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Database: UniProt
Entry: A0A1V3QWC7_9FLAO
LinkDB: A0A1V3QWC7_9FLAO
Original site: A0A1V3QWC7_9FLAO 
ID   A0A1V3QWC7_9FLAO        Unreviewed;       738 AA.
AC   A0A1V3QWC7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, 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=B0E44_12825 {ECO:0000313|EMBL:OOG68746.1};
OS   Flavobacterium sp. A45.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1945862 {ECO:0000313|EMBL:OOG68746.1, ECO:0000313|Proteomes:UP000188437};
RN   [1] {ECO:0000313|EMBL:OOG68746.1, ECO:0000313|Proteomes:UP000188437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A45 {ECO:0000313|EMBL:OOG68746.1,
RC   ECO:0000313|Proteomes:UP000188437};
RA   Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA   Frostegard A.;
RT   "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT   isolation strategy.";
RL   Submitted (FEB-2017) 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:OOG68746.1}.
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DR   EMBL; MUNX01000100; OOG68746.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3QWC7; -.
DR   STRING; 1945862.B0E44_12825; -.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000188437; 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:UP000188437};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..738
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012302219"
FT   DOMAIN          656..725
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   738 AA;  81848 MW;  09F712E2061646FC CRC64;
     MKKAITLACL FVSVFAFSQQ SIDQKVETLL KKMTLEEKIG QLNQYTGDNT ATGPITINSN
     KQNEIKKGLI GSMLNIMGTK YTRQYQELAM QSRLKIPLLF GLDVIHGYKT TFPIPLAEAA
     SWDLTAMELS ARIAATEAAA SGIHWTFAPM ADISRDPRWG RVMEGGGEDT YLGSKIAYAR
     VKGFQGNLGD VNSVMACVKH FAAYGAAVGG RDYNSVDMSN RMLWETYLPP YKAALDAGAA
     TFMNSFNDLN GIPASANNYL LRDILKGKWN FQGFVVSDWG SIGEMVAHGY VKDNKEAALA
     SITAGSDMDM ESNAYRYHLE QLVKENKVPV ALIDDAVKRI LRKKFELGLF DDPYKFCSPE
     REQAALNNPE HTKAAREIAA KSIVLLKNER DVLPLSKGLK TIAFIGPMVK PKRDNHGFWA
     VDVKEIDSTY IVSQWEGLQN KVGKRTKILY AKGCGVEDKS KDGFADALHV ASQAEVIILS
     IGENFNKSGE AKSKSNLQLP GVQEDLIKEL QKTGKPIVIL INAGRPLVFD WVADNMPTIV
     YTWWLGSEAG NAIADVLFGD YNPSGKLPMT FPRTEGQIPI YYNHFNTGRP SVNGDKNYKS
     AYIDLPTTPK FPFGFGLSYT TFEYSNLKLS KKTMKNNEII TVSVNITNTG SVKGEEVVQL
     YLRDRVGSVV RPIIELKDFQ KITLNRGETK TLEFTIDNPK LSFYNNALEF VSESGDFDLM
     IGSSSADIRL KDSFELVK
//
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