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Database: UniProt/TrEMBL
Entry: F8JMG5_STREN
LinkDB: F8JMG5_STREN
Original site: F8JMG5_STREN 
ID   F8JMG5_STREN            Unreviewed;       480 AA.
AC   F8JMG5; G8XET4;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   05-JUL-2017, entry version 45.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=SCATT_p11640 {ECO:0000313|EMBL:AEW99357.1};
OS   Streptomyces cattleya (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC
OS   14057 / NRRL 8057).
OG   Plasmid pSCATT {ECO:0000313|EMBL:AEW99357.1,
OG   ECO:0000313|Proteomes:UP000007842}.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW99357.1, ECO:0000313|Proteomes:UP000007842};
RN   [1] {ECO:0000313|Proteomes:UP000007842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057
RC   {ECO:0000313|Proteomes:UP000007842};
RC   PLASMID=Plasmid pSCATT {ECO:0000313|Proteomes:UP000007842};
RA   Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT   "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL   Submitted (DEC-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; CP003229; AEW99357.1; -; Genomic_DNA.
DR   RefSeq; WP_014151032.1; NC_017585.1.
DR   EnsemblBacteria; AEW99357; AEW99357; SCATT_p11640.
DR   KEGG; sct:SCAT_p0577; -.
DR   KEGG; scy:SCATT_p11640; -.
DR   PATRIC; fig|1003195.11.peg.556; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   Proteomes; UP000007842; Plasmid pSCATT.
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:UP000007842};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Plasmid {ECO:0000313|EMBL:AEW99357.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007842}.
FT   MOD_RES     281    281       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   480 AA;  53668 MW;  670102E8D3C43C47 CRC64;
     MPLKHPHHQA DHPGHGNRDI EVNPIFAREP LSVPRYALPS GEMEPETAYQ LVHDELMLDG
     NARLNLATFV STWAEPAALR LMSECAEKNM IDKDEYPQTA ELENRCVHML ARLWHAPDPR
     HAVGCSTTGS SEAAMLGGLA LKRRWQHRRR AEGKPADRPN LVMGVNVQIC WEKFADYFEV
     EPRYVPMEGD RFHLDARHAV ELCDENTIGV VAVLGSTFDG SYEPVAEIAA ALDDLQRRTG
     LDVPVHVDGA SGGMIAPFLD PDLEWDFRLP RVASINTSGH KYGLVMPGVG WALWRDADAL
     PDDLVFHVNY LGGDMPTFAL NFSRPGAQVV AQYYNFLRLG FDGYRRVQQT CRDVATSLAA
     RIAELGPFEL ITDGSDIPVF AFRVRDEVDN FTVFDVSAAL RERGWLVPAY TFPKNRTDLA
     VLRIVVRNGF SHDLADLLLA DLRRVLPRLE KQPGPYRSEE DAGGFAHGAE TKNPRHPGRH
//
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