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Database: UniProt/TrEMBL
Entry: R9VPN2_9ENTR
LinkDB: R9VPN2_9ENTR
Original site: R9VPN2_9ENTR 
ID   R9VPN2_9ENTR            Unreviewed;       461 AA.
AC   R9VPN2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   05-JUL-2017, entry version 27.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=H650_09405 {ECO:0000313|EMBL:AGN85370.1};
OS   Enterobacter sp. R4-368.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=1166130 {ECO:0000313|EMBL:AGN85370.1, ECO:0000313|Proteomes:UP000014269};
RN   [1] {ECO:0000313|EMBL:AGN85370.1, ECO:0000313|Proteomes:UP000014269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R4-368 {ECO:0000313|EMBL:AGN85370.1};
RX   PubMed=23908287;
RA   Madhaiyan M., Peng N., Ji L.;
RT   "Complete Genome Sequence of Enterobacter sp. Strain R4-368, an
RT   Endophytic N-Fixing Gammaproteobacterium Isolated from Surface-
RT   Sterilized Roots of Jatropha curcas L.";
RL   Genome Announc. 1:e00544-13(2013).
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; CP005991; AGN85370.1; -; Genomic_DNA.
DR   RefSeq; WP_020454887.1; NC_021500.1.
DR   EnsemblBacteria; AGN85370; AGN85370; H650_09405.
DR   KEGG; enr:H650_09405; -.
DR   PATRIC; fig|1166130.5.peg.1760; -.
DR   KO; K01580; -.
DR   OrthoDB; POG091H06F5; -.
DR   BioCyc; ESP1166130:G135U-1744-MONOMER; -.
DR   Proteomes; UP000014269; 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   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000014269};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     268    268       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   461 AA;  51799 MW;  E4098F386EA3AE5C CRC64;
     MDEQYPGIDD IYASLELSSS LEKHQFPAKE RDPRNVFAAV RDELMLDGNS RQNLATFCQT
     WVDDEIRTLM DLSIDKNMID KDEYPQTAEI ESRCVHMLAD LWHSPEAQNT LGCSTIGSSE
     AAMLGGLALK WRWRKKQAAA GKPTDKPNLI CGPVQICWHK FARYFDVELR EIPLQGQRLV
     MNAEEVIKRV DENTIGVVPT MGVTFSCQYE PVKAVHDALD KLQQETGLDI PIHVDGASGG
     FLAPFCAPDI AWDFRLPRVK SINASGHKFG LAPLGAGWVV WREAADLPEE LIFNVNYLGG
     NMPTFALNFS RPGGQVIAQY YNFLRLGREG YTKIHHACYQ TAQYLAREID KLGPFKILFD
     GDSQQGIPAL AWTLRTERAI GGYTLYDLAD RLRSRGWQVP AYSMPAHRED LVIQRVLVRH
     GVSHDLASLL VDDIKRALDY FSRHPVINPL SAEEASGFNH A
//
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