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KCY_METPE
ID   KCY_METPE               Reviewed;         176 AA.
AC   B8GKF9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=Mpal_0468;
OS   Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX   NCBI_TaxID=521011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c;
RX   PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA   Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA   Yavitt J.B., Zinder S.H.;
RT   "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT   Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL   Genome Announc. 3:0-0(2015).
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; CP001338; ACL15842.1; -; Genomic_DNA.
DR   RefSeq; WP_012617161.1; NC_011832.1.
DR   AlphaFoldDB; B8GKF9; -.
DR   SMR; B8GKF9; -.
DR   STRING; 521011.Mpal_0468; -.
DR   EnsemblBacteria; ACL15842; ACL15842; Mpal_0468.
DR   GeneID; 7272792; -.
DR   KEGG; mpl:Mpal_0468; -.
DR   eggNOG; arCOG01037; Archaea.
DR   HOGENOM; CLU_079959_1_0_2; -.
DR   OMA; ADFRFWL; -.
DR   OrthoDB; 110333at2157; -.
DR   Proteomes; UP000002457; 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..176
FT                   /note="Cytidylate kinase"
FT                   /id="PRO_1000125312"
FT   BINDING         7..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00239"
SQ   SEQUENCE   176 AA;  19628 MW;  8E30E6EEFBAA3F81 CRC64;
     MRITISGPPG SGTTSLSKHL AAEHNLKLIS AGEVFRQLAR EKGMDLAAFG ELAENDPSID
     LMIDARQKQI ATEQDDIIVE GRLSGRMVEQ ADLRIWLNAP LTCRVGRIAF RDSVTCEEEA
     MTLTREREAS EAKRYMMYYQ IDISDLSSYH LVLNTERWSV GQLGLIVNCA IAAVRD
 
 
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