ID A0A1Q5M454_9ACTN Unreviewed; 459 AA.
AC A0A1Q5M454;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=AMK33_18840 {ECO:0000313|EMBL:OKK08952.1};
OS Streptomyces sp. CB02400.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703944 {ECO:0000313|EMBL:OKK08952.1, ECO:0000313|Proteomes:UP000185993};
RN [1] {ECO:0000313|EMBL:OKK08952.1, ECO:0000313|Proteomes:UP000185993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02400 {ECO:0000313|EMBL:OKK08952.1,
RC ECO:0000313|Proteomes:UP000185993};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKK08952.1}.
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DR EMBL; LIWB01000007; OKK08952.1; -; Genomic_DNA.
DR RefSeq; WP_073934076.1; NZ_LIWB01000007.1.
DR AlphaFoldDB; A0A1Q5M454; -.
DR Proteomes; UP000185993; 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:UP000185993}.
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; 51061 MW; 77C47AC8602EA4D8 CRC64;
MSDFPRFPPG FVFGAATASY QIEGAAYEDG RGPSIWDTYS HTPGLVANGD TGDVACDHYH
RYPEDVALLR DLGVGSYRFS IAWPRVVPDG TGPVNPKGLD FYSRLVDELL AAGIEPAATL
YHWDLPQALE DRGGWRVRET AERFAEYAAV VAERLGDRVP RWITLNEPWC SAFLGYSVGR
HAPGAREGRG ALAAAHHLLV GHGLAVQALR AAGVREVGIT LNLDHHLPAT DSAADREAVV
RADTLHNLVW TEPILAGRYP DTEEDTWGEL ITAQDFRRDG DLELIRQPLD FLGVNYYRPI
VVADAPYREG DPALRVATDN RYAETSMPGV RHTAMGWPVA PDTFTDLLVD LKEQYGDALP
PVHITENGSS EDDEVSADGA VHDTDRVAYL RDHLTALRAA IDAGVDVRGY YVWSLLDNFE
WAFGYDKRFG IVRVDYDTQE RTPKDSYHWY RRMIAAQRP
//