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O31612 (NADK1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ppnKA
Synonyms:nadF, yjbN
Ordered Locus Names:BSU11610
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Catalytic activity

ATP + NAD+ = ADP + NADP+. Ref.2

Cofactor

Divalent metal ions. Both calcium and manganese ions are more effective activators than zinc, cobalt, copper an magnesium ions at low concentrations. Ref.2

Enzyme regulation

Allosterically inhibited by NADP and activated by quinolinic acid. Strongly inhibited by HgCl2. Ref.2

Subunit structure

Homodimer. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00361.

Sequence similarities

Belongs to the NAD kinase family.

Biophysicochemical properties

Kinetic parameters:

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

KM=0.73 mM for NAD (at pH 7.8 and 25 degrees Celsius) Ref.2

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

pH dependence:

Optimum pH is 9.

Temperature dependence:

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

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
NAD
NADP
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNAD metabolic process

Inferred from electronic annotation. Source: InterPro

NADP biosynthetic process

Inferred from direct assay Ref.2. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from direct assay Ref.2. Source: UniProtKB

NAD binding

Inferred from direct assay Ref.2. Source: UniProtKB

NAD+ kinase activity

Inferred from direct assay Ref.2. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 266266NAD kinase 1 HAMAP-Rule MF_00361
PRO_0000120598

Regions

Nucleotide binding45 – 462NAD By similarity
Nucleotide binding122 – 1232NAD By similarity
Nucleotide binding161 – 1666NAD By similarity

Sites

Active site451Proton acceptor By similarity
Binding site1481NAD By similarity
Binding site1501ATP By similarity
Binding site1581NAD; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
O31612 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 82FA00BC6FE53364

FASTA26630,012
        10         20         30         40         50         60 
MKFAVSSKGD QVSDTLKSKI QAYLLDFDME LDENEPEIVI SVGGDGTLLY AFHRYSDRLD 

        70         80         90        100        110        120 
KTAFVGVHTG HLGFYADWVP HEIEKLVLAI AKTPYHTVEY PLLEVIVTYH ENEREERYLA 

       130        140        150        160        170        180 
LNECTIKSIE GSLVADVEIK GQLFETFRGD GLCLSTPSGS TAYNKALGGA IIHPSIRAIQ 

       190        200        210        220        230        240 
LAEMASINNR VFRTVGSPLL LPSHHDCMIK PRNEVDFQVT IDHLTLLHKD VKSIRCQVAS 

       250        260 
EKVRFARFRP FPFWKRVQDS FIGKGE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL009126 Genomic DNA. Translation: CAB13018.1.
PIRF69844.
RefSeqNP_389043.1. NC_000964.3.

3D structure databases

ProteinModelPortalO31612.
SMRO31612. Positions 1-264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU11610.

Proteomic databases

PaxDbO31612.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13018; CAB13018; BSU11610.
GeneID936414.
KEGGbsu:BSU11610.
PATRIC18974039. VBIBacSub10457_1213.

Organism-specific databases

GenoListBSU11610. [Micado]

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000275803.
KOK00858.
OMAIQMSEIA.
OrthoDBEOG6PZXDR.
PhylomeDBO31612.

Enzyme and pathway databases

BioCycBSUB:BSU11610-MONOMER.
SABIO-RKO31612.

Family and domain databases

Gene3D2.60.200.30. 1 hit.
3.40.50.10330. 1 hit.
HAMAPMF_00361. NAD_kinase.
InterProIPR017438. 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]
PANTHERPTHR20275. PTHR20275. 1 hit.
PfamPF01513. NAD_kinase. 1 hit.
[Graphical view]
SUPFAMSSF111331. SSF111331. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNADK1_BACSU
AccessionPrimary (citable) accession number: O31612
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList