A0A9D1PUB0 · A0A9D1PUB0_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
Site21Transition state stabilizer
Site30Transition state stabilizer
Site167Positions MEP for the nucleophilic attack
Site223Positions MEP for the nucleophilic attack
Binding site293a divalent metal cation (UniProtKB | ChEBI)
Binding site293-2954-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site295a divalent metal cation (UniProtKB | ChEBI)
Site319Transition state stabilizer
Binding site319-3204-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site327a divalent metal cation (UniProtKB | ChEBI)
Binding site341-3434-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site346-3504-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site417-4204-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site418Transition state stabilizer
Binding site4244-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
      ispD
    • Synonyms
      ispDF
    • ORF names
      H9894_00810

Organism names

Accessions

  • Primary accession
    A0A9D1PUB0

Proteomes

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-2862-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Region241-277Disordered
Compositional bias243-267Polar residues
Region287-4452-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Domain288-4372-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
    445
  • Mass (Da)
    47,105
  • Last updated
    2023-05-03 v1
  • Checksum
    D93044E07E856DAE
MPYTLDTAPWLILLAAGQGTRLAAAAGCPKQFLTVDSVPLFWLSVRTCSRVARLGGVVFVFPKDTFESSRDLVRELDRLEPCGLNMAFAVGGARRQDSVASGLAVVPQSARFVLVHDAARPFFSPGLVNALLDRLEAGAQAVIPGLAVTDTIKVVNKAGLVCATPDRSTLRAVQTPQGFSRRALAEAHRTLNTPENTVTDDASLMEEAGHEVLVIDGEAGNIKITNPEDLQLLKKKAETGAEDGSSCTKQAAPDQTVPGQAVSGQAGENGSPAAPDNPDTTGCLVPCTGFGYDVHRYGGDRPLVLAGVPIPCDFQVRAHSDGDVLLHALMDALLGLFGQGDIGMLFPDNDPRYDGADSAQLLAEVLQRMRQARVRLTHADVTVVAQKPRLSPHKKAMQESLCRLLGLGPEHVNVKATTEEGLGFTGDLSGIKAYATVCGLKSETI

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias243-267Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DXHV01000010
EMBL· GenBank· DDBJ
HIV99724.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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