ID   Q91644_XENLA            Unreviewed;       563 AA.
AC   Q91644;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Glutamate decarboxylase 1 {ECO:0000256|ARBA:ARBA00040578};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421};
GN   Name=gad1.1.L {ECO:0000313|Xenbase:XB-GENE-1011702};
GN   Synonyms=GAD {ECO:0000313|EMBL:AAA96273.1}, gad1
GN   {ECO:0000313|Xenbase:XB-GENE-1011702}, gad1.1
GN   {ECO:0000313|Xenbase:XB-GENE-1011702};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAA96273.1};
RN   [1] {ECO:0000313|EMBL:AAA96273.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Watt S.D., Spitzer N.C.;
RL   Submitted (OCT-1995) 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:0000256|ARBA:ARBA00037700}.
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:0000256|ARBA:ARBA00036502};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17786;
CC         Evidence={ECO:0000256|ARBA:ARBA00036502};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; U38225; AAA96273.1; -; mRNA.
DR   RefSeq; NP_001079270.1; NM_001085801.1.
DR   AlphaFoldDB; Q91644; -.
DR   AGR; Xenbase:XB-GENE-1011702; -.
DR   Xenbase; XB-GENE-1011702; gad1.1.L.
DR   OrthoDB; 888358at2759; -.
DR   Bgee; 378551; Expressed in brain and 2 other cell types or tissues.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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 {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Neurotransmitter biosynthesis {ECO:0000256|ARBA:ARBA00022979};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES         374
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   563 AA;  64096 MW;  BE1C11B1AD4F2598 CRC64;
     MLRKENTLPM TCSHCNNVGF LQRNNSLDDK SRIVSSFKER QASKNLLVCE NIEKDSRFGR
     AETDFSNLFA RDLLPAKNGK NSQCSSYWRW LTFFYTMYEK HLIDPPKSYT FTILTNFLKV
     LKASTWSCLK TQSPWSKSWW IVGIPSSMES EQDILASSTS SQQDWISLAW LGNGSHQLLT
     LTCLYEIAPV FVLMEQITLR KMREIIGWTE KDGDGIFSPG GAISNMYSIM AARYKYFPEV
     KTKGMAAVPR LVLFTSEHSH YSIKKTGAAL GFGSENVILI KSDERGKMIP ADLEAKILEA
     KQKGYIPLYV NATAGTTVYG AFDPISEIAD ICEKYNLWLH VDAAWGGGLL MSRRHRHKLN
     GIERANSVTW NPHKMMGVLL QCSAILLREK GILQGCNQMC AGYLFQQDKQ YDVSYDTGDK
     AIQCGRHVDI FKFWLIWKAK GTVGFEAQIN KCLELGEYLY SKIYNRQGYE MVFNGEPEHT
     NICFWYIPPS LRGIPNSQER QEKLHRVAPK IKALMMESGT TMVGYQPHGD KVNFFRMVIS
     NPAATKSDID FLVEEIERLG QDL
//