ID B8PGA7_POSPM Unreviewed; 847 AA.
AC B8PGA7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=POSPLDRAFT_128500 {ECO:0000313|EMBL:EED80096.1};
OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS (Poria monticola).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN [1] {ECO:0000313|EMBL:EED80096.1, ECO:0000313|Proteomes:UP000001743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA Brettin T., Rokhsar D., Berka R., Cullen D.;
RT "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT placenta supports unique mechanisms of lignocellulose conversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; EQ966355; EED80096.1; -; Genomic_DNA.
DR RefSeq; XP_002474718.1; XM_002474673.1.
DR AlphaFoldDB; B8PGA7; -.
DR STRING; 561896.B8PGA7; -.
DR KEGG; ppl:POSPLDRAFT_128500; -.
DR HOGENOM; CLU_004542_4_0_1; -.
DR InParanoid; B8PGA7; -.
DR OMA; YWEDRIS; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000001743; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 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; SSF56988; Anthrax protective antigen; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000001743}.
FT DOMAIN 399..563
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 847 AA; 92991 MW; 3EE82B8FB6DC9DAF CRC64;
MAPSDFAKAD LAEVVEQLTT DEAILLTAGV GFWHTHAVPR LGIPALKTSD GPNGIRGNHF
FMGTPAKCLP SATALGATFD PELIREVGRK LLAEEAKLKA ASVWLGPTCN TQRNPLGGRS
FESFSEDPHL AGMIAAAYIG GVQEGGIAAC IKHFVGNDKE NDRMAYDSIM SERALREIYL
MPFMLAQKYA QPWCYMTAYN RVNGTHVSEN PKIIGDILRK EWGSDALVMS DWFGVYSIDH
AINAGLDLEM PGTNKWRTLD LMNRSIQSRK IMKRTVKERA AKVLELVQKC ATSAPEILDG
DGLEHTRDTP DEKALMRQLA AASIEQKIKK VAIVGGNAKA IVLSGGGSAA LKPSYFTNPY
EGIVQALGEV DKDVEITYSE GARAYMLTPS LDYDIFTETG QRGWMGSWYS HESDESMTPV
AEPLKTQYID ETRMFFSTSY PAELTKRWTL RLKGQLKPRA YDSQFEFGLI SAGRAKLYVD
GKLVVDNWTR QTRGDAFFGS GSTEEKGVFP LKAGVAHAIY VEYCNVRAPA PNDLDEAVMD
SNPGVRLGGA EVQDPDELME TAVRLASEAD AVIAVVGLNA DWETEGYDRT TLALPQRTDE
LVSRVAKANR RTIVVTQAGS SITMPWADEV PAIVHAWYLG NATGEAIGDV VTGKVNPSGR
LSLTFAKRLE DFASHGHFHS ENGKVRYGED LFVGYKHFHH RKISPQFHFG YGLSYTTFKY
SDLTLSAPSV SKDEFSLTAK VTVSNTGPVS GSEIVQLYVT LPSTSELTHP PLMLKAFAKV
KDLLPGTSQV VTLSLDKYAV SYWEERISRW VVESGEYLVR VGKSSAPEDL TLGTTFTIAK
GFEWNGL
//
