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Database: UniProt/TrEMBL
Entry: E8WG52_STRFA
LinkDB: E8WG52_STRFA
Original site: E8WG52_STRFA 
ID   E8WG52_STRFA            Unreviewed;       474 AA.
AC   E8WG52;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   05-JUL-2017, entry version 43.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=Sfla_3455 {ECO:0000313|EMBL:ADW04875.1};
OS   Streptomyces pratensis (strain ATCC 33331 / IAF-45CD).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=591167 {ECO:0000313|EMBL:ADW04875.1, ECO:0000313|Proteomes:UP000002066};
RN   [1] {ECO:0000313|EMBL:ADW04875.1, ECO:0000313|Proteomes:UP000002066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33331 / DSM 40990 / IAF-45CD
RC   {ECO:0000313|Proteomes:UP000002066};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I.,
RA   Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Streptomyces flavogriseus ATCC
RT   33331.";
RL   Submitted (JAN-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; CP002475; ADW04875.1; -; Genomic_DNA.
DR   RefSeq; WP_014155495.1; NC_016114.1.
DR   ProteinModelPortal; E8WG52; -.
DR   STRING; 591167.Sfla_3455; -.
DR   EnsemblBacteria; ADW04875; ADW04875; Sfla_3455.
DR   KEGG; sfa:Sfla_3455; -.
DR   PATRIC; fig|591167.6.peg.3529; -.
DR   eggNOG; ENOG4105CVK; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; POG091H06F5; -.
DR   BioCyc; SPRA591167:G12Y5-3437-MONOMER; -.
DR   Proteomes; UP000002066; 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:UP000002066};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382, ECO:0000313|EMBL:ADW04875.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     287    287       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   474 AA;  52985 MW;  3F72C8988DC79935 CRC64;
     MALHQGRHGR PAPSEEHRRL ALNPFFGEAD PTAPMVAAPP THRLPEDPLP PSTAYRLVHD
     ELMLDGNSRL NLATFVTTWM EPQAGVLMSE CRDKNMIDKD EYPRTAELER RCVAMLADLW
     NAPDPASTVG CSTTGSSEAC MLAGMALKRR WSARNADRYP ATARPNLVMG VNVQVCWEKF
     CTFWEVEPRQ VPMDGERFHL DPQAAAELCD ENTIGVVGIL GSTFDGSYEP IADLCAALDD
     LQERTGLDIP VHVDGASGAM IAPFLDPDLV WDFRLPRVSS INTSGHKYGL VYPGVGWALW
     RSQAELPEEL VFRVNYLGGD MPTFALNFSR PGAQVVAQYY TFLRLGREGY RAVQQASRDI
     ARRLAVQFEA LEDFRLLTRG DELPVFAVTT KPDVQAYDVF DVSRRLRERG WLVPAYTFPA
     NRQDLSVLRV VCRNGFSSDL AELLLDDLRG LLPELRSQAH PLHRDPGVQT AFHH
//
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