A0A0A0HRL0 · A0A0A0HRL0_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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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
Site22Transition state stabilizer
Site149Positions MEP for the nucleophilic attack
Site202Positions MEP for the nucleophilic attack
Binding site229a divalent metal cation (UniProtKB | ChEBI)
Binding site229-2314-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site231a divalent metal cation (UniProtKB | ChEBI)
Site255Transition state stabilizer
Binding site255-2564-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site263a divalent metal cation (UniProtKB | ChEBI)
Binding site277-2794-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site353-3564-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site354Transition state stabilizer
Binding site3604-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3634-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
      rosmuc_01566

Organism names

  • Taxonomic identifier
  • Strain
    • DSM 17069
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Roseovarius

Accessions

  • Primary accession
    A0A0A0HRL0

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2222-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain222-3752-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region223-3802-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
    380
  • Mass (Da)
    40,516
  • Last updated
    2015-01-07 v1
  • Checksum
    B76D532CA7D82AB6
MTTAALIVAAGRGTRAGGDCPKQWQPLLGRRVIDWTLDAFLGAEGIDRILVVLHPDDLDRLAPDPRILVTTGGATRAESVRNGLEVLASDPPDHVLIHDVARCCTKSPYIAYITYKIRSTGLPALAPALPVTDALWTGVDGRVTGTRDRTGLYRAQTPQAFDFTSIIAAHRAHEGDAADDVAVARAAGIDVTILDGDEDNLKITHPHDFKRAEKILGNQMDIRVGSGFDVHRFGPGDHCMLCGVAVPHDRGLQGHSDADVGLHALADAIYGGLAQGDIGRHFPPSDPQWKGAKSHIFLRHAVGLADELGFKINNIDVTLVCERPKITPHAPAMQAALSEITGIAPDRISVKATTSERLGFTGREEGIAAQAVVTLVKPCA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AONH01000007
EMBL· GenBank· DDBJ
KGM88728.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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