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Database: UniProt
Entry: S7VXH7_9FLAO
LinkDB: S7VXH7_9FLAO
Original site: S7VXH7_9FLAO 
ID   S7VXH7_9FLAO            Unreviewed;       738 AA.
AC   S7VXH7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE            EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN   ORFNames=ADIWIN_0210 {ECO:0000313|EMBL:EPR74846.1};
OS   Winogradskyella psychrotolerans RS-3.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=641526 {ECO:0000313|EMBL:EPR74846.1, ECO:0000313|Proteomes:UP000014962};
RN   [1] {ECO:0000313|EMBL:EPR74846.1, ECO:0000313|Proteomes:UP000014962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS-3 {ECO:0000313|EMBL:EPR74846.1,
RC   ECO:0000313|Proteomes:UP000014962};
RX   PubMed=23950132;
RA   Kumar Pinnaka A., Ara S., Singh A., Shivaji S.;
RT   "Draft Genome Sequence of Winogradskyella psychrotolerans RS-3T, Isolated
RT   from the Marine Transect of Kongsfjorden, Ny-Alesund, Svalbard, Arctic
RT   Ocean.";
RL   Genome Announc. 1:e00630-e00613(2013).
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:EPR74846.1}.
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DR   EMBL; ATMR01000007; EPR74846.1; -; Genomic_DNA.
DR   RefSeq; WP_020895811.1; NZ_ATMR01000007.1.
DR   AlphaFoldDB; S7VXH7; -.
DR   STRING; 641526.ADIWIN_0210; -.
DR   PATRIC; fig|641526.4.peg.210; -.
DR   eggNOG; COG1472; Bacteria.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000014962; Unassembled WGS sequence.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:EPR74846.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014962};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..738
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004546495"
FT   DOMAIN          658..727
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   738 AA;  82243 MW;  BF83F860B28323C6 CRC64;
     MKLRFLYIAL ICLFNQSFSQ NYEAKVDSLM QLMTLQEKIG QTVMYGGHWD QTGPFVGADN
     GKYIREGNMG AMLNAMSVKG TRDLQKIAVE ETRLGIPLLF GYDVIHGHRT IFPINLGLSA
     SWDLKMVEES SRIAAEEASA EGIHWTFAPM IDVSREPRWG RISEGAGEDV YLNNEMGKAY
     IHGFQGDDLS QPNTILACAK HYVAYGAAQA GRDYHTTNMG EGELRNVYLP PFKAAVDAGV
     ETFMSAFNEL NGVPTSGNKF TLRDILRDEW KYDGFVVSDY TSINEMIQHG FAKDSIDAAR
     IGMNAGVEMD MMGHVYRLHL QKLVEENKVP EAYINDACKR ILLAKFKLGL FDDPYHYIDE
     EREATTAYKP EFLTKAREIA AASSVLLQNK NNALPLSKNI KKIAFIGPLV KDESDIIGNW
     AAQGDRGGKA VSVFEGISEY LNSNQILYAK GCDILKDDDS GFKEAISISK EADEIVLVMG
     EDHHMSGEAA SRTDLKIPGI QPELIKKIRE ANPNKKITLV LMNGRPLNLS DEVNLVDAIL
     EVWFPGTMGG AATADLLFGT VNPSGKLTVT FPRNVGQVPI YYNMKNTGRP IPESNPKEDY
     KSNYIDVPNT PLFVFGHGLS YTEFKYSHFK LSSENLTFSN TIEASIMITN TGNSDGHEIA
     QLYIHDKVGS VTRPVKELKG FQKIFLKKGE KKTVTFTISV EDLKFYNSEM IYGVETGDFE
     IAITPSSDFK FKHSFQLQ
//
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