ID U4LFR5_PYROM Unreviewed; 820 AA.
AC U4LFR5;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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_08559 {ECO:0000313|EMBL:CCX30362.1};
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:CCX30362.1};
RN [1] {ECO:0000313|EMBL:CCX30362.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX30362.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX30362.1};
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}.
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DR EMBL; HF935439; CCX30362.1; -; Genomic_DNA.
DR AlphaFoldDB; U4LFR5; -.
DR STRING; 1076935.U4LFR5; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR OMA; LDLWDWT; -.
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; 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}.
FT DOMAIN 403..560
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 820 AA; 89761 MW; 720099149A08166C CRC64;
MTGHKPDDTP SQWKSSGSAR VQHLMVSLLS GQDFWRTRAI PSHQIPALKV TDGPNGARGE
YFTDGTPAAL FPCGVSLAAT WNPELLHRIG QALAAETKAR SAQVLLAPTV CLHRSPLGGR
NFESFSEDPL LTGKLAAACI NGLQSEGVGA TVKHFVGNEQ ETWRMSVDSV IEERPLRELY
LKPFEIVVRD AKPWGVMSSY NKVNGVHADM NEFTLQKILR GEWGFDGVVM SDWGGTNSTL
ESIKAGCDLE MPGPTKIRGE QVLEAINDEK LTVEDIDNCV FRILTWIERC GRFDLPLEEL
PETSIDTPST RSLTLEAATE GIVLLKNVSS ILPLGPEVRK IALIGPNVQR AISHGGGSAS
LNPYYQTTPY ESLQSSGKEI LYAPGAETNK WLPLASSCCR TPAGDPGVIL EFYKGDQFLG
PPAVIQHRLK TDLFLWDNAP ASVLPAYSFK IKATITPKTS GTHTFGLSSV GPARLLINGE
VLIDNWNWTI PGEAMFDASI EALATHPMTA GETYEILIES TNAVRPAPKL SPGQPTHGYG
GCRFGFQEEQ TKDLISEAAA VAAEADVAIV IVGLDAEWES EGYDRQSMDL PKDGNQDKLI
EAVAKANPNT VVVVQAGSPV SMPWVEEVMA VVMAWYQGQE AGNALVDILL GKANPSGKLP
MTWPKRLKDT PAYNNWPGED KRVVYGEGLF IGYRHYDRVE VEPQFDFGYG MSYTDFIYSE
PKISGTMRGK ETVQLYIRDP KSRLLRPEKE LKAFVKVDLE PGEAKLVEFS VDKFSVGYYD
PSLGSWIAEE GEFEACVALS AGDIRGSVTF EVTQSFTWVF
//
