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Protein

NAD kinase

Gene

nadK

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates (GTP,UTP) as well as inorganic polyphosphate (poly(P)) as a source of phosphorus. NAD is the preferred substrate for the kinase, but NADH can also be used as phosphoryl acceptor.UniRule annotation1 Publication

Catalytic activityi

ATP + NAD+ = ADP + NADP+.UniRule annotation1 Publication

Cofactori

a divalent metal cationUniRule annotation1 Publication

Kineticsi

  1. KM=0.29 mM for ATP (at pH 6 and 70 degrees Celsius)1 Publication
  2. KM=0.3 mM for NAD (with poly(P) as phosphoryl donor at pH 6.8 and 70 degrees Celsius)1 Publication
  3. KM=0.4 mM for NAD (with ATP as phosphoryl donor at pH 6.8 and 70 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 6.8. At 70 degrees Celsius for 60 minutes, the enzyme does not lose activity in a pH range of 4.0 to 10.5.1 Publication

    Temperature dependencei

    Extremely high thermostability. Upon heating at 95 degrees Celsius for 10 minutes the kinase activity is not lost, but about 80% of the activity is lost upon incubation at 100 degrees Celsius for 10 minutes.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei67 – 671Proton acceptorUniRule annotation
    Binding sitei72 – 721NADUniRule annotation
    Binding sitei148 – 1481NADUniRule annotation
    Binding sitei165 – 1651NADUniRule annotation
    Binding sitei167 – 1671NADUniRule annotation
    Binding sitei175 – 1751NAD; via carbonyl oxygenUniRule annotation
    Binding sitei236 – 2361NADUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi67 – 682NADUniRule annotation
    Nucleotide bindingi137 – 1382NADUniRule annotation
    Nucleotide bindingi178 – 1836NADUniRule annotation

    GO - Molecular functioni

    • ATP binding Source: UniProtKB
    • metal ion binding Source: UniProtKB-HAMAP
    • NAD+ kinase activity Source: UniProtKB
    • NAD binding Source: UniProtKB

    GO - Biological processi

    • NAD metabolic process Source: InterPro
    • NADP biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, NAD, NADP, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciPHOR70601:GJWR-1066-MONOMER.
    BRENDAi2.7.1.23. 5244.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD kinaseUniRule annotation (EC:2.7.1.23UniRule annotation)
    Alternative name(s):
    ATP-dependent NAD kinaseUniRule annotation
    Poly(P)-dependent NAD kinase
    Short name:
    PPNK
    Gene namesi
    Name:nadKUniRule annotation
    Ordered Locus Names:PH1074
    OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
    Taxonomic identifieri70601 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    ProteomesiUP000000752 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 277277NAD kinasePRO_0000120707Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi70601.PH1074.

    Structurei

    3D structure databases

    ProteinModelPortaliO58801.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the NAD kinase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0061.
    HOGENOMiHOG000227222.
    KOiK00858.
    OMAiLAINCGR.

    Family and domain databases

    Gene3Di2.60.200.30. 1 hit.
    3.40.50.10330. 1 hit.
    HAMAPiMF_00361. NAD_kinase.
    InterProiIPR017438. ATP-NAD_kinase_dom_1.
    IPR017437. ATP-NAD_kinase_PpnK-typ_all-b.
    IPR016064. NAD/diacylglycerol_kinase.
    IPR002504. NADK.
    [Graphical view]
    PANTHERiPTHR20275. PTHR20275. 1 hit.
    PfamiPF01513. NAD_kinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF111331. SSF111331. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O58801-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKFGIVARRD KEEALKLAYR VYDFLKVHGY EVVVDKETYE HFPHFKEGDV
    60 70 80 90 100
    IPLDEFDVDF IVAIGGDGTI LRIEHMTKKD IPILSINMGT LGFLTEVEPS
    110 120 130 140 150
    DTFFALNRLI EGEYYIDERI KVRTYIDGEN RVPDALNEVA ILTGIPGKII
    160 170 180 190 200
    HMKYYVDGGL ADEVRADGLV VSTPTGSTGY AMSAGGPFID PRLDVILIAP
    210 220 230 240 250
    LLPLPKTSVP MVIPGSSRID IRMLTDREII LAIDGQYYEH LPPNVEITVV
    260 270
    KSPRKTKFIR FTREIYPKYT IRIKERH
    Length:277
    Mass (Da):31,414
    Last modified:August 1, 1998 - v1
    Checksum:i707053D67637F13F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000001 Genomic DNA. Translation: BAA30173.1.
    AB055976 Genomic DNA. Translation: BAB32784.1.
    PIRiG71101.
    RefSeqiNP_142982.1. NC_000961.1.
    WP_010885160.1. NC_000961.1.

    Genome annotation databases

    EnsemblBacteriaiBAA30173; BAA30173; BAA30173.
    GeneIDi1443395.
    KEGGipho:PH1074.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    BA000001 Genomic DNA. Translation: BAA30173.1.
    AB055976 Genomic DNA. Translation: BAB32784.1.
    PIRiG71101.
    RefSeqiNP_142982.1. NC_000961.1.
    WP_010885160.1. NC_000961.1.

    3D structure databases

    ProteinModelPortaliO58801.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi70601.PH1074.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAA30173; BAA30173; BAA30173.
    GeneIDi1443395.
    KEGGipho:PH1074.

    Phylogenomic databases

    eggNOGiCOG0061.
    HOGENOMiHOG000227222.
    KOiK00858.
    OMAiLAINCGR.

    Enzyme and pathway databases

    BioCyciPHOR70601:GJWR-1066-MONOMER.
    BRENDAi2.7.1.23. 5244.

    Family and domain databases

    Gene3Di2.60.200.30. 1 hit.
    3.40.50.10330. 1 hit.
    HAMAPiMF_00361. NAD_kinase.
    InterProiIPR017438. ATP-NAD_kinase_dom_1.
    IPR017437. ATP-NAD_kinase_PpnK-typ_all-b.
    IPR016064. NAD/diacylglycerol_kinase.
    IPR002504. NADK.
    [Graphical view]
    PANTHERiPTHR20275. PTHR20275. 1 hit.
    PfamiPF01513. NAD_kinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF111331. SSF111331. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
    2. "Inorganic polyphosphate/ATP-NAD kinase of Pyrococcus horikoshii OT-3."
      Ohshima T., Sakuraba H.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
    3. "First archaeal inorganic polyphosphate/ATP-dependent NAD kinase, from hyperthermophilic archaeon Pyrococcus horikoshii: cloning, expression, and characterization."
      Sakuraba H., Kawakami R., Ohshima T.
      Appl. Environ. Microbiol. 71:4352-4358(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, SUBUNIT.
      Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

    Entry informationi

    Entry nameiNADK_PYRHO
    AccessioniPrimary (citable) accession number: O58801
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: August 1, 1998
    Last modified: May 27, 2015
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.