Q9XG54 (OPR1_SOLLC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
12-oxophytodienoate reductase 1
EC=1.3.1.42

Alternative name(s):
12-oxophytodienoate-10,11-reductase 1
Short name=OPDA-reductase 1
LeOPR1

Gene names

Name:

OPR1

Organism

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

Taxonomic identifier

4081 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Specifically cleaves olefinic bonds in alpha,beta-unsaturated carbonyls and may be involved in detoxification or modification of these reactive compounds. May be involved in the biosynthesis or metabolism of oxylipin signaling molecules. In vitro, reduces 9R,13R-12-oxophyodienoic acid (9R,13R-OPDA) to 9R,13R-OPC-8:0, but not 9S,13S-OPDA, the natural precursor of jasmonic acid. Also reduces N-ethylmaleimide and maleic acid. Ref.2
Catalytic activity	8-((1R,2R)-3-oxo-2-((Z)-pent-2-enyl)cyclopentyl)octanoate + NADP+ = (15Z)-12-oxophyto-10,15-dienoate + NADPH. Ref.1
Cofactor	FMN. Ref.2 Ref.3
Pathway	Lipid metabolism; oxylipin biosynthesis.
Subcellular location	Cytoplasm Ref.2.
Tissue specificity	Constitutively expressed in roots, leaves, cotyledons, cells culture and to lower extend in flowers. Ref.1
Induction	Seems to not be influenced by wounding.
Sequence similarities	Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.
Biophysicochemical properties	Kinetic parameters: The highest catalytic efficiency was observed with N-ethylmaleimide. KM=8 µM for N-ethylmaleimide (at pH 7.0 and 25 degrees Celsius) KM=47 µM for maleic acid (at pH 7.0 and 25 degrees Celsius) KM=15 µM for OPDA (at pH 7.0 and 25 degrees Celsius)

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis Oxylipin biosynthesis
Cellular component	Cytoplasm
Ligand	FMN Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxylipin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm 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 – 376

376

12-oxophytodienoate reductase 1

PRO_0000194488

Regions

Nucleotide binding

35 – 37

3

FMN

Nucleotide binding

330 – 331

2

FMN

Region

187 – 190

4

Substrate-binding

Sites

Active site

192

1

Proton donor

Binding site

68

1

FMN; via amide nitrogen

Binding site

110

1

FMN

Binding site

143

1

Substrate

Binding site

239

1

FMN

Binding site

279

1

Substrate; via amide nitrogen By similarity

Binding site

309

1

FMN; via amide nitrogen

Secondary structure

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376

Helix Strand Turn

Details...

Helix

15 – 17

3

Beta strand

20 – 22

3

Beta strand

25 – 28

4

Beta strand

30 – 33

4

Helix

42 – 44

3

Helix

48 – 56

9

Beta strand

63 – 65

3

Helix

73 – 75

3

Helix

87 – 102

16

Beta strand

106 – 112

7

Turn

120 – 122

3

Helix

124 – 126

3

Beta strand

130 – 134

5

Turn

159 – 161

3

Helix

162 – 178

17

Beta strand

182 – 188

7

Helix

193 – 198

6

Turn

200 – 202

3

Beta strand

210 – 212

3

Helix

213 – 231

19

Helix

233 – 235

3

Beta strand

236 – 240

5

Turn

246 – 248

3

Helix

254 – 265

12

Helix

266 – 268

3

Beta strand

271 – 276

6

Helix

294 – 299

6

Beta strand

304 – 309

6

Helix

312 – 320

9

Beta strand

325 – 330

6

Helix

331 – 335

5

Helix

339 – 345

7

Helix

354 – 356

3

Turn

364 – 366

3

Sequences

	Sequence		Length	Mass (Da)
	Q9XG54 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 83CFBEAC7CBC7A8F	FASTA	376	42,415
	10 20 30 40 50 60 MENKVVEEKQ VDKIPLMSPC KMGKFELCHR VVLAPLTRQR SYGYIPQPHA ILHYSQRSTN 70 80 90 100 110 120 GGLLIGEATV ISETGIGYKD VPGIWTKEQV EAWKPIVDAV HAKGGIFFCQ IWHVGRVSNK 130 140 150 160 170 180 DFQPNGEDPI SCTDRGLTPQ IRSNGIDIAH FTRPRRLTTD EIPQIVNEFR VAARNAIEAG 190 200 210 220 230 240 FDGVEIHGAH GYLIDQFMKD QVNDRSDKYG GSLENRCRFA LEIVEAVANE IGSDRVGIRI 250 260 270 280 290 300 SPFAHYNEAG DTNPTALGLY MVESLNKYDL AYCHVVEPRM KTAWEKIECT ESLVPMRKAY 310 320 330 340 350 360 KGTFIVAGGY DREDGNRALI EDRADLVAYG RLFISNPDLP KRFELNAPLN KYNRDTFYTS 370 DPIVGYTDYP FLETMT

References

[1]	"A homolog of old yellow enzyme in tomato: spectral properties and substrate specificity of the recombinant protein." Strassner J., Fuerholz A., Macheroux P., Amrhein N., Schaller A. J. Biol. Chem. 274:35067-35073(1999) [PubMed: 10574986] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CATALYTIC ACTIVITY. Strain: cv. Castlemart II. Tissue: Shoot.
[2]	"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: 12445129] [Abstract] Cited for: FUNCTION, COFACTOR, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION. Strain: cv. Castlemart II. Tissue: Shoot.
[3]	"X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE." Breithaupt C., Strassner J., Breitinger U., Huber R., Macheroux P., Schaller A., Clausen T. Structure 9:419-429(2001) [PubMed: 11377202] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBSTRATE SPECIFICITY, COFACTOR-BINDING.
[4]	"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: 19660473] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH FMN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ242551 mRNA. Translation: CAB43506.1.

RefSeq

NP_001234781.1. NM_001247852.1.

UniGene

Les.22.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ICP	X-ray	1.90	A/B	1-376	[»]
1ICQ	X-ray	2.00	A/B	1-376	[»]
1ICS	X-ray	2.30	A/B	1-376	[»]
3HGR	X-ray	2.30	A/B	1-376	[»]

ProteinModelPortal

Q9XG54.

SMR

Q9XG54. Positions 10-373.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

544239.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

Pfam

PF00724. Oxidored_FMN. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

OPR1_SOLLC

Accession

Primary (citable) accession number: Q9XG54

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	November 1, 1999
Last modified:	December 14, 2011
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program