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Database: UniProt
Entry: A0A0C1CTB6_9FLAO
LinkDB: A0A0C1CTB6_9FLAO
Original site: A0A0C1CTB6_9FLAO 
ID   A0A0C1CTB6_9FLAO        Unreviewed;       881 AA.
AC   A0A0C1CTB6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, 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=OA85_07920 {ECO:0000313|EMBL:KIA87496.1};
OS   Flavobacterium sp. AED.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1423323 {ECO:0000313|EMBL:KIA87496.1, ECO:0000313|Proteomes:UP000031403};
RN   [1] {ECO:0000313|EMBL:KIA87496.1, ECO:0000313|Proteomes:UP000031403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AED {ECO:0000313|EMBL:KIA87496.1,
RC   ECO:0000313|Proteomes:UP000031403};
RA   Gale A.N., Newman J.D.;
RT   "Flavobacterium sp. AED Genome.";
RL   Submitted (OCT-2014) 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   -!- 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:KIA87496.1}.
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DR   EMBL; JSYM01000001; KIA87496.1; -; Genomic_DNA.
DR   RefSeq; WP_039108993.1; NZ_JSYM01000001.1.
DR   AlphaFoldDB; A0A0C1CTB6; -.
DR   STRING; 1423323.OA85_07920; -.
DR   OrthoDB; 9805821at2; -.
DR   Proteomes; UP000031403; 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; 2.
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; 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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR30620:SF16; LYSOSOMAL 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   Pfam; PF07691; PA14; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KIA87496.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..881
FT                   /note="beta-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002142966"
FT   DOMAIN          488..626
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   881 AA;  98109 MW;  D9BA843C5EA11CF4 CRC64;
     MKKTTLVLVL FLGFFNQGFA QKKYPYQNPK LPVEDRLTDL LSRMSLDEKV RQMDMYKGEY
     FKEKENFSKT KSDVKIGNLG IGAIHDIYPR SAKMINDLQS EVIKKNKWGI PALIMCEMLH
     GYLDDESTAF PMSIGLGATW DTNLMDKVGK VIGTEARAHG VHFGLGPNLD VGREPRWGRV
     AETFGEDVYL TGELGLAMIK GMQGNDLTSD RSIIAEPKHF AVHGIPQAGG NSSPVLIGER
     SAREDFLPSF EKAFRKGGAL GTMCAYSELD GIPCAANHWL LTDVLRKEWG FKGIVVSDLG
     AIKYLQTTHY VADSPKESIR QAISAGVDMQ FYDFTNEFWQ QTIIELVNEK KLTMEQIDRA
     AGGVLRLKFL LGLFENPYTD KNLIKERFHS KENQDLALEA GHKSIVLLKN ENNILPLNKD
     IKTIAVIGPN ANASRLGGYS VKNKVGTTIL EGIQQVVGTK ANVLYEEGVS LIVKGQVIPS
     KFLFAPDESQ NGLKGEYFNN RNLEGNPALT RIDNQLEFDW PWSPGDGVSD DDFSIRWTGY
     IKSEKAFDGW LGLSSDDGIR MWIDDQLVID NWTKGATNMV TTPKNIEAGK KYKVRIEMWE
     GGWGARAHLR WNLEKVNFQP AIDIAKKADI AIVVLGESNE LVEENRDVAT LDLHGMQQEL
     IEAIQQTGTP VVCVLLNGRP LSVNWINENI PAVVEAWFPG EAGGKAVADV LFGDYNPGGK
     LPITFPKSVG QLPIYYNQKP SAIHRYVTES ENPLYTFGYG LSYTTFEYSN LSISAAAINA
     DGELKVSVNV KNTGNYDGDE VVQLYINDVY SSVTTPLKTL KGFERVFIKK GETKQVTFTL
     TPDELAIWNR EMKRVVEPGD FEVMVGGNSV DLLKTNFKVL N
//
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