ID   D5DEK8_PRIM3            Unreviewed;       467 AA.
AC   D5DEK8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 75.
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   OrderedLocusNames=BMD_2444 {ECO:0000313|EMBL:ADF39290.1};
OS   Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=592022 {ECO:0000313|EMBL:ADF39290.1, ECO:0000313|Proteomes:UP000002365};
RN   [1] {ECO:0000313|EMBL:ADF39290.1, ECO:0000313|Proteomes:UP000002365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 319 / IMG 1521 {ECO:0000313|Proteomes:UP000002365};
RX   PubMed=21705586; DOI=10.1128/JB.00449-11;
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Koenig S.S., Huot Creasy H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA   Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA   Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA   Bremer E., Jahn D., Ravel J., Vary P.S.;
RT   "Genome sequences of the biotechnologically important Bacillus megaterium
RT   strains QM B1551 and DSM319.";
RL   J. Bacteriol. 193:4199-4213(2011).
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|ARBA:ARBA00000018,
CC         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; CP001982; ADF39290.1; -; Genomic_DNA.
DR   RefSeq; WP_013083277.1; NZ_CP120609.1.
DR   AlphaFoldDB; D5DEK8; -.
DR   KEGG; bmd:BMD_2444; -.
DR   PATRIC; fig|592022.4.peg.2397; -.
DR   HOGENOM; CLU_019582_2_2_9; -.
DR   Proteomes; UP000002365; Chromosome.
DR   GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProt.
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   CDD; cd06450; DOPA_deC_like; 1.
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}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         279
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   467 AA;  53223 MW;  49F0BE982EB72805 CRC64;
     MPQWHPHREQ KNLPDEFPVN PLFSRQGEVT IPRLRISDQG MLPETAYQII HDEIALDGNA
     RLNLATFVTT WMEPDAKRLY GESFDKNMID KDEYPQTAAI EERCVRILAD LWNSPNPDTT
     MGVSTTGSSE ACMLGGLALK RRWQKLRKSK GLSTERPNIV FSSSVQVVWE KFANYWDVEP
     RYVNINADHP YLDPEGVIKA VDENTIGVVP ILGVTYTGVY EPIAAIAKAL DELQEKTGLD
     IPIHIDAASG GFIAPFLQPD LIWDFRLPRV KSINVSGHKY GLVYPGLGWV IWREKEDLPE
     DLIFRVSYLG GNMPTFALNF SRPGAQVLLQ YYNFLRLGKD GYYAVQKTSQ ENALFLSKEI
     GEMEAFEIIA DGSDIPVLAW KLKEGYTPNW TLYDLSRQLR TYGWQVPAYP LPADMEEITI
     MRIVVRNGFS RDLAHLFMVN FKQAVEFLNS LDRPVLKDTK YDNGFHH
//