ID W3XG87_PESFW Unreviewed; 757 AA.
AC W3XG87;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=PFICI_03070 {ECO:0000313|EMBL:ETS85045.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS85045.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
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; KI912110; ETS85045.1; -; Genomic_DNA.
DR RefSeq; XP_007829842.1; XM_007831651.1.
DR AlphaFoldDB; W3XG87; -.
DR STRING; 1229662.W3XG87; -.
DR GeneID; 19268083; -.
DR KEGG; pfy:PFICI_03070; -.
DR eggNOG; ENOG502SMNU; Eukaryota.
DR HOGENOM; CLU_004542_2_1_1; -.
DR InParanoid; W3XG87; -.
DR OMA; LDWNAQH; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000030651; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; 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; 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000030651};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..757
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004834549"
FT DOMAIN 680..746
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 757 AA; 81782 MW; 06F97D415198F748 CRC64;
MATQLGILLL SAASVMASYA SSPPVYPSPP GIGTGKWEEA YVSARELVSQ MTLEEKVNIT
RGFTVSDNVC AGNTGTVPRL NWPGMCLHDA GNGVRATDMV NSYPSAIHAG ASWDKNLTYE
RGLYMGLEFK AKGVNVMLGP NAGPLGRSPL AGRNFEGFSV DPYLSGRLNA ETITGTQDAG
VIAVIKHLIA NEQETYRRPY FGVEAASSNI DDKTLHEYYF WPFMDAVQAG VASAMCSYNR
INNTYGCENS KLMNGLLKTE TSFQGFIMLD WNAVHSLDSA NAGLDMLMPG GGNWGDNLTA
AVHNGSVSED RVTDMAVRIT AAWYLVGQDG TNFPTPGIGM KNLTLPHDIV DARLPESEPI
LLEGAVAGHV LVKNVNEALP LKAKPKMLSV YGYDATIPRT KNTDTVFQLG YFSSPEMTQA
VLGTEQHFDQ AAKGGTIVVG GRAGANAPSY IIDPLAAIQQ RAKADGTWLN WDLDSTNPGV
NAASDACLVF INAISTEGWD RDGLHDDSSD GLVLNVASKC ANTIVVVHTV GVRLVDQWID
HPNVTATIIA HLPGQDSGTA LVQLLYGEAG FSGKLPYTMA KNESDYSVYH VCGKIGPNDT
DPQCDYTEGV YLDYRYFDEK NITPRYEFGY GLTYTTFDFD QLSINSTGLN AALDSHADLW
TIITTVDSTV TNTGPVAGAE VAQLYMAIPN SPPKQLRGFE KVHLQPGESA TVRFELTRRD
LSVWDVASQQ WKVQDGNYTV FVGASSRDVR MTGTIQV
//
