Q92GY7 (KAD_RICCN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 74.
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 | Rickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 272944 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group › ![]() |
Protein attributes
| Sequence length | 212 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 |
| 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 – 212 | 212 | Adenylate kinase HAMAP-Rule MF_00235 | PRO_0000158838 | |||||
Regions | |||||||||
| Nucleotide binding | 7 – 15 | 9 | ATP By similarity | ||||||
| Nucleotide binding | 31 – 59 | 29 | AMP By similarity | ||||||
Sequences
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References
| [1] | "Mechanisms of evolution in Rickettsia conorii and R. prowazekii." Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D. Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-613 / Malish 7. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE006914 Genomic DNA. Translation: AAL03523.1. |
| PIR | A97823. |
| RefSeq | NP_360622.1. NC_003103.1. |
3D structure databases | |
| ProteinModelPortal | Q92GY7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 272944.RC0985. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAL03523; AAL03523; RC0985. |
| GeneID | 928128. |
| KEGG | rco:RC0985. |
| PATRIC | 17889376. VBIRicCon45613_1125. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0563. |
| HOGENOM | HOG000238772. |
| KO | K00939. |
| OMA | QADAMKD. |
| ProtClustDB | PRK00279. |
Enzyme and pathway databases | |
| UniPathway | UPA00588; UER00649. |
Family and domain databases | |
| HAMAP | MF_00235. Adenylate_kinase_Adk. |
| InterPro | IPR006259. Adenyl_kin_sub. IPR000850. Adenylate_kin. IPR007862. Adenylate_kinase_lid-dom. [Graphical view] |
| PANTHER | PTHR23359. PTHR23359. 1 hit. |
| Pfam | PF00406. ADK. 1 hit. PF05191. ADK_lid. 1 hit. [Graphical view] |
| PRINTS | PR00094. ADENYLTKNASE. |
| SUPFAM | SSF57774. Adenylate_kinase_Znf_lid. 1 hit. |
| TIGRFAMs | TIGR01351. adk. 1 hit. |
| PROSITE | PS00113. ADENYLATE_KINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KAD_RICCN | ||||||||
| Accession | Primary (citable) accession number: Q92GY7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Rickettsia conorii (strain Malish 7): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
