B9FSC8 · OPR11_ORYSJ

Function

function

Putative oxophytodienoate reductase that may be involved in the biosynthesis or metabolism of oxylipin signaling molecules.

Cofactor

FMN (UniProtKB | Rhea| CHEBI:58210 )

Features

Showing features for binding site, active site.

136750100150200250300350
TypeIDPosition(s)Description
Binding site26-28FMN (UniProtKB | ChEBI)
Binding site59FMN (UniProtKB | ChEBI)
Binding site101FMN (UniProtKB | ChEBI)
Binding site178-181substrate
Active site183Proton donor
Binding site230FMN (UniProtKB | ChEBI)
Binding site270substrate
Binding site300FMN (UniProtKB | ChEBI)
Binding site321-322FMN (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular FunctionFMN binding
Molecular Functionoxidoreductase activity
Biological Processfatty acid biosynthetic process
Biological Processoxylipin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Putative 12-oxophytodienoate reductase 11
  • EC number
  • Alternative names
    • OPDA-reductase 11 (OsOPR11)

Gene names

    • Name
      OPR11
    • Synonyms
      OPR3
    • ORF names
      OsJ_20711

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Nipponbare
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa

Accessions

  • Primary accession
    B9FSC8

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00004107171-367UniProtPutative 12-oxophytodienoate reductase 11
Modified residue (large scale data)203PTMeXchangePhosphoserine

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    367
  • Mass (Da)
    40,643
  • Last updated
    2009-03-24 v1
  • Checksum
    9D5A967949FFA26F
MSSTAPLLTPYKMGRFDLSHRVVLAPLTRQRSYGNVPQPHAILYYQQRTTKGGLLIAEATGISDTAQGYKDTPGIWTKEQVEAWKPIVDGVHAKGGIFFCQIWHVGRVSNNTFQPNGQAPISSTNKSLKPAVRANGIDVATFSTPRRLETDEIPFVVNDYRVAARNAIEAGFDGVEIHGAHGYLIDQFLKDQVNDRSDKYGGSLENRCRFALEVVQAVTDEIGADKVGIRLSPFASYSEAADSNPEALGLYMANALNKFGILYCHMVEPRMVKLGEKFETPHSLRPIRDAFKGTFIAAGGYNKEDGNKAVSTGYTDLVAYGRLFLSNPDLPERFEIDAPLNKYNRETFYISDPVIGYTDYPFLPSDV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP008212
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AP014962
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CM000143
EMBL· GenBank· DDBJ
EEE65389.1
EMBL· GenBank· DDBJ
Genomic DNA
AK102440
EMBL· GenBank· DDBJ
-mRNA No translation available.

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp