Q02323 (DPSS_PINSY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Dihydropinosylvin synthase EC=2.3.1.- Alternative name(s): Pinosylvin-forming stilbene synthase Stilbene synthase Short name=STS
Organism	Pinus sylvestris (Scots pine)
Taxonomic identifier	3349 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Coniferopsida › Coniferales › Pinaceae › Pinus › Pinus

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	3 malonyl-CoA + dihydrocinnamoyl-CoA = 4 CoA + dihydropinosylvin + 3 CO2.
Pathway	Phytoalexin biosynthesis; hydropinosylvin biosynthesis.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Induction	By stress.
Sequence similarities	Belongs to the chalcone/stilbene synthases family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	transferase activity, transferring acyl groups other than amino-acyl groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 393

393

Dihydropinosylvin synthase

PRO_0000216078

Regions

Region

57 – 60

4

Substrate binding

Region

308 – 310

3

Substrate binding

Sites

Active site

167

1

By similarity

Binding site

270

1

Substrate; via carbonyl oxygen

Experimental info

Mutagenesis

165

1

H → Q: Reduced activity.

Sequence conflict

306

1

H → N in AAB24341. Ref.2

Sequence conflict

310

1

R → P in AAB24341. Ref.2

Sequence conflict

345

1

V → F in AAB24341. Ref.2

Sequence conflict

358

1

Q → E in AAB24341. Ref.2

Sequence conflict

361

1

C → F in AAB24341. Ref.2

Sequence conflict

378

1

Missing in AAB24341. Ref.2

Secondary structure

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393

Helix Strand Turn

Details...

Helix

6 – 13

8

Beta strand

19 – 27

9

Beta strand

32 – 34

3

Turn

35 – 37

3

Helix

38 – 45

8

Helix

52 – 64

13

Beta strand

69 – 71

3

Helix

76 – 80

5

Helix

83 – 86

4

Beta strand

87 – 91

5

Helix

94 – 120

27

Beta strand

129 – 135

7

Beta strand

138 – 141

4

Helix

143 – 151

9

Beta strand

158 – 164

7

Helix

169 – 183

15

Beta strand

188 – 195

8

Helix

197 – 199

3

Helix

209 – 217

9

Beta strand

221 – 230

10

Turn

233 – 235

3

Beta strand

240 – 249

10

Beta strand

256 – 262

7

Beta strand

265 – 270

6

Helix

274 – 290

17

Helix

291 – 293

3

Helix

298 – 300

3

Beta strand

301 – 305

5

Helix

310 – 320

11

Turn

324 – 327

4

Helix

328 – 337

10

Helix

341 – 343

3

Helix

344 – 359

16

Beta strand

362 – 365

4

Beta strand

368 – 377

10

Turn

378 – 380

3

Beta strand

381 – 389

9

Sequences

	Sequence		Length	Mass (Da)
	Q02323 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: D4A00036D3E72641	FASTA	393	42,735
	10 20 30 40 50 60 MGGVDFEGFR KLQRADGFAS ILAIGTANPP NAVDQSTYPD FYFRITGNEH NTELKDKFKR 70 80 90 100 110 120 ICERSAIKQR YMYLTEEILK KNPDVCAFVE VPSLDARQAM LAMEVPRLAK EAAEKAIQEW 130 140 150 160 170 180 GQSKSGITHL IFCSTTTPDL PGADFEVAKL LGLHPSVKRV GVFQHGCFAG GTVLRMAKDL 190 200 210 220 230 240 AENNRGARVL VICSETTAVT FRGPSETHLD SLVGQALFGD GASALIVGAD PIPQVEKACF 250 260 270 280 290 300 EIVWTAQTVV PNSEGAIGGK VREVGLTFQL KGAVPDLISA NIENCMVEAF SQFKISDWNK 310 320 330 340 350 360 LFWVVHPGGR AILDRVEAKL NLDPTKLIPT RHVMSEYGNM SSACVHFILD QTRKASLQNG 370 380 390 CSTTGEGLEM GVLFGFGPGL TIETVVLKSV PIQ

References

[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: 1536925] [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: 1451785] [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: 1400374] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 161-172, MUTAGENESIS.
[4]	"Stilbene synthase from Scots pine (Pinus sylvestris)." Schanz S., Schroeder G., Schroeder J. FEBS Lett. 313:71-74(1992) [PubMed: 1426272] [Abstract] Cited for: CHARACTERIZATION.
[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: 15380179] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS).
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X60753 Genomic DNA. Translation: CAA43165.1.
S50350 mRNA. Translation: AAB24341.2. Sequence problems.
L00659 Genomic DNA. Translation: AAA50524.1.
L00660 Genomic DNA. Translation: AAA50525.1.

PIR

S20514.
S21123.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U0U	X-ray	2.11	A/B/C/D/E/F	1-393	[»]
1XES	X-ray	1.70	A/B/C/D	1-393	[»]
1XET	X-ray	2.00	A/B/C/D	1-393	[»]

ProteinModelPortal

Q02323.

SMR

Q02323. Positions 5-393.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR012328. Chalcone/stilbene_synth_C.
IPR018088. Chalcone/stilbene_synthase_AS.
IPR001099. Chalcone/stilbene_synthase_N.
IPR011141. Polyketide_synthase_type-III.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]

Gene3D

G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.

Pfam

PF02797. Chal_sti_synt_C. 1 hit.
PF00195. Chal_sti_synt_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000451. PKS_III. 1 hit.

SUPFAM

SSF53901. Thiolase-like. 2 hits.

PROSITE

PS00441. CHALCONE_SYNTH. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DPSS_PINSY

Accession

Primary (citable) accession number: Q02323

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	October 19, 2011
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program