A0A841QDR9 · A0A841QDR9_9PROT

  • Protein
    Bifunctional enzyme IspD/IspF
  • Gene
    ispDF
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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
Site15Transition state stabilizer
Site26Transition state stabilizer
Site154Positions MEP for the nucleophilic attack
Site208Positions MEP for the nucleophilic attack
Binding site235a divalent metal cation (UniProtKB | ChEBI)
Binding site235-2374-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site237a divalent metal cation (UniProtKB | ChEBI)
Site261Transition state stabilizer
Binding site261-2624-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site269a divalent metal cation (UniProtKB | ChEBI)
Binding site283-2854-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site359-3624-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site360Transition state stabilizer
Binding site3664-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3694-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
      HNR55_001122

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 4491
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Acetobacteraceae > Acetobacter

Accessions

  • Primary accession
    A0A841QDR9

Proteomes

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-17
ChainPRO_503251025118-384Bifunctional enzyme IspD/IspF

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2282-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain229-3812-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region229-3842-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.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    384
  • Mass (Da)
    40,640
  • Last updated
    2021-09-29 v1
  • Checksum
    2D40BC8700B6CD36
MRVAAILLAAGTGSRYAATTGCATPKQYVLLAGQPVIRHAAEALLPHVSSIQPVGDPSSLNDALQGLAVLPPVQGGQTRQASVRAGLEALDALPPEQKPDLVLVHDGARPYVTGQLVANVVAALAEHPGAIPAVPVADTLKREKDGVIDGTVSREHLFRAQTPQGFRFGLFLDLHRAAASLNATDDAKLLEESGFSVALVPGDEDNIKLTYEADLVRLERLIGPTLLPRVGLGYDVHAFEEGRPLIMCGITIPHTHGLAGHSDADVGIHALCDAIYGALAEGDIGRHFPPSQNEWKDADSARFLIHAGQRIRARGGMLVNADLTLICERPKIGPHAQAMRERLAALLEVDVERISVKATTSERLGFTGREEGIACAATVSVLVP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACHIE010000003
EMBL· GenBank· DDBJ
MBB6456548.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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