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Database: UniProt/TrEMBL
Entry: M2T4C7_COCSN
LinkDB: M2T4C7_COCSN
Original site: M2T4C7_COCSN 
ID   M2T4C7_COCSN            Unreviewed;       549 AA.
AC   M2T4C7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   05-JUL-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=COCSADRAFT_195126 {ECO:0000313|EMBL:EMD69285.1};
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:EMD69285.1, ECO:0000313|Proteomes:UP000016934};
RN   [1] {ECO:0000313|EMBL:EMD69285.1, 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:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; KB445637; EMD69285.1; -; Genomic_DNA.
DR   RefSeq; XP_007694659.1; XM_007696469.1.
DR   EnsemblFungi; EMD69285; EMD69285; COCSADRAFT_195126.
DR   GeneID; 19133920; -.
DR   KEGG; bsc:COCSADRAFT_195126; -.
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: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; 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:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016934}.
FT   MOD_RES     302    302       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   549 AA;  61571 MW;  50900BC6C0E4661A CRC64;
     MAGLARHVDT EELLTTLKDH PMHKAGGRHA ENRATSHITP YSSRYAAGNE LSKFKIPQDG
     APADVVHQLL KDELDLDGRP SLNLASFVGT YMEREGEQLM IENISKNLSD ADEYPAMMDM
     HARCVSIIAH MWGVQKGEKA IGSATTGSSE AIHLGGLAMK RRWQEKRRAE GKDTSNPNII
     MGANAQVALE KFARYFEVEA RILPVSEDSS YRLDPKLVKE NIDENTIGVF VILGSTYTGH
     YEPVEEISEI LDEFEKKTGV DIPIHVDAAS GGFIAPFTHA KAGRKWNFEL PRVKSINTSG
     HKFGLVYAGV GWIIWRDESY LPKHLIFELH YLGGTEESYT LNFSRPGAQV IAQYYNLIHL
     GFSGYRSIME NTLANARLLS RALEHTGWYR CVSDIHRKKG DFKYEKGKEQ YEEGATSEAY
     NPGLPVVAFT LTDGFHKEFP HVKQEAVSNL LRAKQYIIPN YPLPPNEEKT EILRVVVRES
     LSIDMIDRLV TDICGVTEML MNTDAVDLAA FQPSANPSVE KQHASKGLRK EHKHKAQRPT
     KDGVYRTVC
//
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