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Q81GJ9 (NADK1_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 69. 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 1

EC=2.7.1.23
Alternative name(s):
ATP-dependent NAD kinase 1
Gene names
Name:nadK1
Ordered Locus Names:BC_1199
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length265 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
Reference 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 – 265265NAD kinase 1 HAMAP-Rule MF_00361
PRO_0000120593

Regions

Nucleotide binding45 – 462NAD By similarity
Nucleotide binding122 – 1232NAD By similarity

Sites

Active site451Proton acceptor By similarity
Binding site1481NAD By similarity
Binding site1501NAD By similarity
Binding site1851NAD; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81GJ9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 53DA54FC1976DAB8

FASTA26529,766
        10         20         30         40         50         60 
MKFTIMSKGD QSSDTLASTM KEYLLDFGFI MDEKEPDIVI SVGGDGTLLY AFHRYYNRLD 

        70         80         90        100        110        120 
ETAFVGVHTG HLGFYADWLP TEVEKLVIAI AKTPFQVVEY PLLEVIIRYV NGSKESQYLA 

       130        140        150        160        170        180 
MNEATVKSAE GTLVTEVEIR GEYFETFRGD GLCISTPSGS TAYNKALGGA IIHPSIEAIQ 

       190        200        210        220        230        240 
IAEMASINNR VFRTVGSPLV LPKHHTCVLK PAAGMNLQIT VDHLTMVHQD VKSIQYRVAN 

       250        260 
EKVRFVRFRP FPFWKRVRDS FVADK 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP08185.1.
RefSeqNP_830984.1. NC_004722.1.

3D structure databases

ProteinModelPortalQ81GJ9.
SMRQ81GJ9. Positions 1-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226900.BC1199.

Proteomic databases

PRIDEQ81GJ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP08185; AAP08185; BC_1199.
GeneID1203548.
KEGGbce:BC1199.
PATRIC32598111. VBIBacCer54481_1167.

Phylogenomic databases

eggNOGCOG0061.
KOK00858.
OMAQWITIVP.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycBCER226900:GJEU-1199-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 nameNADK1_BACCR
AccessionPrimary (citable) accession number: Q81GJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 69 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