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ispF 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945057, updated on 3-Dec-2024

Summary

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Official Symbol
ispF
Official Full Name
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Primary source
ECOCYC:EG11816
Locus tag
b2746
See related
ASAP:ABE-0009013
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK2741; ygbB
Summary
2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (IspF) catalyzes the fifth step in the methylerythritol phosphate pathway. [More information is available at EcoCyc: EG11816].
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Genomic context

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Sequence:
NC_000913.3 (2871301..2871780, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene murein hydrolase activator NlpD Neighboring gene protein-L-isoaspartate O-methyltransferase Neighboring gene broad specificity 5'(3')-nucleotidase and polyphosphatase Neighboring gene tRNA pseudouridine(13) synthase Neighboring gene 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase Neighboring gene cell division protein FtsB

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. A structure-based approach to ligand discovery for 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase: a target for antimicrobial therapy. Ramsden NL, et al. J Med Chem, 2009 Apr 23. PMID 19320487, Free PMC Article
  2. A double mutation of Escherichia coli2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase disrupts six hydrogen bonds with, yet fails to prevent binding of, an isoprenoid diphosphate. Sgraja T, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2005 Jul 1. PMID 16511114, Free PMC Article
  3. The identification of isoprenoids that bind in the intersubunit cavity of Escherichia coli 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase by complementary biophysical methods. Kemp LE, et al. Acta Crystallogr D Biol Crystallogr, 2005 Jan. PMID 15608374
  4. Characterization of the depletion of 2-C-methyl-D-erythritol-2,4-cyclodiphosphate synthase in Escherichia coli and Bacillus subtilis. Campbell TL, et al. J Bacteriol, 2002 Oct. PMID 12270818, Free PMC Article
  5. Structure of 2C-methyl-D-erythritol 2,4- cyclodiphosphate synthase: an essential enzyme for isoprenoid biosynthesis and target for antimicrobial drug development. Kemp LE, et al. Proc Natl Acad Sci U S A, 2002 May 14. PMID 11997478, Free PMC Article

See all (21) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. the double mutation of Escherichia coli2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase disrupts six hydrogen bonds with, yet fails to prevent binding of, an isoprenoid diphosphate
    Title: A double mutation of Escherichia coli2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase disrupts six hydrogen bonds with, yet fails to prevent binding of, an isoprenoid diphosphate.
  2. MECP synthase binds three metabolites that are produced by enzymes two, three and four stages downstream in isoprenoid biosynthesis
    Title: The identification of isoprenoids that bind in the intersubunit cavity of Escherichia coli 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase by complementary biophysical methods.
Submit: New GeneRIF Correction

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables manganese ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables metal ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables zinc ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway IEA
Inferred from Electronic Annotation
more info
  
involved_in isoprenoid biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in terpenoid biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within ubiquinone biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
NP_417226.1

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    2871301..2871780 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417226.1 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_417226.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A376MH63
    Conserved Domains (1) summary
    PRK00084
    Location:1 → 157
    ispF; 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; Reviewed
Nucleotide Protein
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