ID A0A395N593_9HYPO Unreviewed; 758 AA.
AC A0A395N593;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=FIE12Z_800 {ECO:0000313|EMBL:RFN54953.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN54953.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN54953.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN54953.1,
RC ECO:0000313|Proteomes:UP000265631};
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 -!- 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:RFN54953.1}.
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DR EMBL; PXXK01000013; RFN54953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395N593; -.
DR STRING; 2594813.A0A395N593; -.
DR Proteomes; UP000265631; Unassembled WGS sequence.
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; IPR026891; Fn3-like.
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.
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:UP000265631};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..758
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017473491"
FT DOMAIN 680..746
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 758 AA; 83106 MW; 45E7F56A8569BAD8 CRC64;
MWPSQLLCLA LQATGVLSRP AESQSPQDEY PSPQGQGRGI WKTAYTKAEA FVSQLTLEEK
ANVTRGFAAD NTCAGNTGTI PRLGWPGLCL MDAGNGVRAT DFVNSYPSAL HVGASWDKNL
TYQRGYYMGK EFKAKGVNVL LGPNVGPLGR TPLGGRNWEG FSVDPYLTGK LSAESIIGHQ
EAGVIANVKH FIANEQETYR RPYHGIEAVS SNIDDKTLHE YYLWPFVDSV KAGVASVMCA
YNRVNGTYAC ENSHLMNGIL KSELEFDGFV MLDWNAVHNL ESANAGLDMV MPMGGFWGEN
LTMAVGNGSV KEERVTDMAT RILAAWYLVG QDNDFPTPGI GMKNLSLPHE QIEARIPESR
PILLEGAIAG HVLVKNENKT LPFKKNPKMI SVFGYDATVA PTKNTDKLFE LGYTSSQEMG
QAVLGDEHHF DQAARGGTIV SGGRAAANSP PYISDPLSAI QQRAAKDGNW VNWDLTSPNP
NVNGASDVCL VFINAMATEG WDRDGLHDDF SDALILNVAR QCSNTIVAIH AAGIRLVDQW
IEHPNITATI IAHLPGQDSG EALVKLLYGE ADFSGKLPYT IAKNESDYNV YEPCGVEEGG
KDPQCDFEEG VYLDYRSFDD RGVEPRYEFG YGLSYTQFEY SSLSVKMEQT AEAEAEADLW
DTYATVQATV SNVGERSGEE VVQLYVAVPN SPPKQLRGFE KVKLDKGDSV EVPFEITRRD
LSVWDVVKQD WALQSGNYTI FVGASSRDLP LKESFKIE
//
