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Protein

Strictosidine synthase

Gene

STR1

Organism
Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi: 3alpha(S)-strictosidine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 3alpha(S)-strictosidine from secologanin and tryptamine.
Proteins known to be involved in this subpathway in this organism are:
  1. Strictosidine synthase (STR1)
This subpathway is part of the pathway 3alpha(S)-strictosidine biosynthesis, which is itself part of Alkaloid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 3alpha(S)-strictosidine from secologanin and tryptamine, the pathway 3alpha(S)-strictosidine biosynthesis and in Alkaloid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processAlkaloid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11582
BRENDAi4.3.3.2 1211
UniPathwayi
UPA00311;UER00447

Names & Taxonomyi

Protein namesi
Recommended name:
Strictosidine synthase (EC:4.3.3.2)
Gene namesi
Name:STR1
Synonyms:SSS
OrganismiCatharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Taxonomic identifieri4058 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesApocynaceaeRauvolfioideaeVinceaeCatharanthinaeCatharanthus

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4369

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 311 PublicationAdd BLAST31
ChainiPRO_000003333232 – 352Strictosidine synthaseAdd BLAST321

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi95N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi187N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP18417
SMRiP18417
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the strictosidine synthase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KOiK01757

Family and domain databases

Gene3Di2.120.10.30, 1 hit
InterProiView protein in InterPro
IPR011042 6-blade_b-propeller_TolB-like
IPR018119 Strictosidine_synth_cons-reg
IPR004141 Strictosidine_synthase
PANTHERiPTHR10426 PTHR10426, 1 hit
PfamiView protein in Pfam
PF03088 Str_synth, 1 hit

Sequencei

Sequence statusi: Complete.

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

P18417-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MANFSESKSM MAVFFMFFLL LLSSSSSSSS SSPILKKIFI ESPSYAPNAF
60 70 80 90 100
TFDSTDKGFY TSVQDGRVIK YEGPNSGFTD FAYASPFWNK AFCENSTDPE
110 120 130 140 150
KRPLCGRTYD ISYDYKNSQM YIVDGHYHLC VVGKEGGYAT QLATSVQGVP
160 170 180 190 200
FKWLYAVTVD QRTGIVYFTD VSSIHDDSPE GVEEIMNTSD RTGRLMKYDP
210 220 230 240 250
STKETTLLLK ELHVPGGAEI SADGSFVVVA EFLSNRIVKY WLEGPKKGSA
260 270 280 290 300
EFLVTIPNPG NIKRNSDGHF WVSSSEELDG GQHGRVVSRG IKFDGFGNIL
310 320 330 340 350
QVIPLPPPYE GEHFEQIQEH DGLLYIGSLF HSSVGILVYD DHDNKGNSYV

SS
Length:352
Mass (Da):39,094
Last modified:April 1, 1993 - v2
Checksum:i1D6DD289A00272B8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti285R → S in CAA37671 (PubMed:2395663).Curated1
Sequence conflicti330F → S in CAA37671 (PubMed:2395663).Curated1
Sequence conflicti352S → QLVIN in CAA37671 (PubMed:2395663).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61932 mRNA Translation: CAA43936.1
Y10182 Genomic DNA Translation: CAA71255.1
X53602 mRNA Translation: CAA37671.1
PIRiS22464

Genome annotation databases

KEGGiag:CAA37671

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61932 mRNA Translation: CAA43936.1
Y10182 Genomic DNA Translation: CAA71255.1
X53602 mRNA Translation: CAA37671.1
PIRiS22464

3D structure databases

ProteinModelPortaliP18417
SMRiP18417
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

ChEMBLiCHEMBL4369

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA37671

Phylogenomic databases

KOiK01757

Enzyme and pathway databases

UniPathwayi
UPA00311;UER00447

BioCyciMetaCyc:MONOMER-11582
BRENDAi4.3.3.2 1211

Family and domain databases

Gene3Di2.120.10.30, 1 hit
InterProiView protein in InterPro
IPR011042 6-blade_b-propeller_TolB-like
IPR018119 Strictosidine_synth_cons-reg
IPR004141 Strictosidine_synthase
PANTHERiPTHR10426 PTHR10426, 1 hit
PfamiView protein in Pfam
PF03088 Str_synth, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSTSY_CATRO
AccessioniPrimary (citable) accession number: P18417
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: April 1, 1993
Last modified: February 28, 2018
This is version 94 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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Main funding by: National Institutes of Health

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