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Protein

Pinosylvin synthase

Gene
N/A
Organism
Pinus sylvestris (Scots pine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the production of pinosylvin from cinnamoyl-CoA and malonyl-CoA, and dihydropinosylvin from dihydrocinnamoyl-CoA.1 Publication

Catalytic activityi

3 malonyl-CoA + cinnamoyl-CoA = 4 CoA + pinosylvin + 4 CO2.1 Publication
3 malonyl-CoA + dihydrocinnamoyl-CoA = 4 CoA + dihydropinosylvin + 4 CO2.1 Publication

Kineticsi

  1. KM=1 µM for cinnamoyl-CoA1 Publication
  2. KM=5 µM for dihydrocinnamoyl-CoA1 Publication
  1. Vmax=0.12 nmol/sec/mg enzyme with cinnamoyl-CoA as substrate1 Publication
  2. Vmax=0.15 nmol/sec/mg enzyme with dihydrocinnamoyl-CoA as substrate1 Publication

Pathwayi: hydropinosylvin biosynthesis

This protein is involved in the pathway hydropinosylvin biosynthesis, which is part of Phytoalexin biosynthesis.
View all proteins of this organism that are known to be involved in the pathway hydropinosylvin biosynthesis and in Phytoalexin biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei167 – 1671PROSITE-ProRule annotation
Binding sitei270 – 2701Substrate; via carbonyl oxygen

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BRENDAi2.3.1.146. 4856.
UniPathwayiUPA00374.

Names & Taxonomyi

Protein namesi
Recommended name:
Pinosylvin synthase1 Publication (EC:2.3.1.1461 Publication)
Alternative name(s):
Dihydropinosylvin synthase1 Publication
Pinosylvin-forming stilbene synthase
Stilbene synthase
Short name:
STS
OrganismiPinus sylvestris (Scots pine)
Taxonomic identifieri3349 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinidaePinalesPinaceaePinusPinus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi165 – 1651H → Q: Reduced activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393Pinosylvin synthasePRO_0000216078Add
BLAST

Expressioni

Inductioni

By stress.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
393
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 137Combined sources
Beta strandi19 – 279Combined sources
Beta strandi32 – 343Combined sources
Helixi35 – 373Combined sources
Helixi38 – 458Combined sources
Helixi52 – 6312Combined sources
Beta strandi69 – 713Combined sources
Helixi76 – 805Combined sources
Helixi83 – 864Combined sources
Beta strandi87 – 915Combined sources
Helixi94 – 12027Combined sources
Helixi124 – 1263Combined sources
Beta strandi129 – 1357Combined sources
Beta strandi139 – 1413Combined sources
Helixi143 – 1519Combined sources
Beta strandi158 – 1647Combined sources
Helixi169 – 18214Combined sources
Beta strandi189 – 1957Combined sources
Turni197 – 2004Combined sources
Helixi209 – 2179Combined sources
Beta strandi221 – 23010Combined sources
Turni233 – 2353Combined sources
Beta strandi239 – 24911Combined sources
Beta strandi256 – 2627Combined sources
Beta strandi265 – 2706Combined sources
Helixi274 – 29017Combined sources
Helixi291 – 2933Combined sources
Helixi298 – 3003Combined sources
Beta strandi301 – 3055Combined sources
Helixi310 – 31910Combined sources
Turni324 – 3274Combined sources
Helixi328 – 33710Combined sources
Helixi341 – 3433Combined sources
Helixi344 – 35815Combined sources
Turni364 – 3674Combined sources
Beta strandi369 – 3779Combined sources
Turni378 – 3803Combined sources
Beta strandi381 – 3899Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U0UX-ray2.11A/B/C/D/E/F1-393[»]
1XESX-ray1.70A/B/C/D1-393[»]
1XETX-ray2.00A/B/C/D1-393[»]
ProteinModelPortaliQ02323.
SMRiQ02323. Positions 5-393.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02323.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 604Substrate binding
Regioni308 – 3103Substrate binding

Sequence similaritiesi

Belongs to the chalcone/stilbene synthases family.Curated

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiIPR012328. Chalcone/stilbene_synth_C.
IPR018088. Chalcone/stilbene_synthase_AS.
IPR001099. Chalcone/stilbene_synthase_N.
IPR011141. Polyketide_synthase_type-III.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF02797. Chal_sti_synt_C. 1 hit.
PF00195. Chal_sti_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000451. PKS_III. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
PROSITEiPS00441. CHALCONE_SYNTH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02323-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGVDFEGFR KLQRADGFAS ILAIGTANPP NAVDQSTYPD FYFRITGNEH
60 70 80 90 100
NTELKDKFKR ICERSAIKQR YMYLTEEILK KNPDVCAFVE VPSLDARQAM
110 120 130 140 150
LAMEVPRLAK EAAEKAIQEW GQSKSGITHL IFCSTTTPDL PGADFEVAKL
160 170 180 190 200
LGLHPSVKRV GVFQHGCFAG GTVLRMAKDL AENNRGARVL VICSETTAVT
210 220 230 240 250
FRGPSETHLD SLVGQALFGD GASALIVGAD PIPQVEKACF EIVWTAQTVV
260 270 280 290 300
PNSEGAIGGK VREVGLTFQL KGAVPDLISA NIENCMVEAF SQFKISDWNK
310 320 330 340 350
LFWVVHPGGR AILDRVEAKL NLDPTKLIPT RHVMSEYGNM SSACVHFILD
360 370 380 390
QTRKASLQNG CSTTGEGLEM GVLFGFGPGL TIETVVLKSV PIQ
Length:393
Mass (Da):42,735
Last modified:October 1, 1994 - v1
Checksum:iD4A00036D3E72641
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti306 – 3061H → N in AAB24341 (PubMed:1451785).Curated
Sequence conflicti310 – 3101R → P in AAB24341 (PubMed:1451785).Curated
Sequence conflicti345 – 3451V → F in AAB24341 (PubMed:1451785).Curated
Sequence conflicti358 – 3581Q → E in AAB24341 (PubMed:1451785).Curated
Sequence conflicti361 – 3611C → F in AAB24341 (PubMed:1451785).Curated
Sequence conflicti378 – 3781Missing in AAB24341 (PubMed:1451785).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60753 Genomic DNA. Translation: CAA43165.1.
S50350 mRNA. Translation: AAB24341.2.
L00659 Genomic DNA. Translation: AAA50524.1.
L00660 Genomic DNA. Translation: AAA50525.1.
PIRiS20514.
S21123.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60753 Genomic DNA. Translation: CAA43165.1.
S50350 mRNA. Translation: AAB24341.2.
L00659 Genomic DNA. Translation: AAA50524.1.
L00660 Genomic DNA. Translation: AAA50525.1.
PIRiS20514.
S21123.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U0UX-ray2.11A/B/C/D/E/F1-393[»]
1XESX-ray1.70A/B/C/D1-393[»]
1XETX-ray2.00A/B/C/D1-393[»]
ProteinModelPortaliQ02323.
SMRiQ02323. Positions 5-393.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00374.
BRENDAi2.3.1.146. 4856.

Miscellaneous databases

EvolutionaryTraceiQ02323.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiIPR012328. Chalcone/stilbene_synth_C.
IPR018088. Chalcone/stilbene_synthase_AS.
IPR001099. Chalcone/stilbene_synthase_N.
IPR011141. Polyketide_synthase_type-III.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF02797. Chal_sti_synt_C. 1 hit.
PF00195. Chal_sti_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000451. PKS_III. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
PROSITEiPS00441. CHALCONE_SYNTH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular analysis of chalcone and dihydropinosylvin synthase from Scots pine (Pinus sylvestris), and differential regulation of these and related enzyme activities in stressed plants."
    Fliegmann J., Schroeder G., Schanz S., Britsch L., Schroeder J.
    Plant Mol. Biol. 18:489-503(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Pine stilbene synthase cDNA, a tool for probing environmental stress."
    Schwekendiek A., Pfeffer G., Kindl H.
    FEBS Lett. 301:41-44(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "A single change of histidine to glutamine alters the substrate preference of a stilbene synthase."
    Schroeder G., Schroeder J.
    J. Biol. Chem. 267:20558-20560(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 161-172, FUNCTION, MUTAGENESIS.
  4. "Stilbene synthase from Scots pine (Pinus sylvestris)."
    Schanz S., Schroeder G., Schroeder J.
    FEBS Lett. 313:71-74(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  5. "An aldol switch discovered in stilbene synthases mediates cyclization specificity of type III polyketide synthases."
    Austin M.B., Bowman M.E., Ferrer J.-L., Schroeder J., Noel J.P.
    Chem. Biol. 11:1179-1194(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS), REACTION MECHANISM.
  6. "Crystal structure of stilbene synthase from Pinus sylvestris, complexed with methylmalonyl CoA."
    Ng S.H., Chirgadze D., Spiteller D., Li T.L., Spencer J.B., Blundell T.L.
    Submitted (SEP-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH METHYLMALONYL COA.

Entry informationi

Entry nameiDPSS_PINSY
AccessioniPrimary (citable) accession number: Q02323
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 14, 2015
This is version 86 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.