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P65774

- NADK_SALTY

UniProt

P65774 - NADK_SALTY

Protein

NAD kinase

Gene

nadK

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
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    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.1 PublicationUniRule annotation

    Catalytic activityi

    ATP + NAD+ = ADP + NADP+.1 PublicationUniRule annotation

    Cofactori

    Divalent metal ions.1 PublicationUniRule annotation

    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

    1. ATP binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-HAMAP
    3. NAD+ kinase activity Source: UniProtKB
    4. NAD binding Source: UniProtKB

    GO - Biological processi

    1. NAD metabolic process Source: InterPro
    2. NADP biosynthetic process Source: UniProtKB

    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: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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 – 115
    Helixi22 – 3211
    Beta strandi36 – 405
    Helixi41 – 466
    Helixi57 – 637
    Beta strandi65 – 695
    Helixi73 – 8311
    Beta strandi89 – 935
    Beta strandi95 – 973
    Helixi109 – 1179
    Beta strandi121 – 13414
    Beta strandi142 – 15514
    Beta strandi160 – 1667
    Beta strandi169 – 18214
    Helixi185 – 1884
    Helixi190 – 1934
    Beta strandi204 – 2129
    Beta strandi221 – 2244
    Beta strandi229 – 2335
    Beta strandi240 – 2445
    Beta strandi250 – 2523
    Beta strandi257 – 27216
    Helixi277 – 2859

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiTHEMLYH.
    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.
    IPR016064. ATP-NAD_kinase_PpnK-typ.
    IPR017437. ATP-NAD_kinase_PpnK-typ_all-b.
    IPR002504. PolyP/ATP_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

    MNNHFKCIGI VGHPRHPTAL TTHEMLYRWL CDQGYEVIVE QQIAHELQLK    50
    NVPTGTLAEI GQQADLAVVV GGDGNMLGAA RTLARYDINV IGINRGNLGF 100
    LTDLDPDNAL QQLSDVLEGR YISEKRFLLE AQVCQQDRQK RISTAINEVV 150
    LHPGKVAHMI EFEVYIDETF AFSQRSDGLI ISTPTGSTAY SLSAGGPILT 200
    PSLDAITLVP MFPHTLSARP LVINSSSTIR LRFSHRRSDL EISCDSQIAL 250
    PIQEGEDVLI RRCDYHLNLI HPKDYSYFNT LSTKLGWSKK LF 292
    Length:292
    Mass (Da):32,584
    Last modified:October 11, 2004 - v1
    Checksum:i93585C83A2EEF41C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006468 Genomic DNA. Translation: AAL21572.1.
    RefSeqiNP_461613.1. NC_003197.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006468 Genomic DNA. Translation: AAL21572.1 .
    RefSeqi NP_461613.1. NC_003197.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AN1 X-ray 2.00 A/B/C/D 1-292 [» ]
    ProteinModelPortali P65774.
    SMRi P65774. Positions 4-292.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM2683.

    Proteomic databases

    PRIDEi P65774.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL21572 ; AAL21572 ; STM2683 .
    GeneIDi 1254206.
    KEGGi stm:STM2683.
    PATRICi 32384022. VBISalEnt20916_2828.

    Phylogenomic databases

    HOGENOMi HOG000227221.
    KOi K00858.
    OMAi THEMLYH.
    OrthoDBi EOG6PZXDR.
    PhylomeDBi P65774.

    Enzyme and pathway databases

    BioCyci SENT99287:GCTI-2698-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P65774.

    Family and domain databases

    Gene3Di 2.60.200.30. 1 hit.
    3.40.50.10330. 1 hit.
    HAMAPi MF_00361. NAD_kinase.
    InterProi IPR017438. ATP-NAD_kinase_dom_1.
    IPR016064. ATP-NAD_kinase_PpnK-typ.
    IPR017437. ATP-NAD_kinase_PpnK-typ_all-b.
    IPR002504. PolyP/ATP_NADK.
    [Graphical view ]
    PANTHERi PTHR20275. PTHR20275. 1 hit.
    Pfami PF01513. NAD_kinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF111331. SSF111331. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 67 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