Reviewed, UniProtKB/Swiss-Prot Q8LAH7 (OPR1_ARATH)

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
      Short name=AtOPR1
    FS-AT-I

Gene names

Name:	OPR1
Ordered Locus Names:	At1g76680
ORF Names:	F28O16.5

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 only poorly 9S,13S-OPDA, the natural precursor of jasmonic acid.
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.
Pathway	Lipid metabolism; oxylipin biosynthesis.
Subcellular location	Cytoplasm. Ref.9
Tissue specificity	Mostly expressed in roots, also present in leaves, shoots and flowers. More abundant in cotyledons. In more details, expressed in peduncles, sepals, petals, around the abscission zone of siliques, maturing siliques and developing seeds. Ref.2
Developmental stage	Expressed during leaves senescence, seeds development, and siliques maturation.
Induction	By wounding, locally and systemically, by cold and heat stresses, by jasmonate and by UV-C. Up-regulated during senescence. Seems to not be influenced by UV-A and UV-B. Ref.2 Ref.8
Sequence similarities	Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis Oxylipin biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	FMN Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxylipin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to cadmium ion Inferred from expression pattern. Source: TAIR response to salicylic acid stimulus Inferred from expression pattern. Source: TAIR response to wounding Ref.2 Inferred from expression pattern. Source: TAIR
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	12-oxophytodienoate reductase activity Ref.1 Inferred from direct assay. Source: TAIR FMN binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q8LAH7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 372

372

12-oxophytodienoate reductase 1

PRO_0000194483

Regions

Region

133 – 147

15

Substrate-binding loop By similarity

Region

138 – 139

2

Substrate-binding By similarity

Region

183 – 186

4

Substrate-binding By similarity

Sites

Active site

188

1

Proton donor By similarity

Binding site

33

1

FMN

Binding site

106

1

FMN

Binding site

235

1

FMN

Binding site

327

1

FMN

Experimental info

Sequence conflict

43 – 44

2

Missing in CAA71627. Ref.1

Sequence conflict

184

1

G → R in AAM65337. Ref.6

Secondary structure

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372

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 – 52

9

Beta strand

59 – 61

3

Beta strand

65 – 68

4

Helix

83 – 98

16

Beta strand

102 – 108

7

Helix

116 – 118

3

Helix

120 – 122

3

Beta strand

126 – 129

4

Beta strand

140 – 147

8

Helix

155 – 157

3

Helix

159 – 175

17

Beta strand

178 – 184

7

Helix

189 – 194

6

Turn

196 – 198

3

Beta strand

206 – 208

3

Helix

209 – 227

19

Helix

229 – 231

3

Beta strand

232 – 236

5

Turn

242 – 244

3

Helix

250 – 260

11

Turn

261 – 265

5

Beta strand

267 – 272

6

Helix

289 – 295

7

Beta strand

298 – 305

8

Helix

308 – 316

9

Beta strand

321 – 326

6

Helix

327 – 331

5

Helix

335 – 341

7

Helix

350 – 352

3

Turn

360 – 362

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 26, 2005. Version 2. Checksum: 213C8C850FF691CB	FASTA	372	41,168
	10 20 30 40 50 60 MENGEAKQSV PLLTPYKMGR FNLSHRVVLA PLTRQRSYGN VPQPHAAIYY SQRTTPGGFL 70 80 90 100 110 120 ITEATGVSDT AQGYQDTPGI WTKEHVEAWK PIVDAVHAKG GIFFCQIWHV GRVSNSGFQP 130 140 150 160 170 180 NGKAPISCSD KPLMPQIRSN GIDEALFTPP RRLGIEEIPG IVNDFRLAAR NAMEAGFDGV 190 200 210 220 230 240 EIHGANGYLI DQFMKDTVND RTDEYGGSLQ NRCKFPLEIV DAVAKEIGPD RVGIRLSPFA 250 260 270 280 290 300 DYMESGDTNP GALGLYMAES LNKYGILYCH VIEARMKTMG EVHACPHTLM PMRKAFKGTF 310 320 330 340 350 360 ISAGGFTRED GNEAVSKGRT DLVAYGRWFL ANPDLPKRFQ VDAPLNKYDR PTFYTSDPVV 370 GYTDYPFLES TA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of 12-oxophytodienoate reductase, an enzyme of the octadecanoid signaling pathway from Arabidopsis thaliana. Structural and functional relationship to yeast old yellow enzyme." Schaller F., Weiler E.W. J. Biol. Chem. 272:28066-28072(1997) [PubMed: 9346960] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY. Strain: cv. Columbia.
[2]	"Structure and regulation of OPR1 and OPR2, two closely related genes encoding 12-oxophytodienoic acid-10,11-reductases from Arabidopsis thaliana." Biesgen C., Weiler E.W. Planta 208:155-165(1999) [PubMed: 10333582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Arabidopsis ORF clones." Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R. Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis." Schaller F., Biesgen C., Muessig C., Altmann T., Weiler E.W. Planta 210:979-984(2000) [PubMed: 10872231] [Abstract] Cited for: SUBSTRATE SPECIFICITY.
[8]	"Identical promoter elements are involved in regulation of the OPR1 gene by senescence and jasmonic acid in Arabidopsis." He Y., Gan S. Plant Mol. Biol. 47:595-605(2001) [PubMed: 11725945] [Abstract] Cited for: INDUCTION.
[9]	"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: SUBCELLULAR LOCATION.
[10]	"X-ray structure of gene product from Arabidopsis thaliana At1g76680." Wesenberg G.E., Smith D.W., Phillips G.N. Jr., Johnson K.A., Bingman C.A. Submitted (MAR-2004) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FMN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Y10617 mRNA. Translation: CAA71627.1.
U92460 Genomic DNA. Translation: AAC78440.1.
AC010718 Genomic DNA. Translation: AAF04448.1.
AY074874 mRNA. Translation: AAL75894.1.
BT020365 mRNA. Translation: AAV85720.1.
AY087801 mRNA. Translation: AAM65337.1.

IPI

IPI00548191.

PIR

B96795.

RefSeq

NP_177794.1.

UniGene

At.11155
At.67448
At.73001

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VJI	X-ray	2.00	A	1-372	[»]
2Q3R	X-ray	2.00	A	1-372	[»]

ModBase

Search...

Proteomic databases

PRIDE

Q8LAH7.

Genome annotation databases

GeneID

844001.

GenomeReviews

Gene locus AT1G76680 in contig CT485782_GR.

KEGG

ath:AT1G76680.

NMPDR

fig|3702.1.peg.7194.

Organism-specific databases

GeneFarm

4901. 471.

TAIR

At1g76680.

Enzyme and pathway databases

BRENDA

1.3.1.42. 302.

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_ARATH

Accession

Primary (citable) accession number: Q8LAH7
Secondary accession number(s): O49259, Q9S806

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	April 26, 2005
Last modified:	June 16, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)