ID   KCY_RHOOB               Reviewed;         229 AA.
AC   C1ASX3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   02-SEP-2026, entry version 96.
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=ROP_06580;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AP011115; BAH48905.1; -; Genomic_DNA.
DR   RefSeq; WP_012687908.1; NC_012522.1.
DR   AlphaFoldDB; C1ASX3; -.
DR   SMR; C1ASX3; -.
DR   STRING; 632772.ROP_06580; -.
DR   KEGG; rop:ROP_06580; -.
DR   PATRIC; fig|632772.20.peg.718; -.
DR   HOGENOM; CLU_079959_0_0_11; -.
DR   OrthoDB; 9807434at2; -.
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..229
FT                   /note="Cytidylate kinase"
FT                   /id="PRO_1000125295"
FT   BINDING         12..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00238"
SQ   SEQUENCE   229 AA;  24051 MW;  288A691F136B0069 CRC64;
     MSTSSLIVAM DGPSGTGKSS VSRMLARRLG ARYLDTGAMY RIATLHVLRK GVDLADPDAI
     ADATVGLPWS IGTDPAGEQV LLDGEDVGEE IRGDAVTKAV SAVSAVPAVR ELLVAAQRRL
     ACEAGRIVVE GRDIGTVVLP DADVKIYLTA SAEARAQRRN AQNLAEGRGD DFAAVLADVQ
     RRDHLDSTRA VSPLRPADDS VLVDTSELGI DDVIGRLLLV VSERSGVGQ
//