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Q2RIC1 (NADK_MOOTA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 56. 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:Moth_1509
OrganismMoorella thermoacetica (strain ATCC 39073) [Reference proteome] [HAMAP]
Taxonomic identifier264732 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella

Protein attributes

Sequence length311 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 – 311311NAD kinase HAMAP-Rule MF_00361
PRO_0000229654

Regions

Nucleotide binding67 – 682NAD By similarity
Nucleotide binding140 – 1412NAD By similarity
Nucleotide binding181 – 1866NAD By similarity

Sites

Active site671Proton acceptor By similarity
Binding site721NAD By similarity
Binding site1511NAD By similarity
Binding site1701NAD By similarity
Binding site2401NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2RIC1 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: EDA72D2B0CFDD54D

FASTA31133,684
        10         20         30         40         50         60 
MQRIGMVANL EKPRVRETAL DIINYLESRN VRVLISTRKA AALGCPEKGV AEEEVIAAEG 

        70         80         90        100        110        120 
LLALGGDGTL LRAARLVAPA GTPILGINLG HLGFLTEIEL TELYPALDKL LAGAYRIEER 

       130        140        150        160        170        180 
MMLRGTVQRP EKALTCTALN DIVVTKGAFS RMLRLEVYID TAYLDTYPAD GLIVSSPTGS 

       190        200        210        220        230        240 
TAYSLSAGGP LVSPQLQVMI LTPICPHTLY TRPLVVPGEQ EIRVCVHAPG AEVMLTVDGQ 

       250        260        270        280        290        300 
QGLHLRDGDV IRVTRARTPA RLIRLQDNTF YSLVREKLKE GGSRQDDENP AATVNPETDS 

       310 
KYPHSHPGST G 

« Hide

References

[1]"The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum)."
Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C., Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.
Environ. Microbiol. 10:2550-2573(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39073.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000232 Genomic DNA. Translation: ABC19818.1.
RefSeqYP_430361.1. NC_007644.1.

3D structure databases

ProteinModelPortalQ2RIC1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264732.Moth_1509.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC19818; ABC19818; Moth_1509.
GeneID3831974.
KEGGmta:Moth_1509.
PATRIC22640314. VBIMooThe6753_1635.

Phylogenomic databases

eggNOGCOG0061.
HOGENOMHOG000227222.
KOK00858.
OMATHEMLYH.
OrthoDBEOG6PZXDR.

Enzyme and pathway databases

BioCycMTHE264732:GH0A-1567-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_MOOTA
AccessionPrimary (citable) accession number: Q2RIC1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 24, 2006
Last modified: July 9, 2014
This is version 56 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