A0A1Q4DQJ4 · A0A1Q4DQJ4_9HYPH

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
Site21Transition state stabilizer
Site28Transition state stabilizer
Site160Positions MEP for the nucleophilic attack
Site217Positions MEP for the nucleophilic attack
Binding site245a divalent metal cation (UniProtKB | ChEBI)
Binding site245-2474-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site247a 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 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
      BGP08_16695

Organism names

Accessions

  • Primary accession
    A0A1Q4DQJ4

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2382-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain238-3912-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region239-3972-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
    397
  • Mass (Da)
    41,833
  • Last updated
    2017-04-12 v1
  • Checksum
    F68422C2D38EA9FB
MGDLSTKRVAVVVVAAGRGTRAGGARPKQFRHLRGEPLVRTTLRRLAEHPRIGSVQPVIHPDDAALFQEAASGLTLLPAVSGGATRQASVHAGLEALAAQNPHPDIVLVHDAARPFLTASLIDRAIVAVEAAPAAVPALPVSDTVKTVDLAGRVTRTLDRAMLRAVQTPQAFHFTPLLDAHRRAAQAGRDDFTDDAALAEWAGMAVAVFDGEAENIKMTTAEDFDRTVARDADRLGDIRTGFGFDVHAFGDGDHVTIGGIAIPHPRGLSGHSDADVGLHALVDAILGALADGDIGSHFPPSDPQWRGAASDQFLRFAVQRVAARGGMIAHLDLTLVCELPKIGPHRDAMRARIAEIAGIAISRVAVKATTSERLGFTGRGEGIAAYATATVRLPWQD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MKWA01000002
EMBL· GenBank· DDBJ
OJY46655.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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