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| Annotation rule MF_03170 |
General rule information
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| Accession | MF_03170 |
| Dates | 11-MAR-2013 (Created) 20-NOV-2019 (Last updated, Version 11) |
| Name | Adenylate_kinase_AK4 |
| Scope | Eukaryota; Vertebrata |
| Template | P27144 (KAD4_HUMAN) |
case <OC:Eukaryota>
| Triggered by |
end case
Propagated annotation
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Identifier, protein and gene names
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| Identifier |
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| Protein name |
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| Gene name |
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Comments
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| Function | Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Efficiently phosphorylates AMP and dAMP using ATP as phosphate donor, but phosphorylates only AMP when using GTP as phosphate donor. Also displays broad nucleoside diphosphate kinase activity. |
| Catalytic activity | RHEA:13749: a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-diphosphate + ADP
EC 2.7.4.10 |
| RHEA:44640: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
EC 2.7.4.6 |
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| RHEA:18113: a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP
EC 2.7.4.6 |
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| Subunit | Monomer. |
| Subcellular location | Mitochondrion matrix. |
| 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 GTP/ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP/ATP hydrolysis. |
| Similarity | Belongs to the adenylate kinase family. AK3 subfamily. |
Keywords
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Gene Ontology
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GO:0005759; Cellular component: mitochondrial matrix.
GO:0046899; Molecular function: nucleoside triphosphate adenylate kinase activity.
GO:0006172; Biological process: ADP biosynthetic process.
GO:0046033; Biological process: AMP metabolic process.
GO:0046039; Biological process: GTP metabolic process.
GO:0046034; Biological process: ATP metabolic process.
GO:0046899; Molecular function: nucleoside triphosphate adenylate kinase activity.
GO:0006172; Biological process: ADP biosynthetic process.
GO:0046033; Biological process: AMP metabolic process.
GO:0046039; Biological process: GTP metabolic process.
GO:0046034; Biological process: ATP metabolic process.
Cross-references
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| PROSITE | PS00113; ADENYLATE_KINASE; 1; |
| Pfam | PF00406; ADK; 1; |
| PF05191; ADK_lid; 1; | |
| PRINTS | PR00094; ADENYLTKNASE; 1; |
| TIGRFAMs | TIGR01351; adk; 1; |
Features
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| From: KAD4_HUMAN (P27144) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| NP_BIND | 15 | 20 | NTP | G-x-G-K-G-T | ||||||||
| NP_BIND | 62 | 64 | AMP | x-L-V | ||||||||
| NP_BIND | 89 | 92 | AMP | G-F-P-R | ||||||||
| NP_BIND | 135 | 136 | NTP | V-Y | ||||||||
| REGION | 35 | 64 | NMPbind | |||||||||
| REGION | 125 | 162 | LID | |||||||||
| BINDING | 36 | 36 | AMP | S | ||||||||
| BINDING | 41 | 41 | AMP | R | ||||||||
| BINDING | 96 | 96 | AMP | Q | ||||||||
| BINDING | 126 | 126 | NTP | R | ||||||||
| BINDING | 170 | 170 | AMP | R | ||||||||
| BINDING | 199 | 199 | NTP; via carbonyl oxygen | T | ||||||||
Additional information
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| Size range | 223-231 amino acids |
| Related rules | MF_00235 (KAD); MF_03168 (KAD2); MF_03169 (KAD3); MF_03171 (KAD1); MF_03172 (KCY) |
| Fusion | None |