ID A0A2H3GP17_FUSOX Unreviewed; 751 AA.
AC A0A2H3GP17;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=AU210_011015 {ECO:0000313|EMBL:PCD31360.1};
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:PCD31360.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD31360.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD31360.1,
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:PCD31360.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD31360.1,
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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:PCD31360.1}.
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DR EMBL; MABQ02000007; PCD31360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3GP17; -.
DR STRING; 327505.A0A2H3GP17; -.
DR OrthoDB; 1934916at2759; -.
DR Proteomes; UP000219602; Chromosome 9.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; 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 PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF27; BETA-GLUCOSIDASE; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000219602}.
FT DOMAIN 89..324
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT DOMAIN 360..635
FT /note="Glycoside hydrolase family 3 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01915"
FT REGION 478..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 82738 MW; 5EC245B9DD7DB741 CRC64;
MKSVTPPTLL HHHHPVGRES HQPLTFAKAV KEVSFGHDPS AVASRLLTEL SLTERLHLLD
GDVPFWEGLR GILCDRYNRK PFVMGAIPRL NIPGVKFTDG PRGVVMGSST AFPISMARGA
TWDIELERRV GNAIGLEAKA QGANYFAGVC INLPRHPAWG RIQETYGEDP FLLGEFGVAL
TQGVQNHVMA CVKHFALNSM ENARFRVDVE IEEDVLHEVY LAHFRRVVEA GVASVMSSYN
SVNGEWAGQS KALLTNILRE QWKFTGFVMS DFIFGLRDAA LSVKNGLDIE APFAQQRAMH
LENALRSGEL SWIDVNKLAT RILRTQLEFA SRFLSETPDA SVVFCKEHRQ LAREVAERSI
ILLKNNKINS TPLLPLNEAD VTRLTLIGRL ANKPNTGDKG SSQVFSPTVV TPYQGLKDGI
SNAEIILDDG DSPESAAISA EKADVAVVVV GYDASDEGEF VVPSLQNDPR LSELFPPTKN
SDQKEMLSIV QGNPSQDKQS STSALEVGAG GDRLSLRLRP RDVEIINAVA SVNSKTIVVL
ICAGAVIMEE WKDKVPAIMI SWYAGAEGGH ALADVLLGRV NVGGRLPFSI PQDESHLPDL
DIEASAIKYD RWYGQSLLDK LGVDAAFPLG YGLSYTEFRF SNLEFEPRME STGCNSVKVA
VDVENTGQRS GHHVAQVYGY PNMAEYPHRV LLGFRSVYLR AGELRRIFAD ASLRPIERWV
DGQFCLLVDH FQIEVAAYAG DKHGVRKMCQ L
//
