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Protein

NAD kinase

Gene

nadK

Organism
Escherichia coli (strain K12)
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 (UTP, CTP, GTP, dATP, TTP) as phosphoryl donors, while nucleoside mono- or diphosphates and poly(P) can not.UniRule annotation3 Publications

Catalytic activityi

ATP + NAD+ = ADP + NADP+.UniRule annotation3 Publications

Cofactori

a divalent metal cationUniRule annotation1 Publication

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
  1. 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

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

GO - Biological processi

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

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.
BRENDAi2.7.1.23. 2026.

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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12192. nadK.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

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.

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.
SMRiP0A7B3. Positions 4-292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NAD kinase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0061.
HOGENOMiHOG000227221.
InParanoidiP0A7B3.
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.
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.

P0A7B3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNHFKCIGI VGHPRHPTAL TTHEMLYRWL CTKGYEVIVE QQIAHELQLK
60 70 80 90 100
NVKTGTLAEI GQLADLAVVV GGDGNMLGAA RTLARYDIKV IGINRGNLGF
110 120 130 140 150
LTDLDPDNAQ QQLADVLEGH YISEKRFLLE AQVCQQDCQK RISTAINEVV
160 170 180 190 200
LHPGKVAHMI EFEVYIDEIF AFSQRSDGLI ISTPTGSTAY SLSAGGPILT
210 220 230 240 250
PSLDAITLVP MFPHTLSARP LVINSSSTIR LRFSHRRNDL EISCDSQIAL
260 270 280 290
PIQEGEDVLI RRCDYHLNLI HPKDYSYFNT LSTKLGWSKK LF
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. Curated
The sequence Y00357 differs from that shown. Reason: Frameshift at positions 204, 215 and 282. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_001059169.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC75664; AAC75664; b2615.
BAA16500; BAA16500; BAA16500.
GeneIDi947092.
KEGGieco:b2615.
PATRICi32120629. VBIEscCol129921_2713.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_001059169.1. NZ_CP010445.1.

3D structure databases

ProteinModelPortaliP0A7B3.
SMRiP0A7B3. Positions 4-292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP0A7B3.
PRIDEiP0A7B3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75664; AAC75664; b2615.
BAA16500; BAA16500; BAA16500.
GeneIDi947092.
KEGGieco:b2615.
PATRICi32120629. VBIEscCol129921_2713.

Organism-specific databases

EchoBASEiEB2109.
EcoGeneiEG12192. nadK.

Phylogenomic databases

eggNOGiCOG0061.
HOGENOMiHOG000227221.
InParanoidiP0A7B3.
KOiK00858.
OMAiTHEMLYH.
OrthoDBiEOG6PZXDR.
PhylomeDBiP0A7B3.

Enzyme and pathway databases

BioCyciEcoCyc:MONOMER0-541.
ECOL316407:JW2596-MONOMER.
MetaCyc:MONOMER0-541.
BRENDAi2.7.1.23. 2026.

Miscellaneous databases

PROiP0A7B3.

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. "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: July 22, 2015
This is version 92 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

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.