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Database: UniProt/TrEMBL
Entry: E3RIY7_PYRTT
LinkDB: E3RIY7_PYRTT
Original site: E3RIY7_PYRTT 
ID   E3RIY7_PYRTT            Unreviewed;       524 AA.
AC   E3RIY7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   20-DEC-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_08052 {ECO:0000313|EMBL:EFQ94305.1};
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:EFQ94305.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ94305.1,
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:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; GL533400; EFQ94305.1; -; Genomic_DNA.
DR   RefSeq; XP_003297592.1; XM_003297544.1.
DR   STRING; 861557.XP_003297592.1; -.
DR   EnsemblFungi; EFQ94305; EFQ94305; PTT_08052.
DR   GeneID; 10516083; -.
DR   KEGG; pte:PTT_08052; -.
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:0006536; P:glutamate metabolic process; IEA:InterPro.
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:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001067}.
FT   MOD_RES     300    300       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   524 AA;  59095 MW;  BD343B67D978AD61 CRC64;
     MVHINRVATS KEITEEKAQF EEISASTTIN LSPEDEADDY TATVYGSKYA AEDLPRHEMP
     DREMPPSIAY RLIKDDLTLD GTPTLNLASF VTTYMEDEAE KLMVDAFSKN FIDYEEYPVS
     ADIQNRCVSM IAKLFHAPAD ADANTIGTST IGSSEAIMLG VLAMKKLWQN KRKAEGKPFD
     KPNMIMNSAV QVCWEKACRY FDIEEKYVYC TTDRYVIDPK ECVDLCDENT IGICAILGTT
     YTGEYEDIKA INDLLVERDI DVNIHVDAAS GGFVAPFVNP DLLWDFRLPK VTTINVSGHK
     YGLVYPGVGW VVWRDPAHLP QELVFTINYL GADQASFTLN FSRGASQIIG QYYQLIRLGK
     RGYRRIMLNL TRISDYLAAN LESLGFVIMS QRGGQGLPLV ACRIDEDLGK MYDEFAIAHQ
     LRERGWVVPA YTMAPHSEKM KMLRVVVRED FTKSRCDALI ADFKLALQTL DALDAKKIED
     QKQHAFAMRR RSTLVSPIFK KNAADHFDEE HSLQAKTGKT HAVC
//
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