ID R6DQQ1_9BACE Unreviewed; 937 AA.
AC R6DQQ1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=BN772_00638 {ECO:0000313|EMBL:CDA87249.1};
OS Bacteroides sp. CAG:754.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262750 {ECO:0000313|EMBL:CDA87249.1, ECO:0000313|Proteomes:UP000017906};
RN [1] {ECO:0000313|EMBL:CDA87249.1, ECO:0000313|Proteomes:UP000017906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:754 {ECO:0000313|Proteomes:UP000017906};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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}.
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:CDA87249.1}.
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DR EMBL; CBCP010000300; CDA87249.1; -; Genomic_DNA.
DR AlphaFoldDB; R6DQQ1; -.
DR Proteomes; UP000017906; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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: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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000017906};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..937
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004403710"
FT DOMAIN 741..810
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 937 AA; 104610 MW; E9775B03B3F62C3A CRC64;
MKTIFFSMLI LGTTFAVCAQ QKQDDPRIPN KKDLVTYRLS KNPIYKDGWI DFNKNGKKDI
YEDPNALVED RIEDLLRQMT VEEKTCQMVT LYGYKRVLDD ELPTSEWKNK LWKDGMGAID
EHLNGFRQWG LPPSDNAFVW PASRHAWALN EVQRFFVEET RLGIPVDFTN EGIRGVESYI
ATNFPTQLGL GHTWNRDLIK KVGYITGREG RLLGYTNIYA PILDVGRDQR WGRYEEIYGE
CPYLVSELGV AMTLGMQTDY QVASTAKHFL AYSNNKGGRE GLSRVDPQMS PREVENIHIY
PWKKVIKKGG LLGAMSSYND YDGFPVQSSY YWLMTRLRKD LGFKGYVVSD SDAVEYLHSK
HGTAQNMKES VRQSVEAGLN VRCTFRSPDS YVLPLRELIA EGGLSMETID ERVRDVLRVK
FMVGLFDAPY QMDLKAADRE VNSVENQAVA LQASRESIVL LKNEDNTLPL VKEQIKKISV
CGPNADDVSY ALSHYGPLAV EATSVLQGIK EKMQGQAEVL YTKGCDIVDA NWPESEILPA
ELTDAEQAEI DKAVANALES DVAIVVLGEN GRTCGENKSR SSLDLPGRQL DLLKAVYATG
KPTILVIISG RPNSVNWADR HIPAILEAWY PGSQGGTAVA DVIFGDYNPG GKLTVTFPKT
VGQIPFNFPS KPASQVDGGR VVGLKGNMSR VNGALYPFGY GLSYTTFKYS DLVVTPSVIT
PKQDVTVRFN VTNTGDRAGD EIVQMYVRDI ISSVTTYEKN LRGFERINLQ PGETKEVVFT
VAPEELSLYD KEEKWVVEPG DFRIMVGASS TDIRLSDTLT VIPYQDSKAS GRNKKDINAK
WTGSKGDYLT IPVKDADALD RVFIRWAGLP KEPVHFEIQI SSGGGQFLTV FSGKATKTEH
MQCYKFNKTT VSDIRILITS GKASVAEVKI DKKVPCN
//