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B9ME57 (NADK_ACIET) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 36. 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:Dtpsy_0833
OrganismAcidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)) [Complete proteome] [HAMAP]
Taxonomic identifier535289 [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_1000133569

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
B9ME57 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 260FFA0A32F1C53C

FASTA29831,885
        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 MRGGECVFEA 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 Diaphorobacter sp. TPSY."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TPSY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001392 Genomic DNA. Translation: ACM32311.1.
RefSeqYP_002552311.1. NC_011992.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING535289.Dtpsy_0833.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM32311; ACM32311; Dtpsy_0833.
GeneID7383528.
KEGGdia:Dtpsy_0833.
PATRIC21778698. VBIDiaSp55748_0860.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227221.
KOK00858.
OMAHPSIPGW.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycAEBR535289:GHOO-838-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_ACIET
AccessionPrimary (citable) accession number: B9ME57
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: July 9, 2014
This is version 36 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