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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)DescriptionActionsGraphical viewLength
Active sitei167PROSITE-ProRule annotation1
Binding sitei270Substrate; via carbonyl oxygen1

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)DescriptionActionsGraphical viewLength
Mutagenesisi165H → Q: Reduced activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002160781 – 393Pinosylvin synthaseAdd BLAST393

Expressioni

Inductioni

By stress.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1393
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 13Combined sources7
Beta strandi19 – 27Combined sources9
Beta strandi32 – 34Combined sources3
Helixi35 – 37Combined sources3
Helixi38 – 45Combined sources8
Helixi52 – 63Combined sources12
Beta strandi69 – 71Combined sources3
Helixi76 – 80Combined sources5
Helixi83 – 86Combined sources4
Beta strandi87 – 91Combined sources5
Helixi94 – 120Combined sources27
Helixi124 – 126Combined sources3
Beta strandi129 – 135Combined sources7
Beta strandi139 – 141Combined sources3
Helixi143 – 151Combined sources9
Beta strandi158 – 164Combined sources7
Helixi169 – 182Combined sources14
Beta strandi189 – 195Combined sources7
Turni197 – 200Combined sources4
Helixi209 – 217Combined sources9
Beta strandi221 – 230Combined sources10
Turni233 – 235Combined sources3
Beta strandi239 – 249Combined sources11
Beta strandi256 – 262Combined sources7
Beta strandi265 – 270Combined sources6
Helixi274 – 290Combined sources17
Helixi291 – 293Combined sources3
Helixi298 – 300Combined sources3
Beta strandi301 – 305Combined sources5
Helixi310 – 319Combined sources10
Turni324 – 327Combined sources4
Helixi328 – 337Combined sources10
Helixi341 – 343Combined sources3
Helixi344 – 358Combined sources15
Turni364 – 367Combined sources4
Beta strandi369 – 377Combined sources9
Turni378 – 380Combined sources3
Beta strandi381 – 389Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02323.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni57 – 60Substrate binding4
Regioni308 – 310Substrate binding3

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)DescriptionActionsGraphical viewLength
Sequence conflicti306H → N in AAB24341 (PubMed:1451785).Curated1
Sequence conflicti310R → P in AAB24341 (PubMed:1451785).Curated1
Sequence conflicti345V → F in AAB24341 (PubMed:1451785).Curated1
Sequence conflicti358Q → E in AAB24341 (PubMed:1451785).Curated1
Sequence conflicti361C → F in AAB24341 (PubMed:1451785).Curated1
Sequence conflicti378Missing in AAB24341 (PubMed:1451785).Curated1

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
PDB 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.
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...

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: November 2, 2016
This is version 88 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.