ID   D0VFN3_YEASX            Unreviewed;       585 AA.
AC   D0VFN3;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
GN   Name=GAD1 {ECO:0000313|EMBL:ACY54291.1, ECO:0000313|SGD:S000004862};
GN   OrderedLocusNames=YMR250W {ECO:0000313|SGD:S000004862};
GN   ORFNames=GI527_G0004703 {ECO:0000313|EMBL:KAF1903941.1};
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932 {ECO:0000313|EMBL:ACY54291.1};
RN   [1] {ECO:0000313|EMBL:ACY54291.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MJ2 {ECO:0000313|EMBL:ACY54291.1};
RA   Jiang D.H., Li J., Hou J.H., Xu X.B.;
RT   "Screening of a high yield gamma-aminobutyricacid yeast from the fruit
RT   surface and optimization of its cultural conditions.";
RL   Zhejiang Nong Ye Da Xue Xue Bao 20:396-401(2008).
RN   [2] {ECO:0000313|EMBL:ACY54291.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MJ2 {ECO:0000313|EMBL:ACY54291.1};
RA   Li J., Jiang D.H., Zhou Q.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AIY53684.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=28 {ECO:0000313|EMBL:AIY53684.1};
RA   Bao W.;
RT   "Molecular Cloning of the Glutamic Acid Decarboxylase GAD1 Gene from
RT   Saccharomyces cerevisiae.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:KAF1903941.1, ECO:0000313|Proteomes:UP000470054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INSC1005 {ECO:0000313|EMBL:KAF1903941.1,
RC   ECO:0000313|Proteomes:UP000470054};
RA   Fiddes I.T., Church D.M.;
RT   "Inscripta technologies.";
RL   Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361171};
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   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; GU074586; ACY54291.1; -; Genomic_DNA.
DR   EMBL; KM408173; AIY53684.1; -; Genomic_DNA.
DR   EMBL; JAAEAL010000012; KAF1903941.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0VFN3; -.
DR   SMR; D0VFN3; -.
DR   SGD; S000004862; GAD1.
DR   VEuPathDB; FungiDB:YMR250W; -.
DR   OMA; KNIMQNC; -.
DR   Proteomes; UP000470054; Chromosome xiii.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
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   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
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:0000256|PIRSR:PIRSR602129-50"
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
//