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Q7V3C2 (NADK1_PROMP) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 62. 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:PMM0156
OrganismProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]
Taxonomic identifier59919 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length299 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 – 299299NAD kinase 1 HAMAP-Rule MF_00361
PRO_0000229674

Regions

Nucleotide binding62 – 632NAD By similarity
Nucleotide binding143 – 1442NAD By similarity

Sites

Active site621Proton acceptor By similarity
Binding site671NAD By similarity
Binding site1731NAD By similarity
Binding site1751NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V3C2 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 41F28B70D7F5244E

FASTA29934,128
        10         20         30         40         50         60 
MLIIYRSNSL TAKEASIFCN KTLKERNIKS KRIESDFDNN QLENYFYNLA ALPDLVIVLG 

        70         80         90        100        110        120 
GDGTVLKSAN ALVNYDIPIL SFNIGGNLGF LTQEKDFLFD QSFIKILEKE EFIIDFRNRL 

       130        140        150        160        170        180 
HCDVYSNEKN RERKILKSYD ALNDFYFKSV EEDISPTNQI QIEIDNEKVN EYKGDGLIIS 

       190        200        210        220        230        240 
SSTGSTAYSM AAGGPIVHPS INAFVINPIC PMSLASRPII IPDTSKVVIR VVQKNKREIK 

       250        260        270        280        290 
LWKDGSKCMT IKENDYCEIN KVTKPCKMIK FNKSISYYIT LIKKLDWKGD LSLKNNQNN 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCMP1986 / MED4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548174 Genomic DNA. Translation: CAE18615.1.
RefSeqNP_892277.1. NC_005072.1.

3D structure databases

ProteinModelPortalQ7V3C2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59919.PMM0156.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE18615; CAE18615; PMM0156.
GeneID1726207.
KEGGpmm:PMM0156.
PATRIC23030958. VBIProMar68066_0163.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227222.
KOK00858.
OMAKLHWAGS.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycPMAR59919:GJMQ-160-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_PROMP
AccessionPrimary (citable) accession number: Q7V3C2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 1, 2003
Last modified: July 9, 2014
This is version 62 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