ID   KCY_METS3               Reviewed;         172 AA.
AC   A5UL61;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Cytidylate kinase {ECO:0000255|HAMAP-Rule:MF_00239};
DE            Short=CK {ECO:0000255|HAMAP-Rule:MF_00239};
DE            EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00239};
DE   AltName: Full=Cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00239};
DE            Short=CMP kinase {ECO:0000255|HAMAP-Rule:MF_00239};
GN   Name=cmk {ECO:0000255|HAMAP-Rule:MF_00239}; OrderedLocusNames=Msm_0734;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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_00239};
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_00239};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00239}.
CC   -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00239}.
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DR   EMBL; CP000678; ABQ86939.1; -; Genomic_DNA.
DR   RefSeq; WP_004033247.1; NC_009515.1.
DR   AlphaFoldDB; A5UL61; -.
DR   SMR; A5UL61; -.
DR   STRING; 420247.Msm_0734; -.
DR   EnsemblBacteria; ABQ86939; ABQ86939; Msm_0734.
DR   GeneID; 5217067; -.
DR   KEGG; msi:Msm_0734; -.
DR   PATRIC; fig|420247.28.peg.731; -.
DR   eggNOG; arCOG01037; Archaea.
DR   HOGENOM; CLU_079959_1_0_2; -.
DR   OMA; ADFRFWL; -.
DR   Proteomes; UP000001992; 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   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00239; Cytidyl_kinase_type2; 1.
DR   InterPro; IPR011892; Cyt_kin_arch.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02173; cyt_kin_arch; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..172
FT                   /note="Cytidylate kinase"
FT                   /id="PRO_1000005678"
FT   BINDING         7..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00239"
SQ   SEQUENCE   172 AA;  19189 MW;  B80EA475F6F1F223 CRC64;
     MIITVGGLAG TGTTTTAELL SEKLGIPFVS SGSIFRAMAE EKGMSVLEFS EFAESNDNID
     KEIDKRQAEL AKSSENLILE GRLSAYFVEA DLKLWLMAPL DVRAQRISQR ESKSVDVAKE
     EIKIREESEA LRYLDIHNID ISNLDIYDLM INTDSFDPES ITKIILTTLK VI