ACMSD_CAEEL
ID ACMSD_CAEEL Reviewed; 401 AA.
AC Q8T8B9;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=2-amino-3-carboxymuconate-6-semialdehyde decarboxylase {ECO:0000250|UniProtKB:Q8TDX5};
DE EC=4.1.1.45 {ECO:0000250|UniProtKB:Q8TDX5};
DE AltName: Full=Picolinate carboxylase {ECO:0000250|UniProtKB:Q8TDX5};
GN Name=acsd-1 {ECO:0000312|WormBase:Y71D11A.3b};
GN Synonyms=acmsd {ECO:0000312|WormBase:Y71D11A.3b};
GN ORFNames=Y71D11A.3 {ECO:0000312|WormBase:Y71D11A.3b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:BAB86940.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12140278; DOI=10.1074/jbc.m200819200;
RA Fukuoka S., Ishiguro K., Yanagihara K., Tanabe A., Egashira Y., Sanada H.,
RA Shibata K.;
RT "Identification and expression of a cDNA encoding human alpha-amino-beta-
RT carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD). A key enzyme
RT for the tryptophan-niacine pathway and 'quinolinate hypothesis'.";
RL J. Biol. Chem. 277:35162-35167(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Converts alpha-amino-beta-carboxymuconate-epsilon-
CC semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS).
CC {ECO:0000250|UniProtKB:Q8TDX5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-amino-3-carboxymuconate 6-semialdehyde + H(+) = 2-
CC aminomuconate 6-semialdehyde + CO2; Xref=Rhea:RHEA:16557,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:77634,
CC ChEBI:CHEBI:77803; EC=4.1.1.45;
CC Evidence={ECO:0000250|UniProtKB:Q8TDX5};
CC -!- PATHWAY: Secondary metabolite metabolism; quinolate metabolism.
CC {ECO:0000250|UniProtKB:Q8TDX5}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8TDX5}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ACMSD family. {ECO:0000305}.
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DR EMBL; AB071420; BAB86940.1; -; mRNA.
DR EMBL; FO081503; CCD72053.1; -; Genomic_DNA.
DR RefSeq; NP_001022935.1; NM_001027764.1.
DR AlphaFoldDB; Q8T8B9; -.
DR SMR; Q8T8B9; -.
DR STRING; 6239.Y71D11A.3b; -.
DR EPD; Q8T8B9; -.
DR PaxDb; Q8T8B9; -.
DR PeptideAtlas; Q8T8B9; -.
DR EnsemblMetazoa; Y71D11A.3b.1; Y71D11A.3b.1; WBGene00022104.
DR GeneID; 175280; -.
DR KEGG; cel:CELE_Y71D11A.3; -.
DR UCSC; Y71D11A.3a; c. elegans.
DR CTD; 175280; -.
DR WormBase; Y71D11A.3b; CE32030; WBGene00022104; acsd-1.
DR eggNOG; KOG4245; Eukaryota.
DR InParanoid; Q8T8B9; -.
DR OMA; TTNYKAI; -.
DR OrthoDB; 941496at2759; -.
DR PhylomeDB; Q8T8B9; -.
DR UniPathway; UPA00270; -.
DR PRO; PR:Q8T8B9; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00022104; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; Q8T8B9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0001760; F:aminocarboxymuconate-semialdehyde decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1904985; P:negative regulation of quinolinate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019748; P:secondary metabolic process; IBA:GO_Central.
DR InterPro; IPR032465; ACMSD.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR21240; PTHR21240; 1.
DR Pfam; PF04909; Amidohydro_2; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 2: Evidence at transcript level;
KW Decarboxylase; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..401
FT /note="2-amino-3-carboxymuconate-6-semialdehyde
FT decarboxylase"
FT /id="PRO_0000190983"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
SQ SEQUENCE 401 AA; 45746 MW; 0F74E2BD2FD71D87 CRC64;
MPICEFSATS KSRKIDVHAH VLPKNIPDFQ EKFGYPGFVR LDHKEDGTTH MVKDGKLFRV
VEPNCFDTET RIADMNRANV NVQCLSTVPV MFSYWAKPAD TEIVARFVND DLLAECQKFP
DRLVPLGTLP MNDVQRAVEI FGKRIFFFEI WSPAKKSPEE VKRCVSMGIK GFEVGSHVAE
KSLDHRDFWP LYKLTESFKL STIMPGFCEF FENWGLTTKT PGICEELSVV LFVHPWDMHM
WDGRLDKYWM PWLVGMPSET AQAICSVLMG NILVLFPKLK LCFAHGGGAY PQIRGRVSHG
WNVRPDLCAG KCKVAPNKLD GLLWTDSLVH DPKALELLIN TVGKEHIVLG TDYPFPLGEL
EVGRVVEEYK PFSAKDREDL LWKNAVKMLD IDENLLFNKD F
