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Database: UniProt/TrEMBL
Entry: A0A010SB79_9PEZI
LinkDB: A0A010SB79_9PEZI
Original site: A0A010SB79_9PEZI 
ID   A0A010SB79_9PEZI        Unreviewed;       568 AA.
AC   A0A010SB79;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   18-JUL-2018, entry version 26.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=CFIO01_11476 {ECO:0000313|EMBL:EXF81978.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF81978.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF81978.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF81978.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EXF81978.1}.
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DR   EMBL; JARH01000343; EXF81978.1; -; Genomic_DNA.
DR   RefSeq; XP_007594371.1; XM_007594309.1.
DR   EnsemblFungi; EXF81978; EXF81978; CFIO01_11476.
DR   KEGG; cfj:CFIO01_11476; -.
DR   KO; K01580; -.
DR   Proteomes; UP000020467; 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   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; 2.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000020467};
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:UP000020467}.
FT   MOD_RES     303    303       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   568 AA;  63471 MW;  890C40F280992860 CRC64;
     MPLASHVNPE DIVQRLQATH ITAPGNANAL SHGTSSHIQP YDSRYTSQTN IPKYKIPDEG
     APGDTVFQMI RDELDLDGKP NLNLASFVGT WMEPNATQLM QENLSKNLSD ADEYPAMMEM
     HQRCISIISH LWGVQPGEKA IGSATTGSSE AIHLGGLAMK RRWQLKRKEQ GKDTSKPNIL
     MGSNAQVALE KFARYFDVEA RILPVSKKSH YRLDPALVRE NIDENTIGVF VILGSTYTGH
     YEPVEEISQI LDKYQEETGI DIPIHVDAAS GGFIAPFTHA GVGGSKWNFE LPRVKSINVS
     GHKYGLVYAG LGWIIWRDQS FLPEDLIFEL HYLGGTEKSF TLNFSRPGAQ VIVQYYNLIH
     LGFDGYRSIM ENCLSNARIL AQSLEATGWY TVVSDIHRRA PHKEASGAVK KIVNQAATAV
     AGENAAPGET SADYVAGLPV VSFRLTDEFK AKYEHIKQET ISLMLRAKGW IIPNYPLPPN
     EEKIEILRVV VRETMTFDLL ERLLTDIVEV TETLIENDQI DLQVLKKHHS RRRVRVKGDE
     EKHKKEGAAK EVQNGARKME DGIHRAVC
//
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