ID A0A239RM66_9BACT Unreviewed; 763 AA.
AC A0A239RM66;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=SAMN06298210_10716 {ECO:0000313|EMBL:SNU11046.1};
OS Prevotellaceae bacterium KH2P17.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae.
OX NCBI_TaxID=1945886 {ECO:0000313|EMBL:SNU11046.1, ECO:0000313|Proteomes:UP000214740};
RN [1] {ECO:0000313|EMBL:SNU11046.1, ECO:0000313|Proteomes:UP000214740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH2P17 {ECO:0000313|EMBL:SNU11046.1,
RC ECO:0000313|Proteomes:UP000214740};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) 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};
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DR EMBL; FZRE01000007; SNU11046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239RM66; -.
DR Proteomes; UP000214740; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR30620:SF121; PERIPLASMIC BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR30620; PERIPLASMIC BETA-GLUCOSIDASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000214740};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..763
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011314570"
FT DOMAIN 682..751
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 763 AA; 83492 MW; 8F566E5B2C97D0A4 CRC64;
MKLKNIMGTL AFAAVAALPA TMQAQSGDAR MDKFIDGLMG KMTLEEKLGQ LNLPVTGDIV
TGQAKSSDVA GKIRSGQVGG LFNLKGVDKI REVQKIAVEQ SRLKIPLLFG MDVIHGYETV
FPIPLALSMS WDMDAIERSA RVAAVEASAD GICWTFSPMV DICRDARWGR MSEGNGEDPY
LGSRIAEAMV RGYQGTNLAD PSTVMACVKH FALYGGAEAG RDYNTVDMSR WRMFNYYFPP
YKAAAEAGAG SFMTSFNVVD GIPATGNRWL LTDVLRRMWG FKGFVVTDYT AIAEMTAHGM
GDLQQVSALA LNAGTDMDMV ADGFVGTLAQ SLREGKVSME SIDAACRRIL EAKYKLGLFS
DPYRYLDPKR AKTEIYTDAH RAEARRTAAE TFVLLKNDGR LLPLQRKGRI ALIGPLGNTP
ANMPGTWSVA ADAAKYKSLY QAMKDAVGDK ATVTYAKGSN ICYDERLEAN GSMFGREIRD
GRSDKELLDE ALRTAAQADV IVAAIGETSE FSGESSSRSD LSLFDAQKDL LTALRQTGKP
IVLVNFSGRA TVMTWEAENF AAILNVWFGG SEAGDAICDV LFGDKSPSGR LTVSMPKSVG
QLPLYYNHLN TGRPLEKGKW FTKFRSNYLD VDNEPLFPFG YGLSYTTFGY GPLSLSNASM
TAEGTIRASV TVTNTGNCDA DEVVQLYIRD MVGSVSRPVQ ELRDFRRISL KKGESKTVSF
TINAEKLKFY NNELQYVCEP GEFQVMVGPN SRDVQVQSFT LKD
//
