ID A0A395SEY0_FUSSP Unreviewed; 802 AA.
AC A0A395SEY0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 22-FEB-2023, entry version 12.
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=FSPOR_3671 {ECO:0000313|EMBL:RGP70984.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP70984.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP70984.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP70984.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP70984.1}.
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DR EMBL; PXOF01000048; RGP70984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395SEY0; -.
DR STRING; 5514.A0A395SEY0; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000266152; 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; 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 PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF5; BETA-GLUCOSIDASE M-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 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.
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:UP000266152};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..802
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017224696"
FT DOMAIN 721..789
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 802 AA; 85616 MW; 824E84372BAA599A CRC64;
MFLTSVSGLL ALSVLNHGVL AQNQPDVITD DTYFYGQSPP VYPTPEQAET GSWSIAVSKA
KELVSQLTLE EKVNLTAGGQ TTTGCSGFIP GVPRLGFPGL CLADAGNGVR NTDYVSAFPA
GIHVGASWNP ELTYSRSYHM GSEAKTKGVN ILLGPAFGPL GRVVEGGRNW EGFSNDPYLA
GRLGHEAVTG IQKAGVVACG KHWLAQEQET HRLAAAATKA EAVSSNIDDK TLHELYMWPF
ADAVHAGLAS VMCSYNRANG SYACQNSKLL NGLLKGELGF QGFVVSDWGA QHSGMASALA
GLDVAMPSSI VWGANLTLGV NNGTIPESHV DGMATRILAT WYQLNQDQPD FPTPGHGLAK
DLTAPHPIVD ARNASSKSTL WDGAVEGHVL VKNTNKTLPL KSNLKLVSLF GYSHKAPDKN
NPEPVVKGAM FAPWAIGAQS ANITELNGGF LGNLNLTYSA IAPNGTIISG GGSGAAAASL
ISSPFDAFVS RARKDGTALY WDFESWDPSV NPISEACIVA GNAWASEGWD RPAVYDDYTD
SLINNVADKC ANTIVVLHNA GARLVDGFIG HPNVTAVIYA HLPGQDSGDA LVSLLYGDEN
PSGRLPYTVA CNETDYGVTL KPDLTLAPNK FQHFPQSDFS EGVFIDYRHF DAKNITPRYE
FGFGLSYTTF EYTDLQVSGP EAQASEYPTG ALTEGGRADL WDVVAVVSAK VSNTGDVDGK
EVAQLYVGTP GDDVPVRQLR GFKKPSIKAG ETVEVKFELT RRDLSVWDIV AQEWQLQRGD
YNIFVGSSSR ELPLQSTLMI QS
//
