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A9BHU3 (NADK_PETMO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 43. 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:Pmob_1354
OrganismPetrotoga mobilis (strain DSM 10674 / SJ95) [Complete proteome] [HAMAP]
Taxonomic identifier403833 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaePetrotoga

Protein attributes

Sequence length274 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 – 274274NAD kinase HAMAP-Rule MF_00361
PRO_1000079504

Regions

Nucleotide binding59 – 602NAD By similarity
Nucleotide binding128 – 1292NAD By similarity
Nucleotide binding169 – 1746NAD By similarity

Sites

Active site591Proton acceptor By similarity
Binding site641NAD By similarity
Binding site1581NAD By similarity
Binding site1931NAD; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A9BHU3 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: FBF25E5E4621BAB1

FASTA27430,017
        10         20         30         40         50         60 
MKIFIFYNPL KLSNDDLEEN ILKPFNESNI EVIGYAAAGS TVEEKQAQVA DFFVIFGGDG 

        70         80         90        100        110        120 
TVLKIAEIAA IFSKPVIAVN TGNLGFLSSY SSSEIKELIE DIQKENISFS FRHLLECHVG 

       130        140        150        160        170        180 
TKKVVVLNDI VLLKSQPLGT MNVDVKIEEH TLFSFAGDGL IVSTPTGSTA YALSAGGPII 

       190        200        210        220        230        240 
HPELNVVQLI PLAAHALNIR PFIAPPTQRI EIILKNMSKG FVYVTGDGDI IHRMEPGMSI 

       250        260        270 
FVTSSEMTIK LAQRNGNNYL NALDKKLGFG RRFE 

« Hide

References

[1]"Complete sequence of Petroga mobilis SJ95."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Noll K., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 10674 / SJ95.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000879 Genomic DNA. Translation: ABX32058.1.
RefSeqYP_001568381.1. NC_010003.1.

3D structure databases

ProteinModelPortalA9BHU3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING403833.Pmob_1354.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX32058; ABX32058; Pmob_1354.
GeneID5758165.
KEGGpmo:Pmob_1354.
PATRIC22920450. VBIPetMob40494_1447.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
KOK00858.
OMANLSERGP.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycPMOB403833:GH51-1389-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_PETMO
AccessionPrimary (citable) accession number: A9BHU3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 15, 2008
Last modified: July 9, 2014
This is version 43 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