I9QBB4 · I9QBB4_HELPX

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
Site48Transition state stabilizer
Site55Transition state stabilizer
Site175Positions MEP for the nucleophilic attack
Site227Positions MEP for the nucleophilic attack
Binding site254a divalent metal cation (UniProtKB | ChEBI)
Binding site254-2564-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site256a divalent metal cation (UniProtKB | ChEBI)
Site280Transition state stabilizer
Binding site280-2814-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site288a divalent metal cation (UniProtKB | ChEBI)
Binding site302-3044-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site307-3114-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site378-3814-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site379Transition state stabilizer
Binding site3854-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3884-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
      HPNQ4099_0635

Organism names

  • Taxonomic identifier
  • Strain
    • NQ4099
  • Taxonomic lineage
    Bacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Helicobacteraceae > Helicobacter

Accessions

  • Primary accession
    I9QBB4

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2472-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Region248-4062-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Domain249-4002-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
    406
  • Mass (Da)
    45,428
  • Last updated
    2012-10-03 v1
  • Checksum
    F771160E8D8AA2BE
MSLIRVNGEAFNLSLESLKEDPFETKETLETLVKQTSVVLLAAGESKRFSQTIKKQWLRSNHTPLWLSVYESFKEALDFKEIILVVSGLDYIYIQRHYPEIKLVKGGASRQESVRNALKVIDSAYTLTSDVARGLANMETLKSLFLALQQTSHYCIAPYLPCYDTAIYYNETLDREAIKLIQTPQLSHTKTLQSALNQGDFKDESSAILQAFPNSVSYIEGSKNLHKLTTSDDLKHFAFFFNPAKDTFIGMGFDTHAFIKDKPMVLGGVVLDCEFGLKAHSDGDALLHAVIDAILGAIKGGDIGEWFPDNDPKYKNASSEKLLKIVLDFSQSIGFELFEMGATIFSEIPKITPYKPAILENLSQLLGLEKSQISLKATTMEKMGFIGKQEGLLVQAHVSMRYKQKL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AKNU01000002
EMBL· GenBank· DDBJ
EJB30464.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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