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Database: UniProt/TrEMBL
Entry: G0WHJ9_NAUDC
LinkDB: G0WHJ9_NAUDC
Original site: G0WHJ9_NAUDC 
ID   G0WHJ9_NAUDC            Unreviewed;       586 AA.
AC   G0WHJ9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   25-OCT-2017, entry version 35.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   Name=NDAI0K00690 {ECO:0000313|EMBL:CCD27260.1};
GN   OrderedLocusNames=NDAI_0K00690 {ECO:0000313|EMBL:CCD27260.1};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 /
OS   NBRC 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD27260.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD27260.1, ECO:0000313|Proteomes:UP000000689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC   {ECO:0000313|Proteomes:UP000000689};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S.,
RA   Byrne K.P., Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type
RT   switching accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; HE580277; CCD27260.1; -; Genomic_DNA.
DR   RefSeq; XP_003672503.1; XM_003672455.1.
DR   STRING; 1071378.XP_003672503.1; -.
DR   EnsemblFungi; CCD27260; CCD27260; NDAI_0K00690.
DR   GeneID; 11497548; -.
DR   KEGG; ndi:NDAI_0K00690; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000000689; Chromosome 11.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   GO; GO:0006538; P:glutamate catabolic process; IEA:EnsemblFungi.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000689};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT   MOD_RES     328    328       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   586 AA;  66841 MW;  FB03C15C008FFAA4 CRC64;
     MLHSHSTRQK GVSPPASDRG PSEVDIPQFQ RGPRQSIVGL EDVKLLSSNL QQMSYHGATT
     NTFDESNNKY IIPNHGLPEQ TAYDLIHNEL TLDGNPHLNL ASFVNTTTTQ IANRLIMENI
     DKNLADNDEY PQLIELTQRC ISMLAKLWKS NPDMEPIGCA TTGSSEAIML GGLAMKKIWE
     AKMKKAGKSV EKPNILMSSA CQVALEKFAR YFEVECRLIP VCKESKYCLD PRKLWDYVDE
     NTIGCYVLLG TTYTGHLENV EEVADVLTEI EIQHPSWSNK EIPIHVDGAS GGFIVPFSFE
     ASHMKKFGLE RWGFNNPRVV SINTSGHKFG LTTPGLGWAL WKDQSYLPPE LRFRLKYLGG
     VEETFNLNFS RPGFQVVHQY YNFVSLGFTG YKNHFLKSLF VARTFAYSLL KSEKLQDYIE
     VISGIHERIS DDKVPDNVTD YWENPQDFKP GVPLIAFKLS KHFNEAYPEI PQAIISKLLR
     TRGWIVPNYP LPNSSDDSSN WEVLRVVFRT EMKLDFAQLL IIDIENIITK LLSCYEKVEE
     HAEQEKQTKE GKRQFIYDML LTLASPESEE DEKLKERVTR NYRGTC
//
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