ID A0A0Q0X4G7_9PSED Unreviewed; 465 AA.
AC A0A0Q0X4G7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ORFNames=AQS70_06445 {ECO:0000313|EMBL:KQB54807.1};
OS Pseudomonas endophytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1563157 {ECO:0000313|EMBL:KQB54807.1, ECO:0000313|Proteomes:UP000050342};
RN [1] {ECO:0000313|EMBL:KQB54807.1, ECO:0000313|Proteomes:UP000050342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSTT44 {ECO:0000313|EMBL:KQB54807.1,
RC ECO:0000313|Proteomes:UP000050342};
RA Von Neubeck M., Huptas C., Wenning M., Scherer S.;
RT "Pseudomonas helleri sp. nov. and Pseudomonas weihenstephanensis sp. nov.,
RT isolated from raw cows milk.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQB54807.1}.
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DR EMBL; LLWH01000046; KQB54807.1; -; Genomic_DNA.
DR RefSeq; WP_055101757.1; NZ_LLWH01000046.1.
DR AlphaFoldDB; A0A0Q0X4G7; -.
DR STRING; 1563157.AQS70_06445; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000050342; Unassembled WGS sequence.
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 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 272
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 465 AA; 52158 MW; 07ADE86DBD139BFC CRC64;
MALHRVKRHC ATDPIFGSST LDHAAAIKRF PESEQAASEV YQLVHDELYL DGNSRQNLAT
FCQTWEEDEV HKLMDLSIDK NMIDKDEYPQ SAELESRCIH MLADLWHAPD AANTLGTSTV
GSSEACMLGG LAALWRWRAA RKAAGKSTST PNMVCGPVQV CWHKFARYWD VEIREVPMSE
GHWFMTPEDL DGRVDENTIV VVPTFGQTFT GLYETVKPLS DALDELEKRT GLSVDIHVDG
ASGAFLAPFC APEVLWDFRV ARVKSISTSG HKFGLAPLGA GWVVWRDIKD LPEGLIFHVN
YLGGDMPTFA LNFSRPAGQI IAQYYNFLRL GREGYERIHS ECYATAQFLA RELVKIGPFE
MLFSGDPKLG IPALTWRLKP GAQTNYTLYD LADRLRIRGW LVPAYSLPAN VEDIVVQRIL
VRQGLSIDMA KLLLEDFARN VKFFEDHEPH GFKGREAEAG NHAGR
//
