ID   DCE1_PIG                Reviewed;         594 AA.
AC   P48319;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 114.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7835711; DOI=10.1016/0378-1119(94)00713-3;
RA   Suzuki R., Asami N., Amann E., Wagatsuma M.;
RT   "Sequences of two porcine glutamic acid decarboxylases (65- and 67-kDa
RT   GAD).";
RL   Gene 152:257-260(1995).
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; D31849; BAA06636.1; -; mRNA.
DR   PIR; JC4065; JC4065.
DR   RefSeq; NP_999059.1; NM_213894.1.
DR   AlphaFoldDB; P48319; -.
DR   SMR; P48319; -.
DR   STRING; 9823.ENSSSCP00000023541; -.
DR   PaxDb; P48319; -.
DR   PeptideAtlas; P48319; -.
DR   PRIDE; P48319; -.
DR   Ensembl; ENSSSCT00015079812; ENSSSCP00015032241; ENSSSCG00015059664.
DR   Ensembl; ENSSSCT00070049047; ENSSSCP00070041424; ENSSSCG00070024572.
DR   Ensembl; ENSSSCT00070049050; ENSSSCP00070041427; ENSSSCG00070024572.
DR   GeneID; 396928; -.
DR   KEGG; ssc:396928; -.
DR   CTD; 2571; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   InParanoid; P48319; -.
DR   OrthoDB; 810772at2759; -.
DR   TreeFam; TF314688; -.
DR   Reactome; R-SSC-888568; GABA synthesis.
DR   Reactome; R-SSC-888590; GABA synthesis, release, reuptake and degradation.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Chromosome 15.
DR   Genevisible; P48319; SS.
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_0000146966"
FT   REGION          1..25
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;  66895 MW;  42C7954A537862AF CRC64;
     MASSTPSSSA TSSNAGPDPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF LQRTNSLEEK
     SRLVSAFKER QSSKNLLSCE NSDRDGRFRR TETDFSNLFA RDLLPAKNGE EQTVQFLLEV
     VDILLNYVRK TFDRSTKVLD FHHPHQLLEG MEGFNLELSD HPESLEQILV DCRDTLKYGV
     RTGHPRFFNQ LSTGLDIIGL AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIVGWS
     NKDGDGIFSP GGAISNMYSI MAARYKYFPE VKTKGMAAVP KLVLFTSEHS HYSIKKAGAA
     LGFGTDNVIL IKCNERGKII PADLEAKILE AKQKGYIPLY VNATAGTTVY GAFDPIQEIA
     DICEKYNLWL HVDAAWGGGL LMSRKHRHKL SGIERADSVT WNPHKMMGVL LQCSAILVKE
     KGILQGCNQM CAGYLFQPDK QYDVSYDTGD KAIQCGRHVD IFKFWLMWKA KGTVGFENQI
     NKCLELAEYL YAKIKNREEF EMVFDGEPEH TNVCFWYIPQ SLRGVPDSPE RREKLHRVAP
     KIKALMMESG TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL