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Database: UniProt
Entry: R6KMZ9_9BACE
LinkDB: R6KMZ9_9BACE
Original site: R6KMZ9_9BACE 
ID   R6KMZ9_9BACE            Unreviewed;       784 AA.
AC   R6KMZ9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-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=BN506_02646 {ECO:0000313|EMBL:CDB71361.1};
OS   Bacteroides cellulosilyticus CAG:158.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1263038 {ECO:0000313|EMBL:CDB71361.1, ECO:0000313|Proteomes:UP000018191};
RN   [1] {ECO:0000313|EMBL:CDB71361.1, ECO:0000313|Proteomes:UP000018191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:158 {ECO:0000313|Proteomes:UP000018191};
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, 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:CDB71361.1}.
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DR   EMBL; CBEB010000207; CDB71361.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6KMZ9; -.
DR   Proteomes; UP000018191; 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   Reference proteome {ECO:0000313|Proteomes:UP000018191};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..784
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004423545"
FT   DOMAIN          704..773
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   784 AA;  85539 MW;  8EFE452BB46EA4FD CRC64;
     MKKILKRTSL LLISALMSIA AAQAQKSPQD MDRFIDALMK KMTVEEKIGQ LNLPVTGDIT
     TGQAKSSDVA QKIEKGLVGG LFNLKGVDRI LEVQKLAVEK SRLGIPLLFG MDVIHGYETI
     FPIPLGLSCT WDMAAIEKSA RIAAIEASAD GISWTFSPMV DISRDPRWGR VSEGSGEDPF
     LGGAIAQAMV YGYQGANLQD QLHRNDEIMA CVKHFALYGA GEAGRDYNTV DMSRNRMFNE
     FMYPYEAAVE AGVGSVMASF NEIDGIPATG NKWLLSDLLR GQWGFEGFVV TDFTGISEMI
     EHGVGDLQTV SALALNAGVD MDMVSEGFVG TLMKSIKEGK VRMGTLNTAC RRILEAKYKL
     GLFDNPYKYC DVNRPKRDIF TKEHRDVARK IAGESFVLLK NAPATAQPLV AHSSSPVTAS
     PVLPLKKQGT VAVIGPLGNT RSNMPGTWSV AARLNDYPSL YEGLKEMMAG KVNITYAKGS
     NLIGDAAYEE RATMFGRSLN RDNRTDQELL DEALKVAAGA DVIVAALGES SEMSGESSSR
     TELGLPDVQH TLLEALLKTG KPVVLTLFTG RPLTLNWEQE HVPAILNVWF GGSEAAYAIG
     DVLFGDVNPS GKLTMTFPKN VGQIPLFYNH KNTGRPLAAG KWFEKFRSNY LDVDNEPLYP
     FGYGLSYTTF QYSDIALSTP TLGKDGSVTA VVTVTNTGKH DGAEVVQLYI RDLVGSITRP
     VRELKGFNKI FLRAGESKTV SFTITRDLLR FYDYDLNYVA EPGDFDIMIG GNSQAVKTAK
     LTLK
//
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