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Protein

NAD(P)H dehydrogenase [quinone] 1

Gene

Nqo1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.2 Publications

Catalytic activityi

NAD(P)H + a quinone = NAD(P)+ + a hydroquinone.2 Publications

Cofactori

FAD1 Publication

Kineticsi

kcat is 0.075 min(-1) NADH with as substrate. kcat is 0.074 min(-1) with NADPH as substrate.1 Publication

Manual assertion based on experiment ini

  1. KM=85 µM for NADH1 Publication
  2. KM=39 µM for NADPH1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei12FAD1 Publication1
    Binding sitei67FAD1 Publication1
    Binding sitei156FAD1 Publication1
    Binding sitei201FAD1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi18 – 19FAD1 Publication2
    Nucleotide bindingi104 – 107FAD1 Publication4
    Nucleotide bindingi148 – 151FAD1 Publication4

    GO - Molecular functioni

    • NAD(P)H dehydrogenase (quinone) activity Source: RGD
    • poly(A) RNA binding Source: Ensembl
    • superoxide dismutase activity Source: RGD

    GO - Biological processi

    • aging Source: RGD
    • negative regulation of apoptotic process Source: RGD
    • negative regulation of catalytic activity Source: Ensembl
    • positive regulation of neuron apoptotic process Source: RGD
    • response to estradiol Source: RGD
    • response to ethanol Source: RGD
    • response to nutrient Source: RGD
    • response to organic cyclic compound Source: RGD
    • response to oxidative stress Source: RGD
    • superoxide metabolic process Source: RGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NAD, NADP

    Enzyme and pathway databases

    BRENDAi1.6.5.2. 5301.
    ReactomeiR-RNO-350562. Regulation of ornithine decarboxylase (ODC).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD(P)H dehydrogenase [quinone] 1 (EC:1.6.5.22 Publications)
    Alternative name(s):
    Azoreductase
    DT-diaphorase
    Short name:
    DTD
    Menadione reductase
    NAD(P)H:quinone oxidoreductase 1
    Phylloquinone reductase
    Quinone reductase 1
    Short name:
    QR1
    Gene namesi
    Name:Nqo1
    Synonyms:Nmor1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Chromosome 19

    Organism-specific databases

    RGDi2503. Nqo1.

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    • cytosol Source: RGD
    • extracellular exosome Source: Ensembl
    • neuronal cell body Source: RGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi117 – 118FE → KK: Destroys enzyme activity. 1 Publication2
    Mutagenesisi161V → D: Destroys enzyme activity. 1 Publication1
    Mutagenesisi164D → Q: Destroys enzyme activity. 1 Publication1
    Mutagenesisi195H → A: Induces a very low catalytic efficiency. 1 Publication1

    Chemistry databases

    ChEMBLiCHEMBL3091269.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved2 Publications
    ChainiPRO_00000716252 – 274NAD(P)H dehydrogenase [quinone] 1Add BLAST273

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanine1 Publication1
    Modified residuei82PhosphoserineBy similarity1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP05982.
    PRIDEiP05982.

    2D gel databases

    World-2DPAGE0004:P05982.

    PTM databases

    iPTMnetiP05982.
    PhosphoSitePlusiP05982.

    Expressioni

    Inductioni

    By polycyclic hydrocarbons (Governed by the aromatic hydrocarbon-responsive (AH) locus).

    Gene expression databases

    BgeeiENSRNOG00000012772.
    GenevisibleiP05982. RN.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiP05982. 1 interactor.
    STRINGi10116.ENSRNOP00000017175.

    Structurei

    Secondary structure

    1274
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 10Combined sources6
    Helixi18 – 32Combined sources15
    Beta strandi36 – 41Combined sources6
    Turni42 – 46Combined sources5
    Helixi53 – 55Combined sources3
    Helixi68 – 78Combined sources11
    Helixi83 – 94Combined sources12
    Beta strandi96 – 103Combined sources8
    Helixi111 – 120Combined sources10
    Turni123 – 125Combined sources3
    Helixi133 – 135Combined sources3
    Turni137 – 140Combined sources4
    Beta strandi142 – 148Combined sources7
    Helixi153 – 156Combined sources4
    Helixi165 – 173Combined sources9
    Helixi174 – 178Combined sources5
    Turni179 – 181Combined sources3
    Beta strandi188 – 190Combined sources3
    Helixi193 – 195Combined sources3
    Helixi198 – 212Combined sources15
    Helixi215 – 217Combined sources3
    Helixi226 – 228Combined sources3
    Turni233 – 236Combined sources4
    Helixi241 – 247Combined sources7
    Beta strandi254 – 256Combined sources3
    Turni266 – 270Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1QRDX-ray2.40A/B2-274[»]
    ProteinModelPortaliP05982.
    SMRiP05982.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05982.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni126 – 128Substrate bindingBy similarity3

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG410IKWF. Eukaryota.
    COG2249. LUCA.
    GeneTreeiENSGT00440000033410.
    HOGENOMiHOG000149970.
    HOVERGENiHBG029104.
    InParanoidiP05982.
    KOiK00355.
    OMAiYDKGPFQ.
    OrthoDBiEOG091G183R.
    PhylomeDBiP05982.
    TreeFamiTF300296.

    Family and domain databases

    Gene3Di3.40.50.360. 1 hit.
    InterProiIPR003680. Flavodoxin_fold.
    IPR029039. Flavoprotein-like_dom.
    [Graphical view]
    PfamiPF02525. Flavodoxin_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52218. SSF52218. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P05982-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAVRRALIVL AHAERTSFNY AMKEAAVEAL KKKGWEVVES DLYAMNFNPL
    60 70 80 90 100
    ISRNDITGEP KDSENFQYPV ESSLAYKEGR LSPDIVAEQK KLEAADLVIF
    110 120 130 140 150
    QFPLYWFGVP AILKGWFERV LVAGFAYTYA TMYDKGPFQN KKTLLSITTG
    160 170 180 190 200
    GSGSMYSLQG VHGDMNVILW PIQSGILRFC GFQVLEPQLV YSIGHTPPDA
    210 220 230 240 250
    RVQVLEGWKK RLETVWEESP LYFAPSSLFD LNFQAGFLLK KEVQEEQKKN
    260 270
    KFGLSVGHHL GKSIPADNQI KARK
    Length:274
    Mass (Da):30,947
    Last modified:January 23, 2007 - v4
    Checksum:i40E8801320A20F09
    GO

    Sequence cautioni

    The sequence AAA41988 differs from that shown. Reason: Erroneous initiation.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti31Missing AA sequence (PubMed:3144286).Curated1
    Sequence conflicti80R → G in X17464 (PubMed:2504488).Curated1
    Sequence conflicti135K → Q in AAA41988 (PubMed:3100515).Curated1
    Sequence conflicti216W → E AA sequence (PubMed:3144286).Curated1
    Sequence conflicti227S → E AA sequence (PubMed:3144286).Curated1
    Sequence conflicti263S → I AA sequence (PubMed:3144286).Curated1
    Sequence conflicti269Q → E AA sequence (PubMed:2499768).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J02608 mRNA. Translation: AAA41716.1.
    J02679 mRNA. Translation: AAA41715.1.
    M36660 mRNA. Translation: AAA39829.1.
    J02640 mRNA. Translation: AAA41988.1. Different initiation.
    M31805
    , M31801, M31802, M31804 Genomic DNA. Translation: AAA41989.1.
    M33039, M33038 Genomic DNA. Translation: AAA41990.1.
    BC083542 mRNA. Translation: AAH83542.1.
    X17464 mRNA. No translation available.
    PIRiA34162.
    RefSeqiNP_058696.2. NM_017000.3.
    UniGeneiRn.11234.

    Genome annotation databases

    EnsembliENSRNOT00000017174; ENSRNOP00000017175; ENSRNOG00000012772.
    GeneIDi24314.
    KEGGirno:24314.
    UCSCiRGD:2503. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J02608 mRNA. Translation: AAA41716.1.
    J02679 mRNA. Translation: AAA41715.1.
    M36660 mRNA. Translation: AAA39829.1.
    J02640 mRNA. Translation: AAA41988.1. Different initiation.
    M31805
    , M31801, M31802, M31804 Genomic DNA. Translation: AAA41989.1.
    M33039, M33038 Genomic DNA. Translation: AAA41990.1.
    BC083542 mRNA. Translation: AAH83542.1.
    X17464 mRNA. No translation available.
    PIRiA34162.
    RefSeqiNP_058696.2. NM_017000.3.
    UniGeneiRn.11234.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1QRDX-ray2.40A/B2-274[»]
    ProteinModelPortaliP05982.
    SMRiP05982.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP05982. 1 interactor.
    STRINGi10116.ENSRNOP00000017175.

    Chemistry databases

    ChEMBLiCHEMBL3091269.

    PTM databases

    iPTMnetiP05982.
    PhosphoSitePlusiP05982.

    2D gel databases

    World-2DPAGE0004:P05982.

    Proteomic databases

    PaxDbiP05982.
    PRIDEiP05982.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000017174; ENSRNOP00000017175; ENSRNOG00000012772.
    GeneIDi24314.
    KEGGirno:24314.
    UCSCiRGD:2503. rat.

    Organism-specific databases

    CTDi1728.
    RGDi2503. Nqo1.

    Phylogenomic databases

    eggNOGiENOG410IKWF. Eukaryota.
    COG2249. LUCA.
    GeneTreeiENSGT00440000033410.
    HOGENOMiHOG000149970.
    HOVERGENiHBG029104.
    InParanoidiP05982.
    KOiK00355.
    OMAiYDKGPFQ.
    OrthoDBiEOG091G183R.
    PhylomeDBiP05982.
    TreeFamiTF300296.

    Enzyme and pathway databases

    BRENDAi1.6.5.2. 5301.
    ReactomeiR-RNO-350562. Regulation of ornithine decarboxylase (ODC).

    Miscellaneous databases

    EvolutionaryTraceiP05982.
    PROiP05982.

    Gene expression databases

    BgeeiENSRNOG00000012772.
    GenevisibleiP05982. RN.

    Family and domain databases

    Gene3Di3.40.50.360. 1 hit.
    InterProiIPR003680. Flavodoxin_fold.
    IPR029039. Flavoprotein-like_dom.
    [Graphical view]
    PfamiPF02525. Flavodoxin_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52218. SSF52218. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiNQO1_RAT
    AccessioniPrimary (citable) accession number: P05982
    Secondary accession number(s): Q63478
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: January 23, 2007
    Last modified: November 2, 2016
    This is version 151 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Quinone reductase accepts electrons from both NADH and NADPH with equal efficiency.
    This protein is inhibited by dicoumarol.

    Caution

    PubMed:2480957 sequence seems incorrectly to be attributed to a mouse sequence while it really seems to correspond to the rat sequence.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.