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Database: UniProt/TrEMBL
Entry: R8BAD9_TOGMI
LinkDB: R8BAD9_TOGMI
Original site: R8BAD9_TOGMI 
ID   R8BAD9_TOGMI            Unreviewed;       510 AA.
AC   R8BAD9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   25-OCT-2017, entry version 26.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=UCRPA7_8196 {ECO:0000313|EMBL:EON96253.1};
OS   Togninia minima (strain UCR-PA7) (Esca disease fungus)
OS   (Phaeoacremonium aleophilum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Togniniales; Togniniaceae;
OC   Phaeoacremonium.
OX   NCBI_TaxID=1286976 {ECO:0000313|EMBL:EON96253.1, ECO:0000313|Proteomes:UP000014074};
RN   [1] {ECO:0000313|Proteomes:UP000014074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-PA7 {ECO:0000313|Proteomes:UP000014074};
RX   PubMed=23814032; DOI=10.1128/genomeA.00390-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of the ascomycete Phaeoacremonium aleophilum
RT   strain UCR-PA7, a causal agent of the esca disease complex in
RT   grapevines.";
RL   Genome Announc. 1:E0039013-E0039013(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; KB933350; EON96253.1; -; Genomic_DNA.
DR   RefSeq; XP_007918906.1; XM_007920715.1.
DR   EnsemblFungi; EON96253; EON96253; UCRPA7_8196.
DR   GeneID; 19329026; -.
DR   KEGG; tmn:UCRPA7_8196; -.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000014074; 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   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:UP000014074};
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:UP000014074}.
FT   MOD_RES     290    290       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   510 AA;  57578 MW;  6A82ACF9F05BA276 CRC64;
     MVHLTTIPHP DELDKDIIKE IKKAHLQLAN DDDCFTTSVY GSRFAATDLP KHEMPEREMP
     KEVAYRMIKD ELSLDGNPML NLASFVTTYM EDEAEKLMTE SFSKNFIDYE EYPQSADIQN
     RCVSMIGRLF HAPVGAEEGV GAVGTSCVGS SEAIMLAVLA MKRRWKNARK AAGKSTENPN
     IVMSSAVQVC WEKATRYFEI EEKLVYCTEG RYVIDPEETV NLHAYFIGTT YTGEYEDVKA
     VNDLLVKKGL NVPIHVDAAS GGFVAPFVVP GLEWDFRCER VVSINVSGHK YGLVYPGVGW
     VVWRSAEFLP QELVFNINYL GADQASFTLN FSKGASQVIG QYYQLIRLGK HGYKAIMSNL
     TRTADYLSDS LEALGFIIMS KKSGEGLPLV AFRMTKDEDR NYDEFALAHQ LRVRGWVVPA
     YTMAPHTNDL KMLRVVVRED FTRPRCDALI SDIRQSMCLL DDMDRESIKK QQEFIHKHHT
     ASGKATHNHP KYKKEKHSIQ GKTGKTHAIC
//
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