ID   DCE1_FELCA              Reviewed;         594 AA.
AC   P14748;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 3.
DT   03-AUG-2022, entry version 104.
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   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Occipital cortex;
RX   PubMed=3453123; DOI=10.1523/jneurosci.07-09-02768.1987;
RA   Kobayashi Y., Kaufman D.L., Tobin A.J.;
RT   "Glutamic acid decarboxylase cDNA: nucleotide sequence encoding an
RT   enzymatically active fusion protein.";
RL   J. Neurosci. 7:2768-2772(1987).
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; M18629; AAA51430.1; -; mRNA.
DR   PIR; A46758; A46758.
DR   RefSeq; NP_001009225.1; NM_001009225.1.
DR   RefSeq; XP_019691505.1; XM_019835946.1.
DR   RefSeq; XP_019691506.1; XM_019835947.1.
DR   AlphaFoldDB; P14748; -.
DR   SMR; P14748; -.
DR   STRING; 9685.ENSFCAP00000006586; -.
DR   Ensembl; ENSFCAT00000044700; ENSFCAP00000030985; ENSFCAG00000007099.
DR   GeneID; 493699; -.
DR   KEGG; fca:493699; -.
DR   CTD; 2571; -.
DR   VGNC; VGNC:62430; GAD1.
DR   eggNOG; KOG0629; Eukaryota.
DR   GeneTree; ENSGT00940000155526; -.
DR   InParanoid; P14748; -.
DR   Proteomes; UP000011712; Chromosome C1.
DR   Bgee; ENSFCAG00000007099; Expressed in prefrontal cortex and 7 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR   GO; GO:0016831; F:carboxy-lyase activity; 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; IBA:GO_Central.
DR   GO; GO:0006538; P:glutamate catabolic process; ISS:UniProtKB.
DR   GO; GO:0042136; P:neurotransmitter biosynthetic process; ISS:UniProtKB.
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_0000146962"
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;  66825 MW;  EE1C8D928BC0BD02 CRC64;
     MASSTPSSSA TSSNAGADPN TTNLRPTTYD 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