ID A0A1Y1VHL7_9FUNG Unreviewed; 771 AA.
AC A0A1Y1VHL7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=BCR36DRAFT_580820 {ECO:0000313|EMBL:ORX56513.1},
GN BCR36DRAFT_580821 {ECO:0000313|EMBL:ORX56514.1};
OS Piromyces finnis.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=1754191 {ECO:0000313|EMBL:ORX56513.1, ECO:0000313|Proteomes:UP000193719};
RN [1] {ECO:0000313|EMBL:ORX56513.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Finn {ECO:0000313|EMBL:ORX56513.1}, and finn
RC {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "Genomes of anaerobic fungi encode conserved fungal cellulosomes for
RT biomass hydrolysis.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX56513.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Finn {ECO:0000313|EMBL:ORX56513.1}, and finn
RC {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:ORX56513.1}.
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DR EMBL; MCFH01000007; ORX56513.1; -; Genomic_DNA.
DR EMBL; MCFH01000007; ORX56514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1VHL7; -.
DR STRING; 1754191.A0A1Y1VHL7; -.
DR EnsemblFungi; ORX56513; ORX56513; BCR36DRAFT_580820.
DR EnsemblFungi; ORX56514; ORX56514; BCR36DRAFT_580821.
DR OrthoDB; 2963694at2759; -.
DR Proteomes; UP000193719; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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:SF10; BETA-GLUCOSIDASE F-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:ARBA00023001};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000193719};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..771
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011907583"
FT DOMAIN 631..702
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 718..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..757
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 84663 MW; 2935364598E77AF1 CRC64;
MKFNTVLSTV ALLCASKTLA MTWEEADAKA REWVADLTNE EKITLTTGRE NMQGVCVGSI
DPIERKGFKG ICLQDGPAGV RFGKGTATSW QASINTAATF DRTLLRKVGE AQGNEFYQRG
INFALGPAMG IQRAPASGRI WESFGEDPFY VAQCGLEVVK GIQSQGVVAT SKHFIGNDQE
NNRGSSTSNI PEQALWEVYM EPFYRAVIDG ESNAVMSSYN AINGTYSVQN ERLLTKYLKG
KLGFQGAVVS DWWSIFDVEK SFKAGMDMNM PGGKYWGPDY IGDSFWGEHI QECIDAGIFP
QERLDDAALR IIRTLYKAGQ MENFPDVNLY VDTLTEENIA LNRKVGADSN VLLKNAEAIL
PIKGVNKIAV IGKDSMPTKF CEDMKCSDGT LALGWGSGTT DFKYIIDPLS ALTERAKQDN
IEVVSYGEDD AEGGAEAAKD ADLAIVFVQA DSGEEYITVE GNAGDRLNLD LWHGGNELID
AVASVNENTI VVIHAPGPVN VPFLDKVKGV VFAGMPGQET GHAIADVLFG DVNPSGHLPY
TWAPREDYPA DVKYEPEYPD GGEKMTVYDY NEGLFVGYRW FDKQGIEPTF PFGYGLSYTD
FKYENLEGDM EDDGLYVTLT VTNTGDVAGA AVPMIFLSFP EVVKDHPARV FKGFDKVMLQ
PGESQEVTIF IDNHDLSYFD VDAMEYVKPE EGKYTIYAGS NARDLPLSTS VLANGECESE
NEVDADIDAG DNEDSADEEV EVDAEVDADD NEDSADEEET EALRKRAYKL Y
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