|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5975 |
| Enzyme 1 Name |
Glutamate decarboxylase 2 |
| Enzyme 1 Synonyms |
- 65 kDa glutamic acid decarboxylase
- GAD-65
- Glutamate decarboxylase 65 kDa isoform
|
| Enzyme 1 Gene Name |
GAD2 |
| Enzyme 1 Protein Sequence |
>Glutamate decarboxylase 2
MASPGSGFWSFGSEDGSGDSENPGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGG
SQPPRAAARKAACACDQKPCSCSKVDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQ
YVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFN
QLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFS
PGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLKKGAAALGIGTDSVI
LIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIW
MHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQNCNQ
MHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHVDKCLELAEY
LYNIIKNREGYEMVFDGKPQHTNVCFWYIPPSLRTLEDNEERMSRLSKVAPVIKARMMEY
GTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL
|
| Enzyme 1 Number of Residues |
585 |
| Enzyme 1 Molecular Weight |
65410.8 |
| Enzyme 1 Theoretical pI |
6.89 |
| Enzyme 1 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in carboxy-lyase activity |
| Enzyme 1 Specific Function |
Catalyzes the production of GABA |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- L-glutamate = 4-aminobutanoate + CO2 [RN:R00261]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
Not Available |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q05329  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
DCE2_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1758 bp
ATGGCATCTCCGGGCTCTGGCTTTTGGTCTTTCGGGTCGGAAGATGGCTCTGGGGATTCC
GAGAATCCCGGCACAGCGCGAGCCTGGTGCCAAGTGGCTCAGAAGTTCACGGGCGGCATC
GGAAACAAACTGTGCGCCCTGCTCTACGGAGACGCCGAGAAGCCGGCGGAGAGCGGCGGG
AGCCAACCCCCGCGGGCCGCCGCCCGGAAGGCCGCCTGCGCCTGCGACCAGAAGCCCTGC
AGCTGCTCCAAAGTGGATGTCAACTACGCGTTTCTCCATGCAACAGACCTGCTGCCGGCG
TGTGATGGAGAAAGGCCCACTTTGGCGTTTCTGCAAGATGTTATGAACATTTTACTTCAG
TATGTGGTGAAAAGTTTCGATAGATCAACCAAAGTGATTGATTTCCATTATCCTAATGAG
CTTCTCCAAGAATATAATTGGGAATTGGCAGACCAACCACAAAATTTGGAGGAAATTTTG
ATGCATTGCCAAACAACTCTAAAATATGCAATTAAAACAGGGCATCCTAGATACTTCAAT
CAACTTTCTACTGGTTTGGATATGGTTGGATTAGCAGCAGACTGGCTGACATCAACAGCA
AATACTAACATGTTCACCTATGAAATTGCTCCAGTATTTGTGCTTTTGGAATATGTCACA
CTAAAGAAAATGAGAGAAATCATTGGCTGGCCAGGGGGCTCTGGCGATGGGATATTTTCT
CCCGGTGGCGCCATATCTAACATGTATGCCATGATGATCGCACGCTTTAAGATGTTCCCA
GAAGTCAAGGAGAAAGGAATGGCTGCTCTTCCCAGGCTCATTGCCTTCACGTCTGAACAT
AGTCATTTTTCTCTCAAGAAGGGAGCTGCAGCCTTAGGGATTGGAACAGACAGCGTGATT
CTGATTAAATGTGATGAGAGAGGGAAAATGATTCCATCTGATCTTGAAAGAAGGATTCTT
GAAGCCAAACAGAAAGGGTTTGTTCCTTTCCTCGTGAGTGCCACAGCTGGAACCACCGTG
TACGGAGCATTTGACCCCCTCTTAGCTGTCGCTGACATTTGCAAAAAGTATAAGATCTGG
ATGCATGTGGATGCAGCTTGGGGTGGGGGATTACTGATGTCCCGAAAACACAAGTGGAAA
CTGAGTGGCGTGGAGAGGGCCAACTCTGTGACGTGGAATCCACACAAGATGATGGGAGTC
CCTTTGCAGTGCTCTGCTCTCCTGGTTAGAGAAGAGGGATTGATGCAGAATTGCAACCAA
ATGCATGCCTCCTACCTCTTTCAGCAAGATAAACATTATGACCTGTCCTATGACACTGGA
GACAAGGCCTTACAGTGCGGACGCCACGTTGATGTTTTTAAACTATGGCTGATGTGGAGG
GCAAAGGGGACTACCGGGTTTGAAGCGCATGTTGATAAATGTTTGGAGTTGGCAGAGTAT
TTATACAACATCATAAAAAACCGAGAAGGATATGAGATGGTGTTTGATGGGAAGCCTCAG
CACACAAATGTCTGCTTCTGGTACATTCCTCCAAGCTTGCGTACTCTGGAAGACAATGAA
GAGAGAATGAGTCGCCTCTCGAAGGTGGCTCCAGTGATTAAAGCCAGAATGATGGAGTAT
GGAACCACAATGGTCAGCTACCAACCCTTGGGAGACAAGGTCAATTTCTTCCGCATGGTC
ATCTCAAACCCAGCGGCAACTCACCAAGACATTGACTTCCTGATTGAAGAAATAGAACGC
CTTGGACAAGATTTATAA
|
| Enzyme 1 GenBank Gene ID |
M81882  |
| Enzyme 1 GeneCard ID |
GAD2  |
| Enzyme 1 GenAtlas ID |
GAD2  |
| Enzyme 1 HGNC ID |
HGNC:4093  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
10p11.23 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Karlsen AE, Hagopian WA, Grubin CE, Dube S, Disteche CM, Adler DA, Barmeier H, Mathewes S, Grant FJ, Foster D, et al.: Cloning and primary structure of a human islet isoform of glutamic acid decarboxylase from chromosome 10. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8337-41. [PubMed
]
- Bu DF, Erlander MG, Hitz BC, Tillakaratne NJ, Kaufman DL, Wagner-McPherson CB, Evans GA, Tobin AJ: Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2115-9. [PubMed
]
- Bu DF, Tobin AJ: The exon-intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive from a common ancestral GAD. Genomics. 1994 May 1;21(1):222-8. [PubMed
]
- Mauch L, Abney CC, Berg H, Scherbaum WA, Liedvogel B, Northemann W: Characterization of a linear epitope within the human pancreatic 64-kDa glutamic acid decarboxylase and its autoimmune recognition by sera from insulin-dependent diabetes mellitus patients. Eur J Biochem. 1993 Mar 1;212(2):597-603. [PubMed
]
- Kim J, Richter W, Aanstoot HJ, Shi Y, Fu Q, Rajotte R, Warnock G, Baekkeskov S: Differential expression of GAD65 and GAD67 in human, rat, and mouse pancreatic islets. Diabetes. 1993 Dec;42(12):1799-808. [PubMed
]
- Namchuk M, Lindsay L, Turck CW, Kanaani J, Baekkeskov S: Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes membrane anchored from soluble glutamic acid decarboxylase 65 and is restricted to glutamic acid decarboxylase 65alpha. J Biol Chem. 1997 Jan 17;272(3):1548-57. [PubMed
]
- Kanaani J, el-Husseini Ael-D, Aguilera-Moreno A, Diacovo JM, Bredt DS, Baekkeskov S: A combination of three distinct trafficking signals mediates axonal targeting and presynaptic clustering of GAD65. J Cell Biol. 2002 Sep 30;158(7):1229-38. [PubMed
]
- Corper AL, Stratmann T, Apostolopoulos V, Scott CA, Garcia KC, Kang AS, Wilson IA, Teyton L: A structural framework for deciphering the link between I-Ag7 and autoimmune diabetes. Science. 2000 Apr 21;288(5465):505-11. [PubMed
]
- Fenalti G, Law RH, Buckle AM, Langendorf C, Tuck K, Rosado CJ, Faux NG, Mahmood K, Hampe CS, Banga JP, Wilce M, Schmidberger J, Rossjohn J, El-Kabbani O, Pike RN, Smith AI, Mackay IR, Rowley MJ, Whisstock JC: GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop. Nat Struct Mol Biol. 2007 Apr;14(4):280-6. Epub 2007 Mar 25. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6224 |
| Enzyme 2 Name |
Cysteine sulfinic acid decarboxylase |
| Enzyme 2 Synonyms |
- Cysteine-sulfinate decarboxylase
- Sulfinoalanine decarboxylase
|
| Enzyme 2 Gene Name |
CSAD |
| Enzyme 2 Protein Sequence |
>Cysteine sulfinic acid decarboxylase
MADSEALPSLAGDPVAVEALLRAVFGVVVDEAIQKGTSVSQKVCEWKEPEELKQLLDLEL
RSQGESQKQILERCRAVIRYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEI
APVFVLMEEEVLRKLRALVGWSSGDGIFCPGGSISNMYAVNLARYQRYPDCKQRGLRTLP
PLALFTSKECHYSIQKGAAFLGLGTDSVRVVKADERGKMVPEDLERQIGMAEAEGAVPFL
VSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLLDGIQRADSVA
WNPHKLLAAGLQCSALLLQDTSNLLKRCHGSQASYLFQQDKFYDVALDTGDKVVQCGRRV
DCLKLWLMWKAQGDQGLERRIDQAFVLARYLVEEMKKREGFELVMEPEFVNVCFWFVPPS
LRGKQESPDYHERLSKVAPVLKERMVKEGSMMIGYQPHGTRGNFFRVVVANSALTCADMD
FLLNELERLGQDL
|
| Enzyme 2 Number of Residues |
493 |
| Enzyme 2 Molecular Weight |
55022.8 |
| Enzyme 2 Theoretical pI |
6.44 |
| Enzyme 2 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in carboxy-lyase activity |
| Enzyme 2 Specific Function |
3-sulfino-L-alanine = hypotaurine + CO(2) |
| Enzyme 2 Pathways |
- Taurine and Hypotaurine Metabolism (map00430
)
|
| Enzyme 2 Reactions |
- 3-sulfino-L-alanine = hypotaurine + CO2 [RN:R02466]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
4894560  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q9Y600  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
CSAD_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1482 bp
ATGGCTGACTCAGAAGCACTCCCCTCCCTTGCTGGGGACCCAGTGGCTGTGGAAGCCTTG
CTCCGGGCCGTGTTTGGGGTTGTTGTGGATGAGGCCATTCAGAAAGGAACCAGTGTCTCC
CAGAAGGTCTGTGAGTGGAAGGAGCCTGAGGAGCTGAAGCAGCTGCTGGATTTGGAGCTG
CGGAGCCAGGGCGAGTCACAGAAGCAGATCCTGGAGCGGTGTCGGGCTGTGATTCGCTAC
AGTGTCAAGACTGGTCACCCTCGGTTCTTCAACCAGCTCTTCTCTGGGTTGGATCCCCAT
GCTCTGGCCGGGCGCATTATCACTGAGAGCCTCAACACCAGCCAGTACACATATGAAATC
GCCCCCGTGTTTGTGCTCATGGAAGAGGAGGTGCTGAGGAAACTGCGGGCCCTGGTGGGC
TGGAGCTCTGGGGACGGAATCTTCTGCCCTGGTGGCTCCATCTCCAACATGTATGCTGTA
AATCTGGCCCGCTATCAGCGCTACCCGGATTGCAAGCAGAGGGGCCTCCGCACACTGCCG
CCCCTGGCCCTATTCACATCGAAGGAGTGTCACTACTCCATCCAGAAGGGAGCTGCGTTT
CTGGGACTTGGCACCGACAGTGTCCGAGTGGTCAAGGCTGATGAGAGAGGGAAAATGGTC
CCCGAGGATCTGGAGAGGCAGATTGGTATGGCCGAGGCTGAGGGTGCTGTGCCGTTCCTG
GTCAGTGCCACCTCTGGCACCACTGTGCTAGGGGCCTTTGACCCCCTGGGGGCAATTGCT
GATGTGTGCCAGCGTCATGGGCTATGGCTGCATGTGGATGCTGCCTGGGGTGGGAGCGTC
CTGCTGTCACAGACACACAGGCATCTCCTGGATGGGATCCAGAGGGCTGACTCTGTGGCC
TGGAATCCCCACAAGCTCCTCGCAGCAGGCCTGCAATGCTCTGCACTTCTTCTCCAGGAT
ACCTCGAACCTGCTCAAGCGCTGCCATGGGTCCCAGGCCAGCTACCTTTTCCAGCAGGAC
AAGTTCTACGATGTGGCTCTGGACACGGGAGACAAGGTGGTGCAGTGTGGCCGCCGTGTG
GACTGTCTGAAGCTGTGGCTCATGTGGAAGGCACAGGGCGATCAAGGGCTGGAGCGGCGC
ATCGACCAGGCCTTTGTCCTTGCCCGGTACCTGGTGGAGGAAATGAAGAAGCGGGAAGGG
TTTGAGCTAGTCATGGAGCCTGAGTTTGTCAATGTGTGTTTCTGGTTCGTACCCCCCAGC
CTGCGAGGGAAGCAGGAGAGTCCAGATTACCACGAAAGGCTGTCAAAGGTGGCCCCCGTG
CTCAAGGAGCGCATGGTGAAGGAGGGCTCCATGATGATTGGCTACCAGCCCCACGGGACC
CGGGGCAACTTCTTCCGTGTGGTTGTGGCCAACTCTGCACTGACCTGTGCTGATATGGAC
TTCCTCCTCAACGAGCTGGAGCGGCTAGGCCAGGACCTGTGA
|
| Enzyme 2 GenBank Gene ID |
AF116547  |
| Enzyme 2 GeneCard ID |
CSAD  |
| Enzyme 2 GenAtlas ID |
CSAD  |
| Enzyme 2 HGNC ID |
HGNC:18966  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
12q13.11-q14.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
7966 |
| Enzyme 3 Name |
Hypothetical protein GAD1 |
| Enzyme 3 Synonyms |
Not Available |
| Enzyme 3 Gene Name |
GAD1 |
| Enzyme 3 Protein Sequence |
>Hypothetical protein GAD1
MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEK
SRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEV
VDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGV
RTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWS
SKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAA
LGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIA
DICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKE
KGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQI
NKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAP
KIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL
|
| Enzyme 3 Number of Residues |
594 |
| Enzyme 3 Molecular Weight |
66897 |
| Enzyme 3 Theoretical pI |
7.67 |
| Enzyme 3 GO Classification |
| Function |
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- lyase activity
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Amino acid transport and metabolism |
| Enzyme 3 Specific Function |
Not Available |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
62988850  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q53TQ7  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
Q53TQ7_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1785 bp
ATGGCGTCTTCGACCCCATCTTCGTCCGCAACCTCCTCGAACGCGGGAGCGGACCCCAAT
ACCACTAACCTGCGCCCCACAACGTACGATACCTGGTGCGGCGTGGCCCATGGATGCACC
AGAAAACTGGGGCTCAAGATCTGCGGCTTCTTGCAAAGGACCAACAGCCTGGAAGAGAAG
AGTCGCCTTGTGAGTGCCTTCAAGGAGAGGCAATCCTCCAAGAACCTGCTTTCCTGTGAA
AACAGCGACCGGGATGCCCGCTTCCGGCGCACAGAGACTGACTTCTCTAATCTGTTTGCT
AGAGATCTGCTTCCGGCTAAGAACGGTGAGGAGCAAACCGTGCAATTCCTCCTGGAAGTG
GTGGACATACTCCTCAACTATGTCCGCAAGACATTTGATCGCTCCACCAAGGTGCTGGAC
TTTCATCACCCACACCAGTTGCTGGAAGGCATGGAGGGCTTCAACTTGGAGCTCTCTGAC
CACCCCGAGTCCCTGGAGCAGATCCTGGTTGACTGCAGAGACACCTTGAAGTATGGGGTT
CGCACAGGTCATCCTCGATTTTTCAACCAGCTCTCCACTGGATTGGATATTATTGGCCTA
GCTGGAGAATGGCTGACATCAACGGCCAATACCAACATGTTTACATATGAAATTGCACCA
GTGTTTGTCCTCATGGAACAAATAACACTTAAGAAGATGAGAGAGATAGTTGGATGGTCA
AGTAAAGATGGTGATGGGATATTTTCTCCTGGGGGCGCCATATCCAACATGTACAGCATC
ATGGCTGCTCGCTACAAGTACTTCCCGGAAGTTAAGACAAAGGGCATGGCGGCTGTGCCT
AAACTGGTCCTCTTCACCTCAGAACAGAGTCACTATTCCATAAAGAAAGCTGGGGCTGCA
CTTGGCTTTGGAACTGACAATGTGATTTTGATAAAGTGCAATGAAAGGGGGAAAATAATT
CCAGCTGATTTTGAGGCAAAAATTCTTGAAGCCAAACAGAAGGGATATGTTCCCTTTTAT
GTCAATGCAACTGCTGGCACGACTGTTTATGGAGCTTTTGATCCGATACAAGAGATTGCA
GATATATGTGAGAAATATAACCTTTGGTTGCATGTCGATGCTGCCTGGGGAGGTGGGCTG
CTCATGTCCAGGAAGCACCGCCATAAACTCAACGGCATAGAAAGGGCCAACTCAGTCACC
TGGAACCCTCACAAGATGATGGGCGTGCTGTTGCAGTGCTCTGCCATTCTCGTCAAGGAA
AAGGGTATACTCCAAGGATGCAACCAGATGTGTGCAGGATACCTCTTCCAGCCAGACAAG
CAGTATGATGTCTCCTACGACACCGGGGACAAGGCAATTCAGTGTGGCCGCCACGTGGAT
ATCTTCAAGTTCTGGCTGATGTGGAAAGCAAAGGGCACAGTGGGATTTGAAAACCAGATC
AACAAATGCCTGGAACTGGCTGAATACCTCTATGCCAAGATTAAAAACAGAGAAGAATTT
GAGATGGTTTTCAATGGCGAGCCTGAGCACACAAACGTCTGTTTTTGGTATATTCCACAA
AGCCTCAGGGGTGTGCCAGACAGCCCTCAACGACGGGAAAAGCTACACAAGGTGGCTCCA
AAAATCAAAGCCCTGATGATGGAGTCAGGTACGACCATGGTTGGCTACCAGCCCCAAGGG
GACAAGGCCAACTTCTTCCGGATGGTCATCTCCAACCCAGCCGCTACCCAGTCTGACATT
GACTTCCTCATTGAGGAGATAGAAAGACTGGGCCAGGATCTGTAA
|
| Enzyme 3 GenBank Gene ID |
AC007405  |
| Enzyme 3 GeneCard ID |
GAD1  |
| Enzyme 3 GenAtlas ID |
GAD1  |
| Enzyme 3 HGNC ID |
HGNC:4092  |
| Enzyme 3 Chromosome Location |
2 |
| Enzyme 3 Locus |
2q31 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
Not Available |
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
13113 |
| Enzyme 4 Name |
Chromosome 10 open reading frame 22 |
| Enzyme 4 Synonyms |
- Chromosome 10 open reading frame 22, isoform CRA_a
|
| Enzyme 4 Gene Name |
C10orf22 |
| Enzyme 4 Protein Sequence |
>Chromosome 10 open reading frame 22
MPRDNMASLIQRIARQACLTFRGSGGGRGASDRDAASGPEAPMQPGFPENLSKLKSLLTQ
LRAEDLNIAPRKATLQPLPPNLPPVTYMHIYETDGFSLGVFLLKSGTSIPLHDHPGMHGM
LKVLYGTVRISCMDKLDAGGGQRPRALPPEQQFEPPLQPREREAVRPGVLRSRAEYTEAS
GPCILTPHRDNLHQIDAVEGPAAFLDILAPPYDPDDGRDCHYYRVLEPVRPKEASSSACD
LPREVWLLETPQADDFWCEGEPYPGPKVFP
|
| Enzyme 4 Number of Residues |
270 |
| Enzyme 4 Molecular Weight |
29751 |
| Enzyme 4 Theoretical pI |
Not Available |
| Enzyme 4 GO Classification |
Not Available |
| Enzyme 4 General Function |
Not Available |
| Enzyme 4 Specific Function |
Not Available |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
Not Available |
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
Not Available |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
B1AL29  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
B1AL29_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
Not Available |
| Enzyme 4 GenBank Gene ID |
Not Available |
| Enzyme 4 GeneCard ID |
B1AL29  |
| Enzyme 4 GenAtlas ID |
Not Available |
| Enzyme 4 HGNC ID |
Not Available |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
Not Available |
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
14386 |
| Enzyme 5 Name |
2-aminoethanethiol dioxygenase |
| Enzyme 5 Synonyms |
- Cysteamine dioxygenase
|
| Enzyme 5 Gene Name |
ADO |
| Enzyme 5 Protein Sequence |
>2-aminoethanethiol dioxygenase
MPRDNMASLIQRIARQACLTFRGSGGGRGASDRDAASGPEAPMQPGFPENLSKLKSLLTQ
LRAEDLNIAPRKATLQPLPPNLPPVTYMHIYETDGFSLGVFLLKSGTSIPLHDHPGMHGM
LKVLYGTVRISCMDKLDAGGGQRPRALPPEQQFEPPLQPREREAVRPGVLRSRAEYTEAS
GPCILTPHRDNLHQIDAVEGPAAFLDILAPPYDPDDGRDCHYYRVLEPVRPKEASSSACD
LPREVWLLETPQADDFWCEGEPYPGPKVFP
|
| Enzyme 5 Number of Residues |
270 |
| Enzyme 5 Molecular Weight |
29750.5 |
| Enzyme 5 Theoretical pI |
5.91 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- cysteamine dioxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
- oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in cysteamine dioxygenase activity |
| Enzyme 5 Specific Function |
2-aminoethanethiol + O(2) = hypotaurine |
| Enzyme 5 Pathways |
- Taurine and Hypotaurine Metabolism (map00430
)
|
| Enzyme 5 Reactions |
- 2-aminoethanethiol + O2 = hypotaurine [RN:R02467]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
62177110  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q96SZ5  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
AEDO_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>813 bp
ATGCCCCGAGACAACATGGCCTCCTTGATCCAACGGATCGCCCGCCAGGCTTGCCTCACC
TTCCGGGGCAGCGGGGGCGGCCGCGGCGCTTCCGATCGCGACGCGGCTTCTGGCCCGGAG
GCGCCGATGCAGCCGGGCTTCCCCGAGAACCTGAGCAAGCTGAAGAGCCTCCTGACCCAG
CTCCGCGCCGAGGACTTGAACATCGCCCCGCGCAAGGCCACACTGCAGCCGCTGCCGCCC
AACCTGCCGCCAGTCACCTACATGCACATCTACGAGACGGACGGCTTCAGCCTGGGCGTG
TTCCTGCTCAAGAGCGGCACGTCCATCCCGCTGCACGACCACCCGGGCATGCACGGCATG
CTCAAGGTGCTGTACGGCACCGTGCGCATCAGCTGCATGGACAAGCTAGACGCGGGCGGC
GGGCAACGGCCGCGGGCCTTGCCGCCCGAGCAGCAGTTCGAGCCGCCGCTGCAGCCCCGG
GAGCGAGAAGCCGTGCGGCCGGGCGTGCTGCGTTCGCGGGCCGAGTACACCGAGGCCAGC
GGCCCCTGCATCCTCACACCGCACCGGGACAACCTGCACCAGATCGACGCCGTGGAAGGG
CCTGCCGCCTTCCTGGACATCCTGGCCCCGCCCTACGACCCGGACGATGGCCGGGACTGC
CACTATTACCGGGTGCTGGAGCCGGTCAGGCCCAAGGAGGCCTCCAGCTCGGCCTGTGAC
CTGCCTCGAGAGGTGTGGCTCCTGGAGACCCCACAGGCCGATGACTTCTGGTGCGAGGGA
GAACCCTATCCAGGTCCCAAGGTCTTCCCTTGA
|
| Enzyme 5 GenBank Gene ID |
NM_032804.5  |
| Enzyme 5 GeneCard ID |
ADO  |
| Enzyme 5 GenAtlas ID |
ADO  |
| Enzyme 5 HGNC ID |
HGNC:23506  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
10q21.3 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Dominy JE Jr, Simmons CR, Hirschberger LL, Hwang J, Coloso RM, Stipanuk MH: Discovery and characterization of a second mammalian thiol dioxygenase, cysteamine dioxygenase. J Biol Chem. 2007 Aug 31;282(35):25189-98. Epub 2007 Jun 20. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |