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Protein

Furostanol glycoside 26-O-beta-glucosidase

Gene

F26G

Organism
Cheilocostus speciosus (Crepe ginger) (Costus speciosus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Beta-glucosidase involved in saponin metabolism. Highly specific for the cleavage of C-26-bound glucose moiety of furostanol glycosides such as protogracillin and protodioscin. No activity with nuatigenin glycoside. Convers furostanol glycosides to spirostanol glycosides.2 Publications

Catalytic activityi

Protodioscin + H2O = 26-deglucoprotodiscin + D-glucose.2 Publications

Enzyme regulationi

Partially inhibited by glucono-1,5-lactone, conduritol beta-epoxide and diosgenin, but not by beta-sitosterol or cholesterol.1 Publication

Kineticsi

  1. KM=50 µM for protogracillin1 Publication

    pH dependencei

    Optimum pH is 5.0-5.5.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei110 – 1101SubstrateBy similarity
    Binding sitei214 – 2141SubstrateBy similarity
    Binding sitei259 – 2591SubstrateBy similarity
    Active sitei260 – 2601Proton donorBy similarity
    Binding sitei401 – 4011SubstrateBy similarity
    Active sitei472 – 4721NucleophileBy similarity
    Binding sitei518 – 5181SubstrateBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BRENDAi3.2.1.186. 13331.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Furostanol glycoside 26-O-beta-glucosidase1 Publication (EC:3.2.1.1862 Publications)
    Short name:
    CsF26G1 Publication
    Alternative name(s):
    Protodioscin 26-O-beta-D-glucosidase
    Gene namesi
    Name:F26G1 Publication
    OrganismiCheilocostus speciosus (Crepe ginger) (Costus speciosus)Imported
    Taxonomic identifieri49577 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaZingiberalesCostaceaeCheilocostus

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4444ChloroplastSequence analysisAdd
    BLAST
    Chaini45 – 562518Furostanol glycoside 26-O-beta-glucosidaseSequence analysisPRO_0000430785Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi279 ↔ 285By similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Heterodimer. The N-terminus of the larger subunit is blocked and the smaller subunit might be derived from the larger one.1 Publication

    Protein-protein interaction databases

    IntActiQ42707. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ42707.
    SMRiQ42707. Positions 89-561.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni525 – 5262Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.UniRule annotation

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR033132. Glyco_hydro_1_N_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q42707-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAAQLGLPLV SCHRGASQAA SSSAHLVPGA SAIMQAGNRR QKMRAPALRD
    60 70 80 90 100
    RVVFARVVPV DGSVGFAGSS TEQETAVESA TPTAVPSKVV LGRSSFPRGF
    110 120 130 140 150
    IFGAASAAYQ VEGAWNEGGR GPSIWDTFTH DHPEKIADHS NGDKATDSYK
    160 170 180 190 200
    KYKEDVKLLK DLGLDSYRFS ISWSRILPKG TLQGGINQEG IQYYNDLINE
    210 220 230 240 250
    LLKNGIRPMV TLFHWDVPQA LEDSYKGFRS SEIVNDFKDY ADICFKEFGD
    260 270 280 290 300
    RVKHWITLNE PWSLSTMGYA FGRHAPGRCS TWYGCPAGDS ANEPYEVTHN
    310 320 330 340 350
    LLLAHANAVK IYRDNYKATQ NGEIGITLNS LWYEPYSKSH EDVEAATRAL
    360 370 380 390 400
    DFMFGWYMDP LVNGDYPFIM RALVRDRLPF FTHAESELIK GSYDFIGINY
    410 420 430 440 450
    YTSNYAQHAP VTEDHTPDNS YFDSYVNQSG EKNGVPIGPL QGSWIYFYPR
    460 470 480 490 500
    GLKELLLYVK RRYCNPKIYI TENGTAEVEK EKGVPLHDPE RKEYLTYHLA
    510 520 530 540 550
    QVLQAIREGV RVKGHFTWAL TDNFEWDKGY TERFGLIYID YDKDFNRQPK
    560
    DSTKWFSKFL RT
    Length:562
    Mass (Da):63,649
    Last modified:November 1, 1996 - v1
    Checksum:i76D512881326C9F2
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D83177 mRNA. Translation: BAA11831.1.
    PIRiS78099.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D83177 mRNA. Translation: BAA11831.1.
    PIRiS78099.

    3D structure databases

    ProteinModelPortaliQ42707.
    SMRiQ42707. Positions 89-561.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ42707. 1 interaction.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.2.1.186. 13331.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR033132. Glyco_hydro_1_N_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10353. PTHR10353. 1 hit.
    PfamiPF00232. Glyco_hydro_1. 1 hit.
    [Graphical view]
    PRINTSiPR00131. GLHYDRLASE1.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Molecular cloning and bacterial expression of a cDNA encoding furostanol glycoside 26-O-beta-glucosidase of Costus speciosus."
      Inoue K., Shibuya M., Yamamoto K., Ebizuka Y.
      FEBS Lett. 389:273-277(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, FUNCTION.
      Tissue: LeafImported.
    2. "Purification and characterization of furostanol glycoside 26-O-beta-glucosidase from Costus speciosus rhizomes."
      Inoue K., Ebizuka Y.
      FEBS Lett. 378:157-160(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.

    Entry informationi

    Entry nameiF26G_CHESP
    AccessioniPrimary (citable) accession number: Q42707
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: November 1, 1996
    Last modified: March 16, 2016
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Enzymatic conversion of furostanol glycosides to spirostanol glycosides proceeds only after plants are harvested. Under normal physiological conditions, the enzyme and its substrate might be compartmented spatially and/or chemically.1 Publication

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.