C5H429 · DBR2_ARTAN

Function

function

Involved in the biosynthesis of the antimalarial endoperoxide artemisinin (PubMed:18495659, PubMed:27488942).
Catalyzes the double bond reduction of artemisinic aldehyde to produce (11R)-dihydroartemisinic aldehyde (PubMed:18495659).
Also able to reduce 2-cyclohexen-1-one into cyclohexanone to a lesser extent (PubMed:18495659).

Catalytic activity

Cofactor

FMN (UniProtKB | Rhea| CHEBI:58210 )

Biotechnology

Artemisinin and derivatives (e.g. artesunate), are antimalarial drugs due to their endoperoxidase properties; they also display multiple pharmacological actions against inflammation,viral infections, and cell and tumor proliferation (PubMed:32405226, PubMed:32514287).
Artesunate may be a promising treatment for COVID-19 mediated by the severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) because of its anti-inflammatory activity, NF-kappaB (nuclear factor kappa B)-coronavirus effect and chloroquine-like endocytosis inhibition mechanism (PubMed:32405226, PubMed:32514287).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
19 μMartemisinic aldehyde
790 μM2-cyclohexen-1-one
650 μM+-carvone
95 μMNADPH
770 μMNADH
kcat is 2.6 sec-1 with artemisinic aldehyde as substrate. kcat is 1.8 sec-1 with 2-cyclohexen-1-one as substrate. kcat is 0.86 sec-1 with +-carvone as substrate. kcat is 1.3 sec-1 for the NADH-dependent reduction of artemisinic aldehyde.

pH Dependence

Optimum pH is 7.5.

Pathway

Sesquiterpene biosynthesis.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site27-29FMN (UniProtKB | ChEBI)
Binding site60FMN (UniProtKB | ChEBI)
Binding site102FMN (UniProtKB | ChEBI)
Binding site181FMN (UniProtKB | ChEBI)
Binding site181-184substrate
Active site186Proton donor
Binding site233FMN (UniProtKB | ChEBI)
Binding site279substrate
Binding site317-319FMN (UniProtKB | ChEBI)
Binding site340-341FMN (UniProtKB | ChEBI)
Binding site368substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentperoxisome
Molecular Function12-oxophytodienoate reductase activity
Molecular FunctionFMN binding
Molecular Functionoxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
Biological Processjasmonic acid biosynthetic process
Biological Processoxylipin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Artemisinic aldehyde Delta(11(13)) reductase
  • EC number

Gene names

    • Name
      DBR2
    • Synonyms
      AAR

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Huhao1
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > campanulids > Asterales > Asteraceae > Asteroideae > Anthemideae > Artemisiinae > Artemisia

Accessions

  • Primary accession
    C5H429
  • Secondary accessions
    • A0A2U1QC65
    • R4N2K9
    • S4V8I4
    • S4VAQ7

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004196821-388Artemisinic aldehyde Delta(1113) reductase

Expression

Tissue specificity

Expression at relatively high level in glandular trichomes, and at lower level in leaves and flower buds (PubMed:18495659).
Weakly expressed in roots (PubMed:18495659).
Expressed both in apical and sub-apical cells of glandular secretory trichomes (PubMed:19664791, PubMed:22195571).
Also present in non-glandular trichome cells (PubMed:30851440).

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif386-388Microbody targeting signal

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    388
  • Mass (Da)
    42,585
  • Last updated
    2019-09-18 v2
  • Checksum
    1FA441BEA42027EE
MSENPPTLFSAYKMGNFNLSHRVVLAPMTRCRAINAIPNEALVEYYRQRSTAGGFLITEGTMISPSSAGFPHVPGIFTKEQVEGWKKVVDAAHKEGAVIFCQLWHVGRASHQVYQPGGAAPISSTSKPISKKWEILLPDATYGTYPEPRPLAANEILEVVEDYRVAAINAIEAGFDGIEIHGAHGYLLDQFMKDGINDRTDEYGGSLENRCKFILQVVQAVSAAIATDRVLIRISPAIDHTDAMDSDPRSLGLAVIERLNKLQFKLGSRLAYLHVTQPRYTADGHGQTEAGANGSEEEVAQLMKTWRGAYVGTFICCGGYTRELGLQAVAQGDADLVAFGRYFVSNPDLVLRLKLNAPLNRYDRATFYTHDPVVGYTDYPSLDKGSLL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict4-5in Ref. 1; ACH61780 and 2; AGL34708/AGO50599/AGO50600
Sequence conflict16in Ref. 1; ACH61780
Sequence conflict112in Ref. 2; AGL34708/AGO50600
Sequence conflict137in Ref. 2; AGL34708
Sequence conflict226in Ref. 2; AGO50600
Sequence conflict226in Ref. 1; ACH61780 and 2; AGO50599/AGL34708
Sequence conflict231in Ref. 2; AGO50600
Sequence conflict231in Ref. 1; ACH61780 and 2; AGO50599/AGL34708
Sequence conflict295in Ref. 2; AGO50600
Sequence conflict344in Ref. 2; AGO50600
Sequence conflict384in Ref. 2; AGO50600

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EU704257
EMBL· GenBank· DDBJ
ACH61780.1
EMBL· GenBank· DDBJ
mRNA
JX898526
EMBL· GenBank· DDBJ
AGO50599.1
EMBL· GenBank· DDBJ
mRNA
JX898527
EMBL· GenBank· DDBJ
AGO50600.1
EMBL· GenBank· DDBJ
mRNA
KC505370
EMBL· GenBank· DDBJ
AGL34708.1
EMBL· GenBank· DDBJ
mRNA
PKPP01000231
EMBL· GenBank· DDBJ
PWA95606.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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