ID A0A1Y3NHX0_PIRSE Unreviewed; 773 AA.
AC A0A1Y3NHX0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE Flags: Fragment;
GN ORFNames=PIROE2DRAFT_42946 {ECO:0000313|EMBL:OUM64064.1};
OS Piromyces sp. (strain E2).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=73868 {ECO:0000313|EMBL:OUM64064.1, ECO:0000313|Proteomes:UP000195826};
RN [1] {ECO:0000313|EMBL:OUM64064.1, ECO:0000313|Proteomes:UP000195826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2 {ECO:0000313|EMBL:OUM64064.1,
RC ECO:0000313|Proteomes:UP000195826};
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 "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
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}.
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DR EMBL; KZ150874; OUM64064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3NHX0; -.
DR STRING; 73868.A0A1Y3NHX0; -.
DR OMA; HMAIGTT; -.
DR Proteomes; UP000195826; 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; 3.90.1220.10; Cellulose docking domain, dockering; 3.
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; IPR002883; CBM10/Dockerin_dom.
DR InterPro; IPR009034; Dockerin_dom_fun_sf.
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; PF02013; CBM_10; 3.
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 SUPFAM; SSF64571; Cellulose docking domain, dockering; 3.
DR PROSITE; PS51763; CBM10; 3.
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, ECO:0000313|EMBL:OUM64064.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000195826};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 644..680
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT DOMAIN 691..727
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT DOMAIN 735..772
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT REGION 622..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OUM64064.1"
SQ SEQUENCE 773 AA; 84015 MW; 1D166BAA3809D352 CRC64;
GINSAATFNK ELLYQVGKDQ GTEFYVKGIN IALAPSMNIL RAPASGRVWE NFGEDPYLSG
VCGTQITKGM QDSGVIVAAK HYVANDVEHN REASTSNLDD QTLMEIHVEP FYRTITEGDA
GSVMASYNAI NGVYVVQNKK VLTEILKEGM NFQGFIMSDW WAIHDLEGSF NAGMDMNMPG
GKAWGPDYIN DSFWGPNISN AIKSGKVSSS RLDDAVRRII RTLYRFDQMD NYPSINLKAK
SMHAETNRQA AIESTILLKN ADSVLPLTKK YKKIAVIGKD ADMAQSCTDT ACTNGNIIQG
FGSGTTDFVG VSDPYTSIKN RASKDGITVV SSLSDDASAG ANTAKDADIA LVFVRATSGE
EYIKVDNNKG DRNDLDLWHN GNELVKKVAA VNKNTVVVIH APATVNLPFL NDVKAIIHAG
MPGAESGNAI ASILFGDSNP SGHLPFTWAK REEYCCDVAY PDELPKGGSQ KTVYDYKEGL
FVGYRWFDKK GIVPTFPFGH GLSYTTFDYS NLSVTLEKNG SDVSGLKATF TVENTGAVEG
ATVPMLFVGY PEVSEMGDYP VRGLKAFDKI NLKAGEKKTV TLIVDQHGLS YYNASKKSFV
VPTGGEYTVY VGKSAGDLPL KTSVKNTQGT NENSSSSSTN DTTECSVDGY KCCSKANAKV
KYTDSTGNWG VENGEWCFIK KQDEQPHQSS ECFSTVLGYP CCKGDKVVYT DKNGQWGVEN
NQWCGIGGAQ SATNKCPYQS KNGYPVCTTT TKVVYTDSDK WGVENGNWCI MCN
//
