UniProt: S8B460

Database: UniProt
Entry: S8B460_PENO1

LinkDB:  S8B460_PENO1 
Original site:  S8B460_PENO1

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (18)   
   InterPro (10)   
   Pfam (4)   
   PROSITE (2)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (24)   

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ID   S8B460_PENO1            Unreviewed;       840 AA.
AC   S8B460;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE            EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN   ORFNames=PDE_04251 {ECO:0000313|EMBL:EPS29302.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS29302.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS29302.1, ECO:0000313|Proteomes:UP000019376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(2013).
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; KB644411; EPS29302.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8B460; -.
DR   SMR; S8B460; -.
DR   STRING; 933388.S8B460; -.
DR   eggNOG; ENOG502QR4D; Eukaryota.
DR   HOGENOM; CLU_004542_4_0_1; -.
DR   OrthoDB; 5486783at2759; -.
DR   PhylomeDB; S8B460; -.
DR   UniPathway; UPA00696; -.
DR   Proteomes; UP000019376; 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: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; 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   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
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:UP000019376}.
FT   DOMAIN          395..556
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   840 AA;  91810 MW;  2B247A1E0FAD5FF8 CRC64;
     MAPIDVEKTI EELTLGEKIA LTSGRDFWHT QPVPRLNIPS LRTSDGPNGV RGTRFFNGVP
     AACFPCATAL GATWDADLLA EIGTLMGEEA IAKGTHVILG PTINTQRSPL GGRGFESFSE
     DGVLSGTLAG YMVKGMQEKG VAATLKHFVC NDQEHERLAV NAILTDRALR EIYLMPFQLA
     MRICRSACVM TAYNKINGTH VSENKAIIDD ILRKEWKWEG LIMSDWFGTY SVSEAIEAGL
     DLEMPGKTRW RGEALSHAVT SNKVAEFKLD ERVRNVLNLV NWVDPLGIPE GAEEKALNRP
     EDQALMRRAA AESVVLLKNE DNILPLKKDG SILVIGPNAK IASYCGGGSA SLAPYYTVSP
     FEGVAAKSSG EVKYSQGVYS HKDLPLLGPL MKTEDGKTGF MFKVYNEPPT AGQQRTAVDE
     IHLVSSSGFL ADYVNPKLES LTFYVDMEGY FTPEEDGLYD FGVTVVGTGR LLVDGEVVVD
     NTKNQKQGSA FFGTATIEEQ GTKELKAGQK YKVVFEFGSA PTSDLDTHGI VAFGGGGFRF
     GASRRVGQDE LISSAVEQAK EASQVVIFAG LTSEWETEGY DRDHMDLPPG SDELISRVLE
     VNPNAVVVIQ SGTPITMPWA KDARALVHAW FGGNECGNGI ADVLYGDVNP SGKLPLTFPR
     RLQDNPSYLN FRSERGRTLY GEDIYVGYRY FEKSDVAPAF AFGHGLSYTT FTRSDLKIST
     VPEQAKYAES GEPITATVTV TNTGSVAGAE IVQLWVVPPK TEVSRPVREL KAFKKVFLQP
     GEAKTVELAV EKKLATSWWD EQRGQWISEK GTYQVSITGT GPEELKGEFE VSKTRFWLGL
//

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