Q8DML4 (KAD_THEEB) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 68.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Adenylate kinase Short name=AK EC=2.7.4.3 Alternative name(s): ATP-AMP transphosphorylase | ||||
| Gene names |
| ||||
| Organism | Thermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 197221 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Thermosynechococcus › ![]() |
Protein attributes
| Sequence length | 195 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth 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. |
| Subcellular location | Cytoplasm By similarity. |
| Domain | Consists of three domains, a large central CORE domain and two small peripheral domains, AMP binding and LID. The LID domain closes over the site of phosphoryl transfer upon ATP binding By similarity. HAMAP-Rule MF_00235 |
| Sequence similarities | Belongs to the adenylate kinase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nucleotide biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | AMP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: HAMAP adenylate kinase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 195 | 195 | Adenylate kinase HAMAP-Rule MF_00235 | PRO_0000158868 | |||||
Regions | |||||||||
| Nucleotide binding | 7 – 15 | 9 | ATP By similarity | ||||||
| Nucleotide binding | 31 – 59 | 29 | AMP By similarity | ||||||
Sequences
| ||||||||||||||||||
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. 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. |
| RefSeq | NP_680891.1. NC_004113.1. |
3D structure databases | |
| ProteinModelPortal | Q8DML4. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 197221.tlr0100. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAC07653; BAC07653; BAC07653. |
| GeneID | 1010391. |
| KEGG | tel:tlr0100. |
| PATRIC | 23925382. VBITheElo119873_0103. |
Phylogenomic databases | |
| eggNOG | COG0563. |
| HOGENOM | HOG000238772. |
| KO | K00939. |
| OMA | ERTSGRW. |
Enzyme and pathway databases | |
| UniPathway | UPA00588; UER00649. |
Family and domain databases | |
| HAMAP | MF_00235. Adenylate_kinase_Adk. |
| InterPro | IPR000850. Adenylate_kin. [Graphical view] |
| PANTHER | PTHR23359. PTHR23359. 1 hit. |
| Pfam | PF00406. ADK. 1 hit. [Graphical view] |
| PRINTS | PR00094. ADENYLTKNASE. |
| PROSITE | PS00113. ADENYLATE_KINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KAD_THEEB | ||||||||
| Accession | Primary (citable) accession number: Q8DML4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
