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Database: UniProt/TrEMBL
Entry: H8WWM4_CANO9
LinkDB: H8WWM4_CANO9
Original site: H8WWM4_CANO9 
ID   H8WWM4_CANO9            Unreviewed;       587 AA.
AC   H8WWM4;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   25-OCT-2017, entry version 29.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=CORT_0A04600 {ECO:0000313|EMBL:CCG20848.1};
OS   Candida orthopsilosis (strain 90-125) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1136231 {ECO:0000313|EMBL:CCG20848.1, ECO:0000313|Proteomes:UP000005018};
RN   [1] {ECO:0000313|EMBL:CCG20848.1, ECO:0000313|Proteomes:UP000005018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90-125 {ECO:0000313|Proteomes:UP000005018};
RX   PubMed=22563396; DOI=10.1371/journal.pone.0035750;
RA   Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.;
RT   "Sequence and analysis of the genome of the pathogenic yeast Candida
RT   orthopsilosis.";
RL   PLoS ONE 7:e35750-e35750(2012).
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; HE681719; CCG20848.1; -; Genomic_DNA.
DR   RefSeq; XP_003866288.1; XM_003866240.1.
DR   EnsemblFungi; CCG20848; CCG20848; CORT_0A04600.
DR   GeneID; 14536743; -.
DR   KEGG; cot:CORT_0A04600; -.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000005018; Chromosome 1.
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; 2.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005018};
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}.
FT   MOD_RES     322    322       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   587 AA;  66229 MW;  B50A4651FE08ED75 CRC64;
     MFQLPRFTSI SKQLIRQFTK YPPTMVLSKH IDAYDLEYEL LKDSRKVKLS PDEFNDEYNS
     SKLTPRYVIP KESANEADIY KYMNQNLALD GIPTLNLASF VNTYVDEHQK KLAVENLTKN
     LADNDEYPSL IDIQNRCVTM LSNLWHAPHK IDPNTGAKIV NSLGTATTGS SEAIMLAGLA
     LKKRWQEKRK AEGKSTENPN ILMATCAQVA LEKFAVYFDV ENRLIPINPE SGHLIDTTKI
     KENIDENTIG IFVIMGSTFT GAFEPVEEIS KLLDEVEKEK GLDIRIHVDG ASGGFVAPFA
     FPHLKWDFAV DRVDSINTSG HKFGMTSVGL GWVIWKDESL LPKNLRFSLD YLGGVEETFG
     LNFSRPGFPV ILQYYNFLTF GKEGYTKIFD GCLSNARLLS NYLDKSTYFD VVSVIHKPAS
     AEDQKRLLTR QVKYLPSPTV NENFQPGLPV VAFRFSKEVR DKYPEIPQEL FSTLLRKRGF
     IVPNYHLPPD ETNVEILRVV VRNSLGLALL EKLIEDCTEI AELLIKSAES VREILTNKEQ
     ASKHNTSTIH DLLLSIASGG LQPLRQKQHE RDGHKAGVAK KSYRGTC
//
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