ID   CYDK_THEKO              Reviewed;         278 AA.
AC   Q5JEK6;
DT   27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Cytidine kinase {ECO:0000303|PubMed:25822915};
DE            EC=2.7.1.213 {ECO:0000269|PubMed:25822915};
GN   OrderedLocusNames=TK1843 {ECO:0000312|EMBL:BAD86032.1};
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=25822915; DOI=10.1038/nchembio.1786;
RA   Aono R., Sato T., Imanaka T., Atomi H.;
RT   "A pentose bisphosphate pathway for nucleoside degradation in Archaea.";
RL   Nat. Chem. Biol. 11:355-360(2015).
CC   -!- FUNCTION: Involved in nucleoside degradation. Phosphorylates cytidine
CC       to CMP. Can also act on deoxycytidine and uridine, but is most active
CC       with cytidine. ATP is the most preferred phosphate donor, but it can
CC       also use GTP, CTP or UTP. {ECO:0000269|PubMed:25822915}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.213;
CC         Evidence={ECO:0000269|PubMed:25822915};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:25822915};
CC       Note=Mg(2+) is the preferred cation, followed by Mn(2+) and Co(2+).
CC       {ECO:0000269|PubMed:25822915};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.71 mM for cytidine {ECO:0000269|PubMed:25822915};
CC         KM=4.11 mM for deoxycytidine {ECO:0000269|PubMed:25822915};
CC         KM=5.72 mM for ATP {ECO:0000269|PubMed:25822915};
CC         Vmax=552 umol/min/mg enzyme with cytidine as substrate
CC         {ECO:0000269|PubMed:25822915};
CC         Vmax=446 umol/min/mg enzyme with deoxycytidine as substrate
CC         {ECO:0000269|PubMed:25822915};
CC         Vmax=438 umol/min/mg enzyme toward ATP {ECO:0000269|PubMed:25822915};
CC         Note=kcat is 280 sec(-1) with cytidine as substrate. kcat is 226
CC         sec(-1) with deoxycytidine as substrate. kcat is 222 sec(-1) with ATP
CC         as substrate. {ECO:0000269|PubMed:25822915};
CC       pH dependence:
CC         High levels of activity within a broad pH range of 5.0-9.0.
CC         {ECO:0000269|PubMed:25822915};
CC       Temperature dependence:
CC         Optimum temperature is 90 degrees Celsius.
CC         {ECO:0000269|PubMed:25822915};
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000305}.
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DR   EMBL; AP006878; BAD86032.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5JEK6; -.
DR   SMR; Q5JEK6; -.
DR   STRING; 69014.TK1843; -.
DR   EnsemblBacteria; BAD86032; BAD86032; TK1843.
DR   KEGG; tko:TK1843; -.
DR   PATRIC; fig|69014.16.peg.1800; -.
DR   eggNOG; arCOG00014; Archaea.
DR   HOGENOM; CLU_065902_2_1_2; -.
DR   InParanoid; Q5JEK6; -.
DR   OMA; DMNTRDT; -.
DR   OrthoDB; 98664at2157; -.
DR   PhylomeDB; Q5JEK6; -.
DR   BioCyc; MetaCyc:MON-19661; -.
DR   BRENDA; 2.7.1.213; 5246.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR002139; Ribo/fructo_kinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   Pfam; PF00294; PfkB; 1.
DR   PRINTS; PR00990; RIBOKINASE.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   PROSITE; PS00584; PFKB_KINASES_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Magnesium; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..278
FT                   /note="Cytidine kinase"
FT                   /id="PRO_0000441668"
FT   ACT_SITE        237
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q57849"
FT   BINDING         203..208
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q57849"
SQ   SEQUENCE   278 AA;  30419 MW;  3D5E6A8468BE5B9C CRC64;
     MLDLVVIGHV SIDTLIFPDG RRVTMPGGAA AGVATSAALA GAKVGLVTKI GTDFPKEWLQ
     ALSSVLDISG VQILPGKTIH IQMIYHEDGS VDAPVEMGVA QKMGEIPIPE EYLDAKVFHI
     SPIPPEEQLK LLNRLKGKRV TVDFNPTYKE EYIKRRDLLR EIVSRVEIVF PNEREALMIT
     GAEDVKDAAR ILHGWGAKLV VITRGEKGVL VYDGSFREFP ALPIKPEEIV DPTGGGDAFA
     GGFLAGYSRG RPLEECVRLG LERAREVLKK WGDWSITV