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P0A7B3 (NADK_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NAD kinase

EC=2.7.1.23
Alternative name(s):
ATP-dependent NAD kinase
Gene names
Name:nadK
Synonyms:yfjB, yfjE
Ordered Locus Names:b2615, JW2596
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.9

Catalytic activity

ATP + NAD+ = ADP + NADP+. Ref.6 Ref.7 Ref.9

Cofactor

Divalent metal ions. Ref.6

Enzyme regulation

Competitively and allosterically inhibited by NADH and NADPH at physiological concentrations, whereas inhibition by NADP is only slight. Inhibited by p-chloromercuribenzoate and HgCl2. Ref.6 Ref.7

Subunit structure

Homohexamer. Ref.6

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00361.

Sequence similarities

Belongs to the NAD kinase family.

Biophysicochemical properties

Kinetic parameters:

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

KM=2 mM for NAD (at pH 7 and 37 degrees Celsius) Ref.6 Ref.7 Ref.9

KM=2.5 mM for ATP (at pH 7 and 37 degrees Celsius)

KM=4.1 mM for magnesium (at pH 7 and 37 degrees Celsius)

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

pH dependence:

Optimum pH is between 7.2 and 7.5.

Temperature dependence:

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

Sequence caution

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 292292NAD kinase HAMAP-Rule MF_00361
PRO_0000120616

Regions

Nucleotide binding73 – 742NAD By similarity
Nucleotide binding147 – 1482NAD By similarity
Nucleotide binding188 – 1936NAD By similarity

Sites

Active site731Proton acceptor By similarity
Binding site1581NAD By similarity
Binding site1751NAD By similarity
Binding site1771NAD By similarity
Binding site1851NAD; via carbonyl oxygen By similarity
Binding site2471NAD By similarity
Site1751Responsible for conferring strict specificity to NAD

Experimental info

Mutagenesis1751R → E: Does not exhibit NADH kinase activity in addition to NAD kinase activity. Ref.9
Mutagenesis1751R → G: Exhibits NADH kinase activity in addition to NAD kinase activity. Reduces the Vmax of the NAD kinase activity. Ref.9
Mutagenesis1751R → H: Exhibits NADH kinase activity in addition to NAD kinase activity. Ref.9
Mutagenesis1751R → I: Does not exhibit NADH kinase activity in addition to NAD kinase activity. Ref.9
Mutagenesis1751R → K: Does not exhibit NADH kinase activity in addition to NAD kinase activity. Ref.9
Mutagenesis1751R → Q: Exhibits NADH kinase activity in addition to NAD kinase activity. Ref.9
Mutagenesis1751R → T: Exhibits NADH kinase activity in addition to NAD kinase activity. Ref.9

Sequences

Sequence LengthMass (Da)Tools
P0A7B3 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: D1E631658408F2E1

FASTA29232,566
        10         20         30         40         50         60 
MNNHFKCIGI VGHPRHPTAL TTHEMLYRWL CTKGYEVIVE QQIAHELQLK NVKTGTLAEI 

        70         80         90        100        110        120 
GQLADLAVVV GGDGNMLGAA RTLARYDIKV IGINRGNLGF LTDLDPDNAQ QQLADVLEGH 

       130        140        150        160        170        180 
YISEKRFLLE AQVCQQDCQK RISTAINEVV LHPGKVAHMI EFEVYIDEIF AFSQRSDGLI 

       190        200        210        220        230        240 
ISTPTGSTAY SLSAGGPILT PSLDAITLVP MFPHTLSARP LVINSSSTIR LRFSHRRNDL 

       250        260        270        280        290 
EISCDSQIAL PIQEGEDVLI RRCDYHLNLI HPKDYSYFNT LSTKLGWSKK LF 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB65040.
RefSeqNP_417105.1. NC_000913.3.
YP_490837.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0A7B3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid851428. 4 interactions.
DIPDIP-48103N.
IntActP0A7B3. 3 interactions.
STRING511145.b2615.

Proteomic databases

PaxDbP0A7B3.
PRIDEP0A7B3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75664; AAC75664; b2615.
BAA16500; BAA16500; BAA16500.
GeneID12931613.
947092.
KEGGecj:Y75_p2562.
eco:b2615.
PATRIC32120629. VBIEscCol129921_2713.

Organism-specific databases

EchoBASEEB2109.
EcoGeneEG12192. nadK.

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227221.
KOK00858.
OMATHEMLYH.
OrthoDBEOG6PZXDR.
PhylomeDBP0A7B3.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0A7B3.

Family and domain databases

Gene3D2.60.200.30. 1 hit.
3.40.50.10330. 1 hit.
HAMAPMF_00361. NAD_kinase.
InterProIPR017438. 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]
PANTHERPTHR20275. PTHR20275. 1 hit.
PfamPF01513. NAD_kinase. 1 hit.
[Graphical view]
SUPFAMSSF111331. SSF111331. 1 hit.
ProtoNetSearch...

Other

PROP0A7B3.

Entry information

Entry nameNADK_ECOLI
AccessionPrimary (citable) accession number: P0A7B3
Secondary accession number(s): P37768, P46140, P77490
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: June 11, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene