ID X0IEN9_FUSOX Unreviewed; 861 AA.
AC X0IEN9;
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|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744, ECO:0000256|RuleBase:RU361161};
GN ORFNames=FOPG_12630 {ECO:0000313|EMBL:EXL71664.1};
OS Fusarium oxysporum f. sp. conglutinans race 2 54008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089457 {ECO:0000313|EMBL:EXL71664.1};
RN [1] {ECO:0000313|EMBL:EXL71664.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54008 {ECO:0000313|EMBL:EXL71664.1};
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., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW808.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXL71664.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=54008 {ECO:0000313|EMBL:EXL71664.1};
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 "The Genome Annotation of Fusarium oxysporum PHW808.";
RL Submitted (MAR-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 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; KK033221; EXL71664.1; -; Genomic_DNA.
DR EMBL; KK033221; EXL71665.1; -; Genomic_DNA.
DR EMBL; KK033221; EXL71666.1; -; Genomic_DNA.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000030676; 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:SF27; BETA-GLUCOSIDASE; 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}.
FT DOMAIN 424..584
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 95780 MW; 3ABB459E89E84D63 CRC64;
MNDSNTPSTP DTEYSPPCSP QQKIQHLRDT RSAAREKLAR LTLVEKVSLL TAADFWRTKA
IPEKGIPSIK TTDGPNGARG GVFVGGTKAA LFPCGISLAA TWNKDLLYQV GQHLALEVRA
RSAEMLLAPT VCMHRHPLGG RNFESFSEDP LLTGKLAAQY IKGLQDRGVA ATIKHFVGNE
QETNRLTIDS LITERPLREI YLKPFEIAVR EANPWAVMTS YNLINGVHAD LNKHTLKDIL
RGEWGYEGTV VSDWGGINSS IESVEAGCDI EFPYSSKWRL DKLVTAVNEG RISIEDINQA
AENVLTLVER LKGGDMSPEA PEREDDREET RELIRIAGHE GLTLLKNDGG ILPLCPKSTK
VAVIGPNANR YIAGGGGSAS LNPYYNTIPL DSIRKVSKQK VSFAQGCHIH KWLPVASEYC
TEQSGKPGVH IDWYAGDKFE GNPVVKQRRT NTDLFLWDSA PLSEVGPEWS AVATTYLMPR
TTGKHTISFM SVGPGKLFIN DKLVLDLWDW TEEGEAMFDG SIDYLVDVDM EADKTVELRV
EMTNELRPIS KQKQFGITHK YGGCRIGYKE QDQVDYIQQA VQAARDADVA IVIVGVDAEW
ESEGYDRQTM DLPADGNQDR LIEAVVKANP KTVVINQSGS PVHMPWVDRV PVILQGWYQG
QEAGNALADV LFGIENPSGK LPSTFPKRIE HTPAWHTWPG ENHKVLYGEG LYIGYRHYDH
AKIEPLFPFG HGLSYTTFEY GRPEISTKTL TPDGEIKITL AISNIGARAG AEIVQLYVHD
EKSRLPRPEK ELVAFEKVFL EAEETRHITI KLDKYAVGYY DETVPGWIAE EGAFKVLIGA
SSTDIRQSTR FNVKESFTWV F
//
