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Q9SPP9 (RG1_RAUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Raucaffricine-O-beta-D-glucosidase

Short name=Raucaffricine beta-glucosidase
Short name=RsRG
EC=3.2.1.125
Alternative name(s):
Vomilenine glucosyltransferase
Short name=RsVGT
EC=2.4.1.219
Gene names
Name:RG
Synonyms:VGT
OrganismRauvolfia serpentina (Serpentwood) (Devilpepper)
Taxonomic identifier4060 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesApocynaceaeRauvolfioideaeVinceaeRauvolfiinaeRauvolfia

Protein attributes

Sequence length540 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

Raucaffricine + H2O = D-glucose + vomilenine. Ref.1

UDP-glucose + vomilenine = UDP + raucaffricine. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Biophysicochemical properties

Kinetic parameters:

KM=1.3 mM for raucaffricine (at pH 5 and 28 degrees Celsius, Ref.2 and Ref.1) Ref.1 Ref.2

KM=1.8 mM for strictosidine (at pH 5 and 28 degrees Celsius, Ref.2 and Ref.1)

Vmax=0.5 nmol/sec/µg enzyme with raucaffricine as substrate (at pH 5 and 28 degrees Celsius, Ref.2 and Ref.1)

Vmax=2.6 pmol/sec/µg enzyme with strictosidine as substrate (at pH 5 and 28 degrees Celsius, Ref.2 and Ref.1)

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 540540Raucaffricine-O-beta-D-glucosidase
PRO_0000418400

Regions

Region185 – 1862Substrate binding
Region476 – 4772Substrate binding

Sites

Active site1861Proton donor
Active site4201Nucleophile
Binding site361Substrate
Binding site1401Substrate By similarity
Binding site1931Substrate
Binding site3471Substrate By similarity
Binding site3921Substrate
Binding site4201Substrate
Binding site4691Substrate
Site3901Directs the conformation of W-392
Site3921Control the gate shape and acceptance of substrates

Experimental info

Mutagenesis1861E → D or Q: Loss of activity. Ref.2
Mutagenesis1891T → A: Reduced activity. Ref.2
Mutagenesis1931H → A: Reduced activity. Ref.2
Mutagenesis2001Y → A: Loss of activity. Ref.2
Mutagenesis3901S → G: Reduced activity. Ref.2
Mutagenesis3921W → A: Loss of activity. Ref.2
Mutagenesis4201E → Q: Loss of activity. Ref.2
Mutagenesis4761E → A or L: Loss of activity. Ref.2
Mutagenesis4851F → Y: Reduced activity. Ref.2

Secondary structure

......................................................................................... 540
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9SPP9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 543A24654A4D5E7D

FASTA54060,934
        10         20         30         40         50         60 
MATQSSAVID SNDATRISRS DFPADFIMGT GSSAYQIEGG ARDGGRGPSI WDTFTHRRPD 

        70         80         90        100        110        120 
MIRGGTNGDV AVDSYHLYKE DVNILKNLGL DAYRFSISWS RVLPGGRLSG GVNKEGINYY 

       130        140        150        160        170        180 
NNLIDGLLAN GIKPFVTLFH WDVPQALEDE YGGFLSPRIV DDFCEYAELC FWEFGDRVKH 

       190        200        210        220        230        240 
WMTLNEPWTF SVHGYATGLY APGRGRTSPE HVNHPTVQHR CSTVAPQCIC STGNPGTEPY 

       250        260        270        280        290        300 
WVTHHLLLAH AAAVELYKNK FQRGQEGQIG ISHATQWMEP WDENSASDVE AAARALDFML 

       310        320        330        340        350        360 
GWFMEPITSG DYPKSMKKFV GSRLPKFSPE QSKMLKGSYD FVGLNYYTAS YVTNASTNSS 

       370        380        390        400        410        420 
GSNNFSYNTD IHVTYETDRN GVPIGPQSGS DWLLIYPEGI RKILVYTKKT YNVPLIYVTE 

       430        440        450        460        470        480 
NGVDDVKNTN LTLSEARKDS MRLKYLQDHI FNVRQAMNDG VNVKGYFAWS LLDNFEWGEG 

       490        500        510        520        530        540 
YGVRFGIIHI DYNDNFARYP KDSAVWLMNS FHKNISKLPA VKRSIREDDE EQVSSKRLRK 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF149311 mRNA. Translation: AAF03675.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9SPP9.
SMRQ9SPP9. Positions 17-508.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.125. 257570.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRG1_RAUSE
AccessionPrimary (citable) accession number: Q9SPP9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 11, 2013
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries