KCY_IGNH4
ID KCY_IGNH4 Reviewed; 172 AA.
AC A8AAI6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=Igni_0756;
OS Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignicoccus.
OX NCBI_TaxID=453591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT Nanoarchaeum equitans.";
RL Genome Biol. 9:R158.1-R158.18(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; CP000816; ABU81938.1; -; Genomic_DNA.
DR RefSeq; WP_012122902.1; NC_009776.1.
DR AlphaFoldDB; A8AAI6; -.
DR SMR; A8AAI6; -.
DR STRING; 453591.Igni_0756; -.
DR EnsemblBacteria; ABU81938; ABU81938; Igni_0756.
DR GeneID; 5561748; -.
DR KEGG; iho:Igni_0756; -.
DR eggNOG; arCOG01037; Archaea.
DR HOGENOM; CLU_079959_1_0_2; -.
DR OMA; FIFRDMA; -.
DR OrthoDB; 110333at2157; -.
DR PhylomeDB; A8AAI6; -.
DR Proteomes; UP000000262; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..172
FT /note="Cytidylate kinase"
FT /id="PRO_1000005668"
FT BINDING 8..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00239"
SQ SEQUENCE 172 AA; 19113 MW; 0E5DE3F0F284FC4A CRC64;
MTVVVISGPP GSGKSTVAKK LASELGLRFV SAGSVFRKLA EEIGVSLLEL NEMALKDPEI
DLRIDRMVLE EARRGNVVIE AHLGGWVAAP YADVNVYLTA PLEERAKRIA RRDGISYEEA
LEEILSREEV QWIRFRKLYG FDVASLEIFD LVVNTALMGP EAVVETIKRM LL