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Protein

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

Gene

ACMSD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

Catalytic activityi

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

Pathwayi: quinolate metabolism

This protein is involved in the pathway quinolate metabolism, which is part of Secondary metabolite metabolism.1 Publication
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)DescriptionActionsGraphical viewLength
Metal bindingi6Zinc1 Publication1
Metal bindingi8Zinc1 Publication1
Binding sitei47Substrate1 Publication1
Metal bindingi174Zinc1 Publication1
Metal bindingi291Zinc1 Publication1

GO - Molecular functioni

  • aminocarboxymuconate-semialdehyde decarboxylase activity Source: ParkinsonsUK-UCL
  • hydrolase activity Source: InterPro
  • zinc ion binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • picolinic acid biosynthetic process Source: ParkinsonsUK-UCL
  • protein oligomerization Source: ParkinsonsUK-UCL
  • quinolinate metabolic process Source: UniProtKB
  • regulation of 'de novo' NAD biosynthetic process from tryptophan Source: ParkinsonsUK-UCL
  • regulation of quinolinate biosynthetic process Source: InterPro
  • tryptophan catabolic process Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS14455-MONOMER.
ZFISH:HS14455-MONOMER.
BRENDAi4.1.1.45. 2681.
ReactomeiR-HSA-71240. Tryptophan catabolism.
UniPathwayiUPA00270.

Names & Taxonomyi

Protein namesi
Recommended name:
2-amino-3-carboxymuconate-6-semialdehyde decarboxylase1 Publication (EC:4.1.1.451 Publication)
Alternative name(s):
Picolinate carboxylase1 Publication
Gene namesi
Name:ACMSD
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:19288. ACMSD.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi130013.
OpenTargetsiENSG00000153086.
PharmGKBiPA134973312.

Polymorphism and mutation databases

BioMutaiACMSD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001909791 – 3362-amino-3-carboxymuconate-6-semialdehyde decarboxylaseAdd BLAST336

Proteomic databases

PaxDbiQ8TDX5.
PeptideAtlasiQ8TDX5.
PRIDEiQ8TDX5.

PTM databases

iPTMnetiQ8TDX5.
PhosphoSitePlusiQ8TDX5.

Expressioni

Gene expression databases

BgeeiENSG00000153086.
CleanExiHS_ACMSD.
ExpressionAtlasiQ8TDX5. baseline and differential.
GenevisibleiQ8TDX5. HS.

Organism-specific databases

HPAiHPA010533.
HPA011179.

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MAGEA11P43364-23EBI-749859,EBI-10178634

Protein-protein interaction databases

BioGridi126217. 2 interactors.
IntActiQ8TDX5. 2 interactors.
MINTiMINT-1479806.
STRINGi9606.ENSP00000348459.

Structurei

Secondary structure

1336
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Helixi17 – 21Combined sources5
Beta strandi27 – 33Combined sources7
Beta strandi36 – 41Combined sources6
Beta strandi44 – 50Combined sources7
Helixi51 – 53Combined sources3
Helixi56 – 66Combined sources11
Beta strandi70 – 74Combined sources5
Helixi77 – 80Combined sources4
Helixi86 – 106Combined sources21
Turni108 – 110Combined sources3
Beta strandi111 – 115Combined sources5
Helixi122 – 134Combined sources13
Beta strandi139 – 147Combined sources9
Helixi155 – 157Combined sources3
Helixi158 – 167Combined sources10
Beta strandi170 – 174Combined sources5
Helixi182 – 185Combined sources4
Helixi189 – 192Combined sources4
Helixi194 – 207Combined sources14
Turni208 – 210Combined sources3
Helixi211 – 214Combined sources4
Beta strandi220 – 223Combined sources4
Helixi224 – 226Combined sources3
Helixi229 – 242Combined sources14
Helixi244 – 247Combined sources4
Beta strandi248 – 250Combined sources3
Helixi255 – 258Combined sources4
Beta strandi261 – 265Combined sources5
Helixi271 – 281Combined sources11
Beta strandi285 – 287Combined sources3
Helixi303 – 307Combined sources5
Helixi313 – 320Combined sources8
Helixi322 – 328Combined sources7
Helixi332 – 334Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WM1X-ray2.01A1-336[»]
4IGMX-ray2.39A/B/C/D/E/F1-332[»]
4IGNX-ray2.33A/B/C/D/E/F1-332[»]
4IH3X-ray2.49A/B/C/D/E/F1-332[»]
4OFCX-ray1.99A/B/C/D/E/F1-335[»]
ProteinModelPortaliQ8TDX5.
SMRiQ8TDX5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TDX5.

Family & Domainsi

Sequence similaritiesi

Belongs to the ACMSD family.Curated

Phylogenomic databases

eggNOGiKOG4245. Eukaryota.
COG2159. LUCA.
GeneTreeiENSGT00490000043417.
HOGENOMiHOG000254105.
HOVERGENiHBG050450.
InParanoidiQ8TDX5.
KOiK03392.
OMAiHPWDMQT.
OrthoDBiEOG091G0BZB.
PhylomeDBiQ8TDX5.
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.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q8TDX5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKIDIHSHIL PKEWPDLKKR FGYGGWVQLQ HHSKGEAKLL KDGKVFRVVR
60 70 80 90 100
ENCWDPEVRI REMDQKGVTV QALSTVPVMF SYWAKPEDTL NLCQLLNNDL
110 120 130 140 150
ASTVVSYPRR FVGLGTLPMQ APELAVKEME RCVKELGFPG VQIGTHVNEW
160 170 180 190 200
DLNAQELFPV YAAAERLKCS LFVHPWDMQM DGRMAKYWLP WLVGMPAETT
210 220 230 240 250
IAICSMIMGG VFEKFPKLKV CFAHGGGAFP FTVGRISHGF SMRPDLCAQD
260 270 280 290 300
NPMNPKKYLG SFYTDALVHD PLSLKLLTDV IGKDKVILGT DYPFPLGELE
310 320 330
PGKLIESMEE FDEETKNKLK AGNALAFLGL ERKQFE
Length:336
Mass (Da):38,035
Last modified:June 1, 2002 - v1
Checksum:i892B01D2A77C35A5
GO
Isoform 2Curated (identifier: Q8TDX5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.
     59-83: RIREMDQKGVTVQALSTVPVMFSYW → MGKSSEWCERIAGIQKFVLEKWTKK

Note: No experimental confirmation available.Curated
Show »
Length:278
Mass (Da):31,213
Checksum:i4F7B961D6B0C9185
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0506221 – 58Missing in isoform 2. 1 PublicationAdd BLAST58
Alternative sequenceiVSP_05062359 – 83RIREM…MFSYW → MGKSSEWCERIAGIQKFVLE KWTKK in isoform 2. 1 PublicationAdd BLAST25

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB071418 mRNA. Translation: BAB86938.1.
AC016725 Genomic DNA. Translation: AAY14997.1.
CH471058 Genomic DNA. Translation: EAX11650.1.
CH471058 Genomic DNA. Translation: EAX11651.1.
CH471058 Genomic DNA. Translation: EAX11652.1.
BC016018 mRNA. Translation: AAH16018.1.
BC107420 mRNA. Translation: AAI07421.1.
CCDSiCCDS2173.2. [Q8TDX5-1]
CCDS77464.1. [Q8TDX5-2]
RefSeqiNP_001294912.1. NM_001307983.1. [Q8TDX5-2]
NP_612199.2. NM_138326.2. [Q8TDX5-1]
XP_005263645.1. XM_005263588.4. [Q8TDX5-2]
XP_011508894.1. XM_011510592.2. [Q8TDX5-2]
XP_016858814.1. XM_017003325.1. [Q8TDX5-2]
XP_016858815.1. XM_017003326.1. [Q8TDX5-2]
UniGeneiHs.655728.

Genome annotation databases

EnsembliENST00000356140; ENSP00000348459; ENSG00000153086. [Q8TDX5-1]
ENST00000392928; ENSP00000376659; ENSG00000153086. [Q8TDX5-2]
GeneIDi130013.
KEGGihsa:130013.
UCSCiuc002ttz.4. human. [Q8TDX5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB071418 mRNA. Translation: BAB86938.1.
AC016725 Genomic DNA. Translation: AAY14997.1.
CH471058 Genomic DNA. Translation: EAX11650.1.
CH471058 Genomic DNA. Translation: EAX11651.1.
CH471058 Genomic DNA. Translation: EAX11652.1.
BC016018 mRNA. Translation: AAH16018.1.
BC107420 mRNA. Translation: AAI07421.1.
CCDSiCCDS2173.2. [Q8TDX5-1]
CCDS77464.1. [Q8TDX5-2]
RefSeqiNP_001294912.1. NM_001307983.1. [Q8TDX5-2]
NP_612199.2. NM_138326.2. [Q8TDX5-1]
XP_005263645.1. XM_005263588.4. [Q8TDX5-2]
XP_011508894.1. XM_011510592.2. [Q8TDX5-2]
XP_016858814.1. XM_017003325.1. [Q8TDX5-2]
XP_016858815.1. XM_017003326.1. [Q8TDX5-2]
UniGeneiHs.655728.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WM1X-ray2.01A1-336[»]
4IGMX-ray2.39A/B/C/D/E/F1-332[»]
4IGNX-ray2.33A/B/C/D/E/F1-332[»]
4IH3X-ray2.49A/B/C/D/E/F1-332[»]
4OFCX-ray1.99A/B/C/D/E/F1-335[»]
ProteinModelPortaliQ8TDX5.
SMRiQ8TDX5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126217. 2 interactors.
IntActiQ8TDX5. 2 interactors.
MINTiMINT-1479806.
STRINGi9606.ENSP00000348459.

PTM databases

iPTMnetiQ8TDX5.
PhosphoSitePlusiQ8TDX5.

Polymorphism and mutation databases

BioMutaiACMSD.

Proteomic databases

PaxDbiQ8TDX5.
PeptideAtlasiQ8TDX5.
PRIDEiQ8TDX5.

Protocols and materials databases

DNASUi130013.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356140; ENSP00000348459; ENSG00000153086. [Q8TDX5-1]
ENST00000392928; ENSP00000376659; ENSG00000153086. [Q8TDX5-2]
GeneIDi130013.
KEGGihsa:130013.
UCSCiuc002ttz.4. human. [Q8TDX5-1]

Organism-specific databases

CTDi130013.
DisGeNETi130013.
GeneCardsiACMSD.
H-InvDBHIX0019780.
HGNCiHGNC:19288. ACMSD.
HPAiHPA010533.
HPA011179.
MIMi608889. gene.
neXtProtiNX_Q8TDX5.
OpenTargetsiENSG00000153086.
PharmGKBiPA134973312.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4245. Eukaryota.
COG2159. LUCA.
GeneTreeiENSGT00490000043417.
HOGENOMiHOG000254105.
HOVERGENiHBG050450.
InParanoidiQ8TDX5.
KOiK03392.
OMAiHPWDMQT.
OrthoDBiEOG091G0BZB.
PhylomeDBiQ8TDX5.
TreeFamiTF313232.

Enzyme and pathway databases

UniPathwayiUPA00270.
BioCyciMetaCyc:HS14455-MONOMER.
ZFISH:HS14455-MONOMER.
BRENDAi4.1.1.45. 2681.
ReactomeiR-HSA-71240. Tryptophan catabolism.

Miscellaneous databases

EvolutionaryTraceiQ8TDX5.
GenomeRNAii130013.
PROiQ8TDX5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000153086.
CleanExiHS_ACMSD.
ExpressionAtlasiQ8TDX5. baseline and differential.
GenevisibleiQ8TDX5. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q8TDX5
Secondary accession number(s): Q3B7X3, Q53SR5, Q96KY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: June 1, 2002
Last modified: November 30, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.