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Database: UniProt/TrEMBL
Entry: M7T6Q3_EUTLA
LinkDB: M7T6Q3_EUTLA
Original site: M7T6Q3_EUTLA 
ID   M7T6Q3_EUTLA            Unreviewed;       516 AA.
AC   M7T6Q3;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   20-JUN-2018, entry version 28.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=UCREL1_633 {ECO:0000313|EMBL:EMR72317.1};
OS   Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus)
OS   (Eutypa armeniacae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX   NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR72317.1, ECO:0000313|Proteomes:UP000012174};
RN   [1] {ECO:0000313|Proteomes:UP000012174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX   PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA   Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT   "Draft genome sequence of the grapevine dieback fungus Eutypa lata
RT   UCR-EL1.";
RL   Genome Announc. 1:E0022813-E0022813(2013).
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; KB705475; EMR72317.1; -; Genomic_DNA.
DR   RefSeq; XP_007788591.1; XM_007790400.1.
DR   EnsemblFungi; EMR72317; EMR72317; UCREL1_633.
DR   KEGG; ela:UCREL1_633; -.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000012174; Unassembled WGS sequence.
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; 3.40.640.10; -; 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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000012174};
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:UP000012174}.
FT   MOD_RES     296    296       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   516 AA;  57956 MW;  76458E245125F460 CRC64;
     MVHLAAIPQD SEANKLPEAV SKVSLQLSEE EDSFTTSIYG SRFAAEDLPR LEIPDGEMPK
     EIAYKLIKDE LSLDGNPMLN LASFVTTYME EEAEKLMTDS FSKNFIDYEE YPVSADIQNR
     CVSMIGRLFN APVDDSGSSA PVGTSTIGSS EAIMLGVLAM KRRWKNKRKA EGKSTENPNI
     VMSSAVQVCW EKATRYFEIE EKLVYCTPDR FVIDPVETVN LIDENTIGIC AILGTTYTGE
     YEDVKAVNDL LVERGIDCPI HVDAASGGFV APFVVPDLEW DFRCEKVVSI NVSGHKYGLV
     YPGVGWVVWR AAEFLPQELV FNINYLGADQ ASFTLNFSKG ASQVIGQYYQ LIRLGKKGYK
     AIMSNLTRTG NYLSESLEAL GFIIMSKQSG MGLPLVAFRL PPKEEREWDE FSLAHRLRAR
     GWVVPAYTMA PHTNEMKMLR VVVREDFSKN RCDSLICDIK LCMELLDAMD KETIKKHEQF
     IRTHAMHSGQ SKHNHPKFRN EKHSLQGKHG KTHGVC
//
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