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P83662 (ACMSD_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
2-amino-3-carboxymuconate-6-semialdehyde decarboxylase

EC=4.1.1.45
Alternative name(s):
Picolinate carboxylase
Gene names
Name:ACMSD
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length138 AA.
Sequence statusFragments.
Protein existenceEvidence 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

Secondary metabolite metabolism; quinolate metabolism.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the ACMSD family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›138›1382-amino-3-carboxymuconate-6-semialdehyde decarboxylase
PRO_0000190981

Sites

Metal binding61Zinc By similarity
Metal binding81Zinc By similarity
Metal binding701Zinc By similarity
Metal binding1261Zinc By similarity
Binding site471Substrate By similarity

Amino acid modifications

Modified residue581Phosphothreonine By similarity

Experimental info

Sequence uncertainty231Y or G Ref.1
Sequence uncertainty431G or D Ref.1
Sequence uncertainty481V or R Ref.1
Non-adjacent residues51 – 522
Non-adjacent residues64 – 652
Non-adjacent residues75 – 762
Non-adjacent residues103 – 1042
Non-adjacent residues120 – 1212
Non-terminal residue1381

Sequences

Sequence LengthMass (Da)Tools
P83662 [UniParc].

Last modified November 7, 2003. Version 1.
Checksum: C2A558B31AB57120

FASTA13815,679
        10         20         30         40         50         60 
MKIDIHSHIL PKEWPDLKKR FGYXGWVELQ HHSEGEAKML KDGKVFRVVQ ERFVGLGTLP 

        70         80         90        100        110        120 
MQAPXSLFVH PWDMQYWFPW LIGMPAETTT AXESMMMGGV FEKVXFAHGG GSFPFTVGRI 

       130 
VILGTDYPFP LGELEPGK 

« Hide

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

3D structure databases

ProteinModelPortalP83662.
ModBaseSearch...

Protein-protein interaction databases

STRINGP83662.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameACMSD_PIG
AccessionPrimary (citable) accession number: P83662
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 7, 2003
Last modified: July 27, 2011
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families