ID B6GWQ6_PENRW Unreviewed; 820 AA.
AC B6GWQ6;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Probable beta-glucosidase G {ECO:0000256|ARBA:ARBA00039579};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE AltName: Full=Beta-D-glucoside glucohydrolase G {ECO:0000256|ARBA:ARBA00041276};
DE AltName: Full=Cellobiase G {ECO:0000256|ARBA:ARBA00041601};
DE AltName: Full=Gentiobiase G {ECO:0000256|ARBA:ARBA00041808};
GN ORFNames=Pc12g03630 {ECO:0000313|EMBL:CAP79990.1}, PCH_Pc12g03630
GN {ECO:0000313|EMBL:CAP79990.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP79990.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP79990.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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 -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
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DR EMBL; AM920427; CAP79990.1; -; Genomic_DNA.
DR RefSeq; XP_002557246.1; XM_002557200.1.
DR AlphaFoldDB; B6GWQ6; -.
DR STRING; 500485.B6GWQ6; -.
DR CAZy; GH3; Glycoside Hydrolase Family 3.
DR GeneID; 8311756; -.
DR KEGG; pcs:Pc12g03630; -.
DR VEuPathDB; FungiDB:PCH_Pc12g03630; -.
DR eggNOG; ENOG502QR4D; Eukaryota.
DR HOGENOM; CLU_004542_2_3_1; -.
DR OMA; WIQPANT; -.
DR OrthoDB; 5486783at2759; -.
DR BioCyc; PCHR:PC12G03630-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c12.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
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:SF19; BETA-GLUCOSIDASE G-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:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..820
FT /note="Probable beta-glucosidase G"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002845255"
FT DOMAIN 737..806
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 820 AA; 89534 MW; 654B7081CDECD802 CRC64;
MYHHWLLPKT LVVSVLLPSL AYSQANAGDA GTRSADAFQW IQPANTTILG EYGHSPPVYP
SPKITGTSEW ETALNKAEHF VSSLTLDEKA WLVTGVPGPC IGNIGPVLRL NFTGLCLQDG
PNAVRPSDYV SVFPSGITIA SSWDRDLIYD RFHDLGLEYK GKGAQVALGP VGGALGRTPY
GGRNWEGFSP DPYLTGVAME SGVRGLQDAG VQATIKHWLL YEQETQRSPT LYPNGTLEFS
TYSSNADDRT IHELYMWPFA NAIRAQASAA MCSYNRVNGS YACQNSKLLN GLLKEELGFQ
GYVMTDWSGL HSGVASAQAG TDMDQPGHIE PMTTLLNQTR LSSYFGGNIT LAVRNGTLPE
SRLDDMIKRI MTPYYALRQD QDFPATDPAM AYYNTQFSSS NYSMDSLVFG EKSRDVRQDH
GGRIRQHAAE STVMLKNTNG TLPLKAPTSI AIFGSDAAPN TQGLFIRGPS EIGTLAIGGG
SGNGRFTYLV SPLEAIKARA VQDNTLVQFW LNNTVIKDAN VESLWGATAP EACLVFLKSR
ASERLDRESL AVDQHGDTVV ESVASKCSNT IVVTHSGGMT IMPWADHPNV TAILAAHYPG
QESGHSIVDI LYGAKSLSGK LPYTVPLNAS SVNTAPTTNI TTSGVDDWQS WYSEGLEIDY
RYYHTHKIPV QYEFGFGLSY TNFSMASLRV KPTHPEARIL SQPEALATRP GGNPALWDVL
FEAEVTLQNT GSTSGATVAQ LYISFPDEVS APSLQLRGFE KTYLSPGESY TATFPLMRRD
LSYWNVTQQT WLIPEGDFIL RVGFSSLDLH DSVVLRPVEE
//
