F26G_SOLTO
ID F26G_SOLTO Reviewed; 61 AA.
AC P0DKH4;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Furostanol glycoside 26-O-beta-glucosidase {ECO:0000303|PubMed:16289258};
DE EC=3.2.1.186 {ECO:0000269|PubMed:16289258};
DE AltName: Full=Torvosidase {ECO:0000303|PubMed:16289258};
DE Flags: Fragments;
OS Solanum torvum (Turkey berry) (Solanum ficifolium).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=119830;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, SUBUNIT, GLYCOSYLATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Leaf;
RX PubMed=16289258; DOI=10.1016/j.phytochem.2005.09.035;
RA Arthan D., Kittakoop P., Esen A., Svasti J.;
RT "Furostanol glycoside 26-O-beta-glucosidase from the leaves of Solanum
RT torvum.";
RL Phytochemistry 67:27-33(2006).
CC -!- FUNCTION: Beta-glucosidase highly specific for the cleavage of C-26-
CC bound glucose moiety of furostanol glycosides torvosides A and H.
CC Hydrolyzes only p-nitrophenyl-beta-glucoside, but not p-nitrophenyl-
CC beta-D-fucoside, p-nitrophenyl-beta-L-fucoside, p-nitrophenyl-beta-D-
CC xyloside, p-nitrophenyl-beta-D-galactoside, p-nitrophenyl-beta-D-NAc-
CC glucosamine, p-nitrophenyl-beta-D-mannoside or any of the p-
CC nitrophenyl-alpha-glycosides tested. {ECO:0000269|PubMed:16289258}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + protodioscin = 26-deglucoprotodioscin + D-glucose;
CC Xref=Rhea:RHEA:37895, ChEBI:CHEBI:4167, ChEBI:CHEBI:8588,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:74026; EC=3.2.1.186;
CC Evidence={ECO:0000269|PubMed:16289258};
CC -!- ACTIVITY REGULATION: Inhibited by Hg(2+) and D-glucono-1,5-lactone.
CC {ECO:0000269|PubMed:16289258}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.063 mM for torvoside A {ECO:0000269|PubMed:16289258};
CC KM=0.068 mM for torvoside H {ECO:0000269|PubMed:16289258};
CC KM=1.03 mM for p-nitrophenyl-beta-glucoside
CC {ECO:0000269|PubMed:16289258};
CC KM=0.78 mM for 4-methylumbelliferyl-beta-glucoside
CC {ECO:0000269|PubMed:16289258};
CC Note=kcat is 8.6 sec(-1) for torvoside A. kcat is 7.7 sec(-1) for
CC torvoside B. kcat is 9.1 sec(-1) for p-nitrophenyl-beta-glucoside.
CC kcat is 8.3 sec(-1) for 4-methylumbelliferyl-beta-glucoside.
CC {ECO:0000269|PubMed:16289258};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:16289258};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16289258}.
CC -!- TISSUE SPECIFICITY: Expressed in petioles and leaves, but not in
CC fruits. {ECO:0000269|PubMed:16289258, ECO:0000303|PubMed:16289258}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:16289258}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR AlphaFoldDB; P0DKH4; -.
DR SMR; P0DKH4; -.
DR BRENDA; 3.2.1.186; 13332.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase.
FT CHAIN <1..>61
FT /note="Furostanol glycoside 26-O-beta-glucosidase"
FT /id="PRO_0000430786"
FT ACT_SITE 33
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9XEI3"
FT BINDING 33
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:Q9XEI3"
FT UNSURE 3
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:16289258"
FT UNSURE 13
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:16289258"
FT UNSURE 18
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:16289258"
FT UNSURE 24
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:16289258"
FT UNSURE 31
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:16289258"
FT UNSURE 37
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:16289258"
FT UNSURE 42
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:16289258"
FT UNSURE 43
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:16289258"
FT UNSURE 48
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:16289258"
FT UNSURE 57
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:16289258"
FT UNSURE 59
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:16289258"
FT UNSURE 60
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:16289258"
FT NON_CONS 6..7
FT /evidence="ECO:0000269|PubMed:16289258"
FT NON_CONS 16..17
FT /evidence="ECO:0000269|PubMed:16289258"
FT NON_CONS 27..28
FT /evidence="ECO:0000269|PubMed:16289258"
FT NON_CONS 39..40
FT /evidence="ECO:0000269|PubMed:16289258"
FT NON_CONS 47..48
FT /evidence="ECO:0000269|PubMed:16289258"
FT NON_CONS 54..55
FT /evidence="ECO:0000269|PubMed:16289258"
FT NON_TER 1
FT /evidence="ECO:0000269|PubMed:16289258"
FT NON_TER 61
FT /evidence="ECO:0000269|PubMed:16289258"
SQ SEQUENCE 61 AA; 6766 MW; A5B01CDEBA159A98 CRC64;
MTLEEKIGQM SQIDARRIGA ATALEVRGFL ISDSQGIDRH NLIPMSRIDD AVSRKSLVLL
K
