A0A4U8S489 · A0A4U8S489_9HELI

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
Site18Transition state stabilizer
Site27Transition state stabilizer
Site145Positions MEP for the nucleophilic attack
Site197Positions MEP for the nucleophilic attack
Binding site225a divalent metal cation (UniProtKB | ChEBI)
Binding site225-2274-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site227a divalent metal cation (UniProtKB | ChEBI)
Site251Transition state stabilizer
Binding site251-2524-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site259a divalent metal cation (UniProtKB | ChEBI)
Binding site273-2754-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site278-2824-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site349-3524-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site350Transition state stabilizer
Binding site3564-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3594-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
      LS68_007425

Organism names

  • Taxonomic identifier
  • Strain
    • MIT 05-5293
  • Taxonomic lineage
    Bacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Helicobacteraceae > Helicobacter

Accessions

  • Primary accession
    A0A4U8S489

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2182-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain219-3712-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region219-3802-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase

Sequence similarities

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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    380
  • Mass (Da)
    42,657
  • Last updated
    2019-07-31 v1
  • Checksum
    B9BAB0CB01DCBFD7
MTLDDVSLVMMAAGNSTRFCEAYPVKKQWLRIGDDPLWLFATRKLATALPFKNTFITASPEDFSYMQKISEYPIIKGGQTRCQSLKNALQHIQTPFVLVSDVARWDTDIAVVKTMLESIDDDVSCVVPYMKVADTTFYEGSYLQRESLKLIQTPQLSRVKDLRESLSVDKDFSDESSALHHLGKKIVFVQGNERMNKLTHRTDIWQHQKRLNPPCAKIFVGNGIDIHAFEEGKIMKLGGVKIDSPLGFKAHSDGDVALHALSDAILGAIGAGDIGEWFPDTDDANRNADSKKMLQKIYNFAQSVGYEIINTDITILAQTPKITPYKIMMQECIAKTLGIKKSCVNIKATTTENLGFIGRKEGVCVQANVSMRYIDWRFQE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JROZ02000003
EMBL· GenBank· DDBJ
TLD80559.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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