A0A2G6MZU6 · A0A2G6MZU6_UNCDU

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
Site24Transition state stabilizer
Site31Transition state stabilizer
Site164Positions MEP for the nucleophilic attack
Site218Positions MEP for the nucleophilic attack
Binding site252a divalent metal cation (UniProtKB | ChEBI)
Binding site252-2544-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site254a divalent metal cation (UniProtKB | ChEBI)
Site278Transition state stabilizer
Binding site278-2794-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site286a divalent metal cation (UniProtKB | ChEBI)
Binding site300-3024-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site305-3094-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site376-3794-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site377Transition state stabilizer
Binding site3834-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3864-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
      CSA26_03885

Organism names

Accessions

  • Primary accession
    A0A2G6MZU6

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2452-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain245-3982-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region246-4022-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase

Sequence similarities

Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.
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
    402
  • Mass (Da)
    43,936
  • Last updated
    2018-01-31 v1
  • Checksum
    A2448BB8E52B4E90
MTGRRQQITPRAAVIIPAAGSGSRMKTTVPKQYLELVDRPVLIHTVAAFANHPVISQVIVVVPVERIGETRKLLADYRLDKARVTVVAGGRRRQDSVEKGLEAVEPNHEIVLVHDGARPLISARLIERCYRETVETGAAVAAIPVRDTLKKEGPGRMVTATVDRSELWQAQTPQGAGKVLLEKAFQVHDGRDVTDESSLLERAGIPVRIVLGEITNIKVTTPGDIELAEQLVREGKQPDRRRRQMKIGHGFDAHRFAEGRKLVLGGEEIPFAQGLAGHSDADVVSHALCDAILGALGLGDIGYHFPDNDETYRDICSLNLLDEVVKKAEMSGFEFGNADLTIVCQVPKLAPHIEAMKKNLADYCRVAPAMINIKATTTEKMGYTGRQEGISCHAVVLLRKKG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PDTH01000082
EMBL· GenBank· DDBJ
PIE65466.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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