ID A0A094F4E2_9PEZI Unreviewed; 845 AA.
AC A0A094F4E2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=V498_07988 {ECO:0000313|EMBL:KFY83548.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY83548.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY83548.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
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:KFY83548.1}.
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DR EMBL; JPKA01002519; KFY83548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094F4E2; -.
DR HOGENOM; CLU_004542_4_0_1; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000029270; 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:SF28; BETA-GLUCOSIDASE-RELATED; 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 408..569
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 845 AA; 91719 MW; 03E55C75D6FB7704 CRC64;
MAQENTEPPT PPSPIETLDV EAVLAKLSTS EKVDLLAGID FWHTKAIPKH GIPSLRFTDG
PNGVRGTRFF NGVPAACLPC GTALGATWNV PLLQEAGTLM GKETIAKGAH VILGPTVNMQ
RSPLGGRGFE SFSEDPVLAG SSAAAIVNGI QETGVVASIK HFVANDQEHQ RMAVDSIITE
RALREIYLLP FQIAVRDSKP GSFMSSYNKL GGTHVSENPR ILGDILRKEW GWEGLIMSDW
YGTYSTSEAM NAGLDLEMPG PSRWRGQLVT HVLMANKISK QTLDARVREV LRLVSRVAKT
GVPGNAPEGS RDTPETSALL RKIGGESIVL LKNENKALPL DKAKTVAVIG PNAKIAAYCG
GGSATLLPYY ATTPFDGIAA KATETKYSVG CYSHVLLPLL GQNLKTADGK VGVTFKAFTD
PVEVSDRQPV DVIHLADTYM YLVDYYHPKL TEDLFWTEVE GFFTPDEDGD FEFGLTVHGT
GKLFLDDELL IDNETVQRSG GSFFNVGTVE EVGVKNLKAG QTYKVKVEYA SGVTSKLSDS
DGVVSFGGGG IRIGGARVID PTEEIEKAVT LAKSVDQVVI CAGLNKDWEQ EGHDREHMDL
PGRTNDLISA VADANPNTVV VIQSGCPVRM PWAHKVSSLA QAWYGGNETG NAIADILFGD
VNPSGKLPLS FPVRNEDNPA FLNYRSSHGR VLYGEDIYVG YRFYEATLKA TLFPFGHGIS
YTTFRLSELA ITNDGTNLTV QVLVENTGDR DGSEVVQVYV AQHAPCVKRP LKELKGFAKE
NIAAGKSKVV IVTIETKYAT SYWDEERDTW VSEKDTYDVL VGTTSAETPL KASFEIEESK
WWLGL
//
