ID W3WIP4_PESFW Unreviewed; 858 AA.
AC W3WIP4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=PFICI_15207 {ECO:0000313|EMBL:ETS73032.1};
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:ETS73032.1, 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 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; KI912124; ETS73032.1; -; Genomic_DNA.
DR RefSeq; XP_007841979.1; XM_007843788.1.
DR AlphaFoldDB; W3WIP4; -.
DR STRING; 1229662.W3WIP4; -.
DR GeneID; 19280220; -.
DR KEGG; pfy:PFICI_15207; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_4_0_1; -.
DR InParanoid; W3WIP4; -.
DR OMA; NCHYKIS; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000030651; 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:SF3; BETA-GLUCOSIDASE B-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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030651}.
FT DOMAIN 407..562
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 858 AA; 94986 MW; ECFD78D2A5CD4C93 CRC64;
MADSIGDLDR EVKDLVARLT VDEKISLLAG KNTWETMPIE RLDIPSLKVS DGPNGARGAD
FFDGMTAACF PACVSLAATF DRDLSRRIGQ ALGQEAQTKG AYVVLGPTVC THRSPLGGRN
FEAFSEDPLL SGLMAAEYVK GLQSERVGAT VKHFLANEQD TRRFTVNEII SERALREIYL
RAFEIVLKKS DPWCFMSSYP KVNGRHVDAQ PLFLQTILRE EWGYDGLLMS DWGAVSNAVE
SVKFGLGLEM PGPPSHRIPE AVKKAVLSGL ISAEELDRCA ATFVKLLKRT GKLDDRRKTP
PEKSIDLPEH RHLIREAGAD GIVLLKNHQN ILPIDPRKFK KLALLGPLAN YAAAYGGGSA
SLNCHYKISP YDAFENRLGD QVELSYSKGA HIFRVYPDLI DGSRNREGNQ GFTADFYDNL
ELGGEPVWTE HYARGFFTSM MNDSLKEKPL SARFATSYTP PVSGKHYLSF SGMGPSKLFI
NGEMLSHQQK ETKDSMTFFL GVHEEHRFQY EFCSEKSYEI VVETVPSQVN NSELSLLQGQ
ISAHLGLVYQ EEMEASLYDE AISLAKEADL AICFVGNTVQ WETEGQDLQS MCLPANGSQD
RLVAGVARAN PNTIVVITTG VPVELPWIDD VAALMQGWYA GQETGNSILD VILGDVNPSG
KLPVSWPKKY EHTACYGNFG LDSYESRQVE YVEGVNVGYR HFDHHYDTEK EVRFPFGFGL
GYTSFDILDV KVAGQLVNCP IDTIVVLVTI RNTGSRIGSQ VIQVYLSPPH ASKDNSRPRK
ALVAFEKVKL HPGEEKAVEM GFGRDAAAYW DDRSKDEGGY CWRVEKGVHE IAVGTSSRPS
DLAIVLSLEI PEEFSFGP
//
