ID   KCY_HALH5               Reviewed;         222 AA.
AC   Q9RC80; Q9KCD8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   02-SEP-2026, entry version 130.
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=BH1634;
OS   Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Halalkalibacterium (ex Joshi et al. 2022).
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-168.
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=10484179; DOI=10.1007/s007920050120;
RA   Takami H., Takaki Y., Nakasone K., Sakiyama T., Maeno G., Sasaki R.,
RA   Hirama C., Fuji F., Masui N.;
RT   "Genetic analysis of the chromosome of alkaliphilic Bacillus halodurans C-
RT   125.";
RL   Extremophiles 3:227-233(1999).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAA83919.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000004; BAB05353.1; -; Genomic_DNA.
DR   EMBL; AB024552; BAA83919.1; ALT_INIT; Genomic_DNA.
DR   PIR; B83854; B83854.
DR   RefSeq; WP_010897797.1; NC_002570.2.
DR   AlphaFoldDB; Q9RC80; -.
DR   SMR; Q9RC80; -.
DR   STRING; 272558.gene:10727532; -.
DR   KEGG; bha:BH1634; -.
DR   eggNOG; COG0283; Bacteria.
DR   HOGENOM; CLU_079959_0_2_9; -.
DR   OrthoDB; 9807434at2; -.
DR   Proteomes; UP000001258; Chromosome.
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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..222
FT                   /note="Cytidylate kinase"
FT                   /id="PRO_0000131877"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00238"
SQ   SEQUENCE   222 AA;  24862 MW;  4668F92AB691305B CRC64;
     MKKMNIAIDG PAGAGKSTVA KQVAQALSFL YIDTGAMYRA LTYAAIEHHV SPDDEASLKS
     LLDSIEIKLV DEQSKTRVYV NNTDVTDQVR TEEVTKTVSL VSSHGQVRKE MVRQQRLLAE
     GTNCVLDGRD IGTYVLPNAE LKFFLTATVE ERARRRYEEN IQKGFKQSLE QLIKDIASRD
     EFDSNRSFAP LRKAEDAIEI DTTSLSISEV TQTIIGYVKE RV
//