ID A0A1Y2UR83_9PEZI Unreviewed; 879 AA.
AC A0A1Y2UR83;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=M434DRAFT_154952 {ECO:0000313|EMBL:OTA86441.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA86441.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA86441.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA86441.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(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 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}.
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DR EMBL; KZ112572; OTA86441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2UR83; -.
DR STRING; 1001938.A0A1Y2UR83; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000194361; 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; 2.60.120.260; Galactose-binding domain-like; 1.
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 InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF27; BETA-GLUCOSIDASE; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SMART; SM00758; PA14; 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.
DR PROSITE; PS51820; PA14; 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:UP000194361}.
FT DOMAIN 442..603
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 879 AA; 97164 MW; 190FC16056A0290D CRC64;
MEHIDDSQFD GIDPNASPFE SVDSNTTPDT EFSPPGSPVP KTTVPRDCRS LARQKLAQLT
LEEKVSLLTA ADFWRTKSIP SKGIPAIKTS DGPNGARGGI FVGGTKAALF PCGISLAATW
NKELLYAVGQ HLADEVKARS ANVLLGPTVC MHRHPLGGRN FESFSEDPLL TGKLASKYIQ
GLQSKGVAAT IKHFVANEQE TNRLTIDSVV IERPLRELYL RPFEIAIRES NPWAVMSSYN
LVNGAHADMN IHTLKDILRG EWGYDGTVMS DWGGVNSTIE SIKAGCDIEF PFSSKWRFEK
VLKAIDEGQL TRDDIDTAAE NVLTLVERTK GDDMSAEEAE REDNREETRA LIREVGAEGL
TLLKNEGQIL PLDPKTIKVA VIGPNANRAI AGGGGSASLN PYYNTLPLDS IRAATEQEVV
YAQGCHIHKW LPVASPFCRD KSGEPGVTLE WFSGDKFQGD VIVTQRRTNT DLFLWDSAPL
SQLGPEWSAI ATTYLTPTTS GRHTVSFMSV GPGRLYVDGK LALDLWDWTE EGEAMFDGSI
DYMVDIEMQA GRPVELRIEM TNELRPVSKQ KLFNMTHKYG GCRIGFKEED QVDYLQQAVD
VAREADVAVV IVGLDAEWES EGYDRKTMDL PSNGSQDRLI EAVVKANPRT VVVNQSGSPV
TMPWANKVPT IIQAWYQGQE AGNALADVLF GLRNPSGKLP TTFPRRLEDT PAYHNWPGEN
LRVLYGEGLY IGYRHYDRAN IAPLFPFGHG LSYTTFEYGR PSLSRRILTE SAPIHLIMAV
TNTGSVAGSE TVQVYVRDDK SRLPRPEKEL VAFEKVSLEP QETKHVIVPL DKYAVGYYDD
SVPAWIAEEG TFNVLIGASA SDIRHSVPFE VKESFTWIF
//
