ID   L8JSU5_9BACT            Unreviewed;       752 AA.
AC   L8JSU5;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=C900_03550 {ECO:0000313|EMBL:ELR70569.1};
OS   Fulvivirga imtechensis AK7.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC   Fulvivirga.
OX   NCBI_TaxID=1237149 {ECO:0000313|EMBL:ELR70569.1, ECO:0000313|Proteomes:UP000011135};
RN   [1] {ECO:0000313|EMBL:ELR70569.1, ECO:0000313|Proteomes:UP000011135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK7 {ECO:0000313|EMBL:ELR70569.1,
RC   ECO:0000313|Proteomes:UP000011135};
RA   Nupur N., Khatri I., Kumar R., Subramanian S., Pinnaka A.;
RT   "Genome assembly of Fulvivirga imtechensis AK7.";
RL   Submitted (DEC-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:ELR70569.1}.
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DR   EMBL; AMZN01000051; ELR70569.1; -; Genomic_DNA.
DR   RefSeq; WP_009580926.1; NZ_AMZN01000051.1.
DR   AlphaFoldDB; L8JSU5; -.
DR   STRING; 1237149.C900_03550; -.
DR   PATRIC; fig|1237149.3.peg.3311; -.
DR   eggNOG; COG1472; Bacteria.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000011135; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011135}.
FT   DOMAIN          671..740
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   752 AA;  83097 MW;  8EAA500DE6E8731B CRC64;
     MKKIPLFFIS FIFYGCLTEG NRNQPQTYEN PKIEALIRQM TLEEKVGQLN FYVGDLFNTG
     PTVRTTESDK FDQLIREGKL TGLFNVHGAA YTGRLQKIAV EESRLGIPLL FGADVIHGFK
     TVFPIPLASA ASWDLEAIEK AERVAAIEST AAGINFNFAP MVDISRDPRW GRIAEGAGED
     PFLGSEVAKA RVRGFQEQSL TDPQTMAACV KHFAAYGAPD GGRDYNTVDM SERLLREMYL
     PPYKAGIDAG AATIMTSFNE LNGIAASGSQ FLLRDILRKE WGFKGMVVSD WQSVNEMVAH
     GNAANNAEAA MMALKAGVDM DMMGDVYLEE VPRLVNEGKL DIKFVDEAVR NVLKLKYDLG
     LFDDPYRYSD TIREKNNIRA VEHLEAARDV AKKSIVLLKN KEKLLPLKKS IGTIAVIGPL
     ADNQADMNGT WSFFGEAQHP ITFLQGIKDA VSGQSRVLYA EGCNLYDRSK DKFAEAVNIA
     KKADVVILAV GESAVMNGEA GSRSDIRLPG IQPELVMEIA KTGKPVVALV MSGRPLDLSW
     LDENIPAILE VWTLGSEAGN AAADVLFGDY NPSGKLPVTF PRNVGQVPIY YNHKNTGRPY
     EGDYSEPLSE RIYRSKYRDV QNSPLYPFGY GLSYSTFEYS DITLSADTLN AGESITASVS
     ITNEGPYDGE EVVQLYIRDL VGSVTRPVKE LKGFKKLMIK NGETVKVDFT LSSDDLSFYR
     HDMTYGIEPG DFQIFIGSDS KNVKEQHFVL KN
//