ID KCY_SHEON Reviewed; 230 AA. AC Q8EEH9; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-NOV-2024, entry version 114. 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}; OrderedLocusNames=SO_2403; OS Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG OS 19005 / NCIMB 14063 / MR-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=211586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / RC MR-1; RX PubMed=12368813; DOI=10.1038/nbt749; RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A., RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C., RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J., RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J., RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V., RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.; RT "Genome sequence of the dissimilatory metal ion-reducing bacterium RT Shewanella oneidensis."; RL Nat. Biotechnol. 20:1118-1123(2002). 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; AE014299; AAN55437.1; -; Genomic_DNA. DR RefSeq; NP_717993.1; NC_004347.2. DR RefSeq; WP_011072382.1; NZ_CP053946.1. DR AlphaFoldDB; Q8EEH9; -. DR SMR; Q8EEH9; -. DR STRING; 211586.SO_2403; -. DR PaxDb; 211586-SO_2403; -. DR KEGG; son:SO_2403; -. DR PATRIC; fig|211586.12.peg.2312; -. DR eggNOG; COG0283; Bacteria. DR HOGENOM; CLU_079959_2_0_6; -. DR OrthoDB; 9807434at2; -. DR PhylomeDB; Q8EEH9; -. DR BioCyc; SONE211586:G1GMP-2197-MONOMER; -. DR Proteomes; UP000008186; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004127; F:(d)CMP kinase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA. DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA. DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd02020; CMPK; 1. DR FunFam; 3.40.50.300:FF:000262; Cytidylate kinase; 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; Reference proteome; KW Transferase. FT CHAIN 1..230 FT /note="Cytidylate kinase" FT /id="PRO_0000131970" FT BINDING 12..20 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00238" SQ SEQUENCE 230 AA; 25212 MW; BE48A1DCC01E5570 CRC64; MSERAPVVTI DGPSGAGKGT ISQLLAKHLG WQLLDSGAIY RVLALAAIHH DVELENEESI TLLASHLDVK FLTGNEKDPV QVILEGEDVT TAIRTQECSN AASKVAAFPR VREALLRRQR AFRTAPGLIA DGRDMGTVVF PTASAKLYLT ASAQERAQRR YNQLQDKGFD VNIERLLAEI IERDDRDMNR PVAPLVPAEN ALVIDTSDKG IDEVLELALN YINQKLSSTN //