A0AAE6EEB4 · A0AAE6EEB4_RHIRD

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).

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

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.

TypeIDPosition(s)Description
Site15Transition state stabilizer
Site24Transition state stabilizer
Site157Positions MEP for the nucleophilic attack
Site214Positions MEP for the nucleophilic attack
Binding site242a divalent metal cation (UniProtKB | ChEBI)
Binding site242-2444-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site244a divalent metal cation (UniProtKB | ChEBI)
Site268Transition state stabilizer
Binding site268-2694-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site276a divalent metal cation (UniProtKB | ChEBI)
Binding site290-2924-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site366-3694-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site367Transition state stabilizer
Binding site3734-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3764-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

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
    • ORF names
      CFBP5877_05870

Organism names

Accessions

  • Primary accession
    A0AAE6EEB4

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2352-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain236-3882-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region236-3952-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    395
  • Mass (Da)
    41,622
  • Last updated
    2024-05-29 v1
  • Checksum
    0832ECB60B948CEC
MKFGIVIVAAGRGERAGSPEEGPKQYRPIGGRAVIEHTLTTFLGWNDACPIVVVSHADDAALLSPILGRLDAGERITTVTGGATRQQSVLAGLEAFSSHDLTHVMIHDAVRPFVAADMLERIVALHLGGASGVLPALPVTDTLKRGAGDRVEETVSRQGLYAAQTPQSFSYSDILAAHRAAGASGKTDFTDDASIAEWAGLTVTLTEGSVDNVKLTLKRDIAMADEKLSHALPDVRTGNGYDVHQLEAGDGVTLCGIFIEHDQRLKGHSDADVALHALTDALLATCGAGDIGDHFPPSDPQWKGAASRIFLEHAAKVVRDNGGTIMNADVSLIAEAPRIGPHRQAMREALSDMLGIALERCSVKATTNETIGFVGRREGIAAIATATVVYQGRPL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP039897
EMBL· GenBank· DDBJ
QCL78648.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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