ID   C7LHI0_BRUMC            Unreviewed;       472 AA.
AC   C7LHI0;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
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:ACU49468.1};
GN   OrderedLocusNames=BMI_II334 {ECO:0000313|EMBL:ACU49468.1};
OS   Brucella microti (strain CCM 4915).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=568815 {ECO:0000313|EMBL:ACU49468.1, ECO:0000313|Proteomes:UP000002188};
RN   [1] {ECO:0000313|EMBL:ACU49468.1, ECO:0000313|Proteomes:UP000002188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 4915 {ECO:0000313|EMBL:ACU49468.1,
RC   ECO:0000313|Proteomes:UP000002188};
RX   PubMed=19653890; DOI=10.1186/1471-2164-10-352;
RA   Audic S., Lescot M., Claverie J.-M., Scholz H.C.;
RT   "Brucella microti: the genome sequence of an emerging pathogen.";
RL   BMC Genomics 10:352-352(2009).
CC   -!- FUNCTION: Converts glutamate to gamma-aminobutyrate (GABA), consuming
CC       one intracellular proton in the reaction. The gad system helps to
CC       maintain a near-neutral intracellular pH when cells are exposed to
CC       extremely acidic conditions. The ability to survive transit through the
CC       acidic conditions of the stomach is essential for successful
CC       colonization of the mammalian host by commensal and pathogenic
CC       bacteria. {ECO:0000256|ARBA:ARBA00024984}.
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; CP001579; ACU49468.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7LHI0; -.
DR   KEGG; bmr:BMI_II334; -.
DR   HOGENOM; CLU_019582_0_1_5; -.
DR   BRENDA; 4.1.1.15; 15849.
DR   Proteomes; UP000002188; Chromosome 2.
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   InterPro; IPR021115; Pyridoxal-P_BS.
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.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 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         281
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   472 AA;  53112 MW;  366F30DCCA81D455 CRC64;
     MKITLEVIMT GSNYPARDLI ASVFGTEALQ EIAASRGFPE KEMQANAVYQ IIHDELFLDG
     NARQNLATFC QTWDDDYVHK LMDLSINKNW IDKEEYPQSA AIDLRCVNMV ADLWNAPKFA
     DNATGTNTIG SSEACMLGGM AMKWRWRKKM QEMGKPTDKP NFVCGPVQVC WHKFARYWDV
     EIREIPMEPG RLFMGPEQML EAVDENTIGV VPTFGVTYTG NYEFPEPLQD ALDKLQKTKG
     LDIDIHVDAA SGGFLAPFCA PDIPWDFRLP RVKSISASGH KYGLAPLGCG WVVWRDKEAL
     PEELIFNVDY LGGQVGTFAI NFSRPAGQVI SQYYEFMRLG REGYTKVQQA AYRVAQYIAR
     EIEPLGPYEF ICAGEEKGGI PAVCFRIREG EDPGYSLYDL SERLRLTGWQ VPAFALSGKA
     SDITVMRVMC RRGFEMDLAA LFIRDFKAGI EFFKSHPSPK ITPSMGTGFH HT
//