ID   DCE1_BOVIN              Reviewed;         594 AA.
AC   Q0VCA1;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   RecName: Full=Glutamate decarboxylase 1;
DE            EC=4.1.1.15 {ECO:0000250|UniProtKB:Q99259};
GN   Name=GAD1;
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=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of the inhibitory neurotransmitter
CC       gamma-aminobutyric acid (GABA) with pyridoxal 5'-phosphate as cofactor.
CC       {ECO:0000250|UniProtKB:Q99259}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC         Evidence={ECO:0000250|UniProtKB:Q99259};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17786;
CC         Evidence={ECO:0000250|UniProtKB:Q99259};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q99259};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q99259}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; BC120278; AAI20279.1; -; mRNA.
DR   RefSeq; NP_001069224.1; NM_001075756.2.
DR   RefSeq; XP_005202387.1; XM_005202330.3.
DR   RefSeq; XP_015330341.1; XM_015474855.1.
DR   AlphaFoldDB; Q0VCA1; -.
DR   SMR; Q0VCA1; -.
DR   STRING; 9913.ENSBTAP00000009547; -.
DR   PaxDb; 9913-ENSBTAP00000009547; -.
DR   Ensembl; ENSBTAT00000009547.6; ENSBTAP00000009547.5; ENSBTAG00000007258.6.
DR   GeneID; 517552; -.
DR   KEGG; bta:517552; -.
DR   CTD; 2571; -.
DR   VEuPathDB; HostDB:ENSBTAG00000007258; -.
DR   VGNC; VGNC:29204; GAD1.
DR   eggNOG; KOG0629; Eukaryota.
DR   GeneTree; ENSGT00940000155526; -.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   InParanoid; Q0VCA1; -.
DR   OMA; RHATYHA; -.
DR   OrthoDB; 888358at2759; -.
DR   TreeFam; TF314688; -.
DR   Reactome; R-BTA-888568; GABA synthesis.
DR   Reactome; R-BTA-888590; GABA synthesis, release, reuptake and degradation.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000007258; Expressed in floor plate of diencephalon and 23 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006538; P:glutamate catabolic process; ISS:UniProtKB.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR45677:SF5; GLUTAMATE DECARBOXYLASE 1; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   2: Evidence at transcript level;
KW   Decarboxylase; Lyase; Neurotransmitter biosynthesis; Phosphoprotein;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..594
FT                   /note="Glutamate decarboxylase 1"
FT                   /id="PRO_0000289582"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         190..192
FT                   /ligand="4-aminobutanoate"
FT                   /ligand_id="ChEBI:CHEBI:59888"
FT                   /evidence="ECO:0000250|UniProtKB:Q99259"
FT   BINDING         567
FT                   /ligand="4-aminobutanoate"
FT                   /ligand_id="ChEBI:CHEBI:59888"
FT                   /evidence="ECO:0000250|UniProtKB:Q99259"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48318"
FT   MOD_RES         405
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99259"
SQ   SEQUENCE   594 AA;  66784 MW;  2936F526D5E64EDD CRC64;
     MASSTPSSSA TSSNAGADPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF LQRTNSLEEK
     SRLVSAFKER QSSKNLLSCE NSDKDGRFRR TETDFSNLFA RDLLPAKNGE EQTVQFLLEV
     VDILLNYVRK TFDRSTKVLD FHHPHQLLEG MEGFNLELSD HPESLEQILV DCRDTLKYGV
     RTGHPRFFNQ LSTGLDIIGL AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIVGWS
     SKDGDGIFSP GGAISNMYSI MAARFKYFPE VKTKGMAAVP KLVLFTSEHS HYSIKKAGAA
     LGFGTDNVIL IKCNERGKII PADLETKILE AKQKGYVPLY VNATAGTTVY GAFDPIQEIA
     DICEKYNLWL HVDAAWGGGL LMSQKHRHKL SGIERANSVT WNPHKMMGVL LQCSAILVKE
     KGILQGCNQM CAGYLFQPDK QYDVSYDTGD KAIQCGRHVD IFKFWLMWKA KGTVGFENQI
     NKCLELAEYL YAKIKNREEF EMVFDGEPEH TNVCFWYIPQ SLRGVPDSPE RREKLHRVAP
     KIKALMMESG TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL
//