Reviewed, UniProtKB/Swiss-Prot Q8GYB8 (OPR2_ARATH)

Names and origin

Protein names

Recommended name:
    12-oxophytodienoate reductase 2
    EC=1.3.1.42
Alternative name(s):
    12-oxophytodienoate-10,11-reductase 2
      Short name=OPDA-reductase 2
      Short name=AtOPR2

Gene names

Name:	OPR2
Ordered Locus Names:	At1g76690
ORF Names:	F28O16.6

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	374 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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.
Cofactor	FMN By similarity.
Pathway	Lipid metabolism; oxylipin biosynthesis.
Subcellular location	Cytoplasm. Ref.5
Tissue specificity	Expressed at highest levels in roots and cotyledons, and at lower levels in leaves, shoots and flowers (sepals, petals, maturing siliques and developing pollen). Ref.1
Developmental stage	Expressed during late steps of pollen development. Ref.1
Induction	By wounding, locally and systemically, by cold and heat stresses, and by UV-C. Seems to not be influenced by UV-A and UV-B. Ref.1
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
Ligand	FMN Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	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 wounding Ref.1 Inferred from expression pattern. Source: TAIR
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 – 374	374	12-oxophytodienoate reductase 2		PRO_0000194484
Regions
	Region	135 – 149	15	Substrate-binding loop By similarity
	Region	140 – 141	2	Substrate-binding By similarity
	Region	185 – 188	4	Substrate-binding By similarity
Sites
	Active site	190	1	Proton donor By similarity
	Binding site	35	1	FMN By similarity
	Binding site	108	1	FMN By similarity
	Binding site	237	1	FMN By similarity
	Binding site	329	1	FMN By similarity
Experimental info
	Sequence conflict	174	1	A → T in BAC42387. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8GYB8-1 [UniParc]. Last modified April 26, 2005. Version 2. Checksum: 3168EDF4E857A883	FASTA	374	41,567
	10 20 30 40 50 60 MEMVNAEAKQ SVPLLTPYKM GRFNLSHRVV LAPLTRQKSY GSVPQPHAIL YYSQRTSPGG 70 80 90 100 110 120 FLIAEATGVS DTAQGYPDTP GIWTKEHVEA WKPIVDAVHA KGGIFFCQIW HVGRVSNRGF 130 140 150 160 170 180 QPRRQAPISC TGKPIMPQMR ANGIDEARFT PPRRLSIEEI PGIVNDFRLA ARNAMEAGFD 190 200 210 220 230 240 GVEIHGAHGY LIDQFMKDKV NDRTDEYGGS LQNRCKFALE VVDAVAKEIG PDRVGIRLSP 250 260 270 280 290 300 FADYMESGDT NPEALGLYMV ESLNKYGILY CHMIEPRMKT VGEIAACSHT LMPMREAFKG 310 320 330 340 350 360 TFISAGGFTR EDGNEAVAKG RTDLVAYGRW FLANPDLPKR FQLDAPLNKY NRSTFYTSDP 370 VVGYTDYPSL ESTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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, DEVELOPMENTAL STAGE, INDUCTION. Strain: cv. Columbia.
[2]	"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.
[3]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"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.
[5]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U92460 Genomic DNA. Translation: AAC78441.1. AC010718 Genomic DNA. Translation: AAF04449.1. AK117738 mRNA. Translation: BAC42387.1.
IPI	IPI00542803.
PIR	C96795.
RefSeq	NP_177795.1.
UniGene	At.48382
3D structure databases
HSSP	HSSP built from PDB template 1ICP based on UniProtKB Q9XG54.
SMR	Q8GYB8. Positions 11-371.
ModBase	Search...
Proteomic databases
PRIDE	Q8GYB8.
Genome annotation databases
GeneID	844002.
GenomeReviews	Gene locus AT1G76690 in contig CT485782_GR.
KEGG	ath:AT1G76690.
NMPDR	fig|3702.1.peg.7196.
Organism-specific databases
GeneFarm	4902. 471.
TAIR	At1g76690.
Phylogenomic databases
OMA	Q8GYB8. RISPSGE.
Enzyme and pathway databases
BRENDA	1.3.1.42. 302.
Gene expression databases
GermOnline	AT1G76690. Arabidopsis thaliana.
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

OPR2_ARATH

Accession

Primary (citable) accession number: Q8GYB8
Secondary accession number(s): Q9ZR80

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	April 26, 2005
Last modified:	June 16, 2009
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)