A0A109BMR4 · A0A109BMR4_HYPSL

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
Site21Transition state stabilizer
Site35Transition state stabilizer
Site170Positions MEP for the nucleophilic attack
Site227Positions MEP for the nucleophilic attack
Binding site256a divalent metal cation (UniProtKB | ChEBI)
Binding site256-2584-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site258a divalent metal cation (UniProtKB | ChEBI)
Site282Transition state stabilizer
Binding site282-2834-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site290a divalent metal cation (UniProtKB | ChEBI)
Binding site304-3064-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site380-3834-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site381Transition state stabilizer
Binding site3874-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3904-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
      APY04_0443

Organism names

  • Taxonomic identifier
  • Strain
    • WDL6
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Hyphomicrobiaceae > Hyphomicrobium

Accessions

  • Primary accession
    A0A109BMR4

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-2492-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain250-4022-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region250-4092-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
    409
  • Mass (Da)
    42,480
  • Last updated
    2016-04-13 v1
  • Checksum
    2D8A57A9B46E10F6
MAGATMTTTAVVVVAAGRGTRVEASTGGSASARPKQYRLLAGRPVLSHSLAVLSRHPAITAVVVVRHPDDHALYEEAAAPYADKLVAPVAGGATRQASVLAGLEALTALPGGAPDRVLIHDAARPFLSATLIDDLIAALDASPGAIAAEPVADTLKRADANGRIAATVDRSALWRAQTPQGFHFDAIRDAHRKAADANRHDFTDDAALAEWVGLPVQLVASSGTNMKLTTAADMDLAERILGAATAWETRVGSGFDVHSVAEGDHVWLCGVKIPHTHRLDGHSDADVGLHALTDALLGAIGDGDIGYHFPPSDEQWRGAASRIFLAHAVDLVRLRGGRITNVDVTLLCEAPKVGPHRPEMSATIAEILGIGPDRVGIKATTMERLGFIGRGEGIAAMASATVQLPTAAS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LMTR01000021
EMBL· GenBank· DDBJ
KWT71521.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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