A8FNR8 · ISPDF_CAMJ8

Function

function

Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).

Catalytic activity

Cofactor

a divalent metal cation (UniProtKB | Rhea| CHEBI:60240 )

Pathway

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.

Features

Showing features for site, binding site.

Type
IDPosition(s)Description
Site16Transition state stabilizer
Site23Transition state stabilizer
Site139Positions MEP for the nucleophilic attack
Site191Positions MEP for the nucleophilic attack
Binding site217a divalent metal cation (UniProtKB | ChEBI)
Binding site217-2194-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site219a divalent metal cation (UniProtKB | ChEBI)
Site243Transition state stabilizer
Binding site243-2444-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site251a divalent metal cation (UniProtKB | ChEBI)
Binding site265-2674-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site270-2744-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site341-3444-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site342Transition state stabilizer
Binding site3484-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3514-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity
Molecular Function2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
Molecular Functionmetal ion binding
Biological Processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
Biological Processterpenoid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional enzyme IspD/IspF

Including 2 domains:

  • Recommended name
    2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
  • EC number
  • Alternative names
    • 4-diphosphocytidyl-2C-methyl-D-erythritol synthase
    • MEP cytidylyltransferase
      (MCT
      )
  • Recommended name
    2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
  • EC number
  • Short names
    MECDP-synthase
    ; MECPP-synthase
    ; MECPS

Gene names

    • Name
      ispDF
    • Ordered locus names
      C8J_1508

Organism names

Accessions

  • Primary accession
    A8FNR8

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000735401-371Bifunctional enzyme IspD/IspF

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-2102-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Region211-3712-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase

Sequence similarities

In the N-terminal section; belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.
In the C-terminal section; belongs to the IspF family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    371
  • Mass (Da)
    41,658
  • Last updated
    2007-11-13 v1
  • Checksum
    7E72D30FC89B2DBE
MSEISLIMLAAGNSTRFNTKVKKQFLRLGNDPLWLYATKNLSSFYPFKKIVVTSSNITYMKKFTKNYEFIEGGDTRAESLKKALELIDSEFVMVSDVARVLVSKNLFDRLIENLDKADCITPALKVADTTLFDNEALQREKIKLIQTPQISKTKLLKKALDQNLEFTDDSTAIAAMGGKIWFVEGEENARKLTFKEDLKKLDLPTPSFEIFTGNGFDVHEFGENRPLLLAGVQIHPTMGLKAHSDGDVLAHSLTDAILGAAGLGDIGELYPDTDMKFKNANSMELLKQAYDKVREVGFELINIDICVMAQSPKLKDFKQAMQSNIAHTLDLDEFRINVKATTTEKLGFIGRKEGMAVLSSVNLKYFDWTRL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000814
EMBL· GenBank· DDBJ
ABV53105.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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