KCY_SULIY
ID KCY_SULIY Reviewed; 189 AA.
AC C3NEH0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, 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=YG5714_1442;
OS Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=439386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y.G.57.14 / Yellowstone #1;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001403; ACP45709.1; -; Genomic_DNA.
DR RefSeq; WP_012716182.1; NC_012622.1.
DR AlphaFoldDB; C3NEH0; -.
DR SMR; C3NEH0; -.
DR EnsemblBacteria; ACP45709; ACP45709; YG5714_1442.
DR GeneID; 7809793; -.
DR GeneID; 8761480; -.
DR KEGG; siy:YG5714_1442; -.
DR HOGENOM; CLU_079959_1_0_2; -.
DR OMA; FIFRDMA; -.
DR Proteomes; UP000002308; 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..189
FT /note="Cytidylate kinase"
FT /id="PRO_1000204464"
FT BINDING 7..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00239"
SQ SEQUENCE 189 AA; 21730 MW; 9EB1BE5205D8A3E6 CRC64;
MIIIISGPPG SGKTSVAIKL ANELSYKFIS AGKIFRDIAQ KMGLDIINLN KVAESNFDID
KMVDKKIFEF ILSEKNLIIE SHIAGWLFRE YTNIAIYLWA PLKIRANRIA IRDKISYDQA
ISQIIKREYM HYKRFNKFYG IDINDLSVFD LVINTSNVDV NNIVKLILTY LSLVSQNPQP
LKEKDINDK