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O58801 (NADK_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Poly(P)-dependent NAD kinase
Short name=PPNK
Gene names
Name:nadK
Ordered Locus Names:PH1074
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length277 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 (GTP,UTP) as well as inorganic polyphosphate (poly(P)) as a source of phosphorus. NAD is the preferred substrate for the kinase, but NADH can also be used as phosphoryl acceptor. Ref.3

Catalytic activity

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

Cofactor

Divalent metal ions. Ref.3

Subunit structure

Homotetramer. Ref.3

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00361.

Sequence similarities

Belongs to the NAD kinase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.29 mM for ATP (at pH 6 and 70 degrees Celsius) Ref.3

KM=0.3 mM for NAD (with poly(P) as phosphoryl donor at pH 6.8 and 70 degrees Celsius)

KM=0.4 mM for NAD (with ATP as phosphoryl donor at pH 6.8 and 70 degrees Celsius)

pH dependence:

Optimum pH is 6.8. At 70 degrees Celsius for 60 minutes, the enzyme does not lose activity in a pH range of 4.0 to 10.5.

Temperature dependence:

Extremely high thermostability. Upon heating at 95 degrees Celsius for 10 minutes the kinase activity is not lost, but about 80% of the activity is lost upon incubation at 100 degrees Celsius for 10 minutes.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
NAD
NADP
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Direct protein sequencing
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.3. Source: UniProtKB

NAD binding

Inferred from direct assay Ref.3. Source: UniProtKB

NAD+ kinase activity

Inferred from direct assay Ref.3. 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 – 277277NAD kinase HAMAP-Rule MF_00361
PRO_0000120707

Regions

Nucleotide binding67 – 682NAD By similarity
Nucleotide binding137 – 1382NAD By similarity
Nucleotide binding178 – 1836NAD By similarity

Sites

Active site671Proton acceptor By similarity
Binding site721NAD By similarity
Binding site1481NAD By similarity
Binding site1651NAD By similarity
Binding site1671NAD By similarity
Binding site1751NAD; via carbonyl oxygen By similarity
Binding site2361NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
O58801 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 707053D67637F13F

FASTA27731,414
        10         20         30         40         50         60 
MKFGIVARRD KEEALKLAYR VYDFLKVHGY EVVVDKETYE HFPHFKEGDV IPLDEFDVDF 

        70         80         90        100        110        120 
IVAIGGDGTI LRIEHMTKKD IPILSINMGT LGFLTEVEPS DTFFALNRLI EGEYYIDERI 

       130        140        150        160        170        180 
KVRTYIDGEN RVPDALNEVA ILTGIPGKII HMKYYVDGGL ADEVRADGLV VSTPTGSTGY 

       190        200        210        220        230        240 
AMSAGGPFID PRLDVILIAP LLPLPKTSVP MVIPGSSRID IRMLTDREII LAIDGQYYEH 

       250        260        270 
LPPNVEITVV KSPRKTKFIR FTREIYPKYT IRIKERH 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3."
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.
DNA Res. 5:55-76(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[2]"Inorganic polyphosphate/ATP-NAD kinase of Pyrococcus horikoshii OT-3."
Ohshima T., Sakuraba H.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[3]"First archaeal inorganic polyphosphate/ATP-dependent NAD kinase, from hyperthermophilic archaeon Pyrococcus horikoshii: cloning, expression, and characterization."
Sakuraba H., Kawakami R., Ohshima T.
Appl. Environ. Microbiol. 71:4352-4358(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, SUBUNIT.
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000001 Genomic DNA. Translation: BAA30173.1.
AB055976 Genomic DNA. Translation: BAB32784.1.
PIRG71101.
RefSeqNP_142982.1. NC_000961.1.

3D structure databases

ProteinModelPortalO58801.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING70601.PH1074.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA30173; BAA30173; BAA30173.
GeneID1443395.
KEGGpho:PH1074.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227222.
KOK00858.
OMAPRKTKFV.

Enzyme and pathway databases

BioCycPHOR70601:GJWR-1066-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...

Entry information

Entry nameNADK_PYRHO
AccessionPrimary (citable) accession number: O58801
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: June 11, 2014
This is version 87 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