ID U4LBJ0_PYROM Unreviewed; 853 AA.
AC U4LBJ0;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=PCON_04448 {ECO:0000313|EMBL:CCX17444.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX17444.1};
RN [1] {ECO:0000313|EMBL:CCX17444.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX17444.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX17444.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HF936646; CCX17444.1; -; Genomic_DNA.
DR AlphaFoldDB; U4LBJ0; -.
DR STRING; 1076935.U4LBJ0; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR OMA; YYPSPWA; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000018144; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..853
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004651836"
FT DOMAIN 775..843
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 853 AA; 93182 MW; 543A9FF47E866FD3 CRC64;
MVNIILLAGL VATTLAADLP TQPSSALAYS PPYYPSPRID GGGDWKAAYQ RAKAFVDQLT
LTEKVNLTTG TGWQSDNCVG NVGTIPRLNF PSLCMQDSPL GIRFGTYSSA FPAGMNAAMT
WDRELMYLRG LAMGEEFKGK GVNMALGPVA GPLGRHPEGG RNWEGFSADP MLTGVGMFET
VKGMQDAGVI ATAKHYIGNE QELFRQVGEG RQWGFNITES LSSNIDDRTM HELYLWPFAD
AVRANVGAIM CSYQQVNNSY GCANSKLLNG LLKDELDFQG LVMSDWSAQH SGVASALAGL
DMSMPGDVTF NSGDSYFGGN MTMAVLNGSL PIWRVDDMAT RIMSAYYFTH QDKNFPETNM
NSWTTDDYGY LRYYSKEHYG LVNKQVDVRG QHHKIIRELS AKANILLKNS GVLPLTGKEK
QIALFGSDAG ETPYGPNGHP DRGGNDGTLA MGWGSGTANF PYLVTPLEAI KAKALQLGQV
VQSVLDDYAY SQIKDTARQA SVCLTFVSAD SGEGYIDVDG NRGDRKNLTL WHNGDDLIKT
VASTCKNTVV VIHSVGPVLL EEWIDHPNVT AVLFAGLPGQ ESGNSLTDVL YGAVNPSGRL
PFTIAKHRED YGVKLTNSST VAVPQQDFTE GLFIDYRHFD KNEITPRYEF GYGLSYTTFK
YSHLKIRRLA DPAGYKPAKG MQAKNDAVSK KLDPADYLFP KDFSSWKVGN FIYPYIKSVS
DVKQGSYPAP KGAYDTSAQP VPAAGGAPGG NPSLYENVYE ISVVVTNTGK KAGEEVVQVY
LETGLADDPK IVLRQFEKVM LRVGESKTVK VKLNRRDLMR WSVVKQDWTC TEGKKVVHVG
CSSRQFALSA NLA
//
