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KCY_GEOSM
ID   KCY_GEOSM               Reviewed;         233 AA.
AC   C6E2B2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Cytidylate kinase {ECO:0000255|HAMAP-Rule:MF_00238};
DE            Short=CK {ECO:0000255|HAMAP-Rule:MF_00238};
DE            EC=2.7.4.25 {ECO:0000255|HAMAP-Rule:MF_00238};
DE   AltName: Full=Cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00238};
DE            Short=CMP kinase {ECO:0000255|HAMAP-Rule:MF_00238};
GN   Name=cmk {ECO:0000255|HAMAP-Rule:MF_00238}; OrderedLocusNames=GM21_0993;
OS   Geobacter sp. (strain M21).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter; unclassified Geobacter.
OX   NCBI_TaxID=443144;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M21;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Lovley D.;
RT   "Complete sequence of Geobacter sp. M21.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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_00238};
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_00238};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00238}.
CC   -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00238}.
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DR   EMBL; CP001661; ACT17058.1; -; Genomic_DNA.
DR   RefSeq; WP_012774671.1; NC_012918.1.
DR   AlphaFoldDB; C6E2B2; -.
DR   SMR; C6E2B2; -.
DR   STRING; 443144.GM21_0993; -.
DR   EnsemblBacteria; ACT17058; ACT17058; GM21_0993.
DR   KEGG; gem:GM21_0993; -.
DR   eggNOG; COG0283; Bacteria.
DR   HOGENOM; CLU_079959_0_2_7; -.
DR   OMA; RAITWWM; -.
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_00238; Cytidyl_kinase_type1; 1.
DR   InterPro; IPR003136; Cytidylate_kin.
DR   InterPro; IPR011994; Cytidylate_kinase_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF02224; Cytidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00017; cmk; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..233
FT                   /note="Cytidylate kinase"
FT                   /id="PRO_1000204451"
FT   REGION          183..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         15..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00238"
SQ   SEQUENCE   233 AA;  25191 MW;  6A8C5CCBD2E21B90 CRC64;
     MSVVRENGVI VAIDGPSGAG KSSLTKLLAK RLGYIHIDTG AMFRAVALSA QRAGIASDDD
     AGLAELCRGL DITFARDGEA CRVLANGEDV SREIRTEEIG LLTSTVSARQ PVRQALLEMQ
     RKMGAKGGVI LEGRDIGTVV FPDAEVKFFL SASAEERGRR RYLELAARGE SATLEETIAK
     VVQRDRQDEG REHAPLKQAE DAVPIDSTSL TIEEVLELME RTVKERLAQG DKG
 
 
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