(data stored in SCRATCH zone)

SWISSPROT: B1VQ99_STRGG

ID   B1VQ99_STRGG            Unreviewed;       446 AA.
AC   B1VQ99;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   07-JUN-2017, entry version 58.
DE   RecName: Full=Beta-glucosidase {ECO:0000256|RuleBase:RU361175};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361175};
GN   OrderedLocusNames=SGR_371 {ECO:0000313|EMBL:BAG17200.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17200.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG17200.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism
RT   Streptomyces griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D-
CC       glucosyl residues with release of beta-D-glucose.
CC       {ECO:0000256|RuleBase:RU361175}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|RuleBase:RU361175}.
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DR   EMBL; AP009493; BAG17200.1; -; Genomic_DNA.
DR   RefSeq; WP_012377740.1; NC_010572.1.
DR   ProteinModelPortal; B1VQ99; -.
DR   STRING; 455632.SGR_371; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   EnsemblBacteria; BAG17200; BAG17200; SGR_371.
DR   GeneID; 6215180; -.
DR   KEGG; sgr:SGR_371; -.
DR   PATRIC; fig|455632.4.peg.350; -.
DR   eggNOG; ENOG4105CS2; Bacteria.
DR   eggNOG; COG2723; LUCA.
DR   HOGENOM; HOG000088630; -.
DR   KO; K05350; -.
DR   OMA; IHREYNA; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:InterPro.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   TIGRFAMs; TIGR03356; BGL; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1VQ99.
DR   SWISS-2DPAGE; B1VQ99.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001685};
KW   Glycosidase {ECO:0000256|RuleBase:RU361175};
KW   Hydrolase {ECO:0000256|RuleBase:RU361175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001685}.
SQ   SEQUENCE   446 AA;  49777 MW;  B3F0C135B29F7EFA CRC64;
     MTLNHLPADF VWGASTASYQ VEGATREDGR GPSIWDTFTA RPGAIRDGHT GEAACDHYHR
     YEQDLDLMAE AGLTGYRFSI AWPRIQPSGS GAANTKGLDF YDRLVDGLLA RGIEPVPTLF
     HWDLPQALED EGGWLNRDTA HRFAEYAAIT ADRLGDRVRT WITLNEPFIH MVWGYGLGTH
     APGRTLFLDC LPVAHHQLLG HGLALRELRG RGLRVMLSNN CTPVWPASDT RADHAAAQAY
     DNLHNRLFTD PLLEGTYPDL TAFGAETALD AWIQDGDLDL ISAPLDALGI NYYNPTRVQA
     PAAPDGLPFE EAPIEGYRRT AFDWPVVPDG LRELLVTLKH RYPTALPPLY ITENGCSAED
     VLTPDGKILD PDRIDYVETH LQAVDTAVAQ GVDVRGYFIW TLLDNFEWAE GYHQRFGLVH
     VDHETQVRTP KASFAWYRDL IRAQRG
//

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