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Reviewed, UniProtKB/Swiss-Prot Q8R5M5 (ACMSD_RAT)

Last modified October 13, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    2-amino-3-carboxymuconate-6-semialdehyde decarboxylase
    EC=4.1.1.45
Gene names
Name: Acmsd
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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, 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. Ref.1

Catalytic activity

2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate = 2-aminomuconate semialdehyde + CO2.

Pathway

Secondary metabolite metabolism; quinolate metabolism.

Tissue specificity

Liver and kidney. Very low levels detected in brain. Ref.1 Ref.2

Sequence similarities

Belongs to the ACMSD family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3363362-amino-3-carboxymuconate-6-semialdehyde decarboxylase
PRO_0000190982

Amino acid modifications

Modified residue71Phosphothreonine By similarity
Modified residue1161Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8R5M5-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 4030A54E93DDD04B

FASTA33638,091
        10         20         30         40         50         60 
MKIDIHTHIL PKEWPDLEKR FGYGGWVQLQ QQGKGEAKMM KDGKVFRVIQ QNCWDPEVRI 

        70         80         90        100        110        120 
REMNQKGVTV QALSTVPVMF SYWAKPKDTL ELCQFLNNDL AATVARYPRR FVGLGTLPMQ 

       130        140        150        160        170        180 
APGLAVEEME RCVKELGFPG IQIGSHINMW DLNDPELFPI YTAAERLNCS LFVHPWDMQM 

       190        200        210        220        230        240 
DGRMAKYWLP WLVGMPSETT TAICSMIMGG VFEKFPKLKV CFAHGGGAFP FTIGRIAHGF 

       250        260        270        280        290        300 
NMRPDLCARD NSSDPRKYLG SFYTDSLVHD PLSLKLLTDV IGKDRVILGT DYPFPLGEQE 

       310        320        330 
PGKLIESMAD FDEETKDKLT AGNALTFLGL ERKLFE 

« Hide

References

[1]"Purification and molecular cloning of rat 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase."
Tanabe A., Egashira Y., Fukuoka S., Shibata K., Sanada H.
Biochem. J. 361:567-575(2002) [PubMed: 11802786] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-20 AND 136-152, TISSUE SPECIFICITY.
Strain: Wistar.
Tissue: Liver.
[2]"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: TISSUE SPECIFICITY.

Cross-references

Sequence databases

AB069781 mRNA. Translation: BAB84692.1.
IPIIPI00201953.
RefSeqNP_599199.1.
UniGeneRn.162389

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ8R5M5.

Genome annotation databases

EnsemblENSRNOT00000005206; ENSRNOP00000005206; ENSRNOG00000003884; Rattus norvegicus. [Genome view]
GeneID171385.
KEGGrno:171385.
NMPDRfig|10116.3.peg.9005.

Organism-specific databases

CTD171385.
RGD620868. Acmsd.

Phylogenomic databases

HOVERGENQ8R5M5.

Enzyme and pathway databases

BRENDA4.1.1.45. 248.

Gene expression databases

ArrayExpressQ8R5M5.
GenevestigatorQ8R5M5.
GermOnlineENSRNOG00000003884. Rattus norvegicus.

Family and domain databases

InterProIPR006992. Amidohydro_2.
[Graphical view]
PfamPF04909. Amidohydro_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio622218.

Entry information

Entry nameACMSD_RAT
AccessionPrimary (citable) accession number: Q8R5M5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: June 1, 2002
Last modified: October 13, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents