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Database: UniProt
Entry: R6PL36_9BACT
LinkDB: R6PL36_9BACT
Original site: R6PL36_9BACT 
ID   R6PL36_9BACT            Unreviewed;       762 AA.
AC   R6PL36;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=BN637_01107 {ECO:0000313|EMBL:CDC24290.1};
OS   Prevotella sp. CAG:386.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262925 {ECO:0000313|EMBL:CDC24290.1, ECO:0000313|Proteomes:UP000018046};
RN   [1] {ECO:0000313|EMBL:CDC24290.1, ECO:0000313|Proteomes:UP000018046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:386 {ECO:0000313|Proteomes:UP000018046};
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   -!- 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:CDC24290.1}.
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DR   EMBL; CBEZ010000020; CDC24290.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6PL36; -.
DR   STRING; 1262925.BN637_01107; -.
DR   Proteomes; UP000018046; 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:UP000018046};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..762
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004415403"
FT   DOMAIN          682..751
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   762 AA;  84165 MW;  21825AAC45D114E2 CRC64;
     MKTKNILAAF TLLAASLCPT MAQAQSDEAK MNTFIDNLMN KMTLKEKLGQ LNLPVTGDIV
     TGQAKSSDVA NKIKRGEVGG LFNLKGVEKI KEVQKIAVEQ SRLHIPLLFG MDVIHGYETV
     FPIPFSLSCS WDMEAIKRTA QIAAQECSAD GINWTFSPML DICRDPRWGR MAEGNGEDPY
     LGSCIAKAMV EGYQGQNLAA PNTVMACVKH FALYGGAEAG RDYNTVDMSH WRMFNYYMPP
     YKAAVDAGAL SVMTSFNVVD GIPATGNKWL LTDVLRKMWG FKGMVVTDYT AIQEMTAHGL
     GDLQQVSAMA LNAGTDMDMV ADGFLGTIEK SINEGKVSME TVNTACRRIL EAKYKLGLFD
     DPYKYCNVKR AKKEIYTPQN RAFSREIAAK TFVLLKNEGN LLPLQRKGKI ALIGPLADNS
     KNMSGTWSVA ARLDDNKTIL GSMKKALEGK AEVLYAKGSN LMYDAKREAD ATMFGREMRD
     SRSNEEMLKE ALNVAQQADI IVAAVGESSE MSGECSSRTN LEMPDAQKDL LIALKKTGKP
     IVLVNFSGRA TVMTWEQENF PAILNVWFGG CESGDAICDV LFGDKVPSGK LTATMPKSVG
     QIPLYYNHLN TGRPLKEGKW FSKFTSNYLD IDNDPLYPFG YGLSYTTFKY GKPSLSSNTM
     TNNETISVSV DITNTGNYDA DEIAQMYIRD LAASVSRPVK ELKGFERISI KKGETKTVTF
     TITPEDLKFY NQELEYKNEP GEFEVMVGPN SKDVQTLTFT LK
//
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