A0A2W5HH12 · A0A2W5HH12_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.

Type
IDPosition(s)Description
Site16Transition state stabilizer
Site23Transition state stabilizer
Site153Positions MEP for the nucleophilic attack
Site206Positions MEP for the nucleophilic attack
Binding site228a divalent metal cation (UniProtKB | ChEBI)
Binding site228-2304-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site230a 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
      DI586_08485

Organism names

  • Taxonomic identifier
  • Strain
    • S2_006_000_R2_64
  • Taxonomic lineage
    Bacteria > Bdellovibrionota > Bdellovibrionia > Bdellovibrionales > Pseudobdellovibrionaceae > Micavibrio

Accessions

  • Primary accession
    A0A2W5HH12

Proteomes

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-2212-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain222-3752-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region222-3772-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
    377
  • Mass (Da)
    41,245
  • Last updated
    2018-09-12 v1
  • Checksum
    026FBFBF8848453F
MSEFAVIIVAAGTGSRAGDGLPKQYRDLTGEAVLRHTVNAFLHFPGLVRLCVVINKEHEDLYQNAVRGLGLPEPVIGGATRQESVAKGLKALEGIPADMPVLIHDGARPFIEYETILNCLKKLETAEAITTAIPVHDTLRRSEDGYLGEVIKRENVWLIQTPQGFHYNVIKRAHETMTGEYTDDSQMVSEMGVRVELVPGSRRNIKLTTEDDFKNVKRKITKTGLGYDVHAFGEASTQIRIGGIDIPHTKKLLGHSDADVVLHAITDAIYGTISSGDIGSHFPPSNNQFKNMDSSIFLKKAMQDLKAENGQILHIDTVIICEDPKIGPHRDKIRESIANICNLPVKSVSVKATTSEGLGFTGRREGIAAQALVTIEI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QFOT01000101
EMBL· GenBank· DDBJ
PZP54912.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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