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Database: UniProt
Entry: A0A0A2LSU8_9FLAO
LinkDB: A0A0A2LSU8_9FLAO
Original site: A0A0A2LSU8_9FLAO 
ID   A0A0A2LSU8_9FLAO        Unreviewed;       757 AA.
AC   A0A0A2LSU8;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=Q763_14370 {ECO:0000313|EMBL:KGO79225.1};
OS   Flavobacterium beibuense F44-8.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1406840 {ECO:0000313|EMBL:KGO79225.1, ECO:0000313|Proteomes:UP000030129};
RN   [1] {ECO:0000313|EMBL:KGO79225.1, ECO:0000313|Proteomes:UP000030129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F44-8 {ECO:0000313|EMBL:KGO79225.1,
RC   ECO:0000313|Proteomes:UP000030129};
RA   Zeng Z., Chen C.;
RL   Submitted (SEP-2013) 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:KGO79225.1}.
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DR   EMBL; JRLV01000019; KGO79225.1; -; Genomic_DNA.
DR   RefSeq; WP_035135422.1; NZ_JRLV01000019.1.
DR   AlphaFoldDB; A0A0A2LSU8; -.
DR   STRING; 1406840.Q763_14370; -.
DR   eggNOG; COG1472; Bacteria.
DR   Proteomes; UP000030129; 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:UP000030129};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..757
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002002526"
FT   DOMAIN          677..746
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   757 AA;  83503 MW;  BBAFFA055F1B0BFA CRC64;
     MKRTLLILAV LTVCTANAQK KKSMDKKQDI EQRIDELLIK MTLEEKVGQM NQYNGFWDVT
     GPSPKEGNAA TKYEHLRKGW VGSMLTVRGV KEVRAVQKIA VEETRLGIPL IIGFDVIHGY
     KTLSPIPLAE AASWDMDAIK NSAKTAASEA AASGINWTFG PNVDISRDAR WGRVMEGAGE
     DPFLGSQVAI ARVKGFQGDD LSNPLTIAAC AKHFAAYGFA EAGRDYNTVD IGNATLYNTV
     LPPFKAANDA GVRTYMNSFN ILNGVPATGN SFLQRDILKG KWGFDGFVIT DWASIREMIA
     HGFAEDGAEA SEKAVKAGAD MDMESHLYVY ELVKLVEEGK VDEALIDDAV RRILRVKFEL
     GLFDDPYRYC DEKREKEIIY SKANHEAVLD MAKKSIVLLK NEGNLLPLKK KGQKIALIGS
     LANDKTSPLG SWRIASDDNT AVSVLEGMQQ YKGNTLVFEK GADLTIGKTT FLDELVFNTT
     ERSGFEAAKK AAKEADVVVM VLGEHGFQSG EGRSRTNLDL PGLQQELLEE IYKVNPNIVL
     VLNNGRPLAL PWATENIPTI VEAWHLGTET GNAVAQVLYG DYNPSGKLPM SFPRNVGQVP
     IYYNQHSTGR PTNSDNNVFW SHYSDVEKTP LFAFGHGLSY TTFKYGTIKL NKKTYAKGEP
     VKVSVEVTNT GDYDGKEVVQ LYIRDIAASL SRPVKELKGF ELVPLKKGET KTVTFTLTDK
     ELGFFNNEGE YLVEPGIFKV FVGTSSADNQ ETEFELK
//
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