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Database: UniProt/TrEMBL
Entry: D7CGC7_STRBB
LinkDB: D7CGC7_STRBB
Original site: D7CGC7_STRBB 
ID   D7CGC7_STRBB            Unreviewed;       474 AA.
AC   D7CGC7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   25-OCT-2017, entry version 44.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=SBI_05911 {ECO:0000313|EMBL:ADI09031.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI09031.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI09031.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI09031.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
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; CP002047; ADI09031.1; -; Genomic_DNA.
DR   RefSeq; WP_014178493.1; NC_016582.1.
DR   ProteinModelPortal; D7CGC7; -.
DR   STRING; 749414.SBI_05911; -.
DR   EnsemblBacteria; ADI09031; ADI09031; SBI_05911.
DR   KEGG; sbh:SBI_05911; -.
DR   PATRIC; fig|749414.3.peg.6095; -.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; POG091H06F5; -.
DR   BioCyc; SBIN749414:GHKA-5965-MONOMER; -.
DR   Proteomes; UP000000377; 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:UP000000377};
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:UP000000377}.
FT   MOD_RES     287    287       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   474 AA;  53236 MW;  5CDA608F8E9E1E2D CRC64;
     MTLHTGRHGK RDEGRRRRGV AVNPFYGVAD PVGGMADEVP RNRLPDGPMA PATACQLVHD
     ELMLDVNARL NLATFVTTWM EPQGDQVLFQ CRDKNLIDKD EYPRTAELER RCVAMLAHLW
     HAPEPDSVMG CSTTGSSEAC MLAGMAFKRR WAKRNPARYP GTARPNLVMG VNVQVCWEKF
     CNFWEVEARQ VPMEGDRFHL DPQAAADLCD ENTIGVVTVL GSTFDGSYEP VAEVCAALDD
     LQERTGLDIP VHVDGASGAM VAPFLDTDLV WDFRLPRVAS INTSGHKYGL VYPGVGWVLW
     RTTENLPKEL VFRVNYLGGE LPTFSLTFSR PGSQVAAQYY TFLRLGREGY RAVQQTTRDV
     ARSLAERIEA LGDFRLLTRG DELPVFAFTT AEGVRNFDVF DVSRRLREHN WLVPAYTFPP
     NRQDLSVLRV VCRNGFSADL SDLFLEDLET LLPELRSQPH PLDRPENLAT AFHH
//
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