Reviewed,
UniProtKB/Swiss-Prot P12115 (KAD1_CYPCA)
Last modified
February 9, 2010.
Version 62.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Adenylate kinase isoenzyme 1 Short name=AK 1 EC=2.7.4.3 Alternative name(s): ATP-AMP transphosphorylase 1 Myokinase | ||
| Gene names |
| ||
| Organism | Cyprinus carpio (Common carp) | ||
| Taxonomic identifier | 7962 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Cyprinus |
Protein attributes
| Sequence length | 194 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth. |
| Catalytic activity | ATP + AMP = 2 ADP. |
| Subunit structure | Monomer. |
| Subcellular location | |
| Sequence similarities | Belongs to the adenylate kinase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| PTM | Acetylation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | ATP metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate kinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.1 | ||||||
| Chain | 2 – 194 | 193 | Adenylate kinase isoenzyme 1 | PRO_0000158908 | |||||
Regions | |||||||||
| Nucleotide binding | 15 – 23 | 9 | ATP By similarity | ||||||
| Nucleotide binding | 94 – 101 | 8 | AMP By similarity | ||||||
Sites | |||||||||
| Binding site | 39 | 1 | AMP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.1 | ||||||
Sequences
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References
| [1] | "Amino acid sequence and three-dimensional structure of cytosolic adenylate kinase from carp muscle." Reuner C., Hable M., Wilmanns M., Kiefer E., Schiltz E., Schulz G.E. Protein Seq. Data Anal. 1:335-343(1988) [PubMed: 2851785] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-194, ACETYLATION AT ALA-2, X-RAY CRYSTALLOGRAPHY (5.8 ANGSTROMS). Tissue: Muscle. |
Cross-references
Sequence databases | |
|---|---|
| PIR | KICAC. S00394. |
3D structure databases | |
| SMR | P12115. Positions 1-194. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P12115. |
Enzyme and pathway databases | |
| BRENDA | 2.7.4.3. 3298. |
Family and domain databases | |
| InterPro | IPR000850. Adenylate_kin. IPR006267. Adenylate_kin1. [Graphical view] |
| PANTHER | PTHR23359. Adenylate_kin. 1 hit. |
| Pfam | PF00406. ADK. 1 hit. [Graphical view] |
| PRINTS | PR00094. ADENYLTKNASE. |
| TIGRFAMs | TIGR01360. aden_kin_iso1. 1 hit. |
| PROSITE | PS00113. ADENYLATE_KINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KAD1_CYPCA | ||||||||
| Accession | Primary (citable) accession number: P12115 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

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