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Database: UniProt
Entry: J0WKU3_9FLAO
LinkDB: J0WKU3_9FLAO
Original site: J0WKU3_9FLAO 
ID   J0WKU3_9FLAO            Unreviewed;       761 AA.
AC   J0WKU3;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=HMPREF1320_1384 {ECO:0000313|EMBL:EJF37116.1};
OS   Capnocytophaga sp. oral taxon 335 str. F0486.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=1125720 {ECO:0000313|EMBL:EJF37116.1, ECO:0000313|Proteomes:UP000004158};
RN   [1] {ECO:0000313|EMBL:EJF37116.1, ECO:0000313|Proteomes:UP000004158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0486 {ECO:0000313|EMBL:EJF37116.1,
RC   ECO:0000313|Proteomes:UP000004158};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (MAY-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:EJF37116.1}.
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DR   EMBL; AKFR01000015; EJF37116.1; -; Genomic_DNA.
DR   RefSeq; WP_009417409.1; NZ_AKFR01000015.1.
DR   AlphaFoldDB; J0WKU3; -.
DR   PATRIC; fig|1125720.3.peg.625; -.
DR   Proteomes; UP000004158; 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          680..749
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   761 AA;  83533 MW;  699056F4B4E9B45F CRC64;
     MKKITYCIAM ALAVVACNNS SKTDDKTPVK WESFSGDKNI ERKVDSLLSL MTLEEKIGQL
     TQFAANWDVT GPVMSDDFQP YLEKGLVGSV FNAVTVPGVR KLQDIAVKKT RLGIPILFGY
     DVIHGYKTIF PMSLAEACSW DLDLMRQTAA IAAEEAAADG IKWTFAPMVD LARDPRWGRV
     MEGAGEDPFL GSEIAKARVQ GFQGGTDWHS LSKTNTVLAC VKHFAAYGAA EAGRDYNTAE
     LSQHTLWNAY LPPYKAAIDA GVGTVMASFN EVNGIPATAN RYLMTDILRK QWGFKGFVVT
     DYTGINELVP HGVAVDNKHA AELAINAGID MDMTGANFIK HLKKSVEEGK VKEETINTAV
     RRILEMKFVL GLFDDPYKFL DENRAKTTLM KPEFLQVART AVAKSVVLLK NNAEVLPITP
     DMPKKVALIG PMVKDSINQN GEWQGRGDRE LSASLFKGLQ EVYKDSKVQF SYAKGCTLTA
     TTSADIAKAV ATTRTADVAV VALGEDYNWS GESACLTDIR LRAPQRELLR ALKQTGKPIV
     LLVYSGRPLD LSEESELADA ILQVWFPGTQ SGYGIADVLA GKYNPSGRLV MSFPRNVGQV
     PIYYNHKNTG RPVDPNNPTV DYRSKYEDAP VTPLYPFGYG LSYTTFNISN VQLSSATLSK
     GGKITVTAQV ANTGKRDGEI VVQLYIRDLV GSVTRPVKEL KGFQKVALKA GESKQVQFEI
     TEDLLAFYNA DLKKVTEPGA FKLWVAQHSA DNSNEKDFEL K
//
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