W8S899 · W8S899_9RHOB

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
Site25Transition state stabilizer
Site32Transition state stabilizer
Site160Positions MEP for the nucleophilic attack
Site213Positions MEP for the nucleophilic attack
Binding site240a divalent metal cation (UniProtKB | ChEBI)
Binding site240-2424-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site242a divalent metal cation (UniProtKB | ChEBI)
Site266Transition state stabilizer
Binding site266-2674-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site274a divalent metal cation (UniProtKB | ChEBI)
Binding site288-2904-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site364-3674-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site365Transition state stabilizer
Binding site3714-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3744-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
    • ORF names
      roselon_02887

Organism names

Accessions

  • Primary accession
    W8S899

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2332-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain233-3862-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region234-3892-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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    389
  • Mass (Da)
    40,623
  • Last updated
    2014-05-14 v1
  • Checksum
    629FD62B037A00F6
MSSQTPHGPPFSAAALIVAAGRGTRAGGGLPKQYRDLGGKPVLARTISALDAHPAVRQIVVVRHADDSALFRGACPATRAALSDVAGGASRDASVRAGLSAVADDIDVVLIHDAARPLVSRAVIDGVMDALHSYDGAAPALAVTDALWRGDGTVTGTEDRNGLWRAQTPQGFHLDRIRAAHAHHPGGAADDVGVARAYGLSVAITQGDEANLKITTAGDFARAARFLEDQMDIRTGNGFDVHRFGEGDHVMLCGVAIPHERGLQGHSDADVGLHTVTDAIYGALAMGDIGTHFPPSDPQWKGAESHIFLTHAVDLAAEMGFTLTHADLTLICERPKIGPHAAPMRARLSDLLRIEAARVSVKATTTERLGFPGREEGIAALATVTLVKA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP004372
EMBL· GenBank· DDBJ
AHM05181.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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