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P0A7B3

- NADK_ECOLI

UniProt

P0A7B3 - NADK_ECOLI

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Protein
NAD kinase
Gene
nadK, yfjB, yfjE, b2615, JW2596
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.3 Publications

Catalytic activityi

ATP + NAD+ = ADP + NADP+.3 Publications

Cofactori

Divalent metal ions.1 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. 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 dependencei

Optimum pH is between 7.2 and 7.5.

Temperature dependencei

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

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi73 – 742NAD By similarity
Nucleotide bindingi147 – 1482NAD By similarity
Nucleotide bindingi188 – 1936NAD By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. NAD metabolic process Source: InterPro
  2. 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.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD kinase (EC:2.7.1.23)
Alternative name(s):
ATP-dependent NAD kinase
Gene namesi
Name:nadK
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 By similarity UniRule annotation

GO - Cellular componenti

  1. 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 kinaseUniRule annotation
PRO_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.

Family & Domainsi

Sequence similaritiesi

Belongs to the NAD kinase family.

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...

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

« 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: June 11, 2014
This is version 83 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