ID   B5FDE3_ALIFM            Unreviewed;       464 AA.
AC   B5FDE3;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 91.
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   OrderedLocusNames=VFMJ11_1137 {ECO:0000313|EMBL:ACH65664.1};
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396 {ECO:0000313|EMBL:ACH65664.1, ECO:0000313|Proteomes:UP000001857};
RN   [1] {ECO:0000313|Proteomes:UP000001857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11 {ECO:0000313|Proteomes:UP000001857};
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACH65664.1, ECO:0000313|Proteomes:UP000001857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11 {ECO:0000313|EMBL:ACH65664.1,
RC   ECO:0000313|Proteomes:UP000001857};
RX   PubMed=19182778; DOI=10.1038/nature07660;
RA   Mandel M.J., Wollenberg M.S., Stabb E.V., Visick K.L., Ruby E.G.;
RT   "A single regulatory gene is sufficient to alter bacterial host range.";
RL   Nature 458:215-218(2009).
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; CP001139; ACH65664.1; -; Genomic_DNA.
DR   RefSeq; WP_011261695.1; NC_011184.1.
DR   AlphaFoldDB; B5FDE3; -.
DR   SMR; B5FDE3; -.
DR   GeneID; 77252299; -.
DR   KEGG; vfm:VFMJ11_1137; -.
DR   HOGENOM; CLU_019582_2_2_6; -.
DR   Proteomes; UP000001857; Chromosome I.
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         274
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   464 AA;  52582 MW;  51E50550E542FD6B CRC64;
     MPLHSKNAVR DDLLDDIYSS ADLSLSMPKY KMPEQEHDPR HAYQVIHDEL MMDGNSRQNL
     ATFCQTWVED EVHKLMDECI DKNMIDKDEY PQTAELESRC VHMLADLWNS PDAENTLGCS
     TTGSSEAAML GGMALKWAWR EKMKKLGKPT DKPNMICGPV QVCWHKFARY WDIELREIPM
     EGDRLIMTPE EVIKRCDENT IGVVPTLGVT FTCQYEPVKA VHEALDKLQE ETGLDIPMHI
     DAASGGFLAP FCDPDLEWDF RLPRVKSINA SGHKFGLSPL GVGWVIWRDA SALHEDLIFN
     VNYLGGNMPT FALNFSRPGG QIVAQYYNFL RLGKEGYRKI HQACYDTAVY LSSEIEKLGM
     FEIIYDGKGG IPAMSWSLKE GVDPGFNLFD LSDRIRSRGW QIAAYAMPPK REDLVIMRIL
     VRHGFSRDQA DLLVADLKHC VEFFAKHPIS HGSDELESSG FNHG
//