|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5253 |
| Enzyme 1 Name |
Acyl-coenzyme A thioesterase 12 |
| Enzyme 1 Synonyms |
- Acyl-CoA thioesterase 12
- Acyl-CoA thioester hydrolase 12
- Cytoplasmic acetyl-CoA hydrolase 1
- CACH-1
- hCACH-1
- START domain-containing protein 12
- StARD12
|
| Enzyme 1 Gene Name |
ACOT12 |
| Enzyme 1 Protein Sequence |
>Acyl-coenzyme A thioesterase 12
MERPAPGEVVMSQAIQPAHATARGELSAGQLLKWIDTTACLAAEKHAGVSCVTASVDDIQ
FEETARVGQVITIKAKVTRAFSTSMEISIKVMVQDMLTGIEKLVSVAFSTFVAKPVGKEK
IHLKPVTLLTEQDHVEHNLAAERRKVRLQHEDTFNNLMKESSKFDDLIFDEEEGAVSTRG
TSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSVDMFKFRGPST
VGDRLVFTAIVNNTFQTCVEVGVRVEAFDCQEWAEGRGRHINSAFLIYNAADDKENLITF
PRIQPISKDDFRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDISKQASLSDSNVEALK
KLAAKRGWEVTSTVEKIKIYTLEEHDVLSVWVEKHVGSPAHLAYRLLSDFTKRPLWDPHF
VSCEVIDWVSEDDQLYHITCPILNDDKPKDLVVLVSRRKPLKDGNTYTVAVKSVILPSVP
PSPQYIRSEIICAGFLIHAIDSNSCIVSYFNHMSASILPYFAGNLGGWSKSIEETAASCI
QFLENPPDDGFVSTF
|
| Enzyme 1 Number of Residues |
555 |
| Enzyme 1 Molecular Weight |
62035 |
| Enzyme 1 Theoretical pI |
6.76 |
| Enzyme 1 GO Classification |
| Function |
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 1 General Function |
Lipid transport and metabolism |
| Enzyme 1 Specific Function |
Hydrolyzes acetyl-CoA to acetate and CoA |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- acetyl-CoA + H2O = CoA + acetate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
18307694  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q8WYK0  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
ACO12_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1668 bp
ATGGAGCGGCCGGCGCCCGGCGAGGTGGTCATGAGCCAAGCCATCCAGCCGGCGCACGCC
ACTGCGCGCGGCGAGCTGAGCGCGGGGCAGCTGCTCAAGTGGATCGACACCACCGCCTGC
CTGGCGGCTGAGAAACATGCTGGAGTTTCCTGCGTTACAGCCTCAGTGGATGACATACAG
TTTGAGGAGACAGCTAGAGTTGGACAAGTTATAACCATCAAAGCAAAAGTTACTAGAGCA
TTCAGCACAAGCATGGAGATCAGTATCAAGGTCATGGTACAGGATATGCTCACTGGCATT
GAGAAGCTTGTTAGTGTGGCTTTCTCCACATTTGTAGCCAAACCAGTTGGAAAAGAAAAG
ATTCATTTAAAACCAGTCACACTTCTAACTGAACAAGATCATGTGGAACATAATCTGGCT
GCTGAGAGAAGGAAAGTTCGATTACAACATGAAGATACCTTTAACAATTTAATGAAGGAA
AGTAGCAAATTTGATGATCTCATTTTTGATGAAGAGGAAGGAGCGGTTTCCACAAGGGGC
ACCTCCGTTCAGAGCATTGAACTGGTCCTCCCACCCCATGCAAACCATCACGGAAATACA
TTTGGTGGCCAGATTATGGCGTGGATGGAGACAGTGGCTACTATTTCTGCAAGCCGCCTG
TGTTGGGCTCATCCCTTTCTGAAGTCCGTAGATATGTTTAAGTTCCGGGGACCATCTACA
GTTGGAGATCGTCTTGTCTTCACTGCCATTGTCAACAATACATTTCAGACCTGTGTTGAA
GTTGGAGTTCGCGTGGAGGCCTTTGACTGTCAGGAATGGGCCGAGGGCCGAGGGCGTCAC
ATCAACAGTGCTTTTCTCATTTACAATGCTGCTGATGATAAGGAAAATCTCATCACGTTT
CCCAGAATCCAACCCATTTCAAAGGATGATTTCAGACGCTATCGGGGAGCTATTGCACGC
AAGCGAATTCGCCTAGGCAGAAAATATGTTATTTCCCACAAAGAAGAGGTTCCACTTTGC
ATACACTGGGATATCAGCAAGCAGGCATCCCTGAGTGACAGCAATGTGGAGGCCCTCAAA
AAACTGGCAGCCAAAAGGGGTTGGGAGGTTACCAGCACTGTGGAAAAGATAAAAATATAT
ACTCTGGAAGAGCATGATGTTTTATCTGTTTGGGTTGAAAAGCACGTGGGAAGTCCAGCA
CATTTGGCTTATCGTCTCTTGTCTGACTTTACAAAGCGACCTTTGTGGGACCCCCATTTT
GTGTCCTGTGAAGTCATAGACTGGGTGAGTGAAGATGATCAGCTGTATCACATCACCTGT
CCTATACTGAATGATGACAAACCCAAAGACTTGGTAGTACTCGTATCACGAAGAAAACCC
CTCAAAGATGGTAACACTTACACAGTGGCAGTGAAGTCGGTCATTTTGCCATCGGTCCCC
CCGTCTCCACAGTACATCAGAAGTGAAATCATATGTGCCGGATTTCTCATCCATGCTATT
GACAGCAATTCATGCATCGTATCTTACTTTAACCATATGTCTGCTAGCATCCTTCCTTAC
TTTGCTGGAAATCTTGGTGGCTGGTCAAAATCCATTGAAGAAACAGCAGCCTCTTGTATA
CAGTTCTTAGAGAATCCTCCTGATGATGGGTTTGTAAGCACATTTTAA
|
| Enzyme 1 GenBank Gene ID |
AB078619  |
| Enzyme 1 GeneCard ID |
ACOT12  |
| Enzyme 1 GenAtlas ID |
ACOT12  |
| Enzyme 1 HGNC ID |
HGNC:24436  |
| Enzyme 1 Chromosome Location |
Not Available |
| Enzyme 1 Locus |
Not Available |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
Not Available |
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5266 |
| Enzyme 2 Name |
Acetyl-coenzyme A synthetase, cytoplasmic |
| Enzyme 2 Synonyms |
- Acetate--CoA ligase
- Acyl-activating enzyme
- Acetyl-CoA synthetase
- ACS
- AceCS
- Acyl-CoA synthetase short-chain family member 2
|
| Enzyme 2 Gene Name |
ACSS2 |
| Enzyme 2 Protein Sequence |
>Acetyl-coenzyme A synthetase, cytoplasmic
MGLPEERVRSGSGSRGQEEAGAGGRARSWSPPPEVSRSAHVPSLQRYRELHRRSVEEPRE
FWGDIAKEFYWKTPCPGPFLRYNFDVTKGKIFIEWMKGATTNICYNVLDRNVHEKKLGDK
VAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLAC
ARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEK
GFPVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQISWNQGIDLWWHELMQEAGDEC
EPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIG
WITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFG
DEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPG
ATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTY
FKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV
GHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG
KIMRRVLRKIAQNDHDLGDMSTVADPSVISHLFSHRCLTIQ
|
| Enzyme 2 Number of Residues |
701 |
| Enzyme 2 Molecular Weight |
78580 |
| Enzyme 2 Theoretical pI |
6.43 |
| Enzyme 2 GO Classification |
| Function |
- AMP binding
- CoA-ligase activity
- acetate-CoA ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-sulfur bonds
- nucleotide binding
- purine nucleotide binding
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Lipid transport and metabolism |
| Enzyme 2 Specific Function |
Activates acetate so that it can be used for lipid synthesis or for energy generation |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
8439651  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q9NR19  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
ACSA_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>2106 bp
ATGGGGCTTCCTGAGGAGCGGGTCCGGAGCGGCAGCGGGAGCCGGGGCCAGGAGGAAGCT
GGAGCCGGAGGCCGGGCGCGGAGTTGGTCTCCGCCGCCCGAGGTCAGCCGCTCCGCGCAC
GTCCCCTCGCTGCAGCGCTACCGCGAGCTGCACCGGCGCTCCGTGGAGGAGCCGCGGGAA
TTCTGGGGAGACATTGCCAAGGAATTTTACTGGAAGACTCCATGCCCTGGCCCATTCCTT
CGGTACAACTTTGATGTGACTAAAGGGAAAATCTTCATTGAGTGGATGAAAGGAGCAACT
ACCAACATCTGCTACAATGTACTGGATCGAAATGTCCATGAGAAAAAGCTTGGAGATAAA
GTTGCTTTTTACTGGGAGGGCAATGAGCCAGGGGAGACCACTCAGATCACATACCATCAG
CTTCTGGTCCAAGTGTGTCAGTTCAGCAATGTTCTCCGAAAACAGGGCATTCAGAAGGGG
GACCGAGTGGCCATCTACATGCCTATGATCCCAGAGCTTGTGGTGGCCATGCTGGCATGT
GCCCGCATTGGGGCTTTGCACTCCATTGTGTTTGCAGGCTTCTCTTCAGAGTCTCTATGT
GAACGGATCTTGGATTCCAGCTGCAGTCTTCTCATCACTACAGATGCCTTCTACAGGGGG
GAAAAGCTTGTGAACCTGAAGGAGCTGGCTGACGAGGCCCTGCAGAAGTGTCAGGAGAAG
GGTTTCCCAGTAAGATGCTGCATTGTGGTCAAGCACCTGGGGCGGGCAGAGCTCGGCATG
GGTGACTCCACCAGCCAGTCCCCCCCAATTAAGAGGTCATGCCCAGATGTGCAGATCTCA
TGGAACCAAGGGATTGACTTGTGGTGGCATGAGCTCATGCAAGAGGCAGGGGATGAGTGT
GAGCCCGAGTGGTGTGATGCCGAGGACCCACTCTTCATCCTGTACACCAGTGGCTCCACA
GGCAAACCCAAGGGTGTGGTTCACACAGTTGGGGGCTACATGCTCTATGTAGCCACAACC
TTCAAGTATGTGTTTGACTTCCATGCAGAGGATGTGTTCTGGTGCACGGCAGACATTGGT
TGGATCACTGGTCATTCCTACGTCACCTATGGGCCACTGGCCAATGGTGCCACCAGTGTT
TTGTTTGAGGGGATTCCCACATATCCGGACGTGAACCGCCTGTGGAGCATTGTGGACAAA
TACAAGGTGACCAAGTTCTACACAGCACCCACAGCCATCCGTCTGCTCATGAAGTTTGGA
GATGAGCCTGTCACCAAGCATAGCCGGGCATCCTTGCAGGTGTTAGGCACAGTGGGTGAA
CCCATCAACCCTGAGGCCTGGCTATGGTACCACCGGGTGGTAGGTGCCCAGCGCTGCCCC
ATCGTGGACACCTTCTGGCAAACAGAGACAGGTGGCCACATGTTGACTCCCCTTCCTGGT
GCCACACCCATGAAACCCGGTTCTGCTACTTTCCCATTCTTTGGTGTAGCTCCTGCAATC
CTGAATGAGTCCGGGGAAGAGTTGGAAGGTGAAGCTGAAGGTTATCTGGTGTTCAAGCAG
CCCTGGCCAGGGATCATGCGCACAGTCTATGGGAACCACGAACGCTTTGAGACAACCTAC
TTTAAGAAGTTTCCTGGATACTATGTTACAGGAGATGGCTGCCAGCGGGACCAGGATGGC
TATTACTGGATCACTGGCAGGATTGATGACATGCTCAATGTATCTGGACACCTGCTGAGT
ACAGCAGAGGTGGAGTCAGCACTTGTGGAACATGAGGCTGTTGCAGAGGCAGCTGTGGTG
GGCCACCCTCATCCTGTGAAGGGTGAATGCCTCTACTGCTTTGTCACCTTGTGTGATGGC
CACACCTTCAGCCCCAAGCTCACCGAGGAGCTCAAGAAGCAGATTAGAGAAAAGATTGGC
CCCATTGCCACACCAGACTACATCCAGAATGCACCTGGCTTGCCTAAAACCCGCTCAGGG
AAAATCATGAGGCGAGTGCTTCGGAAGATTGCTCAGAATGACCATGACCTCGGGGACATG
TCTACTGTGGCTGACCCATCTGTCATCAGTCACCTCTTCAGCCACCGCTGCCTGACCATC
CAGTGA
|
| Enzyme 2 GenBank Gene ID |
AF263614  |
| Enzyme 2 GeneCard ID |
ACSS2  |
| Enzyme 2 GenAtlas ID |
ACSS2  |
| Enzyme 2 HGNC ID |
HGNC:15814  |
| Enzyme 2 Chromosome Location |
20 |
| Enzyme 2 Locus |
20q11.22 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Luong A, Hannah VC, Brown MS, Goldstein JL: Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins. J Biol Chem. 2000 Aug 25;275(34):26458-66. [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 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5271 |
| Enzyme 3 Name |
Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor |
| Enzyme 3 Synonyms |
- Acetate--CoA ligase 2
- Acetyl-CoA synthetase 2
- Acyl- CoA synthetase short-chain family member 1
|
| Enzyme 3 Gene Name |
ACSS1 |
| Enzyme 3 Protein Sequence |
>Acetyl-coenzyme A synthetase 2-like, mitochondrial precursor
MAARTLGRGVGRLLGSLRGLSGQPARPPCGVSAPRRAASGPSGSAPAVAAAAAQPGSYPA
LSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVR
KSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVA
AMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVK
HCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGM
PKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLF
ESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPI
NCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVL
MDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEG
GYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKD
SAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELG
DTTTLEDPSIIAEILSVYQKCKDKQAAAK
|
| Enzyme 3 Number of Residues |
689 |
| Enzyme 3 Molecular Weight |
74857 |
| Enzyme 3 Theoretical pI |
7.11 |
| Enzyme 3 GO Classification |
| Function |
- AMP binding
- CoA-ligase activity
- acetate-CoA ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-sulfur bonds
- nucleotide binding
- purine nucleotide binding
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Lipid transport and metabolism |
| Enzyme 3 Specific Function |
Converts acetate to acetyl-CoA so that it can be used for oxidation through the tricarboxylic cycle to produce ATP and CO(2) |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
Not Available |
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
56203089  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q9NUB1  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
ACS2L_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1439 bp
CCAAGTGCAAGGTGGTTATCACCTTCAACCAAGGACTCCGGGGTGGGCGCGTGGTGGAGC
TGAAGAAAATAGTGGATGAGGCTGTGAAGCACTGCCCCACCGTGCAGCATGTCCTGGTGG
CTCACAGGACAGACAACAAGGTCCACATGGGGGATCTGGACGTCCCGCTGGAGCAGGAAA
TGGCCAAGGAGGACCCTGTTTGCGCCCCAGAGAGCATGGGCAGTGAGGACATGCTCTTCA
TGCTGTACACCTCAGGGAGCACCGGAATGCCCAAGGGCATCGTCCATACCCAGGCAGGCT
ACCTGCTCTATGCCGCCCTGACTCACAAGCTTGTGTTTGACCACCAGCCAGGTGACATCT
TTGGCTGTGTGGCCGACATCGGTTGGATTACAGGACACAGCTACGTGGTGTATGGGCCTC
TCTGCAATGGTGCCACCAGCGTCCTTTTTGAGAGCACCCCAGTTTATCCCAATGCTGGTC
GGTACTGGGAGACAGTAGAGAGGTTGAAGATCAATCAGTTCTATGGCGCCCCAACGGCTG
TCCGGCTGTTGCTGAAATACGGTGATGCCTGGGTGAAGAAGTATGATCGCTCCTCCCTGC
GGACCCTGGGGTCAGTGGGAGAGCCCATCAACTGTGAGGCCTGGGAGTGGCTTCACAGGG
TGGTGGGGGACAGCAGGTGCACGCTGGTGGACACCTGGTGGCAGACAGAAACAGGTGGCA
TCTGCATCGCACCACGGCCCTCGGAAGAAGGGGCGGAAATCCTCCCTGCCATGGCGATGA
GGCCCTTCTTTGGCATCGTCCCCGTCCTCATGGATGAGAAGGGCAGCGTCGTGGAGGGCA
GCAACGTCTCCGGGGCCCTGTGCATCTCCCAGGCCTGGCCGGGCATGGCCAGGACCATCT
ATGGCGACCACCAGCGATTTGTGGACGCCTACTTCAAGGCCTACCCAGGCTATTACTTCA
CTGGAGACGGGGCTTACCGAACTGAGGGCGGCTATTACCAGATCACAGGGCGGATGGATG
ATGTCATCAACATCAGTGGCCACCGGCTGGGGACCGCAGAGATTGAGGACGCCATCGCCG
ACCACCCTGCAGTACCAGAAAGTGCTGTCATTGGCTACCCCCACGACATCAAAGGAGAAG
CTGCCTTTGCCTTCATTGTGGTGAAAGATAGTGCGGGTGACTCAGATGTGGTGGTGCAGG
AGCTCAAGTCCATGGTGGCCACCAAGATCGCCAAATATGCTGTGCCTGATGAGATCCTGG
TGGTGAAACGTCTTCCAAAAACCAGGTCTGGGAAGGTCATGCGGCGGCTCCTGAGGAAGA
TCATCACTAGTGAGGCCCAGGAGCTGGGAGACACTACCACCTTGGAGGACCCCAGCATCA
TCGCAGAGATCCTGAGTGTCTACCAGAAGTGCAAGGACAAGCAGGCTGCTGCTAAGTGA
|
| Enzyme 3 GenBank Gene ID |
AL035661  |
| Enzyme 3 GeneCard ID |
ACSS1  |
| Enzyme 3 GenAtlas ID |
ACSS1  |
| Enzyme 3 HGNC ID |
HGNC:16091  |
| Enzyme 3 Chromosome Location |
20 |
| Enzyme 3 Locus |
20p11.23-p11.21 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2001 Apr 27;8(2):85-95. [PubMed
]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5526 |
| Enzyme 4 Name |
4-trimethylaminobutyraldehyde dehydrogenase |
| Enzyme 4 Synonyms |
- TMABADH
- Aldehyde dehydrogenase 9A1
- Aldehyde dehydrogenase E3 isozyme
- Gamma-aminobutyraldehyde dehydrogenase
- R- aminobutyraldehyde dehydrogenase
|
| Enzyme 4 Gene Name |
ALDH9A1 |
| Enzyme 4 Protein Sequence |
>4-trimethylaminobutyraldehyde dehydrogenase
MSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRVIATFTCSGEKEVNLAVQNAKA
AFKIWSQKSGMERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYY
AGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFK
PSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGSVPTGMKI
MEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEI
LDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIY
VPEDPKLKDGYYMRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLA
AGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQL
KTVCVEMGDVESAF
|
| Enzyme 4 Number of Residues |
494 |
| Enzyme 4 Molecular Weight |
53802 |
| Enzyme 4 Theoretical pI |
5.61 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Energy production and conversion |
| Enzyme 4 Specific Function |
Converts gamma-trimethylaminobutyraldehyde into gamma- butyrobetaine. Catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- 4-trimethylammoniobutanal + NAD+ = 4-trimethylammoniobutanoate + NADH + H+
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
1049219  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P49189  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
AL9A1_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1482 bp
ATGAGCACTGGCACCTTCGTCGTGTCGCAGCCGCTCAATTACCGCGGCGGGGCCGCTGGA
GCCGGCGGACGCTCCGGTACCGAGAAAGCTTTCGAGCCAGCAACCGGCCGAGTGATAGCT
ACTTTCACATGTTCAGGAGAAAAGGAAGTAAATTTGGCTGTTCAAAATGCAAAGGCTGCT
TTTAAAATATGGAGTCAAAAATCTGGCATGGAGCGTTGCCGAATCCTTTTGGAGGCTGCC
AGGATAATAAGGGAACGGGAGGATGAAATTGCTACTATGGAGTGCATCAACAATGGCAAG
TCCATCTTTGAGGCCCGCTTGGACATTGACATTTCCTGGCAGTGCCTGGAGTATTATGCG
GGCTTGGCTGCATCCATGGCTGGTGAACACATCCAGCTCCCAGGTGGATCGTTTGGTTAT
ACCAGAAGAGAACCACTTGGGGTATGTGTGGGAATAGGAGCATGGAACTACCCCTTTCAG
ATTGCCTCTTGGAAGTCGGCTCCAGCATTAGCCTGTGGTAATGCCATGGTCTTTAAACCT
TCTCCCTTTACACCTGTTTCTGCATTGCTACTGGCTGAAATCTACAGTGAGGCTGGTGTA
CCTCCTGGGCTCTTCAATGTGGTGCAGGGAGGGGCTGCCACAGGCCAGTTTCTGTGTCAG
CATCCCGATGTGGCCAAAGTCTCCTTCACTGGAAGTGTGCCCACTGGCATGAAGATCATG
GAGATGTCAGCTAAAGGAATCAAACCTGTTACCTTGGAACTTGGAGGCAAATCTCCACTC
ATCATCTTCTCAGACTGTGATATGAACAATGCTGTAAAGGGGGCGCTGATGGCCAACTTC
CTCACACAAGGCCAGGTTTGCTGTAATGGCACAAGAGTATTTGTGCAGAAAGAAATTCTT
GATAAATTTACAGAGGAAGTGGTGAAACAGACCCAAAGGATTAAAATTGGAGATCCCCTT
CTGGAAGATACAAGGATGGGTCCACTCATCAACCGACCACACCTGGAGCGAGTCCTTGGG
TTTGTCAAAGTGGCAAAGGAGCAGGGTGCTAAAGTGTTATGTGGTGGAGATATATATGTA
CCTGAAGATCCCAAATTAAAGGATGGATATTACATGAGACCTTGTGTATTAACTAATTGC
AGAGACGACATGACCTGTGTGAAGGAAGAGATCTTTGGGCCTGTTATGTCCATTTTATCA
TTTGACACTGAAGCTGAGGTTCTAGAAAGAGCCAATGATACCACTTTTGGACTAGCAGCT
GGCGTCTTTACCAGGGACATCCAACGGGCTCATAGAGTGGTAGCTGAGCTTCAGGCTGGG
ACGTGCTTCATTAACAACTATAACGTCAGCCCAGTGGAGTTGCCCTTTGGTGGATATAAG
AAGTCAGGATTTGGCAGAGAGAACGGCCGTGTGACAATCGAATATTATTCACAGCTGAAG
ACTGTGTGTGTGGAGATGGGTGATGTGGAATCTGCTTTTTGA
|
| Enzyme 4 GenBank Gene ID |
U34252  |
| Enzyme 4 GeneCard ID |
ALDH9A1  |
| Enzyme 4 GenAtlas ID |
ALDH9A1  |
| Enzyme 4 HGNC ID |
HGNC:412  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
1q23.1 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Lin SW, Chen JC, Hsu LC, Hsieh CL, Yoshida A: Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression. Genomics. 1996 Jun 15;34(3):376-80. [PubMed
]
- Vaz FM, Fouchier SW, Ofman R, Sommer M, Wanders RJ: Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis. J Biol Chem. 2000 Mar 10;275(10):7390-4. [PubMed
]
- Kikonyogo A, Pietruszko R: Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution. Biochem J. 1996 May 15;316 ( Pt 1):317-24. [PubMed
]
- Kurys G, Shah PC, Kikonygo A, Reed D, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde. Eur J Biochem. 1993 Dec 1;218(2):311-20. [PubMed
]
- Kurys G, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde. J Biol Chem. 1989 Mar 15;264(8):4715-21. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5527 |
| Enzyme 5 Name |
Aldehyde dehydrogenase, dimeric NADP-preferring |
| Enzyme 5 Synonyms |
- ALDH class 3
- ALDHIII
|
| Enzyme 5 Gene Name |
ALDH3A1 |
| Enzyme 5 Protein Sequence |
>Aldehyde dehydrogenase, dimeric NADP-preferring
MSKISEAVKRARAAFSSGRTRPLQFRIQQLEALQRLIQEQEQELVGALAADLHKNEWNAY
YEEVVYVLEEIEYMIQKLPEWAADEPVEKTPQTQQDELYIHSEPLGVVLVIGTWNYPFNL
TIQPMVGAIAAGNAVVLKPSELSENMASLLATIIPQYLDKDLYPVINGGVPETTELLKER
FDHILYTGSTGVGKIIMTAAAKHLTPVTLELGGKSPCYVDKNCDLDVACRRIAWGKFMNS
GQTCVAPDYILCDPSIQNQIVEKLKKSLKEFYGEDAKKSRDYGRIISARHFQRVMGLIEG
QKVAYGGTGDAATRYIAPTILTDVDPQSPVMQEEIFGPVLPIVCVRSLEEAIQFINQREK
PLALYMFSSNDKVIKKMIAETSSGGVAANDVIVHITLHSLPFGGVGNSGMGSYHGKKSFE
TFSHRRSCLVRPLMNDEGLKVRYPPSPAKMTQH
|
| Enzyme 5 Number of Residues |
453 |
| Enzyme 5 Molecular Weight |
50380 |
| Enzyme 5 Theoretical pI |
6.52 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Energy production and conversion |
| Enzyme 5 Specific Function |
ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
178402  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P30838  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
AL3A1_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1362 bp
ATGAGCAAGATCAGCGAGGCCGTGAAGCGCGCCCGCGCCGCCTTCAGCTCGGGCAGGACC
CGTCCGCTGCAGTTCCGATTCCAGCAGCTGGAGGCGCTGCAGCGCCTGATCCAGGAGCAG
GAGCAGGAGCTGGTGGGCGCGCTGGCCGCAGACCTGCACAAGAATGAATGGAACGCCTAC
TATGAGGAGGTGGTGTACGTCCTAGAGGAGATCGAGTACATGATCCAGAAGCTCCCTGAG
TGGGCCGCGGATGAGCCCGTGGAGAAGACGCCCCAGACTCAGCAGGACGAGCTCTACATC
CACTCGGAGCCACTGGGCGTGGTCCTCGTCATTGGCACCTGGAACTACCCCTTCAACCTC
ACCATCCAGCCCATGGTGGGCGCCATCGCTGCAGGGAACGCAGTGGTCCTCAAGCCCTCG
GAGCTGAGTGAGAACATGGCGAGCCTGCTGGCTACCATCATCCCCCAGTACCTGGACAAG
GATCTGTACCCAGTAATCAATGGGGGTGTCCCTGAGACCACGGAGCTGCTCAAGGAGAGG
TTCGACCATATCCTGTACACGGGCAGCACGGGGGTGGGGAAGATCATCATGACGGCTGCT
GCCAAGCACCTGACCCCTGTCACGCTGGAGCTGGGAGGGAAGAGTCCCTGCTACGTGGAC
AAGAACTGTGACCTGGACGTGGCCTGCCGACGCATCGCCTGGGGGAAATTCATGAACAGT
GGCCAGACCTGCGTGGCCCCAGACTACATCCTCTGTGACCCCTCGATCCAGAACCAAATT
GTGGAGAAGCTCAAGAAGTCACTGAAAGAGTTCTACGGGGAAGATGCTAAGAAATCCCGG
GACTATGGAAGAATCATTAGTGCCCGGCACTTCCAGAGGGTGATGGGCCTGATTGAGGGC
CAGAAGGTGGCTTATGGGGGCACCGGGGATGCCGCCACTCGCTACATAGCCCCCACCATC
CTCACGGACGTGGACCCCCAGTCCCCGGTGATGCAAGAGGAGATCTTCGGGCCTGTGCTG
CCCATCGTGTGCGTGCGCAGCCTGGAGGAGGCCATCCAGTTCATCAACCAGCGTGAGAAG
CCCCTGGCCCTCTACATGTTCTCCAGCAACGACAAGGTGATTAAGAAGATGATTGCAGAG
ACATCCAGTGGTGGGGTGGCGGCCAACGATGTCATCGTCCACATCACCTTGCACTCTCTG
CCCTTCGGGGGCGTGGGGAACAGCGGCATGGGATCCTACCATGGCAAGAAGAGCTTCGAG
ACTTTCTCTCACCGCCGCTCTTGCCTGGTGAGGCCTCTGATGAATGATGAAGGCCTGAAG
GTCAGATACCCCCCGAGCCCGGCCAAGATGACCCAGCACTGA
|
| Enzyme 5 GenBank Gene ID |
M74542  |
| Enzyme 5 GeneCard ID |
ALDH3A1  |
| Enzyme 5 GenAtlas ID |
ALDH3A1  |
| Enzyme 5 HGNC ID |
HGNC:405  |
| Enzyme 5 Chromosome Location |
17 |
| Enzyme 5 Locus |
17p11.2 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Hsu LC, Chang WC, Shibuya A, Yoshida A: Human stomach aldehyde dehydrogenase cDNA and genomic cloning, primary structure, and expression in Escherichia coli. J Biol Chem. 1992 Feb 15;267(5):3030-7. [PubMed
]
- Hsu LC, Yoshida A: Human stomach aldehyde dehydrogenase, ALDH3. Adv Exp Med Biol. 1993;328:141-52. [PubMed
]
- Yin SJ, Vagelopoulos N, Wang SL, Jornvall H: Structural features of stomach aldehyde dehydrogenase distinguish dimeric aldehyde dehydrogenase as a 'variable' enzyme. 'Variable' and 'constant' enzymes within the alcohol and aldehyde dehydrogenase families. FEBS Lett. 1991 May 20;283(1):85-8. [PubMed
]
- Tsukamoto N, Chang C, Yoshida A: Mutations associated with Sjogren-Larsson syndrome. Ann Hum Genet. 1997 May;61(Pt 3):235-42. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5528 |
| Enzyme 6 Name |
Alpha-aminoadipic semialdehyde dehydrogenase |
| Enzyme 6 Synonyms |
- Alpha-AASA dehydrogenase
- Delta1-piperideine-6-carboxylate dehydrogenease
- P6c dehydrogenase
- Aldehyde dehydrogenase family 7 member A1
- Antiquitin-1
|
| Enzyme 6 Gene Name |
ALDH7A1 |
| Enzyme 6 Protein Sequence |
>Alpha-aminoadipic semialdehyde dehydrogenase
MSTLLINQPQYAWLKELGLREENEGVYNGSWGGRGEVITTYCPANNEPIARVRQASVADY
EETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQ
EYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIA
MICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVN
LLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQ
RCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEA
KKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWN
NEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRES
GSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ
|
| Enzyme 6 Number of Residues |
511 |
| Enzyme 6 Molecular Weight |
55367 |
| Enzyme 6 Theoretical pI |
6.86 |
| Enzyme 6 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Energy production and conversion |
| Enzyme 6 Specific Function |
L-2-aminoadipate 6-semialdehyde + NAD(P)(+) + H(2)O = L-2-aminoadipate + NAD(P)H |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
797410  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P49419  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
AL7A1_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1536 bp
ATGTCCACTCTCCTCATCAATCAGCCCCAGTATGCGTGGCTGAAAGAGCTGGGGCTCCGC
GAGGAAAACGAGGGCGTGTATAATGGAAGCTGGGGAGGCCGGGGAGAGGTTATTACGACC
TATTGCCCCGCTAACAACGAGCCAATAGCAAGAGTCCGACAGGCCAGTGTGGCAGACTAT
GAAGAAACTGTAAAGAAAGCAAGAGAAGCATGGAAAATCTGGGCAGATATTCCTGCTCCA
AAACGAGGAGAAATAGTAAGACAGATTGGCGATGCCTTGCGGGAGAAGATCCAAGTACTA
GGAAGCTTGGTGTCTTTGGAGATGGGGAAAATCTTAGTGGAAGGTGTGGGTGAAGTTCAG
GAGTATGTGGATATCTGTGACTATGCTGTTGGTTTATCAAGGATGATTGGAGGACCTATC
TTGCCTTCTGAAAGATCTGGCCATGCACTGATTGAGCAGTGGAATCCCGTAGGCCTGGTT
GGAATCATCACGGCATTCAATTTCCCTGTGGCAGTGTATGGTTGGAACAACGCCATCGCC
ATGATCTGTGGAAATGTCTGCCTCTGGAAAGGAGCTCCAACCACTTCCCTCATTAGTGTG
GCTGTCACAAAGATAATAGCCAAGGTTCTGGAGGACAACAAGCTGCCTGGTGCAATTTGT
TCCTTGACTTGTGGTGGAGCAGATATTGGCACAGCAATGGCCAAAGATGAACGAGTGAAC
CTGCTGTCCTTCACTGGGAGCACTCAGGTGGGAAAACAGGTGGGCCTGATGGTGCAGGAG
AGGTTTGGGAGAAGTCTGTTGGAACTTGGAGGAAACAATGCCATTATTGCCTTTGAAGAT
GCAGACCTCAGCTTAGTTGTTCCATCAGCTCTCTTCGCTGCTGTGGGAACAGCTGGCCAG
AGGTGTACCACTGCGAGGCGACTGTTTATACATGAAAGCATCCATGATGAGGTTGTAAAC
AGACTTAAAAAGGCCTATGCACAGATCCGAGTTGGGAACCCATGGGACCCTAATGTTCTC
TATGGGCCACTCCACACCAAGCAGGCAGTGAGCATGTTTCTTGGAGCAGTGGAAGAAGCA
AAGAAAGAAGGTGGCACAGTGGTCTATGGGGGCAAGGTTATGGATCGCCCTGGAAATTAT
GTAGAACCGACAATTGTGACAGGTCTTGGCCACGATGCGTCCATTGCACACACAGAGACT
TTCGCTCCGATTCTCTATGTCTTTAAATTCAAGAATGAAGAAGAGGTCTTTGCATGGAAT
AATGAAGTAAAACAGGGACTTTCAAGTAGCATCTTTACCAAAGATCTGGGCAGAATCTTT
CGCTGGCTTGGACCTAAAGGATCAGACTGTGGCATTGTAAATGTCAACATTCCAACAAGT
GGGGCTGAGATTGGAGGTGCCTTTGGAGGAGAAAAGCACACTGGTGGTGGCAGGGAGTCT
GGCAGTGATGCCTGGAAACAGTACATGAGAAGGTCTACTTGTACTATCAACTACAGTAAA
GACCTTCCTCTGGCCCAAGGAATCAAGTTTCAGTAA
|
| Enzyme 6 GenBank Gene ID |
S74728  |
| Enzyme 6 GeneCard ID |
ALDH7A1  |
| Enzyme 6 GenAtlas ID |
ALDH7A1  |
| Enzyme 6 HGNC ID |
HGNC:877  |
| Enzyme 6 Chromosome Location |
5 |
| Enzyme 6 Locus |
5q31 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Lee P, Kuhl W, Gelbart T, Kamimura T, West C, Beutler E: Homology between a human protein and a protein of the green garden pea. Genomics. 1994 May 15;21(2):371-8. [PubMed
]
- Skvorak AB, Robertson NG, Yin Y, Weremowicz S, Her H, Bieber FR, Beisel KW, Lynch ED, Beier DR, Morton CC: An ancient conserved gene expressed in the human inner ear: identification, expression analysis, and chromosomal mapping of human and mouse antiquitin (ATQ1). Genomics. 1997 Dec 1;46(2):191-9. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5529 |
| Enzyme 7 Name |
Aldehyde dehydrogenase 1A3 |
| Enzyme 7 Synonyms |
- Aldehyde dehydrogenase 6
- Retinaldehyde dehydrogenase 3
- RALDH-3
|
| Enzyme 7 Gene Name |
ALDH1A3 |
| Enzyme 7 Protein Sequence |
>Aldehyde dehydrogenase 1A3
MATANGAVENGQPDRKPPALPRPIRNLEVKFTKIFINNEWHESKSGKKFATCNPSTREQI
CEVEEGDKPDVDKAVEAAQVAFQRGSPWRRLDALSRGRLLHQLADLVERDRATLAALETM
DTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPW
NFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTV
GAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVE
CAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQK
QFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPIL
KFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGF
KMSGNGRELGEYALAEYTEVKTVTIKLGDKNP
|
| Enzyme 7 Number of Residues |
512 |
| Enzyme 7 Molecular Weight |
56109 |
| Enzyme 7 Theoretical pI |
7.29 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Energy production and conversion |
| Enzyme 7 Specific Function |
Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Seems to be the key enzyme in the formation of an RA gradient along the dorso-ventral axis during the early eye development and also in the development of the olfactory system |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
544482  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P47895  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
AL1A3_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1539 bp
ATGGCCACCGCTAACGGGGCCGTGGAAAACGGGCAGCCGGACGGGAAGCCGCCGGCCCTG
CCGCGCCCCATCCGCAACCTGGAGGTCAAGTTCACCAAGATATTTATCAACAATGAATGG
CACGAATCCAAGAGTGGGAAAAAGTTTGCTACATGTAACCCTTCAACTCGGGAGCAAATA
TGTGAAGTGGAAGAAGGAGATAAGCCCGACGTGGACAAGGCTGTGGAGGCTGCACAGGTT
GCCTTCCAGAGGGGCTCGCCATGGCGCCGGCTGGATGCCCTGAGTCGTGGGCGGCTGCTG
CACCAGCTGGCTGACCTGGTGGAGAGGGACCGCGCCACCTTGGCCGCCCTGGAGACGATG
GATACAGGGAAGCCATTTCTTCATGCTTTTTTCATCGACCTGGAGGGCTGTATTAGAACC
CTCAGATACTTTGCAGGGTGGGCAGACAAAATCCAGGGCAAGACCATCCCCACAGATGAC
AACGTCGTATGCTTCACCAGGCATGAGCCCATTGGTGTCTGTGGGGCCATCACTCCATGG
AACTTCCCCCTGCTGATGCTGGTGTGGAAGCTGGCACCCGCCCTCTGCTGTGGGAACACC
ATGGTCCTGAAGCCTGCGGAGCAGACACCTCTCACCGCCCTTTATCTCGGCTCTCTGATC
AAAGAGGCCGGGTTCCCTCCAGGAGTGGTGAACATTGTGCCAGGATTCGGGCCCACAGTG
GGAGCAGCAATTTCTTCTCACCCTCAGATCAACAAGATCGCCTTCACCGGCTCCACAGAG
GTTGGAAAACTGGTTAAAGAAGCTGCGTCCCGGAGCAATCTGAAGCGGGTGACGCTGGAG
CTGGGGGGGAAGAACCCCTGCATCGTGTGTGCGGACGCTGACTTGGACTTGGCAGTGGAG
TGTGCCCATCAGGGAGTGTTCTTCAACCAAGGCCAGTGTTGCACGGCAGCCTCCAGGGTG
TTCGTGGAGGAGCAGGTCTACTCTGAGTTTGTCAGGCGGAGCGTGGAGTATGCCAAGAAA
CGGCCCGTGGGAGACCCCTTCGATGTCAAAACAGAACAGGGGCCTCAGATTGATCAAAAG
CAGTTCGACAAAATCTTAGAGCTGATCGAGAGTGGGAAGAAGGAAGGGGCCAAGCTGGAA
TGCGGGGGCTCAGCCATGGAAGACAAGGGGCTCTTCATCAAACCCACTGTCTTCTCAGAA
GTCACAGACAACATGCGGATTGCCAAAGAGGAGATTTTCGGGCCAGTGCAACCAATACTG
AAGTTCAAAAGTATCGAAGAAGTGATAAAAAGAGCGAATAGCACCGACTATGGACTCACA
GCAGCCGTGTTCACAAAAAATCTCGACAAAGCCCTGAAGTTGGCTTCTGCCTTAGAGTCT
GGAACGGTCTGGATCAACTGCTACAACGCCCTCTATGCACAGGCTCCATTTGGTGGCTTT
AAAATGTCAGGAAATGGCAGAGAACTAGGTGAATACGCTTTGGCCGAATACACAGAAGTG
AAAACTGTCACCATCAAACTTGGCGACAAGAACCCCTGA
|
| Enzyme 7 GenBank Gene ID |
U07919  |
| Enzyme 7 GeneCard ID |
ALDH1A3  |
| Enzyme 7 GenAtlas ID |
ALDH1A3  |
| Enzyme 7 HGNC ID |
HGNC:409  |
| Enzyme 7 Chromosome Location |
15 |
| Enzyme 7 Locus |
15q26.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Hsu LC, Chang WC, Hiraoka L, Hsieh CL: Molecular cloning, genomic organization, and chromosomal localization of an additional human aldehyde dehydrogenase gene, ALDH6. Genomics. 1994 Nov 15;24(2):333-41. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5530 |
| Enzyme 8 Name |
Aldehyde dehydrogenase, mitochondrial precursor |
| Enzyme 8 Synonyms |
- ALDH class 2
- ALDHI
- ALDH-E2
|
| Enzyme 8 Gene Name |
ALDH2 |
| Enzyme 8 Protein Sequence |
>Aldehyde dehydrogenase, mitochondrial precursor
MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPS
TGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLA
ALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCG
QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPG
FGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADM
DWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGP
QVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGP
VMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS
PFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
|
| Enzyme 8 Number of Residues |
517 |
| Enzyme 8 Molecular Weight |
56382 |
| Enzyme 8 Theoretical pI |
7.05 |
| Enzyme 8 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Energy production and conversion |
| Enzyme 8 Specific Function |
An aldehyde + NAD(+) + H(2)O = an acid + NADH |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- an aldehyde + NAD+ + H2O = an acid + NADH + H+
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
Not Available |
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
28606  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P05091  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
ALDH2_HUMAN  |
| Enzyme 8 PDB ID |
1OF7  |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1551 bp
ATGTTGCGCGCTGCCGCCGCTCGGGCCCCGCCTGGCCGCCGCCTCTTGTCAGCCGCCGCC
ACCCAGGCCGTGCCTGCCCCCAACCAGCAGCCCGAGGTCTTCTGCAACCAGATTTTCATA
AACAATGAATGGCACGATGCCGTCAGCAGGAAAACATTCCCCACCGTCAATCCGTCCACT
GGAGAGGTCATCTGTCAGGTAGCTGAAGGGGACAAGGAAGATGTGGACAAGGCACGTGAA
GGCCGCCCGGGCGCCTTCCAGCTGGGCTCACCTTGGCGCCGCATGGACGCATCACACAGC
GGCCGGCTGCTGAACCGCCTGGCCGATCTGATCGAGCGGGACCGGACCTACCTGGCGGCC
TTGGAGACCCTGGACAATGGCAAGCCCTATGTCATCTCCTACCTGGTGGATTTGGACATG
GTCCTCAAATGTCTCCGGTATTATGCCGGCTGGGCTGATAAGTACCACGGGAAAACCATC
CCCATTGACGGAGACTTCTTCAGCTACACACGCCATGAACCTGTGGGGGTGTGCGGGCAG
ATCATTCCGTGGAATTTCCCGCTCCTGATGCAAGCATGGAAGCTGGGCCCAGCCTTGGCA
ACTGGAAACGTGGTTGTGATGAAGGTAGCTGAGCAGACACCCCTCACCGCCCTCTATGTG
GCCAACCTGATCAAGGAGGCTGGCTTTCCCCCTGGTGTGGTCAACATTGTGCCTGGATTT
GGCCCCACGGCTGGGGCCGCCATTGCCTCCCATGAGGATGTGGACAAAGTGGCATTCACA
GGCTCCACTGAGATTGGCCGCGTAATCCAGGTTGCTGCTGGGAGCAGCAACCTCAAGAGA
GTGACCTTGGAGCTGGGGGGGAAGAGCCCCAACATCATCATGTCAGATGCCGATATGGAT
TGGGCCGTGGAACAGGCCCACTTCGCCCTGTTCTTCAACCAGGGCCAGTGCTGCTGTGCC
GGCTCCCGGACCTTCGTGCAGGAGGACATCTATGATGAGTTTGTGGTGCGGAGCGTTGCC
CGGGCCAAGTCTCGGGTGGTCGGGAACCCCTTTGATAGCAAGACCGAGCAGGGGCCGCAG
GTGGATGAAACTCAGTTTAAGAAGATCCTCGGCTACATCAACACGGGGAAGCAAGAGGGG
GCGAAGCTGCTGTGTGGTGGGGGCATTGCTGCTGACCGTGGTTACTTCATCCAGCCCACT
GTGTTTGGAGATGTGCAGGATGGCATGACCATCGCCAAGGAGGAGATCTTCGGGCCAGTG
ATGCAGATCCTGAAGTTCAAGACCATAGAGGAGGTTGTTGGGAGAGCCAACAATTCCACG
TACGGGCTGGCCGCAGCTGTCTTCACAAAGGATTTGGACAAGGCCAATTACCTGTCCCAG
GCCCTCCAGGCGGGCACTGTGTGGGTCAACTGCTATGATGTGTTTGGAGCCCAGTCACCC
TTTGGTGGCTACAAGATGTCGGGGAGTGGCCGGGAGTTGGGCGAGTACGGGCTGCAGGCA
TACACTGAAGTGAAAACTGTCACAGTCAAAGTGCCTCAGAAGAACTCATAA
|
| Enzyme 8 GenBank Gene ID |
X05409  |
| Enzyme 8 GeneCard ID |
ALDH2  |
| Enzyme 8 GenAtlas ID |
ALDH2  |
| Enzyme 8 HGNC ID |
HGNC:404  |
| Enzyme 8 Chromosome Location |
12 |
| Enzyme 8 Locus |
12q24.2 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Evidence for a signal peptide at the amino-terminal end of human mitochondrial aldehyde dehydrogenase. FEBS Lett. 1987 May 11;215(2):233-6. [PubMed
]
- Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Isolation and sequence analysis of a full length cDNA clone coding for human mitochondrial aldehyde dehydrogenase. Nucleic Acids Res. 1987 Apr 10;15(7):3179. [PubMed
]
- Hsu LC, Bendel RE, Yoshida A: Genomic structure of the human mitochondrial aldehyde dehydrogenase gene. Genomics. 1988 Jan;2(1):57-65. [PubMed
]
- Hempel J, Kaiser R, Jornvall H: Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations. Eur J Biochem. 1985 Nov 15;153(1):13-28. [PubMed
]
- Hsu LC, Tani K, Fujiyoshi T, Kurachi K, Yoshida A: Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3771-5. [PubMed
]
- Yoshida A, Ikawa M, Hsu LC, Tani K: Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases. Alcohol. 1985 Jan-Feb;2(1):103-6. [PubMed
]
- Agarwal DP, Goedde HW: Human aldehyde dehydrogenase isozymes and alcohol sensitivity. Isozymes Curr Top Biol Med Res. 1987;16:21-48. [PubMed
]
- Hempel J, Hoog JO, Jornvall H: Mitochondrial aldehyde dehydrogenase. Homology of putative targeting sequence to that of carbamyl phosphate synthetase I revealed by correlation of cDNA and protein data. FEBS Lett. 1987 Sep 28;222(1):95-8. [PubMed
]
- Yoshida A, Huang IY, Ikawa M: Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals. Proc Natl Acad Sci U S A. 1984 Jan;81(1):258-61. [PubMed
]
- Novoradovsky A, Tsai SJ, Goldfarb L, Peterson R, Long JC, Goldman D: Mitochondrial aldehyde dehydrogenase polymorphism in Asian and American Indian populations: detection of new ALDH2 alleles. Alcohol Clin Exp Res. 1995 Oct;19(5):1105-10. [PubMed
]
- Ni L, Zhou J, Hurley TD, Weiner H: Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms. Protein Sci. 1999 Dec;8(12):2784-90. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5531 |
| Enzyme 9 Name |
Fatty aldehyde dehydrogenase |
| Enzyme 9 Synonyms |
- Aldehyde dehydrogenase, microsomal
- Aldehyde dehydrogenase family 3 member A2
- Aldehyde dehydrogenase 10
|
| Enzyme 9 Gene Name |
ALDH3A2 |
| Enzyme 9 Protein Sequence |
>Fatty aldehyde dehydrogenase
MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQE
VITVLGEIDFMLENLPEWVTAKPVKKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQ
PLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVEETTELLKQRFDH
IFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQT
CIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKI
AFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLA
LYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFS
HQRPCLLKSLKREGANKLRYPPNSQSKVDWGKFFLLKRFNKEKLGLLLLTFLGIVAAVLV
KAEYY
|
| Enzyme 9 Number of Residues |
485 |
| Enzyme 9 Molecular Weight |
54849 |
| Enzyme 9 Theoretical pI |
7.99 |
| Enzyme 9 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 9 General Function |
Energy production and conversion |
| Enzyme 9 Specific Function |
Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- an aldehyde + NAD+ + H2O = an acid + NADH + H+
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
1082036  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P51648  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
AL3A2_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1458 bp
ATGGAGCTCGAAGTCCGGCGGGTCCGACAGGCGTTCCTGTCCGGCCGGTCGCGACCTCTG
CGGTTTCGGCTGCAGCAGCTGGAGGCCCTGCGGAGGATGGTGCAGGAGCGCGAGAAGGAT
ATCCTGACGGCCATCGCCGCCGACCTGTGCAAGAGTGAATTCAATGTGTACAGTCAGGAA
GTCATTACTGTCCTTGGGGAAATTGATTTTATGCTTGAGAATCTTCCTGAATGGGTTACT
GCTAAACCAGTTAAGAAGAACGTGCTCACCATGCTGGATGAGGCCTATATTCAGCCACAG
CCTCTGGGAGTGGTGCTGATAATCGGAGCTTGGAATTACCCCTTCGTTCTCACCATTCAG
CCACTGATAGGAGCCATCGCTGCAGGAAATGCTGTGATTATAAAGCCTTCTGAACTGAGT
GAAAATACAGCCAAGATCTTGGCAAAGCTTCTCCCTCAGTATTTAGACCAGGATCTCTAT
ATTGTTATTAATGGTGGTGTTGAGGAAACCACGGAGCTCCTGAAGCAGCGATTTGACCAC
ATTTTCTATACGGGAAACACTGCGGTTGGCAAAATTGTCATGGAAGCTGCTGCCAAGCAT
CTGACCCCTGTGACTCTTGAACTGGGAGGGAAAAGTCCATGTTATATTGATAAAGATTGT
GACCTGGACATTGTTTGCAGACGCATAACCTGGGGAAAATACATGAATTGTGGCCAAACC
TGCATTGCACCCGACTATATTCTCTGTGAAGCATCCCTCCAAAATCAAATTGTATGGAAG
ATTAAGGAAACAGTGAAGGAATTTTATGGAGAAAATATAAAAGAGTCTCCTGATTATGAA
AGGATCATCAATCTTCGTCATTTTAAGAGGATACTAAGTTTGCTTGAAGGACAAAAGATA
GCTTTTGGTGGGGAGACTGATGAGGCCACACGCTACATAGCCCCAACAGTACTTACCGAT
GTTGATCCTAAAACCAAGGTGATGCAAGAAGAAATTTTTGGACCAATTCTTCCAATAGTG
CCTGTGAAAAATGTAGATGAGGCCATAAATTTCATAAATGAACGTGAAAAGCCTCTGGCT
CTTTATGTATTTTCGCATAACCATAAGCTCATCAAACGGATGATTGATGAGACATCCAGT
GGAGGTGTCACAGGCAATGACGTCATTATGCACTTCACGCTCAACTCTTTCCCATTTGGA
GGAGTGGGTTCCAGTGGGATGGGAGCTTATCACGGAAAACATAGTTTTGATACTTTTTCT
CATCAGCGTCCCTGTTTATTAAAAAGTTTAAAGAGAGAAGGTGCTAACAAACTCAGATAT
CCTCCCAACAGCCAGTCAAAGGTGGATTGGGGGAAATTTTTTCTCTTGAAACGGTTCAAC
AAAGAAAAACTCGGTCTCCTGTTGCTCACTTTCCTGGGTATTGTAGCCGCTGTGCTTGTC
AAGGCAGAATATTACTGA
|
| Enzyme 9 GenBank Gene ID |
L47162  |
| Enzyme 9 GeneCard ID |
ALDH3A2  |
| Enzyme 9 GenAtlas ID |
ALDH3A2  |
| Enzyme 9 HGNC ID |
HGNC:403  |
| Enzyme 9 Chromosome Location |
17 |
| Enzyme 9 Locus |
17p11.2 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- De Laurenzi V, Rogers GR, Hamrock DJ, Marekov LN, Steinert PM, Compton JG, Markova N, Rizzo WB: Sjogren-Larsson syndrome is caused by mutations in the fatty aldehyde dehydrogenase gene. Nat Genet. 1996 Jan;12(1):52-7. [PubMed
]
- Rogers GR, Markova NG, De Laurenzi V, Rizzo WB, Compton JG: Genomic organization and expression of the human fatty aldehyde dehydrogenase gene (FALDH). Genomics. 1997 Jan 15;39(2):127-35. [PubMed
]
- Chang C, Yoshida A: Human fatty aldehyde dehydrogenase gene (ALDH10): organization and tissue-dependent expression. Genomics. 1997 Feb 15;40(1):80-5. [PubMed
]
- Sillen A, Jagell S, Wadelius C: A missense mutation in the FALDH gene identified in Sjogren-Larsson syndrome patients originating from the northern part of Sweden. Hum Genet. 1997 Aug;100(2):201-3. [PubMed
]
- Sillen A, Anton-Lamprecht I, Braun-Quentin C, Kraus CS, Sayli BS, Ayuso C, Jagell S, Kuster W, Wadelius C: Spectrum of mutations and sequence variants in the FALDH gene in patients with Sjogren-Larsson syndrome. Hum Mutat. 1998;12(6):377-84. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5532 |
| Enzyme 10 Name |
Aldehyde dehydrogenase X, mitochondrial precursor |
| Enzyme 10 Synonyms |
- Aldehyde dehydrogenase family 1 member B1
- ALDH class 2
|
| Enzyme 10 Gene Name |
ALDH1B1 |
| Enzyme 10 Protein Sequence |
>Aldehyde dehydrogenase X, mitochondrial precursor
MLRFLAPRLLSLQGRTARYSSAAALPSPILNPDIPYNQLFINNEWQDAVSKKTFPTVNPT
TGEVIGHVAEGDRADVDRAVKAAREAFRLGSPWRRMDASERGRLLNLLADLVERDRVYLA
SLETLDNGKPFQESYALDLDEVIKVYRYFAGWADKWHGKTIPMDGQHFCFTRHEPVGVCG
QIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITG
YGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGDSNLKRVTLELGGKSPSIVLADADM
EHAVEQCHEALFFNMGQCCCAGSRTFVEESIYNEFLERTVEKAKQRKVGNPFELDTQQGP
QVDKEQFERVLGYIQLGQKEGAKLLCGGERFGERGFFIKPTVFGGVQDDMRIAKEEIFGP
VQPLFKFKKIEEVVERANNTRYGLAAAVFTRDLDKAMYFTQALQAGTVWVNTYNIVTCHT
PFGGFKESGNGRELGEDGLKAYTEVKTVTIKVPQKNS
|
| Enzyme 10 Number of Residues |
517 |
| Enzyme 10 Molecular Weight |
57239 |
| Enzyme 10 Theoretical pI |
6.79 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 10 General Function |
Energy production and conversion |
| Enzyme 10 Specific Function |
ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- an aldehyde + NAD+ + H2O = an acid + NADH + H+
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
Not Available |
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
1263008  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P30837  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
AL1B1_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1554 bp
ATGCTGCGCTTCCTGGCACCCCGGCTGCTTAGCCTCCAGGGCAGGACCGCCCTCTACTCC
TCGGCAGCAGCCCTCCCAAGCCCCATTCTGAACCCAGACATCCCCTACAACCAGCTGTTC
ATCAACAATGAATGGCAAGATGCAGTCAGCAAGAAGACCTTCCCGACGGTCAACCCTACC
ACCGGGGAGGTCATCGGGCACGTGGCTGAAGGTGACCGGGCTGATGTGGATCGGGCCGTG
AAAGCAGCCCGGGAAGCCTTCCGCCTGGGGTCCCCATGGCGCCGGATGGATGCCTCTGAG
CGGGGCCGGCTGCTGAACCTCCTGGCAGACCTAGTGGAGCGGGATCGAGTCTACTTGGCC
TCACTCGAGACCTTGGACAATGGGAAGCCTTTCCAAGAGTCTTACGCCTTGGACTTGGAT
GAGGTCATCAAGGTGTATCGGTACTTTGCTGGCTGGGCTGACAAGTGGCATGGCAAGACC
ATCCCCATGCATGGCCAGCATTTCTGCTTCACCCGGCATGAGCCCGTTGGTGTCTGTGGC
CAGATCATCCCGTGGAACTTCCCCTTGGTCATGCAGGGTTGGAAACTTGCCCCGGCACTC
GCCACAGGCAACACTGTGGTTATGAAGGTGGCAGAGCAGACCCCCCTCTCTGCCCTGTAT
TTGGCCTCCCTCATCAAGGAGGCAGGCTTTCCCCCTGGGGTGGTGAACATCATCACGGGG
TATGGCCCAACAGCAGGTGCGGCCATCGCCCAGCACATGGATGTTGACAAAGTTGCCTTC
ACCGGTTCCACCGAGGTGGGCCACCTGATCCAGAAAGCAGCTGGCGATTCCAACCTCAAG
AGAGTCACCCTGGAGCTGGGTGGTAAGAGCCCCAGCATCGTGCTGGCCGATGCTGACATG
GAGCATGCCGTGGAGCAGTGCCACGAAGCCCTGTTCTTCAACATGGGCCAGTGCTGCTGT
GCTGGCTCCCGGACCTTCGTGGAAGAATCCATCTACAATGAGTTTCTCGAGAGAACCGTG
GAGAAAGCAAAGCAGAGGAAAGTGGGGAACCCCTTTGAGCTGGACACCCAGCAGGGGCCT
CAGGTGGACAAGGAGCAGTTTGAACGAGTCCTAGGCTACATCCAGCTTGGCCAGAAGGAG
GGCGCAAAACTCCTCTGTGGCGGAGAGCGTTTCGGGGAGCGTGGTTTCTTCATCAAGCCT
ACTGTCTTTGGTGGCGTGCAGGATGACATGAGAATTGCCAAAGAGGAGATCTTTGGGCCT
GTGCAGCCCCTGTTCAAGTTCAAGAAGATTGAGGAGGTGGTTGAGAGGGCCAACAACACC
AGGTATGGCCTGGCTGCGGCTGTGTTCACCCGGGATCTGGACAAGGCCATGTACTTCACC
CAGGCACTCCAGGCCGGGACCGTGTGGGTAAACACCTACAACATCGTCACCTGCCACACG
CCATTTGGAGGGTTTAAGGAATCTGGAAACGGGAGGGAGCTGGGTGAGGATGGGCTTAAG
GCCTACACAGAGGTAAAGACGGTCACCATCAAGGTTCCTCAGAAGAACTCGTAA
|
| Enzyme 10 GenBank Gene ID |
M63967  |
| Enzyme 10 GeneCard ID |
ALDH1B1  |
| Enzyme 10 GenAtlas ID |
ALDH1B1  |
| Enzyme 10 HGNC ID |
HGNC:407  |
| Enzyme 10 Chromosome Location |
9 |
| Enzyme 10 Locus |
9p11.1 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Hsu LC, Chang WC: Cloning and characterization of a new functional human aldehyde dehydrogenase gene. J Biol Chem. 1991 Jul 5;266(19):12257-65. [PubMed
]
- Sherman D, Dave V, Hsu LC, Peters TJ, Yoshida A: Diverse polymorphism within a short coding region of the human aldehyde dehydrogenase-5 (ALDH5) gene. Hum Genet. 1993 Nov;92(5):477-80. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5771 |
| Enzyme 11 Name |
Platelet-activating factor acetylhydrolase precursor |
| Enzyme 11 Synonyms |
- PAF acetylhydrolase
- PAF 2-acylhydrolase
- LDL-associated phospholipase A2
- LDL-PLA(2
- 2-acetyl-1-alkylglycerophosphocholine esterase
- 1-alkyl-2-acetylglycerophosphocholine esterase
|
| Enzyme 11 Gene Name |
PLA2G7 |
| Enzyme 11 Protein Sequence |
>Platelet-activating factor acetylhydrolase precursor
MVPPKLHVLFCLCGCLAVVYPFDWQYINPVAHMKSSAWVNKIQVLMAAASFGQTKIPRGN
GPYSVGCTDLMFDHTNKGTFLRLYYPSQDNDRLDTLWIPNKEYFWGLSKFLGTHWLMGNI
LRLLFGSMTTPANWNSPLRPGEKYPLVVFSHGLGAFRTLYSAIGIDLASHGFIVAAVEHR
DRSASATYYFKDQSAAEIGDKSWLYLRTLKQEEETHIRNEQVRQRAKECSQALSLILDID
HGKPVKNALDLKFDMEQLKDSIDREKIAVIGHSFGGATVIQTLSEDQRFRCGIALDAWMF
PLGDEVYSRIPQPLFFINSEYFQYPANIIKMKKCYSPDKERKMITIRGSVHQNFADFTFA
TGKIIGHMLKLKGDIDSNVAIDLSNKASLAFLQKHLGLHKDFDQWDCLIEGDDENLIPGT
NINTTNQHIMLQNSSGIEKYN
|
| Enzyme 11 Number of Residues |
441 |
| Enzyme 11 Molecular Weight |
50078 |
| Enzyme 11 Theoretical pI |
7.61 |
| Enzyme 11 GO Classification |
| Function |
- 1-alkyl-2-acetylglycerophosphocholine esterase activity
- carboxylic ester hydrolase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
- lipid catabolism
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
- 2-acetyl-1-alkylglycerophosphocholine esterase complex
- protein complex
- unlocalized protein complex
|
|
| Enzyme 11 General Function |
Not Available |
| Enzyme 11 Specific Function |
Modulates the action of platelet-activating factor (PAF) by hydrolyzing the sn-2 ester bond to yield the biologically inactive lyso-PAF. Has a specificity for substrates with a short residue at the sn-2 position. It is inactive against long-chain phospholipids |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
Not Available |
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
780133  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q13093  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
PAFA_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1326 bp
ATGGTGCCACCCAAATTGCATGTGCTTTTCTGCCTCTGCGGCTGCCTGGCTGTGGTTTAT
CCTTTTGACTGGCAATACATAAATCCTGTTGCCCATATGAAATCATCAGCATGGGTCAAC
AAAATACAAGTACTGATGGCTGCTGCAAGCTTTGGCCAAACTAAAATCCCCCGGGGAAAT
GGGCCTTATTCCGTTGGTTGTACAGACTTAATGTTTGATCACACTAATAAGGGCACCTTC
TTGCGTTTATATTATCCATCCCAAGATAATGATCGCCTTGACACCCTTTGGATCCCAAAT
AAAGAATATTTTTGGGGTCTTAGCAAATTTCTTGGAACACACTGGCTTATGGGCAACATT
TTGAGGTTACTCTTTGGTTCAATGACAACTCCTGCAAACTGGAATTCCCCTCTGAGGCCT
GGTGAAAAATATCCACTTGTTGTTTTTTCTCATGGTCTTGGGGCATTCAGGACACTTTAT
TCTGCTATTGGCATTGACCTGGCATCTCATGGGTTTATAGTTGCTGCTGTAGAACACAGA
GATAGATCTGCATCTGCAACTTACTATTTCAAGGACCAATCTGCTGCAGAAATAGGGGAC
AAGTCTTGGCTCTACCTTAGAACCCTGAAACAAGAGGAGGAGACACATATACGAAATGAG
CAGGTACGGCAAAGAGCAAAAGAATGTTCCCAAGCTCTCAGTCTGATTCTTGACATTGAT
CATGGAAAGCCAGTGAAGAATGCATTAGATTTAAAGTTTGATATGGAACAACTGAAGGAC
TCTATTGATAGGGAAAAAATAGCAGTAATTGGACATTCTTTTGGTGGAGCAACGGTTATT
CAGACTCTTAGTGAAGATCAGAGATTCAGATGTGGTATTGCCCTGGATGCATGGATGTTT
CCACTGGGTGATGAAGTATATTCCAGAATTCCTCAGCCCCTCTTTTTTATCAACTCTGAA
TATTTCCAATATCCTGCTAATATCATAAAAATGAAAAAATGCTACTCACCTGATAAAGAA
AGAAAGATGATTACAATCAGGGGTTCAGTCCACCAGAATTTTGCTGACTTCACTTTTGCA
ACTGGCAAAATAATTGGACACATGCTCAAATTAAAGGGAGACATAGATTCAAATGTAGCT
ATTGATCTTAGCAACAAAGCTTCATTAGCATTCTTACAAAAGCATTTAGGACTTCATAAA
GATTTTGATCAGTGGGACTGCTTGATTGAAGGAGATGATGAGAATCTTATTCCAGGGACC
AACATTAACACAACCAATCAACACATCATGTTACAGAACTCTTCAGGAATAGAGAAATAC
AATTAG
|
| Enzyme 11 GenBank Gene ID |
U20157  |
| Enzyme 11 GeneCard ID |
PLA2G7  |
| Enzyme 11 GenAtlas ID |
PLA2G7  |
| Enzyme 11 HGNC ID |
HGNC:9040  |
| Enzyme 11 Chromosome Location |
6 |
| Enzyme 11 Locus |
6p21.2-p12 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Tjoelker LW, Wilder C, Eberhardt C, Stafforini DM, Dietsch G, Schimpf B, Hooper S, Le Trong H, Cousens LS, Zimmerman GA, et al.: Anti-inflammatory properties of a platelet-activating factor acetylhydrolase. Nature. 1995 Apr 6;374(6522):549-53. [PubMed
]
- Tew DG, Southan C, Rice SQ, Lawrence MP, Li H, Boyd HF, Moores K, Gloger IS, Macphee CH: Purification, properties, sequencing, and cloning of a lipoprotein-associated, serine-dependent phospholipase involved in the oxidative modification of low-density lipoproteins. Arterioscler Thromb Vasc Biol. 1996 Apr;16(4):591-9. [PubMed
]
- Tjoelker LW, Eberhardt C, Unger J, Trong HL, Zimmerman GA, McIntyre TM, Stafforini DM, Prescott SM, Gray PW: Plasma platelet-activating factor acetylhydrolase is a secreted phospholipase A2 with a catalytic triad. J Biol Chem. 1995 Oct 27;270(43):25481-7. [PubMed
]
- Stafforini DM, Satoh K, Atkinson DL, Tjoelker LW, Eberhardt C, Yoshida H, Imaizumi T, Takamatsu S, Zimmerman GA, McIntyre TM, Gray PW, Prescott SM: Platelet-activating factor acetylhydrolase deficiency. A missense mutation near the active site of an anti-inflammatory phospholipase. J Clin Invest. 1996 Jun 15;97(12):2784-91. [PubMed
]
- Yamada Y, Yokota M: Loss of activity of plasma platelet-activating factor acetylhydrolase due to a novel Gln281-->Arg mutation. Biochem Biophys Res Commun. 1997 Jul 30;236(3):772-5. [PubMed
]
- Hiramoto M, Yoshida H, Imaizumi T, Yoshimizu N, Satoh K: A mutation in plasma platelet-activating factor acetylhydrolase (Val279-->Phe) is a genetic risk factor for stroke. Stroke. 1997 Dec;28(12):2417-20. [PubMed
]
- Yamada Y, Ichihara S, Fujimura T, Yokota M: Identification of the G994--> T missense in exon 9 of the plasma platelet-activating factor acetylhydrolase gene as an independent risk factor for coronary artery disease in Japanese men. Metabolism. 1998 Feb;47(2):177-81. [PubMed
]
- Yoshida H, Imaizumi T, Fujimoto K, Itaya H, Hiramoto M, Yoshimizu N, Fukushi K, Satoh K: A mutation in plasma platelet-activating factor acetylhydrolase (Val279Phe) is a genetic risk factor for cerebral hemorrhage but not for hypertension. Thromb Haemost. 1998 Sep;80(3):372-5. [PubMed
]
- Kruse S, Mao XQ, Heinzmann A, Blattmann S, Roberts MH, Braun S, Gao PS, Forster J, Kuehr J, Hopkin JM, Shirakawa T, Deichmann KA: The Ile198Thr and Ala379Val variants of plasmatic PAF-acetylhydrolase impair catalytical activities and are associated with atopy and asthma. Am J Hum Genet. 2000 May;66(5):1522-30. Epub 2000 Mar 24. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5772 |
| Enzyme 12 Name |
Acetylcholinesterase precursor |
| Enzyme 12 Synonyms |
- AChE
|
| Enzyme 12 Gene Name |
ACHE |
| Enzyme 12 Protein Sequence |
>Acetylcholinesterase precursor
MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPV
SAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPN
RELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSM
NYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASV
GMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTEL
VACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVG
VVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPE
DPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGY
EIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQ
YVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN
QFDHYSKQDRCSDL
|
| Enzyme 12 Number of Residues |
614 |
| Enzyme 12 Molecular Weight |
67797 |
| Enzyme 12 Theoretical pI |
6.24 |
| Enzyme 12 GO Classification |
| Function |
- carboxylic ester hydrolase activity
- catalytic activity
- cholinesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 12 General Function |
Lipid transport and metabolism |
| Enzyme 12 Specific Function |
Rapidly hydrolyzes choline released into the synapse |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- acetylcholine + H2O = choline + acetate
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
Not Available |
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
177975  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P22303  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
ACES_HUMAN  |
| Enzyme 12 PDB ID |
1F8U  |
| Enzyme 12 PDB File |
Show |
| Enzyme 12 3D Structure |
|
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1845 bp
ATGAGGCCCCCGCAGTGTCTGCTGCACACGCCTTCCCTGGCTTCCCCACTCCTTCTCCTC
CTCCTCTGGCTCCTGGGTGGAGGAGTGGGGGCTGAGGGCCGGGAGGATGCAGAGCTGCTG
GTGACGGTGCGTGGGGGCCGGCTGCGGGGCATTCGCCTGAAGACCCCCGGGGGCCCTGTC
TCTGCTTTCCTGGGCATCCCCTTTGCGGAGCCACCCATGGGACCCCGTCGCTTTCTGCCA
CCGGAGCCCAAGCAGCCTTGGTCAGGGGTGGTAGACGCTACAACCTTCCAGAGTGTCTGC
TACCAATATGTGGACACCCTATACCCAGGTTTTGAGGGCACCGAGATGTGGAACCCCAAC
CGTGAGCTGAGCGAGGACTGCCTGTACCTCAACGTGTGGACACCATACCCCCGGCCTACA
TCCCCCACCCCTGTCCTCGTCTGGATCTATGGGGGTGGCTTCTACAGTGGGGCCTCCTCC
TTGGACGTGTACGATGGCCGCTTCTTGGTACAGGCCGAGAGGACTGTGCTGGTGTCCATG
AACTACCGGGTGGGAGCCTTTGGCTTCCTGGCCCTGCCGGGGAGCCGAGAGGCCCCGGGC
AATGTGGGTCTCCTGGATCAGAGGCTGGCCCTGCAGTGGGTGCAGGAGAACGTGGCAGCC
TTCGGGGGTGACCCGACATCAGTGACGCTGTTTGGGGAGAGCGCGGGAGCCGCCTCGGTG
GGCATGCACCTGCTGTCCCCGCCCAGCCGGGGCCTGTTCCACAGGGCCGTGCTGCAGAGC
GGTGCCCCCAATGGACCCTGGGCCACGGTGGGCATGGGAGAGGCCCGTCGCAGGGCCACG
CAGCTGGCCCACCTTGTGGGCTGTCCTCCAGGCGGCACTGGTGGGAATGACACAGAGCTG
GTAGCCTGCCTTCGGACACGACCAGCGCAGGTCCTGGTGAACCACGAATGGCACGTGCTG
CCTCAAGAAAGCGTCTTCCGGTTCTCCTTCGTGCCTGTGGTAGATGGAGACTTCCTCAGT
GACACCCCAGAGGCCCTCATCAACGCGGGAGACTTCCACGGCCTGCAGGTGCTGGTGGGT
GTGGTGAAGGATGAGGGCTCGTATTTTCTGGTTTACGGGGCCCCAGGCTTCAGCAAAGAC
AACGAGTCTCTCATCAGCCGGGCCGAGTTCCTGGCCGGGGTGCGGGTCGGGGTTCCCCAG
GTAAGTGACCTGGCAGCCGAGGCTGTGGTCCTGCATTACACAGACTGGCTGCATCCCGAG
GACCCGGCACGCCTGAGGGAGGCCCTGAGCGATGTGGTGGGCGACCACAATGTCGTGTGC
CCCGTGGCCCAGCTGGCTGGGCGACTGGCTGCCCAGGGTGCCCGGGTCTACGCCTACGTC
TTTGAACACCGTGCTTCCACGCTCTCCTGGCCCCTGTGGATGGGGGTGCCCCACGGCTAC
GAGATCGAGTTCATCTTTGGGATCCCCCTGGACCCCTCTCGAAACTACACGGCAGAGGAG
AAAATCTTCGCCCAGCGACTGATGCGATACTGGGCCAACTTTGCCCGCACAGGGGATCCC
AATGAGCCCCGAGACCCCAAGGCCCCACAATGGCCCCCGTACACGGCGGGGGCTCAGCAG
TACGTTAGTCTGGACCTGCGGCCGCTGGAGGTGCGGCGGGGGCTGCGCGCCCAGGCCTGC
GCCTTCTGGAACCGCTTCCTCCCCAAATTGCTCAGCGCCACCGACACGCTCGACGAGGCG
GAGCGCCAGTGGAAGGCCGAGTTCCACCGCTGGAGCTCCTACATGGTGCACTGGAAGAAC
CAGTTCGACCACTACAGCAAGCAGGATCGCTGCTCAGACCTGTGA
|
| Enzyme 12 GenBank Gene ID |
M55040  |
| Enzyme 12 GeneCard ID |
ACHE  |
| Enzyme 12 GenAtlas ID |
ACHE  |
| Enzyme 12 HGNC ID |
HGNC:108  |
| Enzyme 12 Chromosome Location |
7 |
| Enzyme 12 Locus |
7q22 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Soreq H, Ben-Aziz R, Prody CA, Seidman S, Gnatt A, Neville L, Lieman-Hurwitz J, Lev-Lehman E, Ginzberg D, Lipidot-Lifson Y, et al.: Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure. Proc Natl Acad Sci U S A. 1990 Dec;87(24):9688-92. [PubMed
]
- 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
]
- Wilson MD, Riemer C, Martindale DW, Schnupf P, Boright AP, Cheung TL, Hardy DM, Schwartz S, Scherer SW, Tsui LC, Miller W, Koop BF: Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5. Nucleic Acids Res. 2001 Mar 15;29(6):1352-65. [PubMed
]
- Karpel R, Ben Aziz-Aloya R, Sternfeld M, Ehrlich G, Ginzberg D, Tarroni P, Clementi F, Zakut H, Soreq H: Expression of three alternative acetylcholinesterase messenger RNAs in human tumor cell lines of different tissue origins. Exp Cell Res. 1994 Feb;210(2):268-77. [PubMed
]
- Chhajlani V, Derr D, Earles B, Schmell E, August T: Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase. FEBS Lett. 1989 Apr 24;247(2):279-82. [PubMed
]
- Velan B, Grosfeld H, Kronman C, Leitner M, Gozes Y, Lazar A, Flashner Y, Marcus D, Cohen S, Shafferman A: The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580----Ala mutant. J Biol Chem. 1991 Dec 15;266(35):23977-84. [PubMed
]
- Shafferman A, Kronman C, Flashner Y, Leitner M, Grosfeld H, Ordentlich A, Gozes Y, Cohen S, Ariel N, Barak D, et al.: Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding. J Biol Chem. 1992 Sep 5;267(25):17640-8. [PubMed
]
- Felder CE, Botti SA, Lifson S, Silman I, Sussman JL: External and internal electrostatic potentials of cholinesterase models. J Mol Graph Model. 1997 Oct;15(5):318-27, 335-7. [PubMed
]
- Kryger G, Harel M, Giles K, Toker L, Velan B, Lazar A, Kronman C, Barak D, Ariel N, Shafferman A, Silman I, Sussman JL: Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II. Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1385-94. [PubMed
]
- Bartels CF, Zelinski T, Lockridge O: Mutation at codon 322 in the human acetylcholinesterase (ACHE) gene accounts for YT blood group polymorphism. Am J Hum Genet. 1993 May;52(5):928-36. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5777 |
| Enzyme 13 Name |
Platelet-activating factor acetylhydrolase IB subunit gamma |
| Enzyme 13 Synonyms |
- PAF acetylhydrolase 29 kDa subunit
- PAF-AH 29 kDa subunit
- PAF-AH subunit gamma
- PAFAH subunit gamma
|
| Enzyme 13 Gene Name |
PAFAH1B3 |
| Enzyme 13 Protein Sequence |
>Platelet-activating factor acetylhydrolase IB subunit gamma
MSGEENPASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQCEIWRE
LFSPLHALNFGIGGDGTQHVLWRLENGELEHIRPKIVVVWVGTNNHGHTAEQVTGGIKAI
VQLVNERQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAALAGHPRAHFLDADPGFVH
SDGTISHHDMYDYLHLSRLGYTPVCRALHSLLLRLLAQDQGQGAPLLEPAP
|
| Enzyme 13 Number of Residues |
231 |
| Enzyme 13 Molecular Weight |
25735 |
| Enzyme 13 Theoretical pI |
6.84 |
| Enzyme 13 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 13 General Function |
Not Available |
| Enzyme 13 Specific Function |
Inactivates paf by removing the acetyl group at the sn-2 position. This is a catalytic subunit. Plays an important role during the development of brain |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
1122219  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q15102  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
PA1B3_HUMAN  |
| Enzyme 13 PDB ID |
1FXW  |
| Enzyme 13 PDB File |
Show |
| Enzyme 13 3D Structure |
|
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>696 bp
ATGAGTGGAGAGGAGAACCCAGCCAGCAAGCCCACGCCGGTGCAGGACGTACAGGGCGAC
GGGCGCTGGATGTCCCTGCACCATCGGTTCGTGGCTGACAGCAAAGATAAGGAACCCGAA
GTCGTCTTCATCGGGGACTCCTTGGTCCAGCTCATGCACCAGTGCGAGATCTGGCGCGAG
CTCTTCTCTCCTCTGCATGCACTTAACTTTGGCATTGGTGGTGACGGCACACAGCATGTA
CTGTGGCGGCTGGAGAATGGGGAGCTGGAACACATCCGGCCCAAGATTGTGGTGGTCTGG
GTGGGCACCAACAACCACGGACACACAGCAGAGCAGGTGACTGGTGGCATCAAGGCCATT
GTGCAACTGGTGAATGAGCGACAGCCCCAGGCCCGGGTTGTGGTGCTGGGCCTGCTTCCG
CGAGGCCAACATCCCAACCCACTTCGGGAGAAGAACCGACAGGTGAACGAGCTGGTACGG
GCGGCACTGGCTGGCCACCCTCGGGCCCACTTCCTAGATGCCGACCCTGGCTTTGTGCAC
TCAGATGGCACCATCAGCCATCATGACATGTATGATTACCTGCATCTGAGCCGCCTGGGC
TACACACCTGTTTGCCGGGCTCTGCACTCCCTGCTTCTGCGTCTGCTGGCCCAAGACCAG
GGCCAAGGTGCTCCCCTGCTGGAGCCCGCACCCTAA
|
| Enzyme 13 GenBank Gene ID |
D63391  |
| Enzyme 13 GeneCard ID |
PAFAH1B3  |
| Enzyme 13 GenAtlas ID |
PAFAH1B3  |
| Enzyme 13 HGNC ID |
HGNC:8576  |
| Enzyme 13 Chromosome Location |
19 |
| Enzyme 13 Locus |
19q13.1 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Adachi H, Tsujimoto M, Hattori M, Arai H, Inoue K: cDNA cloning of human cytosolic platelet-activating factor acetylhydrolase gamma-subunit and its mRNA expression in human tissues. Biochem Biophys Res Commun. 1995 Sep 5;214(1):180-7. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
5780 |
| Enzyme 14 Name |
Platelet-activating factor acetylhydrolase IB subunit beta |
| Enzyme 14 Synonyms |
- PAF acetylhydrolase 30 kDa subunit
- PAF-AH 30 kDa subunit
- PAF-AH subunit beta
- PAFAH subunit beta
|
| Enzyme 14 Gene Name |
PAFAH1B2 |
| Enzyme 14 Protein Sequence |
>Platelet-activating factor acetylhydrolase IB subunit beta
MSQGDSNPAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQYEIWR
ELFSPLHALNFGIGGDTTRHVLWRLKNGELENIKPKVIVVWVGTNNHENTAEEVAGGIEA
IVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDTDGGFV
HSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEETPEEKQTTIA
|
| Enzyme 14 Number of Residues |
229 |
| Enzyme 14 Molecular Weight |
25570 |
| Enzyme 14 Theoretical pI |
5.80 |
| Enzyme 14 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 14 General Function |
Amino acid transport and metabolism |
| Enzyme 14 Specific Function |
Inactivates PAF by removing the acetyl group at the sn-2 position. This is a catalytic subunit |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
2081614  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P68402  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
PA1B2_HUMAN  |
| Enzyme 14 PDB ID |
1FXW  |
| Enzyme 14 PDB File |
Show |
| Enzyme 14 3D Structure |
|
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>690 bp
ATGAGCCAAGGAGACTCAAACCCAGCAGCTATTCCGCATGCAGCAGAAGATATTCAAGGA
GATGACCGATGGATGTCTCAGCACAACAGATTTGTTTTGGACTGTAAAGACAAAGAGCCT
GATGTACTGTTCGTGGGAGACTCCATGGTGCAGTTAATGCAGCAATATGAGATATGGCGA
GAGCTTTTTTCCCCACTTCATGCACTGAATTTTGGAATTGGGGGAGATACAACAAGACAT
GTTTTGTGGAGACTAAAGAATGGAGAACTGGAGAATATTAAGCCTAAGGTCATTGTTGTC
TGGGTAGGAACAAATAACCACGAAAATACAGCAGAAGAAGTAGCAGGTGGGATCGAGGCC
ATTGTACAACTTATCAACACAAGGCAGCCACAGGCCAAAATCATTGTATTGGGTTTGTTA
CCTCGAGGTGAGAAACCCAATCCTTTGAGGCAAAAGAACGCCAAGGTGAACCAACTCCTC
AAGGTTTCGCTGCCGAAGCTTGCCAACGTGCAGCTCCTGGATACCGACGGGGGTTTTGTG
CACTCGGACGGTGCCATCTCCTGCCACGACATGTTTGATTTTCTGCATCTGACAGGAGGG
GGCTATGCAAAGATCTGCAAACCCCTGCATGAACTGATCATGCAGTTGTTGGAGGAAACA
CCTGAGGAGAAACAAACCACCATTGCCTGA
|
| Enzyme 14 GenBank Gene ID |
D63390  |
| Enzyme 14 GeneCard ID |
PAFAH1B2  |
| Enzyme 14 GenAtlas ID |
PAFAH1B2  |
| Enzyme 14 HGNC ID |
HGNC:8575  |
| Enzyme 14 Chromosome Location |
11 |
| Enzyme 14 Locus |
11q23 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Adachi H, Tsujimoto M, Hattori M, Arai H, Inoue K: Differential tissue distribution of the beta- and gamma-subunits of human cytosolic platelet-activating factor acetylhydrolase (isoform I). Biochem Biophys Res Commun. 1997 Apr 7;233(1):10-3. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
5785 |
| Enzyme 15 Name |
Platelet-activating factor acetylhydrolase 2, cytoplasmic |
| Enzyme 15 Synonyms |
- Serine-dependent phospholipase A2
- HSD-PLA2
|
| Enzyme 15 Gene Name |
PAFAH2 |
| Enzyme 15 Protein Sequence |
>Platelet-activating factor acetylhydrolase 2, cytoplasmic
MGVNQSVGFPPVTGPHLVGCGDVMEGQNLQGSFFRLFYPCQKAEETMEQPLWIPRYEYCT
GLAEYLQFNKRCGGLLFNLAVGSCRLPVSWNGPFKTKDSGYPLIIFSHGLGAFRTLYSAF
CMELASRGFVVAVPEHRDRSAATTYFCKQAPEENQPTNESLQEEWIPFRRVEEGEKEFHV
RNPQVHQRVSECLRVLKILQEVTAGQTVFNILPGGLDLMTLKGNIDMSRVAVMGHSFGGA
TAILALAKETQFRCAVALDAWMFPLERDFYPKARGPVFFINTEKFQTMESVNLMKKICAQ
HEQSRIITVLGSVHRSQTDFAFVTGNLIGKFFSTETRGSLDPYEGQEVMVRAMLAFLQKH
LDLKEDYNQWNNLIEGIGPSLTPGAPHHLSSL
|
| Enzyme 15 Number of Residues |
392 |
| Enzyme 15 Molecular Weight |
44036 |
| Enzyme 15 Theoretical pI |
6.89 |
| Enzyme 15 GO Classification |
| Function |
- 1-alkyl-2-acetylglycerophosphocholine esterase activity
- carboxylic ester hydrolase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
- lipid catabolism
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
- 2-acetyl-1-alkylglycerophosphocholine esterase complex
- protein complex
- unlocalized protein complex
|
|
| Enzyme 15 General Function |
Not Available |
| Enzyme 15 Specific Function |
Has a marked selectivity for phospholipids with short acyl chains at the sn-2 position. May share a common physiologic function with the plasma-type enzyme |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
1765864  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q99487  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
PAFA2_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1179 bp
ATGGGGGTCAACCAGTCTGTGGGCTTTCCACCTGTCACAGGACCCCACCTCGTAGGCTGT
GGGGATGTGATGGAGGGTCAGAATCTCCAGGGGAGCTTCTTTCGACTCTTCTACCCCTGC
CAAAAGGCAGAGGAGACCATGGAGCAGCCCCTGTGGATTCCCCGCTATGAGTACTGCACT
GGCCTGGCCGAGTACCTGCAGTTTAATAAGCGCTGCGGGGGCTTGCTGTTCAACCTGGCG
GTGGGATCTTGTCGCCTGCCTGTTAGCTGGAATGGCCCCTTTAAGACAAAGGACTCTGGA
TACCCCTTGATCATCTTCTCCCATGGCCTAGGAGCCTTCAGGACTTTGTATTCAGCCTTC
TGCATGGAGCTGGCCTCACGTGGCTTTGTGGTTGCTGTGCCAGAGCACAGGGACCGGTCA
GCGGCAACCACCTATTTCTGCAAGCAGGCCCCAGAAGAGAACCAGCCCACCAATGAATCG
CTGCAGGAGGAATGGATCCCTTTCCGTCGAGTTGAGGAAGGGGAGAAGGAATTTCATGTT
CGGAATCCCCAGGTGCATCAGCGGGTAAGCGAGTGTTTACGGGTGTTGAAGATCCTGCAA
GAGGTCACTGCTGGGCAGACTGTCTTCAACATCTTGCCTGGTGGCTTGGATCTGATGACT
TTGAAGGGCAACATTGACATGAGCCGTGTGGCTGTGATGGGACATTCATTTGGAGGGGCC
ACAGCTATTCTGGCTTTGGCCAAGGAGACCCAATTTCGGTGTGCGGTGGCTCTGGATGCT
TGGATGTTTCCTCTGGAACGTGACTTTTACCCCAAGGCCCGAGGACCTGTGTTCTTTATC
AATACTGAGAAATTCCAGACAATGGAGAGTGTCAATTTGATGAAGAAGATATGTGCCCAG
CATGAACAGTCTAGGATCATAACCGTTCTTGGTTCTGTTCATCGGAGTCAAACTGACTTT
GCTTTTGTGACTGGCAACTTGATTGGTAAATTCTTCTCCACTGAAACCCGTGGGAGCCTG
GACCCCTATGAAGGGCAGGAGGTTATGGTACGGGCCATGTTGGCCTTCCTGCAGAAGCAC
CTCGACCTGAAAGAAGACTATAATCAATGGAACAACCTTATTGAAGGCATTGGACCGTCG
CTCACCCCAGGGGCCCCCCACCATCTGTCCAGCCTGTAG
|
| Enzyme 15 GenBank Gene ID |
D87845  |
| Enzyme 15 GeneCard ID |
PAFAH2  |
| Enzyme 15 GenAtlas ID |
PAFAH2  |
| Enzyme 15 HGNC ID |
HGNC:8579  |
| Enzyme 15 Chromosome Location |
1 |
| Enzyme 15 Locus |
1p34.3 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Hattori K, Adachi H, Matsuzawa A, Yamamoto K, Tsujimoto M, Aoki J, Hattori M, Arai H, Inoue K: cDNA cloning and expression of intracellular platelet-activating factor (PAF) acetylhydrolase II. Its homology with plasma PAF acetylhydrolase. J Biol Chem. 1996 Dec 20;271(51):33032-8. [PubMed
]
- Rice SQ, Southan C, Boyd HF, Terrett JA, MacPhee CH, Moores K, Gloger IS, Tew DG: Expression, purification and characterization of a human serine-dependent phospholipase A2 with high specificity for oxidized phospholipids and platelet activating factor. Biochem J. 1998 Mar 15;330 ( Pt 3):1309-15. [PubMed
]
- Stafforini DM, McIntyre TM, Zimmerman GA, Prescott SM: Platelet-activating factor acetylhydrolases. J Biol Chem. 1997 Jul 18;272(29):17895-8. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
5810 |
| Enzyme 16 Name |
Aldehyde dehydrogenase 3B2 |
| Enzyme 16 Synonyms |
- Aldehyde dehydrogenase 8
|
| Enzyme 16 Gene Name |
ALDH3B2 |
| Enzyme 16 Protein Sequence |
>Aldehyde dehydrogenase 3B2
MKDEPRSTNLFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGNCVVLKPSE
ISQGTEKVLAEVLPQYLDQSCFAVVLGGPQETGQLLEHKLDYIFFTGSPRVGKIVMTAAT
KHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQERLL
PALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGRVAIGGQSNESDRYIAPTVL
VDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERT
SSGSFGGNEGFTYISLLSVPFGGVGHSGMGRYHGKFTFDTFSHHRTCLLAPSGLEKLKEI
RYPPYTDWNQQLLRWGMGSQSCTLL
|
| Enzyme 16 Number of Residues |
385 |
| Enzyme 16 Molecular Weight |
42670 |
| Enzyme 16 Theoretical pI |
5.97 |
| Enzyme 16 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 16 General Function |
Energy production and conversion |
| Enzyme 16 Specific Function |
An aldehyde + NAD(P)(+) + H(2)O = an acid + NAD(P)H |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
1051281  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P48448  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
AL3B2_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1158 bp
ATGAAGGATGAACCACGGTCCACGAACCTGTTCATGAAGCTGGACTCGGTCTTCATCTGG
AAGGAACCCTTTGGCCTGGTCCTCATCATCGCACCCTGGAACTACCCATTGAACCTGACC
CTGGTGCTCCTGGTGGGCACCCTCCCCGCAGGGAATTGCGTGGTGCTGAAGCCGTCAGAA
ATCAGCCAGGGCACAGAGAAGGTCCTGGCTGAGGTGCTGCCCCAGTACCTGGACCAGAGC
TGCTTTGCCGTGGTGCTGGGCGGACCCCAGGAGACAGGGCAGCTGCTAGAGCACAAGTTG
GACTACATCTTCTTCACAGGGAGCCCTCGTGTGGGCAAGATTGTCATGACTGCTGCCACC
AAGCACCTGACGCCTGTCACCCTGGAGCTGGGGGGCAAGAACCCCTGCTACGTGGACGAC
AACTGCGACCCCCAGACCGTGGCCAACCGCGTGGCCTGGTTCTGCTACTTCAATGCCGGC
CAGACCTGCGTGGCCCCTGACTACGTCCTGTGCAGCCCCGAGATGCAGGAGAGGCTGCTG
CCCGCCCTGCAGAGCACCATCACCCGTTTCTATGGCGACGACCCCCAGAGCTCCCCAAAC
CTGGGCCGCATCATCAACCAGAAACAGTTCCAGCGGCTGCGGGCATTGCTGGGCTGCGGC
CGCGTGGCCATTGGGGGCCAGAGCAACGAGAGCGATCGCTACATCGCCCCCACGGTGCTG
GTGGACGTGCAGGAGACGGAGCCTGTGATGCAGGAGGAGATCTTCGGGCCCATCCTGCCC
ATCGTGAACGTGCAGAGCGTGGACGAGGCCATCAAGTTCATCAACCGGCAGGAGAAGCCC
CTGGCCCTGTACGCCTTCTCCAACAGCAGACAGGTTGTGAACCAGATGCTGGAGCGGACC
AGCAGCGGCAGCTTTGGAGGCAATGAGGGCTTCACCTACATATCTCTGCTGTCCGTGCCA
TTCGGGGGAGTCGGCCACAGTGGGATGGGCCGGTACCACGGCAAGTTCACCTTCGACACC
TTCTCCCACCACCGCACCTGCCTGCTCGCCCCCTCCGGCCTGGAGAAATTAAAGGAGATC
CGCTACCCACCCTATACCGACTGGAACCAGCAGCTGTTACGCTGGGGCATGGGCTCCCAG
AGCTGCACCCTCCTGTGA
|
| Enzyme 16 GenBank Gene ID |
U37519  |
| Enzyme 16 GeneCard ID |
ALDH3B2  |
| Enzyme 16 GenAtlas ID |
ALDH3B2  |
| Enzyme 16 HGNC ID |
HGNC:411  |
| Enzyme 16 Chromosome Location |
11 |
| Enzyme 16 Locus |
11q13 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Hsu LC, Chang WC, Lin SW, Yoshida A: Cloning and characterization of genes encoding four additional human aldehyde dehydrogenase isozymes. Adv Exp Med Biol. 1995;372:159-68. [PubMed
]
- Hsu LC, Chang WC: Sequencing and expression of the human ALDH8 encoding a new member of the aldehyde dehydrogenase family. Gene. 1996 Oct 3;174(2):319-22. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
5811 |
| Enzyme 17 Name |
Aldehyde dehydrogenase 3B1 |
| Enzyme 17 Synonyms |
- Aldehyde dehydrogenase 7
|
| Enzyme 17 Gene Name |
ALDH3B1 |
| Enzyme 17 Protein Sequence |
>Aldehyde dehydrogenase 3B1
MDPLGDTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESE
VSEVAISQGEVTLALRNLRAWMKDERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNL
TLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLGGPQETGQLLEHR
FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA
GQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGC
GRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREK
PLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFD
TFSHHRACLLRSPGMEKLNALRYPPQSPRRLRMLLVAMEAQGCSCTLL
|
| Enzyme 17 Number of Residues |
468 |
| Enzyme 17 Molecular Weight |
51840 |
| Enzyme 17 Theoretical pI |
7.67 |
| Enzyme 17 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 17 General Function |
Energy production and conversion |
| Enzyme 17 Specific Function |
An aldehyde + NAD(P)(+) + H(2)O = an acid + NAD(P)H |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
601780  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
P43353  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
AL3B1_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>1407 bp
ATGGACCCCCTTGGGGACACGCTGCGGCGACTGCGGGAGGCCTTCCACGCGGGGCGCACG
CGGCCAGCTGAGTTCCGGGCTGCGCAGCTCCAAGGCCTGGGCCGCTTCCTGCAAGAAAAC
AAGCAGCTTCTGCACGACGCACTGGCCCAGGACCTGCACAAGTCAGCCTTCGAGTCGGAG
GTGTCTGAGGTTGCCATCAGCCAGGGCGAGGTCACCCTGGCCCTCAGGAACCTCCGGGCC
TGGATGAAGGACGAGCGTGTGCCCAAGAACCTGGCCACGCAGCTGGACTCCGCCTTCATC
CGGAAGGAGCCCTTTGGCCTGGTCCTCATCATTGCGCCCTGGAACTATCCGCTGAACCTG
ACGCTGGTGCCCCTCGTGGGAGCCCTCGCTGCAGGGAACTGTGTGGTGCTGAAGCCATCG
GAGATTAGCAAGAACGTCGAGAAGATCCTGGCCGAGGTGCTGCCCCAATACGTGGACCAG
AGCTGCTTTGCTGTGGTGCTGGGCGGGCCCCAGGAGACGGGGCAGCTGCTAGAGCACAGG
TTCGACTACATCTTCTTCACAGGGAGCCCTCGTGTGGGCAAGATTGTTATGACTGCTGCC
GCCAAGCACCTGACACCTGTCACCCTGGAGCTGGGGGGCAAGAACCCTTGCTACGTGGAC
GACAACTGCGACCCCCAGACCGTGGCCAACCGCGTGGCCTGGTTCCGCTACTTCAACGCC
GGCCAGACCTGCGTGGCCCCCGACTACGTCCTATGCAGCCCTGAGATGCAGGAGAGGCTG
CTGCCTGCCCTGCAGAGCACCATCACCCGTTTCTATGGCGACGACCCCCAGAGCTCCCCA
AACCTGGGCCGCATCATCAACCAGAAACAGTTCCAGCGGCTGCGGGCATTGCTGGGCTGC
GGCCGTGTGGCCATTGGGGGCCAGAGCGATGAGAGCGATCGCTACATCGCCCCCACGGTG
CTGGTGGATGTGCAGGAGATGGAGCCTGTGATGCAGGAGGAGATCTTCGGGCCCATCCTG
CCCATCGTGAACGTGCAGAGCTTGGACGAGGCCATCGAGTTCATCAACCGGCGGGAGAAG
CCCCTGGCCCTGTACGCCTTCTCCAACAGCAGCCAGGTGGTCAAGCGGGTGCTGACCCAG
ACCAGCAGCGGGGGCTTCTGTGGGAACGACGGCTTCATGCACATGACCCTGGCCAGCCTG
CCTTTTGGAGGAGTGGGTGCCAGTGGGATGGGCCGGTACCATGGCAAGTTCTCCTTCGAC
ACCTTCTCCCACCATCGCGCCTGCCTCCTGCGCAGCCCGGGGATGGAGAAGCTCAACGCC
CTCCGCTACCCGCCGCAATCGCCGCGCCGCCTGAGGATGCTGCTGGTGGCCATGGAGGCC
CAAGGCTGCAGCTGCACACTGCTCTGA
|
| Enzyme 17 GenBank Gene ID |
U10868  |
| Enzyme 17 GeneCard ID |
ALDH3B1  |
| Enzyme 17 GenAtlas ID |
ALDH3B1  |
| Enzyme 17 HGNC ID |
HGNC:410  |
| Enzyme 17 Chromosome Location |
11 |
| Enzyme 17 Locus |
11q13 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Hsu LC, Chang WC, Yoshida A: Cloning of a cDNA encoding human ALDH7, a new member of the aldehyde dehydrogenase family. Gene. 1994 Dec 30;151(1-2):285-9. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
5824 |
| Enzyme 18 Name |
Acylphosphatase-2 |
| Enzyme 18 Synonyms |
- Acylphosphate phosphohydrolase 2
- Acylphosphatase, muscle type isozyme
|
| Enzyme 18 Gene Name |
ACYP2 |
| Enzyme 18 Protein Sequence |
>Acylphosphatase-2
MSTAQSLKSVDYEVFGRVQGVCFRMYTEDEARKIGVVGWVKNTSKGTVTGQVQGPEDKVN
SMKSWLSKVGSPSSRIDRTNFSNEKTISKLEYSNFSIRY
|
| Enzyme 18 Number of Residues |
99 |
| Enzyme 18 Molecular Weight |
11140 |
| Enzyme 18 Theoretical pI |
10.01 |
| Enzyme 18 GO Classification |
| Function |
- acylphosphatase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 18 General Function |
Energy production and conversion |
| Enzyme 18 Specific Function |
Its physiological role is not yet clear |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- An acylphosphate + H2O = a carboxylate + phosphate
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
15341747  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
P14621  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
ACYP2_HUMAN  |
| Enzyme 18 PDB ID |
1APS  |
| Enzyme 18 PDB File |
Show |
| Enzyme 18 3D Structure |
|
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>300 bp
ATGTCTACCGCCCAGTCACTCAAATCCGTGGACTACGAGGTGTTCGGAAGAGTGCAGGGT
GTTTGCTTCAGAATGTATACAGAAGATGAAGCTAGGAAAATAGGAGTGGTTGGCTGGGTG
AAGAATACCAGCAAAGGCACCGTGACAGGCCAAGTGCAGGGGCCAGAAGACAAAGTCAAT
TCCATGAAGTCCTGGCTGAGCAAGGTTGGAAGCCCTAGTTCTCGCATTGACCGCACAAAC
TTTTCTAATGAAAAAACCATCTCTAAGCTTGAATACTCTAATTTTAGTATTAGATACTAA
|
| Enzyme 18 GenBank Gene ID |
BC012290  |
| Enzyme 18 GeneCard ID |
ACYP2  |
| Enzyme 18 GenAtlas ID |
ACYP2  |
| Enzyme 18 HGNC ID |
HGNC:180  |
| Enzyme 18 Chromosome Location |
2 |
| Enzyme 18 Locus |
2p16.2 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Manao G, Camici G, Modesti A, Liguri G, Berti A, Stefani M, Cappugi G, Ramponi G: Human skeletal muscle acylphosphatase: the primary structure. Mol Biol Med. 1984 Dec;2(6):369-78. [PubMed
]
- Chiarugi P, Raugei G, Marzocchini R, Fiaschi T, Ciccarelli C, Berti A, Ramponi G: Differential modulation of expression of the two acylphosphatase isoenzymes by thyroid hormone. Biochem J. 1995 Oct 15;311 ( Pt 2):567-73. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
5825 |
| Enzyme 19 Name |
Acylphosphatase-1 |
| Enzyme 19 Synonyms |
- Acylphosphate phosphohydrolase 1
- Acylphosphatase, organ-common type isozyme
- Acylphosphatase, erythrocyte isozyme
|
| Enzyme 19 Gene Name |
ACYP1 |
| Enzyme 19 Protein Sequence |
>Acylphosphatase-1
MAEGNTLISVDYEIFGKVQGVFFRKHTQAEGKKLGLVGWVQNTDRGTVQGQLQGPISKVR
HMQEWLETRGSPKSHIDKANFNNEKVILKLDYSDFQIVK
|
| Enzyme 19 Number of Residues |
99 |
| Enzyme 19 Molecular Weight |
11261 |
| Enzyme 19 Theoretical pI |
9.94 |
| Enzyme 19 GO Classification |
| Function |
- acylphosphatase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 19 General Function |
Energy production and conversion |
| Enzyme 19 Specific Function |
Its physiological role is not yet clear |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- An acylphosphate + H2O = a carboxylate + phosphate
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
1834464  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
P07311  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
ACYP1_HUMAN  |
| Enzyme 19 PDB ID |
2ACY  |
| Enzyme 19 PDB File |
Show |
| Enzyme 19 3D Structure |
|
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>300 bp
ATGGCAGAGGGAAACACCCTGATATCAGTGGATTATGAAATTTTTGGGAAGGTGCAAGGG
GTGTTTTTCCGTAAGCATACTCAGGCTGAGGGTAAAAAGCTGGGATTGGTAGGCTGGGTC
CAGAACACTGACCGGGGCACAGTGCAAGGACAATTGCAAGGTCCAATCTCCAAGGTGCGT
CATATGCAGGAATGGCTTGAAACAAGAGGAAGTCCTAAATCACACATCGACAAAGCAAAC
TTCAACAATGAAAAAGTCATCTTGAAGTTGGATTACTCAGACTTCCAAATTGTAAAATAA
|
| Enzyme 19 GenBank Gene ID |
X84194  |
| Enzyme 19 GeneCard ID |
ACYP1  |
| Enzyme 19 GenAtlas ID |
ACYP1  |
| Enzyme 19 HGNC ID |
HGNC:179  |
| Enzyme 19 Chromosome Location |
14 |
| Enzyme 19 Locus |
14q24.3 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed
]
- Liguri G, Camici G, Manao G, Cappugi G, Nassi P, Modesti A, Ramponi G: A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure. Biochemistry. 1986 Dec 2;25(24):8089-94. [PubMed
]
- Fiaschi T, Raugei G, Marzocchini R, Chiarugi P, Cirri P, Ramponi G: Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphatase. FEBS Lett. 1995 Jun 26;367(2):145-8. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
5826 |
| Enzyme 20 Name |
Aminoacylase-1 |
| Enzyme 20 Synonyms |
- N-acyl-L-amino-acid amidohydrolase
- ACY-1
|
| Enzyme 20 Gene Name |
ACY1 |
| Enzyme 20 Protein Sequence |
>Aminoacylase-1
MTSKGPEEEHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVV
TVLTWPGTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQ
YLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHALRAGFALDEGIANP
TDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAFREKEWQRLQSN
PHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEG
VTLEFAQKWMHPQVTPTDDSNPWWAAFSRVCKDMNLTLEPEIMPAATDNRYIRAVGVPAL
GFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALASVPALPSDS
|
| Enzyme 20 Number of Residues |
408 |
| Enzyme 20 Molecular Weight |
45885 |
| Enzyme 20 Theoretical pI |
6.12 |
| Enzyme 20 GO Classification |
| Function |
- aminoacylase activity
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
- metallopeptidase activity
- peptidase activity
- protein binding
- protein dimerization activity
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- cellular protein metabolism
- macromolecule metabolism
- metabolism
- physiological process
- protein metabolism
- proteolysis
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 20 General Function |
Amino acid transport and metabolism |
| Enzyme 20 Specific Function |
Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) |
| Enzyme 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
- An N-acyl-L-amino acid + H2O = a carboxylate + an L-amino acid
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
178071  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q03154  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
ACY1_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>1227 bp
ATGACCAGCAAGGGTCCCGAGGAGGAGCACCCATCGGTGACGCTCTTCCGCCAGTACCTG
CGTATCCGCACTGTCCAGCCCAAGCCTGACTATGGAGCTGCTGTGGCTTTCTTTGAGGAG
ACAGCCCGCCAGCTGGGCCTGGGCTGTCAGAAAGTAGAGGTGGCACCTGGCTATGTGGTG
ACCGTGTTGACCTGGCCAGGCACCAACCCTACACTCTCCTCCATCTTGCTCAACTCCCAC
ACGGATGTGGTGCCTGTCTTCAAGGAACATTGGAGTCACGACCCCTTTGAGGCCTTCAAG
GATTCTGAGGGCTACATCTATGCCAGGGGTGCCCAGGACATGAAGTGCGTCAGCATCCAG
TACCTGGAAGCTGTGAGGAGGCTGAAGGTGGAGGGCCACCGGTTCCCCAGAACCATCCAC
ATGACCTTTGTGCCTGATGAGGAGGTTGGGGGTCACCAAGGCATGGAGCTGTTCGTGCAG
CGGCCTGAGTTCCACGCCCTGAGGGCAGGCTTTGCCCTGGATGAGGGCATAGCCAATCCC
ACTGATGCCTTCACTGTCTTTTATAGTGAGCGGAGTCCCTGGTGGGTGCGGGTTACCAGC
ACTGGGAGGCCAGGCCATGCCTCACGCTTCATGGAGGACACAGCAGCAGAGAAGCTGCAC
AAGGTTGTAAACTCCATCCTGGCATTCCGGGAGAAGGAATGGCAGAGGCTGCAGTCAAAC
CCCCACCTGAAAGAGGGGTCCGTGACCTCCGTGAACCTGACTAAGCTAGAGGGTGGCGTG
GCCTATAACGTGATACCTGCCACCATGAGCGCCAGCTTTGACTTCCGTGTGGCACCGGAT
GTGGACTTCAAGGCTTTTGAGGAGCAGCTGCAGAGCTGGTGCCAGGCAGCTGGCGAGGGG
GTCACCCTAGAGTTTGCTCAGAAGTGGATGCACCCCCAAGTGACACCTACTGATGACTCA
AACCCTTGGTGGGCAGCTTTTAGCCGGGTCTGCAAGGATATGAACCTCACTCTGGAGCCT
GAGATCATGCCTGCTGCCACTGACAACCGCTATATCCGCGCGGTGGGGGTCCCAGCTCTA
GGCTTCTCACCCATGAACCGCACACCTGTGCTGCTGCACGACCACGATGAACGGCTGCAT
GAGGCTGTGTTCCTCCGTGGGGTGGACATATATACACGCCTGCTGCCTGCCCTTGCCAGT
GTGCCTGCCCTGCCCAGTGACAGCTGA
|
| Enzyme 20 GenBank Gene ID |
L07548  |
| Enzyme 20 GeneCard ID |
ACY1  |
| Enzyme 20 GenAtlas ID |
ACY1  |
| Enzyme 20 HGNC ID |
HGNC:177  |
| Enzyme 20 Chromosome Location |
3 |
| Enzyme 20 Locus |
3p21.1 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Mitta M, Kato I, Tsunasawa S: The nucleotide sequence of human aminoacylase-1. Biochim Biophys Acta. 1993 Aug 19;1174(2):201-3. [PubMed
]
- Cook RM, Burke BJ, Buchhagen DL, Minna JD, Miller YE: Human aminoacylase-1. Cloning, sequence, and expression analysis of a chromosome 3p21 gene inactivated in small cell lung cancer. J Biol Chem. 1993 Aug 15;268(23):17010-7. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
5827 |
| Enzyme 21 Name |
Aspartoacylase |
| Enzyme 21 Synonyms |
- Aminoacylase-2
- ACY-2
|
| Enzyme 21 Gene Name |
ASPA |
| Enzyme 21 Protein Sequence |
>Aspartoacylase
MTSCHIAEEHIQKVAIFGGTHGNELTGVFLVKHWLENGAEIQRTGLEVKPFITNPRAVKK
CTRYIDCDLNRIFDLENLGKKMSEDLPYEVRRAQEINHLFGPKDSEDSYDIIFDLHNTTS
NMGCTLILEDSRNNFLIQMFHYIKTSLAPLPCYVYLIEHPSLKYATTRSIAKYPVGIEVG
PQPQGVLRADILDQMRKMIKHALDFIHHFNEGKEFPPCAIEVYKIIEKVDYPRDENGEIA
AIIHPNLQDQDWKPLHPGDPMFLTLDGKTIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTK
LTLNAKSIRCCLH
|
| Enzyme 21 Number of Residues |
313 |
| Enzyme 21 Molecular Weight |
35736 |
| Enzyme 21 Theoretical pI |
6.51 |
| Enzyme 21 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 21 General Function |
Amino acid transport and metabolism |
| Enzyme 21 Specific Function |
Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it act as a scavenger of NAA from body fluids |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- N-acyl-L-aspartate + H2O = a carboxylate + L-aspartate
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
455834  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
P45381  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
ACY2_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>942 bp
ATGACTTCTTGTCACATTGCTGAAGAACATATACAAAAGGTTGCTATCTTTGGAGGAACC
CATGGGAATGAGCTAACCGGAGTATTTCTGGTTAAGCATTGGCTAGAGAATGGCGCTGAG
ATTCAGAGAACAGGGCTGGAGGTAAAACCATTTATTACTAACCCCAGAGCAGTGAAGAAG
TGTACCAGATATATTGACTGTGACCTGAATCGCATTTTTGACCTTGAAAATCTTGGCAAA
AAAATGTCAGAAGATTTGCCATATGAAGTGAGAAGGGCTCAAGAAATAAATCATTTATTT
GGTCCAAAAGACAGTGAAGATTCCTATGACATTATTTTTGACCTTCACAACACCACCTCT
AACATGGGGTGCACTCTTATTCTTGAGGATTCCAGGAATAACTTTTTAATTCAGATGTTT
CATTACATTAAGACTTCTCTGGCTCCACTACCCTGCTACGTTTATCTGATTGAGCATCCT
TCCCTCAAATATGCGACCACTCGTTCCATAGCCAAGTATCCTGTGGGTATAGAAGTTGGT
CCTCAGCCTCAAGGGGTTCTGAGAGCTGATATCTTGGATCAAATGAGAAAAATGATTAAA
CATGCTCTTGATTTTATACATCATTTCAATGAAGGAAAAGAATTTCCTCCCTGCGCCATT
GAGGTCTATAAAATTATAGAGAAAGTTGATTACCCCCGGGATGAAAATGGAGAAATTGCT
GCTATCATCCATCCTAATCTGCAGGATCAAGACTGGAAACCACTGCATCCTGGGGATCCC
ATGTTTTTAACTCTTGATGGGAAGACGATCCCACTGGGCGGAGACTGTACCGTGTACCCC
GTGTTTGTGAATGAGGCCGCATATTACGAAAAGAAAGAAGCTTTTGCAAAGACAACTAAA
CTAACGCTCAATGCAAAAAGTATTCGCTGCTGTTTACATTAG
|
| Enzyme 21 GenBank Gene ID |
S67156  |
| Enzyme 21 GeneCard ID |
ASPA  |
| Enzyme 21 GenAtlas ID |
ASPA  |
| Enzyme 21 HGNC ID |
HGNC:756  |
| Enzyme 21 Chromosome Location |
17 |
| Enzyme 21 Locus |
17pter-p13 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Kaul R, Gao GP, Balamurugan K, Matalon R: Cloning of the human aspartoacylase cDNA and a common missense mutation in Canavan disease. Nat Genet. 1993 Oct;5(2):118-23. [PubMed
]
- Moore RA, Le Coq J, Faehnle CR, Viola RE: Purification and preliminary characterization of brain aspartoacylase. Arch Biochem Biophys. 2003 May 1;413(1):1-8. [PubMed
]
- Kaul R, Gao GP, Aloya M, Balamurugan K, Petrosky A, Michals K, Matalon R: Canavan disease: mutations among Jewish and non-jewish patients. Am J Hum Genet. 1994 Jul;55(1):34-41. [PubMed
]
- Shaag A, Anikster Y, Christensen E, Glustein JZ, Fois A, Michelakakis H, Nigro F, Pronicka E, Ribes A, Zabot MT, et al.: The molecular basis of canavan (aspartoacylase deficiency) disease in European non-Jewish patients. Am J Hum Genet. 1995 Sep;57(3):572-80. [PubMed
]
- Kaul R, Gao GP, Michals K, Whelan DT, Levin S, Matalon R: Novel (cys152 > arg) missense mutation in an Arab patient with Canavan disease. Hum Mutat. 1995;5(3):269-71. [PubMed
]
- Kobayashi K, Tsujino S, Ezoe T, Hamaguchi H, Nihei K, Sakuragawa N: Missense mutation (I143T) in a Japanese patient with Canavan disease. Hum Mutat. 1998;Suppl 1:S308-9. [PubMed
]
- Rady PL, Vargas T, Tyring SK, Matalon R, Langenbeck U: Novel missense mutation (Y231C) in a turkish patient with canavan disease. Am J Med Genet. 1999 Nov 26;87(3):273-5. [PubMed
]
- Sistermans EA, de Coo RF, van Beerendonk HM, Poll-The BT, Kleijer WJ, van Oost BA: Mutation detection in the aspartoacylase gene in 17 patients with Canavan disease: four new mutations in the non-Jewish population. Eur J Hum Genet. 2000 Jul;8(7):557-60. [PubMed
]
- Zeng BJ, Wang ZH, Ribeiro LA, Leone P, De Gasperi R, Kim SJ, Raghavan S, Ong E, Pastores GM, Kolodny EH: Identification and characterization of novel mutations of the aspartoacylase gene in non-Jewish patients with Canavan disease. J Inherit Metab Dis. 2002 Nov;25(7):557-70. [PubMed
]
- Olsen TR, Tranebjaerg L, Kvittingen EA, Hagenfeldt L, Moller C, Nilssen O: Two novel aspartoacylase gene (ASPA) missense mutations specific to Norwegian and Swedish patients with Canavan disease. J Med Genet. 2002 Sep;39(9):e55. [PubMed
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
5828 |
| Enzyme 22 Name |
Platelet-activating factor acetylhydrolase IB subunit alpha |
| Enzyme 22 Synonyms |
- PAF acetylhydrolase 45 kDa subunit
- PAF-AH 45 kDa subunit
- PAF-AH alpha
- PAFAH alpha
- Lissencephaly-1 protein
- LIS-1
|
| Enzyme 22 Gene Name |
PAFAH1B1 |
| Enzyme 22 Protein Sequence |
>Platelet-activating factor acetylhydrolase IB subunit alpha
MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDVNEELDKKYAGLLEKKWTSVIR
LQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVF
SVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQ
GFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMV
RPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSE
TKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDK
TLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR
|
| Enzyme 22 Number of Residues |
410 |
| Enzyme 22 Molecular Weight |
46638 |
| Enzyme 22 Theoretical pI |
7.40 |
| Enzyme 22 GO Classification |
Not Available |
| Enzyme 22 General Function |
Not Available |
| Enzyme 22 Specific Function |
Required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet- activating factor (PAF) by removing the acetyl group at the SN-2 position. Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing |
| 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 |
349824  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
P43034  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
LIS1_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>1233 bp
ATGGTGCTGTCCCAGAGACAACGAGATGAACTAAATCGAGCTATAGCAGATTATCTTCGT
TCAAATGGCTATGAAGAGGCATATTCAGTTTTTAAAAAGGAAGCTGAATTAGATGTGAAT
GAAGAATTAGATAAAAAGTATGCTGGTCTTTTGGAAAAAAAATGGACATCTGTTATTAGA
TTACAAAAGAAGGTTATGGAATTAGAATCAAAGCTAAATGAAGCAAAAGAAGAATTTACG
TCAGGTGGACCTCTTGGTCAGAAACGAGACCCAAAAGAATGGATTCCCCGTCCGCCAGAA
AAATATGCATTGAGTGGTCACAGGAGTCCAGTCACTCGAGTCATTTTCCATCCTGTGTTC
AGTGTTATGGTCTCTGCTTCAGAGGATGCTACAATTAAGGTGTGGGATTATGAGACTGGA
GATTTTGAACGAACTCTTAAAGGACATACAGACTCTGTACAGGACATTTCATTCGACCAC
AGCGGCAAGCTTCTGGCTTCCTGTTCTGCAGATATGACCATTAAACTATGGGATTTTCAG
GGCTTTGAATGCATCAGAACCATGCACGGCCATGACCACAATGTTTCTTCAGTAGCCATC
ATGCCCAATGGAGATCATATAGTGTCTGCCTCAAGGGATAAAACTATAAAAATGTGGGAA
GTGCAAACTGGCTACTGTGTGAAGACATTCACAGGACACAGAGAATGGGTACGTATGGTA
CGGCCAAATCAAGATGGCACTCTGATAGCCAGCTGTTCCAATGACCAGACTGTGCGTGTA
TGGGTCGTAGCAACAAAGGAATGCAAGGCTGAGCTCCGAGAGCATGAGCATGTGGTAGAA
TGCATTTCCTGGGCTCCAGAAAGCTCATATTCCTCCATCTCTGAAGCAACAGGATCTGAG
ACTAAAAAAAGTGGTAAACCTGGGCCATTCTTGCTGTCTGGATCCAGAGACAAGACTATT
AAGATGTGGGATGTCAGTACTGGCATGTGCCTTATGACCCTCGTGGGTCATGATAACTGG
GTACGTGGAGTTCTGTTCCATTCTGGGGGGAAGTTTATTTTGAGTTGTGCTGATGACAAG
ACCCTACGCGTATGGGATTACAAGAACAAGCGATGCATGAAGACCCTCAATGCGCATGAA
CACTTTGTTACCTCCTTGGATTTCCACAAGACGGCACCCTATGTCGTCACTGGCAGCGTA
GATCAAACAGTAAAAGTGTGGGAGTGCCGTTGA
|
| Enzyme 22 GenBank Gene ID |
L13385  |
| Enzyme 22 GeneCard ID |
PAFAH1B1  |
| Enzyme 22 GenAtlas ID |
PAFAH1B1  |
| Enzyme 22 HGNC ID |
HGNC:8574  |
| Enzyme 22 Chromosome Location |
17 |
| Enzyme 22 Locus |
17p13.3 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Reiner O, Carrozzo R, Shen Y, Wehnert M, Faustinella F, Dobyns WB, Caskey CT, Ledbetter DH: Isolation of a Miller-Dieker lissencephaly gene containing G protein beta-subunit-like repeats. Nature. 1993 Aug 19;364(6439):717-21. [PubMed
]
- Lo Nigro C, Chong CS, Smith AC, Dobyns WB, Carrozzo R, Ledbetter DH: Point mutations and an intragenic deletion in LIS1, the lissencephaly causative gene in isolated lissencephaly sequence and Miller-Dieker syndrome. Hum Mol Genet. 1997 Feb;6(2):157-64. [PubMed
]
- Feng Y, Olson EC, Stukenberg PT, Flanagan LA, Kirschner MW, Walsh CA: LIS1 regulates CNS lamination by interacting with mNudE, a central component of the centrosome. Neuron. 2000 Dec;28(3):665-79. [PubMed
]
- Tai CY, Dujardin DL, Faulkner NE, Vallee RB: Role of dynein, dynactin, and CLIP-170 interactions in LIS1 kinetochore function. J Cell Biol. 2002 Mar 18;156(6):959-68. Epub 2002 Mar 11. [PubMed
]
- Coquelle FM, Caspi M, Cordelieres FP, Dompierre JP, Dujardin DL, Koifman C, Martin P, Hoogenraad CC, Akhmanova A, Galjart N, De Mey JR, Reiner O: LIS1, CLIP-170's key to the dynein/dynactin pathway. Mol Cell Biol. 2002 May;22(9):3089-102. [PubMed
]
- Pilz DT, Kuc J, Matsumoto N, Bodurtha J, Bernadi B, Tassinari CA, Dobyns WB, Ledbetter DH: Subcortical band heterotopia in rare affected males can be caused by missense mutations in DCX (XLIS) or LIS1. Hum Mol Genet. 1999 Sep;8(9):1757-60. [PubMed
]
- Leventer RJ, Cardoso C, Ledbetter DH, Dobyns WB: LIS1 missense mutations cause milder lissencephaly phenotypes including a child with normal IQ. Neurology. 2001 Aug 14;57(3):416-22. [PubMed
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
5829 |
| Enzyme 23 Name |
N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase |
| Enzyme 23 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class L protein
- PIG-L
|
| Enzyme 23 Gene Name |
PIGL |
| Enzyme 23 Protein Sequence |
>N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
MEAMWLLCVALAVLAWGFLWVWDSSERMKSREQGGRLGAESRTLLVIAHPDDEAMFFAPT
VLGLARLRHWVYLLCFSAGNYYNQGETRKKELLQSCDVLGIPLSSVMIIDNRDFPDDPGM
QWDTEHVARVLLQHIEVNGINLVVTFDAGGVSGHSNHIALYAAVRALHSEGKLPKGCSVL
TLQSVNVLRKYISLLDLPLSLLHTQDVLFVLNSKEVAQAKKAMSCHRSQLLWFRRLYIIF
SRYMRINSLSFL
|
| Enzyme 23 Number of Residues |
252 |
| Enzyme 23 Molecular Weight |
28532 |
| Enzyme 23 Theoretical pI |
8.23 |
| Enzyme 23 GO Classification |
Not Available |
| Enzyme 23 General Function |
Not Available |
| Enzyme 23 Specific Function |
Involved in the second step of GPI biosynthesis. De-N- acetylation of N-acetylglucosaminyl-phosphatidylinositol |
| Enzyme 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
- 6-(N-acetyl-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
Not Available |
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
4239986  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q9Y2B2  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
PIGL_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>759 bp
ATGGAAGCAATGTGGCTCCTGTGTGTGGCGTTGGCGGTCTTGGCATGGGGCTTCCTCTGG
GTTTGGGACTCCTCAGAACGAATGAAGAGTCGGGAGCAGGGAGGACGGCTGGGAGCCGAA
AGCCGGACCCTGCTGGTCATAGCGCACCCTGACGATGAAGCCATGTTTTTTGCTCCCACA
GTGCTAGGCTTGGCCCGCCTAAGGCACTGGGTGTACCTGCTTTGCTTCTCTGCAGGAAAT
TACTACAATCAAGGAGAGACTCGTAAGAAAGAACTTTTGCAGAGCTGTGATGTTTTGGGG
ATTCCACTCTCCAGTGTAATGATTATTGACAACAGGGATTTCCCAGATGACCCAGGCATG
CAGTGGGACACAGAGCACGTGGCCAGAGTCCTCCTTCAGCACATAGAAGTGAATGGCATC
AATCTGGTGGTGACTTTCGATGCAGGGGGAGTAAGTGGCCACAGCAATCACATTGCTCTG
TATGCAGCTGTGAGGGCCCTGCACTCAGAAGGGAAGTTACCTAAAGGGTGCTCTGTGCTC
ACGCTTCAGTCTGTGAATGTGCTGCGCAAGTACATCTCCCTTCTGGATCTGCCCTTGTCT
CTGCTTCATACGCAGGATGTCCTCTTCGTGCTCAACAGCAAAGAAGTGGCACAGGCCAAG
AAAGCCATGTCCTGCCACCGCAGCCAGCTCCTCTGGTTCCGCCGCCTCTACATTATCTTC
TCCCGGTACATGAGAATCAACTCACTGAGCTTCCTCTGA
|
| Enzyme 23 GenBank Gene ID |
AB017165  |
| Enzyme 23 GeneCard ID |
PIGL  |
| Enzyme 23 GenAtlas ID |
PIGL  |
| Enzyme 23 HGNC ID |
HGNC:8966  |
| Enzyme 23 Chromosome Location |
17 |
| Enzyme 23 Locus |
17p12-p11.2 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Watanabe R, Ohishi K, Maeda Y, Nakamura N, Kinoshita T: Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis. Biochem J. 1999 Apr 1;339 ( Pt 1):185-92. [PubMed
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
5830 |
| Enzyme 24 Name |
Aspartoacylase-2 |
| Enzyme 24 Synonyms |
- Aminoacylase-3
- ACY-3
- Acylase III
- Hepatitis C virus core-binding protein 1
- HCBP1
|
| Enzyme 24 Gene Name |
ACY3 |
| Enzyme 24 Protein Sequence |
>Aspartoacylase-2
MCSLPVPREPLRRVAVTGGTHGNEMSGVYLARHWLHAPAELQRASFSAVPVLANPAATSG
CRRYVDHDLNRTFTSSFLNSRPTPDDPYEVTRARELNQLLGPKASGQAFDFVLDLHNTTA
NMGTCLIAKSSHEVFAMHLCRHLQLQYPELSCQVFLYQRSGEESYNLDSVAKNGLGLELG
PQPQGVLRADIFSRMRTLVATVLDFIELFNQGTAFPAFEMEAYRPVGVVDFPRTEAGHLA
GTVHPQLQDRDFQPLQPGAPIFQMFSGEDLLYEGESTVYPVFINEAAYYEKGVAFVQTEK
FTFTVPAMPALTPAPSPAS
|
| Enzyme 24 Number of Residues |
319 |
| Enzyme 24 Molecular Weight |
35241 |
| Enzyme 24 Theoretical pI |
5.77 |
| Enzyme 24 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 24 General Function |
Amino acid transport and metabolism |
| Enzyme 24 Specific Function |
N-acyl-L-aspartate + H(2)O = a carboxylate + L-aspartate |
| Enzyme 24 Pathways |
|
| Enzyme 24 Reactions |
- N-acyl-L-aspartate + H2O = a carboxylate + L-aspartate
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
21654856  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q96HD9  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
ACY3_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>960 bp
ATGTGCTCACTGCCTGTGCCCCGGGAGCCCCTGCGTCGCGTGGCTGTGACTGGGGGCACG
CATGGCAACGAGATGTCGGGCGTCTACCTGGCCCGGCACTGGCTGCATGCCCCCGCAGAG
CTGCAGAGAGCCAGCTTCTCCGCTGTGCCTGTGCTGGCCAACCCGGCAGCCACATCCGGC
TGCCGCCGCTACGTGGACCATGACCTCAACCGCACCTTCACCAGCAGCTTCCTCAATTCC
AGGCCCACCCCGGACGACCCATATGAGGTGACAAGAGCCCGAGAGCTGAACCAGCTGCTG
GGGCCCAAGGCCTCGGGCCAGGCCTTTGACTTTGTCCTTGACCTGCACAACACCACGGCC
AACATGGGCACCTGCTTAATCGCGAAGTCCTCCCACGAAGTCTTTGCCATGCACCTGTGC
CGCCATCTGCAGCTGCAGTACCCCGAGCTGTCCTGCCAGGTCTTCCTGTACCAGCGGTCT
GGGGAGGAGAGCTACAACCTGGACTCTGTGGCCAAAAATGGACTGGGTCTGGAGCTGGGC
CCCCAGCCACAGGGTGTGCTGCGGGCTGACATTTTCTCAAGGATGAGGACCCTGGTGGCC
ACAGTTCTGGACTTCATCGAACTCTTCAACCAGGGTACGGCCTTTCCTGCCTTTGAGATG
GAAGCCTATAGACCCGTGGGCGTCGTGGACTTCCCCCGCACCGAGGCCGGGCACCTGGCA
GGCACTGTGCATCCTCAGCTGCAGGACCGAGACTTCCAGCCACTGCAGCCTGGTGCTCCC
ATCTTCCAGATGTTCAGTGGGGAGGACCTGCTCTATGAGGGAGAGTCCACGGTGTACCCC
GTGTTCATTAACGAGGCTGCCTACTATGAGAAGGGCGTTGCCTTTGTCCAGACTGAGAAG
TTCACATTCACCGTGCCTGCCATGCCCGCGCTGACCCCTGCCCCGAGCCCAGCTTCCTAA
|
| Enzyme 24 GenBank Gene ID |
AY040761  |
| Enzyme 24 GeneCard ID |
ACY3  |
| Enzyme 24 GenAtlas ID |
ACY3  |
| Enzyme 24 HGNC ID |
HGNC:24104  |
| Enzyme 24 Chromosome Location |
11 |
| Enzyme 24 Locus |
11q13.2 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
Not Available |
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
6332 |
| Enzyme 25 Name |
Cytochrome P450 17A1 |
| Enzyme 25 Synonyms |
- CYPXVII
- P450-C17
- P450c17
- Steroid 17-alpha-monooxygenase
- Steroid 17-alpha-hydroxylase/17,20 lyase
|
| Enzyme 25 Gene Name |
CYP17A1 |
| Enzyme 25 Protein Sequence |
>Cytochrome P450 17A1
MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKY
GPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAH
WQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVIS
LICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRN
DLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIF
GAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVGFSRTPTISDRNRLLLLEATIREV
LRLRPVAPMLIPHKANVDSSIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNP
AGTQLISPSVSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIP
KVVFLIDSFKVKIKVRQAWREAQAEGST
|
| Enzyme 25 Number of Residues |
508 |
| Enzyme 25 Molecular Weight |
57371 |
| Enzyme 25 Theoretical pI |
8.87 |
| Enzyme 25 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- heme binding
- ion binding
- iron ion binding
- monooxygenase activity
- oxidoreductase activity
- tetrapyrrole binding
- transition metal ion binding
|
| Process |
- cellular metabolism
- electron transport
- generation of precursor metabolites and energy
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 25 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 25 Specific Function |
Conversion of pregnenolone and progesterone to their 17- alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved in sexual development during fetal life and at puberty |
| Enzyme 25 Pathways |
- C21 Steroid Hormone Metabolism (map00140
)
|
| Enzyme 25 Reactions |
- a steroid + AH2 + O2 = a 17alpha-hydroxysteroid + A + H2O
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
Not Available |
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
181342  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
P05093  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
CP17A_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>1527 bp
ATGTGGGAGCTCGTGGCTCTCTTGCTGCTTACCCTAGCTTATTTGTTTTGGCCCAAGAGA
AGGTGCCCTGGTGCCAAGTACCCCAAGAGCCTCCTGTCCCTGCCCCTGGTGGGCAGCCTG
CCATTCCTCCCCAGACATGGCCATATGCATAACAACTTCTTCAAGCTGCAGAAAAAATAT
GGCCCCATCTATTCTGTTCGTATGGGCACCAAGACTACAGTGATTGTCGGCCACCACCAG
CTGGCCAAGGAGGTGCTTATTAAGAAGGGCAAGGACTTCTCTGGGCGGCCTCAAATGGCA
ACTCTAGACATCGCGTCCAACAACCGTAAGGGTATCGCCTTCGCTGACTCTGGCGCACAC
TGGCAGCTGCATCGAAGGCTGGCGATGGCCACCTTTGCCCTGTTCAAGGATGGCGATCAG
AAGCTGGAGAAGATCATTTGTCAGGAAATCAGTACATTGTGTGATATGCTGGCCACCCAC
AACGGACAGTCCATAGACATCTCCTTTCCTGTCTTCGTGGCGGTAACCAATGTCATCTCC
TTGATCTGCTTCAATACCTCCTACAAGAATGGGGACCCTGAGTTGAATGTCATACAGAAT
TACAATGAAGGCATCATAGACAACCTGAGCAAAGACAGCCTGGTGGACCTAGTCCCCTGG
TTGAAGATTTTCCCCAACAAAACCCTGGAAAAATTAAAGAGCCATGTTAAAATACGAAAT
GATCTGCTGAATAAAATACTTGAAAATTACAAGGAGAAATTCCGGAGTGACTCTATCACC
AACATGCTGGACACACTGATGCAAGCCAAGATGAACTCAGATAATGGCAATGCTGGCCCA
GATCAAGATTCAGAGCTGCTTTCAGATAACCACATTCTCACCACCATAGGGGACATCTTT
GGGGCTGGCGTGGAGACCACCACCTCTGTGGTTAAATGGACCCTGGCCTTCCTGCTGCAC
AATCCTCAGGTGAAGAAGAAGCTCTACGAGGAGATTGACCAGAATGTGGGTTTCAGCCGC
ACACCAACTATCAGTGACCGTAACCGTCTCCTCCTGCTGGAGGCCACCATCCGAGAGGTG
CTTCGCCTCAGGCCCGTGGCCCCTATGCTCATCCCCCACAAGGCCAACGTTGACTCCAGC
ATCGGTGAGTTTGCTGTGGACAAGGGCACAGAAGTTATCATCAATCTGTGGGCGCTGCAT
CACAATGAGAAGGAGTGGCACCAGCCGGATCAGTTCATGCCTGAGCGTTTCTTGAATCCA
GCGGGGACCCAGCTCATCTCACCGTCAGTAAGCTATTTGCCCTTCGGAGCAGGACCTCGC
TCCTGTATAGGTGAGATCCTGGCCCGCCAGGAGCTCTTCCTCATCATGGCCTGGCTGCTG
CAGAGGTTCGACCTGGAGGTGCCAGATGATGGGCAGCTGCCCTCCCTGGAAGGCATCCCC
AAGGTGGTCTTTCTGATCGACTCTTTCAAAGTGAAGATCAAGGTGCGCCAGGCCTGGAGG
GAAGCCCAGGCTGAGGGTAGCACCTAA
|
| Enzyme 25 GenBank Gene ID |
M14564  |
| Enzyme 25 GeneCard ID |
CYP17A1  |
| Enzyme 25 GenAtlas ID |
CYP17A1  |
| Enzyme 25 HGNC ID |
HGNC:2593  |
| Enzyme 25 Chromosome Location |
10 |
| Enzyme 25 Locus |
10q24.3 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Chung BC, Picado-Leonard J, Haniu M, Bienkowski M, Hall PF, Shively JE, Miller WL: Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): cloning of human adrenal and testis cDNAs indicates the same gene is expressed in both tissues. Proc Natl Acad Sci U S A. 1987 Jan;84(2):407-11. [PubMed
]
- Picado-Leonard J, Miller WL: Cloning and sequence of the human gene for P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): similarity with the gene for P450c21. DNA. 1987 Oct;6(5):439-48. [PubMed
]
- Bradshaw KD, Waterman MR, Couch RT, Simpson ER, Zuber MX: Characterization of complementary deoxyribonucleic acid for human adrenocortical 17 alpha-hydroxylase: a probe for analysis of 17 alpha-hydroxylase deficiency. Mol Endocrinol. 1987 May;1(5):348-54. [PubMed
]
- Brentano ST, Picado-Leonard J, Mellon SH, Moore CC, Miller WL: Tissue-specific, cyclic adenosine 3',5'-monophosphate-induced, and phorbol ester-repressed transcription from the human P450c17 promoter in mouse cells. Mol Endocrinol. 1990 Dec;4(12):1972-9. [PubMed
]
- Kagimoto M, Winter JS, Kagimoto K, Simpson ER, Waterman MR: Structural characterization of normal and mutant human steroid 17 alpha-hydroxylase genes: molecular basis of one example of combined 17 alpha-hydroxylase/17,20 lyase deficiency. Mol Endocrinol. 1988 Jun;2(6):564-70. [PubMed
]
- Auchus RJ, Miller WL: Molecular modeling of human P450c17 (17alpha-hydroxylase/17,20-lyase): insights into reaction mechanisms and effects of mutations. Mol Endocrinol. 1999 Jul;13(7):1169-82. [PubMed
]
- Yanase T, Kagimoto M, Suzuki S, Hashiba K, Simpson ER, Waterman MR: Deletion of a phenylalanine in the N-terminal region of human cytochrome P-450(17 alpha) results in partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1989 Oct 25;264(30):18076-82. [PubMed
]
- Lin D, Harikrishna JA, Moore CC, Jones KL, Miller WL: Missense mutation serine106----proline causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1991 Aug 25;266(24):15992-8. [PubMed
]
- Yanase T, Waterman MR, Zachmann M, Winter JS, Simpson ER, Kagimoto M: Molecular basis of apparent isolated 17,20-lyase deficiency: compound heterozygous mutations in the C-terminal region (Arg(496)----Cys, Gln(461)----Stop) actually cause combined 17 alpha-hydroxylase/17,20-lyase deficiency. Biochim Biophys Acta. 1992 Aug 25;1139(4):275-9. [PubMed
]
- Ahlgren R, Yanase T, Simpson ER, Winter JS, Waterman MR: Compound heterozygous mutations (Arg 239----stop, Pro 342----Thr) in the CYP17 (P45017 alpha) gene lead to ambiguous external genitalia in a male patient with partial combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Clin Endocrinol Metab. 1992 Mar;74(3):667-72. [PubMed
]
- Imai T, Globerman H, Gertner JM, Kagawa N, Waterman MR: Expression and purification of functional human 17 alpha-hydroxylase/17,20-lyase (P450c17) in Escherichia coli. Use of this system for study of a novel form of combined 17 alpha-hydroxylase/17,20-lyase deficiency. J Biol Chem. 1993 Sep 15;268(26):19681-9. [PubMed
]
- Monno S, Ogawa H, Date T, Fujioka M, Miller WL, Kobayashi M: Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency. J Biol Chem. 1993 Dec 5;268(34):25811-7. [PubMed
]
- Fardella CE, Zhang LH, Mahachoklertwattana P, Lin D, Miller WL: Deletion of amino acids Asp487-Ser488-Phe489 in human cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1993 Aug;77(2):489-93. [PubMed
]
- Fardella CE, Hum DW, Homoki J, Miller WL: Point mutation of Arg440 to His in cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency. J Clin Endocrinol Metab. 1994 Jul;79(1):160-4. [PubMed
]
- Laflamme N, Leblanc JF, Mailloux J, Faure N, Labrie F, Simard J: Mutation R96W in cytochrome P450c17 gene causes combined 17 alpha-hydroxylase/17-20-lyase deficiency in two French Canadian patients. J Clin Endocrinol Metab. 1996 Jan;81(1):264-8. [PubMed
]
- Biason-Lauber A, Kempken B, Werder E, Forest MG, Einaudi S, Ranke MB, Matsuo N, Brunelli V, Schonle EJ, Zachmann M: 17alpha-hydroxylase/17,20-lyase deficiency as a model to study enzymatic activity regulation: role of phosphorylation. J Clin Endocrinol Metab. 2000 Mar;85(3):1226-31. [PubMed
]
- Gupta MK, Geller DH, Auchus RJ: Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency. J Clin Endocrinol Metab. 2001 Sep;86(9):4416-23. [PubMed
]
- Di Cerbo A, Biason-Lauber A, Savino M, Piemontese MR, Di Giorgio A, Perona M, Savoia A: Combined 17alpha-Hydroxylase/17,20-lyase deficiency caused by Phe93Cys mutation in the CYP17 gene. J Clin Endocrinol Metab. 2002 Feb;87(2):898-905. [PubMed
]
- Van Den Akker EL, Koper JW, Boehmer AL, Themmen AP, Verhoef-Post M, Timmerman MA, Otten BJ, Drop SL, De Jong FH: Differential inhibition of 17alpha-hydroxylase and 17,20-lyase activities by three novel missense CYP17 mutations identified in patients with P450c17 deficiency. J Clin Endocrinol Metab. 2002 Dec;87(12):5714-21. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
9280 |
| Enzyme 26 Name |
CGI-14 protein |
| Enzyme 26 Synonyms |
Not Available |
| Enzyme 26 Gene Name |
Not Available |
| Enzyme 26 Protein Sequence |
>CGI-14 protein
MRGDRAGGGPVLQFTNCRILRGGKLLREDLWVRGGRILDPEKLFFEERRVADERRDCGGR
ILAPGFIDVQINGGFGVDFSQATEDVGSGVALVAREILSHGSPPSAPPWSLPTGVYHKVV
PQIPVKSGGPHGQGVLGLHLEGPFISREKRGTHPEAHLRSFEADAFQDLLATYGPLDNVR
IVTLAPELGVARVLRALTAWICVSLGHSVADLRAAEDAVWSGTFITHLFNAMLPFHHRDP
GIVGLLTSDRLPAGRCIFYGMIADGTHTNPAALRIAHRAHPQGLVLVTDAIPALGLGNGR
HTLGQQEVEVDGLTAYVAGTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLL
GLEKSKGTLDFGADADFVVLDDSLHVQATYISGELVWQADAARQ
|
| Enzyme 26 Number of Residues |
404 |
| Enzyme 26 Molecular Weight |
43213 |
| Enzyme 26 Theoretical pI |
Not Available |
| Enzyme 26 GO Classification |
| Function |
- N-acetylglucosamine-6-phosphate deacetylase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
- peptidase activity
- serine-type peptidase activity
|
| Process |
- N-acetylglucosamine metabolism
- amine metabolism
- amino sugar metabolism
- cellular protein metabolism
- glucosamine metabolism
- macromolecule metabolism
- metabolism
- nitrogen compound metabolism
- physiological process
- protein metabolism
- proteolysis
|
| Component |
|
|
| Enzyme 26 General Function |
Carbohydrate transport and metabolism |
| Enzyme 26 Specific Function |
Not Available |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
- N-Acetyl-D-glucosamine 6-phosphate + H2O --> Acetate + D-Glucosamine 6-phosphate
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
4680667  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
Q9Y303  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
Q9Y303_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
Not Available |
| Enzyme 26 GenBank Gene ID |
AF132948  |
| Enzyme 26 GeneCard ID |
Not Available |
| Enzyme 26 GenAtlas ID |
AMDHD2  |
| Enzyme 26 HGNC ID |
HGNC:24262  |
| Enzyme 26 Chromosome Location |
Not Available |
| Enzyme 26 Locus |
Not Available |
| Enzyme 26 SNPs |
Not Available |
| Enzyme 26 General References |
- Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
11649 |
| Enzyme 27 Name |
Citrate lyase subunit beta-like protein, mitochondrial precursor |
| Enzyme 27 Synonyms |
- Citrate lyase beta-like
|
| Enzyme 27 Gene Name |
CLYBL |
| Enzyme 27 Protein Sequence |
>Citrate lyase subunit beta-like protein, mitochondrial precursor
MALRLLRRAARGAAAAALLRLKASLAADIPRLGYSSSSHHKYIPRRAVLYVPGNDEKKIK
KIPSLNVDCAVLDCEDGVAANKKNEARLRIVKTLEDIDLGPTEKCVRVNSVSSGLAEEDL
ETLLQSRVLPSSLMLPKVESPEEIQWFADKFSFHLKGRKLEQPMNLIPFVETAMGLLNFK
AVCEETLKVGPQVGLFLDAVVFGGEDFRASIGATSSKETLDILYARQKIVVIAKAFGLQA
IDLVYIDFRDGAGLLRQSREGAAMGFTGKQVIHPNQIAVVQEQFSPSPEKIKWAEELIAA
FKEHQQLGKGAFTFQGSMIDMPLLKQAQNTVTLATSIKEK
|
| Enzyme 27 Number of Residues |
340 |
| Enzyme 27 Molecular Weight |
37360 |
| Enzyme 27 Theoretical pI |
Not Available |
| Enzyme 27 GO Classification |
| Function |
- carbon-carbon lyase activity
- catalytic activity
- citrate (pro-3S)-lyase activity
- lyase activity
- oxo-acid-lyase activity
|
| Process |
| — |
| Component |
- citrate lyase complex
- protein complex
|
|
| Enzyme 27 General Function |
Carbohydrate transport and metabolism |
| Enzyme 27 Specific Function |
Not Available |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
- Citrate --> Acetate + Oxaloacetate
|
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
19073013  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
Q8N0X4  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
CLYBL_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
Not Available |
| Enzyme 27 GenBank Gene ID |
AF428253  |
| Enzyme 27 GeneCard ID |
Not Available |
| Enzyme 27 GenAtlas ID |
CLYBL  |
| Enzyme 27 HGNC ID |
HGNC:18355  |
| Enzyme 27 Chromosome Location |
Not Available |
| Enzyme 27 Locus |
Not Available |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Morikawa J, Nishimura Y, Uchida A, Tanaka T: Molecular cloning of novel mouse and human putative citrate lyase beta-subunit. Biochem Biophys Res Commun. 2001 Dec 21;289(5):1282-6. [PubMed
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
13088 |
| Enzyme 28 Name |
ACSS2 protein |
| Enzyme 28 Synonyms |
Not Available |
| Enzyme 28 Gene Name |
ACSS2 |
| Enzyme 28 Protein Sequence |
>ACSS2 protein
PMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLK
ELADEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQISWNQGIDL
WWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDF
HAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFY
TAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQ
TETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMR
TVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESA
LVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDY
IQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDMSTVADPSVISHLFSHRCLTIQ
|
| Enzyme 28 Number of Residues |
534 |
| Enzyme 28 Molecular Weight |
59347 |
| Enzyme 28 Theoretical pI |
5.68 |
| Enzyme 28 GO Classification |
| Function |
- AMP binding
- CoA-ligase activity
- acetate-CoA ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-sulfur bonds
- nucleotide binding
- purine nucleotide binding
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 28 General Function |
Lipid 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 |
40226463  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
Q96FY7  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
Q96FY7_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
Not Available |
| Enzyme 28 GenBank Gene ID |
BC010141  |
| Enzyme 28 GeneCard ID |
Q96FY7  |
| Enzyme 28 GenAtlas ID |
ACSS2  |
| Enzyme 28 HGNC ID |
HGNC:15814  |
| Enzyme 28 Chromosome Location |
Not Available |
| Enzyme 28 Locus |
Not Available |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
15063 |
| Enzyme 29 Name |
Aldehyde dehydrogenase 3B1 (Aldehyde dehydrogenase 3 family, member B1, isoform CRA_c) (cDNA FLJ77312, highly similar to Homo sapiens aldehyde dehydrogenase 3 family, member B1 (ALDH3B1),mRNA) |
| Enzyme 29 Synonyms |
Not Available |
| Enzyme 29 Gene Name |
ALDH3B1 |
| Enzyme 29 Protein Sequence |
>Aldehyde dehydrogenase 3B1 (Aldehyde dehydrogenase 3 family, member B1, isoform CRA_c) (cDNA FLJ77312, highly similar to Homo sapiens aldehyde dehydrogenase 3 family, member B1 (ALDH3B1),mRNA)
MDPLGDTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESE
VSEVAISQGEVTLALRNLRAWMKDERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNL
TLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLGGPQETGQLLEHR
FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA
GQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGC
GRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREK
PLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFD
TFSHHRACLLRSPGMEKLNALRYPPQSPRRLRMLLVAMEAQGCSCTLL
|
| Enzyme 29 Number of Residues |
468 |
| Enzyme 29 Molecular Weight |
51840 |
| Enzyme 29 Theoretical pI |
7.67 |
| Enzyme 29 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 29 General Function |
Energy production and conversion |
| 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 |
125950429  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
A3FMP9  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
A3FMP9_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>1407 bp
ATGGACCCCCTTGGGGACACGCTGCGGCGACTGCGGGAGGCCTTCCACGCGGGGCGCACG
CGGCCAGCTGAGTTCCGGGCTGCGCAGCTCCAAGGCCTGGGCCGCTTCCTGCAAGAAAAC
AAGCAGCTTCTGCACGACGCACTGGCCCAGGACCTGCACAAGTCAGCCTTCGAGTCGGAG
GTGTCTGAGGTTGCCATCAGCCAGGGCGAGGTCACCCTGGCCCTCAGGAACCTCCGGGCC
TGGATGAAGGACGAGCGTGTGCCCAAGAACCTGGCCACGCAGCTGGACTCCGCCTTCATC
CGGAAGGAGCCCTTTGGCCTGGTCCTCATCATTGCGCCCTGGAACTATCCGCTGAACCTG
ACGCTGGTGCCCCTCGTGGGAGCCCTCGCTGCAGGGAACTGTGTGGTGCTGAAGCCATCG
GAGATTAGCAAGAACGTCGAGAAGATCCTGGCCGAGGTGCTGCCCCAATACGTGGACCAG
AGCTGCTTTGCTGTGGTGCTGGGCGGGCCCCAGGAGACGGGGCAGCTGCTAGAGCACAGG
TTCGACTACATCTTCTTCACAGGGAGCCCTCGTGTGGGCAAGATTGTTATGACTGCTGCC
GCCAAGCACCTGACACCTGTCACCCTGGAGCTGGGGGGCAAGAACCCTTGCTACGTGGAC
GACAACTGCGACCCCCAGACCGTGGCCAACCGCGTGGCCTGGTTCCGCTACTTCAACGCC
GGCCAGACCTGCGTGGCCCCCGACTACGTCCTATGCAGCCCTGAGATGCAGGAGAGGCTG
CTGCCTGCCCTGCAGAGCACCATCACCCGTTTCTATGGCGACGACCCCCAGAGCTCCCCA
AACCTGGGCCGCATCATCAACCAGAAACAGTTCCAGCGGCTGCGGGCATTGCTGGGCTGC
GGCCGTGTGGCCATTGGGGGCCAGAGCGATGAGAGCGATCGCTACATCGCCCCCACGGTG
CTGGTGGATGTGCAGGAGATGGAGCCTGTGATGCAGGAGGAGATCTTCGGGCCCATCCTG
CCCATCGTGAACGTGCAGAGCTTGGACGAGGCCATCGAGTTCATCAACCGGCGGGAGAAG
CCCCTGGCCCTGTACGCCTTCTCCAACAGCAGCCAGGTGGTCAAGCGGGTGCTGACCCAG
ACCAGCAGCGGGGGCTTCTGTGGGAACGACGGCTTCATGCACATGACCCTGGCCAGCCTG
CCTTTTGGAGGAGTGGGTGCCAGTGGGATGGGCCGGTACCATGGCAAGTTCTCCTTCGAC
ACCTTCTCCCACCATCGCGCCTGCCTCCTGCGCAGCCCGGGGATGGAGAAGCTCAACGCC
CTCCGCTACCCGCCGCAATCGCCGCGCCGCCTGAGGATGCTGCTGGTGGCCATGGAGGCC
CAAGGCTGCAGCTGCACACTGCTCTGA
|
| Enzyme 29 GenBank Gene ID |
EF411198  |
| Enzyme 29 GeneCard ID |
A3FMP9  |
| Enzyme 29 GenAtlas ID |
Not Available |
| Enzyme 29 HGNC ID |
Not Available |
| Enzyme 29 Chromosome Location |
11 |
| Enzyme 29 Locus |
11q13 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
Not Available |
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
15065 |
| Enzyme 30 Name |
Paraoxonase 2 (cDNA FLJ78444, highly similar to Homo sapiens paraoxonase 2, transcript variant 1, mRNA) |
| Enzyme 30 Synonyms |
Not Available |
| Enzyme 30 Gene Name |
PON2 |
| Enzyme 30 Protein Sequence |
>Paraoxonase 2 (cDNA FLJ78444, highly similar to Homo sapiens paraoxonase 2, transcript variant 1, mRNA)
MGRLVAVGLLGIALALLGERLLALRNRLKASREVESVDLPHCHLIKGIEAGSEDIDILPN
GLAFFSVGLKFPGLHSFAPDKPGGILMMDLKEEKPRARELRISRGFDLASFNPHGISTFI
DNDDTVYLFVVNHPEFKNTVEIFKFEEAENSLLHLKTVKHELLPSVNDITAVGPAHFYAT
NDHYFSDPFLKYLETYLNLHWANVVYYSPNEVKVVAEGFDSANGINISPDDKYIYVADIL
AHEIHVLEKHTNMNLTQLKVLELDTLVDNLSIDPSSGDIWVGCHPNGQKLFVYDPNNPPS
SEVLRIQNILSEKPTVTTVYANNGSVLQGSSVASVYDGKLLIGTLYHRALYCEL
|
| Enzyme 30 Number of Residues |
354 |
| Enzyme 30 Molecular Weight |
39381 |
| Enzyme 30 Theoretical pI |
5.35 |
| Enzyme 30 GO Classification |
| Function |
- arylesterase activity
- carboxylic ester hydrolase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 30 General Function |
Not Available |
| Enzyme 30 Specific Function |
Not Available |
| Enzyme 30 Pathways |
Not Available |
| Enzyme 30 Reactions |
Not Available |
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
158255642  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
A4D1H7  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
A4D1H7_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>1065 bp
ATGGGGCGGCTGGTGGCTGTGGGCTTGCTGGGGATCGCGCTGGCGCTCCTGGGCGAGAGG
CTTCTGGCACTCAGAAATCGACTTAAAGCCTCCAGAGAAGTAGAATCTGTAGACCTTCCA
CACTGCCACCTGATTAAAGGAATTGAAGCTGGCTCTGAAGATATTGACATACTTCCCAAT
GGTCTGGCTTTTTTTAGTGTGGGTCTAAAATTCCCAGGACTCCACAGCTTTGCACCAGAT
AAGCCTGGAGGAATACTAATGATGGATCTAAAAGAAGAAAAACCAAGGGCACGGGAATTA
AGAATCAGTCGTGGGTTTGATTTGGCCTCATTCAATCCACATGGCATCAGCACTTTCATA
GACAACGATGACACAGTTTATCTCTTTGTTGTAAACCACCCAGAATTCAAGAATACAGTG
GAAATTTTTAAATTTGAAGAAGCAGAAAATTCTCTGTTGCATCTGAAAACAGTCAAACAT
GAGCTTCTTCCAAGTGTGAATGACATCACAGCTGTTGGACCGGCACATTTCTATGCCACA
AATGACCACTACTTCTCTGATCCTTTCTTAAAGTATTTAGAAACATACTTGAACTTACAC
TGGGCAAATGTTGTTTACTACAGTCCAAATGAAGTTAAAGTGGTAGCAGAAGGATTTGAT
TCAGCAAATGGGATCAATATTTCACCTGATGATAAGTATATCTATGTTGCTGACATATTG
GCTCATGAAATTCATGTTTTGGAAAAACACACTAATATGAATTTAACTCAGTTGAAGGTA
CTTGAGCTGGATACACTGGTGGATAATTTATCTATTGATCCTTCCTCGGGGGACATCTGG
GTAGGCTGTCATCCTAATGGCCAGAAGCTCTTCGTGTATGACCCGAACAATCCTCCCTCG
TCAGAGGTTCTCCGCATCCAGAACATTCTATCTGAGAAGCCTACAGTGACTACAGTTTAT
GCCAACAATGGGTCTGTTCTCCAAGGAAGTTCTGTAGCCTCAGTGTATGATGGGAAGCTG
CTCATAGGCACTTTATACCACAGAGCCTTGTATTGTGAACTCTAA
|
| Enzyme 30 GenBank Gene ID |
AK291103  |
| Enzyme 30 GeneCard ID |
A4D1H7  |
| Enzyme 30 GenAtlas ID |
Not Available |
| Enzyme 30 HGNC ID |
Not Available |
| Enzyme 30 Chromosome Location |
Not Available |
| Enzyme 30 Locus |
Not Available |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
15066 |
| Enzyme 31 Name |
Paraoxonase 3 (HCG2023324, isoform CRA_a) |
| Enzyme 31 Synonyms |
Not Available |
| Enzyme 31 Gene Name |
PON3 |
| Enzyme 31 Protein Sequence |
>Paraoxonase 3 (HCG2023324, isoform CRA_a)
MGKLVALVLLGVGLSLVGEMFLAFRERVNASREVEPVEPENCHLIEELESGSEDIDILPS
GLAFISSGLKYPGMPNFAPDEPGKIFLMDLNEQNPRAQALEISGGFDKELFNPHGISIFI
DKDNTVYLYVVNHPHMKSTVEIFKFEEQQRSLVYLKTIKHELLKSVNDIVVLGPEQFYAT
RDHYFTNSLLSFFEMILDLRWTYVLFYSPREVKVVAKGFCSANGITVSADQKYVYVADVA
AKNIHIMEKHDNWDLTQLKVIQLGTLVDNLTVDPATGDILAGCHPNPMKLLNYNPEDPPG
SEVLRIQNVLSEKPRVSTVYANNGSVLQGTSVASVYHGKILIGTVFHKTLYCEL
|
| Enzyme 31 Number of Residues |
354 |
| Enzyme 31 Molecular Weight |
39608 |
| Enzyme 31 Theoretical pI |
5.10 |
| Enzyme 31 GO Classification |
| Function |
- arylesterase activity
- carboxylic ester hydrolase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
| — |
| Component |
|
|
| Enzyme 31 General Function |
Not Available |
| Enzyme 31 Specific Function |
Not Available |
| Enzyme 31 Pathways |
Not Available |
| Enzyme 31 Reactions |
Not Available |
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
Not Available |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
A4D1H8  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
A4D1H8_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
Not Available |
| Enzyme 31 GenBank Gene ID |
CH236949  |
| Enzyme 31 GeneCard ID |
A4D1H8  |
| Enzyme 31 GenAtlas ID |
Not Available |
| Enzyme 31 HGNC ID |
Not Available |
| Enzyme 31 Chromosome Location |
Not Available |
| Enzyme 31 Locus |
Not Available |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed
]
|
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
15067 |
| Enzyme 32 Name |
Platelet-activating factor acetylhydrolase 2, 40kDa (Platelet- activating factor acetylhydrolase 2, 40kDa, isoform CRA_a) |
| Enzyme 32 Synonyms |
Not Available |
| Enzyme 32 Gene Name |
PAFAH2 |
| Enzyme 32 Protein Sequence |
>Platelet-activating factor acetylhydrolase 2, 40kDa (Platelet- activating factor acetylhydrolase 2, 40kDa, isoform CRA_a)
MGVNQSVGFPPVTGPHLVGCGDVMEGQNLQGSFFRLFYPCQKAEETMEQPLWIPRYEYCT
GLAEYLQFNKRCGGLLFNLAVGSCRLPVSWNGPFKTKDSGYPLIIFSHGLGAFRTLYSAF
CMELASRGFVVAVPEHRDRSAATTYFCKQAPEENQPTNESLQEEWIPFRRVEEGEKEFHV
RNPQVHQRVSECLRVLKILQEVTAGQTVFNILPGGLDLMTLKGNIDMSRVAVMGHSFGGA
TAILALAKETQFRCAVALDAWMFPLERDFYPKARGPVFFINTEKFQTMESVNLMKKICAQ
HEQSRIITVLGSVHRSQTDFAFVTGNLIGKFFSTETRGSLDPYEGQEVMVRAMLAFLQKH
LDLKEDYNQWNNLIEGIGPSLTPGAPHHLSSL
|
| Enzyme 32 Number of Residues |
392 |
| Enzyme 32 Molecular Weight |
44036 |
| Enzyme 32 Theoretical pI |
6.89 |
| Enzyme 32 GO Classification |
| Function |
- 1-alkyl-2-acetylglycerophosphocholine esterase activity
- carboxylic ester hydrolase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
- lipid catabolism
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
- 2-acetyl-1-alkylglycerophosphocholine esterase complex
- protein complex
- unlocalized protein complex
|
|
| Enzyme 32 General Function |
Not Available |
| Enzyme 32 Specific Function |
Not Available |
| Enzyme 32 Pathways |
Not Available |
| Enzyme 32 Reactions |
Not Available |
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
55859645  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
Q5SY02  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
Q5SY02_HUMAN  |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>1179 bp
ATGGGGGTCAACCAGTCTGTGGGCTTTCCACCTGTCACAGGACCCCACCTCGTAGGCTGT
GGGGATGTGATGGAGGGTCAGAATCTCCAGGGGAGCTTCTTTCGACTCTTCTACCCCTGC
CAAAAGGCAGAGGAGACCATGGAGCAGCCCCTGTGGATTCCCCGCTATGAGTACTGCACT
GGCCTGGCCGAGTACCTGCAGTTTAATAAGCGCTGCGGGGGCTTGCTGTTCAACCTGGCG
GTGGGATCTTGTCGCCTGCCTGTTAGCTGGAATGGCCCCTTTAAGACAAAGGACTCTGGA
TACCCCTTGATCATCTTCTCCCATGGCCTAGGAGCCTTCAGGACTTTGTATTCAGCCTTC
TGCATGGAGCTGGCCTCACGTGGCTTTGTGGTTGCTGTGCCAGAGCACAGGGACCGGTCA
GCGGCAACCACCTATTTCTGCAAGCAGGCCCCAGAAGAGAACCAGCCCACCAATGAATCG
CTGCAGGAGGAATGGATCCCTTTCCGTCGAGTTGAGGAAGGGGAGAAGGAATTTCATGTT
CGGAATCCCCAGGTGCATCAGCGGGTAAGCGAGTGTTTACGGGTGTTGAAGATCCTGCAA
GAGGTCACTGCTGGGCAGACTGTCTTCAACATCTTGCCTGGTGGCTTGGATCTGATGACT
TTGAAGGGCAACATTGACATGAGCCGTGTGGCTGTGATGGGACATTCATTTGGAGGGGCC
ACAGCTATTCTGGCTTTGGCCAAGGAGACCCAATTTCGGTGTGCGGTGGCTCTGGATGCT
TGGATGTTTCCTCTGGAACGTGACTTTTACCCCAAGGCCCGAGGACCTGTGTTCTTTATC
AATACTGAGAAATTCCAGACAATGGAGAGTGTCAATTTGATGAAGAAGATATGTGCCCAG
CATGAACAGTCTAGGATCATAACCGTTCTTGGTTCTGTTCATCGGAGTCAAACTGACTTT
GCTTTTGTGACTGGCAACTTGATTGGTAAATTCTTCTCCACTGAAACCCGTGGGAGCCTG
GACCCCTATGAAGGGCAGGAGGTTATGGTACGGGCCATGTTGGCCTTCCTGCAGAAGCAC
CTCGACCTGAAAGAAGACTATAATCAATGGAACAACCTTATTGAAGGCATTGGACCGTCG
CTCACCCCAGGGGCCCCCCACCATCTGTCCAGCCTGTAG
|
| Enzyme 32 GenBank Gene ID |
AL592064  |
| Enzyme 32 GeneCard ID |
Q5SY02  |
| Enzyme 32 GenAtlas ID |
PAFAH2  |
| Enzyme 32 HGNC ID |
HGNC:8579  |
| Enzyme 32 Chromosome Location |
Not Available |
| Enzyme 32 Locus |
Not Available |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
Not Available |
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
15068 |
| Enzyme 33 Name |
cDNA FLJ76635, highly similar to Homo sapiens phosphatidylinositol glycan, class L (PIGL), mRNA (Phosphatidylinositol glycan, class L, isoform CRA_b) |
| Enzyme 33 Synonyms |
Not Available |
| Enzyme 33 Gene Name |
PIGL |
| Enzyme 33 Protein Sequence |
>cDNA FLJ76635, highly similar to Homo sapiens phosphatidylinositol glycan, class L (PIGL), mRNA (Phosphatidylinositol glycan, class L, isoform CRA_b)
MEAMWLLCVALAVLAWGFLWVWDSSERMKSREQGGRLGAESRTLLVIAHPDDEAMFFAPT
VLGLARLRHWVYLLCFSAGNYYNQGETRKKELLQSCDVLGIPLSSVMIIDNRDFPDDPGM
QWDTEHVARVLLQHIEVNGINLVVTFDAGGVSGHSNHIALYAAVRALHSEGKLPKGCSVL
TLQSVNVLRKYISLLDLPLSLLHTQDVLFVLNSKEVAQAKKAMSCHRSQLLWFRRLYIIF
SRYMRINSLSFL
|
| Enzyme 33 Number of Residues |
252 |
| Enzyme 33 Molecular Weight |
28532 |
| Enzyme 33 Theoretical pI |
8.23 |
| Enzyme 33 GO Classification |
Not Available |
| Enzyme 33 General Function |
Not Available |
| Enzyme 33 Specific Function |
Not Available |
| Enzyme 33 Pathways |
Not Available |
| Enzyme 33 Reactions |
Not Available |
| Enzyme 33 Pfam Domain Function |
Not Available |
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
158259325  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
A8KA67  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
A8KA67_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>759 bp
ATGGAAGCAATGTGGCTCCTGTGTGTGGCGTTGGCGGTCTTGGCATGGGGCTTCCTCTGG
GTTTGGGACTCCTCAGAACGAATGAAGAGTCGGGAGCAGGGAGGACGGCTGGGAGCCGAA
AGCCGGACCCTGCTGGTCATAGCGCACCCTGACGATGAAGCCATGTTTTTTGCTCCCACA
GTGCTAGGCTTGGCCCGCCTAAGGCACTGGGTGTACCTGCTTTGCTTCTCTGCAGGAAAT
TACTACAATCAAGGAGAGACTCGTAAGAAAGAACTTTTGCAGAGCTGTGATGTTTTGGGG
ATTCCACTCTCCAGTGTAATGATTATTGACAACAGGGATTTCCCAGATGACCCAGGCATG
CAGTGGGACACAGAGCACGTGGCCAGAGTCCTCCTTCAGCACATAGAAGTGAATGGCATC
AATCTGGTGGTGACTTTCGATGCAGGGGGAGTAAGTGGCCACAGCAATCACATTGCTCTG
TATGCAGCTGTGAGGGCCCTGCACTCAGAAGGGAAGTTACCTAAAGGGTGCTCTGTGCTC
ACGCTTCAGTCTGTGAATGTGCTGCGCAAGTACATCTCCCTTCTGGATCTGCCCTTGTCT
CTGCTTCATACGCAGGATGTCCTCTTCGTGCTCAACAGCAAAGAAGTGGCACAGGCCAAG
AAAGCCATGTCCTGCCACCGCAGCCAGCTCCTCTGGTTCCGCCGCCTCTACATTATCTTC
TCCCGGTACATGAGAATCAACTCACTGAGCTTCCTCTGA
|
| Enzyme 33 GenBank Gene ID |
AK292932  |
| Enzyme 33 GeneCard ID |
A8KA67  |
| Enzyme 33 GenAtlas ID |
Not Available |
| Enzyme 33 HGNC ID |
Not Available |
| Enzyme 33 Chromosome Location |
17 |
| Enzyme 33 Locus |
17p12-p11.2 |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
Not Available |
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
16427 |
| Enzyme 34 Name |
cDNA, FLJ93559, Homo sapiens platelet-activating factor acetylhydrolase, isoformIb, alpha subunit 45kDa (PAFAH1B1), mRNA (Platelet-activating factor acetylhydrolase, isoform Ib, alpha subunit 45kDa) |
| Enzyme 34 Synonyms |
Not Available |
| Enzyme 34 Gene Name |
PAFAH1B1 |
| Enzyme 34 Protein Sequence |
>cDNA, FLJ93559, Homo sapiens platelet-activating factor acetylhydrolase, isoformIb, alpha subunit 45kDa (PAFAH1B1), mRNA (Platelet-activating factor acetylhydrolase, isoform Ib, alpha subunit 45kDa)
MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDVNEELDKKYAGLLEKKWTSVIR
LQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVF
SVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQ
GFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMV
RPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSE
TKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDK
TLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR
|
| Enzyme 34 Number of Residues |
410 |
| Enzyme 34 Molecular Weight |
46638 |
| Enzyme 34 Theoretical pI |
7.40 |
| Enzyme 34 GO Classification |
Not Available |
| Enzyme 34 General Function |
Not Available |
| Enzyme 34 Specific Function |
Not Available |
| Enzyme 34 Pathways |
Not Available |
| Enzyme 34 Reactions |
Not Available |
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
Not Available |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
B2R7Q7  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
B2R7Q7_HUMAN  |
| Enzyme 34 PDB ID |
1UUJ  |
| Enzyme 34 PDB File |
Show |
| Enzyme 34 3D Structure |
|
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
Not Available |
| Enzyme 34 GenBank Gene ID |
AK313078  |
| Enzyme 34 GeneCard ID |
B2R7Q7  |
| Enzyme 34 GenAtlas ID |
Not Available |
| Enzyme 34 HGNC ID |
Not Available |
| Enzyme 34 Chromosome Location |
17 |
| Enzyme 34 Locus |
17p13.3 |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
Not Available |
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
16428 |
| Enzyme 35 Name |
cDNA FLJ31531 fis, clone NT2RI2000585, highly similar to Sialate O-acetylesterase (EC 3.1.1.53) |
| Enzyme 35 Synonyms |
- SubName: Sialic acid acetylesterase
|
| Enzyme 35 Gene Name |
SIAE |
| Enzyme 35 Protein Sequence |
>cDNA FLJ31531 fis, clone NT2RI2000585, highly similar to Sialate O-acetylesterase (EC 3.1.1.53)
MVAPGLVLGLVLPLILWADRSAGIGFRFASYINNDMVLQKEPAGAVIWGFGTPGATVTVT
LRQGQETIMKKVTSVKAHSDTWMVVLDPMKPGGPFEVMAQQTLEKINFTLRVHDVLFGDV
WLCSGQSNMQMTVLQIFNATRELSNTAAYQSVRILSVSPIQAEQELEDLVAVDLQWSKPT
SENLGHGYFKYMSAVCWLFGRHLYDTLQYPIGLIASSWGGTPIEAWSSGRSLKACGVPKQ
GSIPYDSVTGPSKHSVLWNAMIHPLCNMTLKGVVWYQGESNINYNTDLYNCTFPALIEDW
RETFHRGSQGQTERFFPFGLVQLSSDLSKKSSDDGFPQIRWHQTADFGYVPNPKMPNTFM
AVAMDLCDRDSPFGSIHPRDKQTVAYRLHLGARALAYGEKNLTFEGPLPEKIELLAHKGL
LNLTYYQQIQVQKKDNKIFEISCCSDHRCKWLPASMNTVSTQSLTLAIDSCHGTVVALRY
AWTTWPCEYKQCPLYHPSSALPAPPFIAFITDQGPGHQSNVAK
|
| Enzyme 35 Number of Residues |
523 |
| Enzyme 35 Molecular Weight |
58315 |
| Enzyme 35 Theoretical pI |
7.35 |
| Enzyme 35 GO Classification |
Not Available |
| Enzyme 35 General Function |
Not Available |
| Enzyme 35 Specific Function |
Not Available |
| Enzyme 35 Pathways |
Not Available |
| Enzyme 35 Reactions |
- N-acetyl-O-acetylneuraminate + H2O = N-acetylneuraminate + acetate [RN:R01810] ALL_REAC R01810
|
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
Not Available |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
B3KPB0  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
B3KPB0_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
Not Available |
| Enzyme 35 GenBank Gene ID |
AK056093  |
| Enzyme 35 GeneCard ID |
B3KPB0  |
| Enzyme 35 GenAtlas ID |
Not Available |
| Enzyme 35 HGNC ID |
Not Available |
| Enzyme 35 Chromosome Location |
11 |
| Enzyme 35 Locus |
11q24 |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 General References |
Not Available |
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
16429 |
| Enzyme 36 Name |
cDNA FLJ16680 fis, clone TLIVE2008221, highly similar to Acyl-coenzyme A thioesterase 12 (EC 3.1.2.1) |
| Enzyme 36 Synonyms |
- SubName: Acyl-CoA thioesterase 12, isoform CRA_b
|
| Enzyme 36 Gene Name |
ACOT12 |
| Enzyme 36 Protein Sequence |
>cDNA FLJ16680 fis, clone TLIVE2008221, highly similar to Acyl-coenzyme A thioesterase 12 (EC 3.1.2.1)
MERPAPGEVVMSQAIQPAHATARGELSAGQLLKWIDTTACLAAEKHAGVSCVTASVDDIQ
FEETARVGQVITIKAKVTRAFSTSMEISIKVMVQDMLTGIEKLVSVAFSTFVAKPVGKEK
IHLKPVTLLTEQDHVEHNLAAERRKVRLQHEDTFNNLMKESSKFDDLIFDEEEGAVSTRG
TSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSVDMFKFRGPST
VGDRLVFTAIVNNTFQTCVEVGVRVEAFDCQEWAEGRGRHINSAFLIYNAADDKENLITF
PRIQPISKDDFRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDISKQASLSDSNVEALK
KLAAKRGWEVTSTVEKIKIYTLEEHDVLSVWVEKHVGSPAHLAYRLLSDFTKRPLWDPHF
VSCEVIDWVSEDDQLYHITCPILNDDKPKDLVVLVSRRKPLKDGNTYTVAVKSVILPSVP
PSPQYIRSEIICAGFLIHAIDSNSCIVSYFNHMSASILPYFAGNLGGWSKSIEETAASCI
QFLENPPDDGFVSTF
|
| Enzyme 36 Number of Residues |
555 |
| Enzyme 36 Molecular Weight |
62035 |
| Enzyme 36 Theoretical pI |
6.76 |
| Enzyme 36 GO Classification |
| Function |
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 36 General Function |
Lipid transport and metabolism |
| Enzyme 36 Specific Function |
Not Available |
| Enzyme 36 Pathways |
Not Available |
| Enzyme 36 Reactions |
- acetyl-CoA + H2O = CoA + acetate [RN:R00227] ALL_REAC R00227
|
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
Not Available |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
B3KVK9  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
B3KVK9_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
Not Available |
| Enzyme 36 GenBank Gene ID |
AK122960  |
| Enzyme 36 GeneCard ID |
B3KVK9  |
| Enzyme 36 GenAtlas ID |
Not Available |
| Enzyme 36 HGNC ID |
Not Available |
| Enzyme 36 Chromosome Location |
Not Available |
| Enzyme 36 Locus |
Not Available |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
Not Available |
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
16430 |
| Enzyme 37 Name |
cDNA, FLJ92383, Homo sapiens acylphosphatase 1, erythrocyte (common) type (ACYP1), mRNA (Acylphosphatase 1, erythrocyte (Common) type) |
| Enzyme 37 Synonyms |
Not Available |
| Enzyme 37 Gene Name |
ACYP1 |
| Enzyme 37 Protein Sequence |
>cDNA, FLJ92383, Homo sapiens acylphosphatase 1, erythrocyte (common) type (ACYP1), mRNA (Acylphosphatase 1, erythrocyte (Common) type)
MAEGNTLISVDYEIFGKVQGVFFRKHTQAEGKKLGLVGWVQNTDRGTVQGQLQGPISKVR
HMQEWLETRGSPKSHIDKANFNNEKVILKLDYSDFQIVK
|
| Enzyme 37 Number of Residues |
99 |
| Enzyme 37 Molecular Weight |
11261 |
| Enzyme 37 Theoretical pI |
9.94 |
| Enzyme 37 GO Classification |
| Function |
- acylphosphatase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 37 General Function |
Energy production and conversion |
| Enzyme 37 Specific Function |
Not Available |
| Enzyme 37 Pathways |
Not Available |
| Enzyme 37 Reactions |
Not Available |
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
Not Available |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
B2R590  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
B2R590_HUMAN  |
| Enzyme 37 PDB ID |
2ACY  |
| Enzyme 37 PDB File |
Show |
| Enzyme 37 3D Structure |
|
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
Not Available |
| Enzyme 37 GenBank Gene ID |
AK312101  |
| Enzyme 37 GeneCard ID |
B2R590  |
| Enzyme 37 GenAtlas ID |
Not Available |
| Enzyme 37 HGNC ID |
Not Available |
| Enzyme 37 Chromosome Location |
14 |
| Enzyme 37 Locus |
14q24.3 |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
Not Available |
| Enzyme 37 Metabolite References |
Not Available |