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UniProt functional annotation for P27142 | ||
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| UniProt code: P27142. |
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| Organism: | |
Geobacillus stearothermophilus (Bacillus stearothermophilus). |
| Taxonomy: | |
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus. |
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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. {ECO:0000255|HAMAP- Rule:MF_00235, ECO:0000269|PubMed:1554691}. |
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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_00235, ECO:0000269|PubMed:1554691}; |
| Biophysicochemical properties: | |
Temperature dependence: Optimum temperature is 65 degrees Celsius. Thermal denaturation midpoint (Tm) is 74.5 degrees Celsius. {ECO:0000269|PubMed:1554691}; |
| Pathway: | |
Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}. |
| Subunit: | |
Monomer. {ECO:0000255|HAMAP-Rule:MF_00235}. |
| Subcellular location: | |
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00235}. |
| 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. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain. {ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000305|PubMed:1554691, ECO:0000305|PubMed:9715904}. |
| Similarity: | |
Belongs to the adenylate kinase family. {ECO:0000255|HAMAP- Rule:MF_00235}. |
Annotations taken from UniProtKB at the EBI.