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O66490 (KAD_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Adenylate kinase

Short name=AK
EC=2.7.4.3
Alternative name(s):
ATP-AMP transphosphorylase
ATP:AMP phosphotransferase
Adenylate monophosphate kinase
Gene names
Name:adk
Ordered Locus Names:aq_078
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism By similarity. HAMAP-Rule MF_00235

Catalytic activity

ATP + AMP = 2 ADP. HAMAP-Rule MF_00235

Pathway

Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. HAMAP-Rule MF_00235

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00235

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00235.

Domain

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. HAMAP-Rule MF_00235

Sequence similarities

Belongs to the adenylate kinase family.

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processAMP salvage

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

adenylate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 206206Adenylate kinase HAMAP-Rule MF_00235
PRO_0000158718

Regions

Nucleotide binding10 – 156ATP HAMAP-Rule MF_00235
Nucleotide binding57 – 593AMP HAMAP-Rule MF_00235
Nucleotide binding82 – 854AMP HAMAP-Rule MF_00235
Nucleotide binding133 – 1342ATP HAMAP-Rule MF_00235
Region30 – 5930NMPbind HAMAP-Rule MF_00235
Region123 – 15331LID HAMAP-Rule MF_00235

Sites

Binding site311AMP
Binding site891AMP
Binding site1201ATP
Binding site1241ATP
Binding site1611AMP
Binding site1891ATP; via carbonyl oxygen

Secondary structure

........................................ 206
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O66490 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 2310B49B11CBC71E

FASTA20623,231
        10         20         30         40         50         60 
MILVFLGPPG AGKGTQAKRL AKEKGFVHIS TGDILREAVQ KGTPLGKKAK EYMERGELVP 

        70         80         90        100        110        120 
DDLIIALIEE VFPKHGNVIF DGFPRTVKQA EALDEMLEKK GLKVDHVLLF EVPDEVVIER 

       130        140        150        160        170        180 
LSGRRINPET GEVYHVKYNP PPPGVKVIQR EDDKPEVIKK RLEVYREQTA PLIEYYKKKG 

       190        200 
ILRIIDASKP VEEVYRQVLE VIGDGN 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
[2]"Intrinsic motions along an enzymatic reaction trajectory."
Henzler-Wildman K.A., Thai V., Lei M., Ott M., Wolf-Watz M., Fenn T., Pozharski E., Wilson M.A., Petsko G.A., Karplus M., Hubner C.G., Kern D.
Nature 450:838-844(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG AP5A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC06438.1.
PIRG70307.
RefSeqNP_213050.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RGXX-ray1.90A1-206[»]
2RH5X-ray2.48A/B/C1-206[»]
3SR0X-ray1.56A/B1-206[»]
ProteinModelPortalO66490.
SMRO66490. Positions 1-203.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_078.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC06438; AAC06438; aq_078.
GeneID1192503.
KEGGaae:aq_078.
PATRIC20957855. VBIAquAeo85532_0068.

Phylogenomic databases

eggNOGCOG0563.
HOGENOMHOG000238772.
KOK00939.
OMANEKMNAP.
OrthoDBEOG679TH4.
ProtClustDBCLSK2459789.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-65-MONOMER.
UniPathwayUPA00588; UER00649.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00235. Adenylate_kinase_Adk.
InterProIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PRINTSPR00094. ADENYLTKNASE.
SUPFAMSSF52540. SSF52540. 1 hit.
SSF57774. SSF57774. 1 hit.
TIGRFAMsTIGR01351. adk. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO66490.

Entry information

Entry nameKAD_AQUAE
AccessionPrimary (citable) accession number: O66490
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 95 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways