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Database: UniProt
Entry: W9JWX0_FUSOX
LinkDB: W9JWX0_FUSOX
Original site: W9JWX0_FUSOX 
ID   W9JWX0_FUSOX            Unreviewed;       868 AA.
AC   W9JWX0;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=FOZG_13407 {ECO:0000313|EMBL:EWZ33703.1};
OS   Fusarium oxysporum Fo47.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660027 {ECO:0000313|EMBL:EWZ33703.1};
RN   [1] {ECO:0000313|EMBL:EWZ33703.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo47 {ECO:0000313|EMBL:EWZ33703.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum Fo47.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EWZ33703.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Fo47 {ECO:0000313|EMBL:EWZ33703.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of the Genome Sequence of Fusarium oxysporum Fo47.";
RL   Submitted (JUN-2012) 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         ECO:0000256|RuleBase:RU361161};
CC   -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC       {ECO:0000256|ARBA:ARBA00004987, ECO:0000256|RuleBase:RU361161}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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DR   EMBL; JH717905; EWZ33703.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:FOZG_13407; -.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000030766; 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:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF28; 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; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361161};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361161}.
SQ   SEQUENCE   868 AA;  96721 MW;  FFB3DC5BD039094B CRC64;
     MTLVKAQPPL NNGHVRNEAK EWAQDKISQM TLEEKVLLLT GEDLWRTNAI PRLGISRIKT
     SDGPVGVRGG IFTDGVSAAS APTGVSLAAT WDLSVIRDVC SVLIHEAKSK EVDVLLGPTV
     CIPRTPLGGR NFEAYSEDPY LTGKIAGEFI NHLQDAGIGA CIKHLAANDQ ETRRFFIDEK
     IPDRALREIA LQPFQIAIRD SNPWTVMTAY NKINGTFCSA HDFLIQDVLR KEWGWDGLVM
     SDWFGTNSVV PSVKAGLDLE MPGPVRRRGK HLIDAYQKGL VDLSFIDASA SRVLELVHKV
     GKSNIPDWKE GKEKADDLPE HRAIFRRAGA EGIVLLKNSA KLLPLSNLDG RRIAILGPNA
     LRSVATGGGS SNLAPHYRTT PYQSIKSEIA AKFPTAKVHA HAGILTHRYI PLVDQNVMTN
     PETGKPGFQL CLYRNMNHGG QPFMVEHRPS SNLVCYDGLP PELTTGERYS YRGRTVLKPK
     TTGLHEFSLS SCGPGKLMLD GEVIIDIERH WWSPKSSLFM SYGSPEKRVK VYMEAGREYE
     LLLESISREP KPYNLDYMAE LEREEVQDGG RVGFMENPGD LDRFFQDGIG MARDSDVAIV
     VVGKDHEWET ETSDMVSMDL PGRSNEFISA VAAANPNTIV VNQTGSPITM PWKDKVSAII
     QAWYQGQEQG NCLADVLLGT VNPSGKLPIT FPKRIEDTPP YDNYPGKNDV VYYGEGIYAG
     YRFYDHRKIE PLFPFGTGLS YTTFEYSNMR ISGNEFHEEA GIEVEVDVTN IGPRDGKEIV
     QFYVGQINPR LHRPVRELKG WEKIFVPVGQ TVTARMKIDK VSLSYWDDSV AKWVIEKDAE
     YRVTAAKDSS DEGLTAAFRS PKEYQWVN
//
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