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Database: UniProt
Entry: A0A0F6A227_9GAMM
LinkDB: A0A0F6A227_9GAMM
Original site: A0A0F6A227_9GAMM 
ID   A0A0F6A227_9GAMM        Unreviewed;       459 AA.
AC   A0A0F6A227;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=RN22_02610 {ECO:0000313|EMBL:KKD62061.1};
OS   Grimontia sp. AD028.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Grimontia.
OX   NCBI_TaxID=1581149 {ECO:0000313|EMBL:KKD62061.1, ECO:0000313|Proteomes:UP000033732};
RN   [1] {ECO:0000313|EMBL:KKD62061.1, ECO:0000313|Proteomes:UP000033732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD028 {ECO:0000313|EMBL:KKD62061.1,
RC   ECO:0000313|Proteomes:UP000033732};
RA   Adrian T.-G.-S., Chan K.-G.;
RT   "Genome sequencing of Grimontia sp. AD028.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKD62061.1}.
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DR   EMBL; LASY01000009; KKD62061.1; -; Genomic_DNA.
DR   RefSeq; WP_046302972.1; NZ_LASY01000009.1.
DR   AlphaFoldDB; A0A0F6A227; -.
DR   PATRIC; fig|1581149.3.peg.4827; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000033732; 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   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         273
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   459 AA;  51619 MW;  947D18CED101BE0E CRC64;
     MGLHFTNKQD PEIEDIYEEA LSQTQLPKYS LPQQSQSPEL IAQLLKDELL MDGNARQNLA
     TFCSTWMEPS VHDLMDVCID KNMIDKDEYP QTAEIEARCV HILAKLWNSP ESDTTVGCST
     TGSSEAAILG GLAMKWNWRA KREAQGKPAD KPNIVCGPVQ ICWHKFARYF DVEMREIPLD
     GDEVCMNPDK LSEYVDENTI GVVPTLGVTY TCVFEPVETI SKKLDELQAE TGLDIPIHVD
     GASGGFIAPF VSPELKWDFR LPRVVSINSS GHKYGLAPLG VGWVVWRDKQ HLPEDLVFNV
     DYLGGNMPTF ALNFSRPGGQ IVAQYYNFLR LGFDGYKGIQ TTCLKTAQWL ADEIAKIGPF
     DLFYDGRGGL PALSYSLNEG DWGFTLYDLS DRMRMRGWQI ASYPLPGNRQ DTVIQRIMIR
     HGVSKDMVAL LLEDLKRCVD YFKQYPQVHS GATSTFHHG
//
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