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A0A0R2PLL8 · A0A0R2PLL8_9MICO

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
Site18Transition state stabilizer
Site25Transition state stabilizer
Site156Positions MEP for the nucleophilic attack
Site209Positions MEP for the nucleophilic attack
Binding site236a divalent metal cation (UniProtKB | ChEBI)
Binding site236-2384-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site238a divalent metal cation (UniProtKB | ChEBI)
Site262Transition state stabilizer
Binding site262-2634-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site270a divalent metal cation (UniProtKB | ChEBI)
Binding site284-2864-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site357-3604-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site358Transition state stabilizer
Binding site3674-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
      ABR66_05330

Organism names

Accessions

  • Primary accession
    A0A0R2PLL8

Proteomes

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-2292-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Region230-3822-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Domain231-3792-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
    382
  • Mass (Da)
    39,264
  • Last updated
    2016-01-20 v1
  • MD5 Checksum
    3AC4E7FBD6C556B3ABF0B0CA136CAA8F
MPRVTTAVVLVAAGSGSRLGSPFPKAFVSLEGKTLLQHCVERLGEWSRPHTVVLVVPEGWQEPARALLTSSPGARVVTGGATRTASVRAGLAALGEDTDVVLIHDAARVLMPLDVFDRVVEAVEAGAPGAIPHVLVVDTLVRISPETLITEGGPNRDELGGVQTPQGFVASKLIAAYEAVAGDFSDDAAVMREAGHDVVGVAGDVRGFKITYPEDLTRAASVLGASVTPLVGVAMDVHQFDENTPLRLAGLTWEGEKGLSGHSDGDVVLHAIVDAALQAARLGDLGEHFGVDRPEFAGADSSVFLSHALSLLHAQGLRVSSVGVQVIGNAPKIGPRRLEAQETLTALVGAPVALSATTTDGLGLTGRGEGVAAIATVVLSTT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LIAY01000081
EMBL· GenBank· DDBJ
KRO38932.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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