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Database: UniProt/TrEMBL
Entry: D6B201_9ACTN
LinkDB: D6B201_9ACTN
Original site: D6B201_9ACTN 
ID   D6B201_9ACTN            Unreviewed;       474 AA.
AC   D6B201;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   25-APR-2018, entry version 55.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=SSHG_05799 {ECO:0000313|EMBL:EFE85357.2};
OS   Streptomyces albus J1074.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=457425 {ECO:0000313|EMBL:EFE85357.2, ECO:0000313|Proteomes:UP000005105};
RN   [1] {ECO:0000313|Proteomes:UP000005105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J1074 {ECO:0000313|Proteomes:UP000005105};
RA   Molnar K.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000005105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J1074 {ECO:0000313|Proteomes:UP000005105};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M.,
RA   Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z.,
RA   Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.D.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J.,
RA   Yandava C., Straight P., Clardy J., Hung D., Kolter R., Mekalanos J.,
RA   Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M., Galagan J.,
RA   Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces albus strain J1074.";
RL   Submitted (DEC-2008) 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; DS999645; EFE85357.2; -; Genomic_DNA.
DR   RefSeq; WP_003952231.1; NZ_DS999645.1.
DR   ProteinModelPortal; D6B201; -.
DR   STRING; 457425.SSHG_05799; -.
DR   EnsemblBacteria; EFE85357; EFE85357; SSHG_05799.
DR   KEGG; salb:XNR_0119; -.
DR   PATRIC; fig|457425.27.peg.126; -.
DR   eggNOG; COG0076; LUCA.
DR   KO; K01580; -.
DR   BioCyc; SALB457425:G1HGK-121-MONOMER; -.
DR   Proteomes; UP000005105; Unassembled WGS sequence.
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   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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:UP000005105};
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}.
FT   MOD_RES     281    281       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   474 AA;  52678 MW;  6EB259B1304F0E61 CRC64;
     MSAAGGETSD GARLSLNPFH LAADPAAAML SVPPVRRLSA HSLPPEVARR ILHDEVMLDG
     NARQNLATFV TTWMEPEGAA VMAECRDKNL IDKDEYPRTA EIERRCVAIL ADLWHAPDAD
     RAVGCSTTGS SEACMLAGMA MKRRWAHRHG DRYPASARPN LVMGINVQVC WEKFCDYWEV
     EPRMVPMEGE RFHLDPQAAA DLCDENTIGV VGILGSTYDG SYEPVQELCA ALDALQERTG
     WDVPVHVDGA SGAMVAPFLD PDLVWDFRLE RVVSINTSGH KYGLVYPGVG WAVWRSAEYL
     PDDLVFRVDY LGGTMPTFAL NFSRPGSQVA AQYYVFLRLG REGFRQVQQA GRDIATHLAH
     GIEELGDFRL LTRGDQLPAF AFTTGADVRA YDVFDVSRRL RETGWLVPAY TCPPHRQDLS
     VLRIVCRNGF TRDLADMLLH DLGRLLPELR RQSPHPGERP SPSTAFHHSA ERGR
//
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