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UniProt functional annotation for P07170 | ||
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| UniProt code: P07170. |
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| Organism: | |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). |
| Taxonomy: | |
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. |
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| 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. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. {ECO:0000255|HAMAP- Rule:MF_03168, ECO:0000269|PubMed:18433446, ECO:0000269|PubMed:2848829, ECO:0000269|PubMed:2850178}. |
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| 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; Evidence={ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:2850178}; |
| Subunit: | |
Monomer. {ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369, ECO:0000269|PubMed:8594191}. |
| Subcellular location: | |
Cytoplasm, cytosol {ECO:0000255|HAMAP- Rule:MF_03168, ECO:0000269|PubMed:12045196, ECO:0000269|PubMed:2850178}. Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:12045196, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:2850178}. Note=90% cytoplasmic, 10% mitochondrial. {ECO:0000269|PubMed:2850178}. |
| 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. {ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000305|PubMed:24374639, ECO:0000305|PubMed:7635152, ECO:0000305|PubMed:8594191}. |
| Disruption phenotype: | |
The phenotype of disruption mutants is pet, showing that complementation by another adenylate kinase isozyme occurs only under fermentative conditions. The disruption completely destroys the activity in mitochondria, whereas in the cytoplasmic fraction about 10% is retained. {ECO:0000269|PubMed:2850178}. |
| Miscellaneous: | |
Present with 123000 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}. |
| Similarity: | |
Belongs to the adenylate kinase family. AK2 subfamily. {ECO:0000255|HAMAP-Rule:MF_03168}. |
Annotations taken from UniProtKB at the EBI.