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Database: UniProt/TrEMBL
Entry: G8PNP3_PSEUV
LinkDB: G8PNP3_PSEUV
Original site: G8PNP3_PSEUV 
ID   G8PNP3_PSEUV            Unreviewed;       458 AA.
AC   G8PNP3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   20-DEC-2017, entry version 36.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   Name=gadA {ECO:0000313|EMBL:AEV39535.1};
GN   OrderedLocusNames=PSE_5033 {ECO:0000313|EMBL:AEV39535.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV39535.1, ECO:0000313|Proteomes:UP000005634};
RN   [1] {ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA   Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile and
RT   symbiotically interacting bacteria.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; CP003147; AEV39535.1; -; Genomic_DNA.
DR   RefSeq; WP_014287232.1; NC_016642.1.
DR   STRING; 911045.PSE_5033; -.
DR   EnsemblBacteria; AEV39535; AEV39535; PSE_5033.
DR   KEGG; psf:PSE_5033; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; POG091H06F5; -.
DR   Proteomes; UP000005634; 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   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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005634};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:AEV39535.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005634}.
FT   MOD_RES     271    271       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   458 AA;  51724 MW;  B88FA91693D80021 CRC64;
     MPLWKTCASE SPDIYATARA VEGLAKARIP ETGVSPEEAY NLVRDELYLD GNARQNLATF
     CTTWVEDEVH KLMADCIDKN MIDKDEYPQT AEIEARCVHI IASLWNSPEA EETIGCSTTG
     SSEAAMLGGL ALKWAWRDRR KKEGKPHDKP NMVCGPVQVC WHKFAKYFDV ELRQIPLSEG
     SLHMRPEQLK DYVDENTICV VPTLGVTFTG VYEPVKEICQ ELDRLQTETG LDIPVHVDAA
     SGGFVAPFLH PELLWDFRLD RVKSINASGH KFGLAPLGVG WVIWRDKKEL PSDLVFNVDY
     LGGNMPTFAL NFSRPGGQIV IQYYNFMRLG WDGYRDIQSA CAENAQYLAE KLSELPELDI
     LYDGNGALPC VCYRLKHPDK AHYTLYDLSE RVRMNGWQIA SYPLPSDMED TVVQRVMIRH
     GVSHDAVEQL YLDIKKALNY LDKNNIKWSE AGPSFSHG
//
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