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A9KG94 (NADK_COXBN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 49. 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

EC=2.7.1.23
Alternative name(s):
ATP-dependent NAD kinase
Gene names
Name:nadK
Ordered Locus Names:CBUD_1384
OrganismCoxiella burnetii (strain Dugway 5J108-111) [Complete proteome] [HAMAP]
Taxonomic identifier434922 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length299 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 – 299299NAD kinase HAMAP-Rule MF_00361
PRO_1000079486

Regions

Nucleotide binding78 – 792NAD By similarity
Nucleotide binding151 – 1522NAD By similarity
Nucleotide binding192 – 1976NAD By similarity

Sites

Active site781Proton acceptor By similarity
Binding site1621NAD By similarity
Binding site1791NAD By similarity
Binding site1811NAD By similarity
Binding site2521NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A9KG94 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 3EE43037906FED0F

FASTA29932,892
        10         20         30         40         50         60 
MLKIVSKPSF NRIALMGREG VEGVPETLAA LKDYLVSLNR EVILEENAAH MIDGSRLLTV 

        70         80         90        100        110        120 
PANDLKKKAD LLIVVGGDGS LLNAAHIAVP QQLPVLGINR GRLGFLTDIP PNELTQISDI 

       130        140        150        160        170        180 
LDGHYREEVR FLLEGTVEEG DEIVAQGIAL NDIVLLPGNA PKMIEFDIFI NDEFVCNQRA 

       190        200        210        220        230        240 
DGLIITTPTG STAYALSGGG PILHPQLNAM ALVPMFPHTL SSRPIVVDAE SQIKITISPE 

       250        260        270        280        290 
NDVSPYVSND GQERVSIKPG GNVYTRKYHY PLHLIHPTDY NYYDTLRRKL DWEKRAAKV 

« Hide

References

[1]"Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Dugway 5J108-111.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000733 Genomic DNA. Translation: ABS78008.1.
RefSeqYP_001424736.1. NC_009727.1.

3D structure databases

ProteinModelPortalA9KG94.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING434922.CBUD_1384.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS78008; ABS78008; CBUD_1384.
GeneID5458897.
KEGGcbd:CBUD_1384.
PATRIC17922585. VBICoxBur32972_1385.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227221.
KOK00858.
OMATHEMLYH.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycCBUR434922:GJTP-1469-MONOMER.

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 nameNADK_COXBN
AccessionPrimary (citable) accession number: A9KG94
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: July 9, 2014
This is version 49 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