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KCY_HALS3
ID   KCY_HALS3               Reviewed;         192 AA.
AC   B0R685;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=OE_3429F;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(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_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; AM774415; CAP14254.1; -; Genomic_DNA.
DR   RefSeq; WP_010903263.1; NC_010364.1.
DR   AlphaFoldDB; B0R685; -.
DR   SMR; B0R685; -.
DR   PRIDE; B0R685; -.
DR   EnsemblBacteria; CAP14254; CAP14254; OE_3429F.
DR   GeneID; 5953084; -.
DR   GeneID; 62887117; -.
DR   KEGG; hsl:OE_3429F; -.
DR   HOGENOM; CLU_079959_1_0_2; -.
DR   OMA; ADFRFWL; -.
DR   PhylomeDB; B0R685; -.
DR   Proteomes; UP000001321; 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_00239; Cytidyl_kinase_type2; 1.
DR   InterPro; IPR011892; Cyt_kin_arch.
DR   InterPro; IPR011994; Cytidylate_kinase_dom.
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..192
FT                   /note="Cytidylate kinase"
FT                   /id="PRO_1000100708"
FT   BINDING         7..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00239"
SQ   SEQUENCE   192 AA;  21632 MW;  4BEC104FDFC0AB85 CRC64;
     MLVTISGPPG SGKSTVASTL ADHLSYEHIS GGDIFRGLAE DRDLTLAEFN ELAEEDPQID
     KDLDRRLRET ARGRDDIVLE SRLAGWMAGE YADIKIWLDA PMSVRARRIA EREDKTPAAA
     RAETEAREES ETQRYEEYYA IDFDDITIYD LSVNTARWGP DAVTDIVLDA VDAYQAERDE
     GPTPIENVRY QF
 
 
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