ID A0A094JHJ9_9PEZI Unreviewed; 813 AA.
AC A0A094JHJ9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 30.
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=V502_09334 {ECO:0000313|EMBL:KFZ08468.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ08468.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ08468.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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 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 -!- 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:KFZ08468.1}.
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DR EMBL; JPKE01003040; KFZ08468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094JHJ9; -.
DR STRING; 1420915.A0A094JHJ9; -.
DR HOGENOM; CLU_004542_2_1_1; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000029308; 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:SF5; BETA-GLUCOSIDASE M-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029308};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..813
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001905271"
FT DOMAIN 735..801
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 813 AA; 87213 MW; E207639AB90D5EB8 CRC64;
MVSFTSRLTT ASYLSLSIFA GTAFGQNITD DTYFYGQSPS VLPSPEIPGT LSWQTAHTKA
VALVSQMTLA ERANITVGYD PTTGCSGVTG TVPRLGWEGL CLADAGQGLR ATDFVNAYPA
GISVGSSWNK ALTLQRATHM AAEFKKKGVH VLLGPVVGPL GRVALGGRNW EGFSNDPYLS
GSLVHDTIKG IQNAGVIASV KHFIGNEQEV NRNPIAANAA TGGIGGGGGL ASTSPGNVSQ
KVESVSSNID DKTMHELYLW PFADAVHAGS ASVMCSYQRI NNTYGCHNQK TQNGLLKTEL
GFEGFVVSDW GAQHAGIASA EGGLDMAMPN GGFFWGEDGS NLTTFVQNGS IPEARLTDMA
TRIVAAWYQL GQDRDFPPVS LPALYNVSHK AVNARDPASK PILLQGAIEG HVLVKNVNKA
LPFKKPKLLS LFGYDAVAPP RVNLVDANFN YKFGFLSNTD FFWRDAFAPP FTNPGQIGPN
GTLIVGGGSG GTAPAYISAP FDALQERAYT DGFQLLWDFH STAPLVDQAS DACLVFINAF
ATEGVDREGL HDDYSDDIIL NVASACSNTI VVIHNAGIRL VDTWIEHPNI TAVIFAHLPG
QDSGRAAVSL LFGDESPSGK MTYTVAKNES DYNVPVAQPA DEFFFFPQDD FTEGVYIDYR
DFDRKNITPR YEFGFGLTYT TFEYSDLSVS LVQNASTSRT APESPIIEGG MESLWDVIAT
ASAVITNTGD VTAKEVAQLY VHIPGGPVRQ LRGFDKVEIA PGESETVRFT LLRRDLSDWN
VAEQAWVLQQ GSYPVWVGAS SRNLPLSGEL TIS
//
