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Database: UniProt
Entry: D6KER2_9ACTN
LinkDB: D6KER2_9ACTN
Original site: D6KER2_9ACTN 
ID   D6KER2_9ACTN            Unreviewed;       453 AA.
AC   D6KER2;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Beta-glucosidase {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361175};
GN   ORFNames=SSTG_05437 {ECO:0000313|EMBL:EFF89567.2};
OS   Streptomyces sp. e14.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=645465 {ECO:0000313|EMBL:EFF89567.2, ECO:0000313|Proteomes:UP000004704};
RN   [1] {ECO:0000313|EMBL:EFF89567.2, ECO:0000313|Proteomes:UP000004704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=e14 {ECO:0000313|Proteomes:UP000004704};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Streptomyces sp. strain e14.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00000448,
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; GG753627; EFF89567.2; -; Genomic_DNA.
DR   RefSeq; WP_009192654.1; NZ_GG753627.1.
DR   AlphaFoldDB; D6KER2; -.
DR   STRING; 645465.SSTG_05437; -.
DR   eggNOG; COG2723; Bacteria.
DR   OrthoDB; 9765195at2; -.
DR   Proteomes; UP000004704; Unassembled WGS sequence.
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:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
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   NCBIfam; TIGR03356; BGL; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361175};
KW   Hydrolase {ECO:0000256|RuleBase:RU361175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004704}.
FT   ACT_SITE        170
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   ACT_SITE        355
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT   BINDING         24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         402
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT   BINDING         409..410
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ   SEQUENCE   453 AA;  49802 MW;  F369B0C5C30C8554 CRC64;
     MSDPIDLAAF PHDFAWGTAT SAYQIEGAAA EDGRAPSIWD TFSHTPGKVD NDDHGDVACD
     HYHRWPEDIA LMKELGTDAY RLSIAWPRVV PDGDGPVNAK GLAFYDRLVD GLLEAGLTPN
     VTVYHWDLPQ TLQDRGGWNE RATAEHLAEY ASVVAGRLGD RVTRWATLNE PLCSAWIGHL
     EGRMAPGLTD LTTAVRASYH LLLGHGLATQ AIRAAVPNAQ IGLVTNHSTV AAASTSPEDV
     AAAARMDGHT NRWWLDPIHG RGFPADMREL YGVELPEQTG DLETIAAPLD WHGLNYYFPV
     TVENDPDGPV PYAREVRLPD VPRTGMDWQV DADGLESLLL RLTDDYGVRR LYVTENGSAF
     PDTVGPDGAV HDPGRTRYLE QHLAACARAV RKGAPLAGYY AWSLLDNFEW AYGYDKRFGL
     VHVDYATQKR TVKTSGRRYA EIVRAHRQGS ATA
//
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