ID B3C6L2_9BACE Unreviewed; 814 AA.
AC B3C6L2;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 24-JAN-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_00548 {ECO:0000313|EMBL:EDV06986.1};
OS Bacteroides intestinalis DSM 17393.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=471870 {ECO:0000313|EMBL:EDV06986.1, ECO:0000313|Proteomes:UP000004596};
RN [1] {ECO:0000313|EMBL:EDV06986.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV06986.1,
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:EDV06986.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV06986.1,
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:EDV06986.1}.
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DR EMBL; ABJL02000006; EDV06986.1; -; Genomic_DNA.
DR RefSeq; WP_007660315.1; NZ_ABJL02000006.1.
DR AlphaFoldDB; B3C6L2; -.
DR STRING; 471870.BACINT_00548; -.
DR eggNOG; COG1472; Bacteria.
DR OrthoDB; 9805821at2; -.
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:SF16; LYSOSOMAL 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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..814
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002785292"
FT DOMAIN 726..795
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 814 AA; 89930 MW; FB1AEBE9E0F47ADF CRC64;
MKKKVICSVL LGLMVSGQLV GADYIKPKKD KKTGISYYDL NKNGHLDIYE NPAFAVEERV
RALLSQMTLE EKVGQMLTSL GWPMYERQGN TICLTEQLVR EIEEYHTGSL WGFMRADPWT
QRTLTTGLTP ALAAKASNML QKYAIEHGRL GIPLFLAEEC PHGHMAIGTT VFPTSIGQAS
TWNPELIRRM GRAIATEASA QGAHIGYGPV LDLARDPRWS RVEETYGEDA YLNGVMGAAL
VKGFQGEFPR TKGKVIATLK HFAAYGWTEG GHNGGSAHVG NREMEEAIYP PFREAVAAGA
LSVMSSYNEI DGIPCTANSN LLTGLLKERW QFKGFVVSDL YAIGGLREHG VADTDYEAAV
KAVNAGVDSD LGTNVYAGQL VNAVKRGDVQ EVVINKAVSR ILALKFHMGL FDHPFVDERE
PEQVVASTEH LELAREVARQ SIILLKNKNE LLPLNKKTKT IAVIGPNADN IYNMLGDYTA
PQSESSVVTV LDGIRQKVSN DTHIIYAKGC AVRDSSKSGF QEAIEAARQS DVVVMVMGGS
SARDFSSKYE ETGAAKVSDS HISDMESGEG YDRSTLELLG RQRELIREVG KLNKPIVLVL
IKGRPLLLEG IEAEVDAIVD AWYPGMQGGN AVADVLFGDY NPAGRLTISV PRSVGQLPVY
YNTKRKGNRS KYIEEEGTPR YPFGYGLSYT SFNYSDLKAE VVEAEDSCLV NISVKVRNEG
SRDGDEVVQL YLRDEVASFT TPFKQLCGFQ RIHLKVGETK EITFRLDKKS LALYMQNEEW
AVEPGRFTLM LGGSSEQIYQ QKEIEITKRY TFKM
//