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O31612

- NADK1_BACSU

UniProt

O31612 - NADK1_BACSU

Protein

NAD kinase 1

Gene

ppnKA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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.1 PublicationUniRule annotation

    Catalytic activityi

    ATP + NAD+ = ADP + NADP+.1 PublicationUniRule annotation

    Cofactori

    Divalent metal ions. Both calcium and manganese ions are more effective activators than zinc, cobalt, copper an magnesium ions at low concentrations.1 PublicationUniRule annotation

    Enzyme regulationi

    Allosterically inhibited by NADP and activated by quinolinic acid. Strongly inhibited by HgCl2.1 Publication

    Kineticsi

    Kcat is 8 sec(-1) for kinase activity with NAD (at pH 7.8 and 25 degrees Celsius).

    1. KM=0.73 mM for NAD (at pH 7.8 and 25 degrees Celsius)1 Publication

    Vmax=3.82 µmol/min/mg enzyme (at pH 7.8 and 25 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 9.1 Publication

    Temperature dependencei

    Optimum temperature is 35 degrees Celsius. Half of the activity is lost after treatment at 40 degrees Celsius for 15 minutes.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei45 – 451Proton acceptorUniRule annotation
    Binding sitei148 – 1481NADUniRule annotation
    Binding sitei150 – 1501ATPBy similarity
    Binding sitei158 – 1581NAD; via carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi45 – 462NADUniRule annotation
    Nucleotide bindingi122 – 1232NADUniRule annotation
    Nucleotide bindingi161 – 1666NADUniRule 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

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, NAD, NADP, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU11610-MONOMER.
    SABIO-RKO31612.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD kinase 1UniRule 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:ppnKA
    Synonyms:nadF, yjbN
    Ordered Locus Names:BSU11610
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU11610. [Micado]

    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 – 266266NAD kinase 1PRO_0000120598Add
    BLAST

    Proteomic databases

    PaxDbiO31612.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi224308.BSU11610.

    Structurei

    3D structure databases

    ProteinModelPortaliO31612.
    SMRiO31612. Positions 1-264.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the NAD kinase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0061.
    HOGENOMiHOG000275803.
    KOiK00858.
    OMAiIQMSEIA.
    OrthoDBiEOG6PZXDR.
    PhylomeDBiO31612.

    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.
    IPR002504. PolyP/ATP_NADK.
    [Graphical view]
    PANTHERiPTHR20275. PTHR20275. 1 hit.
    PfamiPF01513. NAD_kinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF111331. SSF111331. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O31612-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFAVSSKGD QVSDTLKSKI QAYLLDFDME LDENEPEIVI SVGGDGTLLY    50
    AFHRYSDRLD KTAFVGVHTG HLGFYADWVP HEIEKLVLAI AKTPYHTVEY 100
    PLLEVIVTYH ENEREERYLA LNECTIKSIE GSLVADVEIK GQLFETFRGD 150
    GLCLSTPSGS TAYNKALGGA IIHPSIRAIQ LAEMASINNR VFRTVGSPLL 200
    LPSHHDCMIK PRNEVDFQVT IDHLTLLHKD VKSIRCQVAS EKVRFARFRP 250
    FPFWKRVQDS FIGKGE 266
    Length:266
    Mass (Da):30,012
    Last modified:January 1, 1998 - v1
    Checksum:i82FA00BC6FE53364
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB13018.1.
    PIRiF69844.
    RefSeqiNP_389043.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13018; CAB13018; BSU11610.
    GeneIDi936414.
    KEGGibsu:BSU11610.
    PATRICi18974039. VBIBacSub10457_1213.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL009126 Genomic DNA. Translation: CAB13018.1 .
    PIRi F69844.
    RefSeqi NP_389043.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali O31612.
    SMRi O31612. Positions 1-264.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU11610.

    Proteomic databases

    PaxDbi O31612.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13018 ; CAB13018 ; BSU11610 .
    GeneIDi 936414.
    KEGGi bsu:BSU11610.
    PATRICi 18974039. VBIBacSub10457_1213.

    Organism-specific databases

    GenoListi BSU11610. [Micado ]

    Phylogenomic databases

    eggNOGi COG0061.
    HOGENOMi HOG000275803.
    KOi K00858.
    OMAi IQMSEIA.
    OrthoDBi EOG6PZXDR.
    PhylomeDBi O31612.

    Enzyme and pathway databases

    BioCyci BSUB:BSU11610-MONOMER.
    SABIO-RK O31612.

    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.
    IPR002504. PolyP/ATP_NADK.
    [Graphical view ]
    PANTHERi PTHR20275. PTHR20275. 1 hit.
    Pfami PF01513. NAD_kinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF111331. SSF111331. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    2. "Allosteric regulation of Bacillus subtilis NAD kinase by quinolinic acid."
      Garavaglia S., Galizzi A., Rizzi M.
      J. Bacteriol. 185:4844-4850(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, NOMENCLATURE.
      Strain: 168.

    Entry informationi

    Entry nameiNADK1_BACSU
    AccessioniPrimary (citable) accession number: O31612
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 99 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, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3