A0A0D6QHS9 · A0A0D6QHS9_9BACT

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
Site19Transition state stabilizer
Site24Transition state stabilizer
Site155Positions MEP for the nucleophilic attack
Site211Positions MEP for the nucleophilic attack
Binding site236a divalent metal cation (UniProtKB | ChEBI)
Binding site236-2384-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site238a divalent metal cation (UniProtKB | ChEBI)
Site261Transition state stabilizer
Binding site261-2624-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site269a divalent metal cation (UniProtKB | ChEBI)
Binding site283-2854-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site288-2924-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site359-3624-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site360Transition state stabilizer
Binding site3664-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3694-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
      PSR1_01479

Organism names

  • Taxonomic identifier
  • Strain
    • PSR-1
  • Taxonomic lineage
    Bacteria > Myxococcota > Myxococcia > Myxococcales > Cystobacterineae > Anaeromyxobacteraceae > Anaeromyxobacter

Accessions

  • Primary accession
    A0A0D6QHS9

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2292-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Region230-3862-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Domain231-3812-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
    386
  • Mass (Da)
    39,098
  • Last updated
    2015-05-27 v1
  • Checksum
    192D670F65BDAC70
MIRGERVIGILAAGGSGQRAGVAKQWLVLGGETVLRRSARVLAACDAVDGLVVVVPPGDEARGEAELAGLGKPVRAVTGGAARADSVRNGLAAADGAVVLVHDAARPFASAALAGRVAEAAARDGAALAALPATDTVKRADAGAEVPRVVETLDRRTVWLAQTPQGFRRAVLEQAYAAAGPSASAATDECALVEAAGAPVTLVPGEAGNFKITGPDDVRRARALLEAPVATGVGYDTHRFAPGRRLVLGGVEFEGDGLLGHSDADVCAHAIGDAILGAAGLGDLGRHFPDTDPRWKGVSSLALLREIAAKAAERGWRVGNCDVTLAAKRPKIAPRAEEMRARLAGALGISPAQVNVKATTGEGMGFVGREEGVAAHAIALLVRAAG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BAZG01000031
EMBL· GenBank· DDBJ
GAO02606.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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