ID B8P3C1_POSPM Unreviewed; 776 AA.
AC B8P3C1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=POSPLDRAFT_107557 {ECO:0000313|EMBL:EED84644.1};
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:EED84644.1, 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 -!- 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; EQ966247; EED84644.1; -; Genomic_DNA.
DR RefSeq; XP_002470190.1; XM_002470145.1.
DR AlphaFoldDB; B8P3C1; -.
DR STRING; 561896.B8P3C1; -.
DR KEGG; ppl:POSPLDRAFT_107557; -.
DR HOGENOM; CLU_004542_2_3_1; -.
DR InParanoid; B8P3C1; -.
DR OMA; VNDTYAC; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000001743; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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:SF10; BETA-GLUCOSIDASE F-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:ARBA00023001};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000001743}.
FT DOMAIN 696..765
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 776 AA; 84685 MW; 1997B1B1C9DDC5B8 CRC64;
MYKLAPSALL WRDSGTPVLG QHQGCTLPRF VMLLAGNAWA EAYAKAEAFV AGLTLEQKVN
VSTGVYWEQG LCVGNIGEVA DLRGLCLQDS PLGVRYTDYN TAFPAGISTA ATFNRTMMRL
RGQQMGEEFR GKGVNVALGP MMNMGRVAQA GRNWEGFGTD PFLSGEAAYE TTLGLQSAGV
QACAKHYIDY EQEYKRTQES SEVDDRTQHE IYLKPFLRAV MAGTASVMCS YNMINDTYSC
ENDRTLNQLL KGELGFRGYV MSDWGAQEST LSAMAGLDMS MPGDITLGSG NSWWGPNLTA
FVENGTIPLS RMDDMATRIM ASYYLLGQDQ DYPNDGRLIP NAVSFNAFNQ YDQVHNLHID
VQADHYQIVR EIGHAGAVLL KNTNGALPLN APRNVVLIGS DAGNGAMGAN GYTDRGGDDG
ILGMGWGSGT DNYPYLISPM DAMQVRARQD GTTLMNWYYD WDTEGAATAA IQFEAAIVFV
NSDSGEGYIE VDGNLGDRNN LTLWHNADNL ITAVASQNNN TIVVAHSVGP SIIDSWVENP
NVTAIIWAGV AGQEAGNAIV DVLYGDYNPS GRLPYTIAKR LEDYGVFLTL GGNGSTILSV
PYTEGLFYDY RHFDEYNITP RYEFGYGLSY TTFEYYNLAT SIVPQYDPTD YALEAAWAAG
VPTPQGEGSS VALWLHRPFV QVSFEVQNTG AVAGTEIPQV YVHFPTGIGE PPSWLKGFDA
VYIEPGEVTT VTVTISRYDL SIWDVVAQGW VKPAGEITFS VGASSRDFRL QGYIPI
//
