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Database: UniProt/SWISS-PROT
Entry: GADA_VIBF1
LinkDB: GADA_VIBF1
Original site: GADA_VIBF1 
ID   GADA_VIBF1              Reviewed;         464 AA.
AC   Q5E5Y7;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-OCT-2017, entry version 85.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000303|PubMed:28446608};
DE            EC=4.1.1.15 {ECO:0000269|PubMed:28446608};
GN   Name=gadA {ECO:0000303|PubMed:28446608};
GN   OrderedLocusNames=VF_1064 {ECO:0000312|EMBL:AAW85559.1};
OS   Vibrio fischeri (strain ATCC 700601 / ES114).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium
RT   with pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=28446608; DOI=10.1074/jbc.M116.763193;
RA   Pan S., Nikolakakis K., Adamczyk P.A., Pan M., Ruby E.G., Reed J.L.;
RT   "Model-enabled gene search (MEGS) allows fast and direct discovery of
RT   enzymatic and transport gene functions in the marine bacterium Vibrio
RT   fischeri.";
RL   J. Biol. Chem. 292:10250-10261(2017).
CC   -!- FUNCTION: Catalyzes the pyridoxal-dependent decarboxylation of
CC       glutamate to produce 4-aminobutanoate. Has weak activity with
CC       aspartate, but cannot complement an E. coli panD deletion mutant.
CC       {ECO:0000269|PubMed:28446608}.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000269|PubMed:28446608}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:28446608};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=61.7 mM for glutamate (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:28446608};
CC         Note=kcat is 0.055 sec(-1) at 37 degrees Celsius.
CC         {ECO:0000269|PubMed:28446608};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
DR   EMBL; CP000020; AAW85559.1; -; Genomic_DNA.
DR   RefSeq; WP_011261695.1; NC_006840.2.
DR   RefSeq; YP_204447.1; NC_006840.2.
DR   ProteinModelPortal; Q5E5Y7; -.
DR   SMR; Q5E5Y7; -.
DR   STRING; 312309.VF_1064; -.
DR   EnsemblBacteria; AAW85559; AAW85559; VF_1064.
DR   GeneID; 3278475; -.
DR   KEGG; vfi:VF_1064; -.
DR   PATRIC; fig|312309.11.peg.1067; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; YTGRLFT; -.
DR   OrthoDB; POG091H06F5; -.
DR   Proteomes; UP000000537; Chromosome I.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IDA:UniProtKB.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Decarboxylase; Lyase; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    464       Glutamate decarboxylase.
FT                                /FTId=PRO_0000440873.
FT   MOD_RES     274    274       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250|UniProtKB:P80041}.
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
//
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