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O31612

- NADK1_BACSU

UniProt

O31612 - NADK1_BACSU

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Protein
NAD kinase 1
Gene
ppnKA, nadF, yjbN, BSU11610
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 Publication

Catalytic activityi

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

Cofactori

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

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)

pH dependencei

Optimum pH is 9.

Temperature dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei45 – 451Proton acceptor By similarity
Binding sitei148 – 1481NAD By similarity
Binding sitei150 – 1501ATP By similarity
Binding sitei158 – 1581NAD; via carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi45 – 462NAD By similarity
Nucleotide bindingi122 – 1232NAD By similarity
Nucleotide bindingi161 – 1666NAD By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. NAD binding Source: UniProtKB
  3. NAD+ kinase activity Source: UniProtKB
  4. metal ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. NAD metabolic process Source: InterPro
  2. NADP biosynthetic process Source: UniProtKB
Complete GO annotation...

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 1 (EC:2.7.1.23)
Alternative name(s):
ATP-dependent NAD kinase
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 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 – 266266NAD kinase 1UniRule annotation
PRO_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.

Family & Domainsi

Sequence similaritiesi

Belongs to the NAD kinase family.

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 98 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

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