ID KCY_CHICK Reviewed; 196 AA. AC Q5ZKE7; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 24-JAN-2024, entry version 116. DE RecName: Full=UMP-CMP kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE EC=2.7.4.14 {ECO:0000255|HAMAP-Rule:MF_03172}; DE AltName: Full=Deoxycytidylate kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE Short=CK {ECO:0000255|HAMAP-Rule:MF_03172}; DE Short=dCMP kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE AltName: Full=Nucleoside-diphosphate kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE EC=2.7.4.6 {ECO:0000255|HAMAP-Rule:MF_03172}; DE AltName: Full=Uridine monophosphate/cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE Short=UMP/CMP kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE Short=UMP/CMPK {ECO:0000255|HAMAP-Rule:MF_03172}; GN Name=CMPK; Synonyms=CMPK1 {ECO:0000255|HAMAP-Rule:MF_03172}; GN ORFNames=RCJMB04_11f2; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=CB; TISSUE=Bursa of Fabricius; RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6; RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., RA Hayashizaki Y., Buerstedde J.-M.; RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene RT function analysis."; RL Genome Biol. 6:R6.1-R6.9(2005). 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. {ECO:0000255|HAMAP-Rule:MF_03172}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03172}; 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03172}; 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03172}; 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03172}; 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; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03172}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03172}; CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_03172}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03172}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03172}. CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172}. Note=Predominantly CC nuclear. {ECO:0000255|HAMAP-Rule:MF_03172}. 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. {ECO:0000255|HAMAP-Rule:MF_03172}. CC -!- SIMILARITY: Belongs to the adenylate kinase family. UMP-CMP kinase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03172}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ720137; CAG31796.1; -; mRNA. DR RefSeq; NP_001026735.1; NM_001031564.1. DR AlphaFoldDB; Q5ZKE7; -. DR SMR; Q5ZKE7; -. DR STRING; 9031.ENSGALP00000017049; -. DR PaxDb; 9031-ENSGALP00000041616; -. DR GeneID; 429100; -. DR KEGG; gga:429100; -. DR CTD; 51727; -. DR VEuPathDB; HostDB:geneid_429100; -. DR eggNOG; KOG3079; Eukaryota. DR InParanoid; Q5ZKE7; -. DR OMA; DVCVQRC; -. DR PhylomeDB; Q5ZKE7; -. DR TreeFam; TF354283; -. DR Reactome; R-GGA-499943; Interconversion of nucleotide di- and triphosphates. DR PRO; PR:Q5ZKE7; -. DR Proteomes; UP000000539; Chromosome 8. DR Bgee; ENSGALG00000010481; Expressed in colon and 14 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA. DR GO; GO:0004127; F:cytidylate kinase activity; IBA:GO_Central. DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:UniProtKB. DR GO; GO:0033862; F:UMP kinase activity; IBA:GO_Central. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0046705; P:CDP biosynthetic process; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006225; P:UDP biosynthetic process; IBA:GO_Central. DR CDD; cd01428; ADK; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1. DR HAMAP; MF_03172; Adenylate_kinase_UMP_CMP_kin; 1. DR InterPro; IPR000850; Adenylat/UMP-CMP_kin. DR InterPro; IPR033690; Adenylat_kinase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006266; UMP_CMP_kinase. DR NCBIfam; TIGR01359; UMP_CMP_kin_fam; 1. DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1. DR PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1. DR Pfam; PF00406; ADK; 1. DR PRINTS; PR00094; ADENYLTKNASE. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. PE 2: Evidence at transcript level; KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; KW Pyrimidine biosynthesis; Reference proteome; Transferase. FT CHAIN 1..196 FT /note="UMP-CMP kinase" FT /id="PRO_0000292024" FT REGION 33..63 FT /note="NMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT REGION 133..143 FT /note="LID" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 13..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 39 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 61..63 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 93..96 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 100 FT /ligand="CMP" FT /ligand_id="ChEBI:CHEBI:60377" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 134 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 140 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 151 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 179 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" SQ SEQUENCE 196 AA; 22172 MW; AF93779E27A247FA CRC64; MKPVVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGDLLRD ERKRPGSQYG ELIENYIKEG EIVPVEITIS LLKRAMDQTM AANSQKNKFL IDGFPRNEDN LQGWNKTMDG KADVSFVLFF DCDNEICIGR CLERGKSSGR SDDNRESLEK RIHTYLQSTR PIIDLYERMG KVRRVDASKS VDEVFEKVVQ IFDKEG //