ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8LAH7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name OPR1_ARATH
Primary accession number Q8LAH7
Secondary accession numbers O49259 Q9S806
Integrated into Swiss-Prot on April 26, 2005
Sequence was last modified on April 26, 2005 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 49)
Name and origin of the protein
Protein name 12-oxophytodienoate reductase 1
Synonyms EC 1.3.1.42
12-oxophytodienoate-10,11-reductase 1
OPDA-reductase 1
AtOPR1
FS-AT-I
Gene name
Name: OPR1
OrderedLocusNames: At1g76680
ORFNames: F28O16.5
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
STRAIN=cv. Columbia;
DOI=10.1074/jbc.272.44.28066; PubMed=9346960 [NCBI, ExPASy, EBI, Israel, Japan]
Schaller F., Weiler E.W.;
"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.";
J. Biol. Chem. 272:28066-28072(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1007/s004250050545; PubMed=10333582 [NCBI, ExPASy, EBI, Israel, Japan]
Biesgen C., Weiler E.W.;
"Structure and regulation of OPR1 and OPR2, two closely related genes encoding 12-oxophytodienoic acid-10,11-reductases from Arabidopsis thaliana.";
Planta 208:155-165(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
SUBSTRATE SPECIFICITY.
DOI=10.1007/s004250050706; PubMed=10872231 [NCBI, ExPASy, EBI, Israel, Japan]
Schaller F., Biesgen C., Muessig C., Altmann T., Weiler E.W.;
"12-Oxophytodienoate reductase 3 (OPR3) is the isoenzyme involved in jasmonate biosynthesis.";
Planta 210:979-984(2000).
[8]
INDUCTION.
DOI=10.1023/A:1012211011538; PubMed=11725945 [NCBI, ExPASy, EBI, Israel, Japan]
He Y., Gan S.;
"Identical promoter elements are involved in regulation of the OPR1 gene by senescence and jasmonic acid in Arabidopsis.";
Plant Mol. Biol. 47:595-605(2001).
[9]
SUBCELLULAR LOCATION.
PubMed=12445129 [NCBI, ExPASy, EBI, Israel, Japan]
Strassner J., Schaller F., Frick U.B., Howe G.A., Weiler E.W., Amrhein N., Macheroux P., Schaller A.;
"Characterization and cDNA-microarray expression analysis of 12-oxophytodienoate reductases reveals differential roles for octadecanoid biosynthesis in the local versus the systemic wound response.";
Plant J. 32:585-601(2002).
[10]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FMN.
Wesenberg G.E., Smith D.W., Phillips G.N. Jr., Johnson K.A., Bingman C.A.;
"X-ray structure of gene product from Arabidopsis thaliana At1g76680.";
Submitted (MAR-2004) to the PDB data bank.
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.
  • PATHWAY: Lipid metabolism; oxylipin biosynthesis.
  • SUBCELLULAR LOCATION: Cytoplasm.
  • ALTERNATIVE PRODUCTS: 1 named isoform [FASTA] produced by alternative splicing. A number of isoforms are produced. According to EST sequences.
    Name1
    Isoform IDQ8LAH7-1
    This is the isoform sequence displayed in this entry.
  • 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.
  • 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.
  • SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y10617; CAA71627.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U92460; AAC78440.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC010718; AAF04448.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY074874; AAL75894.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT020365; AAV85720.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY087801; AAM65337.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B96795; B96795.
RefSeq NP_177794.1; -.
UniGene At.11155
3D structure databases
PDB
1VJI; X-ray; 2.00 A; A=1-372.[ExPASy / RCSB / EBI]
2Q3R; X-ray; 2.00 A; A=1-372.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1VJI; -.
2Q3R; -.
ModBase Q8LAH7.
Organism-specific databases
GeneFarm 4901; 471.
TAIR At1g76680; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0016629; Molecular function: 12-oxophytodienoate reductase activity (inferred from electronic annotation from EC).
GO:0010181; Molecular function: FMN binding (inferred from electronic annotation from InterPro).
GO:0009695; Biological process: jasmonic acid biosynthetic process (traceable author statement from TAIR).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0046686; Biological process: response to cadmium ion (inferred from expression pattern from TAIR).
GO:0009751; Biological process: response to salicylic acid stimulus (inferred from expression pattern from TAIR).
QuickGo view.
Family and domain databases
InterPro IPR013785; Aldolase_TIM.
IPR001155; OxRdtase_FMN_N.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF00724; Oxidored_FMN; 1.
Pfam graphical view of domain structure.
Proteomics databases
PRIDE Q8LAH7; -.
Genome annotation databases
GeneID 844001; -.
GenomeReviews CT485782_GR; AT1G76680.
KEGG ath:AT1G76680; -.
NMPDR fig|3702.1.peg.7194; -.
Other
ProtoNet Q8LAH7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Fatty acid biosynthesis; Flavoprotein; FMN; Lipid synthesis; NADP; Oxidoreductase; Oxylipin biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   372  372     12-oxophytodienoate reductase 1. PRO_0000194483
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). 
ACT_SITE   188   188        Proton donor (By similarity). 
BINDING   33    33        FMN. 
BINDING   106   106        FMN. 
BINDING   235   235        FMN. 
BINDING   327   327        FMN. 
CONFLICT   43    44        Missing (in Ref. 1; CAA71627). 
CONFLICT   184   184        G -> R (in Ref. 6; AAM65337). 
HELIX   11    13  3      
STRAND   16    18  3      
STRAND   21    24  4      
STRAND   26    29  4      
HELIX   38    40  3      
HELIX   44    52  9      
STRAND   59    61  3      
STRAND   65    68  4      
HELIX   83    98  16      
STRAND   102   108  7      
HELIX   116   118  3      
HELIX   120   122  3      
STRAND   126   129  4      
STRAND   140   147  8      
HELIX   155   157  3      
HELIX   159   175  17      
STRAND   178   184  7      
HELIX   189   194  6      
TURN   196   198  3      
STRAND   206   208  3      
HELIX   209   227  19      
HELIX   229   231  3      
STRAND   232   236  5      
TURN   242   244  3      
HELIX   250   260  11      
TURN   261   265  5      
STRAND   267   272  6      
HELIX   289   295  7      
STRAND   298   305  8      
HELIX   308   316  9      
STRAND   321   326  6      
HELIX   327   331  5      
HELIX   335   341  7      
HELIX   350   352  3      
TURN   360   362  3      
Sequence information
Length: 372 AA [This is the length of the unprocessed precursor] Molecular weight: 41168 Da [This is the MW of the unprocessed precursor] CRC64: 213C8C850FF691CB [This is a checksum on the sequence]
        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 

Q8LAH7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!