ID   DCE_YEAST               Reviewed;         585 AA.
AC   Q04792; D6W076;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Glutamate decarboxylase;
DE            Short=GAD;
DE            EC=4.1.1.15;
GN   Name=GAD1; OrderedLocusNames=YMR250W; ORFNames=YM9920.04;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- MISCELLANEOUS: Present with 1200 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; Z48639; CAA88577.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10150.1; -; Genomic_DNA.
DR   PIR; S53072; S53072.
DR   RefSeq; NP_013976.1; NM_001182756.1.
DR   AlphaFoldDB; Q04792; -.
DR   SMR; Q04792; -.
DR   BioGRID; 35428; 77.
DR   DIP; DIP-2552N; -.
DR   IntAct; Q04792; 3.
DR   MINT; Q04792; -.
DR   STRING; 4932.YMR250W; -.
DR   iPTMnet; Q04792; -.
DR   MaxQB; Q04792; -.
DR   PaxDb; 4932-YMR250W; -.
DR   PeptideAtlas; Q04792; -.
DR   EnsemblFungi; YMR250W_mRNA; YMR250W; YMR250W.
DR   GeneID; 855291; -.
DR   KEGG; sce:YMR250W; -.
DR   AGR; SGD:S000004862; -.
DR   SGD; S000004862; GAD1.
DR   VEuPathDB; FungiDB:YMR250W; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_3_1; -.
DR   InParanoid; Q04792; -.
DR   OMA; KNIMQNC; -.
DR   OrthoDB; 2783360at2759; -.
DR   BioCyc; YEAST:YMR250W-MONOMER; -.
DR   BioGRID-ORCS; 855291; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q04792; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04792; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IMP:SGD.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR   GO; GO:0006538; P:glutamate catabolic process; IMP:SGD.
DR   Gene3D; 3.90.1150.160; -; 1.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   1: Evidence at protein level;
KW   Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..585
FT                   /note="Glutamate decarboxylase"
FT                   /id="PRO_0000146977"
FT   REGION          35..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         318
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   585 AA;  65990 MW;  DDD22868CEB7B955 CRC64;
     MLHRHGSKQK NFENIAGKVV HDLAGLQLLS NDVQKSAVQS GHQGSNNMRD TSSQGMANKY
     SVPKKGLPAD LSYQLIHNEL TLDGNPHLNL ASFVNTFTTD QARKLIDENL TKNLADNDEY
     PQLIELTQRC ISMLAQLWHA NPDEEPIGCA TTGSSEAIML GGLAMKKRWE HRMKNAGKDA
     SKPNIIMSSA CQVALEKFTR YFEVECRLVP VSHRSHHMLD PESLWDYVDE NTIGCFVILG
     TTYTGHLENV EKVADVLSQI EAKHPDWSNT DIPIHADGAS GGFIIPFGFE KEHMKAYGME
     RWGFNHPRVV SMNTSGHKFG LTTPGLGWVL WRDESLLADE LRFKLKYLGG VEETFGLNFS
     RPGFQVVHQY FNFVSLGHSG YRTQFQNSLF VARAFSFELL NSSKLPGCFE IVSSIHESIE
     NDSAPKSVKD YWEHPQAYKP GVPLVAFKLS KKFHEEYPEV PQAILSSLLR GRGWIIPNYP
     LPKATDGSDE KEVLRVVFRS EMKLDLAQLL IVDIESILTK LIHSYEKVCH HIELASEQTP
     ERKSSFIYEM LLALASPQDD IPTPDEIEKK NKLKETTTRN YRGTC
//