C5H429 · DBR2_ARTAN
- ProteinArtemisinic aldehyde Delta(11(13)) reductase
- GeneDBR2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids388 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- (11R)-dihydroartemisinic aldehyde + NADP+ = +-artemisinic aldehyde + H+ + NADPHThis reaction proceeds in the backward direction.
Cofactor
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).
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 μM | artemisinic aldehyde | |||||
790 μM | 2-cyclohexen-1-one | |||||
650 μM | +-carvone | |||||
95 μM | NADPH | |||||
770 μM | NADH |
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 27-29 | FMN (UniProtKB | ChEBI) | ||||
Sequence: PMT | ||||||
Binding site | 60 | FMN (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 102 | FMN (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 181 | FMN (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 181-184 | substrate | ||||
Sequence: HGAH | ||||||
Active site | 186 | Proton donor | ||||
Sequence: Y | ||||||
Binding site | 233 | FMN (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 279 | substrate | ||||
Sequence: R | ||||||
Binding site | 317-319 | FMN (UniProtKB | ChEBI) | ||||
Sequence: CGG | ||||||
Binding site | 340-341 | FMN (UniProtKB | ChEBI) | ||||
Sequence: GR | ||||||
Binding site | 368 | substrate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | peroxisome | |
Molecular Function | 12-oxophytodienoate reductase activity | |
Molecular Function | FMN binding | |
Molecular Function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor | |
Biological Process | jasmonic acid biosynthetic process | |
Biological Process | oxylipin biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameArtemisinic aldehyde Delta(11(13)) reductase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > campanulids > Asterales > Asteraceae > Asteroideae > Anthemideae > Artemisiinae > Artemisia
Accessions
- Primary accessionC5H429
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000419682 | 1-388 | Artemisinic aldehyde Delta(1113) reductase | |||
Sequence: MSENPPTLFSAYKMGNFNLSHRVVLAPMTRCRAINAIPNEALVEYYRQRSTAGGFLITEGTMISPSSAGFPHVPGIFTKEQVEGWKKVVDAAHKEGAVIFCQLWHVGRASHQVYQPGGAAPISSTSKPISKKWEILLPDATYGTYPEPRPLAANEILEVVEDYRVAAINAIEAGFDGIEIHGAHGYLLDQFMKDGINDRTDEYGGSLENRCKFILQVVQAVSAAIATDRVLIRISPAIDHTDAMDSDPRSLGLAVIERLNKLQFKLGSRLAYLHVTQPRYTADGHGQTEAGANGSEEEVAQLMKTWRGAYVGTFICCGGYTRELGLQAVAQGDADLVAFGRYFVSNPDLVLRLKLNAPLNRYDRATFYTHDPVVGYTDYPSLDKGSLL |
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).
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
Structure
Sequence
- Sequence statusComplete
- Length388
- Mass (Da)42,585
- Last updated2019-09-18 v2
- Checksum1FA441BEA42027EE
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 4-5 | in Ref. 1; ACH61780 and 2; AGL34708/AGO50599/AGO50600 | ||||
Sequence: NP → K | ||||||
Sequence conflict | 16 | in Ref. 1; ACH61780 | ||||
Sequence: N → K | ||||||
Sequence conflict | 112 | in Ref. 2; AGL34708/AGO50600 | ||||
Sequence: Q → K | ||||||
Sequence conflict | 137 | in Ref. 2; AGL34708 | ||||
Sequence: L → M | ||||||
Sequence conflict | 226 | in Ref. 2; AGO50600 | ||||
Sequence: A → G | ||||||
Sequence conflict | 226 | in Ref. 1; ACH61780 and 2; AGO50599/AGL34708 | ||||
Sequence: A → T | ||||||
Sequence conflict | 231 | in Ref. 2; AGO50600 | ||||
Sequence: L → G | ||||||
Sequence conflict | 231 | in Ref. 1; ACH61780 and 2; AGO50599/AGL34708 | ||||
Sequence: L → I | ||||||
Sequence conflict | 295 | in Ref. 2; AGO50600 | ||||
Sequence: S → SDH | ||||||
Sequence conflict | 344 | in Ref. 2; AGO50600 | ||||
Sequence: V → I | ||||||
Sequence conflict | 384 | in Ref. 2; AGO50600 | ||||
Sequence: K → Q |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |