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UniProt functional annotation for P20425 | ||
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| UniProt code: P20425. |
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| Organism: | |
Dictyostelium discoideum (Slime mold). |
| Taxonomy: | |
Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; Dictyosteliaceae; Dictyostelium. |
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| Function: | |
Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:2156849}. |
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| Catalytic activity: | |
Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP- Rule:MF_03172, ECO:0000269|PubMed:2156849}; |
| Catalytic activity: | |
Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP- Rule:MF_03172, ECO:0000269|PubMed:2156849}; |
| Catalytic activity: | |
Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400, ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223, ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP- Rule:MF_03172, ECO:0000269|PubMed:2156849}; |
| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:8703943}; Note=Binds 1 Mg(2+) ion per monomer. The Mg(2+) ion binds to water and substrates. {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:8703943}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=25 uM for ATP {ECO:0000269|PubMed:2156849}; KM=0.4 mM for UMP {ECO:0000269|PubMed:2156849}; KM=0.1 mM for CMP {ECO:0000269|PubMed:2156849}; |
| Subunit: | |
Monomer. {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:10426946, ECO:0000269|PubMed:9280438}. |
| Subcellular location: | |
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03172}. |
| 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_03172, ECO:0000305|PubMed:10426946, ECO:0000305|PubMed:8703943, ECO:0000305|PubMed:9280438}. |
| Similarity: | |
Belongs to the adenylate kinase family. UMP-CMP kinase subfamily. {ECO:0000255|HAMAP-Rule:MF_03172}. |
| Sequence caution: | |
Sequence=AAA33272.1; Type=Erroneous initiation; Evidence={ECO:0000305}; |
Annotations taken from UniProtKB at the EBI.