4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (P62615)

Identification
Name:4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
Synonyms:
  • CMK
  • 4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
Gene Name:ispE
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
Specific Function:Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. Phosphorylates isopentenyl phosphate at low rates. Also acts on isopentenol, and, much less efficiently, dimethylallyl alcohol. Dimethylallyl monophosphate does not serve as a substrate
Cellular Location:Not Available
SMPDB Pathways:
  • Secondary metabolites: isoprenoid biosynthesis (nonmevalonate pathway) PW000975
  • Secondary metabolites: methylerythritol phosphate and polyisoprenoid biosynthesis PW000958
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.04-(Cytidine 5'-diphospho)-2-C-methyl-D-erythritol + 1.0Adenosine triphosphate ↔ 1.02-Phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol + 1.0ADP + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.04-(Cytidine 5'-diphospho)-2-C-methyl-D-erythritol + 1.0Adenosine triphosphate ↔ 1.02-Phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol + 1.0ADP
ReactionCard
SMPDB Reactions:
1.04-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol+1.0Thumb+1.0Thumb → 1.0Adenosine diphosphate+1.0Thumb+1.02-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol+1.0Thumb+1.0Thumb
1.04-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol + 1.0Adenosine triphosphate + 1.04-(Cytidine 5'-diphospho)-2-C-methyl-D-erythritol → 1.0Adenosine diphosphate + 1.0Hydrogen ion + 1.02-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol + 1.0ADP + 1.02-Phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.04-(Cytidine 5'-diphospho)-2-C-methyl-D-erythritol + 1.0Adenosine triphosphate ↔ 1.02-Phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol + 1.0ADP + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.04-(Cytidine 5'-diphospho)-2-C-methyl-D-erythritol + 1.0Adenosine triphosphate ↔ 1.02-Phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol + 1.0ADP
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.04-(Cytidine 5'-diphospho)-2-C-methyl-D-erythritol → 1.0ADP + 1.02-Phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB200492-Phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritolMetaboCard
ECMDB200834-(Cytidine 5'-diphospho)-2-C-methyl-D-erythritolMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
GO Classification:
Function
4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
kinase activity
nucleoside binding
purine nucleoside binding
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
cellular lipid metabolic process
cellular metabolic process
isoprenoid metabolic process
lipid metabolic process
metabolic process
phosphate metabolic process
phosphorus metabolic process
phosphorylation
primary metabolic process
terpenoid biosynthetic process
terpenoid metabolic process
Gene Properties
Blattner:b1208
Gene OrientationCounterclockwise
Centisome Percentage:27.18
Left Sequence End1261249
Right Sequence End1262100
Gene Sequence:
>852 bp
ATGCGGACACAGTGGCCCTCTCCGGCAAAACTTAATCTGTTTTTATACATTACCGGTCAG
CGTGCGGATGGTTACCACACGCTGCAAACGCTGTTTCAGTTTCTTGATTACGGCGACACC
ATCAGCATTGAGCTTCGTGACGATGGGGATATTCGTCTGTTAACGCCCGTTGAAGGCGTG
GAACATGAAGATAACCTGATCGTTCGCGCAGCGCGATTGTTGATGAAAACTGCGGCAGAC
AGCGGGCGTCTTCCGACGGGAAGCGGTGCGAATATCAGCATTGACAAGCGTTTGCCGATG
GGCGGCGGTCTCGGCGGTGGTTCATCCAATGCCGCGACGGTCCTGGTGGCATTAAATCAT
CTCTGGCAATGCGGGCTAAGCATGGATGAGCTGGCGGAAATGGGGCTGACGCTGGGCGCA
GATGTTCCTGTCTTTGTTCGGGGGCATGCCGCGTTTGCCGAAGGCGTTGGTGAAATACTA
ACGCCGGTGGATCCGCCAGAGAAGTGGTATCTGGTGGCGCACCCTGGTGTAAGTATTCCG
ACTCCGGTGATTTTTAAAGATCCTGAACTCCCGCGCAATACGCCAAAAAGGTCAATAGAA
ACGTTGCTAAAATGTGAATTCAGCAATGATTGCGAGGTTATCGCAAGAAAACGTTTTCGC
GAGGTTGATGCGGTGCTTTCCTGGCTGTTAGAATACGCCCCGTCGCGCCTGACTGGGACA
GGGGCCTGTGTCTTTGCTGAATTTGATACAGAGTCTGAAGCCCGCCAGGTGCTAGAGCAA
GCCCCGGAATGGCTCAATGGCTTTGTGGCGAAAGGCGCTAATCTTTCCCCATTGCACAGA
GCCATGCTTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:283
Protein Molecular Weight:30925
Protein Theoretical pI:5
PDB File:1OJ4
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
MRTQWPSPAKLNLFLYITGQRADGYHTLQTLFQFLDYGDTISIELRDDGDIRLLTPVEGV
EHEDNLIVRAARLLMKTAADSGRLPTGSGANISIDKRLPMGGGLGGGSSNAATVLVALNH
LWQCGLSMDELAEMGLTLGADVPVFVRGHAAFAEGVGEILTPVDPPEKWYLVAHPGVSIP
TPVIFKDPELPRNTPKRSIETLLKCEFSNDCEVIARKRFREVDAVLSWLLEYAPSRLTGT
GACVFAEFDTESEARQVLEQAPEWLNGFVAKGANLSPLHRAML
References
External Links:
ResourceLink
Uniprot ID:P62615
Uniprot Name:ISPE_ECOLI
GenBank Gene ID:AB037116
Genebank Protein ID:7527350
PDB ID:1OJ4
Ecogene ID:EG11294
Ecocyc:EG11294
ColiBase:b1208
Kegg Gene:b1208
EchoBASE ID:EB1271
CCDB:ISPE_ECOLI
BacMap:16129171
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
  • 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
  • Ikemi, M., Murakami, K., Hashimoto, M., Murooka, Y. (1992). "Cloning and characterization of genes involved in the biosynthesis of delta-aminolevulinic acid in Escherichia coli." Gene 121:127-132. Pubmed: 1427085
  • Lange, B. M., Croteau, R. (1999). "Isopentenyl diphosphate biosynthesis via a mevalonate-independent pathway: isopentenyl monophosphate kinase catalyzes the terminal enzymatic step." Proc Natl Acad Sci U S A 96:13714-13719. Pubmed: 10570138
  • Luttgen, H., Rohdich, F., Herz, S., Wungsintaweekul, J., Hecht, S., Schuhr, C. A., Fellermeier, M., Sagner, S., Zenk, M. H., Bacher, A., Eisenreich, W. (2000). "Biosynthesis of terpenoids: YchB protein of Escherichia coli phosphorylates the 2-hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol." Proc Natl Acad Sci U S A 97:1062-1067. Pubmed: 10655484
  • 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
  • Post, D. A., Hove-Jensen, B., Switzer, R. L. (1993). "Characterization of the hemA-prs region of the Escherichia coli and Salmonella typhimurium chromosomes: identification of two open reading frames and implications for prs expression." J Gen Microbiol 139:259-266. Pubmed: 7679718
  • Sauret-Gueto, S., Ramos-Valdivia, A., Ibanez, E., Boronat, A., Rodriguez-Concepcion, M. (2003). "Identification of lethal mutations in Escherichia coli genes encoding enzymes of the methylerythritol phosphate pathway." Biochem Biophys Res Commun 307:408-415. Pubmed: 12859972
  • Strohmaier, H., Remler, P., Renner, W., Hogenauer, G. (1995). "Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is growth phase regulated primarily at the transcriptional level in Escherichia coli K-12." J Bacteriol 177:4488-4500. Pubmed: 7543480