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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-Experimental evidence at protein leveli

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

Catalytic activityi

A n-alkanal + NAD(P)+ = an alk-2-enal + NAD(P)H.4 Publications

Enzyme regulationi

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

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

    GO - Molecular functioni

    • 2-alkenal reductase [NAD(P)] activity Source: TAIR

    GO - Biological processi

    • response to cadmium ion Source: TAIR
    • response to oxidative stress Source: TAIR

    Keywordsi

    Molecular functionOxidoreductase
    LigandNADP

    Enzyme and pathway databases

    BioCyciARA:AT5G16970-MONOMER.
    MetaCyc:AT5G16970-MONOMER.

    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
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 5

    Organism-specific databases

    AraportiAT5G16970.
    TAIRilocus:2148131. AT5G16970.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: TAIR
    • nucleoplasm Source: UniProtKB-SubCell
    • nucleus Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002180731 – 345NADPH-dependent oxidoreductase 2-alkenal reductaseAdd BLAST345

    Proteomic databases

    PaxDbiQ39172.
    PRIDEiQ39172.

    PTM databases

    iPTMnetiQ39172.

    Expressioni

    Tissue specificityi

    Expressed in leaves.1 Publication

    Inductioni

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

    Gene expression databases

    ExpressionAtlasiQ39172. baseline and differential.
    GenevisibleiQ39172. AT.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi16836. 2 interactors.
    IntActiQ39172. 1 interactor.
    STRINGi3702.AT5G16970.1.

    Structurei

    Secondary structure

    1345
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 10Combined sources9
    Beta strandi14 – 17Combined sources4
    Helixi20 – 22Combined sources3
    Beta strandi23 – 31Combined sources9
    Beta strandi36 – 39Combined sources4
    Beta strandi41 – 45Combined sources5
    Beta strandi47 – 49Combined sources3
    Helixi54 – 58Combined sources5
    Turni63 – 68Combined sources6
    Beta strandi79 – 89Combined sources11
    Beta strandi91 – 93Combined sources3
    Beta strandi99 – 112Combined sources14
    Turni116 – 118Combined sources3
    Beta strandi120 – 122Combined sources3
    Helixi131 – 133Combined sources3
    Turni134 – 136Combined sources3
    Helixi138 – 148Combined sources11
    Turni149 – 151Combined sources3
    Beta strandi158 – 163Combined sources6
    Helixi167 – 178Combined sources12
    Beta strandi182 – 189Combined sources8
    Helixi190 – 198Combined sources9
    Beta strandi203 – 207Combined sources5
    Helixi208 – 210Combined sources3
    Helixi215 – 221Combined sources7
    Beta strandi226 – 233Combined sources8
    Helixi235 – 242Combined sources8
    Beta strandi245 – 253Combined sources9
    Helixi257 – 259Combined sources3
    Helixi273 – 277Combined sources5
    Beta strandi280 – 283Combined sources4
    Helixi286 – 292Combined sources7
    Helixi293 – 305Combined sources13
    Beta strandi313 – 318Combined sources6
    Helixi319 – 321Combined sources3
    Helixi323 – 330Combined sources8
    Beta strandi335 – 343Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliQ39172.
    SMRiQ39172.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ39172.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1196. Eukaryota.
    COG2130. LUCA.
    HOGENOMiHOG000294663.
    InParanoidiQ39172.
    KOiK08070.
    OMAiIVAWEEY.
    OrthoDBiEOG09360DUC.
    PhylomeDBiQ39172.

    Family and domain databases

    InterProiView protein in InterPro
    IPR013149. ADH_C.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    PfamiView protein in Pfam
    PF00107. ADH_zinc_N. 1 hit.
    SMARTiView protein in SMART
    SM00829. PKS_ER. 1 hit.
    SUPFAMiSSF50129. SSF50129. 2 hits.
    SSF51735. SSF51735. 1 hit.

    Sequencei

    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
    Checksum:i5AFCEBB2948B2680
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti223P → T in AAM53276 (PubMed:14593172).Curated1

    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.
    UniGeneiAt.22432.

    Genome annotation databases

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

    Entry informationi

    Entry nameiAER_ARATH
    AccessioniPrimary (citable) accession number: Q39172
    Secondary accession number(s): Q501A9, Q8L865
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: May 10, 2017
    This is version 126 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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