ID A0A395MPX7_9HYPO Unreviewed; 891 AA.
AC A0A395MPX7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 22-FEB-2023, entry version 16.
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=FIE12Z_5739 {ECO:0000313|EMBL:RFN50001.1};
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:RFN50001.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN50001.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN50001.1,
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 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:RFN50001.1}.
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DR EMBL; PXXK01000154; RFN50001.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395MPX7; -.
DR STRING; 2594813.A0A395MPX7; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000265631; 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:SF12; BETA-GLUCOSIDASE A-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:UP000265631};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..891
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017240357"
FT DOMAIN 813..882
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 768..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 96465 MW; D04A2EB19FC62E8B CRC64;
MKANWLAAAA LLAAGTDAAA APQVPGTLAG VKIARDNDLA YSPPHYPSPW MNPNAQGWED
AYAKAKEFVS QLTLLEKVNL TTGVGWENER CVGNVGSIPR MGMRGLCLQD GPLGIRFSDY
NSAFPAGVSA GASWSKALWY ERGKLMGTEF KEKGIDILLG PASGPLGRHA AGGRNWEGFT
VDPYAAGHAM AESIRGIQDA GVIATAKHYI ANEQEHFRQS GEVKSREFNI TESLSSNIDD
KTMHELYNWP FADAVHAGVG AIMCSYNQIN NSYGCQNSKL LNGILKDEMG FQGFVMSDWA
AQHTGAASAV AGLDMTMPGD TAFDSGYSFW GGNLTLAVVN GTVPAWRIDD MATRIMAAFF
KVGKTVEDLP EINFSSWTRD EEGFLQTYSK ENPAKVNHGV NVQHDHKRHI RESAAKGTVL
LKNTDGALPL KKPKFLAVIG EDAGSNPAGP NGCNDRGCDN GTLAMSWGSG TSNFPYLITP
DQGIQRQAVE DGTRYESILA NNQWPQTQAL VSQPNVTAIV FANANAGEGY IEVDGNYGDR
KNLTLWKNGD ELIKNVSAIC PNTIVVLHTV GPVLLTEWHN NPNITAIVWA GVPGQESGNA
IADILYGKTS PGRSVFTWGR TQESYGTEVL YEANNGEGAP QEDFTEGNFI DYRHFDRRSP
STNGKRASND SAAPLYEFGF GLSWTTFEYS DLEVKRVSNA SYSPPVGETI PAPTFGNFST
NLEDYTFPSG IRYLYRFIYP YLNTSSSAEE ASGDVEGRFG ATAEEFLPPN AVNGSAQPRL
PSSGAPGGNP QLWDVLYTVT ATIKNTGDAT SDEVPQLYVG LGGENEPVRV LRGFERLENI
APGESAKFTA QLTRRDLSNW DVNSQNWVIT DHAKKIWVGS SSRNLPLSAT L
//
