A0A4Z1R9V4 · A0A4Z1R9V4_9HYPH

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
      CFBP5507_05540

Organism names

  • Taxonomic identifier
  • Strain
    • CFBP5507
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Rhizobiaceae > Rhizobium/Agrobacterium group > Agrobacterium

Accessions

  • Primary accession
    A0A4Z1R9V4

Proteomes

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-2352-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
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)
    41,685
  • Last updated
    2019-09-18 v1
  • Checksum
    C6FF21F2CEBCC0E8
MKLGIVIVAAGRGERAGSPEEGPKQYRPIGGRAVIEHTLSTFLDWDHASPIVIVSHVDDAALLSPILQRLDSGGRIVTVTGGSTRQQSVLAGLEALASEELTHVMIHDAVRPFVPVDMLDRIVALHRAGASSVLPALPVTDTLKRGAGNVVAETISRQGLYAAQTPQSFTFDDILGAHRAASASGKTDFTDDASIAEWAGLTVTLTEGSVDNVKLTLKRDITMADEKLSNGLPDVRTGNGYDVHQLEAGDGVTLCGIFIEHDQRLKGHSDADVALHALTDALLATCGAGDIGDHFPPSDPQWKGAASSIFLEHAAKVVRDNGGTIMNADVSLIAEAPRIGPHRQAMREALSDMLGIALERCSVKATTNETIGFVGRREGIAAIATATVVYRGRPL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP109968
EMBL· GenBank· DDBJ
UYZ08465.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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