A0A6L2R586 · A0A6L2R586_9BACT

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
Site20Transition state stabilizer
Site27Transition state stabilizer
Site163Positions MEP for the nucleophilic attack
Site216Positions MEP for the nucleophilic attack
Binding site242a divalent metal cation (UniProtKB | ChEBI)
Binding site242-2444-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site244a divalent metal cation (UniProtKB | ChEBI)
Site271Transition state stabilizer
Binding site271-2724-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site279a divalent metal cation (UniProtKB | ChEBI)
Binding site293-2954-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site298-3024-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site369-3724-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site370Transition state stabilizer
Binding site3764-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3794-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
      ZNDK_0519

Organism names

  • Taxonomic identifier
  • Strain
    • ZnDsv-02
  • Taxonomic lineage
    Bacteria > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae > Desulfovibrio

Accessions

  • Primary accession
    A0A6L2R586

Proteomes

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-2352-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain236-3892-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region236-4052-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
    405
  • Mass (Da)
    43,588
  • Last updated
    2020-10-07 v1
  • Checksum
    EB5632EFD57C96B5
MPDAFQKPWALILAAGQSNRAAAGRPKQFLPWRGVPLYWHSARAMSHSACIGGIVFVFPADARNEEEKRLQDLHRHDNLGLPFLTADGGPLRQDSVRLGLALVPQTVKHVLIHDAARPFLQPALIRGVCATLHQGAVAVVPAVPVTDTIKVVANNLVTATLPRNTLSAVQTPQGFRLDLLRRAHAAARAPMTDDAALMEQAGHDVRVIAGDAANTKITWTGDLDLLADPPPMPCPRVGFGYDVHRYVGKDQGRPLKLGGIAIAGAPEVAAHSDGDVLLHALADALLGCAGMDDIGRHFPDSDERYNNISSTVLLDHVLELLRNQNIVLQNVDMTIIAQKPRIYPYSAEIRKNVARLLGLSVTRVNLKATTEEGLGFTGRCEGVKVCAIASALTDLPNLSQTTLAF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BLLL01000004
EMBL· GenBank· DDBJ
GFH62748.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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