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Q9SPP9

- RG1_RAUSE

UniProt

Q9SPP9 - RG1_RAUSE

Protein

Raucaffricine-O-beta-D-glucosidase

Gene

RG

Organism
Rauvolfia serpentina (Serpentwood) (Devilpepper)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Glucosidase specifically involved in alkaloid biosynthesis leading to the accumulation of several alkaloids, including ajmaline, an important plant-derived pharmaceutical used in the treatment of heart disorders.1 Publication

    Catalytic activityi

    Raucaffricine + H2O = D-glucose + vomilenine.1 Publication
    UDP-glucose + vomilenine = UDP + raucaffricine.1 Publication

    Kineticsi

    1. KM=1.3 mM for raucaffricine (at pH 5 and 28 degrees Celsius, PubMed:22004291, PubMed:10975500)2 Publications
    2. KM=1.8 mM for strictosidine (at pH 5 and 28 degrees Celsius, PubMed:22004291, PubMed:10975500)2 Publications

    Vmax=0.5 nmol/sec/µg enzyme with raucaffricine as substrate (at pH 5 and 28 degrees Celsius, PubMed:22004291, PubMed:10975500)2 Publications

    Vmax=2.6 pmol/sec/µg enzyme with strictosidine as substrate (at pH 5 and 28 degrees Celsius, PubMed:22004291, PubMed:10975500)2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361Substrate1 Publication
    Binding sitei140 – 1401SubstrateBy similarity
    Active sitei186 – 1861Proton donor
    Binding sitei193 – 1931Substrate1 Publication
    Binding sitei347 – 3471SubstrateBy similarity
    Sitei390 – 3901Directs the conformation of W-392
    Binding sitei392 – 3921Substrate1 Publication
    Sitei392 – 3921Control the gate shape and acceptance of substrates
    Active sitei420 – 4201Nucleophile
    Binding sitei420 – 4201Substrate1 Publication
    Binding sitei469 – 4691Substrate1 Publication

    GO - Molecular functioni

    1. raucaffricine beta-glucosidase activity Source: UniProtKB
    2. vomilenine glucosyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. alkaloid biosynthetic process Source: UniProtKB
    2. carbohydrate metabolic process Source: InterPro
    3. metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase, Transferase

    Keywords - Biological processi

    Alkaloid metabolism

    Enzyme and pathway databases

    BRENDAi3.2.1.125. 257570.

    Protein family/group databases

    CAZyiGH1. Glycoside Hydrolase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Raucaffricine-O-beta-D-glucosidase (EC:3.2.1.125)
    Short name:
    Raucaffricine beta-glucosidase
    Short name:
    RsRG
    Alternative name(s):
    Vomilenine glucosyltransferase (EC:2.4.1.219)
    Short name:
    RsVGT
    Gene namesi
    Name:RG
    Synonyms:VGT
    OrganismiRauvolfia serpentina (Serpentwood) (Devilpepper)
    Taxonomic identifieri4060 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesApocynaceaeRauvolfioideaeVinceaeRauvolfiinaeRauvolfia

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi186 – 1861E → D or Q: Loss of activity. 1 Publication
    Mutagenesisi189 – 1891T → A: Reduced activity. 1 Publication
    Mutagenesisi193 – 1931H → A: Reduced activity. 1 Publication
    Mutagenesisi200 – 2001Y → A: Loss of activity. 1 Publication
    Mutagenesisi390 – 3901S → G: Reduced activity. 1 Publication
    Mutagenesisi392 – 3921W → A: Loss of activity. 1 Publication
    Mutagenesisi420 – 4201E → Q: Loss of activity. 1 Publication
    Mutagenesisi476 – 4761E → A or L: Loss of activity. 1 Publication
    Mutagenesisi485 – 4851F → Y: Reduced activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 540540Raucaffricine-O-beta-D-glucosidasePRO_0000418400Add
    BLAST

    Structurei

    Secondary structure

    1
    540
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 163
    Helixi19 – 213
    Beta strandi27 – 315
    Helixi34 – 374
    Helixi50 – 578
    Helixi59 – 613
    Helixi63 – 653
    Turni68 – 725
    Helixi74 – 8815
    Beta strandi91 – 966
    Helixi99 – 1024
    Helixi108 – 1103
    Helixi114 – 12916
    Beta strandi133 – 1419
    Helixi145 – 1517
    Helixi153 – 1553
    Helixi159 – 17416
    Turni175 – 1773
    Beta strandi180 – 1856
    Helixi187 – 1959
    Turni235 – 2373
    Helixi238 – 26023
    Helixi262 – 2654
    Beta strandi268 – 28215
    Helixi286 – 29914
    Helixi301 – 3044
    Helixi306 – 3094
    Helixi314 – 3207
    Helixi321 – 3233
    Helixi329 – 3357
    Beta strandi340 – 35415
    Helixi367 – 3704
    Beta strandi373 – 3764
    Beta strandi378 – 3814
    Beta strandi382 – 3854
    Helixi398 – 41114
    Beta strandi414 – 4218
    Helixi433 – 4364
    Helixi440 – 45819
    Beta strandi463 – 4697
    Helixi477 – 4793
    Beta strandi482 – 4843
    Beta strandi487 – 4904
    Turni492 – 4965
    Beta strandi498 – 5003
    Helixi502 – 51110

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3U57X-ray2.43A/B1-513[»]
    3U5UX-ray2.20A/B1-513[»]
    3U5YX-ray2.30A/B1-513[»]
    3ZJ6X-ray2.40A/B1-540[»]
    4A3YX-ray2.15A/B1-540[»]
    4ATDX-ray2.10A/B1-513[»]
    4ATLX-ray2.52A/B1-513[»]
    4EK7X-ray2.30A/B1-513[»]
    ProteinModelPortaliQ9SPP9.
    SMRiQ9SPP9. Positions 17-508.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni185 – 1862Substrate binding
    Regioni476 – 4772Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 1 family.Curated

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    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.

    Q9SPP9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATQSSAVID SNDATRISRS DFPADFIMGT GSSAYQIEGG ARDGGRGPSI    50
    WDTFTHRRPD MIRGGTNGDV AVDSYHLYKE DVNILKNLGL DAYRFSISWS 100
    RVLPGGRLSG GVNKEGINYY NNLIDGLLAN GIKPFVTLFH WDVPQALEDE 150
    YGGFLSPRIV DDFCEYAELC FWEFGDRVKH WMTLNEPWTF SVHGYATGLY 200
    APGRGRTSPE HVNHPTVQHR CSTVAPQCIC STGNPGTEPY WVTHHLLLAH 250
    AAAVELYKNK FQRGQEGQIG ISHATQWMEP WDENSASDVE AAARALDFML 300
    GWFMEPITSG DYPKSMKKFV GSRLPKFSPE QSKMLKGSYD FVGLNYYTAS 350
    YVTNASTNSS GSNNFSYNTD IHVTYETDRN GVPIGPQSGS DWLLIYPEGI 400
    RKILVYTKKT YNVPLIYVTE NGVDDVKNTN LTLSEARKDS MRLKYLQDHI 450
    FNVRQAMNDG VNVKGYFAWS LLDNFEWGEG YGVRFGIIHI DYNDNFARYP 500
    KDSAVWLMNS FHKNISKLPA VKRSIREDDE EQVSSKRLRK 540
    Length:540
    Mass (Da):60,934
    Last modified:May 1, 2000 - v1
    Checksum:i543A24654A4D5E7D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF149311 mRNA. Translation: AAF03675.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF149311 mRNA. Translation: AAF03675.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3U57 X-ray 2.43 A/B 1-513 [» ]
    3U5U X-ray 2.20 A/B 1-513 [» ]
    3U5Y X-ray 2.30 A/B 1-513 [» ]
    3ZJ6 X-ray 2.40 A/B 1-540 [» ]
    4A3Y X-ray 2.15 A/B 1-540 [» ]
    4ATD X-ray 2.10 A/B 1-513 [» ]
    4ATL X-ray 2.52 A/B 1-513 [» ]
    4EK7 X-ray 2.30 A/B 1-513 [» ]
    ProteinModelPortali Q9SPP9.
    SMRi Q9SPP9. Positions 17-508.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 3.2.1.125. 257570.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10353. PTHR10353. 1 hit.
    Pfami PF00232. Glyco_hydro_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00131. GLHYDRLASE1.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and functional bacterial expression of a plant glucosidase specifically involved in alkaloid biosynthesis."
      Warzecha H., Gerasimenko I., Kutchan T.M., Stoeckigt J.
      Phytochemistry 54:657-666(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 80-111; 319-326; 403-408; 410-425 AND 428-438, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: BENTH. ex KURZ.
      Tissue: Protoplast.
    2. "Structures of alkaloid biosynthetic glucosidases decode substrate specificity."
      Xia L., Ruppert M., Wang M., Panjikar S., Lin H., Rajendran C., Barleben L., Stoeckigt J.
      ACS Chem. Biol. 7:226-234(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-513 IN COMPLEX WITH SUBSTRATE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-186; THR-189; HIS-193; TYR-200; SER-390; TRP-392; GLU-420; GLU-476 AND PHE-485.

    Entry informationi

    Entry nameiRG1_RAUSE
    AccessioniPrimary (citable) accession number: Q9SPP9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 11, 2013
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 71 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3