ID A0A2H3G341_FUSOX Unreviewed; 838 AA.
AC A0A2H3G341;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=AU210_013901 {ECO:0000313|EMBL:PCD24786.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD24786.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD24786.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD24786.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD24786.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD24786.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
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 -!- 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:PCD24786.1}.
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DR EMBL; MABQ02000010; PCD24786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3G341; -.
DR STRING; 327505.A0A2H3G341; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000219602; Chromosome 12.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000219602}.
FT DOMAIN 403..563
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 838 AA; 91264 MW; 93665E1905559663 CRC64;
MHILQRQPID VESTLASLTL AEKISLLSGS DFWNSQAISS HGISSVKCTD GPNGARGGRF
FNPVPALCIP CGTGLGATWN PDLLYSAGQL LSRECDAKGA HVWLGPTVNL VRGPLNGRGF
ESFSEDPHLS GVLATAIING VQSRGTAAAL KHFVANDQET AKMSTDICMS ERALREVYLK
PFQMAVRDAK PKIVMSSYNK VNGVHVSESR KLLKDVLRSE WGFDGLVISD WYGTYGCTDA
LNAGVDIEMP GPSRHRADKA LVAVVSGKVS RKTIDERARK VLELGNATAS ARVSTKESTR
DSPEDRALNR RLATESLVLL KNSDKILPIN PQDCEDIAII GPNAKLPAAC GGGSANLRPY
YTSSVFQGIS DQLPSNANVH FEPGVFGHVL LPYFTGDHVT DQNGLPGVSI SFFNEPESAW
QTRKPFDQQS IPDTTYQLMD YDHPERGGTF YMSMTAYYKP DIEGTYEFGL ASYGVSRLYI
DEHLVIDNAT SQTHAGMFFG HGSREERGTY DMKAGKTYRL RVEAGSASTS ITTGGSFIPI
PGGACRLGGC LKLDPEQGIR RAVTVAKKCK HTFVVVGLNA DFEKEGKDRE SMSLPPHVDD
LVSAVLKAQP NAIVVTQAGN PIEIPWRHQA KTILHSWYGG NETGNAVADV VFGKVNPSGK
LPVTFPSRLQ DGPTFLSFGS DNGRIYYSED VFVGHRWFDA RGIEPAFEFG HGLSYTTFST
SNILVAEDGV RVEVKNTGKM AGAEVVMLYV SYDAAKSGQK SRFHRPVRTL IGFQKVFLEP
GQEATAFVAL DKYSTAVWDE TADSWLCEAG TYTASFRSSS DSLEVSFKVE RDLYWNGA
//
