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Q58327

- NPPNK_METJA

UniProt

Q58327 - NPPNK_METJA

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
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (01 Jun 1998)
      Previous versions | rss
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    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

    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-SubCell

    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.
    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

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    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

    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 1, 2014
    This is version 94 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