Cytidylate kinase (P0A6I0)

Identification
Name:Cytidylate kinase
Synonyms:
  • CK
  • Cytidine monophosphate kinase
  • CMP kinase
  • Protein mssA
  • p25
Gene Name:cmk
Enzyme Class:
Biological Properties
General Function:Involved in cytidylate kinase activity
Specific Function:ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Uridine 5'-monophosphate ↔ 1.0ADP + 1.0Uridine 5'-diphosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Cytidine monophosphate ↔ 1.0ADP + 1.0CDP
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0dCMP ↔ 1.0ADP + 1.0dCDP
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0dCMP + 1.0Uridine 5'-monophosphate ↔ 1.0ADP + 1.0dCDP + 1.0Uridine 5'-diphosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Uridine 5'-monophosphate ↔ 1.0ADP + 1.0Uridine 5'-diphosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Cytidine monophosphate ↔ 1.0ADP + 1.0CDP
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0dCMP ↔ 1.0ADP + 1.0dCDP
ReactionCard
1.0Thumb+1.0Thumb ? 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0dCMP ? 1.0ADP + 1.0dCDP
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0dCMP → 1.0ADP + 1.0dCDP
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01546CDPMetaboCard
ECMDB00095Cytidine monophosphateMetaboCard
ECMDB01245dCDPMetaboCard
ECMDB01202dCMPMetaboCard
ECMDB21526Deoxycytidine 5'-phosphateMetaboCard
ECMDB00295Uridine 5'-diphosphateMetaboCard
ECMDB00288Uridine 5'-monophosphateMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
cytidylate kinase activity
kinase activity
nucleobase, nucleoside, nucleotide kinase activity
nucleoside binding
nucleotide kinase activity
purine nucleoside binding
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
cellular nitrogen compound metabolic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
Gene Properties
Blattner:b0910
Gene OrientationClockwise
Centisome Percentage:20.70
Left Sequence End960424
Right Sequence End961107
Gene Sequence:
>684 bp
ATGACGGCAATTGCCCCGGTTATTACCATTGATGGCCCAAGCGGTGCAGGGAAAGGCACC
TTGTGTAAGGCTATGGCGGAAGCGTTGCAATGGCATCTGCTGGACTCGGGTGCAATTTAT
CGCGTACTGGCATTGGCGGCATTACATCACCATGTTGATGTTGCGTCGGAAGATGCGCTG
GTACCGCTGGCATCCCATCTGGATGTACGTTTTGTGTCGACCAATGGCAATCTGGAAGTG
ATCCTCGAAGGGGAAGATGTCAGCGGCGAAATTCGTACTCAGGAAGTGGCGAATGCAGCT
TCACAAGTCGCGGCATTCCCACGCGTTCGTGAAGCATTATTGCGTCGCCAACGCGCGTTT
CGCGAATTACCAGGTCTGATTGCCGATGGCCGCGACATGGGAACGGTGGTATTCCCTGAT
GCACCAGTGAAAATTTTCCTTGACGCCTCCTCGGAAGAACGTGCGCATCGCCGCATGCTA
CAGTTGCAGGAGAAGGGCTTTAGTGTTAACTTTGAGCGCCTTTTGGCCGAGATCAAAGAA
CGCGACGACCGCGATCGTAACCGAGCGGTAGCGCCACTGGTTCCGGCAGCCGATGCTTTA
GTGTTGGATTCCACCACCTTAAGCATTGAGCAAGTGATTGAAAAAGCGCTACAATACGCG
CGCCAGAAATTGGCTCTCGCATAA
Protein Properties
Pfam Domain Function:
Protein Residues:227
Protein Molecular Weight:24746
Protein Theoretical pI:6
PDB File:1KDT
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Cytidylate kinase
MTAIAPVITIDGPSGAGKGTLCKAMAEALQWHLLDSGAIYRVLALAALHHHVDVASEDAL
VPLASHLDVRFVSTNGNLEVILEGEDVSGEIRTQEVANAASQVAAFPRVREALLRRQRAF
RELPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQLQEKGFSVNFERLLAEIKE
RDDRDRNRAVAPLVPAADALVLDSTTLSIEQVIEKALQYARQKLALA
References
External Links:
ResourceLink
Uniprot ID:P0A6I0
Uniprot Name:KCY_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651431
PDB ID:1KDT
Ecogene ID:EG11265
Ecocyc:EG11265
ColiBase:b0910
Kegg Gene:b0910
EchoBASE ID:EB1244
CCDB:KCY_ECOLI
BacMap:16128877
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Briozzo, P., Golinelli-Pimpaneau, B., Gilles, A. M., Gaucher, J. F., Burlacu-Miron, S., Sakamoto, H., Janin, J., Barzu, O. (1998). "Structures of escherichia coli CMP kinase alone and in complex with CDP: a new fold of the nucleoside monophosphate binding domain and insights into cytosine nucleotide specificity." Structure 6:1517-1527. Pubmed: 9862805
  • Fricke, J., Neuhard, J., Kelln, R. A., Pedersen, S. (1995). "The cmk gene encoding cytidine monophosphate kinase is located in the rpsA operon and is required for normal replication rate in Escherichia coli." J Bacteriol 177:517-523. Pubmed: 7836281
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Pedersen, S., Skouv, J., Kajitani, M., Ishihama, A. (1984). "Transcriptional organization of the rpsA operon of Escherichia coli." Mol Gen Genet 196:135-140. Pubmed: 6384724
  • Schnier, J., Isono, K. (1982). "The DNA sequence of the gene rpsA of Escherichia coli coding for ribosomal protein S1." Nucleic Acids Res 10:1857-1865. Pubmed: 6281725
  • Schultz, C. P., Ylisastigui-Pons, L., Serina, L., Sakamoto, H., Mantsch, H. H., Neuhard, J., Barzu, O., Gilles, A. M. (1997). "Structural and catalytic properties of CMP kinase from Bacillus subtilis: a comparative analysis with the homologous enzyme from Escherichia coli." Arch Biochem Biophys 340:144-153. Pubmed: 9126287
  • Yamanaka, K., Ogura, T., Koonin, E. V., Niki, H., Hiraga, S. (1994). "Multicopy suppressors, mssA and mssB, of an smbA mutation of Escherichia coli." Mol Gen Genet 243:9-16. Pubmed: 8190075