ID B3C7U1_9BACE Unreviewed; 766 AA.
AC B3C7U1;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=BACINT_01635 {ECO:0000313|EMBL:EDV06546.1};
OS Bacteroides intestinalis DSM 17393.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=471870 {ECO:0000313|EMBL:EDV06546.1, ECO:0000313|Proteomes:UP000004596};
RN [1] {ECO:0000313|EMBL:EDV06546.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV06546.1,
RC ECO:0000313|Proteomes:UP000004596};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides intestinalis (DSM 17393).";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDV06546.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV06546.1,
RC ECO:0000313|Proteomes:UP000004596};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2008) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:EDV06546.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABJL02000007; EDV06546.1; -; Genomic_DNA.
DR AlphaFoldDB; B3C7U1; -.
DR STRING; 471870.BACINT_01635; -.
DR eggNOG; COG1472; Bacteria.
DR Proteomes; UP000004596; 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; IPR019800; Glyco_hydro_3_AS.
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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..766
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002785356"
FT DOMAIN 686..755
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 766 AA; 84479 MW; E7CFD7D9E099F1F8 CRC64;
MKSMRQLILK VQSFLILLVL VSANMQAQKS PVDMDRFIDD LMKKMTLEEK IGQLNLPVTG
EITTGQAKSS NVAKRIRAGE VGGLFNLKGV ERIRDVQKQA VEESRLGIPL LFGMDVIHGY
ETVFPIPLGL SCTWNMTAIE ESARIAAIEA SADGICWTFS PMVDVSRDPR WGRVSEGNGE
DPFLGAEIAR AMVRGYQGKD MSSNDEIMAC VKHFALYGAS EAGRDYNTVD MSHQRMFNEY
MLPYQAAVEE GVGSVMASFN EVDGVPATGN KWLMTDVLRK QWNFDGFVVT DYTGITEMTD
HGMGDTQTVA ALALNAGVDM DMVSDAFTST LKKSLEEGKV SVKAVDAACR RILEAKYKLG
LFDNPYKYCD ITRPKKQIFT KEHRAIARKT ASESFVLLKN ENSVLPLAKK GTIAVVGPLA
DSRSNMPGTW SVAAVMNKYP SLIEGLKEVV GGKAKILTAK GSNLMSDAEY EERATMFGRT
LHRDNRTDKE LLDEALAVAA KSDVIVAALG ESSEMSGESS CRTDLEMPDT QRVLLQELLK
TGKPVVLVLF TGRPLVLNWE QENVPAILNV WFGGSEAALA IGDVLFGNVN PSGKLTTTFP
KSVGQIPLFY NHKNTGRPLP QGAWFQKFRS NYLDVDNEPL YPFGYGLSYT TFSYSDITLD
KSSMNINGEI MATVTVTNTG KYDGSEVVQL YIRDLIGSVT RPVKELKGFE KIFLKAGESK
QVSFKLTADM LKFYNYNLDF VCEPGDFEVM IGGDSRDVNK ALFSLQ
//