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Q72Z91 (NADK2_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 2

EC=2.7.1.23
Alternative name(s):
ATP-dependent NAD kinase 2
Gene names
Name:nadK2
Ordered Locus Names:BCE_4778
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_00361

Catalytic activity

ATP + NAD+ = ADP + NADP+. HAMAP-Rule MF_00361

Cofactor

Divalent metal ions By similarity. HAMAP-Rule MF_00361

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00361.

Sequence similarities

Belongs to the NAD kinase family.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

NADP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

NAD+ kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

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 – 267267NAD kinase 2 HAMAP-Rule MF_00361
PRO_0000229600

Regions

Nucleotide binding52 – 532NAD By similarity
Nucleotide binding124 – 1252NAD By similarity
Nucleotide binding164 – 1696NAD By similarity

Sites

Active site521Proton acceptor By similarity
Binding site1511NAD By similarity
Binding site1531NAD By similarity
Binding site1881NAD; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q72Z91 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 641C15E116374141

FASTA26730,376
        10         20         30         40         50         60 
MADRRNLFFF YGDDKAKLVE KMKPIYRILE ENGFTILDHP KNANAIVSVG DDATFLQAVR 

        70         80         90        100        110        120 
KTGFREDCLY AGISTKDEIS FYCDFHIDHV DIALQEITKN EIEVRKYPTI EVDVDGSTSF 

       130        140        150        160        170        180 
HCLNEFSLRS SIIKTFVVDV HVDNLYFETF RGDGLVVSTP TGSTAYNKSL RGAVVDPLIP 

       190        200        210        220        230        240 
CFQVSELASL NNNTYRTLGS PFILNHERTL TLKLRPDGND YPVIGMDNEA LSIKQVEKAV 

       250        260 
VRLSDKQIKT VKLKNNSFWE KVQRTFL 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017194 Genomic DNA. Translation: AAS43679.1.
RefSeqNP_981071.1. NC_003909.8.

3D structure databases

ProteinModelPortalQ72Z91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING222523.BCE_4778.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS43679; AAS43679; BCE_4778.
GeneID2751078.
KEGGbca:BCE_4778.
PATRIC18858168. VBIBacCer118379_4579.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000275803.
KOK00858.
OMADDLHFET.
OrthoDBEOG6PZXDR.

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 nameNADK2_BACC1
AccessionPrimary (citable) accession number: Q72Z91
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 63 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