AC MF_03172; DC Protein; auto c? TR HAMAP; MF_03172; -; 1; level=0 XX Names: Adenylate_kinase_UMP_CMP_kin XX ID KCY case DE RecName: Full=UMP-CMP kinase; DE EC=2.7.4.14; DE AltName: Full=Deoxycytidylate kinase; DE Short=CK; DE Short=dCMP kinase; DE AltName: Full=Nucleoside-diphosphate kinase; DE EC=2.7.4.6; DE AltName: Full=Uridine monophosphate/cytidine monophosphate kinase; DE Short=UMP/CMP kinase; DE Short=UMP/CMPK; else case DE RecName: Full=Uridylate kinase; DE Short=UK; DE EC=2.7.4.14; DE AltName: Full=ATP:UMP phosphotransferase; DE AltName: Full=Deoxycytidylate kinase; DE Short=CK; DE Short=dCMP kinase; DE AltName: Full=Uridine monophosphate kinase; DE Short=UMP kinase; DE Short=UMPK; else DE RecName: Full=UMP-CMP kinase; DE EC=2.7.4.14; DE AltName: Full=Deoxycytidylate kinase; DE Short=CK; DE Short=dCMP kinase; DE AltName: Full=Uridine monophosphate/cytidine monophosphate kinase; DE Short=UMP/CMP kinase; DE Short=UMP/CMPK; end case case GN Name=CMPK1; Synonyms=CMPK; else case GN Name=URA6; else case GN Name=pyrK; end case XX case CC -!- FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside CC monophosphates at the expense of ATP. Plays an important role in de CC novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP CC as phosphate acceptors. Also displays broad nucleoside diphosphate CC kinase activity. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, CC ChEBI:CHEBI:456216; EC=2.7.4.14; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, CC ChEBI:CHEBI:456216; EC=2.7.4.14; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'- CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, CC ChEBI:CHEBI:456216; EC=2.7.4.6; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'- CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; else case CC -!- FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside CC monophosphates at the expense of ATP. Plays an important role in de CC novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CC dUMP as phosphate acceptors, but can also use CMP, dCMP and AMP. else CC -!- FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside CC monophosphates at the expense of ATP. Plays an important role in de CC novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP CC as phosphate acceptors. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, CC ChEBI:CHEBI:456216; EC=2.7.4.14; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, CC ChEBI:CHEBI:456216; EC=2.7.4.14; end case CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:456216; EC=2.7.4.14; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per monomer.; CC -!- SUBUNIT: Monomer. case CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly CC cytoplasmic. else case CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly nuclear. else CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. end case CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two CC small peripheral domains, NMPbind and LID, which undergo movements CC during catalysis. The LID domain closes over the site of phosphoryl CC transfer upon ATP binding. Assembling and dissambling the active center CC during each catalytic cycle provides an effective means to prevent ATP CC hydrolysis. CC -!- SIMILARITY: Belongs to the adenylate kinase family. UMP-CMP kinase CC subfamily. XX DR PROSITE; PS00113; ADENYLATE_KINASE; 1; trigger=no DR Pfam; PF00406; ADK; 1; trigger=no DR PRINTS; PR00094; ADENYLTKNASE; 1; trigger=no DR NCBIfam; TIGR01359; UMP_CMP_kin_fam; 1; trigger=no XX KW ATP-binding KW Kinase KW Nucleotide-binding KW Pyrimidine biosynthesis KW Transferase KW Cytoplasm KW Nucleus XX GO GO:0005737; C:cytoplasm GO GO:0005634; C:nucleus case not GO GO:0004127; F:cytidylate kinase activity end case GO GO:0009041; F:UMP/dUMP kinase activity GO GO:0006221; P:pyrimidine nucleotide biosynthetic process XX FT From: KCY_YEAST (P15700) FT BINDING 26..31 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G-x-G-K-G-T FT BINDING 74..76 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT Condition: x-[IL]-[VL] FT BINDING 104..107 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT Condition: G-[FY]-P-R FT REGION 46..76 FT /note="NMPbind" FT REGION 141..151 FT /note="LID" FT BINDING 52 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT Condition: R case FT BINDING 111 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT Condition: Q end case FT BINDING 142 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: R FT BINDING 148 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT Condition: R FT BINDING 159 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT Condition: R FT BINDING 187 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT From: KCY_DICDI (P20425) case not FT BINDING 98 FT /ligand="CMP" FT /ligand_id="ChEBI:CHEBI:60377" FT Condition: N end case XX Size: 191-231; Related: MF_00235; MF_03168; MF_03169; MF_03170; MF_03171; Template: P15700; P20425; P30085; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: in CAEEL Plasmid: None Comments: None XX # Revision 1.17 2023/06/01 //