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Protein

2-amino-3-carboxymuconate-6-semialdehyde decarboxylase

Gene

Acmsd

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

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

Pathwayi: quinolate metabolism

This protein is involved in the pathway quinolate metabolism, which is part of Secondary metabolite metabolism.
View all proteins of this organism that are known to be involved in the pathway quinolate metabolism and in Secondary metabolite metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi6 – 61ZincBy similarity
Metal bindingi8 – 81ZincBy similarity
Binding sitei47 – 471SubstrateBy similarity
Metal bindingi174 – 1741ZincBy similarity
Metal bindingi291 – 2911ZincBy similarity

GO - Molecular functioni

GO - Biological processi

  • nicotinamide metabolic process Source: RGD
  • quinolinate metabolic process Source: UniProtKB
  • regulation of quinolinate biosynthetic process Source: InterPro
  • tryptophan catabolic process Source: Reactome
  • tryptophan metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.1.1.45. 5301.
ReactomeiR-RNO-71240. Tryptophan catabolism.
UniPathwayiUPA00270.

Names & Taxonomyi

Protein namesi
Recommended name:
2-amino-3-carboxymuconate-6-semialdehyde decarboxylase (EC:4.1.1.45)
Alternative name(s):
Picolinate carboxylase
Gene namesi
Name:Acmsd
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620868. Acmsd.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3363362-amino-3-carboxymuconate-6-semialdehyde decarboxylasePRO_0000190982Add
BLAST

Proteomic databases

PaxDbiQ8R5M5.
PRIDEiQ8R5M5.

PTM databases

iPTMnetiQ8R5M5.
PhosphoSiteiQ8R5M5.

Expressioni

Tissue specificityi

Liver and kidney. Very low levels detected in brain.2 Publications

Gene expression databases

BgeeiENSRNOG00000003884.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005206.

Structurei

3D structure databases

ProteinModelPortaliQ8R5M5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ACMSD family.Curated

Phylogenomic databases

eggNOGiKOG4245. Eukaryota.
COG2159. LUCA.
HOGENOMiHOG000254105.
HOVERGENiHBG050450.
InParanoidiQ8R5M5.
KOiK03392.
PhylomeDBiQ8R5M5.

Family and domain databases

InterProiIPR032465. ACMSD.
IPR006680. Amidohydro-rel.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR21240:SF3. PTHR21240:SF3. 1 hit.
PfamiPF04909. Amidohydro_2. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8R5M5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIDIHTHIL PKEWPDLEKR FGYGGWVQLQ QQGKGEAKMM KDGKVFRVIQ
60 70 80 90 100
QNCWDPEVRI REMNQKGVTV QALSTVPVMF SYWAKPKDTL ELCQFLNNDL
110 120 130 140 150
AATVARYPRR FVGLGTLPMQ APGLAVEEME RCVKELGFPG IQIGSHINMW
160 170 180 190 200
DLNDPELFPI YTAAERLNCS LFVHPWDMQM DGRMAKYWLP WLVGMPSETT
210 220 230 240 250
TAICSMIMGG VFEKFPKLKV CFAHGGGAFP FTIGRIAHGF NMRPDLCARD
260 270 280 290 300
NSSDPRKYLG SFYTDSLVHD PLSLKLLTDV IGKDRVILGT DYPFPLGEQE
310 320 330
PGKLIESMAD FDEETKDKLT AGNALTFLGL ERKLFE
Length:336
Mass (Da):38,091
Last modified:June 1, 2002 - v1
Checksum:i4030A54E93DDD04B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB069781 mRNA. Translation: BAB84692.1.
RefSeqiNP_599199.1. NM_134372.1.
UniGeneiRn.162389.

Genome annotation databases

GeneIDi171385.
KEGGirno:171385.
UCSCiRGD:620868. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB069781 mRNA. Translation: BAB84692.1.
RefSeqiNP_599199.1. NM_134372.1.
UniGeneiRn.162389.

3D structure databases

ProteinModelPortaliQ8R5M5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005206.

PTM databases

iPTMnetiQ8R5M5.
PhosphoSiteiQ8R5M5.

Proteomic databases

PaxDbiQ8R5M5.
PRIDEiQ8R5M5.

Protocols and materials databases

DNASUi171385.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi171385.
KEGGirno:171385.
UCSCiRGD:620868. rat.

Organism-specific databases

CTDi130013.
RGDi620868. Acmsd.

Phylogenomic databases

eggNOGiKOG4245. Eukaryota.
COG2159. LUCA.
HOGENOMiHOG000254105.
HOVERGENiHBG050450.
InParanoidiQ8R5M5.
KOiK03392.
PhylomeDBiQ8R5M5.

Enzyme and pathway databases

UniPathwayiUPA00270.
BRENDAi4.1.1.45. 5301.
ReactomeiR-RNO-71240. Tryptophan catabolism.

Miscellaneous databases

PROiQ8R5M5.

Gene expression databases

BgeeiENSRNOG00000003884.

Family and domain databases

InterProiIPR032465. ACMSD.
IPR006680. Amidohydro-rel.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR21240:SF3. PTHR21240:SF3. 1 hit.
PfamiPF04909. Amidohydro_2. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiACMSD_RAT
AccessioniPrimary (citable) accession number: Q8R5M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: June 1, 2002
Last modified: September 7, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.