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Database: UniProt/TrEMBL
Entry: W0L9S7_9GAMM
LinkDB: W0L9S7_9GAMM
Original site: W0L9S7_9GAMM 
ID   W0L9S7_9GAMM            Unreviewed;       466 AA.
AC   W0L9S7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   25-OCT-2017, entry version 26.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=Z042_13770 {ECO:0000313|EMBL:AHG20573.1};
OS   Chania multitudinisentens RB-25.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Chania.
OX   NCBI_TaxID=1441930 {ECO:0000313|EMBL:AHG20573.1, ECO:0000313|Proteomes:UP000019030};
RN   [1] {ECO:0000313|EMBL:AHG20573.1, ECO:0000313|Proteomes:UP000019030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RB-25 {ECO:0000313|EMBL:AHG20573.1,
RC   ECO:0000313|Proteomes:UP000019030};
RA   Robson E.H.J.;
RT   "Isolation of Serratia multitudinisentens RB-25 from Ex-Landfill
RT   site.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AHG20573.1, ECO:0000313|Proteomes:UP000019030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RB-25 {ECO:0000313|EMBL:AHG20573.1,
RC   ECO:0000313|Proteomes:UP000019030};
RA   Chan K.-G.;
RL   Submitted (MAR-2015) 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:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; CP007044; AHG20573.1; -; Genomic_DNA.
DR   RefSeq; WP_024912750.1; NZ_JAJC01000019.1.
DR   EnsemblBacteria; AHG20573; AHG20573; Z042_13770.
DR   GeneID; 32579202; -.
DR   KEGG; sfo:Z042_13770; -.
DR   PATRIC; fig|1441930.4.peg.2731; -.
DR   KO; K01580; -.
DR   Proteomes; UP000019030; 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:UP000019030};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019030}.
FT   MOD_RES     273    273       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   466 AA;  52320 MW;  100919F368DC31A0 CRC64;
     MDKTNVFTNY NENDDVYASI DLAKSMPKSV FPAEERNPRN VFNAIRDELM LDGNSRQNLA
     TFCQTWVDDE IRELMDLSID KNMIDKDEYP QTAEIEARCV RMLADLWNSP TPETTLGCST
     IGSSEAAMLG GLALKWQWRK KRAEQGLTAD KPNLICGPVQ ICWHKFARYF DVELREIPLE
     GDRLIMSPEE VLKRVDENTI GVVPTLGVTF TCQYEPVKAV SDALDKLQNE TGLDIPMHVD
     GASGGFLAPF CVPELEWDFR LPRVKSINTS GHKFGLAPLG AGWIVWREVS DLPEELIFNV
     NYLGGNMPTF ALNFSRPGGQ IVAQYYNFLR LGREGYAKIH NACYATAQYL AEEIGKIGPF
     EILFDGDSSK GIPALAWKLK DNAALGGYNL YDLADKLRSR GWQVPAYSMP AHREDLVIQR
     ILVRHGVSYD LGCLLIDDIK RALDYFANHP VTHPLSEEEA SGFNHG
//
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