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HAMAP rule MF_03172

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General rule information [?]

Accession MF_03172
Dates 15-MAR-2013 (Created)
28-JUN-2024 (Last updated, Version 18)
Name Adenylate_kinase_UMP_CMP_kin
Scope(s) Eukaryota
Template(s) P15700 (KCY_YEAST); P20425 (KCY_DICDI); P30085 (KCY_HUMAN); [ Recover all ]
Triggered by
case c? <OC:Eukaryota>
HAMAP; MF_03172 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier KCY
case <OC:Vertebrata>
Protein name RecName: Full=UMP-CMP kinase;
                 EC=2.7.4.14;
AltName: Full=Deoxycytidylate kinase;
                 Short=CK;
                 Short=dCMP kinase;
AltName: Full=Nucleoside-diphosphate kinase;
                 EC=2.7.4.6;
AltName: Full=Uridine monophosphate/cytidine monophosphate kinase;
                 Short=UMP/CMP kinase;
                 Short=UMP/CMPK;
else case <OC:Fungi>
Protein name RecName: Full=Uridylate kinase;
                 Short=UK;
                 EC=2.7.4.14;
AltName: Full=ATP:UMP phosphotransferase;
AltName: Full=Deoxycytidylate kinase;
                 Short=CK;
                 Short=dCMP kinase;
AltName: Full=Uridine monophosphate kinase;
                 Short=UMP kinase;
                 Short=UMPK;
else
Protein name RecName: Full=UMP-CMP kinase;
                 EC=2.7.4.14;
AltName: Full=Deoxycytidylate kinase;
                 Short=CK;
                 Short=dCMP kinase;
AltName: Full=Uridine monophosphate/cytidine monophosphate kinase;
                 Short=UMP/CMP kinase;
                 Short=UMP/CMPK;
end case
case <OC:Vertebrata>
Gene name Name=CMPK1; Synonyms=CMPK;
else case <OC:Saccharomycotina>
Gene name Name=URA6;
else case <OC:Dictyostelia>
Gene name Name=pyrK;
end case

Comments [?]

case <OC:Vertebrata>
FUNCTIONCatalyzes 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. Also displays broad nucleoside diphosphate kinase activity.
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;
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;
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 case <OC:Fungi>
FUNCTIONCatalyzes 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 dUMP as phosphate acceptors, but can also use CMP, dCMP and AMP.
else
FUNCTIONCatalyzes 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.
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;
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;
end case
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;
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per monomer.;
SUBUNITMonomer.
case <OC:Fungi>
SUBCELLULAR LOCATIONCytoplasm. Nucleus. Note=Predominantly cytoplasmic.
else case <OC:Vertebrata>
SUBCELLULAR LOCATIONNucleus. Cytoplasm. Note=Predominantly nuclear.
else
SUBCELLULAR LOCATIONCytoplasm. Nucleus.
end case
DOMAINConsists 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.
SIMILARITYBelongs to the adenylate kinase family. UMP-CMP kinase subfamily.

Keywords [?]

ATP-binding
Kinase
Nucleotide-binding
Pyrimidine biosynthesis
Transferase
Cytoplasm
Nucleus

Gene Ontology [?]

GO:0005737; Cellular component:cytoplasm
GO:0005634; Cellular component:nucleus
case not <OCellular component:Fungi>
GO:0004127; Molecular function:(d)CMP kinase activity
end case
GO:0009041; Molecular function:UMP/dUMP kinase activity
GO:0006221; Biological process:pyrimidine nucleotide biosynthetic process

Cross-references [?]

PROSITE PS00113; ADENYLATE_KINASE; 1;
Pfam PF00406; ADK; 1;
PRINTS PR00094; ADENYLTKNASE; 1;
NCBIfam TIGR01359; UMP_CMP_kin_fam; 1;

Features [?]

From: KCY_YEAST (P15700)
Key From To Description Tag Condition FTGroup
BINDING 26 31 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G-x-G-K-G-T
BINDING 74 76 /ligand="a ribonucleoside 5'-phosphate"
/ligand_id="ChEBI:CHEBI:58043"		 x-[IL]-[VL]
BINDING 104 107 /ligand="a ribonucleoside 5'-phosphate"
/ligand_id="ChEBI:CHEBI:58043"		 G-[FY]-P-R
REGION 46 76 /note="NMPbind"
REGION 141 151 /note="LID"
BINDING 52 52 /ligand="a ribonucleoside 5'-phosphate"
/ligand_id="ChEBI:CHEBI:58043"		 R
case <OC:Fungi>
BINDING 111 111 /ligand="a ribonucleoside 5'-phosphate"
/ligand_id="ChEBI:CHEBI:58043"		 Q
end case
BINDING 142 142 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 R
BINDING 148 148 /ligand="a ribonucleoside 5'-phosphate"
/ligand_id="ChEBI:CHEBI:58043"		 R
BINDING 159 159 /ligand="a ribonucleoside 5'-phosphate"
/ligand_id="ChEBI:CHEBI:58043"		 R
BINDING 187 187 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
From: KCY_DICDI (P20425)
Key From To Description Tag Condition FTGroup
case not <OC:Fungi>
BINDING 98 98 /ligand="CMP"
/ligand_id="ChEBI:CHEBI:60377"		 N
end case

Additional information [?]

Size range 191-231 amino acids
Related rules MF_00235
MF_03168
MF_03169
MF_03170
MF_03171
Fusion Nter: None Cter: None



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