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A1W4H1 (NADK_ACISJ) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 52. 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:Ajs_0904
OrganismAcidovorax sp. (strain JS42) [Complete proteome] [HAMAP]
Taxonomic identifier232721 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length298 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 – 298298NAD kinase HAMAP-Rule MF_00361
PRO_1000005389

Regions

Nucleotide binding80 – 812NAD By similarity
Nucleotide binding154 – 1552NAD By similarity
Nucleotide binding195 – 2006NAD By similarity

Sites

Active site801Proton acceptor By similarity
Binding site1821NAD By similarity
Binding site1841NAD By similarity
Binding site2191NAD; via carbonyl oxygen By similarity
Binding site2531NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A1W4H1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 2613E7C2AE714468

FASTA29831,915
        10         20         30         40         50         60 
MKPIFRRVAV IGKYPGPGAV SASDSARQII ESIAQFVTQQ DCELTLEAET AAHTGLTQYH 

        70         80         90        100        110        120 
TLDVEGIGRQ CDLCLVVGGD GTMLGVGRRL AGYGTPLVGI NQGRLGFITD IPLEGYQDAL 

       130        140        150        160        170        180 
TPILHGDYEE DVRPLMQACV MRSGECVFEA LALNDVVVNR GSTSGMVELR VEVDGVFVSN 

       190        200        210        220        230        240 
QRADGLIVAS PTGSTAYALS AGGPMLHPSI PGWVLVPIAP HTLSNRPIVL SDATEVAIEV 

       250        260        270        280        290 
AGGRDISANF DMQSLASLQH GDRILVRRSA HRVCFLHPRG WSYFATLRKK LGWYEGGS 

« Hide

References

[1]"Complete sequence of chromosome 1 of Acidovorax sp. JS42."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JS42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000539 Genomic DNA. Translation: ABM41146.1.
RefSeqYP_985222.1. NC_008782.1.

3D structure databases

ProteinModelPortalA1W4H1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING232721.Ajs_0904.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM41146; ABM41146; Ajs_0904.
GeneID4671215.
KEGGajs:Ajs_0904.
PATRIC20687078. VBIAciSp27161_1093.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227221.
KOK00858.
OMAHPSIPGW.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycASP232721:GHWE-909-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_ACISJ
AccessionPrimary (citable) accession number: A1W4H1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: July 9, 2014
This is version 52 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