ID   B4EWN7_PROMH            Unreviewed;       463 AA.
AC   B4EWN7;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 96.
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   Name=gadB {ECO:0000313|EMBL:CAR42970.1};
GN   OrderedLocusNames=PMI1407 {ECO:0000313|EMBL:CAR42970.1};
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507 {ECO:0000313|EMBL:CAR42970.1, ECO:0000313|Proteomes:UP000008319};
RN   [1] {ECO:0000313|EMBL:CAR42970.1, ECO:0000313|Proteomes:UP000008319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320 {ECO:0000313|EMBL:CAR42970.1,
RC   ECO:0000313|Proteomes:UP000008319};
RX   PubMed=18375554; DOI=10.1128/JB.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR42970.1; -; Genomic_DNA.
DR   RefSeq; WP_004243150.1; NC_010554.1.
DR   AlphaFoldDB; B4EWN7; -.
DR   EnsemblBacteria; CAR42970; CAR42970; PMI1407.
DR   GeneID; 6803402; -.
DR   KEGG; pmr:PMI1407; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_2_2_6; -.
DR   Proteomes; UP000008319; Chromosome.
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   MOD_RES         271
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   463 AA;  52232 MW;  BE390CE6A50CBF6A CRC64;
     MNKKTPSYSS LDDVYASVDL SQSLPKTHFP QQESHPRHVF DAVRDELMLD GNSRQNLATF
     CQTWVDDEIR DLMNLSIDKN MIDKDEYPQT AEIENRCVHM LADLWHSPDP LNTLGCSTIG
     SSEAAMLGGL ALKWQWRKKR LAAGKATDKP NLICGPVQVC WHKFARYFDV ELREIPLEGD
     RLMMSPEEVI KRVDENTIGV VPTLGVTFTC TYEPVKAVHD ALDQLQKETG LDIPIHVDGA
     SGGFLAPFCA PDLEWDFRLP RVKSINSSGH KFGLAPLGSG WVVWREAKDL PEELIFNVNY
     LGGNMPTFAL NFSRPGGQII AQYYNFLRLG REGYAKIHNA CYHTAQYLAR EIEKLGPFEM
     IFSGDSQKGI PALAWKLKKE AKVSYSLYDI ADKLRSRGWQ VPAYSMPADR QDLVIQRILV
     RHGVSLDLAT LLIEDMKRTL DYFEKHPVST PLSEEDGGGF NHS
//