HAMAP rule MF_03171
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_03171 |
| Accession | MF_03171 |
| Dates | 11-MAR-2013 (Created)
1-JUN-2023 (Last updated, Version 13) |
| Name | Adenylate_kinase_AK1 |
| Scope(s) |
Eukaryota Metazoa |
| Template(s) | P00568 (KAD1_HUMAN); P00571 (KAD1_PIG); [ Recover all ] |
| Triggered by |
case c? <OC:Eukaryota>
HAMAP; MF_03171 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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| Identifier | KAD1 |
| case <OC:Vertebrata> | |
| Protein name | RecName: Full=Adenylate kinase isoenzyme 1; Short=AK 1; EC=2.7.4.3; EC=2.7.4.6; AltName: Full=ATP-AMP transphosphorylase 1; AltName: Full=ATP:AMP phosphotransferase; AltName: Full=Adenylate monophosphate kinase; AltName: Full=Myokinase; |
| else | |
| Protein name | RecName: Full=Adenylate kinase isoenzyme 1; Short=AK 1; EC=2.7.4.3; AltName: Full=ATP-AMP transphosphorylase 1; AltName: Full=ATP:AMP phosphotransferase; AltName: Full=Adenylate monophosphate kinase; |
| end case | |
| case <OC:Vertebrata> | |
| Gene name | Name=AK1; |
| end case | |
Comments
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| case <OC:Vertebrata> | |
| FUNCTION | Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. |
| CATALYTIC ACTIVITY | Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'- deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; |
| CATALYTIC ACTIVITY | Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'- triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; |
| else | |
| 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. |
| end case | |
| CATALYTIC ACTIVITY | Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; |
| SUBUNIT | Monomer. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| 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. |
| SIMILARITY | Belongs to the adenylate kinase family. AK1 subfamily. |
Keywords
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| ATP-binding | |
| Kinase | |
| Nucleotide-binding | |
| Transferase | |
| Cytoplasm | |
| case <FTTag:acetyl> | |
| Acetylation | |
| end case | |
Gene Ontology
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| GO:0005737; Cellular component:cytoplasm |
| GO:0004017; Molecular function:adenylate kinase activity |
| GO:0006172; Biological process:ADP biosynthetic process |
| GO:0046033; Biological process:AMP metabolic process |
| GO:0046034; Biological process:ATP metabolic process |
Cross-references
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| PROSITE | PS00113; ADENYLATE_KINASE; 1; |
| Pfam | PF00406; ADK; 1; |
| PRINTS | PR00094; ADENYLTKNASE; 1; |
| NCBIfam | TIGR01360; aden_kin_iso1; 1; |
Features
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| From: KAD1_HUMAN (P00568) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 18 | 23 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
G-S-G-K-G-T | ||||||||
| BINDING | 65 | 67 | /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215" |
x-L-V | ||||||||
| BINDING | 94 | 97 | /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215" |
G-Y-P-R | ||||||||
| REGION | 38 | 67 | /note="NMPbind" | |||||||||
| REGION | 131 | 141 | /note="LID" | |||||||||
| BINDING | 39 | 39 | /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215" |
[ST] | ||||||||
| BINDING | 44 | 44 | /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215" |
R | ||||||||
| BINDING | 101 | 101 | /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215" |
Q | ||||||||
| BINDING | 132 | 132 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
R | ||||||||
| BINDING | 138 | 138 | /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215" |
R | ||||||||
| BINDING | 149 | 149 | /ligand="AMP" /ligand_id="ChEBI:CHEBI:456215" |
R | ||||||||
| BINDING | 177 | 177 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
|||||||||
| case <OC:Mammalia> | ||||||||||||
| MOD_RES | 1 | 1 | /note="N-acetylmethionine" | acetyl | M | |||||||
| end case | ||||||||||||
Additional information
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| Size range | 193-211 amino acids |
| Related rules |
MF_00235 MF_03168 MF_03169 MF_03170 MF_03172 |
| Fusion | Nter: None Cter: None |