ID   ACMSD_PIG               Reviewed;         138 AA.
AC   P83662;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2003, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=2-amino-3-carboxymuconate-6-semialdehyde decarboxylase;
DE            EC=4.1.1.45;
DE   AltName: Full=Picolinate carboxylase;
DE   Flags: Fragments;
GN   Name=ACMSD;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Brain {ECO:0000269|PubMed:12140278};
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).
CC   -!- FUNCTION: Converts alpha-amino-beta-carboxymuconate-epsilon-
CC       semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can
CC       be converted non-enzymatically to quinolate (QA), a key precursor of
CC       NAD, and a potent endogenous excitotoxin of neuronal cells which is
CC       implicated in the pathogenesis of various neurodegenerative disorders.
CC       In the presence of ACMSD, ACMS is converted to AMS, a benign
CC       catabolite. ACMSD ultimately controls the metabolic fate of tryptophan
CC       catabolism along the kynurenine pathway.
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   -!- PATHWAY: Secondary metabolite metabolism; quinolate metabolism.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       ACMSD family. {ECO:0000305}.
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DR   InParanoid; P83662; -.
DR   UniPathway; UPA00270; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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: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; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR21240; PTHR21240; 3.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   1: Evidence at protein level;
KW   Decarboxylase; Direct protein sequencing; Lyase; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..>138
FT                   /note="2-amino-3-carboxymuconate-6-semialdehyde
FT                   decarboxylase"
FT                   /id="PRO_0000190981"
FT   BINDING         6
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   UNSURE          23
FT                   /note="Y or G"
FT   UNSURE          43
FT                   /note="G or D"
FT   UNSURE          48
FT                   /note="V or R"
FT   NON_CONS        51..52
FT                   /evidence="ECO:0000305"
FT   NON_CONS        64..65
FT                   /evidence="ECO:0000305"
FT   NON_CONS        75..76
FT                   /evidence="ECO:0000305"
FT   NON_CONS        103..104
FT                   /evidence="ECO:0000305"
FT   NON_CONS        120..121
FT                   /evidence="ECO:0000305"
FT   NON_TER         138
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   138 AA;  15679 MW;  C2A558B31AB57120 CRC64;
     MKIDIHSHIL PKEWPDLKKR FGYXGWVELQ HHSEGEAKML KDGKVFRVVQ ERFVGLGTLP
     MQAPXSLFVH PWDMQYWFPW LIGMPAETTT AXESMMMGGV FEKVXFAHGG GSFPFTVGRI
     VILGTDYPFP LGELEPGK