ID   E1WKP2_BACF6            Unreviewed;       480 AA.
AC   E1WKP2;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
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:CBW21055.1};
GN   OrderedLocusNames=BF638R_0459 {ECO:0000313|EMBL:CBW21055.1};
OS   Bacteroides fragilis (strain 638R).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=862962 {ECO:0000313|EMBL:CBW21055.1, ECO:0000313|Proteomes:UP000008560};
RN   [1] {ECO:0000313|EMBL:CBW21055.1, ECO:0000313|Proteomes:UP000008560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638R {ECO:0000313|EMBL:CBW21055.1,
RC   ECO:0000313|Proteomes:UP000008560};
RX   PubMed=20829291; DOI=10.1099/mic.0.042978-0;
RA   Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., Bertalan M.,
RA   Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., Bignell A.,
RA   Barron A., Clark L., Bentley S.D., Parkhill J.;
RT   "Twenty-eight divergent polysaccharide loci specifying within- and amongst-
RT   strain capsule diversity in three strains of Bacteroides fragilis.";
RL   Microbiology 156:3255-3269(2010).
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; FQ312004; CBW21055.1; -; Genomic_DNA.
DR   RefSeq; WP_005784276.1; NC_016776.1.
DR   AlphaFoldDB; E1WKP2; -.
DR   GeneID; 66330502; -.
DR   KEGG; bfg:BF638R_0459; -.
DR   PATRIC; fig|862962.3.peg.471; -.
DR   HOGENOM; CLU_019582_2_2_10; -.
DR   Proteomes; UP000008560; 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         274
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   480 AA;  54594 MW;  2D028490E1BA5B09 CRC64;
     MEDLNFRKGD AKTEAFGSNR MLQPSPVEKI PDGPTTPEIA YQMVKDETFA QTQPRLNLAT
     FVTTYMDDYA TKLMNEAINI NYIDETEYPR IAVMNGKCIN IVANLWNSPE KDTWKTGALA
     IGSSEACMLG GVAAWLRWRK KRQAQGKPFD KPNFVISTGF QVVWEKFAQL WQIEMRQVPL
     TLDKTTLDPE EALKMCDENT ICVVPIQGVT WTGLNDDVEA LDKALDAYNA KTGYDIPIHV
     DAASGGFILP FLYPDTKWDF RLKWVLSISV SGHKFGLVYP GLGWVVWKGK EYLPEEMAFS
     VNYLGANITQ VGLNFSRPAA QILGQYYQFI RLGFQGYKEV QYNSLQIAKY IHSQIAKMTP
     FVNYSEDVVN PLFIWYMKPE YAKNAKWTLY DLQDKLAQHG WMVPAYTLPA KLQDYVVMRV
     VVRQGFSRDM ADMLLGDIKN AIAELEKLEY PTSTRIAQEK NLPVEAKVFN HTGKPQAAKK
//