A0A7G5ILP2 · A0A7G5ILP2_9SPHN

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.

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
Site148Positions MEP for the nucleophilic attack
Site201Positions MEP for the nucleophilic attack
Binding site226a divalent metal cation (UniProtKB | ChEBI)
Binding site226-2284-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site228a divalent metal cation (UniProtKB | ChEBI)
Site252Transition state stabilizer
Binding site252-2534-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site260a divalent metal cation (UniProtKB | ChEBI)
Binding site274-2764-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site350-3534-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site351Transition state stabilizer
Binding site3574-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3604-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
      H3309_07480

Organism names

  • Taxonomic identifier
  • Strain
    • M6
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingosinicellaceae > Sandaracinobacteroides

Accessions

  • Primary accession
    A0A7G5ILP2

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2192-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Region220-3792-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Domain221-3722-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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    379
  • Mass (Da)
    39,126
  • Last updated
    2021-02-10 v1
  • Checksum
    1E137AFF2A6DEB35
MHTAALIVAAGRGTRAGGALPKQYQPLAGAPVIAHALAAFARHARVSHLHAVIAPEDEALFLNAANGFNVTHSPGGATRQDSVRLGLAALPAHITHVLIHDAARPFVPADMIDRILDALETHPAALPVLPIVDSLRTGDTLMTGEIPRDTLWRAQTPQGFELAAIRAAHAAAAPGHTDDAAIAHAAGLAVALVPGDEHAMKLTHAADFARAAALLPTRTTSGTGFDVHRFGRGDHVWLCGVRVPHSAGVIGHSDADVALHALTDAILGAIGDGDIGTHFPPSDPQWKGASSDRFLAHAAGLVSARGGVIDHVDLTIIAEAPKVGPHRAAFTARLAEILAAHAPLISVKATTTERLGFTGRGEGIAAQAIATVTLPRYSL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP059851
EMBL· GenBank· DDBJ
QMW24284.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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