ID KCY_LISMO Reviewed; 224 AA.
AC Q8Y5W6;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 118.
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=lmo1939;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL591981; CAD00017.1; -; Genomic_DNA.
DR PIR; AC1317; AC1317.
DR RefSeq; NP_465463.1; NC_003210.1.
DR RefSeq; WP_003723586.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y5W6; -.
DR SMR; Q8Y5W6; -.
DR STRING; 169963.gene:17594624; -.
DR PaxDb; 169963-lmo1939; -.
DR EnsemblBacteria; CAD00017; CAD00017; CAD00017.
DR GeneID; 984888; -.
DR KEGG; lmo:lmo1939; -.
DR PATRIC; fig|169963.11.peg.1986; -.
DR eggNOG; COG0283; Bacteria.
DR HOGENOM; CLU_079959_0_2_9; -.
DR OrthoDB; 9807434at2; -.
DR PhylomeDB; Q8Y5W6; -.
DR BioCyc; LMON169963:LMO1939-MONOMER; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA.
DR GO; GO:0004127; F:cytidylate kinase activity; IBA:GO_Central.
DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IBA:GO_Central.
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; 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..224
FT /note="Cytidylate kinase"
FT /id="PRO_0000131930"
FT BINDING 11..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00238"
SQ SEQUENCE 224 AA; 24817 MW; 1CEBA268137C3A66 CRC64;
MTKKICIAID GPAAAGKSTV AKIVAKKLRF VYIDTGAMYR AVTYIALKNN IAYEDEKAIA
ALLQKTVIRF EPGEVQQVFV GSENVTEVIR SIEVTNHVSI VAAHPSIREA LQERQQVFAT
EGGIVMDGRD IGTAVLPNAE LKIFLLASVE ERAERRYKEN MAKGFTGDLD QLKKEIEERD
HLDYTRTHSP LKKADDAIEV DTTSMSIDQV ANKILSLAEL KINN
//
