KCY_DESA1
ID KCY_DESA1 Reviewed; 185 AA.
AC B8D5U4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=DKAM_1149;
OS Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 /
OS 1221n) (Desulfurococcus kamchatkensis).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Desulfurococcus.
OX NCBI_TaxID=490899;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18924 / JCM 16383 / VKM B-2413 / 1221n;
RX PubMed=19114480; DOI=10.1128/jb.01525-08;
RA Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V.,
RA Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Complete genome sequence of the anaerobic, protein-degrading
RT hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.";
RL J. Bacteriol. 191:2371-2379(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; CP001140; ACL11475.1; -; Genomic_DNA.
DR RefSeq; WP_012608816.1; NC_011766.1.
DR AlphaFoldDB; B8D5U4; -.
DR SMR; B8D5U4; -.
DR STRING; 490899.DKAM_1149; -.
DR EnsemblBacteria; ACL11475; ACL11475; DKAM_1149.
DR GeneID; 7171240; -.
DR KEGG; dka:DKAM_1149; -.
DR eggNOG; arCOG01037; Archaea.
DR HOGENOM; CLU_079959_1_0_2; -.
DR OMA; ADFRFWL; -.
DR Proteomes; UP000006903; 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..185
FT /note="Cytidylate kinase"
FT /id="PRO_1000125310"
FT BINDING 8..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00239"
SQ SEQUENCE 185 AA; 20955 MW; AE81BD4D8345461A CRC64;
MVKIVFSGPP GSGKTTQAKR VAEYYGLKYF SAGSLFREYA RRKGVSLEEL SRIALEDPSI
DLEIDRMTLE TVRDSDDIVI DGHLAAWIVS DIVDLKIYVT APLTLRILRV AGRDNTPLGK
ALAETLIREY SQRRRFMEYY GIDIYDTSIF DLTINTKLIG VEEAFNIIKS IIDKILKEKH
GSMSE
