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 16-OCT-2013, entry version 65. DE RecName: Full=Cytidylate kinase; DE Short=CK; DE EC=2.7.4.25; DE AltName: Full=Cytidine monophosphate kinase; DE Short=CMP kinase; GN Name=cmk; OrderedLocusNames=SO_2403; OS Shewanella oneidensis (strain MR-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=211586; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=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., RA Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J., RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., RA Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A., RA White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M., RA Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J., RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., RA 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: ATP + (d)CMP = ADP + (d)CDP. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 CC subfamily. 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 ProteinModelPortal; Q8EEH9; -. DR SMR; Q8EEH9; 5-227. DR STRING; 211586.SO_2403; -. DR EnsemblBacteria; AAN55437; AAN55437; SO_2403. DR GeneID; 1170120; -. DR KEGG; son:SO_2403; -. DR PATRIC; 23524425; VBISheOne101494_2312. DR eggNOG; COG0283; -. DR HOGENOM; HOG000242849; -. DR KO; K00945; -. DR OMA; HIDTGAM; -. DR ProtClustDB; PRK00023; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004127; F:cytidylate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-HAMAP. 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 PANTHER; PTHR21299:SF2; PTHR21299:SF2; 1. DR Pfam; PF02224; Cytidylate_kin; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00017; cmk; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 230 Cytidylate kinase. FT /FTId=PRO_0000131970. FT NP_BIND 12 20 ATP (By similarity). 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 //