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Database: UniProt
Entry: A0A495KNP6_9FLAO
LinkDB: A0A495KNP6_9FLAO
Original site: A0A495KNP6_9FLAO 
ID   A0A495KNP6_9FLAO        Unreviewed;       784 AA.
AC   A0A495KNP6;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=C8C84_2437 {ECO:0000313|EMBL:RKS02712.1};
OS   Flavobacterium sp. 102.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2135623 {ECO:0000313|EMBL:RKS02712.1, ECO:0000313|Proteomes:UP000270484};
RN   [1] {ECO:0000313|EMBL:RKS02712.1, ECO:0000313|Proteomes:UP000270484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=102 {ECO:0000313|EMBL:RKS02712.1,
RC   ECO:0000313|Proteomes:UP000270484};
RA   Chistoserdova L.;
RT   "Synthetic bacterial communities of pure cultures isolated from sediment of
RT   Lake Washington, USA.";
RL   Submitted (OCT-2018) 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:RKS02712.1}.
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DR   EMBL; RBKX01000001; RKS02712.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495KNP6; -.
DR   Proteomes; UP000270484; 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}.
FT   DOMAIN          703..772
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   784 AA;  86067 MW;  19DEBE07ED7BB3E9 CRC64;
     MNGCYSRLKN NNINQSKMKV KLTIILLLIA GFVSAQKAKK SKTPIVIAPK EIFVSDLLSK
     MTLEEKIGQL NLPTSGDITT GQANSSNIAK KIEEGKVGGL FNIKSVQKIR EVQKIAVEKS
     RLKIPLLFGM DVIHGYETTF PIPLGLSCTW DMNLIKRSAQ IAAQEASADG INWTFSPMVD
     ISRDPRWGRV SEGSGEDPYL GSQIAKAMVT GYQGDDLSKN NTILSCVKHF ALYGAPEGGR
     DYNTVDMSKI RMYNDYLPPY KAAVDAGTAS VMASFNEIDG IPATGNKWLL TDLLRKDWGF
     KGFVVTDYTG INEMTEHGMG DLQTVSALAL NAGVEMDMVG EGFLLTLKKS LEEGKVTMQQ
     IDNAVRLILN AKYDLGLFLD PYKYCDANRA KTEIFTSTHR SEARKIAAES LVLLKNENQT
     LPLKKSGTIG VIGPLADAKE NMAGTWSVAT KQENSVSLIA GIQSVVGVSA KILYAKGSNL
     DYDAALEERA TMFGKTLHRD QRTNEELLFE ALKIANQSDV IVAALGESAE MSGESSSRTN
     LEIPQAQKDL LQALLKTGKP VVLVLFDGRP LVITEENKTV PAILNVWFAG SEAGYAIADV
     LFGNENPSGK LTATFPRSVG QVPIYYAAKN TGRPLGNKEG IFEKFKSNYI DERNEPLFPF
     GFGLSYTTFN YANLSLSSTK MSFNETIKAT VDITNTGDFD GKEVVQLYIR DIVGSVTRPV
     KELKGFQKIN LKKGEKQMVT FEISVEDLKF YNTNLQFVAE PGKFEVFIGT NSDTINKIEF
     DLVN
//
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