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B4S665 (NADK_PROA2) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 42. 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:Paes_2165
OrganismProsthecochloris aestuarii (strain DSM 271 / SK 413) [Complete proteome] [HAMAP]
Taxonomic identifier290512 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeProsthecochloris

Protein attributes

Sequence length285 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 – 285285NAD kinase HAMAP-Rule MF_00361
PRO_1000120877

Regions

Nucleotide binding66 – 672NAD By similarity
Nucleotide binding137 – 1382NAD By similarity
Nucleotide binding178 – 1836NAD By similarity

Sites

Active site661Proton acceptor By similarity
Binding site1481NAD By similarity
Binding site1651NAD By similarity
Binding site1671NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
B4S665 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 14EEA6254E495B01

FASTA28531,182
        10         20         30         40         50         60 
MKFAIVVNIN REDALELAQE LTSWLQERGL SYVLDSVSGE KTGIEPSMAM EELNKDCDAF 

        70         80         90        100        110        120 
ISLGGDGTLL FTSHYSVTKP VIGINVGHLG FLAEFSKAEM FEAVEQVLNG TYSIHVRSQL 

       130        140        150        160        170        180 
EAEVTMNGGL KHLTALNDVV IEKGAYPRIP TFIIKLDDEL LSAYRADGII IATSTGSTAY 

       190        200        210        220        230        240 
SLSAGGPIIA PKSNVFVITP ICPHMLTVRP IVISDDKTIQ ISVEAHGGEF PLNCDGHVSK 

       250        260        270        280 
MLLPGETIIV RKSEQIINLV ENKNRRYCEI LRSKLLWGHE HQSGS 

« Hide

References

[1]"Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 271 / SK 413.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001108 Genomic DNA. Translation: ACF47167.1.
RefSeqYP_002016814.1. NC_011059.1.

3D structure databases

ProteinModelPortalB4S665.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290512.Paes_2165.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF47167; ACF47167; Paes_2165.
GeneID6458706.
KEGGpaa:Paes_2165.
PATRIC23044272. VBIProAes37017_2300.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227222.
KOK00858.
OMASAYRADG.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycPAES290512:GHUT-2214-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_PROA2
AccessionPrimary (citable) accession number: B4S665
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 42 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