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Database: UniProt/TrEMBL
Entry: E3RMN0_PYRTT
LinkDB: E3RMN0_PYRTT
Original site: E3RMN0_PYRTT 
ID   E3RMN0_PYRTT            Unreviewed;       548 AA.
AC   E3RMN0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   25-OCT-2017, entry version 35.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=PTT_09720 {ECO:0000313|EMBL:EFQ93027.1};
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Pleosporaceae; Pyrenophora.
OX   NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN   [1] {ECO:0000313|EMBL:EFQ93027.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ93027.1,
RC   ECO:0000313|Proteomes:UP000001067};
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F.,
RA   Moffat C.S., Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora
RT   teres f. teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
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; GL534021; EFQ93027.1; -; Genomic_DNA.
DR   RefSeq; XP_003298885.1; XM_003298837.1.
DR   STRING; 861557.XP_003298885.1; -.
DR   EnsemblFungi; EFQ93027; EFQ93027; PTT_09720.
DR   GeneID; 10523338; -.
DR   KEGG; pte:PTT_09720; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000001067; 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:UP000001067};
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:UP000001067}.
FT   MOD_RES     301    301       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   548 AA;  61188 MW;  19D60AE9FFB824E2 CRC64;
     MAGLARHVDT DELLKTLQDH PMHKAGGHHA SRATSHITPY SSRYAAGVEL SKFKIPHDGA
     PADVVHQLLK DELDLDGRPS LNLASFVGTY MEKEAEQLMI ENLSKNMSDA DEYPAMMDMH
     ARCVSIIANM WGAQKGEKAI GSATTGSSEA IHLGGLAMKR RWQEKRQAEG KDTSKPNIIM
     GANAQVALEK FARYFEVEAR ILPVSEESSY RLDPKLVKEN IDENTIGIFV ILGSTYTGHY
     EPVEEISDIL DAFEKETGND IPIHVDAASG GFIAPFTHAK AGKKWNFELP RVKSINTSGH
     KFGLVYAGVG WIIWRDESYL PKHLIFELHY LGGTEESYTL NFSRPGAQII AQYYNLIHLG
     FSGYRGIMEN TLANARLLSR ALEHTGWYRC VSDIHRKKGD FKYEKGKKQY DEGETSADYN
     AGLPVVAFTL TDDFHKEFPH VKQEAVSNLL RAKQYIIPNY PLPPGEEKTE ILRVVVRESL
     SLDMIDRLVT DICGVTEMLM KTDAVDLAAF QPGASPSIEK QHANKGLKKE HKHKAQRPSS
     DGVYRTVC
//
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