F26G_HELSP
ID F26G_HELSP Reviewed; 562 AA.
AC Q42707;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Furostanol glycoside 26-O-beta-glucosidase {ECO:0000303|PubMed:8766714};
DE Short=CsF26G {ECO:0000303|PubMed:8766714};
DE EC=3.2.1.186 {ECO:0000269|PubMed:8549824, ECO:0000269|PubMed:8766714};
DE AltName: Full=Protodioscin 26-O-beta-D-glucosidase;
DE Flags: Precursor;
GN Name=F26G {ECO:0000303|PubMed:8549824};
OS Hellenia speciosa (Crepe ginger) (Cheilocostus speciosus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Costaceae;
OC Hellenia.
OX NCBI_TaxID=49577 {ECO:0000312|EMBL:BAA11831.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY,
RP AND FUNCTION.
RC TISSUE=Leaf {ECO:0000312|EMBL:BAA11831.1};
RX PubMed=8766714; DOI=10.1016/0014-5793(96)00601-1;
RA Inoue K., Shibuya M., Yamamoto K., Ebizuka Y.;
RT "Molecular cloning and bacterial expression of a cDNA encoding furostanol
RT glycoside 26-O-beta-glucosidase of Costus speciosus.";
RL FEBS Lett. 389:273-277(1996).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=8549824; DOI=10.1016/0014-5793(95)01447-0;
RA Inoue K., Ebizuka Y.;
RT "Purification and characterization of furostanol glycoside 26-O-beta-
RT glucosidase from Costus speciosus rhizomes.";
RL FEBS Lett. 378:157-160(1996).
CC -!- FUNCTION: Beta-glucosidase involved in saponin metabolism. Highly
CC specific for the cleavage of C-26-bound glucose moiety of furostanol
CC glycosides such as protogracillin and protodioscin. No activity with
CC nuatigenin glycoside. Convers furostanol glycosides to spirostanol
CC glycosides. {ECO:0000269|PubMed:8549824, ECO:0000269|PubMed:8766714}.
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:8549824, ECO:0000269|PubMed:8766714};
CC -!- ACTIVITY REGULATION: Partially inhibited by glucono-1,5-lactone,
CC conduritol beta-epoxide and diosgenin, but not by beta-sitosterol or
CC cholesterol. {ECO:0000269|PubMed:8549824}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for protogracillin {ECO:0000269|PubMed:8549824};
CC pH dependence:
CC Optimum pH is 5.0-5.5. {ECO:0000269|PubMed:8549824};
CC -!- SUBUNIT: Heterodimer. The N-terminus of the larger subunit is blocked
CC and the smaller subunit might be derived from the larger one.
CC {ECO:0000269|PubMed:8549824}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- MISCELLANEOUS: Enzymatic conversion of furostanol glycosides to
CC spirostanol glycosides proceeds only after plants are harvested. Under
CC normal physiological conditions, the enzyme and its substrate might be
CC compartmented spatially and/or chemically.
CC {ECO:0000303|PubMed:8549824}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000255|RuleBase:RU003690}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D83177; BAA11831.1; -; mRNA.
DR PIR; S78099; S78099.
DR AlphaFoldDB; Q42707; -.
DR SMR; Q42707; -.
DR IntAct; Q42707; 1.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR KEGG; ag:BAA11831; -.
DR BRENDA; 3.2.1.186; 13331.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Disulfide bond; Glycosidase;
KW Hydrolase; Plastid; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..562
FT /note="Furostanol glycoside 26-O-beta-glucosidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430785"
FT ACT_SITE 260
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q25BW5"
FT ACT_SITE 472
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q25BW5"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q25BW5"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q25BW5"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q25BW5"
FT BINDING 401
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q25BW5"
FT BINDING 518
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q25BW5"
FT BINDING 525..526
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q25BW5"
FT DISULFID 279..285
FT /evidence="ECO:0000250|UniProtKB:P26205"
SQ SEQUENCE 562 AA; 63649 MW; 76D512881326C9F2 CRC64;
MAAQLGLPLV SCHRGASQAA SSSAHLVPGA SAIMQAGNRR QKMRAPALRD RVVFARVVPV
DGSVGFAGSS TEQETAVESA TPTAVPSKVV LGRSSFPRGF IFGAASAAYQ VEGAWNEGGR
GPSIWDTFTH DHPEKIADHS NGDKATDSYK KYKEDVKLLK DLGLDSYRFS ISWSRILPKG
TLQGGINQEG IQYYNDLINE LLKNGIRPMV TLFHWDVPQA LEDSYKGFRS SEIVNDFKDY
ADICFKEFGD RVKHWITLNE PWSLSTMGYA FGRHAPGRCS TWYGCPAGDS ANEPYEVTHN
LLLAHANAVK IYRDNYKATQ NGEIGITLNS LWYEPYSKSH EDVEAATRAL DFMFGWYMDP
LVNGDYPFIM RALVRDRLPF FTHAESELIK GSYDFIGINY YTSNYAQHAP VTEDHTPDNS
YFDSYVNQSG EKNGVPIGPL QGSWIYFYPR GLKELLLYVK RRYCNPKIYI TENGTAEVEK
EKGVPLHDPE RKEYLTYHLA QVLQAIREGV RVKGHFTWAL TDNFEWDKGY TERFGLIYID
YDKDFNRQPK DSTKWFSKFL RT
