ID A0A0A2JNV7_PENEN Unreviewed; 857 AA.
AC A0A0A2JNV7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=beta-glucosidase {ECO:0000256|RuleBase:RU361161};
DE EC=3.2.1.21 {ECO:0000256|RuleBase:RU361161};
GN ORFNames=PEX2_004230 {ECO:0000313|EMBL:KGO57069.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO57069.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO57069.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO57069.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC involved in the degradation of cellulosic biomass. Catalyzes the last
CC step releasing glucose from the inhibitory cellobiose.
CC {ECO:0000256|ARBA:ARBA00024983}.
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:KGO57069.1}.
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DR EMBL; JQFZ01000155; KGO57069.1; -; Genomic_DNA.
DR RefSeq; XP_016598757.1; XM_016737701.1.
DR AlphaFoldDB; A0A0A2JNV7; -.
DR STRING; 27334.A0A0A2JNV7; -.
DR GeneID; 27673120; -.
DR HOGENOM; CLU_004542_2_0_1; -.
DR OrthoDB; 5486783at2759; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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 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.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 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:UP000030143};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..857
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001989783"
FT DOMAIN 767..841
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 857 AA; 92267 MW; FC8DC48F9BA0CE2C CRC64;
MAPWAHLALV SLLTPLLLAS PVPDESDSTT ALHARAAEGY ESPPYYPTPP GGWIPDWSEA
YSKAHHLVSN MTLAEKVNLT TGTGFFMGPC VGQTGSVPRL GIPNLCLQDS PLGIRNSDHN
TAFPPGITGV GLGEEARGKG VNVLLGPSVG ALGRKPRGGR NWEGFGADPT LQAFGGAQTV
KGMQSTGAIA AIKHFIGNEQ EMHRMSSVVT KGYSSNIDDR TLHELYLWPF AEGVRAGVGS
LMTAYSDVNS SSCSQNSKLI NGILKDELGF QGFVMTDWLG HYSGVASAIA GLDMAMPGDG
AVPLFGDSYW GSELSRSVLN GSVPVDRLND MVQRIVATWY KYKQDENYPL PNFSTNTQDK
EGLIYPGALI SPSGIVNQFV DVKGDHNITA RAVAREAITL LKNDMDILPL HSNDSLKIFG
TDAGGNPDGL NSCVDQGCNK GVLTMGWGSG TARLPYLITP QEAISNITKN AEFHITDKFP
SDVTANDNDI ALVFISADSG ENYITVEGNP GDRTIAGLNA WHNGDDLVKA AAEKFSNVVV
IIHTVGPILM EEWIELKSVK AVVVAHLPGQ EAGNSLTDIL FGDYSPSGHM PYTIPRSEDN
YPDSVDLISQ PFGQIQDTYT EGLYIDYRHF IKANITPRYA FGHGLSYTTF NFSQPSLSTG
TLLDSAYPAA RPTKPLTPSY NTSIPDASEV AWSSTSFTRI WRYIYPYLLN PQLITATKKY
SYPDGYSTEP HAVPRAGGGE GGNPALFETV FSVQLEVQNT GKRTGKAVAQ LYVELPSSLG
LDTPALQLRQ FEKTKELAPG QSQTVTLHLT RKDVSVWDVV VQDWKAPVNG QGIKIWVGNS
VADLPVLCVV GGKCSIQ
//
