Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q58327

- NPPNK_METJA

UniProt

Q58327 - NPPNK_METJA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 PublicationUniRule annotation
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)1 Publication

Vmax=93.4 µmol/min/mg enzyme toward ATP (for kinase activity at pH 8.5 and at 85 degrees Celsius)1 Publication

Vmax=99.2 µmol/min/mg enzyme toward NAD (for kinase activity at pH 8.5 and at 85 degrees Celsius)1 Publication

Vmax=212 µmol/min/mg enzyme toward NADP (for phosphatase activity at pH 8.5 and at 85 degrees Celsius)1 Publication

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

Vmax=236 µmol/min/mg enzyme toward NADPH (for phosphatase activity at pH 8.5 and at 85 degrees Celsius)1 Publication

Temperature dependencei

Optimum temperature is 100 degrees Celsius for phosphatase and kinase activies. Both are inactive below 60 degrees Celsius.1 Publication

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi362 – 3632NADUniRule annotation
Nucleotide bindingi436 – 4372NADUniRule annotation
Nucleotide bindingi477 – 4826NADUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. dephosphorylation Source: GOC
  2. lysine metabolic process Source: InterPro
  3. NAD metabolic process Source: InterPro
  4. NADP biosynthetic process Source: UniProtKB
  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 kinaseUniRule annotation (EC:2.7.1.23UniRule annotation)
Alternative name(s):
ATP-dependent NAD kinaseUniRule annotation
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 UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 574574Bifunctional NADP phosphatase/NAD kinasePRO_0000120700Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi243232.MJ0917.

Structurei

3D structure databases

ProteinModelPortaliQ58327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 297297NADP phosphataseAdd
BLAST
Regioni302 – 574273NAD kinaseAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0061.
InParanoidiQ58327.
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

        10         20         30         40         50
MVIMEGFKIA MKVIDEIDKK IKPLIGWEKA DEVVKIGADG TPTKRIDVIA
60 70 80 90 100
ENMAINILEK FSGGILISEE IGLKVVGDEL EYIFILDPID GTYNALKSIP
110 120 130 140 150
IYSTSIAVAK IKGEDKKLIR ENINNIDWIK SFIANKYTIN DLYVGIVKNL
160 170 180 190 200
ATGDLYYAIK GEGSFLEKDG EKIKIETKNI KDLKEASVGL FVYGLSNDLL
210 220 230 240 250
EFLKERKVRR VRLFGSMALE MCYVVSGALD AYINVNENSR LCDIAGAYVI
260 270 280 290 300
CREGNAIVTN KNGKPLNMKL HLMERTSLIV SNKYLHKKLI ALFGNRWIIK
310 320 330 340 350
PVKFGIVVRE DKEEAINLAI EICKYLKDKN IPFCVEDFLR ERVGGDKFDI
360 370 380 390 400
SAISHIIAIG GDGTILRASR LVNGETIPII AVNMGKVGFL AEFCKDEVFE
410 420 430 440 450
IIDKVIYGEY EIEKRSKLSC KIIKDNRVIK TPSALNEMVV ITKNPAKILE
460 470 480 490 500
FDVYVNDTLV ENVRADGIIV STPTGSTAYS LSAGGPIVEP NVDCFIISPI
510 520 530 540 550
CPFKLSSRPL VISASNRIKL KLKLEKPALL VIDGSVEYEI NKDDELIFEK
560 570
SDSYAYFVKG QSFYNKLSRC LGIK
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.
InParanoidi Q58327.
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: October 29, 2014
This is version 95 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 (PubMed:16192277).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