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Database: UniProt/TrEMBL
Entry: S5VSK1_STRC3
LinkDB: S5VSK1_STRC3
Original site: S5VSK1_STRC3 
ID   S5VSK1_STRC3            Unreviewed;       468 AA.
AC   S5VSK1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   05-JUL-2017, entry version 32.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=B446_20640 {ECO:0000313|EMBL:AGS70940.1};
OS   Streptomyces collinus (strain DSM 40733 / Tu 365).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS70940.1, ECO:0000313|Proteomes:UP000015423};
RN   [1] {ECO:0000313|Proteomes:UP000015423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40733 / Tu 365 {ECO:0000313|Proteomes:UP000015423};
RA   Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA   Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT   "The complete genome sequence of Streptomyces collinus Tu 365.";
RL   Submitted (OCT-2012) 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; CP006259; AGS70940.1; -; Genomic_DNA.
DR   RefSeq; WP_020941396.1; NC_021985.1.
DR   EnsemblBacteria; AGS70940; AGS70940; B446_20640.
DR   GeneID; 32539380; -.
DR   KEGG; sci:B446_20640; -.
DR   PATRIC; fig|1214242.5.peg.4231; -.
DR   KO; K01580; -.
DR   OrthoDB; POG091H06F5; -.
DR   BioCyc; SCOL1214242:G13G0-4161-MONOMER; -.
DR   Proteomes; UP000015423; 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:UP000015423};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015423}.
FT   MOD_RES     281    281       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   468 AA;  52245 MW;  8C745545E16D03CA CRC64;
     MALHEGPEKH NERPMSVNPF FGQANPVAEM TQAPPKHRLP DSPLPPDTAA QLVHDELMLD
     GNSRLNLATF VTTWMEPQAG DLMAECRDKN MIDKDEYPRT AELERRCVAM LADLWNAPDP
     AAAVGCSTTG SSEACMLAGM ALKRRWAKRN ADRYPGARPN LVMGVNVQVC WEKFCNFWEV
     EARLVPMEGD RYHLDPQAAA ELCDENTIGV VGILGSTFDG SYEPIADLCA ALDALQERTG
     LDVPVHVDGA SGAMVAPFLD EDLVWDFRLP RVASINTSGH KYGLVYPGVG WALWRDGESL
     PEELVFRVNY LGGDMPTFAL NFSRPGAQVV AQYYTFLRLG REGYRAVQQT TRDVATELAD
     RIEALDDFRL LTRGDELPVF AFTTAPGVES YDVFDLSRRL RESGWLVPAY TFPPNREDLS
     VVRIVCRNGF SRDLADLFMD DLSRLLPELR RQPHPQTRDK AAATSFHH
//
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