Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q58327 (NPPNK_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. 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:
Bifunctional NADP phosphatase/NAD kinase

Including the following 2 domains:

  1. NAD kinase
    EC=2.7.1.23
    Alternative name(s):
    ATP-dependent NAD kinase
    Poly(P)-dependent NAD kinase
    Short name=PPNK
  2. NADP phosphatase
    Short name=NADPase
    Short name=pNPPase
    EC=3.1.3.-
Gene names
Ordered Locus Names:MJ0917
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the regulation of the intracellular balance between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of NADP. Catalyzes the phosphorylation and dephosphorylation of NAD and NADP, respectively. Although it shows conflicting dual activities and is able to supply NADP, it seems that its physiological role is to prevent excess accumulation of NADP. Kinase can use ATP and other nucleoside triphosphates (UTP, TTP, CTP, GTP) as well as inorganic polyphosphate (poly(P)) as phosphoryl donors, however poly(P) is not considered to be the physiological phosphoryl donor. NAD is the preferred substrate for the kinase, but NADH can also be used as phosphoryl acceptor. Phosphatase can use NADP or NADPH as phosphoryl donor, but NADP is the preferred substrate. Phosphatase also has an activity toward the terminal phosphate group at C-2 of adenosine in 2'-AMP and toward the phosphate group at C-1 of fructose 1,6-bisphosphate, but not toward inositol 1-phosphate. Ref.2

Catalytic activity

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

NADP+ + H2O = NAD+ + phosphate. Ref.2

Cofactor

Magnesium. NAD and pNPPase kinase show maximum activities at 50 and 20mM magnesium, respectively. Ref.2

Enzyme regulation

Phosphatase activity is slightly inhibited by ADP, NADPH and ATP, and moderately inhibited by NAD and 5'-AMP. Kinase activity is slightly inhibited by ADP and NADP. Ref.2

Subunit structure

Homotetramer. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00361.

Miscellaneous

The phosphatase is inert toward the substrates of NAD kinase (NAD, NADH, ATP, and poly(P)). This demonstrates that the phosphatase activity never interferes with the NAD kinase activity by degrading its substrates (Ref.2).

Sequence similarities

In the N-terminal section; belongs to the inositol monophosphatase family.

In the C-terminal section; belongs to the NAD kinase family.

Biophysicochemical properties

Kinetic parameters:

Kcat is 399 sec(-1) for kinase activity with ATP as substrate. Kcat is 424 sec(-1) for kinase activity with NAD as substrate. Kcat is 906 sec(-1) for phosphatase activity with fructose 1,6-bisphosphate and NADP as substrates. Kcat is 1007 sec(-1) for phosphatase activity with NADPH as substrate.

KM=0.35 mM for ATP (for kinase activity at pH 8.5 and at 85 degrees Celsius) Ref.2

KM=3 mM for NAD (for kinase activity at pH 8.5 and at 85 degrees Celsius)

Vmax=93.4 µmol/min/mg enzyme toward ATP (for kinase activity at pH 8.5 and at 85 degrees Celsius)

Vmax=99.2 µmol/min/mg enzyme toward NAD (for kinase activity at pH 8.5 and at 85 degrees Celsius)

Vmax=212 µmol/min/mg enzyme toward NADP (for phosphatase activity at pH 8.5 and at 85 degrees Celsius)

Vmax=212 µmol/min/mg enzyme toward fructose 1,6-bisphosphate (for phosphatase activity at pH 8.5 and at 85 degrees Celsius)

Vmax=236 µmol/min/mg enzyme toward NADPH (for phosphatase activity at pH 8.5 and at 85 degrees Celsius)

Temperature dependence:

Optimum temperature is 100 degrees Celsius for phosphatase and kinase activies. Both are inactive below 60 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 574574Bifunctional NADP phosphatase/NAD kinase HAMAP-Rule MF_00361
PRO_0000120700

Regions

Nucleotide binding362 – 3632NAD By similarity
Nucleotide binding436 – 4372NAD By similarity
Nucleotide binding477 – 4826NAD By similarity
Region1 – 297297NADP phosphatase HAMAP-Rule MF_00361
Region302 – 574273NAD kinase HAMAP-Rule MF_00361

Sites

Active site3621Proton acceptor By similarity
Metal binding691Magnesium 1 By similarity
Metal binding871Magnesium 1 By similarity
Metal binding871Magnesium 2 By similarity
Metal binding901Magnesium 2 By similarity
Metal binding2431Magnesium 2 By similarity
Binding site901Substrate By similarity
Binding site3671NAD By similarity
Binding site4471NAD By similarity
Binding site4641NAD By similarity
Binding site4661NAD By similarity
Binding site4741NAD; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q58327 [UniParc].

Last modified June 1, 1998. Version 2.
Checksum: 89A1AF944BD99DB1

FASTA57464,119
        10         20         30         40         50         60 
MVIMEGFKIA MKVIDEIDKK IKPLIGWEKA DEVVKIGADG TPTKRIDVIA ENMAINILEK 

        70         80         90        100        110        120 
FSGGILISEE IGLKVVGDEL EYIFILDPID GTYNALKSIP IYSTSIAVAK IKGEDKKLIR 

       130        140        150        160        170        180 
ENINNIDWIK SFIANKYTIN DLYVGIVKNL ATGDLYYAIK GEGSFLEKDG EKIKIETKNI 

       190        200        210        220        230        240 
KDLKEASVGL FVYGLSNDLL EFLKERKVRR VRLFGSMALE MCYVVSGALD AYINVNENSR 

       250        260        270        280        290        300 
LCDIAGAYVI CREGNAIVTN KNGKPLNMKL HLMERTSLIV SNKYLHKKLI ALFGNRWIIK 

       310        320        330        340        350        360 
PVKFGIVVRE DKEEAINLAI EICKYLKDKN IPFCVEDFLR ERVGGDKFDI SAISHIIAIG 

       370        380        390        400        410        420 
GDGTILRASR LVNGETIPII AVNMGKVGFL AEFCKDEVFE IIDKVIYGEY EIEKRSKLSC 

       430        440        450        460        470        480 
KIIKDNRVIK TPSALNEMVV ITKNPAKILE FDVYVNDTLV ENVRADGIIV STPTGSTAYS 

       490        500        510        520        530        540 
LSAGGPIVEP NVDCFIISPI CPFKLSSRPL VISASNRIKL KLKLEKPALL VIDGSVEYEI 

       550        560        570 
NKDDELIFEK SDSYAYFVKG QSFYNKLSRC LGIK 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii."
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. expand/collapse author list , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]"MJ0917 in archaeon Methanococcus jannaschii is a novel NADP phosphatase/NAD kinase."
Kawai S., Fukuda C., Mukai T., Murata K.
J. Biol. Chem. 280:39200-39207(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-8, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB98922.1.
PIRE64414.
RefSeqNP_247912.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ58327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ0917.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB98922; AAB98922; MJ_0917.
GeneID1451806.
KEGGmja:MJ_0917.

Phylogenomic databases

eggNOGCOG0061.
KOK00858.
OMAVIVPICP.

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.
IPR021175. Bifunctional_PpnK_predicted.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR002504. PolyP/ATP_NADK.
[Graphical view]
PANTHERPTHR20275. PTHR20275. 1 hit.
PfamPF00459. Inositol_P. 2 hits.
PF01513. NAD_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF036641. Bifunctional_PpnK_predicted. 1 hit.
PRINTSPR00377. IMPHPHTASES.
SUPFAMSSF111331. SSF111331. 1 hit.
PROSITEPS00629. IMP_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNPPNK_METJA
AccessionPrimary (citable) accession number: Q58327
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 92 of the entry and version 2 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

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names