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Protein

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

Gene

Acmsd

Organism
Mus musculus (Mouse)
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

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.1.1.45. 3474.
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
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2386323. 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_0000190980Add
BLAST

Proteomic databases

MaxQBiQ8R519.
PaxDbiQ8R519.
PRIDEiQ8R519.

PTM databases

iPTMnetiQ8R519.
PhosphoSiteiQ8R519.

Expressioni

Tissue specificityi

Highest expression in kidney with lower levels in liver and brain.1 Publication

Inductioni

By streptozocin-induced diabetes. Repressed by low protein diet.1 Publication

Gene expression databases

BgeeiENSMUSG00000026348.
CleanExiMM_ACMSD.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

IntActiQ8R519. 1 interaction.
MINTiMINT-4086727.
STRINGi10090.ENSMUSP00000048482.

Structurei

3D structure databases

ProteinModelPortaliQ8R519.
SMRiQ8R519. Positions 1-335.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ACMSD family.Curated

Phylogenomic databases

eggNOGiKOG4245. Eukaryota.
COG2159. LUCA.
GeneTreeiENSGT00490000043417.
HOGENOMiHOG000254105.
HOVERGENiHBG050450.
InParanoidiQ8R519.
KOiK03392.
OMAiHPWDMQT.
OrthoDBiEOG091G0BZB.
PhylomeDBiQ8R519.
TreeFamiTF313232.

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.

Q8R519-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIDIHTHIL PKEWPDLEKR FGYGGWVQLQ QQGKGEAKMI KDGKLFRVIQ
60 70 80 90 100
QNCWDPEVRI REMNQKGVTV QALSTVPVMF SYWAKPKDTL ELCQFLNNDL
110 120 130 140 150
AATVARYPRR FVGLGTLPMQ APELAVEEME RCVKALGFPG IQIGSHINTW
160 170 180 190 200
DLNDPELFPI YAAAERLNCS LFVHPWDMQM DGRMAKYWLP WLVGMPSETT
210 220 230 240 250
MAICSMIMGG VFEKFPKLKV CFAHGGGAFP FTIGRIAHGF NMRPDLCAQD
260 270 280 290 300
NPSDPRKYLG SFYTDSLVHD PLSLKLLTDV IGKDKVMLGT DYPFPLGEQE
310 320 330
PGKLIESMAE FDEETKDKLT AGNALAFLGL ERKLFE
Length:336
Mass (Da):38,027
Last modified:January 9, 2007 - v2
Checksum:iB01104827D161A9A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK143962 mRNA. Translation: BAE25634.1.
BC139281 mRNA. Translation: AAI39282.1.
AB071419 mRNA. Translation: BAB86939.1.
CCDSiCCDS15247.1.
RefSeqiNP_001028213.1. NM_001033041.2.
UniGeneiMm.25735.

Genome annotation databases

EnsembliENSMUST00000038006; ENSMUSP00000048482; ENSMUSG00000026348.
GeneIDi266645.
KEGGimmu:266645.
UCSCiuc007ckv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK143962 mRNA. Translation: BAE25634.1.
BC139281 mRNA. Translation: AAI39282.1.
AB071419 mRNA. Translation: BAB86939.1.
CCDSiCCDS15247.1.
RefSeqiNP_001028213.1. NM_001033041.2.
UniGeneiMm.25735.

3D structure databases

ProteinModelPortaliQ8R519.
SMRiQ8R519. Positions 1-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R519. 1 interaction.
MINTiMINT-4086727.
STRINGi10090.ENSMUSP00000048482.

PTM databases

iPTMnetiQ8R519.
PhosphoSiteiQ8R519.

Proteomic databases

MaxQBiQ8R519.
PaxDbiQ8R519.
PRIDEiQ8R519.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038006; ENSMUSP00000048482; ENSMUSG00000026348.
GeneIDi266645.
KEGGimmu:266645.
UCSCiuc007ckv.1. mouse.

Organism-specific databases

CTDi130013.
MGIiMGI:2386323. Acmsd.

Phylogenomic databases

eggNOGiKOG4245. Eukaryota.
COG2159. LUCA.
GeneTreeiENSGT00490000043417.
HOGENOMiHOG000254105.
HOVERGENiHBG050450.
InParanoidiQ8R519.
KOiK03392.
OMAiHPWDMQT.
OrthoDBiEOG091G0BZB.
PhylomeDBiQ8R519.
TreeFamiTF313232.

Enzyme and pathway databases

UniPathwayiUPA00270.
BRENDAi4.1.1.45. 3474.

Miscellaneous databases

ChiTaRSiAcmsd. mouse.
PROiQ8R519.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026348.
CleanExiMM_ACMSD.

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_MOUSE
AccessioniPrimary (citable) accession number: Q8R519
Secondary accession number(s): B9EI97, Q3UNW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: January 9, 2007
Last modified: September 7, 2016
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.