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Database: UniProt
Entry: C3QAZ2_9BACE
LinkDB: C3QAZ2_9BACE
Original site: C3QAZ2_9BACE 
ID   C3QAZ2_9BACE            Unreviewed;       759 AA.
AC   C3QAZ2;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=BSAG_00836 {ECO:0000313|EMBL:EEO49126.1};
OS   Bacteroides sp. D1.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=556258 {ECO:0000313|EMBL:EEO49126.1, ECO:0000313|Proteomes:UP000003361};
RN   [1] {ECO:0000313|EMBL:EEO49126.1, ECO:0000313|Proteomes:UP000003361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1 {ECO:0000313|EMBL:EEO49126.1,
RC   ECO:0000313|Proteomes:UP000003361};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Sibley C.,
RA   White A., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. D1.";
RL   Submitted (MAY-2011) 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:EEO49126.1}.
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DR   EMBL; ACAB02000043; EEO49126.1; -; Genomic_DNA.
DR   RefSeq; WP_008770592.1; NZ_JH114337.1.
DR   AlphaFoldDB; C3QAZ2; -.
DR   HOGENOM; CLU_004542_5_1_10; -.
DR   Proteomes; UP000003361; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161}.
FT   DOMAIN          679..748
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   759 AA;  83941 MW;  3286AEEC4E194B27 CRC64;
     MKIRNLISCA LCGLTLFACS PSGGGKDREM DRFITDLMDR MTLREKLGQL NLPSGGDLVT
     GSVMNGELSD MIRKQEIGGF FNVKGIQKIN ALQHLAVEES RLKIPLLVGA DVIHGYETIF
     PIPLALSCSW DTLAVERMAR ISAIEASADG INWTFSPMVD ICRDGRWGRI AEGNGEDPYL
     GSLMAKAYVR GYQGNNMQGN DEILACVKHF ALYGASESGR DYNTVDMSRL RMYNEYLAPY
     KAAVDAGVGS IMSSFNIVDG IPATANKWLL TDLLRNEWGF GGLLVTDYNS IAEMSSHGVA
     PLKEASIRAL QAGTDMDMVS CGFLNTLEES LKEAKVTEEQ INMACRRVLE AKYKLGLFSN
     PYKYCDALRA KEKLYTPEHR SAARAIAAET FVLLKNDNNL LPLEQKGRIA LIGPMADARN
     NMCGMWSMTC TPSRHRTLLE GIRAAAGDKA EILYAKGSNI YYDAETEKAA TGIRPLERGD
     NRELLDEALR VASRSDIIVA ALGECAEMSG ESASRTSLEI PDAQQDLLKA LVKTGKPVVL
     LLFTGRPLVL NWEDANVHSI LNVWFGGSET GDAVADVLFG KITPSGKLTT TFPRSVGQLP
     LFYNHLNTGR PDPDSHIFNR YASNYLDESN EPLYPFGYGL SYTDFVYGEL QISSETLPKN
     GELTVSVTVT NKGNYDGYET VQLYLRDIYA EVARPMKELK GFERIFLKSG ESRDVKFVIT
     KDDLKFYNSE LHYVYEPGEF DVMVGPNSRD VQTKSFQAE
//
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