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P18417 (STSY_CATRO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Synonyms:SSS
OrganismCatharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Taxonomic identifier4058 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsGentianalesApocynaceaeRauvolfioideaeVinceaeCatharanthus

Protein attributes

Sequence length352 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.

Sequence similarities

Belongs to the strictosidine synthase family.

Ontologies

Keywords
   Biological processAlkaloid metabolism
   Cellular componentVacuole
   DomainSignal
   Molecular functionLyase
   PTMGlycoprotein
   Technical termDirect 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 – 3131 Ref.1
Chain32 – 352321Strictosidine synthase
PRO_0000033332

Amino acid modifications

Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2851R → S in CAA37671. Ref.3
Sequence conflict3301F → S in CAA37671. Ref.3
Sequence conflict3521S → QLVIN in CAA37671. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P18417 [UniParc].

Last modified April 1, 1993. Version 2.
Checksum: 1D6DD289A00272B8

FASTA35239,094
        10         20         30         40         50         60 
MANFSESKSM MAVFFMFFLL LLSSSSSSSS SSPILKKIFI ESPSYAPNAF TFDSTDKGFY 

        70         80         90        100        110        120 
TSVQDGRVIK YEGPNSGFTD FAYASPFWNK AFCENSTDPE KRPLCGRTYD ISYDYKNSQM 

       130        140        150        160        170        180 
YIVDGHYHLC VVGKEGGYAT QLATSVQGVP FKWLYAVTVD QRTGIVYFTD VSSIHDDSPE 

       190        200        210        220        230        240 
GVEEIMNTSD RTGRLMKYDP STKETTLLLK ELHVPGGAEI SADGSFVVVA EFLSNRIVKY 

       250        260        270        280        290        300 
WLEGPKKGSA EFLVTIPNPG NIKRNSDGHF WVSSSEELDG GQHGRVVSRG IKFDGFGNIL 

       310        320        330        340        350 
QVIPLPPPYE GEHFEQIQEH DGLLYIGSLF HSSVGILVYD DHDNKGNSYV SS 

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References

[1]"Coordinated regulation of two indole alkaloid biosynthetic genes from Catharanthus roseus by auxin and elicitors."
Pasquali G., Goddijn O.J.M., de Waal A., Verpoorte R., Schilperoort R.A., Hoge J.H.C., Memelink J.
Plant Mol. Biol. 18:1121-1131(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-52.
Strain: cv. G. Don.
[2]Pasquali G., Erven A., Menke F., Memelink J.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: cv. Morning mist.
[3]"Nucleotide sequence of a cDNA encoding the vacuolar protein strictosidine synthase from Catharanthus roseus."
McKnight T.D., Roessner C.A., Devagupta R., Scott A.I., Nessler C.L.
Nucleic Acids Res. 18:4939-4939(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-352.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61932 mRNA. Translation: CAA43936.1.
Y10182 Genomic DNA. Translation: CAA71255.1.
X53602 mRNA. Translation: CAA37671.1.
PIRS22464.

3D structure databases

ProteinModelPortalP18417.
SMRP18417. Positions 33-339.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11582.
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

ChEMBLCHEMBL4369.

Entry information

Entry nameSTSY_CATRO
AccessionPrimary (citable) accession number: P18417
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: April 1, 1993
Last modified: April 3, 2013
This is version 77 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families