ID   ACMSD_BOVIN             Reviewed;         336 AA.
AC   Q0II68;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=2-amino-3-carboxymuconate-6-semialdehyde decarboxylase;
DE            EC=4.1.1.45;
DE   AltName: Full=Picolinate carboxylase;
GN   Name=ACMSD;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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   EMBL; BC122781; AAI22782.1; -; mRNA.
DR   RefSeq; NP_001069162.1; NM_001075694.1.
DR   AlphaFoldDB; Q0II68; -.
DR   SMR; Q0II68; -.
DR   STRING; 9913.ENSBTAP00000010575; -.
DR   PaxDb; Q0II68; -.
DR   PRIDE; Q0II68; -.
DR   Ensembl; ENSBTAT00000010575; ENSBTAP00000010575; ENSBTAG00000008039.
DR   GeneID; 515030; -.
DR   KEGG; bta:515030; -.
DR   CTD; 130013; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008039; -.
DR   VGNC; VGNC:25544; ACMSD.
DR   eggNOG; KOG4245; Eukaryota.
DR   GeneTree; ENSGT00490000043417; -.
DR   HOGENOM; CLU_039329_1_2_1; -.
DR   InParanoid; Q0II68; -.
DR   OMA; TTNYKAI; -.
DR   OrthoDB; 941496at2759; -.
DR   TreeFam; TF313232; -.
DR   UniPathway; UPA00270; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000008039; Expressed in metanephros cortex and 29 other tissues.
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:0008270; F:zinc ion binding; IEA:Ensembl.
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..336
FT                   /note="2-amino-3-carboxymuconate-6-semialdehyde
FT                   decarboxylase"
FT                   /id="PRO_0000270786"
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         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         291
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   336 AA;  37923 MW;  4C859894716055C2 CRC64;
     MKIDIHTHIL PREWPDLKKR FGYGGWVQLQ HNGKGEAKML KDGKVFRVVQ ENCWDPEARL
     REMDQTGVTV QALSTVPVMF SYWAKPQDTL DLCQLLNNDL AATIASHPRR FVGLGTLPMQ
     APELAVKEME RCVRKLGFPG VQIGSHINEW DLNARELFPV YAEAERLNCS LFVHPWDMQM
     DGRMAKYWFP WLIGMPAETT AAICSMIMGG VFEKFPKLKV CFAHGGGSFP FTVGRISHGF
     SMRPDLCAQD NPTNPKKYLG SFYTDSLVHD PLALKLLTDV IGKDKVILGT DYPFPLGELE
     PGKLIESMGE FDAETKDKLK AGNALEFLGL ERKQFE