ID   G4MR06_PYRO7            Unreviewed;       517 AA.
AC   G4MR06;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
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=MGG_02378 {ECO:0000313|EMBL:EHA56541.1};
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:EHA56541.1, ECO:0000313|Proteomes:UP000009058};
RN   [1] {ECO:0000313|EMBL:EHA56541.1, ECO:0000313|Proteomes:UP000009058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958
RC   {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]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=70-15;
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Yandava C., Wortman J., 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; CM001231; EHA56541.1; -; Genomic_DNA.
DR   RefSeq; XP_003709153.1; XM_003709105.1.
DR   AlphaFoldDB; G4MR06; -.
DR   STRING; 242507.G4MR06; -.
DR   EnsemblFungi; MGG_02378T0; MGG_02378T0; MGG_02378.
DR   GeneID; 2681475; -.
DR   KEGG; mgr:MGG_02378; -.
DR   VEuPathDB; FungiDB:MGG_02378; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_2_1; -.
DR   InParanoid; G4MR06; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000009058; Chromosome 1.
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:UP000009058}.
FT   REGION          485..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..517
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         297
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   517 AA;  58105 MW;  AD629BBD28201B89 CRC64;
     MVHLTSIPSH EEADDKIVSG VKKVHLQLAN DEDKFTTSVY GSRFAIDDLP KHEMAENEMP
     KEVAYRMIKD ELSLDGNPML NLASFVTTYM EEEAEKLMAD SFSKNFIDYE EYPQSADIQN
     RCVAMIGRLF NAPVGASEGV GAVGTSCVGS SEAIMLAVLA MKKRWKNKRL AEGKSVDKPN
     LIMSSAVQVC WEKATRYFEV EEKLVYCSPD RYVIDPKETV DLVDENTIGI CVILGTTYTG
     EYEDVRAVND LLNERGLETP IHVDAASGGF VAPFVVPDLE WDFRCDRVVS INVSGHKYGL
     VYPGVGWVVW RSAEFLPQEL VFNINYLGAD QASFTLNFSK GASQVIGQYY QLIRLGKHGY
     RAIMSNLTRT ADYLSDSLEA LGFGIMSKKS GEGLPLVAFR LTPDEDRIYD EFAIAHQLRV
     RGWVVPAYTM APHTENLKML RVVVREDFTR NRCDALIADV KLSLELLNQM DKKELERHQD
     VIHKHGTHSG KASHNHPRFR KEKHSLQGKH GKTHAVC
//