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Database: UniProt/TrEMBL
Entry: W6YXF8_COCMI
LinkDB: W6YXF8_COCMI
Original site: W6YXF8_COCMI 
ID   W6YXF8_COCMI            Unreviewed;       524 AA.
AC   W6YXF8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   25-OCT-2017, entry version 23.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=COCMIDRAFT_109402 {ECO:0000313|EMBL:EUC40214.1};
OS   Bipolaris oryzae ATCC 44560.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC40214.1, ECO:0000313|Proteomes:UP000054032};
RN   [1] {ECO:0000313|EMBL:EUC40214.1, ECO:0000313|Proteomes:UP000054032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC40214.1,
RC   ECO:0000313|Proteomes:UP000054032};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R.,
RA   Martin J., Schackwitz W., Grimwood J., MohdZainudin N., Xue C.,
RA   Wang R., Manning V.A., Dhillon B., Tu Z.J., Steffenson B.J.,
RA   Salamov A., Sun H., Lowry S., LaButti K., Han J., Copeland A.,
RA   Lindquist E., Barry K., Schmutz J., Baker S.E., Ciuffetti L.M.,
RA   Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector
RT   coding capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(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; KI964186; EUC40214.1; -; Genomic_DNA.
DR   RefSeq; XP_007693273.1; XM_007695083.1.
DR   EnsemblFungi; EUC40214; EUC40214; COCMIDRAFT_109402.
DR   GeneID; 19119423; -.
DR   KEGG; bor:COCMIDRAFT_109402; -.
DR   KO; K01580; -.
DR   Proteomes; UP000054032; 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:UP000054032};
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     300    300       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   524 AA;  59451 MW;  471FE90A16981084 CRC64;
     MVHINRVATF KEISEERARF DDIATTSTIN LSPDDEVDDF TATVYGSKYA AEDLPKYEMP
     EREMPPQVAY RMIKDDLTLD GTPTLNLASF VTTYMEEEVE KLMVDAFSKN FIDYEEYPVS
     ADIQNRCVSM IARLFNAPST DDANIIGTST IGSSEAIMLG VLAMKKLWQN KRKAEGKPYD
     KPNMVMNSAV QVCWEKACRY FDIEEKYVYC TADRYVIDPK ECVDLCDENT IGICAILGTT
     YTGEYEDIKA INDLLVERDI DVNIHVDAAS GGFVAPFVNP GLLWDFRLPK VTTINASGHK
     YGLVYPGVGW VVWRDPQYLP QELVFNINYL GADQASFTLN FSRGASQIIG QYYQLIRLGK
     RGYRRIMLNL TRTADYLAAN LESMGFVIMS QRGGEGLPLV ACRIDEDLGK QYDEFAIAHQ
     LRERGWVVPA YTMAPHSEKM KMLRVVVRED FTKSRCDALI ADFKLALQTL DALDAKRIQE
     HKEHQFAMRR RSTLVSPVFQ KKATDHFEEN HSLQAKTGKT HAVC
//
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