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P0A7B3

- NADK_ECOLI

UniProt

P0A7B3 - NADK_ECOLI

Protein

NAD kinase

Gene

nadK

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (07 Jun 2005)
      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 (UTP, CTP, GTP, dATP, TTP) as phosphoryl donors, while nucleoside mono- or diphosphates and poly(P) can not.3 PublicationsUniRule annotation

    Catalytic activityi

    ATP + NAD+ = ADP + NADP+.3 PublicationsUniRule annotation

    Cofactori

    Divalent metal ions.1 PublicationUniRule annotation

    Enzyme regulationi

    Competitively and allosterically inhibited by NADH and NADPH at physiological concentrations, whereas inhibition by NADP is only slight. Inhibited by p-chloromercuribenzoate and HgCl2.2 Publications

    Kineticsi

    Kcat is 55 sec(-1) for kinase activity with ATP. Kcat is 125 sec(-1) for kinase activity with NAD.

    1. KM=2 mM for NAD (at pH 7 and 37 degrees Celsius)3 Publications
    2. KM=2.5 mM for ATP (at pH 7 and 37 degrees Celsius)3 Publications
    3. KM=4.1 mM for magnesium (at pH 7 and 37 degrees Celsius)3 Publications

    Vmax=12.86 µmol/min/mg enzyme (at pH 7 and 37 degrees Celsius)3 Publications

    pH dependencei

    Optimum pH is between 7.2 and 7.5.3 Publications

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius and half of the activity is lost on treatment at 65 degrees Celsius for 10 minutes.3 Publications

    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 NAD
    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: EcoCyc
    4. NAD binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, NAD, NADP, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:MONOMER0-541.
    ECOL316407:JW2596-MONOMER.
    MetaCyc:MONOMER0-541.

    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
    Synonyms:yfjB, yfjE
    Ordered Locus Names:b2615, JW2596
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12192. nadK.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytosol Source: EcoCyc

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi175 – 1751R → E: Does not exhibit NADH kinase activity in addition to NAD kinase activity. 1 Publication
    Mutagenesisi175 – 1751R → G: Exhibits NADH kinase activity in addition to NAD kinase activity. Reduces the Vmax of the NAD kinase activity. 1 Publication
    Mutagenesisi175 – 1751R → H: Exhibits NADH kinase activity in addition to NAD kinase activity. 1 Publication
    Mutagenesisi175 – 1751R → I: Does not exhibit NADH kinase activity in addition to NAD kinase activity. 1 Publication
    Mutagenesisi175 – 1751R → K: Does not exhibit NADH kinase activity in addition to NAD kinase activity. 1 Publication
    Mutagenesisi175 – 1751R → Q: Exhibits NADH kinase activity in addition to NAD kinase activity. 1 Publication
    Mutagenesisi175 – 1751R → T: Exhibits NADH kinase activity in addition to NAD kinase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 292292NAD kinasePRO_0000120616Add
    BLAST

    Proteomic databases

    PaxDbiP0A7B3.
    PRIDEiP0A7B3.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7B3.

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Protein-protein interaction databases

    BioGridi851428. 4 interactions.
    DIPiDIP-48103N.
    IntActiP0A7B3. 3 interactions.
    STRINGi511145.b2615.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A7B3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the NAD kinase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0061.
    HOGENOMiHOG000227221.
    KOiK00858.
    OMAiTHEMLYH.
    OrthoDBiEOG6PZXDR.
    PhylomeDBiP0A7B3.

    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.

    P0A7B3-1 [UniParc]FASTAAdd to Basket

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    MNNHFKCIGI VGHPRHPTAL TTHEMLYRWL CTKGYEVIVE QQIAHELQLK    50
    NVKTGTLAEI GQLADLAVVV GGDGNMLGAA RTLARYDIKV IGINRGNLGF 100
    LTDLDPDNAQ QQLADVLEGH YISEKRFLLE AQVCQQDCQK RISTAINEVV 150
    LHPGKVAHMI EFEVYIDEIF AFSQRSDGLI ISTPTGSTAY SLSAGGPILT 200
    PSLDAITLVP MFPHTLSARP LVINSSSTIR LRFSHRRNDL EISCDSQIAL 250
    PIQEGEDVLI RRCDYHLNLI HPKDYSYFNT LSTKLGWSKK LF 292
    Length:292
    Mass (Da):32,566
    Last modified:June 7, 2005 - v1
    Checksum:iD1E631658408F2E1
    GO

    Sequence cautioni

    The sequence X07863 differs from that shown. Reason: Frameshift at several positions.
    The sequence Y00357 differs from that shown. Reason: Frameshift at positions 204, 215 and 282.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U36840 Genomic DNA. Translation: AAA79785.1.
    U00096 Genomic DNA. Translation: AAC75664.1.
    AP009048 Genomic DNA. Translation: BAA16500.1.
    X07863 Genomic DNA. No translation available.
    Y00357 Genomic DNA. No translation available.
    PIRiB65040.
    RefSeqiNP_417105.1. NC_000913.3.
    YP_490837.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75664; AAC75664; b2615.
    BAA16500; BAA16500; BAA16500.
    GeneIDi12931613.
    947092.
    KEGGiecj:Y75_p2562.
    eco:b2615.
    PATRICi32120629. VBIEscCol129921_2713.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U36840 Genomic DNA. Translation: AAA79785.1 .
    U00096 Genomic DNA. Translation: AAC75664.1 .
    AP009048 Genomic DNA. Translation: BAA16500.1 .
    X07863 Genomic DNA. No translation available.
    Y00357 Genomic DNA. No translation available.
    PIRi B65040.
    RefSeqi NP_417105.1. NC_000913.3.
    YP_490837.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0A7B3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 851428. 4 interactions.
    DIPi DIP-48103N.
    IntActi P0A7B3. 3 interactions.
    STRINGi 511145.b2615.

    Proteomic databases

    PaxDbi P0A7B3.
    PRIDEi P0A7B3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75664 ; AAC75664 ; b2615 .
    BAA16500 ; BAA16500 ; BAA16500 .
    GeneIDi 12931613.
    947092.
    KEGGi ecj:Y75_p2562.
    eco:b2615.
    PATRICi 32120629. VBIEscCol129921_2713.

    Organism-specific databases

    EchoBASEi EB2109.
    EcoGenei EG12192. nadK.

    Phylogenomic databases

    eggNOGi COG0061.
    HOGENOMi HOG000227221.
    KOi K00858.
    OMAi THEMLYH.
    OrthoDBi EOG6PZXDR.
    PhylomeDBi P0A7B3.

    Enzyme and pathway databases

    BioCyci EcoCyc:MONOMER0-541.
    ECOL316407:JW2596-MONOMER.
    MetaCyc:MONOMER0-541.

    Miscellaneous databases

    PROi P0A7B3.

    Gene expression databases

    Genevestigatori P0A7B3.

    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. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Sequence analysis and transcriptional regulation of the Escherichia coli grpE gene, encoding a heat shock protein."
      Lipinska B., King J., Ang D., Georgopoulos C.
      Nucleic Acids Res. 16:7545-7562(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-163.
      Strain: B178.
    5. "Nucleotide sequence and LexA regulation of the Escherichia coli recN gene."
      Rostas K., Morton S.J., Picksley S.M., Lloyd R.G.
      Nucleic Acids Res. 15:5041-5049(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 194-292.
      Strain: K12.
    6. "Molecular characterization of Escherichia coli NAD kinase."
      Kawai S., Mori S., Mukai T., Hashimoto W., Murata K.
      Eur. J. Biochem. 268:4359-4365(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR, SUBUNIT.
      Strain: K12 / MG1655 / ATCC 47076.
    7. "Negative modulation of Escherichia coli NAD kinase by NADPH and NADH."
      Zerez C.R., Moul D.E., Gomez E.G., Lopez V.M., Andreoli A.J.
      J. Bacteriol. 169:184-188(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
      Strain: K12 / MG1655 / ATCC 47076.
    8. "Intrinsic and extrinsic approaches for detecting genes in a bacterial genome."
      Borodovsky M., Rudd K.E., Koonin E.V.
      Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    9. "Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution."
      Mori S., Kawai S., Shi F., Mikami B., Murata K.
      J. Biol. Chem. 280:24104-24112(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-175, BIOPHYSICOCHEMICAL PROPERTIES, BINDING SPECIFICITY.

    Entry informationi

    Entry nameiNADK_ECOLI
    AccessioniPrimary (citable) accession number: P0A7B3
    Secondary accession number(s): P37768, P46140, P77490
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 84 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, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3