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P68175 (STSY_RAUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Strictosidine synthase
EC=4.3.3.2
Gene names
Name:STR1
OrganismRauvolfia serpentina (Serpentwood) (Devilpepper)
Taxonomic identifier4060 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Gentianales › Apocynaceae › Rauvolfioideae › Vinceae › Rauvolfia

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the stereospecific condensation of tryptamine with secologanin to form strictosidine, the key intermediate of indole alkaloid biosynthesis.

Catalytic activity

3-alpha-(S)-strictosidine + H2O = tryptamine + secologanin.

Pathway

Alkaloid biosynthesis; 3alpha(S)-strictosidine biosynthesis; 3alpha(S)-strictosidine from secologanin and tryptamine: step 1/1.

Subunit structure

Monomer.

Subcellular location

Vacuole.

Tissue specificity

Expressed predominantly, but not exclusively, in the root. Ref.2

Sequence similarities

Belongs to the strictosidine synthase family.

Ontologies

Keywords
   Biological processAlkaloid metabolism
   Cellular componentVacuole
   DomainSignal
   Molecular functionLyase
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processalkaloid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentvacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionstrictosidine synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 344322Strictosidine synthase
PRO_0000033334

Amino acid modifications

Glycosylation911N-linked (GlcNAc...) Potential

Secondary structure

1 .................................................................... 344
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P68175 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 7CD38882621F768A

FASTA34438,162
        10         20         30         40         50         60 
MAKLSDSQTM ALFTVFLLFL SSSLALSSPI LKEILIEAPS YAPNSFTFDS TNKGFYTSVQ 

        70         80         90        100        110        120 
DGRVIKYEGP NSGFVDFAYA SPYWNKAFCE NSTDAEKRPL CGRTYDISYN LQNNQLYIVD 

       130        140        150        160        170        180 
CYYHLSVVGS EGGHATQLAT SVDGVPFKWL YAVTVDQRTG IVYFTDVSTL YDDRGVQQIM 

       190        200        210        220        230        240 
DTSDKTGRLI KYDPSTKETT LLLKELHVPG GAEVSADSSF VLVAEFLSHQ IVKYWLEGPK 

       250        260        270        280        290        300 
KGTAEVLVKI PNPGNIKRNA DGHFWVSSSE ELDGNMHGRV DPKGIKFDEF GNILEVIPLP 

       310        320        330        340 
PPFAGEHFEQ IQEHDGLLYI GTLFHGSVGI LVYDKKGNSF VSSH

« Hide

References

[1]"The cDNA clone for strictosidine synthase from Rauvolfia serpentina. DNA sequence determination and expression in Escherichia coli."
Kutchan T.M., Hampp N., Lottspeich F., Beyreuther K., Zenk M.H.
FEBS Lett. 237:40-44(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Strictosidine synthase from Rauvolfia serpentina: analysis of a gene involved in indole alkaloid biosynthesis."
Bracher D., Kutchan T.M.
Arch. Biochem. Biophys. 294:717-723(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y00756 mRNA. Translation: CAA68725.1.
X62334 Genomic DNA. Translation: CAA44208.1.
PIRS01325.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FP8X-ray2.30A/B23-344[»]
2FP9X-ray2.96A/B23-344[»]
2FPBX-ray2.80A/B23-344[»]
2FPCX-ray3.00A/B23-344[»]
2V91X-ray3.01A/B32-333[»]
2VAQX-ray3.01A/B23-344[»]
3V1SX-ray2.33A/B23-344[»]
ProteinModelPortalP68175.
SMRP68175. Positions 29-333.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00311; UER00447.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR018119. Strictosidine_synth_cons-reg.
[Graphical view]
PfamPF03088. Str_synth. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP68175.

Entry information

Entry nameSTSY_RAUSE
AccessionPrimary (citable) accession number: P68175
Secondary accession number(s): P15324
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: October 25, 2004
Last modified: April 3, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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