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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//