ID A0A2U9PBP6_STRAS Unreviewed; 459 AA.
AC A0A2U9PBP6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=DMT42_35445 {ECO:0000313|EMBL:AWT47032.1};
OS Streptomyces actuosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1885 {ECO:0000313|EMBL:AWT47032.1, ECO:0000313|Proteomes:UP000247634};
RN [1] {ECO:0000313|EMBL:AWT47032.1, ECO:0000313|Proteomes:UP000247634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25421 {ECO:0000313|EMBL:AWT47032.1,
RC ECO:0000313|Proteomes:UP000247634};
RA Liu W., Sun F., Hu Y.;
RT "The complete genome sequence of a nosiheptide producer Streptomyces
RT actuosus ATCC 25421: deducing the ability of producing a new class III
RT lantibiotics.";
RL Submitted (JUN-2018) 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; CP029788; AWT47032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9PBP6; -.
DR KEGG; sact:DMT42_35445; -.
DR OrthoDB; 9765195at2; -.
DR Proteomes; UP000247634; 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:UP000247634}.
FT ACT_SITE 167
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT ACT_SITE 366
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-1"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 166
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 413
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
FT BINDING 420..421
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617736-2"
SQ SEQUENCE 459 AA; 50930 MW; 36C83B963E711FA6 CRC64;
MSDFPRFPAG FVFGAATASY QIEGAAAEDG RGPSIWDTYS HTPGRTANGD TGDVACDHYH
RYPEDVALLG ELGVDSYRFS IAWPRIVPDG SGPVNAKGLD FYDRLVDELL AAGIEPAATL
YHWDLPQALE DRGGWRVRET AERFAEYTAV AAERLGDRVP RWITLNEPWC SAFLGYSVGR
HAPGAREGRG ALAAAHRLLV GHGLAVRELR AAGVREVGIT LNLDRNLPAS DSDADRAAVV
RADTQHNLVW TEPLLAGRYP ASEEETWGEL ITGQDFRRDG DLELIGQPLD FLGINYYRPI
VVADAPYREA DPARRVATDN RYAEVRLEGV RHTAMNWPVV PETFTDLLVD LKERYGEALP
PVHITENGSA EADEVGADGA VHDADRVAYL RDHLTALRAA MDAGVDVRGY YVWSLLDNFE
WALGYDKRFG IVRVDYATQR RTPKDSYRWY RAMIAAQRG
//
