KCY_METST
ID KCY_METST Reviewed; 173 AA.
AC Q2NFY4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Msp_0881;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000102; ABC57269.1; -; Genomic_DNA.
DR RefSeq; WP_011406468.1; NC_007681.1.
DR AlphaFoldDB; Q2NFY4; -.
DR SMR; Q2NFY4; -.
DR STRING; 339860.Msp_0881; -.
DR EnsemblBacteria; ABC57269; ABC57269; Msp_0881.
DR GeneID; 41325456; -.
DR KEGG; mst:Msp_0881; -.
DR eggNOG; arCOG01037; Archaea.
DR HOGENOM; CLU_079959_1_0_2; -.
DR OMA; ADFRFWL; -.
DR OrthoDB; 110333at2157; -.
DR Proteomes; UP000001931; 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..173
FT /note="Cytidylate kinase"
FT /id="PRO_1000005679"
FT BINDING 7..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00239"
SQ SEQUENCE 173 AA; 19626 MW; B9FBAD9B944A3CDE CRC64;
MIITIGGLAG TGTSTTAKTL SQEINIPFIS AGDVFRQMAV ENNMTLLEFS EFAEGNDNID
KALDKRQAEI ANNSENLIVE GRISAFFVNA DYRIWLKAPD NVRAERISYR EDKSLDTVKQ
EIAERTASER KRYMEIHDID IDNLDIYDLI INTDTFNIES TVNIIKKCIE NKK
