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Q8Y8D7 (NADK1_LISMO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. 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 1

EC=2.7.1.23
Alternative name(s):
ATP-dependent NAD kinase
Gene names
Name:nadK1
Ordered Locus Names:lmo0968
OrganismListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]
Taxonomic identifier169963 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length264 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. Ref.2 Ref.3

Catalytic activity

ATP + NAD+ = ADP + NADP+. Ref.2

Cofactor

Divalent metal ions By similarity. HAMAP-Rule MF_00361

Enzyme regulation

Competitively inhibited by 5'-thioacetyladenosine (TAA) and di-(5'-thioadenosine) (DTA). Ref.2 Ref.3

Subunit structure

Homotetramer. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00361.

Sequence similarities

Belongs to the NAD kinase family.

Biophysicochemical properties

Kinetic parameters:

Kcat is 13.78 sec(-1) for kinase activity with ATP (at pH 7.5 and 30 degrees Celsius). Kcat is 13.12 sec(-1) for kinase activity with NAD (at pH 7.5 and 30 degrees Celsius).

KM=2.8 mM for ATP (at pH 7.5 and 30 degrees Celsius) Ref.2

Vmax=6.67 µmol/min/mg enzyme (at pH 7.5 and 30 degrees Celsius)

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
NAD
NADP
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNAD metabolic process

Inferred from electronic annotation. Source: InterPro

NADP biosynthetic process

Inferred from direct assay Ref.3. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from direct assay Ref.2. Source: UniProtKB

NAD binding

Inferred from direct assay Ref.2. Source: UniProtKB

NAD+ kinase activity

Inferred from direct assay Ref.2. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264NAD kinase 1 HAMAP-Rule MF_00361
PRO_0000120632

Regions

Nucleotide binding45 – 462NAD HAMAP-Rule MF_00361
Nucleotide binding122 – 1232NAD HAMAP-Rule MF_00361
Nucleotide binding161 – 1666NAD HAMAP-Rule MF_00361

Sites

Active site451Proton acceptor Ref.2
Binding site461NAD; via amide nitrogen
Binding site1481NAD By similarity
Binding site1501NAD Probable
Binding site1581NAD; via carbonyl oxygen
Binding site2231NAD

Experimental info

Mutagenesis451D → N: Only minor changes in the structure and a 10-fold decrease in the kinase activity. Ref.2
Mutagenesis2231H → E: Twice less active than the wild-type. Its activity toward DTA is increased 2-fold. Ref.2 Ref.3

Secondary structure

.................................................. 264
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8Y8D7 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 00E0BCC4CAD30653

FASTA26429,933
        10         20         30         40         50         60 
MKYMITSKGD EKSDLLRLNM IAGFGEYDME YDDVEPEIVI SIGGDGTFLS AFHQYEERLD 

        70         80         90        100        110        120 
EIAFIGIHTG HLGFYADWRP AEADKLVKLL AKGEYQKVSY PLLKTTVKYG IGKKEATYLA 

       130        140        150        160        170        180 
LNESTVKSSG GPFVVDVVIN DIHFERFRGD GLCMSTPSGT TAYNKSLGGA LMHPSIEAMQ 

       190        200        210        220        230        240 
LTEMASINNR VYRTIGSPLV FPKHHVVSLQ PVNDKDFQIS VDHLSILHRD VQEIRYEVSA 

       250        260 
KKIHFARFRS FPFWRRVHDS FIED 

« Hide

References

« Hide 'large scale' references
[1]"Comparative genomics of Listeria species."
Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. expand/collapse author list , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.
Science 294:849-852(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-679 / EGD-e.
[2]"NAD kinases use substrate-assisted catalysis for specific recognition of NAD."
Poncet-Montange G., Assairi L., Arold S., Pochet S., Labesse G.
J. Biol. Chem. 282:33925-33934(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF WILD-TYPE AND MUTANT ASN-45 IN COMPLEX WITH NAD AND NAD ANALOGS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-45 AND HIS-223, ACTIVE SITE, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[3]"Screening and in situ synthesis using crystals of a NAD kinase lead to a potent antistaphylococcal compound."
Gelin M., Poncet-Montange G., Assairi L., Morellato L., Huteau V., Dugue L., Dussurget O., Pochet S., Labesse G.
Structure 20:1107-1117(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF WILD-TYPE AND MUTANT GLU-223 IN COMPLEX WITH NAD ANALOGS, FUNCTION, MUTAGENESIS OF HIS-223, ENZYME REGULATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591977 Genomic DNA. Translation: CAC99046.1.
PIRAH1195.
RefSeqNP_464493.1. NC_003210.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I1WX-ray2.34A/B/C/D1-264[»]
2I29X-ray2.10A1-264[»]
2I2AX-ray2.10A1-264[»]
2I2BX-ray2.10A1-264[»]
2I2CX-ray1.85A1-264[»]
2I2DX-ray2.22A1-264[»]
2I2FX-ray1.90A1-264[»]
2Q5FX-ray1.90A1-264[»]
3V7UX-ray1.97A1-264[»]
3V7WX-ray2.01A1-264[»]
3V7YX-ray1.97A1-264[»]
3V80X-ray2.03A1-264[»]
3V8MX-ray2.48A1-264[»]
3V8NX-ray2.38A1-264[»]
3V8PX-ray2.29A1-264[»]
3V8QX-ray2.37A1-264[»]
3V8RX-ray2.39A1-264[»]
4DY6X-ray2.20A1-264[»]
ProteinModelPortalQ8Y8D7.
SMRQ8Y8D7. Positions 1-264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING169963.lmo0968.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC99046; CAC99046; CAC99046.
GeneID986453.
KEGGlmo:lmo0968.
PATRIC20311034. VBILisMon69206_0995.

Organism-specific databases

GenoListLMO0968.

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000275803.
KOK00858.
OMAQWITIVP.
OrthoDBEOG6PZXDR.
PhylomeDBQ8Y8D7.

Enzyme and pathway databases

BioCycLMON169963:LMO0968-MONOMER.

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

EvolutionaryTraceQ8Y8D7.

Entry information

Entry nameNADK1_LISMO
AccessionPrimary (citable) accession number: Q8Y8D7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 76 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references