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Database: UniProt
Entry: A0A1H1Q546_9FLAO
LinkDB: A0A1H1Q546_9FLAO
Original site: A0A1H1Q546_9FLAO 
ID   A0A1H1Q546_9FLAO        Unreviewed;       739 AA.
AC   A0A1H1Q546;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=SAMN04489797_1052 {ECO:0000313|EMBL:SDS18545.1};
OS   Winogradskyella sediminis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=1382466 {ECO:0000313|EMBL:SDS18545.1, ECO:0000313|Proteomes:UP000198963};
RN   [1] {ECO:0000313|EMBL:SDS18545.1, ECO:0000313|Proteomes:UP000198963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA_55 {ECO:0000313|EMBL:SDS18545.1,
RC   ECO:0000313|Proteomes:UP000198963};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; LT629774; SDS18545.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1Q546; -.
DR   STRING; 1249933.SAMN04489797_1052; -.
DR   Proteomes; UP000198963; Chromosome I.
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          658..727
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   739 AA;  81868 MW;  C25DF842A72E0419 CRC64;
     MKLRFLYIIL CGTLSTGFSQ NYEAKVDSLM NLMTLQEKIG QTVMYSGHWD QTGPFVGADN
     GKYIREGNMG AMLNAMSVKG TRDLQKIAVE ESRLGIPLLF GYDVIHGHRT IFPINLGLSA
     SWDLIMVEES SRIAAEEASA EGIHWTFAPM IDVSREPRWG RISEGAGEDV FLNNEIGKAY
     IHGFQGDDLS QPNTILACAK HYVAYGAAQA GRDYHTTNMG EGELRNVYLP PFKAAVDAGV
     ETFMSAFNEL NGVPTSGNKF TLRDILRDEW KFDGFVVSDY TSINEMIQHG FAKDSIDAAR
     IGMNAGVDMD MVGHVYRLHL KTLVEEGKVS EAYINDACKR ILLAKFKLGL FDDPYRYIDE
     SREANTAYKP EFLAKAREIA AASSVLLQNN NKVLPLSKKT KSIAFIGPLV KDEADILGNW
     AAKGERGGKA VSVFEGVSEY LKANQILYAK GCDILNDDRS GFKEAISISQ KADEIVLVMG
     ENHHMSGEAA SRTDLKIPGI QPELIKKIRE ANPNKNITLV LMNGRPLNLS DEVNLVDAIL
     EVWFPGTMGG AATADLLFGT VNPSGKLTVT FPRNVGQVPI YYNMKNTGRP IPENNPKQDY
     KSNYIDVPNT PLFVFGHGLS YTKFRYSDLK LSSENLTFSN TIEASVTITN TGNIDGFEIV
     QLYIHDKVGS VTRPVKELKG FQKIFLKKGE SKTVTFTISA EDLKFYNSDM IYGVEIGEFE
     IAIAPSSDFK FKHTFNLND
//
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