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Protein

NADP-dependent alkenal double bond reductase P1

Gene

P1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of the 7-8 double bond of phenylpropanal substrates, such as p-coumaryl aldehyde and coniferyl aldehyde (in vitro). Has activity towards toxic substrates, such as 4-hydroxy-(2E)-nonenal (in vitro). May play a distinct role in plant antioxidant defense and is possibly involved in NAD(P)/NAD(P)H homeostasis.1 Publication

Catalytic activityi

A n-alkanal + NAD(P)+ = an alk-2-enal + NAD(P)H.1 Publication

Kineticsi

  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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531Substrate
    Binding sitei81 – 811Substrate
    Binding sitei192 – 1921NADP
    Binding sitei208 – 2081NADP
    Binding sitei232 – 2321NADP
    Binding sitei334 – 3341NADP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi166 – 1694NADP
    Nucleotide bindingi254 – 2607NADP
    Nucleotide bindingi284 – 2863NADP

    GO - Molecular functioni

    • 2-alkenal reductase [NAD(P)] activity Source: TAIR
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • response to cadmium ion Source: TAIR
    • response to oxidative stress Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADP-dependent alkenal double bond reductase P1 (EC:1.3.1.74)
    Short name:
    DBR1
    Gene namesi
    Name:P1
    Ordered Locus Names:At5g16970
    ORF Names:F2K13_120
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 5

    Organism-specific databases

    TAIRiAT5G16970.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: TAIR
    • nucleus Source: TAIR
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 345345NADP-dependent alkenal double bond reductase P1PRO_0000218073Add
    BLAST

    Proteomic databases

    PaxDbiQ39172.
    PRIDEiQ39172.

    PTM databases

    iPTMnetiQ39172.

    Expressioni

    Gene expression databases

    ExpressionAtlasiQ39172. baseline and differential.
    GenevisibleiQ39172. AT.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi16836. 2 interactions.
    IntActiQ39172. 1 interaction.
    STRINGi3702.AT5G16970.1.

    Structurei

    Secondary structure

    1
    345
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 109Combined sources
    Beta strandi14 – 174Combined sources
    Helixi20 – 223Combined sources
    Beta strandi23 – 319Combined sources
    Beta strandi36 – 394Combined sources
    Beta strandi41 – 455Combined sources
    Beta strandi47 – 493Combined sources
    Helixi54 – 585Combined sources
    Turni63 – 686Combined sources
    Beta strandi79 – 8911Combined sources
    Beta strandi91 – 933Combined sources
    Beta strandi99 – 11214Combined sources
    Turni116 – 1183Combined sources
    Beta strandi120 – 1223Combined sources
    Helixi131 – 1333Combined sources
    Turni134 – 1363Combined sources
    Helixi138 – 14811Combined sources
    Turni149 – 1513Combined sources
    Beta strandi158 – 1636Combined sources
    Helixi167 – 17812Combined sources
    Beta strandi182 – 1898Combined sources
    Helixi190 – 1989Combined sources
    Beta strandi203 – 2075Combined sources
    Helixi208 – 2103Combined sources
    Helixi215 – 2217Combined sources
    Beta strandi226 – 2338Combined sources
    Helixi235 – 2428Combined sources
    Beta strandi245 – 2539Combined sources
    Helixi257 – 2593Combined sources
    Helixi273 – 2775Combined sources
    Beta strandi280 – 2834Combined sources
    Helixi286 – 2927Combined sources
    Helixi293 – 30513Combined sources
    Beta strandi313 – 3186Combined sources
    Helixi319 – 3213Combined sources
    Helixi323 – 3308Combined sources
    Beta strandi335 – 3439Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 1-345.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ39172.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1196. Eukaryota.
    COG2130. LUCA.
    HOGENOMiHOG000294663.
    InParanoidiQ39172.
    KOiK08070.
    OMAiKCRETIT.
    PhylomeDBiQ39172.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    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

    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.
    PIRiS57611.
    RefSeqiNP_197199.1. NM_121703.3.
    UniGeneiAt.22432.

    Genome annotation databases

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

    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.
    PIRiS57611.
    RefSeqiNP_197199.1. NM_121703.3.
    UniGeneiAt.22432.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 1-345.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi16836. 2 interactions.
    IntActiQ39172. 1 interaction.
    STRINGi3702.AT5G16970.1.

    PTM databases

    iPTMnetiQ39172.

    Proteomic databases

    PaxDbiQ39172.
    PRIDEiQ39172.

    Protocols and materials databases

    DNASUi831560.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    TAIRiAT5G16970.

    Phylogenomic databases

    eggNOGiKOG1196. Eukaryota.
    COG2130. LUCA.
    HOGENOMiHOG000294663.
    InParanoidiQ39172.
    KOiK08070.
    OMAiKCRETIT.
    PhylomeDBiQ39172.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ39172.
    PROiQ39172.

    Gene expression databases

    ExpressionAtlasiQ39172. baseline and differential.
    GenevisibleiQ39172. AT.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 2 hits.
    SSF51735. SSF51735. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Arabidopsis thaliana NADPH oxidoreductase homologs confer tolerance of yeasts toward the thiol-oxidizing drug diamide."
      Babiychuk E., Kushnir S., Belles-Boix E., van Montagu M., Inze D.
      J. Biol. Chem. 270:26224-26231(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Mechanistic and structural studies of apoform, binary, and ternary complexes of the Arabidopsis alkenal double bond reductase At5g16970."
      Youn B., Kim S.J., Moinuddin S.G., Lee C., Bedgar D.L., Harper A.R., Davin L.B., Lewis N.G., Kang C.
      J. Biol. Chem. 281:40076-40088(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES AND NADP, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiP1_ARATH
    AccessioniPrimary (citable) accession number: Q39172
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: June 8, 2016
    This is version 119 of the entry and version 1 of the sequence. [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

    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.