ID   G5EHP8_PYRO7            Unreviewed;       572 AA.
AC   G5EHP8;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 80.
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=MGCH7_ch7g572 {ECO:0000313|EMBL:EAQ71165.1}, MGG_02817
GN   {ECO:0000313|EMBL:EHA46178.1};
OS   Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Magnaporthe oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507 {ECO:0000313|EMBL:EAQ71165.1};
RN   [1] {ECO:0000313|EMBL:EHA46178.1, ECO:0000313|Proteomes:UP000009058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 {ECO:0000313|EMBL:EHA46178.1}, and 70-15 / ATCC MYA-4617
RC   / FGSC 8958 {ECO:0000313|Proteomes:UP000009058};
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M., Kulkarni R., Xu J.R., Pan H., Read N.D., Lee Y.H.,
RA   Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S., Soanes D.M.,
RA   Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M., Kim S.,
RA   Lebrun M.H., Bohnert H., Coughlan S., Butler J., Calvo S., Ma L.J.,
RA   Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
RN   [2] {ECO:0000313|EMBL:EAQ71165.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=70-15 {ECO:0000313|EMBL:EAQ71165.1};
RA   Thon M.R., Pan H., Diener A., Papalas J., Taro A., Mitchell T., Dean R.A.;
RT   "The sequence of Magnaporthe grisea chromosome 7.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EHA46178.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=70-15 {ECO:0000313|EMBL:EHA46178.1};
RA   Ma L.-J., Dean R.A., Gowda M., Nunes C., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Yandava C., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Magnaporthe oryzae 70-15.";
RL   Submitted (MAY-2011) 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}.
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DR   EMBL; CM000230; EAQ71165.1; -; Genomic_DNA.
DR   EMBL; CM001237; EHA46178.1; -; Genomic_DNA.
DR   RefSeq; XP_003720921.1; XM_003720873.1.
DR   STRING; 242507.G5EHP8; -.
DR   EnsemblFungi; MGG_02817T0; MGG_02817T0; MGG_02817.
DR   GeneID; 2682370; -.
DR   KEGG; mgr:MGG_02817; -.
DR   VEuPathDB; FungiDB:MGG_02817; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_3_1; -.
DR   OMA; KNIMQNC; -.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000009058; Chromosome 7.
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; 3.90.1150.160; -; 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:SF3; 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:UP000009058}.
FT   REGION          526..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..559
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         304
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   572 AA;  63947 MW;  99129F5A7637E6DC CRC64;
     MVLSRHVNPD DIVQHLHNSS LKEQDGDNDT RTQAAISHLT PYSSRYASNV SLPKYKLPKE
     GAEADTVYSM IRDELDLDGK PNLNLASFVG TYLEDNAQKL MVENIAKNLS DADEYPAMIS
     MQQRCVSILA HLWNVQKGEK AIGSATTGSS EAIQLGGLAM KRRWQEARRA AGKDDSKPNI
     IMGANAQVAL EKFARYFDVE ARILPVSEKS RYRLDADMVR DNIDENTIGI FIILGSTYTG
     HYEPIEEISE ILDKYQAETG HDIPIHVDGA SGAFIAPFTH AQAGGPKWDF SLPRVKSINT
     SGHKYGLVTA GVGWIVWRDE SFLPKHLIFE LHYLGGTEES YTLNFSRPGA QVITQYFNLV
     HLGFSGYRAI MENCLANARL LSKSLEATGW YTCVSDIHRR VETAGSNGSN GKQKEPEVTP
     EHAKETSADY VAGLPVVAFC FSDEFRRQFP HVKQETVSVL LRARQWIIPN YALPPNEEKT
     EILRVVVRES MSLDLLDRLL SDICEVTQKL MDEDELDLNV LQGSRHKGPC TKADVSKEGR
     AQAKKERDDR HKKHQATGRT GRMETGVHRS TC
//