KCY_SHEAM
ID KCY_SHEAM Reviewed; 231 AA.
AC A1S6D4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Sama_1735;
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-2006) 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; CP000507; ABL99940.1; -; Genomic_DNA.
DR RefSeq; WP_011759848.1; NC_008700.1.
DR AlphaFoldDB; A1S6D4; -.
DR SMR; A1S6D4; -.
DR STRING; 326297.Sama_1735; -.
DR EnsemblBacteria; ABL99940; ABL99940; Sama_1735.
DR KEGG; saz:Sama_1735; -.
DR eggNOG; COG0283; Bacteria.
DR HOGENOM; CLU_079959_2_0_6; -.
DR OMA; RAITWWM; -.
DR OrthoDB; 776861at2; -.
DR Proteomes; UP000009175; 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_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; Reference proteome;
KW Transferase.
FT CHAIN 1..231
FT /note="Cytidylate kinase"
FT /id="PRO_1000048271"
FT BINDING 12..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00238"
SQ SEQUENCE 231 AA; 24951 MW; 2E9A311BEF7CC5A0 CRC64;
MSERAPVVTI DGPSGAGKGT IAHLLAKHYG WQLLDSGAIY RVLALAALHH NVELENEEAI
TLLAAHLDVQ FLAGGDKDAI KVVLEGEDVT GAIRTQECSN AASKVAAFPR VREALLRRQR
AFCQAPGLIA DGRDMGTVVF PTAPAKLYLT ASAEERAQRR YNQLQDKGFD VKIDRLLAEI
QERDDRDMNR PVAPLVPADD ALVIDTTGIG IDDVFAQCVA HINDKLSASG F
