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Database: UniProt/TrEMBL
Entry: M2QTY9_COCSN
LinkDB: M2QTY9_COCSN
Original site: M2QTY9_COCSN 
ID   M2QTY9_COCSN            Unreviewed;       524 AA.
AC   M2QTY9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-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=COCSADRAFT_154177 {ECO:0000313|EMBL:EMD58599.1};
OS   Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot
OS   and spot blotch fungus) (Bipolaris sorokiniana).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD58599.1, ECO:0000313|Proteomes:UP000016934};
RN   [1] {ECO:0000313|EMBL:EMD58599.1, ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A.,
RA   Barry K.W., Condon B.J., Copeland A.C., Dhillon B., Glaser F.,
RA   Hesse C.N., Kosti I., LaButti K., Lindquist E.A., Lucas S.,
RA   Salamov A.A., Bradshaw R.E., Ciuffetti L., Hamelin R.C., Kema G.H.J.,
RA   Lawrence C., Scott J.A., Spatafora J.W., Turgeon B.G.,
RA   de Wit P.J.G.M., Zhong S., Goodwin S.B., Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in
RT   the genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
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; KB445655; EMD58599.1; -; Genomic_DNA.
DR   RefSeq; XP_007705688.1; XM_007707498.1.
DR   EnsemblFungi; EMD58599; EMD58599; COCSADRAFT_154177.
DR   GeneID; 19131655; -.
DR   KEGG; bsc:COCSADRAFT_154177; -.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000016934; 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:UP000016934};
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:UP000016934}.
FT   MOD_RES     300    300       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   524 AA;  59435 MW;  E41DF340FCFADAF0 CRC64;
     MVHINRVATF KEISDERAQF DDIATASTIN LSPDDEIDDF TATVYGSKYA AEDLPKYEMP
     EREMPPQVAY RMIKDDLTLD GTPTLNLASF VTTYMEEEVE KLMVDAFSKN FIDYEEYPVS
     ADIQNRCVSM IARLFNAPST DDANIIGTST IGSSEAIMLG VLAMKKLWQN KRKAEGKPYD
     KPNMVMNSAV QVCWEKACRY FDIEEKYVYC TADRYVIDPK ECVDLCDENT IGICAILGTT
     YTGEYEDIKA INDLLIERDI DVNIHVDAAS GGFVAPFVNP GLLWDFRLPK VTTINASGHK
     YGLVYPGVGW VIWRDPQYLP QELVFNINYL GADQASFTLN FSRGASQIIG QYYQLIRLGK
     RGYRRIMLNL TRTADYLAAN LESMGFVIMS QRGGEGLPLV ACRIDEDLGK QYDEFAIAHQ
     LRERGWVVPA YTMAPHSEKM KMLRVVVRED FTKSRCDALI ADFKLALQTL DALDARRIQD
     HKEHQFAMRR RSTLVSPVFQ KKATDHFEEN HSLQAKTGKT HAVC
//
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