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C1FPA6 (NADK_CLOBJ) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 35. 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:CLM_2096
OrganismClostridium botulinum (strain Kyoto / Type A2) [Complete proteome] [HAMAP]
Taxonomic identifier536232 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length281 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 – 281281NAD kinase HAMAP-Rule MF_00361
PRO_1000133564

Regions

Nucleotide binding61 – 622NAD By similarity
Nucleotide binding134 – 1352NAD By similarity
Nucleotide binding175 – 1806NAD By similarity

Sites

Active site611Proton acceptor By similarity
Binding site1451NAD By similarity
Binding site1641NAD By similarity
Binding site2341NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
C1FPA6 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 84B6ECA58EEFA50C

FASTA28131,690
        10         20         30         40         50         60 
MKNIGININT DKDISRNILD KIFQYIHEEC SEAKIKVFYD SKGLDNEESR ALDAVMVLGG 

        70         80         90        100        110        120 
DGTILGTARA LAKYDVPIFG INRGHLGFLA EIELEDCKEA IKNLFKGQYK IEDRIMLKCD 

       130        140        150        160        170        180 
LKGIDKKDDF LALNDIVLTK GNLSRIVKYS IYVDDVWYTT FVADGVIVAT PTGSTAYSLS 

       190        200        210        220        230        240 
AGGPIVYPDL DVLEIAPICP HSLGIRPILL NGNSKINIRV LKKYEDPVLT IDGQRYKKVT 

       250        260        270        280 
VNEVTISKSK YKCRLIKFKD KDYFKILRTK ISYRSRECEG E 

« Hide

References

[1]"Genome sequence of Clostridium botulinum A2 Kyoto."
Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C., Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Kyoto / Type A2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001581 Genomic DNA. Translation: ACO83423.1.
RefSeqYP_002804268.1. NC_012563.1.

3D structure databases

ProteinModelPortalC1FPA6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING536232.CLM_2096.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO83423; ACO83423; CLM_2096.
GeneID7767401.
KEGGcby:CLM_2096.
PATRIC19380681. VBICloBot91161_1966.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227222.
KOK00858.
OMARWEALCL.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycCBOT536232:GCO3-2027-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_CLOBJ
AccessionPrimary (citable) accession number: C1FPA6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: July 9, 2014
This is version 35 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