ID   A1JR00_YERE8            Unreviewed;       466 AA.
AC   A1JR00;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 99.
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=gadA {ECO:0000313|EMBL:CAL13720.1};
GN   Synonyms=gadS {ECO:0000313|EMBL:CAL13720.1};
GN   OrderedLocusNames=YE3693 {ECO:0000313|EMBL:CAL13720.1};
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305 {ECO:0000313|EMBL:CAL13720.1, ECO:0000313|Proteomes:UP000000642};
RN   [1] {ECO:0000313|EMBL:CAL13720.1, ECO:0000313|Proteomes:UP000000642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081 {ECO:0000313|Proteomes:UP000000642};
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(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; AM286415; CAL13720.1; -; Genomic_DNA.
DR   RefSeq; WP_011817231.1; NC_008800.1.
DR   RefSeq; YP_001007848.1; NC_008800.1.
DR   AlphaFoldDB; A1JR00; -.
DR   KEGG; yen:YE3693; -.
DR   PATRIC; fig|393305.7.peg.3933; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_019582_0_1_6; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000000642; 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         276
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   466 AA;  52486 MW;  E9AD51E2773B30B6 CRC64;
     MTRKSLDDYR SDLLDSRFGS KAIRNISENK VFPKEEMRED IAFQIISDEL FLDGNARQNL
     ATFCQTWDDD NVHKLMDLSI NKNWIDKEEY PQSAAIDMRC VNMMADLWNA PTPKGAQGVG
     TNTIGSSEAC MLGGMAMKWR WRKKMEAAGK PTNKPNFVCG PVQVCWHKFA RYWEVEIREI
     PMIPGQLFMD PQRMIEACDE NTIGVVPTFG VTYTGNYELP KPLHDALDKL QKDTGLDIDM
     HIDAASGGFL APFVAPDIEW DFRLPRVKSI STSGHKFGLA PLGCGWVIWR DAAALPEELI
     FNVDYLGGQV GTFAINFSRP TGQVISQYYE FIRLGREGYT KVQSACYQVA EFLAKEIAPL
     GPYEFYCSGG PYEGIPAICF RIKKGAKAGY TLYDLSERLR LRGWQVPAFT LSGKMSDVVV
     MRIMCRRGFE MDFAGLLLDD FKSSLKYLSE HPSLGGEASQ NSFSHT
//