A0A426VW07 · A0A426VW07_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.

TypeIDPosition(s)Description
Site16Transition state stabilizer
Site23Transition state stabilizer
Site140Positions MEP for the nucleophilic attack
Site192Positions MEP for the nucleophilic attack
Binding site219a divalent metal cation (UniProtKB | ChEBI)
Binding site219-2214-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site221a divalent metal cation (UniProtKB | ChEBI)
Site245Transition state stabilizer
Binding site245-2464-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site253a divalent metal cation (UniProtKB | ChEBI)
Binding site267-2694-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site272-2764-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site343-3464-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site344Transition state stabilizer
Binding site3504-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3534-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
      P794_08540

Organism names

Accessions

  • Primary accession
    A0A426VW07

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2122-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Region213-3732-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Domain214-3652-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase

Sequence similarities

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
    373
  • Mass (Da)
    41,276
  • Last updated
    2019-05-08 v1
  • Checksum
    BFEEA340681CF60F
MSDTTLILLGAGNSTRFKCNVKKQWLYTKDTPLWLHVAEHFEKVADFGQIIIVSSAEDITLMEQYADYLYVEGGDSRQASLHNALAHVTSEYVLVSDIARCCVPHDMIERILAAKSKGSCIVPALPVSDTLYLGDSPVDREQAKIIQTPQLSVTKTLRKALQTEHLFTDDSSAVAFMGEKVHFVEGSTEAHKLTTIADLRKLSCIQEPSARTLTGFGLDIHPFEKDKEMFLCGVKIDVEYGFKAHSDGDVAIHALIDALLGASGMGDIGEFYPDTDESYKGMNSKKLLTDTVNRLKTHGYEIGNIDLTILAQAPKILPYKKEMRKTIASLLGIKNHFVNIKATTAEKLGFVGRKEGVTVHAVANLTYFNWKHI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JQIX01000061
EMBL· GenBank· DDBJ
RRS30094.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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