ID   DCE1_CANLF              Reviewed;         594 AA.
AC   A0PA85;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Glutamate decarboxylase 1;
DE            EC=4.1.1.15 {ECO:0000250|UniProtKB:Q99259};
DE   AltName: Full=67 kDa glutamic acid decarboxylase;
DE            Short=GAD-67;
DE   AltName: Full=Glutamate decarboxylase 67 kDa isoform;
GN   Name=GAD1; Synonyms=GAD67;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=18981669; DOI=10.1292/jvms.70.1107;
RA   Arata S., Hashizume C., Kikusui T., Takeuchi Y., Mori Y.;
RT   "Sequences of canine glutamate decarboxylase (GAD) 1 and GAD2 genes, and
RT   variation of their genetic polymorphisms among five dog breeds.";
RL   J. Vet. Med. Sci. 70:1107-1110(2008).
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; AB261624; BAF37949.1; -; mRNA.
DR   RefSeq; NP_001091012.1; NM_001097543.1.
DR   AlphaFoldDB; A0PA85; -.
DR   SMR; A0PA85; -.
DR   STRING; 9612.ENSCAFP00000039685; -.
DR   Ensembl; ENSCAFT00000109479; ENSCAFP00000074319; ENSCAFG00000012560.
DR   Ensembl; ENSCAFT00030020730; ENSCAFP00030018077; ENSCAFG00030011184.
DR   Ensembl; ENSCAFT00040048453; ENSCAFP00040042327; ENSCAFG00040025904.
DR   Ensembl; ENSCAFT00845045887; ENSCAFP00845036025; ENSCAFG00845025996.
DR   GeneID; 478794; -.
DR   KEGG; cfa:478794; -.
DR   CTD; 2571; -.
DR   VEuPathDB; HostDB:ENSCAFG00845025996; -.
DR   VGNC; VGNC:41067; GAD1.
DR   eggNOG; KOG0629; Eukaryota.
DR   GeneTree; ENSGT00940000155526; -.
DR   InParanoid; A0PA85; -.
DR   OrthoDB; 810772at2759; -.
DR   Reactome; R-CFA-888568; GABA synthesis.
DR   Proteomes; UP000002254; Chromosome 36.
DR   GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR   GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR   GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
DR   GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0006538; P:glutamate catabolic process; ISS:UniProtKB.
DR   GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR   GO; GO:0042136; P:neurotransmitter biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0018352; P:protein-pyridoxal-5-phosphate linkage; IEA:Ensembl.
DR   GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR   Gene3D; 3.40.640.10; -; 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   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 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_0000289581"
FT   REGION          1..22
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;  66794 MW;  DD1463E28DE668F1 CRC64;
     MASSTPSSSA TSSNAGADPN TANLRPTTYD TWCGVAHGCT RKLGLKICGF LQRTNSLEEK
     SRLVSAFKER QSSKNLLSCE NSDRDGRFRR TETDFSNLFA RDLLPAKNGE EQTVQFLLEV
     VDILLNYVRK TFDRSTKVLD FHHPHQLLEG MEGFNLELSD HPESLEQILV DCRDTLKYGV
     RTGHPRFFNQ LSTGLDIIGL AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIVGWS
     SKDGDGIFSP GGAISNMYSI MAARYKFFPE VKTKGMAAVP KLVLFTSEHS HYSIKKAGAA
     LGFGTDNVIL IKCNERGKII PADLEAKILE AKQKGYVPLY VNATAGTTVY GAFDPIQEIA
     DICEKYNLWL HVDAAWGGGL LMSRKHRHKL SGIERANSVT WNPHKMMGVL LQCSAILVKE
     KGILQGCNQM CAGYLFQPDK QYDVSYDTGD KAIQCGRHVD IFKFWLMWKA KGTVGFENQI
     NKCLELAEYL YAKIKNREEF EMVFDGEPEH TNVCFWYIPQ SLRGIPDSPE RREKLHRVAP
     KIKALMMESG TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL