ID V6KUP6_STRRC Unreviewed; 454 AA.
AC V6KUP6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=M878_07185 {ECO:0000313|EMBL:EST35151.1};
OS Streptomyces roseochromogenus subsp. oscitans DS 12.976.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST35151.1, ECO:0000313|Proteomes:UP000017984};
RN [1] {ECO:0000313|EMBL:EST35151.1, ECO:0000313|Proteomes:UP000017984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS 12.976 {ECO:0000313|EMBL:EST35151.1,
RC ECO:0000313|Proteomes:UP000017984};
RX PubMed=24407645;
RA Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces roseochromogenes subsp. oscitans DS
RT 12.976, Producer of the Aminocoumarin Antibiotic Clorobiocin.";
RL Genome Announc. 2:e01147-e01113(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EST35151.1}.
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DR EMBL; AWQX01000061; EST35151.1; -; Genomic_DNA.
DR RefSeq; WP_023545428.1; NZ_CM002285.1.
DR AlphaFoldDB; V6KUP6; -.
DR STRING; 1352936.M878_07185; -.
DR PATRIC; fig|1352936.5.peg.1531; -.
DR HOGENOM; CLU_001859_1_3_11; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000017984; 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: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:UP000017984}.
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 454 AA; 49701 MW; CCD1C613BD406313 CRC64;
MSERIDLAAL PHDFLWGTAT AAYQIEGAVA EDGRTPSIWD TFSHTPGKIA NGDTGDVACD
HYHRWREDIG LMRQLGVNAY RLSVAWPRVV PGGTGPVNPK GLAFYDELVD DLLEAGITPS
VTLYHWDLPQ MLQDRGGWPE RDTAFALAEY ASAAAARLGD RVKLWATLNE PSCSAWIGHL
EGKMAPGWTD LTAAVRASVH LLLGHGLATQ AIRAAAPGAQ AGIVNNLSTV DAATGRPEDI
AAARRHDGHV NRWWLDPVHG RGFPADMIDT YGIELPLKAG DLETIATPLD WLGLNYYFPA
HVADAPDGPA PYVRAVRRDG VPRTGMDWEI DASGIETLLL RLTEEYGARK IYVTENGSAF
PDVVRPDGSI DDPERQDYLE THLAACASAA RRGAPLAGYF AWSLLDNFEW AYGYDKRFGL
VHVDYRTQVR TIKGSGNRYA DLVRGHRGQT RRAA
//
