P83662 (ACMSD_PIG) Reviewed, UniProtKB/Swiss-Prot
Last modified
July 27, 2011.
Version 30.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase EC=4.1.1.45 Alternative name(s): Picolinate carboxylase | ||
| Gene names |
| ||
| Organism | Sus scrofa (Pig) [Complete proteome] | ||
| Taxonomic identifier | 9823 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 138 AA. |
| Sequence status | Fragments. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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. Ref.1 UniProtKB Q8TDX5 |
| Catalytic activity | 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate = 2-aminomuconate semialdehyde + CO2. |
| Pathway | |
| Subunit structure | Monomer By similarity. |
| Sequence similarities | Belongs to the ACMSD family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding Zinc |
| Molecular function | Decarboxylase Lyase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | quinolinate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | cytosol Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | aminocarboxymuconate-semialdehyde decarboxylase activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›138 | ›138 | 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase | PRO_0000190981 | |||||
Sites | |||||||||
| Metal binding | 6 | 1 | Zinc By similarity | ||||||
| Metal binding | 8 | 1 | Zinc By similarity | ||||||
| Metal binding | 70 | 1 | Zinc By similarity | ||||||
| Metal binding | 126 | 1 | Zinc By similarity | ||||||
| Binding site | 47 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 58 | 1 | Phosphothreonine By similarity | ||||||
Experimental info | |||||||||
| Sequence uncertainty | 23 | 1 | Y or G Ref.1 | ||||||
| Sequence uncertainty | 43 | 1 | G or D Ref.1 | ||||||
| Sequence uncertainty | 48 | 1 | V or R Ref.1 | ||||||
| Non-adjacent residues | 51 – 52 | 2 | |||||||
| Non-adjacent residues | 64 – 65 | 2 | |||||||
| Non-adjacent residues | 75 – 76 | 2 | |||||||
| Non-adjacent residues | 103 – 104 | 2 | |||||||
| Non-adjacent residues | 120 – 121 | 2 | |||||||
| Non-terminal residue | 138 | 1 | |||||||
Sequences
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References
| [1] | "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'." Fukuoka S., Ishiguro K., Yanagihara K., Tanabe A., Egashira Y., Sanada H., Shibata K. J. Biol. Chem. 277:35162-35167(2002) [PubMed: 12140278] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Brain. |
Cross-references
Entry information
| Entry name | ACMSD_PIG | ||||||||
| Accession | Primary (citable) accession number: P83662 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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