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A0A1D2TTA8 · A0A1D2TTA8_9CAUL

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
Site15Transition state stabilizer
Site22Transition state stabilizer
Site149Positions MEP for the nucleophilic attack
Site204Positions MEP for the nucleophilic attack
Binding site231a divalent metal cation (UniProtKB | ChEBI)
Binding site231-2334-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site233a divalent metal cation (UniProtKB | ChEBI)
Site257Transition state stabilizer
Binding site257-2584-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site265a divalent metal cation (UniProtKB | ChEBI)
Binding site279-2814-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site355-3584-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site356Transition state stabilizer
Binding site3624-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3654-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
      ABS77_05845

Organism names

Accessions

  • Primary accession
    A0A1D2TTA8

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-2242-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain225-3772-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region225-3812-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
    381
  • Mass (Da)
    39,801
  • Last updated
    2016-11-30 v1
  • MD5 Checksum
    B04D0DD656254801DB5DA2BB3356A436
MEFSAVIVAAGASTRAGPGLAKPWRDLVGRPVIAWSIEALAGAGATRIVVVTTADRREDAAALLAGLPSPQVVIGGASRADSVQAGLAALDAGDDTPVLIHDAARPFVPRACIEALLAALGDHDGAIPGLPLADTLKRASPLIEETVPREGLWRVQTPQAFRLGRLRAAYAALSPGTEPTDDASVVEADGGRVVVTPGDPMLMKLTYPEDFAMAERLAGAARITRIGQGVDAHRWGPGDAVWLCGVRIDHDQTLIGHSDADAGLHALTDAILGAIGAGDIGEHFPPSDPQWKGAASDRFLLRAVEILTNRGGRLLNADVTLVCERPKIRPHRDAMRARLAELLGLPLDRISVKATTTEGMGFTGRQEGLLAQAVVAVETPA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MEEW01000059
EMBL· GenBank· DDBJ
ODT62797.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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