ID A0A5C3MP06_9AGAM Unreviewed; 787 AA.
AC A0A5C3MP06;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 10.
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=OE88DRAFT_1053198 {ECO:0000313|EMBL:TFK46096.1};
OS Heliocybe sulcata.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Heliocybe.
OX NCBI_TaxID=5364 {ECO:0000313|EMBL:TFK46096.1, ECO:0000313|Proteomes:UP000305948};
RN [1] {ECO:0000313|EMBL:TFK46096.1, ECO:0000313|Proteomes:UP000305948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OMC1185 {ECO:0000313|EMBL:TFK46096.1,
RC ECO:0000313|Proteomes:UP000305948};
RX PubMed=30886374; DOI=.1038/s41559-019-0834-1;
RA Varga T., Krizsan K., Foldi C., Dima B., Sanchez-Garcia M.,
RA Sanchez-Ramirez S., Szollosi G.J., Szarkandi J.G., Papp V., Albert L.,
RA Andreopoulos W., Angelini C., Antonin V., Barry K.W., Bougher N.L.,
RA Buchanan P., Buyck B., Bense V., Catcheside P., Chovatia M., Cooper J.,
RA Damon W., Desjardin D., Finy P., Geml J., Haridas S., Hughes K., Justo A.,
RA Karasinski D., Kautmanova I., Kiss B., Kocsube S., Kotiranta H.,
RA LaButti K.M., Lechner B.E., Liimatainen K., Lipzen A., Lukacs Z.,
RA Mihaltcheva S., Morgado L.N., Niskanen T., Noordeloos M.E., Ohm R.A.,
RA Ortiz-Santana B., Ovrebo C., Racz N., Riley R., Savchenko A., Shiryaev A.,
RA Soop K., Spirin V., Szebenyi C., Tomsovsky M., Tulloss R.E., Uehling J.,
RA Grigoriev I.V., Vagvolgyi C., Papp T., Martin F.M., Miettinen O.,
RA Hibbett D.S., Nagy L.G.;
RT "Megaphylogeny resolves global patterns of mushroom evolution.";
RL Nat. Ecol. Evol. 3:668-678(2019).
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 -!- 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; ML213533; TFK46096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C3MP06; -.
DR STRING; 5364.A0A5C3MP06; -.
DR Proteomes; UP000305948; Unassembled WGS sequence.
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: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: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 Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000305948};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..787
FT /note="Probable beta-glucosidase G"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5022665028"
FT DOMAIN 703..774
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 787 AA; 84755 MW; 4B364DCC2F6E3E28 CRC64;
MVTSSYWVVS LALLACGAAA QWQSGSYGYS PPVYPSPNTT GLGGWQSALA KADAFLSQLT
LDEKAQMVTG TLGPCTGNIP PIPRLGFNGL CLQDGPLAIR QADFASVFPA GLTAAASWDR
GLIYQRGVEV AEEFKGKGAH VMLGPVSGPM GRSAYGGRNW EGFSPDPYLN GVATERTIKG
IQSVGVQACV KHYIGNEQET QRNPSISSDG QTIEAVSSNI DDRTIHELYS WPFADAVRAG
VSSVMCSYNR LNQSYACQNS YTLNGILKTE FGFQGYVVSD WGATHSGVAA IEAGLDMDMP
GSIDFTSTTS SFFGQNITIA VENGTLAEER VDDMIRRVMT PYFYLNQDQG FPTVDPSSMY
LNGFSSESEW VYQFDLNGTS NRDVRANHAA LIRELGASAT VLLKNTNGAL PLKAPKYIGV
FGNDAGDLTN SLYFVGQYEY GTLPVGGGSG TGRFSYVVPP LDAIKARAKK DGALVQYILN
NTMASTDLST LYPPAQELDV CLVFLKTWAS ESYDRSSLEV DWDGNALVEA IAANCNNTIV
VTHSGGINVL PFATHPNVTA ILAAHYPGEE SGNSIVDVLY GDVNPSGRLP YTIALNESDY
TIPILNLTNP GPNDWQVDFT ESLLIDYRYF DYANKSVLYE FGYGLSYTTF SLAGMSIEDV
AGGRLSELPP AQAVVPGGNP ALFETVLKVT AHVRNTGGVA DAAVPQLYVG MPSSVPPRTP
PKQLRGFDKV PLVPGEVGKV VFELTRRDVS YWDVEAQQWR IPEGTFTLSL GFSSRDIRQS
ATFCALC
//
