ID KCY_BURM7 Reviewed; 228 AA. AC A3MHN9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 04-NOV-2026, entry version 87. DE RecName: Full=Cytidylate kinase {ECO:0000255|HAMAP-Rule:MF_00238}; DE Short=CK {ECO:0000255|HAMAP-Rule:MF_00238}; DE EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00238}; DE AltName: Full=Cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00238}; DE Short=CMP kinase {ECO:0000255|HAMAP-Rule:MF_00238}; GN Name=cmk {ECO:0000255|HAMAP-Rule:MF_00238}; GN OrderedLocusNames=BMA10247_0200; OS Burkholderia mallei (strain NCTC 10247). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320389; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 10247; RX PubMed=20333227; DOI=10.1093/gbe/evq003; RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S., RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J., RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P., RA Nierman W.C.; RT "Continuing evolution of Burkholderia mallei through genome reduction and RT large-scale rearrangements."; RL Genome Biol. Evol. 2:102-116(2010). CC -!- CATALYTIC ACTIVITY: CC Reaction=CMP + ATP = CDP + ADP; Xref=Rhea:RHEA:11600, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, CC ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00238}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dCMP + ATP = dCDP + ADP; Xref=Rhea:RHEA:25094, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, CC ChEBI:CHEBI:456216; EC=2.7.4.25; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00238}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00238}. CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00238}. 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; CP000548; ABO04174.1; -; Genomic_DNA. DR RefSeq; WP_004189396.1; NC_009080.1. DR AlphaFoldDB; A3MHN9; -. DR SMR; A3MHN9; -. DR GeneID; 92978200; -. DR KEGG; bmaz:BM44_2791; -. DR KEGG; bmn:BMA10247_0200; -. DR PATRIC; fig|320389.8.peg.3150; -. DR OMA; AAAMGWH; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0036430; F:CMP kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0036431; F:dCMP kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IEA:TreeGrafter. DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd02020; CMPK; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00238; Cytidyl_kinase_type1; 1. DR InterPro; IPR003136; Cytidylate_kin. DR InterPro; IPR011994; Cytidylate_kinase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR00017; cmk; 1. DR PANTHER; PTHR21299:SF2; CYTIDYLATE KINASE; 1. DR PANTHER; PTHR21299; CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE; 1. DR Pfam; PF02224; Cytidylate_kin; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase. FT CHAIN 1..228 FT /note="Cytidylate kinase" FT /id="PRO_1000048196" FT BINDING 17..25 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00238" SQ SEQUENCE 228 AA; 24367 MW; 84471B8596B1EBBE CRC64; MKSTRPFHPT PVITIDGPTA SGKGTVAALV AAHLGFHLLD SGALYRLAAL ASIRYQVEPD DADALASLVD GLHITFREGC AQLDGVDVSD EIRAEAVGNR ASAIAVHASV RAALVARQRA FRKTPGLVAD GRDMGTLIFP DAVLKVFLTA SVEARAARRH KQLMQKGFSA NIDNLLQDLR ERDARDSNRA AAPLKPAADA KPLDTSALTI EQSVEQVLAW YRELGQPA //