A0A3R7V7K2 · A0A3R7V7K2_9PROT

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
Site158Positions MEP for the nucleophilic attack
Site214Positions MEP for the nucleophilic attack
Binding site241a divalent metal cation (UniProtKB | ChEBI)
Binding site241-2434-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site243a divalent metal cation (UniProtKB | ChEBI)
Site267Transition state stabilizer
Binding site267-2684-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site275a divalent metal cation (UniProtKB | ChEBI)
Binding site289-2914-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site365-3684-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site366Transition state stabilizer
Binding site3724-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3754-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmembrane
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
      ispD
    • Synonyms
      ispDF
    • ORF names
      CBD54_003960

Organism names

Accessions

  • Primary accession
    A0A3R7V7K2

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane43-60Helical

Keywords

  • Cellular component

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2352-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain235-3872-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region235-3932-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.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    393
  • Mass (Da)
    44,355
  • Last updated
    2019-04-10 v1
  • Checksum
    A94F0F231124EF62
MQKKINKSLAGIILASGSGSRMKRTXPKQYLLINDISLLEINIEIFFSLPYLTYLIVVISKKHFRFYKAIKXKYKNVFFIEGGKSRQESAFNALNFLKKFTCEYVMIHDAARPFVSKXLIDNLYGKLLKVRTAVVPVVKIQDTIKFCXKNXVTKDINRNNLFLTQTPQLFEYKTLYKAYLHNEKILNNFTDDAQIFAKGNSIIHTVKGDIDNTKITTNKDWINKINMMKENFTTKIGHGFDTHKLIKGKKITLFGIRIPHKFKLLGHSDADVGVHAIIDALLGSCSLGDIGKHFPDTXXKIKGXNSLXMLSKXQXLXXDAXAXISXIDCTLVGESPKIAKYTXKMCIXXAKTLXTQKEXISIKATTTEGLGFTGRKEGISCYCVATIKQEKKI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NHIR02000048
EMBL· GenBank· DDBJ
RPH07241.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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