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Database: UniProt/TrEMBL
Entry: A0A194XSY8_9HELO
LinkDB: A0A194XSY8_9HELO
Original site: A0A194XSY8_9HELO 
ID   A0A194XSY8_9HELO        Unreviewed;       555 AA.
AC   A0A194XSY8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=LY89DRAFT_181885 {ECO:0000313|EMBL:KUJ23420.1};
OS   Phialocephala scopiformis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiales incertae sedis; Phialocephala.
OX   NCBI_TaxID=149040 {ECO:0000313|EMBL:KUJ23420.1, ECO:0000313|Proteomes:UP000070700};
RN   [1] {ECO:0000313|EMBL:KUJ23420.1, ECO:0000313|Proteomes:UP000070700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 120377 {ECO:0000313|EMBL:KUJ23420.1,
RC   ECO:0000313|Proteomes:UP000070700};
RG   DOE Joint Genome Institute;
RA   Walker A.K., Frasz S.L., Seifert K.A., Miller J.D., Mondo S.J.,
RA   Labutti K., Lipzen A., Dockter R., Kennedy M., Grigoriev I.V.,
RA   Spatafora J.W.;
RT   "Full genome of DAOMC 229536 Phialocephala scopiformis, a fungal
RT   endophyte of spruce producing the potent anti-insectan compound
RT   rugulosin.";
RL   Submitted (OCT-2015) 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}.
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DR   EMBL; KQ947405; KUJ23420.1; -; Genomic_DNA.
DR   RefSeq; XP_018077775.1; XM_018205618.1.
DR   EnsemblFungi; KUJ23420; KUJ23420; LY89DRAFT_181885.
DR   GeneID; 28815344; -.
DR   KEGG; psco:LY89DRAFT_181885; -.
DR   KO; K01580; -.
DR   Proteomes; UP000070700; 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; 2.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000070700};
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:UP000070700}.
FT   MOD_RES     303    303       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   555 AA;  61464 MW;  620D026EE0470EA9 CRC64;
     MSLAKHVDPD EIISGLQKMQ MNEGGHNHAH TKGGTSHITP YSTRYASKQE ISKFIIPQEG
     APADAVHQML KDELDLDGRP NLNLASFVGT YMETHAEQLM FENISKNMSD ADEYPAMMQM
     HARCVSIISH LWGVQKGEKA IGSATTGSSE AIHLGGLAMK RRWQEKRTAA GKDTSKPNII
     MGSNAQVALE KFARYFEVEA RILPVTQKSN YRLDPELVKQ NIDENTIGIF VILGSTYTGH
     YEPVEEISQI LDAYEAETGV DIPIHVDAAS GGFVAPFTHA KAGGPKWNFE LPRVKSINTS
     GHKFGLVYAG VGWIIWRDET LLPKHLVFEL HYLGGTEESY TLNFSRPGAQ VIAQYYNLIH
     LGFSGYRQIM ENCMSNARLL SKSLEATGWY TCISDIHRKK GVFTFPGVSA AVFSKENETS
     ADYNAGLPVV AFRFSDEFKQ EFPHIKQVDV SNLMRAKQYI IPNYPLPPDE ESTEILRVVV
     RESMSFDLLD RLISDLCATT QGLIDNDKGD LSILGGARDN SAEKKHSSTG SQPHSKGQGH
     GGKRPMTEGV HRAVC
//
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