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Showing Protein 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase (HMDBP00261)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 4 metabolites
Identification
HMDB Protein ID HMDBP00261
Secondary Accession Numbers
  • 5493
Name 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
Synonyms
  1. Picolinate carboxylase
Gene Name ACMSD
Protein Type Enzyme
Biological Properties
General Function Involved in catalytic activity
Specific Function Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal cells which is implicated in the pathogenesis of various neurodegenerative disorders. In the presence of ACMSD, ACMS is converted to AMS, a benign catabolite. ACMSD ultimately controls the metabolic fate of tryptophan catabolism along the kynurenine pathway.
Pathways
  • quinolate metabolism
  • Tryptophan metabolism
  • Tryptophan metabolism
Reactions
2-Amino-3-carboxymuconic acid semialdehyde → 2-Aminomuconic acid semialdehyde + CO(2) details
2-Amino-3-carboxymuconic acid semialdehyde → 2-Aminomuconic acid semialdehyde + Carbon dioxide details
GO Classification
Biological Process
tryptophan catabolic process
quinolinate metabolic process
Cellular Component
cytosol
Function
catalytic activity
Molecular Function
metal ion binding
aminocarboxymuconate-semialdehyde decarboxylase activity
Process
metabolic process
Cellular Location Not Available
Gene Properties
Chromosome Location 2
Locus 2q21.3
SNPs ACMSD
Gene Sequence 
>1011 bp
ATGAAAATTGACATCCATAGTCATATTCTACCAAAAGAATGGCCAGATCTAAAAAAGAGG
TTTGGCTACGGAGGCTGGGTGCAGCTCCAACACCACAGCAAGGGAGAAGCAAAGTTGTTG
AAAGATGGGAAAGTCTTCAGAGTGGTGCGAGAGAATTGCTGGGATCCAGAAGTTCGTATT
AGAGAAATGGACCAAAAAGGAGTAACAGTGCAAGCCCTTTCCACAGTTCCTGTCATGTTT
AGCTACTGGGCCAAACCTGAGGACACTTTAAACCTGTGCCAGCTTTTAAACAACGACCTT
GCCAGCACCGTTGTGAGCTACCCCAGGAGGTTCGTGGGTCTGGGGACGTTGCCCATGCAG
GCCCCTGAGCTGGCGGTCAAGGAGATGGAGCGCTGTGTGAAAGAGCTGGGCTTTCCCGGG
GTCCAAATTGGCACCCACGTCAACGAGTGGGACCTGAACGCGCAGGAGCTCTTTCCTGTC
TATGCGGCAGCCGAAAGGCTGAAGTGTTCCCTGTTCGTGCATCCCTGGGACATGCAGATG
GATGGACGAATGGCCAAATACTGGCTCCCTTGGCTTGTAGGAATGCCAGCAGAGACCACC
ATAGCCATTTGCTCCATGATCATGGGTGGAGTATTTGAGAAGTTTCCCAAACTGAAAGTG
TGTTTCGCACATGGTGGTGGTGCCTTCCCCTTCACAGTGGGAAGAATCTCCCATGGATTC
AGCATGCGCCCAGATCTGTGTGCCCAGGACAACCCCATGAACCCGAAGAAATACCTTGGT
TCCTTTTACACAGATGCTTTGGTTCATGATCCTCTGTCCCTCAAGCTGTTAACAGATGTC
ATAGGAAAGGATAAAGTCATTTTGGGAACCGATTACCCCTTTCCACTAGGTGAGCTGGAA
CCTGGGAAACTAATAGAGTCCATGGAAGAATTTGATGAAGAAACAAAGAATAAACTCAAA
GCCGGCAATGCCCTGGCATTTTTGGGTCTTGAGAGAAAACAATTTGAATGA
Protein Properties
Number of Residues 336
Molecular Weight 38035.045
Theoretical pI 6.985
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
MKIDIHSHILPKEWPDLKKRFGYGGWVQLQHHSKGEAKLLKDGKVFRVVRENCWDPEVRI
REMDQKGVTVQALSTVPVMFSYWAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQ
APELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMQM
DGRMAKYWLPWLVGMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGF
SMRPDLCAQDNPMNPKKYLGSFYTDALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGELE
PGKLIESMEEFDEETKNKLKAGNALAFLGLERKQFE
GenBank ID Protein 19911227
UniProtKB/Swiss-Prot ID Q8TDX5
UniProtKB/Swiss-Prot Entry Name ACMSD_HUMAN
PDB IDs
GenBank Gene ID AB071418
GeneCard ID ACMSD
GenAtlas ID ACMSD
HGNC ID HGNC:19288
References
General References
  1. 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:15489334 ]
  2. Fukuoka S, Ishiguro K, Yanagihara K, Tanabe A, Egashira Y, Sanada H, Shibata K: Identification and expression of a cDNA encoding human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD). A key enzyme for the tryptophan-niacine pathway and "quinolinate hypothesis". J Biol Chem. 2002 Sep 20;277(38):35162-7. Epub 2002 Jul 24. [PubMed:12140278 ]
  3. Garavaglia S, Perozzi S, Galeazzi L, Raffaelli N, Rizzi M: The crystal structure of human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase in complex with 1,3-dihydroxyacetonephosphate suggests a regulatory link between NAD synthesis and glycolysis. FEBS J. 2009 Nov;276(22):6615-23. doi: 10.1111/j.1742-4658.2009.07372.x. Epub 2009 Oct 16. [PubMed:19843166 ]