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Database: UniProt
Entry: A0A4R6QB85_9FLAO
LinkDB: A0A4R6QB85_9FLAO
Original site: A0A4R6QB85_9FLAO 
ID   A0A4R6QB85_9FLAO        Unreviewed;       766 AA.
AC   A0A4R6QB85;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 9.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=BC748_1647 {ECO:0000313|EMBL:TDP59397.1};
OS   Flavobacterium dankookense.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=706186 {ECO:0000313|EMBL:TDP59397.1, ECO:0000313|Proteomes:UP000295260};
RN   [1] {ECO:0000313|EMBL:TDP59397.1, ECO:0000313|Proteomes:UP000295260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25687 {ECO:0000313|EMBL:TDP59397.1,
RC   ECO:0000313|Proteomes:UP000295260};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2019) 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:TDP59397.1}.
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DR   EMBL; SNXR01000013; TDP59397.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R6QB85; -.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000295260; 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:UP000295260};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..766
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5020933330"
FT   DOMAIN          685..754
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   766 AA;  84157 MW;  510BB75DE3C3C8A4 CRC64;
     MKPTKNLLLL FLFLSGISLN AQKKATKTIA PKEQFIAELM AKMTIDEKIG QLNLPTSGDI
     TTGQANSSNV AKNIEQGKVG GLFNIKSVAK IKEVQKIAVE KSRLKIPLLF GMDVIHGYET
     TFPIPLGLSC TWDMNAIKRS AQIAAQEASA DGINWTFSPM VDISRDPRWG RVSEGSGEDA
     YLGSQVAKAM VTGYQGDDLS KNNTLLSCVK HFALYGAPEA GRDYNTVDMS RIRMYNEYFP
     PYKAAIDAGV GSVMASFNEI DGIPATGNKW LMTDVLRKQW GFKGFVVTDY TGIMEMEYHG
     VGDLQTVSAL ALKAGIEMDM VSDGFLGTLK KSLDEGKVTI QEIDRAVRLI LNAKYDLGLF
     HDPYRYCDEK RAKTEIFTTL NRSEARKIAA QSLVLLKNDN QLLPLKKSGT VAVIGPLADA
     KENMAGTWSV ATKQENSISL LAGIQSVVGT SAKVLYAKGS NLDYDEQLEE RATMFGKTLH
     RDKRTKEELL SEAVKIANQS DVIILAIGES AEFSGESSSR TNIKIPQAQK DLLAALQKTG
     KPIVLTLFTG RPLDLTDENA TVPAILNTWF AGSEAGYAIA DVLFGNENPS GKLTMTFPRT
     IGQIPIYYAA KNTGRPLGNK EGKFEKFKTN YIDERNEPLF PFGFGLSYTT FSYGNLSISS
     NKMAANETIK VSVPVTNSGN YDGKEVVQLY IRDVVGSVTR PIKELKGFQK IEFKKGETKT
     VTFEITIDDL KFYNSDLQFV AEPGKFEVFI GTNSDTTSKI EFDLVN
//
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