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Q8DML4 (KAD_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:tlr0100
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length195 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. 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 termComplete 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 – 195195Adenylate kinase HAMAP-Rule MF_00235
PRO_0000158868

Regions

Nucleotide binding10 – 156ATP By similarity
Nucleotide binding57 – 593AMP By similarity
Nucleotide binding85 – 884AMP By similarity
Region30 – 5930NMPbind By similarity
Region126 – 14015LID By similarity

Sites

Binding site311AMP By similarity
Binding site361AMP By similarity
Binding site921AMP By similarity
Binding site1271ATP By similarity
Binding site1371AMP By similarity
Binding site1481AMP By similarity
Binding site1761ATP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DML4 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 4CBB5069B0E477BD

FASTA19521,524
        10         20         30         40         50         60 
MRLILFGGPG SGKGTQAAIL TTLLGIPHIS TGDILRAERA AGTLLGQQAQ SYMDRGELVP 

        70         80         90        100        110        120 
DQVIVDMVAN RLQQPDTAAG WLLDGFPRNG AQAAVFEEML KSIHQDYDYL LFLDVPAAIL 

       130        140        150        160        170        180 
QERALNRAKQ AVNGQQRSDD TPETILKRLQ VYERETLPMI QQYMSHPKFV PIDGTRTIEE 

       190 
VTAAIQARIG EVNRV 

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC07653.1.
RefSeqNP_680891.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DML4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tlr0100.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC07653; BAC07653; BAC07653.
GeneID1010391.
KEGGtel:tlr0100.
PATRIC23925382. VBITheElo119873_0103.

Phylogenomic databases

eggNOGCOG0563.
HOGENOMHOG000238772.
KOK00939.
OMAHVLEIAV.
OrthoDBEOG679TH4.

Enzyme and pathway databases

UniPathwayUPA00588; UER00649.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00235. Adenylate_kinase_Adk.
InterProIPR000850. Adenylat/UMP-CMP_kin.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PRINTSPR00094. ADENYLTKNASE.
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKAD_THEEB
AccessionPrimary (citable) accession number: Q8DML4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 74 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

PATHWAY comments

Index of metabolic and biosynthesis pathways