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Database: UniProt
Entry: A0A139I901_9PEZI
LinkDB: A0A139I901_9PEZI
Original site: A0A139I901_9PEZI 
ID   A0A139I901_9PEZI        Unreviewed;       516 AA.
AC   A0A139I901;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
GN   ORFNames=AC579_826 {ECO:0000313|EMBL:KXT11200.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT11200.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT11200.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT11200.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC         Evidence={ECO:0000256|RuleBase:RU361171};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, 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 EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXT11200.1}.
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DR   EMBL; LFZO01000216; KXT11200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139I901; -.
DR   STRING; 113226.A0A139I901; -.
DR   Proteomes; UP000073492; 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; 3.90.1150.160; -; 1.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF6; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000073492}.
FT   MOD_RES         296
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   516 AA;  58598 MW;  769755671FFFC456 CRC64;
     MVHLAKVATD RELDAKLVPG LEGLDLTNIP DEDEFTTSVY GSKYAAADLP RHEMPDGEMP
     REMAYRMIKD DLTLDGVPTL NLASFVTTYM EAEAEKLMVE AFSKNFIDYE EYPVSADIQN
     RCVSMIARLF NIPTHDDNTN AMGTSTIGSS EAIMLGTLAM KKRWQNKRKA EGKDYSRPNI
     VMNSAVQVCW EKAARYFDVE EKYVYCTNDR FTIDPEEAVN LVDENTIGIC SILGTTYTGE
     YEDTKKINDL LIERNIDCPI HVDAASGGFV APFVNPNLVW DFRLEKVVSI NVSGHKYGLV
     YPGVGWVVWR DPDFLPKELI FNINYLGADQ ASFTLNFSRG ASQVIGQYYQ LIRLGKKGYR
     SIMFNLTRTA DYLSAAVQKM GFILMSQTKG RGLPLVAFRL NPEHGHKFDE FAVAHQLRER
     GWVVPAYTMA PNAGKLKMMR VVVREDFSRW RCDALIKDIA LALHELKSLD EKSLQQQREH
     MRMQHAATQW RKKTNNHYAD EEHSLKGKHG KTHGVC
//
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