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Entry version 34 (23 Feb 2022)
Sequence version 2 (18 Sep 2019)
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Protein

Artemisinic aldehyde Delta(11(13)) reductase

Gene

DBR2

Organism
Artemisia annua (Sweet wormwood)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).

1 Publication1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FMNBy similarity

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

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.1 Publication
  1. KM=19 µM for artemisinic aldehyde1 Publication
  2. KM=790 µM for 2-cyclohexen-1-one1 Publication
  3. KM=650 µM for (+)-carvone1 Publication
  4. KM=95 µM for NADPH1 Publication
  5. KM=770 µM for NADH1 Publication

pH dependencei

Optimum pH is 7.5.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Sesquiterpene biosynthesis

This protein is involved in Sesquiterpene biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in Sesquiterpene biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei60FMN; via amide nitrogenCombined sources1 Publication1
Binding sitei102FMNCombined sources1 Publication1
Binding sitei181FMNCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei186Proton donorBy similarity1
Binding sitei233FMNCombined sources1 Publication1
Binding sitei279Substrate; via amide nitrogenCombined sources1 Publication1
Binding sitei368SubstrateCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi27 – 29FMNCombined sources1 Publication3
Nucleotide bindingi317 – 319FMNCombined sources1 Publication3
Nucleotide bindingi340 – 341FMNCombined sources1 Publication2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
LigandFlavoprotein, FMN, NADP

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.3.1.92, 7150

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Artemisinic aldehyde Delta(11(13)) reductase1 Publication (EC:1.3.1.921 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:DBR22 Publications
Synonyms:AAR1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiArtemisia annua (Sweet wormwood)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri35608 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeAnthemideaeArtemisiinaeArtemisia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000245207 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unassembled WGS sequence

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

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:32514287, PubMed:32405226). 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:32514287, PubMed:32405226).2 Publications

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004196821 – 388Artemisinic aldehyde Delta(11(13)) reductaseAdd BLAST388

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
C5H429

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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:22195571, PubMed:19664791). Also present in non-glandular trichome cells (PubMed:30851440).4 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
35608.C5H429

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1388
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
C5H429

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni181 – 184Substrate-bindingCombined sources1 Publication4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi386 – 388Microbody targeting signalSequence analysis3

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013785, Aldolase_TIM
IPR001155, OxRdtase_FMN_N
IPR045247, Oye-like

The PANTHER Classification System

More...
PANTHERi
PTHR22893, PTHR22893, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00724, Oxidored_FMN, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

C5H429-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSENPPTLFS AYKMGNFNLS HRVVLAPMTR CRAINAIPNE ALVEYYRQRS
60 70 80 90 100
TAGGFLITEG TMISPSSAGF PHVPGIFTKE QVEGWKKVVD AAHKEGAVIF
110 120 130 140 150
CQLWHVGRAS HQVYQPGGAA PISSTSKPIS KKWEILLPDA TYGTYPEPRP
160 170 180 190 200
LAANEILEVV EDYRVAAINA IEAGFDGIEI HGAHGYLLDQ FMKDGINDRT
210 220 230 240 250
DEYGGSLENR CKFILQVVQA VSAAIATDRV LIRISPAIDH TDAMDSDPRS
260 270 280 290 300
LGLAVIERLN KLQFKLGSRL AYLHVTQPRY TADGHGQTEA GANGSEEEVA
310 320 330 340 350
QLMKTWRGAY VGTFICCGGY TRELGLQAVA QGDADLVAFG RYFVSNPDLV
360 370 380
LRLKLNAPLN RYDRATFYTH DPVVGYTDYP SLDKGSLL
Length:388
Mass (Da):42,585
Last modified:September 18, 2019 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1FA441BEA42027EE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti4 – 5NP → K in ACH61780 (PubMed:18495659).Curated2
Sequence conflicti4 – 5NP → K in AGL34708 (PubMed:23638869).Curated2
Sequence conflicti4 – 5NP → K in AGO50599 (PubMed:23638869).Curated2
Sequence conflicti4 – 5NP → K in AGO50600 (PubMed:23638869).Curated2
Sequence conflicti16N → K in ACH61780 (PubMed:18495659).Curated1
Sequence conflicti112Q → K in AGL34708 (PubMed:23638869).Curated1
Sequence conflicti112Q → K in AGO50600 (PubMed:23638869).Curated1
Sequence conflicti137L → M in AGL34708 (PubMed:23638869).Curated1
Sequence conflicti226A → G in AGO50600 (PubMed:23638869).Curated1
Sequence conflicti226A → T in ACH61780 (PubMed:18495659).Curated1
Sequence conflicti226A → T in AGO50599 (PubMed:23638869).Curated1
Sequence conflicti226A → T in AGL34708 (PubMed:23638869).Curated1
Sequence conflicti231L → G in AGO50600 (PubMed:23638869).Curated1
Sequence conflicti231L → I in ACH61780 (PubMed:18495659).Curated1
Sequence conflicti231L → I in AGO50599 (PubMed:23638869).Curated1
Sequence conflicti231L → I in AGL34708 (PubMed:23638869).Curated1
Sequence conflicti295S → SDH in AGO50600 (PubMed:23638869).Curated1
Sequence conflicti344V → I in AGO50600 (PubMed:23638869).Curated1
Sequence conflicti384K → Q in AGO50600 (PubMed:23638869).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
EU704257 mRNA Translation: ACH61780.1
JX898526 mRNA Translation: AGO50599.1
JX898527 mRNA Translation: AGO50600.1
KC505370 mRNA Translation: AGL34708.1
PKPP01000231 Genomic DNA Translation: PWA95606.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:ACH61780

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU704257 mRNA Translation: ACH61780.1
JX898526 mRNA Translation: AGO50599.1
JX898527 mRNA Translation: AGO50600.1
KC505370 mRNA Translation: AGL34708.1
PKPP01000231 Genomic DNA Translation: PWA95606.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5DXXX-ray1.45A1-388[»]
5DXYX-ray1.77A1-388[»]
5DY2X-ray1.57A1-388[»]
5DY3X-ray1.82A1-388[»]
SMRiC5H429
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi35608.C5H429

Proteomic databases

PRIDEiC5H429

Genome annotation databases

KEGGiag:ACH61780

Enzyme and pathway databases

BRENDAi1.3.1.92, 7150

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785, Aldolase_TIM
IPR001155, OxRdtase_FMN_N
IPR045247, Oye-like
PANTHERiPTHR22893, PTHR22893, 1 hit
PfamiView protein in Pfam
PF00724, Oxidored_FMN, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDBR2_ARTAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: C5H429
Secondary accession number(s): A0A2U1QC65
, R4N2K9, S4V8I4, S4VAQ7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: September 18, 2019
Last modified: February 23, 2022
This is version 34 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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