ID A0A5Q4BQP2_9PEZI Unreviewed; 808 AA.
AC A0A5Q4BQP2;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN Name=BglK {ECO:0000313|EMBL:TQN69342.1};
GN ORFNames=CSHISOI_05904 {ECO:0000313|EMBL:TQN69342.1};
OS Colletotrichum shisoi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=2078593 {ECO:0000313|EMBL:TQN69342.1, ECO:0000313|Proteomes:UP000326340};
RN [1] {ECO:0000313|EMBL:TQN69342.1, ECO:0000313|Proteomes:UP000326340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-2018a {ECO:0000313|EMBL:TQN69342.1,
RC ECO:0000313|Proteomes:UP000326340};
RX PubMed=31527702;
RA Gan P., Tsushima A., Hiroyama R., Narusaka M., Takano Y., Narusaka Y.,
RA Kawaradani M., Damm U., Shirasu K.;
RT "Colletotrichum shisoi sp. nov., an anthracnose pathogen of Perilla
RT frutescens in Japan: molecular phylogenetic, morphological and genomic
RT evidence.";
RL Sci. Rep. 9:13349-13349(2019).
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:TQN69342.1}.
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DR EMBL; PUHP01000534; TQN69342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5Q4BQP2; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000326340; 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; 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; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF56988; Anthrax protective antigen; 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:UP000326340}.
FT DOMAIN 403..562
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 808 AA; 88528 MW; 3F482EEA30FEA624 CRC64;
MQPPPKKLVD IDQVIENATL AEKISLLAGS DFWHSTPLPQ FDVPAIKCTD GPNGVRGSRF
FNPVPALCIP CGSGLGATWN PDLIEEAGQL LSKECDAKGA HVWLGPTVNI IRSPLNGRGF
ESFSEDPHLS GILAAAIIRG VQSRGTLAAL KHLVANDQET DKMSLDVCMS DRALREVYLL
PFQIALRDSN PRVLMSSYNK IGGLHVSENP KILRDILRTE WGFNGLIMSD WYGTYSCEAA
LNAGVDIEMP GPSRYREKEA LAAVFSGQVS HHTIDERARK VLQFVNDAAS ARVAEQETTR
DVPEDRILNR RLAGEGIVLL KNSEHILPLR PEDCDEVAVI GPNADLPAAC GGGSASLRPY
YTSSVLGGIQ DSLPASSKVH YEPGVFGHVL LPAFTADHVC TDTVEARVTI EVFNEPHTVK
HRKPFDRVTI PDTTYQLMDY GHPKKEETFF MSMRATFVPK HTDIYEFGLA TYGISDLFIN
NELVIDNSTE QTPGGMFFGK GSAEKRATYD MKAGERYCLR VEAGSASTSK VKGGSLLAIP
GGACRLGGCR KINAEEGIQR AVDRAKRCRY TFVVAGLNAD LEKEGKDRET MDMPPHVDEL
IEAVLKARPN AVVITQAGNP VSMPWRRRAN TLLHSWYGGN EAGNAVADVI FGRINPSGKL
PMTFPARLED NPAFLGFGSD NGKVHYSEDV FVGYKWYEAR KTEVAFPFGH GLSYTSFQIS
DLQVKPSRVE VIVKNTGKVA GAEVVCLYIK YATRSPKSRF ARPLRSLMGF TKIFLESGEG
TYTASVTAGE TSLEGTFQIQ KDVFWNGL
//
