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Q6MII5 (NADK_BDEBA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 61. 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:Bd3172
OrganismBdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) [Complete proteome] [HAMAP]
Taxonomic identifier264462 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaBdellovibrionalesBdellovibrionaceaeBdellovibrio

Protein attributes

Sequence length303 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 – 303303NAD kinase HAMAP-Rule MF_00361
PRO_0000229610

Regions

Nucleotide binding85 – 862NAD By similarity
Nucleotide binding159 – 1602NAD By similarity

Sites

Active site851Proton acceptor By similarity
Binding site901NAD By similarity
Binding site1871NAD By similarity
Binding site1891NAD By similarity
Binding site2241NAD; via carbonyl oxygen By similarity
Binding site2591NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6MII5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 4DBF66BB2D940451

FASTA30333,807
        10         20         30         40         50         60 
MKKSSMDKEH KQSKLVLKEN GSIGLVYRLE TAQAVSLAKK VAEFLKERGF EVFTCPDQKV 

        70         80         90        100        110        120 
VAGTKAAKTK KHMDDLKLVI VLGGDGTYLR AVRLLEGRSV PILGFNMGSL GFLTAHSADS 

       130        140        150        160        170        180 
CFDIIEKTLE GKMVQRPRSM IYSKILRKGK VRAEYHALND MVIERGSMSQ LINTAIYSEK 

       190        200        210        220        230        240 
FLVSQVKADG FIVASPSGST AYNLAAGGPI CHPESPVFVV TPVAPHSLTS RPLLFPDDRE 

       250        260        270        280        290        300 
LSFRLEGKTQ KAHFIVDGQK MTELTADDEV IVSRSCYDHW MVREANHNYF HLLREKLKFG 


DRN 

« Hide

References

[1]"A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective."
Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C.
Science 303:689-692(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15356 / DSM 50701 / NCIB 9529 / HD100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842654 Genomic DNA. Translation: CAE80928.1.
RefSeqNP_969935.1. NC_005363.1.

3D structure databases

ProteinModelPortalQ6MII5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264462.Bd3172.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE80928; CAE80928; Bd3172.
GeneID2736781.
KEGGbba:Bd3172.
PATRIC21080694. VBIBdeBac73187_2902.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227222.
KOK00858.
OMATHEMLYH.
OrthoDBEOG6PZXDR.

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_BDEBA
AccessionPrimary (citable) accession number: Q6MII5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 61 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