ID   Q1RBS9_ECOUT            Unreviewed;       489 AA.
AC   Q1RBS9;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
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:ABE07185.1};
GN   OrderedLocusNames=UTI89_C1707 {ECO:0000313|EMBL:ABE07185.1};
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE07185.1, ECO:0000313|Proteomes:UP000001952};
RN   [1] {ECO:0000313|EMBL:ABE07185.1, ECO:0000313|Proteomes:UP000001952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC {ECO:0000313|Proteomes:UP000001952};
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE07185.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1RBS9; -.
DR   KEGG; eci:UTI89_C1707; -.
DR   HOGENOM; CLU_019582_2_1_6; -.
DR   Proteomes; UP000001952; 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   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         299
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   489 AA;  55440 MW;  D885B97966EBCAF7 CRC64;
     MHLLTLSINP TFLMRSNHFK EFKMDKKQVT DLRSELLDSR FGAKSISTIA ESKRFPLHEM
     RDDVAFQIIN DELYLDGNAR QNLATFCQTW DDDNVHKLMD LSINKNWIDK EEYPQSAAID
     LRCVNMVADL WHAPAPKNGQ AVGTNTIGSS EACMLGGMAM KWRWRKRMEA AGKPTNKPNL
     VCGPVQICWH KFARYWDVEL REIPMRPGQL FMDPKRMIEA CDENTIGVVP TFGVTYTGNY
     EFPQPLHDAL DKFQADTGID IDMHIDAASG GFLAPFVAPD IVWDFRLPRV KSISASGHKF
     GLAPLGCGWV IWRDEEALPQ ELVFNVDYLG GQIGTFAINF SRPAGQVIAQ YYEFLRLGRE
     GYTKVQNASY QVAAYLADEI AKLGPYEFIC TGRPDEGIPA VCFKLKDGED PGYTLYDLSE
     RLRLRGWQVP AFTLGGEATD IVVMRIMCRR GFEMDFAELL LEDYKASLKY LSDHPKLQGI
     AQQNSFKHT
//