ID   A0LU96_ACIC1            Unreviewed;       255 AA.
AC   A0LU96;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   02-SEP-2026, entry version 106.
DE   RecName: Full=Cytidylate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE            Short=CK {ECO:0000256|HAMAP-Rule:MF_00238};
DE            EC=2.7.4.25 {ECO:0000256|HAMAP-Rule:MF_00238};
DE   AltName: Full=Cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_00238};
DE            Short=CMP kinase {ECO:0000256|HAMAP-Rule:MF_00238};
GN   Name=cmk {ECO:0000256|HAMAP-Rule:MF_00238};
GN   OrderedLocusNames=Acel_1234 {ECO:0000313|EMBL:ABK53006.1};
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Acidothermales;
OC   Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK53006.1, ECO:0000313|Proteomes:UP000008221};
RN   [1] {ECO:0000313|EMBL:ABK53006.1, ECO:0000313|Proteomes:UP000008221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B
RC   {ECO:0000313|Proteomes:UP000008221};
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00048478, ECO:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00047615, ECO:0000256|HAMAP-
CC         Rule:MF_00238};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238}.
CC   -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009427, ECO:0000256|HAMAP-Rule:MF_00238}.
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DR   EMBL; CP000481; ABK53006.1; -; Genomic_DNA.
DR   RefSeq; WP_011720069.1; NC_008578.1.
DR   AlphaFoldDB; A0LU96; -.
DR   FunCoup; A0LU96; 38.
DR   STRING; 351607.Acel_1234; -.
DR   KEGG; ace:Acel_1234; -.
DR   eggNOG; COG0283; Bacteria.
DR   HOGENOM; CLU_079959_0_0_11; -.
DR   InParanoid; A0LU96; -.
DR   OrthoDB; 9807434at2; -.
DR   Proteomes; UP000008221; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00238}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00238};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00238};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00238}; Reference proteome {ECO:0000313|Proteomes:UP000008221};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00238}.
FT   DOMAIN          12..226
FT                   /note="Cytidylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF02224"
FT   REGION          229..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         16..24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00238"
SQ   SEQUENCE   255 AA;  26846 MW;  BCC8BF4F4261DACF CRC64;
     MKTRDELRSM VIAIDGPAGA GKSTVARAVA RRLGLRYLDT GAMYRAVTLW VLRNGVSLTD
     ERAVSAAARH VVDILDLALA PDHPAVRLDG VDVTDAVRGP EVTQAVSAVS AVPEVRSVLV
     GRQRELIGDG GIVVEGRDIG TTVWPTAAVK IFLTADSRVR AARRHADTVA ARGTTDVDDV
     HDDLRRRDQL DQSRAASPLT AAADAVVLDS TDLDVDAVLD RILSLVAERL GSGGDPTSPS
     DAGLDRTVNP SPATP
//