ID   KCY_SHEPW               Reviewed;         230 AA.
AC   B8CMH3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=swp_2489;
OS   Shewanella piezotolerans (strain WP3 / JCM 13877).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=225849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP3 / JCM 13877;
RX   PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA   Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA   Bartlett D.H., Yu J., Hu S., Xiao X.;
RT   "Environmental adaptation: genomic analysis of the piezotolerant and
RT   psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT   WP3.";
RL   PLoS ONE 3:E1937-E1937(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CMP = ADP + CDP; 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=ATP + dCMP = ADP + dCDP; 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; CP000472; ACJ29230.1; -; Genomic_DNA.
DR   RefSeq; WP_020912588.1; NC_011566.1.
DR   AlphaFoldDB; B8CMH3; -.
DR   SMR; B8CMH3; -.
DR   STRING; 225849.swp_2489; -.
DR   PRIDE; B8CMH3; -.
DR   EnsemblBacteria; ACJ29230; ACJ29230; swp_2489.
DR   KEGG; swp:swp_2489; -.
DR   eggNOG; COG0283; Bacteria.
DR   HOGENOM; CLU_079959_2_0_6; -.
DR   OMA; RAITWWM; -.
DR   OrthoDB; 776861at2; -.
DR   Proteomes; UP000000753; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02020; CMPK; 1.
DR   Gene3D; 3.40.50.300; -; 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   Pfam; PF02224; Cytidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00017; cmk; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..230
FT                   /note="Cytidylate kinase"
FT                   /id="PRO_1000119027"
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;  24984 MW;  CC14E86AC4A7AB94 CRC64;
     MLERAPVVTV DGPSGAGKGT ISQLLAEKLG YKLLDSGAIY RVLALAAIHH NVELDNEESL
     TLLAAHLDVQ FITGNESKGI KVVLEGEDVS TTIRSQECSN AASKVAAFPR VREALLRRQR
     AFAEAPGLIA DGRDMGTVVF PATPAKLFLT ASAEERAQRR YNQLQDNGFD VKIDQLLSEI
     KERDDRDMNR SVAPLVPAED ALVIDTTNIS IEDVLAMALT HIHKSFQVPA