Q8LAH7 (OPR1_ARATH) 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=AtOPR1
Short name=OPDA-reductase 1
FS-AT-I

Gene names

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

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	372 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 only poorly 9S,13S-OPDA, the natural precursor of jasmonic acid. Can detoxify the explosive 2,4,6-trinitrotoluene (TNT) in vitro and in vivo by catalyzing its nitroreduction to form hydroxylamino-dinitrotoluene (HADNT). Ref.11
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.10.
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. Induced by the explosive 2,4,6-trinitrotoluene (TNT). Ref.2 Ref.9 Ref.11
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 Reference proteome
Gene Ontology (GO)
Biological process	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 Inferred from expression pattern Ref.2. Source: TAIR
Cellular component	cytosol Inferred from direct assay. Source: TAIR
Molecular function	12-oxophytodienoate reductase activity Inferred from direct assay Ref.1. 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

Nucleotide binding

31 – 33

3

FMN

Nucleotide binding

326 – 327

2

FMN

Region

183 – 186

4

Substrate-binding By similarity

Sites

Active site

188

1

Proton donor By similarity

Binding site

64

1

FMN; via amide nitrogen

Binding site

106

1

FMN

Binding site

139

1

Substrate By similarity

Binding site

235

1

FMN

Binding site

275

1

Substrate; via amide nitrogen By similarity

Binding site

305

1

FMN; via amide nitrogen

Experimental info

Sequence conflict

43 – 44

2

Missing in CAA71627. Ref.1

Sequence conflict

184

1

G → R in AAM65337. Ref.7

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]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"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.
[6]	"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.
[7]	"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].
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"The role of oxophytodienoate reductases in the detoxification of the explosive 2,4,6-trinitrotoluene by Arabidopsis." Beynon E.R., Symons Z.C., Jackson R.G., Lorenz A., Rylott E.L., Bruce N.C. Plant Physiol. 151:253-261(2009) [PubMed: 19605548] [Abstract] Cited for: FUNCTION, INDUCTION.
[12]	"X-ray structure of Arabidopsis At1g77680, 12-oxophytodienoate reductase isoform 1." Fox B.G., Malone T.E., Johnson K.A., Madson S.E., Aceti D., Bingman C.A., Blommel P.G., Buchan B., Burns B., Cao J., Cornilescu C., Doreleijers J., Ellefson J., Frederick R., Geetha H., Hruby D., Jeon W.B., Kimball T. , Kunert J., Markley J.L., Newman C., Olson A., Peterson F.C., Phillips G.N. Jr., Primm J., Ramirez B., Rosenberg N.S., Runnels M., Seder K., Shaw J., Smith D.W., Sreenath H., Song J., Sussman M.R., Thao S., Troestler D., Tyler E., Tyler R., Ulrich E., Vinarov D., Vojtik F., Volkman B.F., Wesenberg G., Wrobel R.L., Zhang J., Zhao Q., Zolnai Z. Proteins 61:206-208(2005) [PubMed: 16080145] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FMN.
[13]	"Ensemble refinement of protein crystal structures: validation and application." Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr. Structure 15:1040-1052(2007) [PubMed: 17850744] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FMN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y10617 mRNA. Translation: CAA71627.1.
U92460 Genomic DNA. Translation: AAC78440.1.
AC010718 Genomic DNA. Translation: AAF04448.1.
CP002684 Genomic DNA. Translation: AEE35875.1.
AY074874 mRNA. Translation: AAL75894.1.
BT020365 mRNA. Translation: AAV85720.1.
AY087801 mRNA. Translation: AAM65337.1.

IPI

IPI00548191.

PIR

B96795.

RefSeq

NP_177794.1. NM_106318.3.

UniGene

At.11155.
At.67448.
At.73001.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q8LAH7.

SMR

Q8LAH7. Positions 9-369.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8LAH7. 1 interaction.

STRING

Q8LAH7.

Proteomic databases

PRIDE

Q8LAH7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT1G76680.1; AT1G76680.1; AT1G76680.

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.

Phylogenomic databases

eggNOG

KOG0134.

GeneTree

EPGT00050000000754.

HOGENOM

HBG583461.

InParanoid

Q8LAH7.

PhylomeDB

Q8LAH7.

ProtClustDB

CLSN2682783.

Gene expression databases

Genevestigator

Q8LAH7.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

KO

K05894.

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:	November 16, 2011
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program