CTGGAAACGCACAAGCTGGCCTCGCTCTGGAAAGACCAGGCTGTCGTTGAGATCAACATT
GCTGTGATCCATAGTTTTCAGAAGCAGAATGTGACCATCATGGACCACCACTCGGCTGCA
GAATCCTTCATGAAGTACATGCAGAATGAATACCGGTCCCGTGGGGGCTGCCCGGCAGAC
TGGATTTGGCTGGTCCCTCCCATGTCTGGGAGCATCACCCCCGTGTTTCACCAGGAGATG
CTGAACTACGTCCTGTCCCCTTTCTACTACTATCAGGTAGAGGCCTGGAAAACCCATGTC
TGGCAGGACGAGAAGCGGAGACCCAAGAGAAGAGAGATTCCATTGAAAGTCTTGGTCAAA
GCTGTGCTCTTTGCCTGTATGCTGATGCGCAAGACAATGGCGTCCCGAGTCAGAGTCACC
ATCCTCTTTGCGACAGAGACAGGAAAATCAGAGGCGCTGGCCTGGGACCTGGGGGCCTTA
TTCAGCTGTGCCTTCAACCCCAAGGTTGTCTGCATGGATAAGTACAGGCTGAGCTGCCTG
GAGGAGGAACGGCTGCTGTTGGTGGTGACCAGTACGTTTGGCAATGGAGACTGCCCTGGC
AATGGAGAGAAACTGAAGAAATCGCTCTTCATGCTGAAAGAGCTCAACAACAAATTCAGG
TACGCTGTGTTTGGCCTCGGCTCCAGCATGTACCCTCGGTTCTGCGCCTTTGCTCATGAC
ATTGATCAGAAGCTGTCCCACCTGGGGGCCTCTCAGCTCACCCCGATGGGAGAAGGGGAT
GAGCTCAGTGGGCAGGAGGACGCCTTCCGCAGCTGGGCCGTGCAAACCTTCAAGGCAGCC
TGTGAGACGTTTGATGTCCGAGGCAAACAGCACATTCAGATCCCCAAGCTCTACACCTCC
AATGTGACCTGGGACCCGCACCACTACAGGCTCGTGCAGGACTCACAGCCTTTGGACCTC
AGCAAAGCCCTCAGCAGCATGCATGCCAAGAACGTGTTCACCATGAGGCTCAAATCTCGG
CAGAATCTACAAAGTCCGACATCCAGCCGTGCCACCATCCTGGTGGAACTCTCCTGTGAG
GATGGCCAAGGCCTGAACTACCTGCCGGGGGAGCACCTTGGGGTTTGCCCAGGCAACCAG
CCGGCCCTGGTCCAAGGCATCCTGGAGCGAGTGGTGGATGGCCCCACACCCCACCAGACA
GTGCGCCTGGAGGACCTGGATGAGAGTGGCAGCTACTGGGTCAGTGACAAGAGGCTGCCC
CCCTGCTCACTCAGCCAGGCCCTCACCTACTCCCCGGACATCACCACACCCCCAACCCAG
CTGCTGCTCCAAAAGCTGGCCCAGGTGGCCACAGAAGAGCCTGAGAGACAGAGGCTGGAG
GCCCTGTGCCAGCCCTCAGAGTACAGCAAGTGGAAGTTCACCAACAGCCCCACATTCCTG
GAGGTGCTAGAGGAGTTCCCGTCCCTGCGGGTGTCTGCTGGCTTCCTGCTTTCCCAGCTC
CCCATTCTGAAGCCCAGGTTCTACTCCATCAGCTCCTCCCGGGATCACACGCCCACGGAG
ATCCACCTGACTGTGGCCGTGGTCACCTACCACACCGGAGATGGCCAGGGTCCCCTGCAC
CACGGTGTCTGCAGCACATGGCTCAACAGCCTGAAGCCCCAAGACCCAGTGCCCTGCTTT
GTGCGGAATGCCAGCGCCTTCCACCTCCCCGAGGATCCCTCCCATCCTTGCATCCTCATC
GGGCCTGGCACAGGCATCGTGCCCTTCCGCAGTTTCTGGCAGCAACGGCTCCATGACTCC
CAGCACAAGGGAGTGCGGGGAGGCCGCATGACCTTGGTGTTTGGGTGCCGCCGCCCAGAT
GAGGACCACATCTACCAGGAGGAGATGCTGGAGATGGCCCAGAAGGGGGTGCTGCATGCG
GTGCACACAGCCTATTCCCGCCTGCCTGGCAAGCCCAAGGTCTATGTTCAGGACATCCTG
CGGCAGCAGCTGGCCAGCGAGGTGCTCCGTGTGCTCCACAAGGAGCCAGGCCACCTCTAT
GTTTGCGGGGATGTGCGCATGGCCCGGGACGTGGCCCACACCCTGAAGCAGCTGGTGGCT
GCCAAGCTGAAATTGAATGAGGAGCAGGTCGAGGACTATTTCTTTCAGCTCAAGAGCCAG
AAGCGCTATCACGAAGATATCTTCGGTGCTGTATTTCCTTACGAGGCGAAGAAGGACAGG
GTGGCGGTGCAGCCCAGCAGCCTGGAGATGTCAGCGCTCTGA
|
| Enzyme 14 GenBank Gene ID |
L09210  |
| Enzyme 14 GeneCard ID |
NOS2A  |
| Enzyme 14 GenAtlas ID |
NOS2A  |
| Enzyme 14 HGNC ID |
HGNC:7873  |
| Enzyme 14 Chromosome Location |
17 |
| Enzyme 14 Locus |
17q11.2-q12 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Geller DA, Lowenstein CJ, Shapiro RA, Nussler AK, Di Silvio M, Wang SC, Nakayama DK, Simmons RL, Snyder SH, Billiar TR: Molecular cloning and expression of inducible nitric oxide synthase from human hepatocytes. Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3491-5. [PubMed
]
- Sherman PA, Laubach VE, Reep BR, Wood ER: Purification and cDNA sequence of an inducible nitric oxide synthase from a human tumor cell line. Biochemistry. 1993 Nov 2;32(43):11600-5. [PubMed
]
- Charles IG, Palmer RM, Hickery MS, Bayliss MT, Chubb AP, Hall VS, Moss DW, Moncada S: Cloning, characterization, and expression of a cDNA encoding an inducible nitric oxide synthase from the human chondrocyte. Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):11419-23. [PubMed
]
- Maier R, Bilbe G, Rediske J, Lotz M: Inducible nitric oxide synthase from human articular chondrocytes: cDNA cloning and analysis of mRNA expression. Biochim Biophys Acta. 1994 Sep 21;1208(1):145-50. [PubMed
]
- Park CS, Pardhasaradhi K, Gianotti C, Villegas E, Krishna G: Human retina expresses both constitutive and inducible isoforms of nitric oxide synthase mRNA. Biochem Biophys Res Commun. 1994 Nov 30;205(1):85-91. [PubMed
]
- Hokari A, Zeniya M, Esumi H: Cloning and functional expression of human inducible nitric oxide synthase (NOS) cDNA from a glioblastoma cell line A-172. J Biochem (Tokyo). 1994 Sep;116(3):575-81. [PubMed
]
- Guo FH, De Raeve HR, Rice TW, Stuehr DJ, Thunnissen FB, Erzurum SC: Continuous nitric oxide synthesis by inducible nitric oxide synthase in normal human airway epithelium in vivo. Proc Natl Acad Sci U S A. 1995 Aug 15;92(17):7809-13. [PubMed
]
- Luss H, Li RK, Shapiro RA, Tzeng E, McGowan FX, Yoneyama T, Hatakeyama K, Geller DA, Mickle DA, Simmons RL, Billiar TR: Dedifferentiated human ventricular cardiac myocytes express inducible nitric oxide synthase mRNA but not protein in response to IL-1, TNF, IFNgamma, and LPS. J Mol Cell Cardiol. 1997 Apr;29(4):1153-65. [PubMed
]
- McLay JS, Chatterjee P, Nicolson AG, Jardine AG, McKay NG, Ralston SH, Grabowski P, Haites NE, MacLeod AM, Hawksworth GM: Nitric oxide production by human proximal tubular cells: a novel immunomodulatory mechanism? Kidney Int. 1994 Oct;46(4):1043-9. [PubMed
]
- Bloch KD, Wolfram JR, Brown DM, Roberts JD Jr, Zapol DG, Lepore JJ, Filippov G, Thomas JE, Jacob HJ, Bloch DB: Three members of the nitric oxide synthase II gene family (NOS2A, NOS2B, and NOS2C) colocalize to human chromosome 17. Genomics. 1995 Jun 10;27(3):526-30. [PubMed
]
- Taylor BS, Alarcon LH, Billiar TR: Inducible nitric oxide synthase in the liver: regulation and function. Biochemistry (Mosc). 1998 Jul;63(7):766-81. [PubMed
]
- Glynne PA, Darling KE, Picot J, Evans TJ: Epithelial inducible nitric-oxide synthase is an apical EBP50-binding protein that directs vectorial nitric oxide output. J Biol Chem. 2002 Sep 6;277(36):33132-8. Epub 2002 Jun 21. [PubMed
]
- Li H, Raman CS, Glaser CB, Blasko E, Young TA, Parkinson JF, Whitlow M, Poulos TL: Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase. J Biol Chem. 1999 Jul 23;274(30):21276-84. [PubMed
]
- Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC: Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation. Nat Struct Biol. 1999 Mar;6(3):233-42. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
6216 |
| Enzyme 15 Name |
Nitric-oxide synthase, brain |
| Enzyme 15 Synonyms |
- NOS type I
- Neuronal NOS
- N-NOS
- nNOS
- Constitutive NOS
- NC-NOS
- bNOS
|
| Enzyme 15 Gene Name |
NOS1 |
| Enzyme 15 Protein Sequence |
>Nitric-oxide synthase, brain
MEDHMFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQA
GDIILAVNGRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTI
RVTQPLGPPTKAVDLSHQPPAGKEQPLAVDGASGPGNGPQHAYDDGQEAGSLPHANGLAP
RPPGQDPAKKATRVSLQGRGENNELLKEIEPVLSLLTSGSRGVKGGAPAKAEMKDMGIQV
DRDLDGKSHKPLPLGVENDRVFNDLWGKGNVPVVLNNPYSEKEQPPTSGKQSPTKNGSPS
KCPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLF
PLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRC
VGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVW
NSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQ
IPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGV
RDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSAT
ESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHV
WKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCE
IFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVQ
EERKSYKVRFNSVSSYSDSQKSSGDGPDLRDNFESAGPLANVRFSVFGLGSRAYPHFCAF
GHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANN
SLISNDRSWKRNKFRLTFVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFV
RLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGV
ISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEY
EEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIV
SYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAP
FRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSRE
PDKPKKYVQDILQEQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAE
DAGVFISRMRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS
|
| Enzyme 15 Number of Residues |
1434 |
| Enzyme 15 Molecular Weight |
160972 |
| Enzyme 15 Theoretical pI |
7.44 |
| Enzyme 15 GO Classification |
| Function |
- FAD binding
- FMN binding
- NADP binding
- adenyl nucleotide binding
- binding
- calmodulin binding
- catalytic activity
- cation binding
- coenzyme binding
- cofactor binding
- electron transporter activity
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- nitric-oxide synthase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
- protein binding
- purine nucleotide binding
- tetrapyrrole binding
- transition metal ion binding
- transporter activity
|
| Process |
- biosynthesis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- nitric oxide biosynthesis
- physiological process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Inorganic ion transport and metabolism |
| Enzyme 15 Specific Function |
Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter |
| Enzyme 15 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 15 Reactions |
- L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
642526  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P29475  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
NOS1_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>4305 bp
ATGGAGGATCACATGTTCGGTGTTCAGCAAATCCAGCCCAATGTCATTTCTGTTCGTCTC
TTCAAGCGCAAAGTTGGGGGCCTGGGATTTCTGGTGAAGGAGCGGGTCAGTAAGCCGCCC
GTGATCATCTCTGACCTGATTCGTGGGGGCGCCGCAGAGCAGAGTGGCCTCATCCAGGCC
GGAGACATCATTCTTGCGGTCAACGGCCGGCCCTTGGTGGACCTGAGCTATGACAGCGCC
CTGGAGGTACTCAGAGGCATTGCCTCTGAGACCCACGTGGTCCTCATTCTGAGGGGCCCT
GAAGGTTTCACCACGCACCTGGAGACCACCTTTACAGGTGATGGGACCCCCAAGACCATC
CGGGTGACACAGCCCCTGGGTCCCCCCACCAAAGCCGTGGATCTGTCCCACCAGCCACCG
GCCGGCAAAGAACAGCCCCTGGCAGTGGATGGGGCCTCGGGTCCCGGGAATGGGCCTCAG
CATGCCTACGATGATGGGCAGGAGGCTGGCTCACTCCCCCATGCCAACGGCCTGGCCCCC
AGGCCCCCAGGCCAGGACCCCGCGAAGAAAGCAACCAGAGTCAGCCTCCAAGGCAGAGGG
GAGAACAATGAACTGCTCAAGGAGATAGAGCCTGTGCTGAGCCTTCTCACCAGTGGGAGC
AGAGGGGTCAAGGGAGGGGCACCTGCCAAGGCAGAGATGAAAGATATGGGAATCCAGGTG
GACAGAGATTTGGACGGCAAGTCACACAAACCTCTGCCCCTCGGCGTGGAGAACGACCGA
GTCTTCAATGACCTATGGGGGAAGGGCAATGTGCCTGTCGTCCTCAACAACCCATATTCA
GAGAAGGAGCAGCCCCCCACCTCAGGAAAACAGTCCCCCACAAAGAATGGCAGCCCCTCC
AAGTGTCCACGCTTCCTCAAGGTCAAGAACTGGGAGACTGAGGTGGTTCTCACTGACACC
CTCCACCTTAAGAGCACATTGGAAACGGGATGCACTGAGTACATCTGCATGGGCTCCATC
ATGCATCCTTCTCAGCATGCAAGGAGGCCTGAAGACGTCCGCACAAAAGGACAGCTCTTC
CCTCTCGCCAAAGAGTTTATTGATCAATACTATTCATCAATTAAAAGATTTGGCTCCAAA
GCCCACATGGAAAGGCTGGAAGAGGTGAACAAAGAGATCGACACCACTAGCACTTACCAG
CTCAAGGACACAGAGCTCATCTATGGGGCCAAGCACGCCTGGCGGAATGCCTCGCGCTGT
GTGGGCAGGATCCAGTGGTCCAAGCTGCAGGTATTCGATGCCCGTGACTGCACCACGGCC
CACGGGATGTTCAACTACATCTGTAACCATGTCAAGTATGCCACCAACAAAGGGAACCTC
AGGTCTGCCATCACCATATTCCCCCAGAGGACAGACGGCAAGCACGACTTCCGAGTCTGG
AACTCCCAGCTCATCCGCTACGCTGGCTACAAGCAGCCTGACGGCTCCACCCTGGGGGAC
CCAGCCAATGTGCAGTTCACAGAGATATGCATACAGCAGGGCTGGAAACCGCCTAGAGGC
CGCTTCGATGTCCTGCCGCTCCTGCTTCAGGCCAACGGCAATGACCCTGAGCTCTTCCAG
ATTCCTCCAGAGCTGGTGTTGGAAGTTCCCATCAGGCACCCCAAGTTTGAGTGGTTCAAG
GACCTGGGGCTGAAGTGGTACGGCCTCCCCGCCGTGTCCAACATGCTCCTAGAGATTGGC
GGCCTGGAGTTCAGCGCCTGTCCCTTCAGTGGCTGGTACATGGGCACAGAGATTGGTGTC
CGCGACTACTGTGACAACTCCCGCTACAATATCCTGGAGGAAGTGGCCAAGAAGATGAAC
TTAGACATGAGGAAGACGTCCTCCCTGTGGAAGGACCAGGCGCTGGTGGAGATCAATATC
GCGGTTCTCTATAGCTTCCAGAGTGACAAAGTGACCATTGTTGACCATCACTCCGCCACC
GAGTCCTTCATTAAGCACATGGAGAATGAGTACCGCTGCCGGGGGGGCTGCCCTGCCGAC
TGGGTGTGGATCGTGCCCCCCATGTCCGGAAGCATCACCCCTGTGTTCCACCAGGAGATG
CTCAACTACCGGCTCACCCCCTCCTTCGAATACCAGCCTGATCCCTGGAACACGCATGTC
TGGAAAGGCACCAACGGGACCCCCACAAAGCGGCGAGCCATCGGCTTCAAGAAGCTAGCA
GAAGCTGTCAAGTTCTCGGCCAAGCTGATGGGGCAGGCTATGGCCAAGAGGGTGAAAGCG
ACCATCCTCTATGCCACAGAGACAGGCAAATCGCAAGCTTATGCCAAGACCTTGTGTGAG
ATCTTCAAACACGCCTTTGATGCCAAGGTGATGTCCATGGAAGAATATGACATTGTGCAC
CTGGAACATGAAACTCTGGTCCTTGTGGTCACCAGCACCTTTGGCAATGGAGATCCCCCT
GAGAATGGGGAGAAATTCGGCTGTGCTTTGATGGAAATGAGGCACCCCAACTCTGTGCAG
GAAGAAAGGAAGAGCTACAAGGTCCGATTCAACAGCGTCTCCTCCTACTCTGACTCCCAA
AAATCATCAGGCGATGGGCCCGACCTCAGAGACAACTTTGAGAGTGCTGGACCCCTGGCC
AATGTGAGGTTCTCAGTTTTTGGCCTCGGCTCACGAGCATACCCTCACTTTTGCGCCTTC
GGACACGCTGTGGACACCCTCCTGGAAGAACTGGGAGGGGAGAGGATCCTGAAGATGAGG
GAAGGGGATGAGCTCTGTGGGCAGGAAGAGGCTTTCAGGACCTGGGCCAAGAAGGTCTTC
AAGGCAGCCTGTGATGTCTTCTGTGTGGGAGATGATGTCAACATTGAAAAGGCCAACAAT
TCCCTCATCAGCAATGATCGCAGCTGGAAGAGAAACAAGTTCCGCCTCACCTTTGTGGCC
GAAGCTCCAGAACTCACACAAGGTCTATCCAATGTCCACAAAAAGCGAGTCTCAGCTGCC
CGGCTCCTTAGCCGTCAAAACCTCCAGAGCCCTAAATCCAGTCGGTCAACTATCTTCGTG
CGTCTCCACACCAACGGGAGCCAGGAGCTGCAGTACCAGCCTGGGGACCACCTGGGTGTC
TTCCCTGGCAACCACGAGGACCTCGTGAATGCCCTGATCGAGCGGCTGGAGGACGCGCCG
CCTGTCAACCAGATGGTGAAAGTGGAACTGCTGGAGGAGCGGAACACGGCTTTAGGTGTC
ATCAGTAACTGGACAGACGAGCTCCGCCTCCCGCCCTGCACCATCTTCCAGGCCTTCAAG
TACTACCTGGACATCACCACGCCACCAACGCCTCTGCAGCTGCAGCAGTTTGCCTCCCTA
GCTACCAGCGAGAAGGAGAAGCAGCGTCTGCTGGTCCTCAGCAAGGGTTTGCAGGAGTAC
GAGGAATGGAAATGGGGCAAGAACCCCACCATCGTGGAGGTGCTGGAGGAGTTCCCATCT
ATCCAGATGCCGGCCACCCTGCTCCTGACCCAGCTGTCCCTGCTGCAGCCCCGCTACTAT
TCCATCAGCTCCTCCCCAGACATGTACCCTGATGAAGTGCACCTCACTGTGGCCATCGTT
TCCTACCGCACTCGAGATGGAGAAGGACCAATTCACCACGGCGTATGCTCCTCCTGGCTC
AACCGGATACAGGCTGACGAACTGGTCCCCTGTTTCGTGAGAGGAGCACCCAGCTTCCAC
CTGCCCCGGAACCCCCAAGTCCCCTGCATCCTCGTTGGACCAGGCACCGGCATTGCCCCT
TTCCGAAGCTTCTGGCAACAGCGGCAATTTGATATCCAACACAAAGGAATGAACCCCTGC
CCCATGGTCCTGGTCTTCGGGTGCCGGCAATCCAAGATAGATCATATCTACAGGGAAGAG
ACCCTGCAGGCCAAGAACAAGGGGGTCTTCAGAGAGCTGTACACGGCTTACTCCCGGGAG
CCAGACAAACCAAAGAAGTACGTGCAGGACATCCTGCAGGAGCAGCTGGCGGAGTCTGTG
TACCGAGCCCTGAAGGAGCAAGGGGGCCACATATACGTCTGTGGGGACGTCACCATGGCT
GCTGATGTCCTCAAAGCCATCCAGCGCATCATGACCCAGCAGGGGAAGCTCTCGGCAGAG
GACGCCGGCGTATTCATCAGCCGGATGAGGGATGACAACCGATACCATGAGGATATTTTT
GGAGTCACCCTGCGAACGTACGAAGTGACCAACCGCCTTAGATCTGAGTCCATTGCCTTC
ATTGAAGAGAGCAAAAAAGACACCGATGAGGTTTTCAGCTCCTAA
|
| Enzyme 15 GenBank Gene ID |
U17327  |
| Enzyme 15 GeneCard ID |
NOS1  |
| Enzyme 15 GenAtlas ID |
NOS1  |
| Enzyme 15 HGNC ID |
HGNC:7872  |
| Enzyme 15 Chromosome Location |
12 |
| Enzyme 15 Locus |
12q24.2-q24.31 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Hall AV, Antoniou H, Wang Y, Cheung AH, Arbus AM, Olson SL, Lu WC, Kau CL, Marsden PA: Structural organization of the human neuronal nitric oxide synthase gene (NOS1). J Biol Chem. 1994 Dec 30;269(52):33082-90. [PubMed
]
- Fujisawa H, Ogura T, Kurashima Y, Yokoyama T, Yamashita J, Esumi H: Expression of two types of nitric oxide synthase mRNA in human neuroblastoma cell lines. J Neurochem. 1994 Jul;63(1):140-5. [PubMed
]
- Nakane M, Schmidt HH, Pollock JS, Forstermann U, Murad F: Cloned human brain nitric oxide synthase is highly expressed in skeletal muscle. FEBS Lett. 1993 Jan 25;316(2):175-80. [PubMed
]
- Park CS, Gianotti C, Park R, Krishna G: Neuronal isoform of nitric oxide synthase is expressed at low levels in human retina. Cell Mol Neurobiol. 1996 Aug;16(4):499-515. [PubMed
]
- Wang Y, Goligorsky MS, Lin M, Wilcox JN, Marsden PA: A novel, testis-specific mRNA transcript encoding an NH2-terminal truncated nitric-oxide synthase. J Biol Chem. 1997 Apr 25;272(17):11392-401. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
6217 |
| Enzyme 16 Name |
Nitric-oxide synthase, endothelial |
| Enzyme 16 Synonyms |
- EC-NOS
- NOS type III
- NOSIII
- Endothelial NOS
- eNOS
- Constitutive NOS
- cNOS
|
| Enzyme 16 Gene Name |
NOS3 |
| Enzyme 16 Protein Sequence |
>Nitric-oxide synthase, endothelial
MGNLKSVAQEPGPPCGLGLGLGLGLCGKQGPATPAPEPSRAPASLLPPAPEHSPPSSPLT
QPPEGPKFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLQGRPSPGPPAP
EQLLSQARDFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRN
APRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGD
FRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEPP
ELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMST
EIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDH
HAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPW
KGSAAKGTGITRKKTFKEVANAVKISASLMGTVMAKRVKATILYGSETGRAQSYAQQLGR
LFRKAFDPRVLCMDEYDVVSLEHETLVLVVTSTFGNGDPPENGESFAAALMEMSGPYNSS
PRPEQHKSYKIRFNSISCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHF
CAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGWAQAAFQAACETFCVGEDAKAAA
RDIFSPKRSWKRQRYRLSAQAEGLQLLPGLIHVHRRKMFQATIRSVENLQSSKSTRATIL
VRLDTGGQEGLQYQPGDHIGVCPPNRPGLVEALLSRVEDPPAPTEPVAVEQLEKGSPGGP
PPGWVRDPRLPPCTLRQALTFFLDITSPPSPQLLRLLSTLAEEPREQQELEALSQDPRRY
EEWKWFRCPTLLEVLEQFPSVALPAPLLLTQLPLLQPRYYSVSSAPSTHPGEIHLTVAVL
AYRTQDGLGPLHYGVCSTWLSQLKPGDPVPCFIRGAPSFRLPPDPSLPCILVGPGTGIAP
FRGFWQERLHDIESKGLQPTPMTLVFGCRCSQLDHLYRDEVQNAQQRGVFGRVLTAFSRE
PDNPKTYVQDILRTELAAEVHRVLCLERGHMFVCGDVTMATNVLQTVQRILATEGDMELD
EAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERQLRGAVPWAFDPPGSDT
NSP
|
| Enzyme 16 Number of Residues |
1203 |
| Enzyme 16 Molecular Weight |
133290 |
| Enzyme 16 Theoretical pI |
7.27 |
| Enzyme 16 GO Classification |
| Function |
- FMN binding
- binding
- catalytic activity
- monooxygenase activity
- nitric-oxide synthase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
|
| Process |
- biosynthesis
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- nitric oxide biosynthesis
- physiological process
|
| Component |
| — |
|
| Enzyme 16 General Function |
Inorganic ion transport and metabolism |
| Enzyme 16 Specific Function |
Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. No mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets |
| Enzyme 16 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 16 Reactions |
- L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
189212  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P29474  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
NOS3_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>3612 bp
ATGGGCAACTTGAAGAGCGTGGCCCAGGAGCCTGGGCCACCCTGCGGCCTGGGGCTGGGG
CTGGGCCTTGGGCTGTGCGGCAAGCAGGGCCCAGCCACCCCGGCCCCTGAGCCCAGCCGG
GCCCCAGCATCCCTACTCCCACCAGCGCCAGAACACAGCCCCCCGAGCTCCCCGCTAACC
CAGCCCCCAGAGGGGCCCAAGTTCCCTCGTGTGAAGAACTGGGAGGTGGGGAGCATCACC
TATGACACCCTCAGCGCCCAGGCGCAGCAGGATGGGCCCTGCACCCCAAGACGCTGCCTG
GGCTCCCTGGTATTTCCACGGAAACTACAGGGCCGGCCCTCCCCCGGCCCCCCGGCCCCT
GAGCAGCTGCTGAGTCAGGCCCGGGACTTCATCAACCAGTACTACAGCTCCATTAAGAGG
AGCGGCTCCCAGGCCCACGAACAGCGGCTTCAAGAGGTGGAAGCCGAGGTGGCAGCCACA
GGCACCTACCAGCTTAGGGAGAGCGAGCTGGTGTTCGGGGCTAAGCAGGCCTGGCGCAAC
GCTCCCCGCTGCGTGGGCCGGATCCAGTGGGGGAAGCTGCAGGTGTTCGATGCCCGGGAC
TGCAGGTCTGCACAGGAAATGTTCACCTACATCTGCAACCACATCAAGTATGCCACCAAC
CGGGGCAACCTTCGCTCGGCCATCACAGTGTTCCCGCAGCGCTGCCCTGGCCGAGGAGAC
TTCCGAATCTGGAACAGCCAGCTGGTGCGCTACGCGGGCTACCGGCAGCAGGACGGCTCT
GTGCGGGGGGACCCAGCCAACGTGGAGATCACCGAGCTCTGCATTCAGCACGGCTGGACC
CCAGGAAACGGTCGCTTCGACGTGCTGCCCCTGCTGCTGCAGGCCCCAGATGAGCCCCCA
GAACTCTTCCTTCTGCCCCCCGAGCTGGTCCTTGAGGTGCCCCTGGAGCACCCCACGCTG
GAGTGGTTTGCAGCCCTGGGCCTGCGCTGGTACGCCCTCCCGGCAGTGTCCAACATGCTG
CTGGAAATTGGGGGCCTGGAGTTCCCCGCAGCCCCCTTCAGTGGCTGGTACATGAGCACT
GAGATCGGCACGAGGAACCTGTGTGACCCTCACCGCTACAACATCCTGGAGGATGTGGCT
GTCTGCATGGACCTGGATACCCGGACCACCTCGTCCCTGTGGAAAGACAAGGCAGCAGTG
GAAATCAACGTGGCCGTGCTGCACAGTTACCAGCTAGCCAAAGTCACCATCGTGGACCAC
CACGCCGCCACGGCCTCTTTCATGAAGCACCTGGAGAATGAGCAGAAGGCCAGGGGGGGC
TGCCCTGCAGACTGGGCCTGGATCGTGCCCCCCATCTCGGGCAGCCTCACTCCTGTTTTC
CATCAGGAGATGGTCAACTATTTCCTGTCCCCGGCCTTCCGCTACCAGCCAGACCCCTGG
AAGGGGAGTGCCGCCAAGGGCACCGGCATCACCAGGAAGAAGACCTTTAAAGAAGTGGCC
AACGCCGTGAAGATCTCCGCCTCGCTCATGGGCACGGTGATGGCGAAGCGAGTGAAGGCG
ACAATCCTGTATGGCTCCGAGACCGGCCGGGCCCAGAGCTACGCACAGCAGCTGGGGAGA
CTCTTCCGGAAGGCTTTTGATCCCCGGGTCCTGTGTATGGATGAGTATGACGTGGTGTCC
CTCGAACACGAGACGCTGGTGCTGGTGGTAACCAGCACATTTGGGAATGGGGATCCCCCG
GAGAATGGAGAGAGCTTTGCAGCTGCCCTGATGGAGATGTCCGGCCCCTACAACAGCTCC
CCTCGGCCGGAACAGCACAAGAGTTATAAGATCCGCTTCAACAGCATCTCCTGCTCAGAC
CCACTGGTGTCCTCTTGGCGGCGGAAGAGGAAGGAGTCCAGTAACACAGACAGTGCAGGG
GCCCTGGGCACCCTCAGGTTCTGTGTGTTCGGGCTCGGCTCCCGGGCATACCCCCACTTC
TGCGCCTTTGCTCGTGCCGTGGACACACGGCTGGAGGAACTGGGCGGGGAGCGGCTGCTG
CAGCTGGGCCAGGGCGACGAGCTGTGCGGCCAGGAGGAGGCCTTCCGAGGCTGGGCCCAG
GCTGCCTTCCAGGCCGCCTGTGAGACCTTCTGTGTGGGAGAGGATGCCAAGGCCGCCGCC
CGAGACATCTTCAGCCCCAAACGGAGCTGGAAGCGCCAGAGGTACCGGCTGAGCGCCCAG
GCCGAGGGCCTGCAGTTGCTGCCAGGTCTGATCCACGTGCACAGGCGGAAGATGTTCCAG
GCTACAATCCGCTCAGTGGAAAACCTGCAAAGCAGCAAGTCCACGAGGGCCACCATCCTG
GTGCGCCTGGACACCGGAGGCCAGGAGGGGCTGCAGTACCAGCCGGGGGACCACATAGGT
GTCTGCCCGCCCAACCGGCCCGGCCTTGTGGAGGCGCTGCTGAGCCGCGTGGAGGACCCG
CCGGCGCCCACTGAGCCCGTGGCAGTAGAGCAGCTGGAGAAGGGCAGCCCTGGTGGCCCT
CCCCCCGGCTGGGTGCGGGACCCCCGGCTGCCCCCGTGCACGCTGCGCCAGGCTCTCACC
TTCTTCCTGGACATCACCTCCCCACCCAGCCCTCAGCTCTTGCGGCTGCTCAGCACCTTG
GCAGAAGAGCCCAGGGAACAGCAGGAGCTGGAGGCCCTCAGCCAGGATCCCCGACGCTAC
GAGGAGTGGAAGTGGTTCCGCTGCCCCACGCTGCTGGAGGTGCTGGAGCAGTTCCCGTCG
GTGGCGCTGCCTGCCCCACTGCTCCTCACCCAGCTGCCTCTGCTCCAGCCCCGGTACTAC
TCAGTCAGCTCGGCACCCAGCACCCACCCAGGAGAGATCCACCTCACTGTAGCTGTGCTG
GCATACAGGACTCAGGATGGGCTGGGCCCCCTGCACTATGGAGTCTGCTCCACGTGGCTA
AGCCAGCTCAAGCCCGGAGACCCTGTGCCCTGCTTCATCCGGGGGGCTCCCTCCTTCCGG
CTGCCACCCGATCCCAGCTTGCCCTGCATCCTGGTGGGTCCAGGCACTGGCATTGCCCCC
TTCCGGGGATTCTGGCAGGAGCGGCTGCATGACATTGAGAGCAAAGGGCTGCAGCCCACT
CCCATGACTTTGGTGTTCGGCTGCCGATGCTCCCAACTTGACCATCTCTACCGCGACGAG
GTGCAGAACGCCCAGCAGCGCGGGGTGTTTGGCCGAGTCCTCACCGCCTTCTCCCGGGAA
CCTGACAACCCCAAGACCTACGTGCAGGACATCCTGAGGACGGAGCTGGCTGCGGAGGTG
CACCGCGTGCTGTGCCTCGAGCGGGGCCACATGTTTGTCTGCGGCGATGTTACCATGGCA
ACCAACGTCCTGCAGACCGTGCAGCGCATCCTGGCGACGGAGGGCGACATGGAGCTGGAC
GAGGCCGGCGACGTCATCGGCGTGCTGCGGGATCAGCAACGCTACCACGAAGACATTTTC
GGGCTCACGCTGCGCACCCAGGAGGTGACAAGCCGCATACGCACCCAGAGCTTTTCCTTG
CAGGAGCGTCAGTTGCGGGGCGCAGTGCCCTGGGCGTTCGACCCTCCCGGCTCAGACACC
AACAGCCCCTGA
|
| Enzyme 16 GenBank Gene ID |
M93718  |
| Enzyme 16 GeneCard ID |
NOS3  |
| Enzyme 16 GenAtlas ID |
NOS3  |
| Enzyme 16 HGNC ID |
HGNC:7876  |
| Enzyme 16 Chromosome Location |
7 |
| Enzyme 16 Locus |
7q36 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Janssens SP, Shimouchi A, Quertermous T, Bloch DB, Bloch KD: Cloning and expression of a cDNA encoding human endothelium-derived relaxing factor/nitric oxide synthase. J Biol Chem. 1992 Jul 25;267(21):14519-22. [PubMed
]
- Marsden PA, Schappert KT, Chen HS, Flowers M, Sundell CL, Wilcox JN, Lamas S, Michel T: Molecular cloning and characterization of human endothelial nitric oxide synthase. FEBS Lett. 1992 Aug 3;307(3):287-93. [PubMed
]
- Marsden PA, Heng HH, Scherer SW, Stewart RJ, Hall AV, Shi XM, Tsui LC, Schappert KT: Structure and chromosomal localization of the human constitutive endothelial nitric oxide synthase gene. J Biol Chem. 1993 Aug 15;268(23):17478-88. [PubMed
]
- Nadaud S, Bonnardeaux A, Lathrop M, Soubrier F: Gene structure, polymorphism and mapping of the human endothelial nitric oxide synthase gene. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1027-33. [PubMed
]
- Miyahara K, Kawamoto T, Sase K, Yui Y, Toda K, Yang LX, Hattori R, Aoyama T, Yamamoto Y, Doi Y, et al.: Cloning and structural characterization of the human endothelial nitric-oxide-synthase gene. Eur J Biochem. 1994 Aug 1;223(3):719-26. [PubMed
]
- Robinson LJ, Weremowicz S, Morton CC, Michel T: Isolation and chromosomal localization of the human endothelial nitric oxide synthase (NOS3) gene. Genomics. 1994 Jan 15;19(2):350-7. [PubMed
]
- Sase K, Michel T: Expression of constitutive endothelial nitric oxide synthase in human blood platelets. Life Sci. 1995;57(22):2049-55. [PubMed
]
- Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC: Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation. Nat Struct Biol. 1999 Mar;6(3):233-42. [PubMed
]
- Rosenfeld RJ, Garcin ED, Panda K, Andersson G, Aberg A, Wallace AV, Morris GM, Olson AJ, Stuehr DJ, Tainer JA, Getzoff ED: Conformational changes in nitric oxide synthases induced by chlorzoxazone and nitroindazoles: crystallographic and computational analyses of inhibitor potency. Biochemistry. 2002 Nov 26;41(47):13915-25. [PubMed
]
- Yoshimura M, Yasue H, Nakayama M, Shimasaki Y, Sumida H, Sugiyama S, Kugiyama K, Ogawa H, Ogawa Y, Saito Y, Miyamoto Y, Nakao K: A missense Glu298Asp variant in the endothelial nitric oxide synthase gene is associated with coronary spasm in the Japanese. Hum Genet. 1998 Jul;103(1):65-9. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
6348 |
| Enzyme 17 Name |
Riboflavin kinase |
| Enzyme 17 Synonyms |
- ATP:riboflavin 5'-phosphotransferase
- Flavokinase
|
| Enzyme 17 Gene Name |
RFK |
| Enzyme 17 Protein Sequence |
>Riboflavin kinase
MPRADCIMRHLPYFCRGQVVRGFGRGSKQLGIPTANFPEQVVDNLPADISTGIYYGWASV
GSGDVHKMVVSIGWNPYYKNTKKSMETHIMHTFKEDFYGEILNVAIVGYLRPEKNFDSLE
SLISAIQGDIEEAKKRLELPEHLKIKEDNFFQVSKSKIMNGH
|
| Enzyme 17 Number of Residues |
162 |
| Enzyme 17 Molecular Weight |
18410 |
| Enzyme 17 Theoretical pI |
8.22 |
| Enzyme 17 GO Classification |
| Function |
- catalytic activity
- kinase activity
- riboflavin kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolism
- metabolism
- physiological process
- riboflavin and derivative metabolism
- riboflavin biosynthesis
- riboflavin metabolism
- vitamin metabolism
- water-soluble vitamin metabolism
|
| Component |
| — |
|
| Enzyme 17 General Function |
Coenzyme transport and metabolism |
| Enzyme 17 Specific Function |
Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN) |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- ATP + riboflavin = ADP + FMN
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
7023634  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q969G6  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
RIFK_HUMAN  |
| Enzyme 17 PDB ID |
1Q9S  |
| Enzyme 17 PDB File |
Show |
| Enzyme 17 3D Structure |
|
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>489 bp
ATGCCCCGAGCGGACTGCATTATGAGGCACCTGCCTTACTTCTGCCGGGGTCAAGTGGTG
CGGGGCTTCGGCCGCGGCTCCAAGCAGCTGGGCATCCCCACAGCTAATTTTCCTGAGCAA
GTGGTAGATAATCTTCCAGCTGATATATCCACTGGTATTTACTATGGTTGGGCCAGTGTT
GGAAGTGGAGATGTCCATAAGATGGTGGTGAGCATAGGATGGAACCCATATTACAAGAAT
ACGAAGAAGTCTATGGAAACACATATCATGCATACCTTCAAAGAGGACTTCTATGGGGAA
ATCCTCAGTGTGGCCATTGTTGGCTACCTGAGACCAGAAAAGAACTTTGATTCTTTAGAG
TCACTTATTTCAGCAATTCAAGGTGATATTGAAGAAGCTAAGAAACGACTAGAGTTACCA
GAACATTTGAAAATCAAAGAAGACAATTTCTTCCAGGTTTCTAAAAGCAAAATAATGAAT
GGCCACTGA
|
| Enzyme 17 GenBank Gene ID |
AK002011  |
| Enzyme 17 GeneCard ID |
RFK  |
| Enzyme 17 GenAtlas ID |
RFK  |
| Enzyme 17 HGNC ID |
HGNC:30324  |
| Enzyme 17 Chromosome Location |
9 |
| Enzyme 17 Locus |
9q21.13 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Karthikeyan S, Zhou Q, Mseeh F, Grishin NV, Osterman AL, Zhang H: Crystal structure of human riboflavin kinase reveals a beta barrel fold and a novel active site arch. Structure. 2003 Mar;11(3):265-73. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
8658 |
| Enzyme 18 Name |
Phosphopantothenoylcysteine decarboxylase |
| Enzyme 18 Synonyms |
- PPC-DC
- CoaC
|
| Enzyme 18 Gene Name |
PPCDC |
| Enzyme 18 Protein Sequence |
>Phosphopantothenoylcysteine decarboxylase
MEPKASCPAAAPLMERKFHVLVGVTGSVAALKLPLLVSKLLDIPGLEVAVVTTERAKHFY
SPQDIPVTLYSDADEWEMWKSRSDPVLHIDLRRWADLLLVAPLDANTLGKVASGICDNLL
TCVMRAWDRSKPLLFCPAMNTAMWEHPITAQQVDQLKAFGYVEIPCVAKKLVCGDEGLGA
MAEVGTIVDKVKEVLFQHSGFQQS
|
| Enzyme 18 Number of Residues |
204 |
| Enzyme 18 Molecular Weight |
22413 |
| Enzyme 18 Theoretical pI |
6.01 |
| Enzyme 18 GO Classification |
Not Available |
| Enzyme 18 General Function |
Coenzyme transport and metabolism |
| Enzyme 18 Specific Function |
Necessary for the biosynthesis of coenzyme A. Catalyzes the decarboxylation of 4-phosphopantothenoylcysteine to form 4'- phosphopantotheine |
| Enzyme 18 Pathways |
- Pantothenate and CoA Biosynthesis (map00770
)
|
| Enzyme 18 Reactions |
- N-[(R)-4'-phosphopantothenoyl]-L-cysteine = pantotheine 4'-phosphate + CO2
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
Not Available |
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
10197638  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q96CD2  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
COAC_HUMAN  |
| Enzyme 18 PDB ID |
1QZU  |
| Enzyme 18 PDB File |
Show |
| Enzyme 18 3D Structure |
|
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>384 bp
ATGTGGAAGAGCCGCTCTGACCCAGTTCTGCACATTGACCTGCGGAGGTGGGCAGACCTC
CTGCTGGTGGCTCCTCTTGATGCCAACACTCTGGGGAAGGTGGCCAGTGGCATCTGTGAC
AACTTGCTTACCTGCGTCATGCGGGCCTGGGACCGCAGCAAGCCCCTGCTCTTCTGCCCG
GCCATGAACACCGCCATGTGGGAGCACCCGATCACAGCGCAGCAGGTAGACCAGCTCAAG
GCCTTTGGCTATGTCGAGATCCCCTGTGTGGCCAAGAAGCTGGTGTGCGGAGATGAAGGT
CTCGGGGCCATGGCTGAAGTGGGGACCATCGTGGACAAAGTGAAAGAAGTCCTCTTCCAG
CACAGTGGCTTCCAGCAGAGTTGA
|
| Enzyme 18 GenBank Gene ID |
AF182419  |
| Enzyme 18 GeneCard ID |
PPCDC  |
| Enzyme 18 GenAtlas ID |
PPCDC  |
| Enzyme 18 HGNC ID |
HGNC:28107  |
| Enzyme 18 Chromosome Location |
15 |
| Enzyme 18 Locus |
15q24.2 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- 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
]
- Daugherty M, Polanuyer B, Farrell M, Scholle M, Lykidis A, de Crecy-Lagard V, Osterman A: Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics. J Biol Chem. 2002 Jun 14;277(24):21431-9. Epub 2002 Mar 28. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
12937 |
| Enzyme 19 Name |
Lysophosphatidic acid phosphatase type 6 precursor |
| Enzyme 19 Synonyms |
- Acid phosphatase 6, lysophosphatidic
- Acid phosphatase-like protein 1
- PACPL1
|
| Enzyme 19 Gene Name |
ACP6 |
| Enzyme 19 Protein Sequence |
>Lysophosphatidic acid phosphatase type 6 precursor
MITGVFSMRLWTPVGVLTSLAYCLHQRRVALAELQEADGQCPVDRSLLKLKMVQVVFRHG
ARSPLKPLPLEEQVEWNPQLLEVPPQTQFDYTVTNLAGGPKPYSPYDSQYHETTLKGGMF
AGQLTKVGMQQMFALGERLRKNYVEDIPFLSPTFNPQEVFIRSTNIFRNLESTRCLLAGL
FQCQKEGPIIIHTDEADSEVLYPNYQSCWSLRQRTRGRRQTASLQPGISEDLKKVKDRMG
IDSSDKVDFFILLDNVAAEQAHNLPSCPMLKRFARMIEQRAVDTSLYILPKEDRESLQMA
VGPFLHILESNLLKAMDSATAPDKIRKLYLYAAHDVTFIPLLMTLGIFDHKWPPFAVDLT
MELYQHLESKEWFVQLYYHGKEQVPRGCPDGLCPLDMFLNAMSVYTLSPEKYHALCSQTQ
VMEVGNEE
|
| Enzyme 19 Number of Residues |
428 |
| Enzyme 19 Molecular Weight |
48887 |
| Enzyme 19 Theoretical pI |
6.44 |
| Enzyme 19 GO Classification |
| Function |
- acid phosphatase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 19 General Function |
Not Available |
| Enzyme 19 Specific Function |
Hydrolyzes lysophosphatidic acid to monoacylglycerol |
| Enzyme 19 Pathways |
- gamma-Hexachlorocyclohexane Degradation (map00361
)
- Riboflavin Metabolism (map00740
)
- Two-component system - General (map02020
)
|
| Enzyme 19 Reactions |
- a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626] ALL_REAC R00626 > R00548 R03024
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
6691475  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9NPH0  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
PPA6_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
Not Available |
| Enzyme 19 GenBank Gene ID |
AB031478  |
| Enzyme 19 GeneCard ID |
Q9NPH0  |
| Enzyme 19 GenAtlas ID |
ACP6  |
| Enzyme 19 HGNC ID |
HGNC:29609  |
| Enzyme 19 Chromosome Location |
Not Available |
| Enzyme 19 Locus |
Not Available |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Hiroyama M, Takenawa T: Isolation of a cDNA encoding human lysophosphatidic acid phosphatase that is involved in the regulation of mitochondrial lipid biosynthesis. J Biol Chem. 1999 Oct 8;274(41):29172-80. [PubMed
]
- Takayama I, Daigo Y, Ward SM, Sanders KM, Walker RL, Horowitz B, Yamanaka T, Fujino MA: Novel human and mouse genes encoding an acid phosphatase family member and its downregulation in W/W(V) mouse jejunum. Gut. 2002 Jun;50(6):790-6. [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
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
13058 |
| Enzyme 20 Name |
Growth-inhibiting protein 16 |
| Enzyme 20 Synonyms |
- Hydroxyacid oxidase 2
- Long chain, isoform CRA_b
|
| Enzyme 20 Gene Name |
GIG16 |
| Enzyme 20 Protein Sequence |
>Growth-inhibiting protein 16
MSLVCLTDFQAHAREQLSKSTRDFIEGGADDSITRDDNIAAFKRIRLRPRYLRDVSEVDT
RTTIQGEEISAPICIAPTGFHCLVWPDGEMSTARAAQAAGICYITSTFASCSLEDIVIAA
PEGLRWFQLYVHPDLQLNKQLIQRVESLGFKALVITLDTPVCGNRRHDIRNQLRRNLTLT
DLQSPKKGNAIPYFQMTPISTSLCWNDLSWFQSITRLPIILKGILTKEDAELAVKHNVQG
IIVSNHGGRQLDEVLASIDALTEVVAAVKGKIEVYLDGGVRTGNDVLKALALGAKCIFLG
RPILWGLACKGEHGVKEVLNILTNEFHTSMALTGCRSVAEINRNLVQFSRL
|
| Enzyme 20 Number of Residues |
351 |
| Enzyme 20 Molecular Weight |
38839 |
| Enzyme 20 Theoretical pI |
7.69 |
| Enzyme 20 GO Classification |
| Function |
- FMN binding
- binding
- catalytic activity
- nucleotide binding
- oxidoreductase activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 20 General Function |
Energy production and conversion |
| 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 |
46981963  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q2TU86  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
Q2TU86_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
Not Available |
| Enzyme 20 GenBank Gene ID |
AY513277  |
| Enzyme 20 GeneCard ID |
Q2TU86  |
| Enzyme 20 GenAtlas ID |
GIG16  |
| Enzyme 20 HGNC ID |
HGNC:4810  |
| 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 |
13102 |
| Enzyme 21 Name |
FAD synthetase |
| Enzyme 21 Synonyms |
- FMN adenylyltransferase
- FAD pyrophosphorylase
- Flavin adenine dinucleotide synthetase[Includes: Molybdenum cofactor biosynthesis protein-like region
- FAD synthetase region]
|
| Enzyme 21 Gene Name |
FLAD1 |
| Enzyme 21 Protein Sequence |
>FAD synthetase
MGWDLGTRLFQRQEQRSRLSRIWLEKTRVFLEGSTRTPALPHCLFWLLQVPSTQDPLFPG
YGPQCPVDLAGPPCLRPLFGGLGGYWRALQRGREGRTMTSRASELSPGRSVTAGIIIVGD
EILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIG
PTHDDVTFEAVAQAFGDELKPHPKLEAATKALGGEGWEKLSLVPSSARLHYGTDPCTGQP
FRFPLVSVRNVYLFPGIPELLRRVLEGMKGLFQNPAVQFHSKELYVAADEASIAPILAEA
QAHFGRRLGLGSYPDWGSNYYQVKLTLDSEEEGPLEECLAYLTARLPQGSLVPYMPNAVE
QASEAVYKLAESGSSLGKKVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLHLFHAAV
QRKLPDVPNPLQILYIRSISPFPELEQFLQDTIKRYNLQMLEAEGSMKQALGELQARHPQ
LEAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFLRQLFVPYCILY
DRGYTSLGSRENTVRNPALKCLSPGGHPTYRPAYLLENEEEERNSRT
|
| Enzyme 21 Number of Residues |
587 |
| Enzyme 21 Molecular Weight |
65266 |
| Enzyme 21 Theoretical pI |
6.92 |
| Enzyme 21 GO Classification |
| Function |
- amine binding
- amino acid binding
- binding
- carboxyl- and carbamoyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- Mo-molybdopterin cofactor biosynthesis
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- coenzyme biosynthesis
- coenzyme metabolism
- cofactor metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 21 General Function |
Not Available |
| Enzyme 21 Specific Function |
Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- ATP + FMN = diphosphate + FAD [RN:R00161] ALL_REAC R00161
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
91805307  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q8NFF5  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
FAD1_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
Not Available |
| Enzyme 21 GenBank Gene ID |
DQ458779  |
| Enzyme 21 GeneCard ID |
Q8NFF5  |
| Enzyme 21 GenAtlas ID |
FLAD1  |
| Enzyme 21 HGNC ID |
HGNC:24671  |
| Enzyme 21 Chromosome Location |
Not Available |
| Enzyme 21 Locus |
Not Available |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
13990 |
| Enzyme 22 Name |
NADPH-dependent FMN and FAD containing oxidoreductase |
| Enzyme 22 Synonyms |
- NADPH dependent diflavin oxidoreductase 1
- cDNA FLJ75288, highly similar to Homo sapiens NADPH dependent diflavin oxidoreductase 1
- NDOR1, mRNA
|
| Enzyme 22 Gene Name |
NR1 |
| Enzyme 22 Protein Sequence |
>NADPH-dependent FMN and FAD containing oxidoreductase
MPSPQLLVLFGSQTGTAQDVSERLGREARRRRLGCRVQALDSYPVVNLINEPLVIFVCAT
TGQGDPPDNMKNFWRFIFRKNLPSTALCQMDFAVLGLGDSSYAKFNFVAKKLHRRLLQLG
GSALLPVCLGDDQHELGPDAAVDPWLRDLWDRVLGLYPPPPGLTEIPPGVPLPSKFTLLF
LQEAPSTGSEGQRVAHPGSQEPPSESKPFLAPMISNQRVTGPSHFQDVRLIEFDILGSGI
SFAAGDVVLIQPSNSAAHVQRFCQVLGLDPDQLFMLQPREPDVSSPTRLPQPCSMRHLVS
HYLDIASVPRRSFFELLACLSLHELEREKLLEFSSAQGQEELFEYCNRPRRTILEVLCDF
PHTAAAIPPDYLLDLIPVIRPRAFSIASSLLTHPSRLQILVAVVQFQTRLKEPRRGLCSS
WLASLDPGQGPVRVPLWVRPGSLAFPETPDTPVIMVGPGTGVAPFRAAIQERVAQGQTGN
FLFFGCRWRDQDFYWEAEWQELEKRDCLTLIPAFSREQEQKVYVQHRLRELGSLVWELLD
RQGAYFYLAGNAKSMPADVSEALMSIFQEEGGLCSPDAAAYLARLQQTRRFQTETWA
|
| Enzyme 22 Number of Residues |
597 |
| Enzyme 22 Molecular Weight |
66763 |
| Enzyme 22 Theoretical pI |
6.30 |
| Enzyme 22 GO Classification |
| Function |
- FMN binding
- binding
- catalytic activity
- electron transporter activity
- nucleotide binding
- oxidoreductase activity
- transporter activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 22 General Function |
Inorganic ion 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 |
6694369  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q9UHB4  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
Q9UHB4_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>1794 bp
ATGCCGAGCCCGCAGCTTCTGGTGCTCTTCGGCAGCCAGACAGGCACGGCTCAGGATGTG
TCGGAGAGACTGGGTCGCGAGGCCCGGCGCCGGCGGCTTGGCTGCCGGGTGCAGGCCCTG
GACTCCTACCCGGTGGTGAATCTGATTAACGAGCCCCTGGTGATATTTGTTTGTGCAACT
ACAGGCCAAGGAGACCCCCCTGACAACATGAAGAACTTCTGGAGGTTTATATTCCGGAAG
AACCTGCCCTCCACTGCCCTCTGTCAGATGGACTTTGCCGTCCTGGGCCTCGGGGACTCC
TCATACGCCAAGTTCAACTTCGTGGCCAAGAAGCTGCACCGACGGCTACTGCAGCTTGGG
GGCAGCGCCCTCCTGCCCGTGTGCCTGGGCGATGACCAGCATGAGCTGGGGCCCGACGCT
GCTGTGGACCCCTGGCTGCGAGACTTGTGGGACAGGGTTCTGGGGCTGTACCCGCCGCCT
CCGGGCCTCACTGAGATCCCTCCCGGAGTCCCCCTGCCCTCCAAGTTCACCCTGCTGTTC
CTCCAAGAGGCACCCAGCACGGGCTCTGAGGGGCAGCGGGTAGCTCACCCCGGCTCTCAG
GAGCCCCCGTCAGAGTCGAAGCCCTTCCTAGCACCCATGATCTCCAACCAGAGAGTCACC
GGCCCCTCCCACTTCCAGGACGTTCGGCTGATTGAGTTTGACATCTTGGGCTCTGGCATC
AGCTTTGCTGCTGGTGATGTGGTGCTGATTCAGCCCTCCAACTCGGCTGCCCATGTCCAG
CGGTTCTGCCAGGTGCTGGGCCTGGACCCTGACCAGCTCTTCATGCTGCAGCCGCGGGAG
CCAGATGTCTCCTCCCCCACGAGGCTGCCCCAGCCCTGCTCCATGCGGCACCTCGTGTCC
CACTACCTGGACATCGCCAGCGTGCCTCGCCGCTCCTTCTTCGAACTCCTGGCCTGTCTA
TCCCTCCATGAGCTGGAGCGGGAGAAGCTGCTGGAGTTCAGTTCTGCCCAAGGCCAGGAG
GAGCTCTTTGAATACTGCAACCGGCCCCGCAGGACCATCCTGGAGGTGCTCTGTGACTTC
CCGCACACAGCTGCCGCCATCCCTCCCGACTACCTGTTGGACCTCATCCCCGTTATCCGG
CCGAGGGCCTTCTCCATCGCCTCCTCGCTGCTGACTCACCCCTCACGGCTGCAGATCCTC
GTGGCTGTAGTGCAGTTCCAGACTCGCCTCAAGGAGCCCCGCCGGGGCCTCTGCTCCTCC
TGGCTGGCATCCCTGGACCCTGGGCAAGGACCTGTCCGGGTGCCCCTCTGGGTGCGGCCT
GGGAGTCTGGCCTTCCCAGAGACACCAGACACACCTGTGATCATGGTGGGGCCTGGCACT
GGGGTAGCCCCCTTCCGAGCAGCCATCCAGGAGCGTGTGGCCCAGGGCCAGACTGGAAAC
TTCTTGTTTTTTGGCTGCCGCTGGCGGGACCAAGACTTCTACTGGGAGGCTGAGTGGCAG
GAGCTGGAGAAGCGGGACTGTCTGACCCTCATCCCTGCCTTCTCCCGGGAACAGGAGCAG
AAAGTATATGTGCAGCACCGGCTCCGGGAGCTGGGGTCGCTTGTGTGGGAACTGCTGGAC
CGCCAGGGTGCATACTTCTACCTGGCAGGCAACGCCAAGTCCATGCCAGCGGACGTCTCG
GAAGCCCTGATGTCCATCTTCCAGGAGGAGGGTGGACTCTGCAGCCCGGACGCAGCCGCG
TATCTAGCCAGGCTCCAGCAGACACGGCGCTTCCAGACAGAGACGTGGGCCTGA
|
| Enzyme 22 GenBank Gene ID |
AF199509  |
| Enzyme 22 GeneCard ID |
Q9UHB4  |
| Enzyme 22 GenAtlas ID |
NDOR1  |
| Enzyme 22 HGNC ID |
HGNC:29838  |
| Enzyme 22 Chromosome Location |
Not Available |
| Enzyme 22 Locus |
Not Available |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Paine MJ, Garner AP, Powell D, Sibbald J, Sales M, Pratt N, Smith T, Tew DG, Wolf CR: Cloning and characterization of a novel human dual flavin reductase. J Biol Chem. 2000 Jan 14;275(2):1471-8. [PubMed
]
- 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 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
14007 |
| Enzyme 23 Name |
Iodotyrosine dehalogenase 1 precursor |
| Enzyme 23 Synonyms |
- IYD-1
|
| Enzyme 23 Gene Name |
IYD |
| Enzyme 23 Protein Sequence |
>Iodotyrosine dehalogenase 1 precursor
MYFLTPILVAILCILVVWIFKNADRSMEKKKGEPRTRAEARPWVDEDLKDSSDLHQAEED
ADEWQESEENVEHIPFSHNHYPEKEMVKRSQEFYELLNKRRSVRFISNEQVPMEVIDNVI
RTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINYMKRMGHRWVTDLKKLRTNW
IKEYLDTAPILILIFKQVHGFAANGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTP
LNCGPRLRVLLGRPAHEKLLMLLPVGYPSKEATVPDLKRKPLDQIMVTV
|
| Enzyme 23 Number of Residues |
289 |
| Enzyme 23 Molecular Weight |
33360 |
| Enzyme 23 Theoretical pI |
7.71 |
| Enzyme 23 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 23 General Function |
Energy production and conversion |
| Enzyme 23 Specific Function |
Catalyzes the oxidative NADPH-dependent deiodination of monoiodotyrosine (L-MIT) or diiodotyrosine (L-DIT). Acts during the hydrolysis of thyroglobulin to liberate iodide, which can then reenter the hormone-producing pathways. Acts more efficiently on monoiodotyrosine than on diiodotyrosine |
| Enzyme 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
Not Available |
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
31322698  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q6PHW0  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
IYD1_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>870 bp
ATGTATTTCCTGACTCCCATCTTGGTAGCCATTCTCTGCATTTTGGTTGTGTGGATCTTT
AAAAATGCCGACAGAAGCATGGAGAAAAAGAAGGGGGAGCCTAGAACCAGGGCCGAAGCT
CGCCCCTGGGTGGATGAAGACTTAAAAGACAGCAGTGACCTGCACCAAGCAGAAGAAGAT
GCTGATGAATGGCAAGAATCAGAAGAAAATGTTGAACACATCCCCTTCTCTCATAACCAC
TATCCTGAGAAGGAAATGGTTAAGAGGTCTCAGGAATTTTATGAACTTCTCAATAAGAGA
CGGTCAGTCAGGTTCATAAGTAATGAGCAAGTCCCAATGGAAGTCATTGATAATGTCATC
AGAACGGCAGGAACAGCCCCGAGTGGGGCTCACACAGAGCCCTGGACCTTCGTGGTTGTG
AAGGACCCAGACGTGAAGCACAAGATTCGAAAGATCATTGAGGAGGAAGAGGAGATCAAC
TACATGAAAAGGATGGGACATCGCTGGGTCACAGACCTCAAGAAACTGAGAACCAACTGG
ATTAAAGAGTACTTGGATACTGCCCCTATTTTGATTCTCATTTTCAAACAAGTACATGGT
TTCGCCGCAAATGGCAAGAAAAAAGTCCACTACTACAATGAGATCAGTGTTTCCATCGCT
TGTGGCATCCTGCTAGCTGCCCTGCAGAATGCAGGTCTGGTGACTGTCACTACCACTCCT
CTCAACTGTGGCCCTCGACTGAGGGTGCTCCTGGGCCGCCCCGCACATGAAAAGCTGCTG
ATGCTGCTCCCCGTGGGGTACCCCAGCAAGGAGGCCACGGTGCCTGACCTCAAGCGCAAA
CCTCTGGACCAGATCATGGTGACAGTGTAG
|
| Enzyme 23 GenBank Gene ID |
AY259176  |
| Enzyme 23 GeneCard ID |
Q6PHW0  |
| Enzyme 23 GenAtlas ID |
IYD  |
| Enzyme 23 HGNC ID |
HGNC:21071  |
| Enzyme 23 Chromosome Location |
Not Available |
| Enzyme 23 Locus |
Not Available |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
14008 |
| Enzyme 24 Name |
tRNA wybutosine-synthesizing protein 1 homolog |
| Enzyme 24 Synonyms |
- tRNA-yW-synthesizing protein
- Radical S-adenosyl methionine and flavodoxin domain- containing protein 1
|
| Enzyme 24 Gene Name |
TYW1 |
| Enzyme 24 Protein Sequence |
>tRNA wybutosine-synthesizing protein 1 homolog
MDPSADTWDLFSPLISLWINRFYIYLGFAVSISLWICVQIVIKTQGKNLQEKSVPKAAQD
LMTNGYVSLQEKDIFVSGVKIFYGSQTGTAKGFATVLAEAVTSLDLPVAIINLKEYDPDD
HLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFRFGKTYLKGMRYAVFGLG
NSAYASHFNKVGKNVDKWLWMLGAHRVMSRGEGDCDVVKSKHGSIEADFRAWKTKFISQL
QALQKGERKKSCGGHCKKGKCESHQHGSEEREEGSHEQDELHHRDTEEEEPFESSSEEEF
GGEDHQSLNSIVDVEDLGKIMDHVKKEKREKEQQEEKSGLFRNMGRNEDGERRAMITPAL
REALTKQGYQLIGSHSGVKLCRWTKSMLRGRGGCYKHTFYGIESHRCMETTPSLACANKC
VFCWRHHTNPVGTEWRWKMDQPEMILKEAIENHQNMIKQFKGVPGVKAERFEEGMTVKHC
ALSLVGEPIMYPEINRFLKLLHQCKISSFLVTNAQFPAEIRNLEPVTQLYVSVDASTKDS
LKKIDRPLFKDFWQRFLDSLKALAVKQQRTVYRLTLVKAWNVDELQAYAQLVSLGNPDFI
EVKGVTYCGESSASSLTMAHVPWHEEVVQFVHELVDLIPEYEIACEHEHSNCLLIAHRKF
KIGGEWWTWIDYNRFQELIQEYEDSGGSKTFSAKDYMARTPHWALFGASERGFDPKDTRH
QRKNKSKAISGC
|
| Enzyme 24 Number of Residues |
732 |
| Enzyme 24 Molecular Weight |
83703 |
| Enzyme 24 Theoretical pI |
6.87 |
| Enzyme 24 GO Classification |
| Function |
- FMN binding
- binding
- catalytic activity
- cation binding
- electron transporter activity
- ion binding
- iron ion binding
- nucleotide binding
- oxidoreductase activity
- transition metal ion binding
- transporter activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 24 General Function |
Energy production and conversion |
| Enzyme 24 Specific Function |
Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA |
| Enzyme 24 Pathways |
Not Available |
| Enzyme 24 Reactions |
Not Available |
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
7023232  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q9NV66  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
TYW1_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>2199 bp
ATGGATCCTTCTGCGGATACATGGGACCTCTTCTCACCTTTAATATCATTATGGATAAAC
AGGTTTTACATTTATTTGGGCTTTGCTGTTAGCATTAGCCTTTGGATTTGTGTCCAGATT
GTCATCAAGACGCAGGGCAAGAACTTACAGGAAAAATCTGTTCCAAAAGCAGCTCAGGAT
TTGATGACAAATGGTTATGTCTCCCTTCAAGAGAAAGACATCTTTGTGTCTGGAGTGAAG
ATTTTTTATGGTTCTCAGACTGGAACAGCAAAGGGATTCGCAACAGTTCTTGCTGAAGCA
GTTACATCCCTGGATCTGCCTGTGGCCATTATTAATCTAAAAGAATATGATCCAGATGAT
CATCTGATAGAAGAGGTGACTAGTAAAAATGTCTGTGTCTTCCTGGTTGCGACATACACT
GACGGCCTACCAACTGAAAGTGCAGAGTGGTTCTGCAAATGGTTAGAGGAAGCATCCATT
GATTTTCGATTTGGCAAAACTTACCTGAAGGGTATGAGATATGCGGTATTTGGCCTGGGA
AATTCTGCCTATGCTAGCCACTTCAACAAGGTTGGCAAAAATGTTGACAAGTGGCTCTGG
ATGCTTGGCGCGCATCGTGTGATGAGTCGAGGGGAGGGCGACTGCGACGTGGTTAAAAGC
AAGCACGGCAGCATTGAGGCCGACTTCAGAGCATGGAAGACCAAGTTCATCTCCCAGCTG
CAGGCACTTCAGAAAGGGGAGAGAAAGAAGTCCTGTGGCGGCCACTGCAAGAAAGGCAAA
TGTGAATCTCACCAACATGGCTCAGAGGAGAGGGAGGAAGGATCTCATGAGCAGGATGAA
TTGCATCATAGAGACACCGAGGAGGAAGAACCCTTTGAGAGCTCCAGTGAAGAAGAGTTT
GGTGGTGAGGACCATCAGAGCCTAAATTCCATTGTTGATGTTGAAGATTTGGGCAAAATT
ATGGATCATGTGAAGAAAGAAAAGAGAGAAAAGGAACAGCAGGAAGAGAAGTCTGGTTTG
TTCAGGAACATGGGGAGGAATGAAGATGGTGAAAGAAGAGCTATGATAACTCCTGCTCTC
CGAGAAGCCCTTACTAAACAAGGTTATCAGTTGATTGGGAGCCACTCGGGGGTGAAGCTT
TGCAGGTGGACAAAGTCCATGCTCCGAGGGAGAGGAGGTTGTTACAAACACACATTCTAT
GGAATTGAGAGCCATCGCTGCATGGAAACCACCCCGAGCTTGGCGTGTGCTAATAAATGT
GTCTTCTGTTGGCGGCACCACACCAACCCCGTGGGCACTGAGTGGCGGTGGAAGATGGAC
CAGCCTGAAATGATCTTGAAGGAAGCCATTGAAAACCATCAGAACATGATTAAGCAGTTT
AAAGGAGTACCGGGCGTCAAAGCAGAACGCTTTGAAGAAGGAATGACGGTAAAGCACTGT
GCATTGTCCCTCGTGGGAGAACCAATAATGTACCCAGAGATCAACAGGTTTTTGAAGCTA
CTCCACCAGTGTAAAATTTCCAGCTTCCTGGTCACAAACGCACAATTTCCTGCGGAAATC
AGGAACCTCGAGCCGGTTACTCAGCTGTATGTCAGTGTGGATGCCAGTACCAAAGACAGC
CTGAAGAAAATCGACCGCCCACTCTTCAAGGATTTCTGGCAGAGATTCCTTGACAGTTTA
AAAGCCTTGGCAGTCAAGCAACAACGAACTGTCTACAGACTGACGCTCGTGAAAGCATGG
AATGTGGACGAGCTCCAGGCCTACGCGCAGCTCGTGTCCCTGGGAAATCCTGACTTCATC
GAAGTGAAGGGCGTTACCTACTGCGGAGAAAGTTCAGCAAGCAGTCTTACCATGGCCCAC
GTGCCCTGGCATGAGGAAGTGGTACAGTTTGTCCGCGAGCTGGTGGATCTGATCCCCGAA
TATGAAATTGCATGTGAACACGAACACTCTAATTGCCTCCTGATAGCACACAGAAAGTTT
AAAATTGGTGGTGAATGGTGGACATGGATCAATTATAACCGCTTCCAGGAGCTCATCCAG
GAATATGAAGATAGTGGTGGATCAAAAACGTTCAGCGCAAAGGATTATATGGCCAGAACT
CCTCACTGGGCATTATTTGGTGCCAGTGAAAGAGGCTTTGATCCCAAGGACACAAGACAT
CAGAGAAAGAACAAATCAAAGGCTATTTCTGGATGTTGA
|
| Enzyme 24 GenBank Gene ID |
AK001762  |
| Enzyme 24 GeneCard ID |
Q9NV66  |
| Enzyme 24 GenAtlas ID |
TYW1  |
| Enzyme 24 HGNC ID |
HGNC:25598  |
| Enzyme 24 Chromosome Location |
Not Available |
| Enzyme 24 Locus |
Not Available |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
14009 |
| Enzyme 25 Name |
tRNA wybutosine-synthesizing protein 1 homolog B |
| Enzyme 25 Synonyms |
Not Available |
| Enzyme 25 Gene Name |
Not Available |
| Enzyme 25 Protein Sequence |
>tRNA wybutosine-synthesizing protein 1 homolog B
MDPSADTWDLSSPLISLWINRFYIYLGFAVSISLWICVQIVIEMQGFATVLAEAVTSLDL
PVAIINLKEYDPDDHLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFRFGK
TYLKGMRDAVFGLGNSAYASHFNKVGKNVDKWLWMLGVHRVMSRGEGDCDVVKSKHGSIE
ANFRAWKTKFISQLQALQKGERKKSCGGHCKKGKCESHQHGSEEREEGSQEQDELHHRDT
KEEEPFESSSEEEFGGEDHQSLNSIVDVEDLGKIMDHVKKEKREKEQQEEKSGLFRNMGR
NEDGERRAMITPALREALTKQVDAPRERSLLQTHILWNESHRCMETTPSLACANKCVFCW
WHHNNPVGTEWLWKMDQPEMILKEAIENHQNMIKQFKGVPGVKAERFEEGMTVKHCALSL
VGEPIMYPEINRFLKLLHQCKISSFLVTNAQFPAEIRNLEPVTQLYVSVDASTKDSLKKI
DRPLFKDFWQQFLDSLKALAVKQQRTVYRLTLVKAWNVDELQAYAQLVSLGNPDFIEVKG
VTYCRESSASSLTMAHVPWHEEVVQFVRELVDLIPEYEIACEHEHSNCLLIAHRKFKIGG
EWWTWIDYNRFQELIQEYEDSGGSKTFSAKDYMARTPHWALFGANERSFDPKDTRHQRKN
KSKAISGC
|
| Enzyme 25 Number of Residues |
668 |
| Enzyme 25 Molecular Weight |
76917 |
| Enzyme 25 Theoretical pI |
6.22 |
| Enzyme 25 GO Classification |
| Function |
- FMN binding
- binding
- catalytic activity
- cation binding
- electron transporter activity
- ion binding
- iron ion binding
- nucleotide binding
- oxidoreductase activity
- transition metal ion binding
- transporter activity
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 25 General Function |
Energy production and conversion |
| Enzyme 25 Specific Function |
Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
Not Available |
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
46250014  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
Q6NUM6  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
TYW1B_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>2007 bp
ATGGATCCTTCTGCGGATACATGGGACCTCTCCTCACCTTTAATATCATTATGGATAAAC
AGGTTTTACATTTATCTGGGCTTTGCTGTTAGCATTAGCCTTTGGATTTGTGTCCAGATT
GTCATCGAGATGCAGGGATTTGCAACAGTTCTTGCTGAAGCAGTTACGTCCCTGGATCTG
CCTGTGGCCATTATTAATCTAAAAGAATATGATCCAGATGATCATCTGATAGAAGAGGTG
ACTAGTAAAAATGTCTGTGTCTTCCTGGTTGCGACATACACTGACGGCCTACCAACCGAA
AGTGCAGAGTGGTTCTGCAAATGGTTAGAGGAAGCATCCATTGATTTTCGATTTGGCAAA
ACTTACCTGAAGGGTATGAGAGATGCGGTATTTGGCCTGGGAAATTCTGCCTATGCTAGC
CACTTCAACAAGGTTGGCAAAAATGTTGACAAGTGGCTCTGGATGCTTGGCGTGCATCGT
GTGATGAGTCGAGGGGAGGGCGACTGCGACGTGGTTAAAAGCAAGCACGGCAGCATTGAG
GCCAACTTCAGAGCATGGAAGACCAAGTTCATCTCCCAGCTGCAGGCACTTCAGAAAGGG
GAGAGAAAGAAGTCCTGTGGCGGCCACTGCAAGAAAGGCAAATGTGAATCTCACCAACAT
GGCTCAGAGGAGAGGGAGGAAGGATCTCAAGAGCAGGACGAATTGCATCACAGAGACACC
AAGGAGGAAGAACCCTTCGAGAGCTCCAGTGAAGAAGAGTTTGGTGGTGAGGACCATCAG
AGCCTAAATTCCATTGTTGATGTTGAAGATTTGGGCAAAATTATGGATCACGTGAAGAAA
GAAAAGAGAGAAAAGGAACAGCAGGAAGAGAAGTCTGGTTTGTTCAGGAACATGGGGAGG
AATGAAGATGGTGAAAGAAGAGCTATGATAACTCCTGCTCTCCGAGAAGCCCTTACTAAA
CAAGTCGATGCTCCGAGGGAGAGGAGCTTGTTACAAACACACATTCTATGGAATGAGAGC
CATCGCTGCATGGAAACCACCCCGAGCTTGGCGTGTGCTAATAAATGTGTCTTCTGTTGG
TGGCACCACAACAACCCTGTGGGCACTGAATGGTTGTGGAAGATGGACCAGCCTGAAATG
ATCTTGAAGGAAGCCATTGAAAACCATCAGAACATGATTAAGCAGTTTAAAGGAGTACCG
GGCGTCAAAGCAGAACGCTTTGAAGAAGGAATGACGGTAAAGCACTGTGCATTGTCCCTC
GTGGGAGAACCAATAATGTACCCAGAGATCAACAGGTTTTTGAAGCTACTCCACCAGTGT
AAAATCTCCAGCTTCCTGGTCACAAATGCACAATTTCCTGCGGAAATCAGGAACCTCGAG
CCAGTTACTCAGCTGTATGTCAGTGTGGATGCCAGTACCAAAGACAGCCTGAAGAAAATC
GACCGCCCACTCTTCAAGGATTTCTGGCAGCAATTCCTTGACAGTTTAAAAGCCTTGGCA
GTCAAGCAACAACGAACTGTCTACAGACTGACGCTCGTGAAAGCATGGAACGTGGACGAG
CTCCAGGCCTACGCGCAGCTCGTGTCCCTGGGGAATCCTGACTTCATCGAAGTGAAGGGC
GTTACCTACTGCAGAGAAAGTTCAGCAAGCAGTCTTACCATGGCCCATGTGCCCTGGCAT
GAGGAAGTGGTACAGTTTGTCCGCGAGCTGGTGGATCTGATCCCCGAATATGAAATTGCA
TGTGAACACGAACACTCTAATTGCCTCCTGATAGCACACAGAAAGTTTAAAATTGGTGGT
GAATGGTGGACATGGATCGATTATAACCGCTTCCAGGAGCTCATCCAGGAATATGAAGAT
AGTGGTGGATCAAAAACGTTCAGCGCAAAGGATTATATGGCCAGAACTCCTCACTGGGCA
TTATTTGGTGCCAATGAAAGAAGCTTTGATCCCAAGGACACAAGACATCAGAGAAAGAAC
AAATCAAAGGCTATTTCTGGATGTTGA
|
| Enzyme 25 GenBank Gene ID |
BC068520  |
| Enzyme 25 GeneCard ID |
Q6NUM6  |
| Enzyme 25 GenAtlas ID |
TYW1B  |
| Enzyme 25 HGNC ID |
HGNC:33908  |
| Enzyme 25 Chromosome Location |
Not Available |
| Enzyme 25 Locus |
Not Available |
| Enzyme 25 SNPs |
Not Available |
| Enzyme 25 General References |
Not Available |
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
15208 |
| Enzyme 26 Name |
cDNA FLJ78493, highly similar to Homo sapiens hydroxyacid oxidase (glycolate oxidase) 1 (HAO1), mRNA (Hydroxyacid oxidase (Glycolate oxidase) 1, isoform CRA_a) |
| Enzyme 26 Synonyms |
Not Available |
| Enzyme 26 Gene Name |
HAO1 |
| Enzyme 26 Protein Sequence |
>cDNA FLJ78493, highly similar to Homo sapiens hydroxyacid oxidase (glycolate oxidase) 1 (HAO1), mRNA (Hydroxyacid oxidase (Glycolate oxidase) 1, isoform CRA_a)
MLPRLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAET
DLSTSVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAE
AGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYLGNRLDDVRNRFKLPPQ
LRMKNFETSTLSFSPEENFGDDSGLAAYVAKAIDPSISWEDIKWLRRLTSLPIVAKGILR
GDDAREAVKHGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDV
LKALALGAKAVFVGRPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLV
RKNPLAVSKI
|
| Enzyme 26 Number of Residues |
370 |
| Enzyme 26 Molecular Weight |
40925 |
| Enzyme 26 Theoretical pI |
8.29 |
| Enzyme 26 GO Classification |
Not Available |
| Enzyme 26 General Function |
Energy production and conversion |
| Enzyme 26 Specific Function |
Not Available |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
Not Available |
| Enzyme 26 Pfam Domain Function |
Not Available |
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
158259869  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
A8K058  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
A8K058_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>1113 bp
ATGCTCCCCCGGCTAATTTGTATCAATGATTATGAACAACATGCTAAATCAGTACTTCCA
AAGTCTATATATGACTATTACAGGTCTGGGGCAAATGATGAAGAAACTTTGGCTGATAAT
ATTGCAGCATTTTCCAGATGGAAGCTGTATCCAAGGATGCTCCGGAATGTTGCTGAAACA
GATCTGTCGACTTCTGTTTTAGGACAGAGGGTCAGCATGCCAATATGTGTGGGGGCTACG
GCCATGCAGCGCATGGCTCATGTGGACGGCGAGCTTGCCACTGTGAGAGCCTGTCAGTCC
CTGGGAACGGGCATGATGTTGAGTTCCTGGGCCACCTCCTCAATTGAAGAAGTGGCGGAA
GCTGGTCCTGAGGCACTTCGTTGGCTGCAACTGTATATCTACAAGGACCGAGAAGTCACC
AAGAAGCTAGTGCGGCAGGCAGAGAAGATGGGCTACAAGGCCATATTTGTGACAGTGGAC
ACACCTTACCTGGGCAACCGTCTGGATGATGTGCGTAACAGATTCAAACTGCCGCCACAA
CTCAGGATGAAAAATTTTGAAACCAGTACTTTATCATTTTCTCCTGAGGAAAATTTTGGA
GACGACAGTGGACTTGCTGCATATGTGGCTAAAGCAATAGACCCATCTATCAGCTGGGAA
GATATCAAATGGCTGAGAAGACTGACATCATTGCCAATTGTTGCAAAGGGCATTTTGAGA
GGTGATGATGCCAGGGAGGCTGTTAAACATGGCTTGAATGGGATCTTGGTGTCGAATCAT
GGGGCTCGACAACTCGATGGGGTGCCAGCCACTATTGATGTTCTGCCAGAAATTGTGGAG
GCTGTGGAAGGGAAGGTGGAAGTCTTCCTGGACGGGGGTGTGCGGAAAGGCACTGATGTT
CTGAAAGCTCTGGCTCTTGGCGCCAAGGCTGTGTTTGTGGGGAGACCAATCGTTTGGGGC
TTAGCTTTCCAGGGGGAGAAAGGTGTTCAAGATGTCCTCGAGATACTAAAGGAAGAATTC
CGGTTGGCCATGGCTCTGAGTGGGTGCCAGAATGTGAAAGTCATCGACAAGACATTGGTG
AGGAAAAATCCTTTGGCCGTTTCCAAGATCTGA
|
| Enzyme 26 GenBank Gene ID |
AK289423  |
| Enzyme 26 GeneCard ID |
A8K058  |
| Enzyme 26 GenAtlas ID |
Not Available |
| Enzyme 26 HGNC ID |
Not Available |
| Enzyme 26 Chromosome Location |
20 |
| Enzyme 26 Locus |
20p12 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
Not Available |
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
15247 |
| Enzyme 27 Name |
Testicular acid phosphatase |
| Enzyme 27 Synonyms |
Not Available |
| Enzyme 27 Gene Name |
ACPT |
| Enzyme 27 Protein Sequence |
>Testicular acid phosphatase
MAGLGFWGHPAGPLLLLLLLVLPPRALPEGPLVFVALVFRHGDRAPLASYPMDPHKEVAS
TLWPRGLGQLTTEGVRQQLELGRFLRSRYEAFLSPEYRREEVYIRSTDFDRTLESAQANL
AGLFPEAAPGSPEARWRPIPVHTVPVAEDKLLRFPMRSCPRYHELLREATEAAEYQEALE
GWTGFLSRLENFTGLSLVGEPLRRAWKVLDTLMCQQAHGLPLPAWASPDVLRTLAQISAL
DIGAHVGPPRAAEKAQLTGGILLNAILANFSRVQRLGLPLKMVMYSAHDSTLLALQGALG
LYDGHTPPYAACLGFEFRKHLGNPAKDGGNVTVSLFYRNDSAHLPLPLSLPGCPAPCPLG
RFYQLTAPARPPAHGVSCHGPYEAAIPPAPVVPLLAGAVAVLVALSLGLGLLAWRPGCLR
ALGGPV
|
| Enzyme 27 Number of Residues |
426 |
| Enzyme 27 Molecular Weight |
46090 |
| Enzyme 27 Theoretical pI |
8.29 |
| Enzyme 27 GO Classification |
| Function |
- acid phosphatase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 27 General Function |
Not Available |
| Enzyme 27 Specific Function |
Dephosphorylates receptor tyrosine-protein kinase erbB-4 and inhibits the ligand-induced proteolytic cleavage |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
Not Available |
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
12958660  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
Q9BZG2  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
PPAT_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>1281 bp
ATGGCCGGCCTGGGGTTTTGGGGCCACCCTGCTGGACCTCTCCTGCTGCTGCTGCTGCTG
GTGCTGCCACCCCGGGCCCTGCCAGAAGGACCCCTGGTGTTCGTGGCTCTGGTATTCCGC
CATGGCGACCGGGCCCCGCTGGCCTCCTACCCCATGGACCCACACAAGGAGGTGGCCTCC
ACCCTGTGGCCACGAGGCCTGGGCCAGCTGACCACGGAGGGGGTCCGCCAGCAGCTGGAG
CTGGGCCGCTTCCTGAGGAGCCGCTACGAGGCCTTCCTGAGTCCGGAGTACCGGCGGGAG
GAGGTGTACATCCGCAGCACGGACTTTGACCGCACGCTGGAGAGTGCCCAGGCCAACCTT
GCCGGGCTGTTTCCCGAGGCTGCTCCAGGGAGCCCCGAGGCCCGCTGGAGGCCGATCCCG
GTGCACACGGTGCCCGTGGCTGAGGATAAGCTGCTGAGGTTCCCCATGCGCAGCTGTCCC
CGATACCACGAGCTGCTGCGGGAGGCCACCGAGGCCGCCGAGTACCAGGAGGCCCTGGAG
GGCTGGACGGGCTTCCTGAGTCGCCTGGAGAACTTCACGGGACTGTCGCTGGTTGGAGAG
CCACTGCGCAGGGCATGGAAGGTTCTGGACACCCTCATGTGCCAGCAAGCCCACGGTCTT
CCACTACCAGCCTGGGCCTCCCCAGATGTCCTGCGGACTCTTGCCCAGATCTCGGCTTTG
GATATTGGAGCCCACGTGGGCCCACCCCGGGCAGCAGAGAAGGCCCAGCTGACAGGGGGG
ATCCTGCTGAATGCTATCCTTGCAAACTTCTCCCGGGTCCAGCGCCTGGGGCTGCCCCTC
AAGATGGTCATGTACTCAGCTCATGACAGCACCCTGCTGGCCCTCCAGGGGGCCCTGGGC
CTCTATGATGGACACACCCCGCCATATGCTGCCTGCCTCGGCTTTGAGTTCCGGAAGCAC
CTGGGGAATCCCGCCAAAGATGGAGGGAATGTCACCGTCTCCCTCTTCTACCGCAATGAC
TCCGCCCACCTGCCCCTGCCTCTCAGCCTCCCCGGGTGCCCGGCCCCCTGTCCACTAGGC
CGCTTCTACCAGCTGACTGCCCCGGCCCGGCCTCCCGCCCATGGGGTCTCCTGCCATGGC
CCCTATGAGGCTGCCATCCCCCCAGCTCCAGTGGTGCCCCTGCTGGCCGGAGCTGTAGCT
GTGCTGGTGGCACTCAGCTTGGGGCTGGGCCTGCTGGCCTGGAGACCAGGGTGCCTGCGG
GCCTTGGGGGGCCCCGTGTGA
|
| Enzyme 27 GenBank Gene ID |
AF321918  |
| Enzyme 27 GeneCard ID |
Q9BZG2  |
| Enzyme 27 GenAtlas ID |
ACPT  |
| Enzyme 27 HGNC ID |
HGNC:14376  |
| Enzyme 27 Chromosome Location |
19 |
| Enzyme 27 Locus |
19q13.4 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Yousef GM, Diamandis M, Jung K, Diamandis EP: Molecular cloning of a novel human acid phosphatase gene (ACPT) that is highly expressed in the testis. Genomics. 2001 Jun 15;74(3):385-95. [PubMed
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
16490 |
| Enzyme 28 Name |
Sarcosine dehydrogenase |
| Enzyme 28 Synonyms |
Not Available |
| Enzyme 28 Gene Name |
SARDH |
| Enzyme 28 Protein Sequence |
>Sarcosine dehydrogenase
MASLSRALRVAAAHPRQSPTRGMGPCNLSSAAGPTAEKSVPYQRTLKEGQGTSVVAQGPS
RPLPSTANVVVIGGGSLGCQTLYHLAKLGMSGAVLLERERLTSGTTWHTAGLLWQLRPSD
VEVELLAHTRRVVSRELEEETGLHTGWIQNGGLFIASNRQRLDEYKRLMSLGKAYGVESH
VLSPAETKTLYPLMNVDDLYGTLYVPHDGTMDPAGTCTTLARAASARGAQVIENCPVTGI
RVWTDDFGVRRVAGVETQHGSIQTPCVVNCAGVWASAVGRMAGVKVPLVAMHHAYVVTER
IEGIQNMPNVRDHDASVYLRLQGDALSVGGYEANPIFWEEVSDKFAFGLFDLDWEVFTQH
IEGAINRVPVLEKTGIKSTVCGPESFTPDHKPLMGEAPELRGFFLGCGFNSAGMMLGGGC
GQELAHWIIHGRPEKDMHGYDIRRFHHSLTDHPRWIRERSHESYAKNYSVVFPHDEPLAG
RNMRRDPLHEELLGQGCVFQERHGWERPGWFHPRGPAPVLEYDYYGAYGSRAHEDYAYRR
LLADEYTFAFPPHHDTIKKECLACRGAAAVFDMSYFGKFYLVGLDARKAADWLFSADVSR
PPGSTVYTCMLNHRGGTESDLTVSRLAPSHQASPLAPAFEGDGYYLAMGGAVAQHNWSHI
TTVLQDQKSQCQLIDSSEDLGMISIQGPASRAILQEVLDADLSNEAFPFSTHKLLRAAGH
LVRAMRLSFVGELGWELHIPKASCVPVYRAVMAAGAKHGLINAGYRAIDSLSIEKGYRHW
HADLRPDDSPLEAGLAFTCKLKSPVPFLGREALEQQRAAGLRRRLVCFTMEDKVPMFGLE
AIWRNGQVVGHVRRADFGFAIDKTIAYGYIHDPSGGPVSLDFVKSGDYALERMGVTYGAQ
AHLKSPFDPNNKRVKGIY
|
| Enzyme 28 Number of Residues |
918 |
| Enzyme 28 Molecular Weight |
101038 |
| Enzyme 28 Theoretical pI |
7.26 |
| Enzyme 28 GO Classification |
| Function |
- aminomethyltransferase activity
- catalytic activity
- methyltransferase activity
- oxidoreductase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- glycine catabolism
- glycine metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 28 General Function |
Amino acid transport and metabolism |
| Enzyme 28 Specific Function |
Not Available |
| Enzyme 28 Pathways |
Not Available |
| Enzyme 28 Reactions |
Not Available |
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
Not Available |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
B2RMR5  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
B2RMR5_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
Not Available |
| Enzyme 28 GenBank Gene ID |
BC136363  |
| Enzyme 28 GeneCard ID |
B2RMR5  |
| Enzyme 28 GenAtlas ID |
SARDH  |
| Enzyme 28 HGNC ID |
HGNC:10536  |
| Enzyme 28 Chromosome Location |
Not Available |
| Enzyme 28 Locus |
Not Available |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
Not Available |
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
16534 |
| Enzyme 29 Name |
Putative uncharacterized protein ACP1 |
| Enzyme 29 Synonyms |
Not Available |
| Enzyme 29 Gene Name |
ACP1 |
| Enzyme 29 Protein Sequence |
>Putative uncharacterized protein ACP1
MAEQATKSVLFVCLGNICRSPIAEAVFRKLVTDQNISENWRVDSAATSGYEIGNPPDYRG
QSCMKRHGIPMSHVARQVPSLDLKLCVLCFSGSLTAVLFLTGTWAGPQTQEL
|
| Enzyme 29 Number of Residues |
112 |
| Enzyme 29 Molecular Weight |
12230 |
| Enzyme 29 Theoretical pI |
7.85 |
| Enzyme 29 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphoprotein phosphatase activity
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
- protein tyrosine phosphatase activity
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid dephosphorylation
- protein modification
|
| Component |
| — |
|
| Enzyme 29 General Function |
Signal transduction mechanisms |
| Enzyme 29 Specific Function |
Not Available |
| Enzyme 29 Pathways |
Not Available |
| Enzyme 29 Reactions |
Not Available |
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
Not Available |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
B5MCC7  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
B5MCC7_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
Not Available |
| Enzyme 29 GenBank Gene ID |
AC079779  |
| Enzyme 29 GeneCard ID |
B5MCC7  |
| Enzyme 29 GenAtlas ID |
ACP1  |
| Enzyme 29 HGNC ID |
HGNC:122  |
| Enzyme 29 Chromosome Location |
Not Available |
| Enzyme 29 Locus |
Not Available |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
Not Available |
| Enzyme 29 Metabolite References |
Not Available |