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Q58327

- NPPNK_METJA

UniProt

Q58327 - NPPNK_METJA

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Protein
Bifunctional NADP phosphatase/NAD kinase
Gene
MJ0917
Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + NAD+ = ADP + NADP+.1 Publication
NADP+ + H2O = NAD+ + phosphate.1 Publication

Cofactori

Magnesium. NAD and pNPPase kinase show maximum activities at 50 and 20mM magnesium, respectively.1 Publication

Enzyme regulationi

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.1 Publication

Kineticsi

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.

  1. KM=0.35 mM for ATP (for kinase activity at pH 8.5 and at 85 degrees Celsius)1 Publication
  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 dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi69 – 691Magnesium 1 By similarity
Metal bindingi87 – 871Magnesium 1 By similarity
Metal bindingi87 – 871Magnesium 2 By similarity
Metal bindingi90 – 901Magnesium 2 By similarity
Binding sitei90 – 901Substrate By similarity
Metal bindingi243 – 2431Magnesium 2 By similarity
Active sitei362 – 3621Proton acceptor By similarity
Binding sitei367 – 3671NAD By similarity
Binding sitei447 – 4471NAD By similarity
Binding sitei464 – 4641NAD By similarity
Binding sitei466 – 4661NAD By similarity
Binding sitei474 – 4741NAD; via carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi362 – 3632NAD By similarity
Nucleotide bindingi436 – 4372NAD By similarity
Nucleotide bindingi477 – 4826NAD By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. NAD binding Source: UniProtKB
  3. NAD+ kinase activity Source: UniProtKB
  4. NADP phosphatase activity Source: UniProtKB
  5. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. NAD metabolic process Source: InterPro
  2. NADP biosynthetic process Source: UniProtKB
  3. dephosphorylation Source: GOC
  4. lysine metabolic process Source: InterPro
  5. phosphatidylinositol phosphorylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, NAD, NADP, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional NADP phosphatase/NAD kinase
Including the following 2 domains:
NAD kinase (EC:2.7.1.23)
Alternative name(s):
ATP-dependent NAD kinase
Poly(P)-dependent NAD kinase
Short name:
PPNK
NADP phosphatase (EC:3.1.3.-)
Short name:
NADPase
Short name:
pNPPase
Gene namesi
Ordered Locus Names:MJ0917
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
ProteomesiUP000000805: Chromosome

Subcellular locationi

Cytoplasm By similarity 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 – 574574Bifunctional NADP phosphatase/NAD kinaseUniRule annotation
PRO_0000120700Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi243232.MJ0917.

Structurei

3D structure databases

ProteinModelPortaliQ58327.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 297297NADP phosphataseUniRule annotation
Add
BLAST
Regioni302 – 574273NAD kinaseUniRule annotation
Add
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0061.
KOiK00858.
OMAiVIVPICP.

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.
IPR021175. Bifunctional_PpnK_predicted.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR002504. PolyP/ATP_NADK.
[Graphical view]
PANTHERiPTHR20275. PTHR20275. 1 hit.
PfamiPF00459. Inositol_P. 2 hits.
PF01513. NAD_kinase. 1 hit.
[Graphical view]
PIRSFiPIRSF036641. Bifunctional_PpnK_predicted. 1 hit.
PRINTSiPR00377. IMPHPHTASES.
SUPFAMiSSF111331. SSF111331. 1 hit.
PROSITEiPS00629. IMP_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q58327-1 [UniParc]FASTAAdd to Basket

« Hide

MVIMEGFKIA MKVIDEIDKK IKPLIGWEKA DEVVKIGADG TPTKRIDVIA    50
ENMAINILEK FSGGILISEE IGLKVVGDEL EYIFILDPID GTYNALKSIP 100
IYSTSIAVAK IKGEDKKLIR ENINNIDWIK SFIANKYTIN DLYVGIVKNL 150
ATGDLYYAIK GEGSFLEKDG EKIKIETKNI KDLKEASVGL FVYGLSNDLL 200
EFLKERKVRR VRLFGSMALE MCYVVSGALD AYINVNENSR LCDIAGAYVI 250
CREGNAIVTN KNGKPLNMKL HLMERTSLIV SNKYLHKKLI ALFGNRWIIK 300
PVKFGIVVRE DKEEAINLAI EICKYLKDKN IPFCVEDFLR ERVGGDKFDI 350
SAISHIIAIG GDGTILRASR LVNGETIPII AVNMGKVGFL AEFCKDEVFE 400
IIDKVIYGEY EIEKRSKLSC KIIKDNRVIK TPSALNEMVV ITKNPAKILE 450
FDVYVNDTLV ENVRADGIIV STPTGSTAYS LSAGGPIVEP NVDCFIISPI 500
CPFKLSSRPL VISASNRIKL KLKLEKPALL VIDGSVEYEI NKDDELIFEK 550
SDSYAYFVKG QSFYNKLSRC LGIK 574
Length:574
Mass (Da):64,119
Last modified:June 1, 1998 - v2
Checksum:i89A1AF944BD99DB1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L77117 Genomic DNA. Translation: AAB98922.1.
PIRiE64414.
RefSeqiNP_247912.1. NC_000909.1.
WP_010870431.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB98922; AAB98922; MJ_0917.
GeneIDi1451806.
KEGGimja:MJ_0917.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L77117 Genomic DNA. Translation: AAB98922.1 .
PIRi E64414.
RefSeqi NP_247912.1. NC_000909.1.
WP_010870431.1. NC_000909.1.

3D structure databases

ProteinModelPortali Q58327.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243232.MJ0917.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB98922 ; AAB98922 ; MJ_0917 .
GeneIDi 1451806.
KEGGi mja:MJ_0917.

Phylogenomic databases

eggNOGi COG0061.
KOi K00858.
OMAi VIVPICP.

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.
IPR021175. Bifunctional_PpnK_predicted.
IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR002504. PolyP/ATP_NADK.
[Graphical view ]
PANTHERi PTHR20275. PTHR20275. 1 hit.
Pfami PF00459. Inositol_P. 2 hits.
PF01513. NAD_kinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036641. Bifunctional_PpnK_predicted. 1 hit.
PRINTSi PR00377. IMPHPHTASES.
SUPFAMi SSF111331. SSF111331. 1 hit.
PROSITEi PS00629. IMP_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiNPPNK_METJA
AccessioniPrimary (citable) accession number: Q58327
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: June 1, 1998
Last modified: September 3, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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 (1 Publication).

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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