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Protein

NAD kinase

Gene

nadK

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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 as a source of phosphorus. NADH can not replace NAD as a substrate.UniRule annotation1 Publication

Catalytic activityi

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

Cofactori

a divalent metal cationUniRule annotation1 Publication

Enzyme regulationi

Allosterically inhibited by NADPH and NADH. NADPH is the primary inhibitor during aerobic growth and NADH during anaerobic growth.1 Publication

Kineticsi

  1. KM=2.1 mM for NAD1 Publication
  2. KM=2.7 mM for ATP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei73 – 731Proton acceptorUniRule annotation
    Binding sitei158 – 1581NADUniRule annotation
    Binding sitei175 – 1751NADUniRule annotation
    Sitei175 – 1751Responsible for conferring strict specificity to NADBy similarity
    Binding sitei177 – 1771NADUniRule annotation
    Binding sitei185 – 1851NAD; via carbonyl oxygenUniRule annotation
    Binding sitei247 – 2471NADUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi73 – 742NADUniRule annotation
    Nucleotide bindingi147 – 1482NADUniRule annotation
    Nucleotide bindingi188 – 1936NADUniRule 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

    BioCyciSENT99287:GCTI-2698-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD kinaseUniRule annotation (EC:2.7.1.23UniRule annotation)
    Alternative name(s):
    ATP-dependent NAD kinaseUniRule annotation
    Gene namesi
    Name:nadKUniRule annotation
    Ordered Locus Names:STM2683
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014 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 – 292292NAD kinasePRO_0000120655Add
    BLAST

    Proteomic databases

    PRIDEiP65774.

    Interactioni

    Subunit structurei

    Equilibrium mixture of dimer and tetramer. It is converted entirely to tetramer in the presence of the inhibitor NADPH.2 Publications

    Protein-protein interaction databases

    STRINGi99287.STM2683.

    Structurei

    Secondary structure

    1
    292
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 115Combined sources
    Helixi22 – 3211Combined sources
    Beta strandi36 – 405Combined sources
    Helixi41 – 466Combined sources
    Helixi57 – 637Combined sources
    Beta strandi65 – 695Combined sources
    Helixi73 – 8311Combined sources
    Beta strandi89 – 935Combined sources
    Beta strandi95 – 973Combined sources
    Helixi109 – 1179Combined sources
    Beta strandi121 – 13414Combined sources
    Beta strandi142 – 15514Combined sources
    Beta strandi160 – 1667Combined sources
    Beta strandi169 – 18214Combined sources
    Helixi185 – 1884Combined sources
    Helixi190 – 1934Combined sources
    Beta strandi204 – 2129Combined sources
    Beta strandi221 – 2244Combined sources
    Beta strandi229 – 2335Combined sources
    Beta strandi240 – 2445Combined sources
    Beta strandi250 – 2523Combined sources
    Beta strandi257 – 27216Combined sources
    Helixi277 – 2859Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AN1X-ray2.00A/B/C/D1-292[»]
    ProteinModelPortaliP65774.
    SMRiP65774. Positions 4-292.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP65774.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the NAD kinase family.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000227221.
    KOiK00858.
    OMAiGMVELRV.
    OrthoDBiEOG6PZXDR.
    PhylomeDBiP65774.

    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.

    P65774-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNNHFKCIGI VGHPRHPTAL TTHEMLYRWL CDQGYEVIVE QQIAHELQLK
    60 70 80 90 100
    NVPTGTLAEI GQQADLAVVV GGDGNMLGAA RTLARYDINV IGINRGNLGF
    110 120 130 140 150
    LTDLDPDNAL QQLSDVLEGR YISEKRFLLE AQVCQQDRQK RISTAINEVV
    160 170 180 190 200
    LHPGKVAHMI EFEVYIDETF AFSQRSDGLI ISTPTGSTAY SLSAGGPILT
    210 220 230 240 250
    PSLDAITLVP MFPHTLSARP LVINSSSTIR LRFSHRRSDL EISCDSQIAL
    260 270 280 290
    PIQEGEDVLI RRCDYHLNLI HPKDYSYFNT LSTKLGWSKK LF
    Length:292
    Mass (Da):32,584
    Last modified:October 11, 2004 - v1
    Checksum:i93585C83A2EEF41C
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE006468 Genomic DNA. Translation: AAL21572.1.
    RefSeqiNP_461613.1. NC_003197.1.
    WP_001059155.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL21572; AAL21572; STM2683.
    GeneIDi1254206.
    KEGGistm:STM2683.
    PATRICi32384022. VBISalEnt20916_2828.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE006468 Genomic DNA. Translation: AAL21572.1.
    RefSeqiNP_461613.1. NC_003197.1.
    WP_001059155.1. NC_003197.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AN1X-ray2.00A/B/C/D1-292[»]
    ProteinModelPortaliP65774.
    SMRiP65774. Positions 4-292.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi99287.STM2683.

    Proteomic databases

    PRIDEiP65774.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL21572; AAL21572; STM2683.
    GeneIDi1254206.
    KEGGistm:STM2683.
    PATRICi32384022. VBISalEnt20916_2828.

    Phylogenomic databases

    HOGENOMiHOG000227221.
    KOiK00858.
    OMAiGMVELRV.
    OrthoDBiEOG6PZXDR.
    PhylomeDBiP65774.

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-2698-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP65774.

    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: LT2 / SGSC1412 / ATCC 700720.
    2. "Evidence that feedback inhibition of NAD kinase controls responses to oxidative stress."
      Grose J.H., Joss L., Velick S.F., Roth J.R.
      Proc. Natl. Acad. Sci. U.S.A. 103:7601-7606(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, NOMENCLATURE.
    3. "The crystal structure of a putative kinase from Salmonella typhimurim LT2."
      Midwest center for structural genomics (MCSG)
      Submitted (AUG-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiNADK_SALTY
    AccessioniPrimary (citable) accession number: P65774
    Secondary accession number(s): Q8XFN1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: May 27, 2015
    This is version 72 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

    3D-structure, Complete proteome, Reference proteome

    Documents

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