Q9FEW9 (OPR3_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
12-oxophytodienoate reductase 3
EC=1.3.1.42

Alternative name(s):
12-oxophytodienoate-10,11-reductase 3
Short name=OPDA-reductase 3
LeOPR3

Gene names

Name:

OPR3

Organism

Solanum lycopersicum (Tomato) (Lycopersicon esculentum) [Reference proteome]

Taxonomic identifier

4081 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Specifically cleaves olefinic bonds in cyclic enones. Involved in the biosynthesis of jasmonic acid (JA) and perhaps in biosynthesis or metabolism of other oxylipin signaling moleclules. It is required for the spatial and temporal regulation of JA levels during dehiscence of anthers, promoting the stomium degeneration program By similarity. In vitro, reduces 9S,13S-12-oxophytodienoic acid (9S,13S-OPDA) and 9R,13R-OPDA to 9S,13S-OPC-8:0 and 9R,13R-OPC-8:0, respectively.
Catalytic activity	8-((1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl)octanoate + NADP+ = (15Z)-12-oxophyto-10,15-dienoate + NADPH.
Cofactor	FMN By similarity. Ref.1
Pathway	Lipid metabolism; oxylipin biosynthesis.
Subcellular location	Peroxisome Ref.1.
Tissue specificity	Expressed in roots and to lower extend in leaves and flowers.
Induction	By wounding, locally and systemically.
Sequence similarities	Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Oxylipin biosynthesis
Cellular component	Peroxisome
Ligand	FMN Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	oxylipin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	12-oxophytodienoate reductase activity Inferred from electronic annotation. Source: EC FMN binding 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 – 396

396

12-oxophytodienoate reductase 3

PRO_0000194489

Regions

Nucleotide binding

31 – 33

3

FMN

Nucleotide binding

342 – 343

2

FMN By similarity

Region

185 – 188

4

Substrate-binding By similarity

Region

342 – 343

2

FMN

Motif

394 – 396

3

Microbody targeting signal Potential

Sites

Active site

190

1

Proton donor By similarity

Binding site

64

1

FMN; via amide nitrogen

Binding site

106

1

FMN

Binding site

237

1

FMN

Binding site

283

1

Substrate; via amide nitrogen By similarity

Binding site

321

1

FMN; via amide nitrogen

Secondary structure

1

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396

Helix Strand Turn

Details...

Helix

11 – 13

3

Beta strand

16 – 18

3

Beta strand

21 – 24

4

Beta strand

26 – 29

4

Helix

38 – 40

3

Helix

44 – 53

10

Beta strand

59 – 61

3

Beta strand

65 – 68

4

Beta strand

74 – 76

3

Helix

83 – 98

16

Beta strand

102 – 108

7

Helix

116 – 118

3

Helix

120 – 122

3

Beta strand

126 – 128

3

Beta strand

138 – 140

3

Beta strand

146 – 148

3

Helix

157 – 159

3

Helix

160 – 176

17

Beta strand

180 – 185

6

Helix

191 – 196

6

Turn

198 – 200

3

Beta strand

208 – 210

3

Helix

211 – 229

19

Helix

231 – 233

3

Beta strand

234 – 238

5

Helix

244 – 246

3

Helix

252 – 270

19

Beta strand

275 – 280

6

Turn

286 – 289

4

Beta strand

290 – 292

3

Turn

293 – 296

4

Helix

297 – 311

15

Beta strand

312 – 314

3

Beta strand

316 – 321

6

Helix

324 – 332

9

Beta strand

337 – 342

6

Helix

343 – 347

5

Helix

351 – 357

7

Helix

366 – 368

3

Turn

376 – 378

3

Sequences

	Sequence		Length	Mass (Da)
	Q9FEW9 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: C9550E54D2EAF75B	FASTA	396	43,520
	10 20 30 40 50 60 MASSAQDGNN PLFSPYKMGK FNLSHRVVLA PMTRCRALNN IPQAALGEYY EQRATAGGFL 70 80 90 100 110 120 ITEGTMISPT SAGFPHVPGI FTKEQVREWK KIVDVVHAKG AVIFCQLWHV GRASHEVYQP 130 140 150 160 170 180 AGAAPISSTE KPISNRWRIL MPDGTHGIYP KPRAIGTYEI SQVVEDYRRS ALNAIEAGFD 190 200 210 220 230 240 GIEIHGAHGY LIDQFLKDGI NDRTDEYGGS LANRCKFITQ VVQAVVSAIG ADRVGVRVSP 250 260 270 280 290 300 AIDHLDAMDS NPLSLGLAVV ERLNKIQLHS GSKLAYLHVT QPRYVAYGQT EAGRLGSEEE 310 320 330 340 350 360 EARLMRTLRN AYQGTFICSG GYTRELGIEA VAQGDADLVS YGRLFISNPD LVMRIKLNAP 370 380 390 LNKYNRKTFY TQDPVVGYTD YPFLQGNGSN GPLSRL

References

[1]	"Characterization and cDNA-microarray expression analysis of 12-oxophytodienoate reductases reveals differential roles for octadecanoid biosynthesis in the local versus the systemic wound response." Strassner J., Schaller F., Frick U.B., Howe G.A., Weiler E.W., Amrhein N., Macheroux P., Schaller A. Plant J. 32:585-601(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], COFACTOR, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION. Strain: cv. Castlemart II. Tissue: Shoot.
[2]	"Crystal structure of 12-oxophytodienoate reductase 3 from tomato: self-inhibition by dimerization." Breithaupt C., Kurzbauer R., Lilie H., Schaller A., Strassner J., Huber R., Macheroux P., Clausen T. Proc. Natl. Acad. Sci. U.S.A. 103:14337-14342(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH FMN.
[3]	"Structural basis of substrate specificity of plant 12-oxophytodienoate reductases." Breithaupt C., Kurzbauer R., Schaller F., Stintzi A., Schaller A., Huber R., Macheroux P., Clausen T. J. Mol. Biol. 392:1266-1277(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FMN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ278332 mRNA. Translation: CAC21424.1.

RefSeq

NP_001233873.1. NM_001246944.1.

UniGene

Les.3762.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HS6	X-ray	1.90	A/B	1-396	[»]
2HS8	X-ray	1.90	A/B	1-396	[»]
2HSA	X-ray	1.50	A/B	1-396	[»]
3HGO	X-ray	2.30	A/B	1-396	[»]
3HGS	X-ray	2.00	A/B	1-396	[»]

ProteinModelPortal

Q9FEW9.

SMR

Q9FEW9. Positions 10-385.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

Solyc07g007870.2.1; Solyc07g007870.2.1; Solyc07g007870.2.

GeneID

543763.

Enzyme and pathway databases

UniPathway

UPA00382.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR013785. Aldolase_TIM.
IPR001155. OxRdtase_FMN_N.
[Graphical view]

Pfam

PF00724. Oxidored_FMN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9FEW9.

Entry information

Entry name

OPR3_SOLLC

Accession

Primary (citable) accession number: Q9FEW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	March 1, 2001
Last modified:	April 3, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program