UniProtKB - Q39172 (AER_ARATH)
NADPH-dependent oxidoreductase 2-alkenal reductase
AER
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 PublicationsCatalytic activityi
Activity regulationi
Kineticsi
- KM=0.53 mM for p-coumaryl aldehyde1 Publication
- KM=0.41 mM for coniferyl aldehyde1 Publication
- KM=0.28 mM for 4-hydroxy-(2E)-nonenal1 Publication
- KM=10 µM for trans-1,3 diphenyl-2-propenone1 Publication
- KM=3.7 µM for trans-1,4-diphenyl-2-butene-1,4-dione1 Publication
- KM=6.6 µM for traumatin1 Publication
- KM=0.65 µM for 9,10-phenanthrenequinone1 Publication
- KM=11 µM for 5-Hydroxy-1,4-naphtoquinone1 Publication
- KM=152 µM for 1,4-Benzoquinone1 Publication
- KM=25 µM for decyl-plastoquinone1 Publication
- KM=20 µM for ferricytochrome c1 Publication
- KM=128 µM for azodicarboxylic acid bis[dimethylamide]1 Publication
- KM=120 µM for 1,10-(azocarbonyl)-dipeperidine1 Publication
- KM=3.4 µM for azocarbonamide1 Publication
- KM=2.5 µM for NADPH for 9,10-phenanthrenequinone-reduction1 Publication
- KM=8.2 µM for NADPH for azodicarboxylic acid bis[dimethylamide]-reduction1 Publication
- KM=13.4 µM for 4-hydroxy-(2E)-nonenal1 Publication
- KM=145 µM for 4-hydroxy-(2E)-hexenal1 Publication
- KM=5.9 µM for (2E)-nonenal1 Publication
- KM=232 µM for (2E)-hexenal1 Publication
- KM=1420 µM for (2E)-pentenal1 Publication
- KM=4650 µM for propenal1 Publication
- KM=55 µM for 3-buten-2-one1 Publication
- KM=5.2 µM for 3-penten-2-one1 Publication
- KM=11.3 µM for (2E),(6Z)-nonadienal1 Publication
- KM=1.24 µM for 4-oxo-(2E)-nonenal1 Publication
- KM=10.0 µM for 9-oxo-10(E),12(Z)-octadecadienoic acid1 Publication
- KM=3.92 µM for 13-oxo-9(Z),11(E)-octadecadienoic acid1 Publication
- KM=0.673 µM for 3-nonen-2-one1 Publication
pH dependencei
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 53 | SubstrateCombined sources | 1 | |
Binding sitei | 188 | NADP; via amide nitrogenCombined sources | 1 | |
Binding sitei | 192 | NADPCombined sources | 1 | |
Binding sitei | 208 | NADPCombined sources | 1 | |
Binding sitei | 232 | NADP; via carbonyl oxygenCombined sources | 1 | |
Binding sitei | 254 | NADPCombined sources | 1 | |
Binding sitei | 260 | NADPCombined sources | 1 | |
Binding sitei | 260 | SubstrateCombined sources | 1 | |
Binding sitei | 330 | NADP; via carbonyl oxygenCombined sources | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 52 – 53 | NADPCombined sources | 2 | |
Nucleotide bindingi | 163 – 169 | NADPCombined sources | 7 | |
Nucleotide bindingi | 284 – 286 | NADPCombined sources | 3 | |
Nucleotide bindingi | 334 – 336 | NADPCombined sources | 3 |
GO - Molecular functioni
- 2-alkenal reductase [NAD(P)+] activity Source: TAIR
GO - Biological processi
- response to oxidative stress Source: TAIR
Keywordsi
Molecular function | Oxidoreductase |
Ligand | NADP |
Enzyme and pathway databases
BioCyci | ARA:AT5G16970-MONOMER |
SABIO-RKi | Q39172 |
Names & Taxonomyi
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 |
Gene namesi | Name:AER1 Publication Synonyms:P11 Publication Ordered Locus Names:At5g16970Imported ORF Names:F2K13_120Imported |
Organismi | Arabidopsis thaliana (Mouse-ear cress) |
Taxonomic identifieri | 3702 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis |
Proteomesi |
|
Organism-specific databases
Araporti | AT5G16970 |
TAIRi | locus:2148131, AT5G16970 |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Nucleus
- nucleoplasm 1 Publication
Cytosol
- cytosol Source: TAIR
Nucleus
- nucleoplasm Source: UniProtKB-SubCell
- nucleus Source: TAIR
Other locations
- plastid Source: TAIR
Keywords - Cellular componenti
Cytoplasm, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000218073 | 1 – 345 | NADPH-dependent oxidoreductase 2-alkenal reductaseAdd BLAST | 345 |
Proteomic databases
PaxDbi | Q39172 |
PRIDEi | Q39172 |
ProteomicsDBi | 244727 |
PTM databases
iPTMneti | Q39172 |
Expressioni
Tissue specificityi
Inductioni
Gene expression databases
ExpressionAtlasi | Q39172, baseline and differential |
Genevisiblei | Q39172, AT |
Interactioni
Subunit structurei
Homodimer.
2 PublicationsProtein-protein interaction databases
BioGRIDi | 16836, 2 interactors |
IntActi | Q39172, 1 interactor |
STRINGi | 3702.AT5G16970.1 |
Structurei
Secondary structure
3D structure databases
SMRi | Q39172 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q39172 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG1196, Eukaryota |
HOGENOMi | CLU_026673_29_1_1 |
InParanoidi | Q39172 |
OMAi | AYSGWQE |
OrthoDBi | 884151at2759 |
PhylomeDBi | Q39172 |
Family and domain databases
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 |
PANTHERi | PTHR43205, PTHR43205, 1 hit |
Pfami | View protein in Pfam PF16884, ADH_N_2, 1 hit PF00107, ADH_zinc_N, 1 hit |
SMARTi | View protein in SMART SM00829, PKS_ER, 1 hit |
SUPFAMi | SSF50129, SSF50129, 2 hits SSF51735, SSF51735, 1 hit |
i Sequence
Sequence statusi: Complete.
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 223 | P → T in AAM53276 (PubMed:14593172).Curated | 1 |
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 |
PIRi | S57611 |
RefSeqi | NP_197199.1, NM_121703.4 |
Genome annotation databases
EnsemblPlantsi | AT5G16970.1; AT5G16970.1; AT5G16970 |
GeneIDi | 831560 |
Gramenei | AT5G16970.1; AT5G16970.1; AT5G16970 |
KEGGi | ath:AT5G16970 |
Similar proteinsi
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 |
PIRi | S57611 |
RefSeqi | NP_197199.1, NM_121703.4 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2J3H | X-ray | 2.50 | A/B | 1-345 | [»] | |
2J3I | X-ray | 2.80 | A/B | 1-345 | [»] | |
2J3J | X-ray | 2.80 | A/B | 1-345 | [»] | |
2J3K | X-ray | 2.80 | A/B | 1-345 | [»] | |
SMRi | Q39172 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 16836, 2 interactors |
IntActi | Q39172, 1 interactor |
STRINGi | 3702.AT5G16970.1 |
PTM databases
iPTMneti | Q39172 |
Proteomic databases
PaxDbi | Q39172 |
PRIDEi | Q39172 |
ProteomicsDBi | 244727 |
Protocols and materials databases
DNASUi | 831560 |
Genome annotation databases
EnsemblPlantsi | AT5G16970.1; AT5G16970.1; AT5G16970 |
GeneIDi | 831560 |
Gramenei | AT5G16970.1; AT5G16970.1; AT5G16970 |
KEGGi | ath:AT5G16970 |
Organism-specific databases
Araporti | AT5G16970 |
TAIRi | locus:2148131, AT5G16970 |
Phylogenomic databases
eggNOGi | KOG1196, Eukaryota |
HOGENOMi | CLU_026673_29_1_1 |
InParanoidi | Q39172 |
OMAi | AYSGWQE |
OrthoDBi | 884151at2759 |
PhylomeDBi | Q39172 |
Enzyme and pathway databases
BioCyci | ARA:AT5G16970-MONOMER |
SABIO-RKi | Q39172 |
Miscellaneous databases
EvolutionaryTracei | Q39172 |
PROi | PR:Q39172 |
Gene expression databases
ExpressionAtlasi | Q39172, baseline and differential |
Genevisiblei | Q39172, AT |
Family and domain databases
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 |
PANTHERi | PTHR43205, PTHR43205, 1 hit |
Pfami | View protein in Pfam PF16884, ADH_N_2, 1 hit PF00107, ADH_zinc_N, 1 hit |
SMARTi | View protein in SMART SM00829, PKS_ER, 1 hit |
SUPFAMi | SSF50129, SSF50129, 2 hits SSF51735, SSF51735, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | AER_ARATH | |
Accessioni | Q39172Primary (citable) accession number: Q39172 Secondary accession number(s): Q501A9, Q8L865 | |
Entry historyi | Integrated 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. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Plant Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Arabidopsis thaliana
Arabidopsis thaliana: entries and gene names - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families