ID A0A165T6J8_9APHY Unreviewed; 465 AA.
AC A0A165T6J8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
GN ORFNames=DAEQUDRAFT_722091 {ECO:0000313|EMBL:KZT72999.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT72999.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT72999.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT72999.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58; Evidence={ECO:0000256|ARBA:ARBA00036824};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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DR EMBL; KV429038; KZT72999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165T6J8; -.
DR STRING; 1314783.A0A165T6J8; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF1; GLUCAN 1,3-BETA-GLUCOSIDASE I_II-RELATED; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:KZT72999.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..465
FT /note="glucan 1,3-beta-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007866886"
FT DOMAIN 123..359
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 36..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 51203 MW; 328B90B30072F4D0 CRC64;
MTSTFTCILL FLASATAVWA QQCRLIAHND LASAPTQTSG SGGGSPASIS ATATGAQPSA
SASTNASSFN YGTDVIRGVN LGGWFVLEPW ITPSIFENTN NTDIVDEYTF GQLLDADYAS
SVLEQHWNTW ITEDDLKAIN AAGLNHVRIP IGYWSVPITS ADTNYSTDVS PYVTGAWPYI
LRALNWANEN SVHVILDLHG APASQNGFDN SGQRGSADWA NNSTNIERTL DIIRFIAGKV
GGMVNVIELL NEPAGWVSDI GSAIGPYWKD GYSVVRNVTG MENQVMIGDA FLGVDDWQNF
LLPPEGEDVI MDYHQYQVFN YDQLELSQDQ HINYTCQINA TLAPYAKSNL RTITGEWSNA
ITDCAKWLNG RNVGARWDGT YTSGQQTFGS CDGMTGNFST FSTDYKTFLR KYWEAQVAIG
ESVQGWIFWT WKAENADEWS YQRGLEGGWI PQDPTDRMYP DICSS
//
