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UniProtKB - Q39172 (AER_ARATH)

Entry version 147 (23 Feb 2022)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
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Protein

NADPH-dependent oxidoreductase 2-alkenal reductase

Gene

AER

Organism
Arabidopsis thaliana (Mouse-ear cress)
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 detoxification of reactive carbonyls (PubMed:10848984, PubMed:12514241, PubMed:16299173).

Acts on lipid peroxide-derived reactive aldehydes (PubMed:12514241).

Specific to a double bond activated by an adjacent carbonyl group (PubMed:12514241).

Can use both quinones and diamide as substrates, but not menadione, ferricyanide or phylloquinone (PubMed:10848984).

Can use 4-hydroxy-(2E)-nonenal (HNE), 4-hydroxy-(2E)-hexenal (HHE), (2E)-nonenal, (2E)-hexenal, (2E)-pentenal, propenal (acrolein), 3-buten-2-one and 3-penten-2-one, but not (R)---carvone, n-nonanal, n-hexanal, (3Z)-hexanal, cyclohex-2-en-1-one or 12-oxo phytodienoic acid (OPDA) as electron acceptors (PubMed:12514241).

Catalyzes the reduction of the alpha,beta-unsaturated bond of 2-alkenals, of lipid peroxide-derived oxenes 9-oxo-10(E),12(Z)-octadecadienoic acid (9-KODE) and 13-oxo-9(Z),11(E)-octadecadienoic acid (13-KODE), as well as 4-oxo-(2E)-nonenal and 4-hydroxynonenal (PubMed:16299173).

Can use 12-oxo-10(E) dodecanoate (traumatin), trans-1,3 diphenyl-2-propenone, trans-1,4-diphenyl-2-butene-1,4-dione, 9-oxo-12,13-epoxy-(10E)-octadecenoic acid (trans-EKODE-1b) and 9,13-dihydroxy-10-oxo-11-octadecenoic acid as substrates (PubMed:26678323).

Catalyzes the reduction of the 7-8 double bond of phenylpropanal substrates, such as p-coumaryl aldehyde and coniferyl aldehyde (in vitro) (PubMed:17028190).

Has activity towards toxic substrates, such as 4-hydroxy-(2E)-nonenal (in vitro) (PubMed:17028190).

May play a distinct role in plant antioxidant defense and is possibly involved in NAD(P)/NAD(P)H homeostasis (PubMed:17028190).

5 Publications

<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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by N-ethylmaleimide and p-chloromercuribenzoic acid.1 Publication

<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 3.8 sec(-1) for trans-1,3 diphenyl-2-propenone. kcat is 4.9 sec(-1) for trans-1,4-diphenyl-2-butene-1,4-dione. kcat is 10 sec(-1) for traumatin (PubMed:26678323). kcat is 98 sec(-1) for 9,10-phenanthrenequinone. kcat is 1.9 sec(-1) for 5-Hydroxy-1,4-naphtoquinone. kcat is 12 sec(-1) for 1,4-Benzoquinone. kcat is 0.10 sec(-1) for decyl-plastoquinone. kcat is 0.03 sec(-1) for ferricytochrome c. kcat is 95 sec(-1) for azodicarboxylic acid bis[dimethylamide]. kcat is 42 sec(-1) for 1,10-(azocarbonyl)-dipeperidine. kcat is 31 sec(-1) for azocarbonamide (PubMed:10848984). kcat is 88 sec(-1) for 4-hydroxy-(2E)-nonenal. kcat is 42 sec(-1) for 4-hydroxy-(2E)-hexenal. kcat is 51 sec(-1) for (2E)-nonenal. kcat is 63 sec(-1) for (2E)-hexenal. kcat is 35 sec(-1) for (2E)-pentenal. kcat is 40 sec(-1) for propenal. kcat is 83 sec(-1) for 3-buten-2-one. kcat is 103 sec(-1) for 3-penten-2-one (PubMed:12514241). kcat is 33.9 sec(-1) for (2E),(6Z)-nonadienal. kcat is 20.1 sec(-1) for 4-oxo-(2E)-nonenal. kcat is 0.94 sec(-1) for 9-oxo-10(E),12(Z)-octadecadienoic acid. kcat is 1.10 sec(-1) for 13-oxo-9(Z),11(E)-octadecadienoic acid. kcat is 18.9 sec(-1) for 3-nonen-2-one (PubMed:16299173).4 Publications
  1. KM=0.53 mM for p-coumaryl aldehyde1 Publication
  2. KM=0.41 mM for coniferyl aldehyde1 Publication
  3. KM=0.28 mM for 4-hydroxy-(2E)-nonenal1 Publication
  4. KM=10 µM for trans-1,3 diphenyl-2-propenone1 Publication
  5. KM=3.7 µM for trans-1,4-diphenyl-2-butene-1,4-dione1 Publication
  6. KM=6.6 µM for traumatin1 Publication
  7. KM=0.65 µM for 9,10-phenanthrenequinone1 Publication
  8. KM=11 µM for 5-Hydroxy-1,4-naphtoquinone1 Publication
  9. KM=152 µM for 1,4-Benzoquinone1 Publication
  10. KM=25 µM for decyl-plastoquinone1 Publication
  11. KM=20 µM for ferricytochrome c1 Publication
  12. KM=128 µM for azodicarboxylic acid bis[dimethylamide]1 Publication
  13. KM=120 µM for 1,10-(azocarbonyl)-dipeperidine1 Publication
  14. KM=3.4 µM for azocarbonamide1 Publication
  15. KM=2.5 µM for NADPH for 9,10-phenanthrenequinone-reduction1 Publication
  16. KM=8.2 µM for NADPH for azodicarboxylic acid bis[dimethylamide]-reduction1 Publication
  17. KM=13.4 µM for 4-hydroxy-(2E)-nonenal1 Publication
  18. KM=145 µM for 4-hydroxy-(2E)-hexenal1 Publication
  19. KM=5.9 µM for (2E)-nonenal1 Publication
  20. KM=232 µM for (2E)-hexenal1 Publication
  21. KM=1420 µM for (2E)-pentenal1 Publication
  22. KM=4650 µM for propenal1 Publication
  23. KM=55 µM for 3-buten-2-one1 Publication
  24. KM=5.2 µM for 3-penten-2-one1 Publication
  25. KM=11.3 µM for (2E),(6Z)-nonadienal1 Publication
  26. KM=1.24 µM for 4-oxo-(2E)-nonenal1 Publication
  27. KM=10.0 µM for 9-oxo-10(E),12(Z)-octadecadienoic acid1 Publication
  28. KM=3.92 µM for 13-oxo-9(Z),11(E)-octadecadienoic acid1 Publication
  29. KM=0.673 µM for 3-nonen-2-one1 Publication

pH dependencei

Optimum pH is 8.0 for 9,10-phenanthrenequinone-reduction. Optimum pH is 6.5-7.0 for azodicarboxylic acid bis[dimethylamide]-reduction (PubMed:10848984). Optimum pH is 6.0 with (2E)-hexenal or 4-hydroxy-(2E)-nonenal as substrate (PubMed:12514241).2 Publications

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 sitei53SubstrateCombined sources1
Binding sitei188NADP; via amide nitrogenCombined sources1
Binding sitei192NADPCombined sources1
Binding sitei208NADPCombined sources1
Binding sitei232NADP; via carbonyl oxygenCombined sources1
Binding sitei254NADPCombined sources1
Binding sitei260NADPCombined sources1
Binding sitei260SubstrateCombined sources1
Binding sitei330NADP; via carbonyl oxygenCombined sources1

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 bindingi52 – 53NADPCombined sources2
Nucleotide bindingi163 – 169NADPCombined sources7
Nucleotide bindingi284 – 286NADPCombined sources3
Nucleotide bindingi334 – 336NADPCombined sources3

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

  • response to oxidative stress Source: TAIR
Complete GO annotation on QuickGO ...

<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
LigandNADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		ARA:AT5G16970-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q39172

<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:
NADPH-dependent oxidoreductase 2-alkenal reductase1 Publication (EC:1.3.1.-1 Publication, EC:1.3.1.744 Publications)
Short name:
AtAER1 Publication
Alternative name(s):
NADP-dependent alkenal double bond reductase P11 Publication
Short name:
DBR11 Publication
NADPH-azodicarbonyl/quinone reductase1 Publication
NADPH:2-alkenal/one alpha,beta-hydrogenase1 Publication
Short name:
ALH1 Publication
P1-zeta-crystallin protein1 Publication
Short name:
P1-ZCr1 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:AER1 Publication
Synonyms:P11 Publication
Ordered Locus Names:At5g16970Imported
ORF Names:F2K13_120Imported
<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>OrganismiArabidopsis thaliana (Mouse-ear cress)
<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 identifieri3702 [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 lineageiEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis
<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
  • UP000006548 <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: Chromosome 5

Organism-specific databases

Arabidopsis Information Portal

More...Araporti		AT5G16970

The Arabidopsis Information Resource

More...TAIRi		locus:2148131, AT5G16970

<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, Nucleus

<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_00002180731 – 345NADPH-dependent oxidoreductase 2-alkenal reductaseAdd BLAST345

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q39172

PRoteomics IDEntifications database

More...PRIDEi		Q39172

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		244727

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q39172

<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

Expressed in leaves.1 Publication

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated upon treatment with paraquat, t-butylhydroperoxide, diamide, and menadione.1 Publication

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q39172, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q39172, AT

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		16836, 2 interactors

Protein interaction database and analysis system

More...IntActi		Q39172, 1 interactor

STRING: functional protein association networks

More...STRINGi		3702.AT5G16970.1

<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

1345
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		Q39172

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q39172

<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

<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

Belongs to the NADP-dependent oxidoreductase L4BD family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1196, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_026673_29_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q39172

Identification of Orthologs from Complete Genome Data

More...OMAi		AYSGWQE

Database of Orthologous Groups

More...OrthoDBi		884151at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q39172

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013149, ADH_C
IPR041694, ADH_N_2
IPR011032, GroES-like_sf
IPR045010, MDR_fam
IPR036291, NAD(P)-bd_dom_sf
IPR020843, PKS_ER

The PANTHER Classification System

More...PANTHERi		PTHR43205, PTHR43205, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF16884, ADH_N_2, 1 hit
PF00107, ADH_zinc_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00829, PKS_ER, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50129, SSF50129, 2 hits
SSF51735, SSF51735, 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.

Q39172-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTATNKQVIL KDYVSGFPTE SDFDFTTTTV ELRVPEGTNS VLVKNLYLSC 
        60         70         80         90        100
DPYMRIRMGK PDPSTAALAQ AYTPGQPIQG YGVSRIIESG HPDYKKGDLL 
       110        120        130        140        150
WGIVAWEEYS VITPMTHAHF KIQHTDVPLS YYTGLLGMPG MTAYAGFYEV 
       160        170        180        190        200
CSPKEGETVY VSAASGAVGQ LVGQLAKMMG CYVVGSAGSK EKVDLLKTKF 
       210        220        230        240        250
GFDDAFNYKE ESDLTAALKR CFPNGIDIYF ENVGGKMLDA VLVNMNMHGR 
       260        270        280        290        300
IAVCGMISQY NLENQEGVHN LSNIIYKRIR IQGFVVSDFY DKYSKFLEFV 
       310        320        330        340 
LPHIREGKIT YVEDVADGLE KAPEALVGLF HGKNVGKQVV VVARE
Length:345
Mass (Da):38,134
Last modified:November 1, 1996 - v1
<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:i5AFCEBB2948B2680
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 conflicti223P → T in AAM53276 (PubMed:14593172).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
Z49768 mRNA Translation: CAA89838.1
AL391141 Genomic DNA Translation: CAC01710.1
CP002688 Genomic DNA Translation: AED92364.1
AY120718 mRNA Translation: AAM53276.1
BT022058 mRNA Translation: AAY25470.1

Protein sequence database of the Protein Information Resource

More...PIRi		S57611

NCBI Reference Sequences

More...RefSeqi		NP_197199.1, NM_121703.4

Genome annotation databases

Ensembl plant genome annotation project

More...EnsemblPlantsi		AT5G16970.1; AT5G16970.1; AT5G16970

Database of genes from NCBI RefSeq genomes

More...GeneIDi		831560

Gramene; a comparative resource for plants

More...Gramenei		AT5G16970.1; AT5G16970.1; AT5G16970

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ath:AT5G16970

<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
Z49768 mRNA Translation: CAA89838.1
AL391141 Genomic DNA Translation: CAC01710.1
CP002688 Genomic DNA Translation: AED92364.1
AY120718 mRNA Translation: AAM53276.1
BT022058 mRNA Translation: AAY25470.1
PIRiS57611
RefSeqiNP_197199.1, NM_121703.4

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
2J3HX-ray2.50A/B1-345[»]
2J3IX-ray2.80A/B1-345[»]
2J3JX-ray2.80A/B1-345[»]
2J3KX-ray2.80A/B1-345[»]
SMRiQ39172
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi16836, 2 interactors
IntActiQ39172, 1 interactor
STRINGi3702.AT5G16970.1

PTM databases

iPTMnetiQ39172

Proteomic databases

PaxDbiQ39172
PRIDEiQ39172
ProteomicsDBi244727

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		831560

Genome annotation databases

EnsemblPlantsiAT5G16970.1; AT5G16970.1; AT5G16970
GeneIDi831560
GrameneiAT5G16970.1; AT5G16970.1; AT5G16970
KEGGiath:AT5G16970

Organism-specific databases

AraportiAT5G16970
TAIRilocus:2148131, AT5G16970

Phylogenomic databases

eggNOGiKOG1196, Eukaryota
HOGENOMiCLU_026673_29_1_1
InParanoidiQ39172
OMAiAYSGWQE
OrthoDBi884151at2759
PhylomeDBiQ39172

Enzyme and pathway databases

BioCyciARA:AT5G16970-MONOMER
SABIO-RKiQ39172

Miscellaneous databases

EvolutionaryTraceiQ39172

Protein Ontology

More...PROi		PR:Q39172

Gene expression databases

ExpressionAtlasiQ39172, baseline and differential
GenevisibleiQ39172, AT

Family and domain databases

InterProiView protein in InterPro
IPR013149, ADH_C
IPR041694, ADH_N_2
IPR011032, GroES-like_sf
IPR045010, MDR_fam
IPR036291, NAD(P)-bd_dom_sf
IPR020843, PKS_ER
PANTHERiPTHR43205, PTHR43205, 1 hit
PfamiView protein in Pfam
PF16884, ADH_N_2, 1 hit
PF00107, ADH_zinc_N, 1 hit
SMARTiView protein in SMART
SM00829, PKS_ER, 1 hit
SUPFAMiSSF50129, SSF50129, 2 hits
SSF51735, SSF51735, 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 nameiAER_ARATH
<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: Q39172
Secondary accession number(s): Q501A9, Q8L865
<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: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 23, 2022
This is version 147 of the entry and version 1 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. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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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