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 13-FEB-2019, entry version 146.
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;
OC Saccharomycetes; 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.,
RA Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
RA Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome
RT 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.,
RA Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT 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.,
RA Dephoure N., 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
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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 ProteinModelPortal; Q04792; -.
DR SMR; Q04792; -.
DR BioGrid; 35428; 71.
DR DIP; DIP-2552N; -.
DR IntAct; Q04792; 3.
DR MINT; Q04792; -.
DR STRING; 4932.YMR250W; -.
DR MaxQB; Q04792; -.
DR PaxDb; Q04792; -.
DR PRIDE; Q04792; -.
DR EnsemblFungi; YMR250W_mRNA; YMR250W_mRNA; YMR250W.
DR GeneID; 855291; -.
DR KEGG; sce:YMR250W; -.
DR EuPathDB; FungiDB:YMR250W; -.
DR SGD; S000004862; GAD1.
DR HOGENOM; HOG000070228; -.
DR InParanoid; Q04792; -.
DR KO; K01580; -.
DR OMA; RPNLVMG; -.
DR BioCyc; YEAST:YMR250W-MONOMER; -.
DR PRO; PR:Q04792; -.
DR Proteomes; UP000002311; Chromosome XIII.
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; 3.40.640.10; -; 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 PANTHER; PTHR43321; PTHR43321; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Decarboxylase; Lyase; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1 585 Glutamate decarboxylase.
FT /FTId=PRO_0000146977.
FT MOD_RES 318 318 N6-(pyridoxal phosphate)lysine.
FT {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
//
