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B1JW12 (NADK_BURCC) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 44. 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:Bcenmc03_0714
OrganismBurkholderia cenocepacia (strain MC0-3) [Complete proteome] [HAMAP]
Taxonomic identifier406425 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length300 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 – 300300NAD kinase HAMAP-Rule MF_00361
PRO_1000120833

Regions

Nucleotide binding75 – 762NAD By similarity
Nucleotide binding149 – 1502NAD By similarity
Nucleotide binding190 – 1956NAD By similarity

Sites

Active site751Proton acceptor By similarity
Binding site1771NAD By similarity
Binding site1791NAD By similarity
Binding site2141NAD; via carbonyl oxygen By similarity
Binding site2481NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
B1JW12 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: B46096E4B0D37A9B

FASTA30032,290
        10         20         30         40         50         60 
MKTGNQFKTV ALVGRSNTPG IAEPLATLAD SIATLGFEVV FEGDTAREIG IAGYPALTPA 

        70         80         90        100        110        120 
EIGARADVAI VLGGDGTMLG IGRQLAPYRT PLIGINHGRL GFITDIAASD MQALVPVMLA 

       130        140        150        160        170        180 
GKFEREERSL LEARIVRDGE PIYHALAFND VVVNRSGFSG MVELRASVDG RYMYNQRSDG 

       190        200        210        220        230        240 
LIVATPTGST AYALSSAGPI LHPQLAGIVL VPIAPHALSN RPIVLPDDSK IAIQIVGGRD 

       250        260        270        280        290        300 
VNVNFDMQSF TSLELNDTIE VRRSKHTVPF LHPIGYSYYT TLRKKLHWNE HASNEDDKAS 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3."
Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Tiedje J., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC0-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000958 Genomic DNA. Translation: ACA89892.1.
RefSeqYP_001764014.1. NC_010508.1.

3D structure databases

ProteinModelPortalB1JW12.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING406425.Bcenmc03_0714.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA89892; ACA89892; Bcenmc03_0714.
GeneID6122395.
KEGGbcm:Bcenmc03_0714.
PATRIC19088404. VBIBurCen61509_0738.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227221.
KOK00858.
OMATHEMLYH.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycBCEN406425:GHD9-737-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_BURCC
AccessionPrimary (citable) accession number: B1JW12
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: July 9, 2014
This is version 44 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