KCY_YERPY
ID KCY_YERPY Reviewed; 230 AA.
AC B1JRD8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=YPK_2669;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) 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; CP000950; ACA68946.1; -; Genomic_DNA.
DR RefSeq; WP_002211324.1; NZ_CP009792.1.
DR PDB; 4E22; X-ray; 2.32 A; A=1-230.
DR PDBsum; 4E22; -.
DR AlphaFoldDB; B1JRD8; -.
DR SMR; B1JRD8; -.
DR EnsemblBacteria; ACA68946; ACA68946; YPK_2669.
DR GeneID; 66842149; -.
DR KEGG; ypy:YPK_2669; -.
DR PATRIC; fig|502800.11.peg.3369; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..230
FT /note="Cytidylate kinase"
FT /id="PRO_1000100707"
FT BINDING 12..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00238"
FT TURN 2..4
FT /evidence="ECO:0007829|PDB:4E22"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:4E22"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:4E22"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:4E22"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:4E22"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:4E22"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:4E22"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:4E22"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:4E22"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:4E22"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:4E22"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:4E22"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:4E22"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:4E22"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:4E22"
FT HELIX 151..165
FT /evidence="ECO:0007829|PDB:4E22"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:4E22"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:4E22"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4E22"
FT HELIX 209..223
FT /evidence="ECO:0007829|PDB:4E22"
SQ SEQUENCE 230 AA; 25195 MW; 529E89F71198679F CRC64;
MTAIAPVITV DGPSGAGKGT LCKALAESLN WRLLDSGAIY RVLALAALHH QVDISTEEAL
VPLAAHLDVR FVSQNGQLQV ILEGEDVSNE IRTETVGNTA SQAAAFPRVR EALLRRQRAF
REAPGLIADG RDMGTIVFPD APVKIFLDAS SQERAHRRML QLQERGFNVN FERLLAEIQE
RDNRDRNRSV APLVPAADAL VLDSTSMSIE QVIEQALAYA QRILALPLKK
