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Protein

NAD kinase

Gene

nadK

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
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 (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.UniRule annotation1 Publication

Catalytic activityi

ATP + NAD+ = ADP + NADP+.UniRule annotation1 Publication

Cofactori

a divalent metal cationUniRule annotation1 Publication

Kineticsi

  1. KM=0.29 mM for ATP (at pH 6 and 70 degrees Celsius)1 Publication
  2. KM=0.3 mM for NAD (with poly(P) as phosphoryl donor at pH 6.8 and 70 degrees Celsius)1 Publication
  3. KM=0.4 mM for NAD (with ATP as phosphoryl donor at pH 6.8 and 70 degrees Celsius)1 Publication

pH dependencei

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 10.5.1 Publication

Temperature dependencei

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei67 – 671Proton acceptorUniRule annotation
Binding sitei72 – 721NADUniRule annotation
Binding sitei148 – 1481NADUniRule annotation
Binding sitei165 – 1651NADUniRule annotation
Binding sitei167 – 1671NADUniRule annotation
Binding sitei175 – 1751NAD; via carbonyl oxygenUniRule annotation
Binding sitei236 – 2361NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi67 – 682NADUniRule annotation
Nucleotide bindingi137 – 1382NADUniRule annotation
Nucleotide bindingi178 – 1836NADUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. NAD metabolic process Source: InterPro
  2. NADP biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, NAD, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1066-MONOMER.
BRENDAi2.7.1.23. 5244.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD kinaseUniRule annotation (EC:2.7.1.23UniRule annotation)
Alternative name(s):
ATP-dependent NAD kinaseUniRule annotation
Poly(P)-dependent NAD kinase
Short name:
PPNK
Gene namesi
Name:nadKUniRule annotation
Ordered Locus Names:PH1074
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000000752 Componenti: Chromosome

Subcellular locationi

  1. Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 277277NAD kinasePRO_0000120707Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi70601.PH1074.

Family & Domainsi

Sequence similaritiesi

Belongs to the NAD kinase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0061.
HOGENOMiHOG000227222.
KOiK00858.
OMAiLAINCGR.

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.

O58801-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFGIVARRD KEEALKLAYR VYDFLKVHGY EVVVDKETYE HFPHFKEGDV
60 70 80 90 100
IPLDEFDVDF IVAIGGDGTI LRIEHMTKKD IPILSINMGT LGFLTEVEPS
110 120 130 140 150
DTFFALNRLI EGEYYIDERI KVRTYIDGEN RVPDALNEVA ILTGIPGKII
160 170 180 190 200
HMKYYVDGGL ADEVRADGLV VSTPTGSTGY AMSAGGPFID PRLDVILIAP
210 220 230 240 250
LLPLPKTSVP MVIPGSSRID IRMLTDREII LAIDGQYYEH LPPNVEITVV
260 270
KSPRKTKFIR FTREIYPKYT IRIKERH
Length:277
Mass (Da):31,414
Last modified:August 1, 1998 - v1
Checksum:i707053D67637F13F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30173.1.
AB055976 Genomic DNA. Translation: BAB32784.1.
PIRiG71101.
RefSeqiNP_142982.1. NC_000961.1.
WP_010885160.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA30173; BAA30173; BAA30173.
GeneIDi1443395.
KEGGipho:PH1074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30173.1.
AB055976 Genomic DNA. Translation: BAB32784.1.
PIRiG71101.
RefSeqiNP_142982.1. NC_000961.1.
WP_010885160.1. NC_000961.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH1074.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA30173; BAA30173; BAA30173.
GeneIDi1443395.
KEGGipho:PH1074.

Phylogenomic databases

eggNOGiCOG0061.
HOGENOMiHOG000227222.
KOiK00858.
OMAiLAINCGR.

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1066-MONOMER.
BRENDAi2.7.1.23. 5244.

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. 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.

Entry informationi

Entry nameiNADK_PYRHO
AccessioniPrimary (citable) accession number: O58801
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: April 29, 2015
This is version 94 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

Documents

  1. 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.