ID A0A2G8RYC2_9APHY Unreviewed; 906 AA.
AC A0A2G8RYC2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=beta-glucosidase {ECO:0000256|ARBA:ARBA00012744};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
GN ORFNames=GSI_12274 {ECO:0000313|EMBL:PIL26516.1};
OS Ganoderma sinense ZZ0214-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL26516.1, ECO:0000313|Proteomes:UP000230002};
RN [1] {ECO:0000313|EMBL:PIL26516.1, ECO:0000313|Proteomes:UP000230002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL26516.1,
RC ECO:0000313|Proteomes:UP000230002};
RX PubMed=26046933; DOI=10.1038/srep11087;
RA Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA Li X., Schwartz D.C., Wang Y., Chen S.;
RT "Chromosome-level genome map provides insights into diverse defense
RT mechanisms in the medicinal fungus Ganoderma sinense.";
RL Sci. Rep. 5:11087-11087(2015).
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}.
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:PIL26516.1}.
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DR EMBL; AYKW01000045; PIL26516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8RYC2; -.
DR STRING; 1077348.A0A2G8RYC2; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000230002; 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:UP000230002};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..906
FT /note="beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013600721"
FT DOMAIN 826..895
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT REGION 98..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 95519 MW; 1D154BD8F0596312 CRC64;
MALILNSRLS ALCAFLLLTL SVHAAPSDSA SSGASSTLAS GSTFLGSSSA ATSAAATDST
FLGSSSSVSS LAATSPSSAT SAPATSSSVL ASSGESSKIT SGASLPSNAS VTSAAATTTP
GAPATETTHF TLPISSYPFT PFPAPSGTPI PGVYPATSPN SPPPVGSELI PDFGPAWAAA
REKAKTLVAS FSLEQKANVS TGVGWMGGRC VGNIPAVGDW PGLCLEDSPL GVRFTDFATA
FPAGVNAAAT WNRTLIRARG KAIGQEFKGK GAHVGLGPMM NMGRIAQGGR NWEGFGADPF
LTGEAAYETV LGWQEGGSQA CAKHYINNEQ EHLREHESSD VDDRTEHEIY VHPFMRAVQA
GVASVMCSYN QVNATWACEN DRTLNQVLKG ELGFQGYVMS DWGAHHSTLA AVAGLDMSMP
GDITFNSGTS WWGANLTAFV ENGTIASSRV DDMAERIIAA WYLLGQDEDY PDVSFNAFFP
NDPATNEHVD VQDDHYKVVR EIGAASTVLL KNVDGALPLH KPKSVAIIGN DAGPSSLGPN
GYSDRGGDDG TLAMGWGSGT ANFPYLITPL EAVQARARQD RSSVSWFLNN WDLSGAQSTA
INQDVALVFV NADSGEDYIT VDGNEGDRKN LTLWGNANSL IGAVAEANPN TIVVVHSVGP
AIIEPWIDNP NITAVLWAGL PGQESGNSLV DVLYGAVSPS GRLPYTIAKD PADYPAQLIT
GGDPNETILI EYTEDLNIDY RYFDVNDIEP RFEFGFGLSY TSFAYSSLRV SPVTQGDSTS
VALEQAWARG EASPNVEGGS TALWLHRPAF EVTFKVRNTG KVQGGEIPQL YLHFPSSAGE
PPSVLRGFSD VLLQPGQSKT VTLTLSRYDL SIWDSEAQGW RKPEGQFTFS VGASSRDFRL
KGSIPL
//