A0A249PA80 · A0A249PA80_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.

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
Site21Transition state stabilizer
Site30Transition state stabilizer
Site164Positions MEP for the nucleophilic attack
Site221Positions MEP for the nucleophilic attack
Binding site250a divalent metal cation (UniProtKB | ChEBI)
Binding site250-2524-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site252a divalent metal cation (UniProtKB | ChEBI)
Site276Transition state stabilizer
Binding site276-2774-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site284a divalent metal cation (UniProtKB | ChEBI)
Binding site298-3004-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site374-3774-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site375Transition state stabilizer
Binding site3814-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3844-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
      SJ05684_c13010

Organism names

  • Taxonomic identifier
  • Strain
    • CCBAU 05684
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Rhizobiaceae > Sinorhizobium/Ensifer group > Sinorhizobium

Accessions

  • Primary accession
    A0A249PA80

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-2432-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain244-3962-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region244-4042-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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    404
  • Mass (Da)
    42,857
  • Last updated
    2017-12-20 v1
  • Checksum
    97B65A0532F9A4AA
MQPEEQFSCGVVIVAAGRGERAGQSAEGPKQYRTIGDRPVIAHTLDIFATWPGAGPIVVVIHPDDEALFAAARMCMSGRADLSVVHGGATRQLSVLAGLEALSGTGAPYVMIHDAVRPFIDHALLGRCREALGSGAEAVLPAIAVADTLKRTTEGRLVEETVPRAGLYAAQTPQCFRLEAILAAHRRASASGRSDFTDDASIAEWAGLPVLLVEGAADNVKLTLKRDISMADERLSRHAVPDVRTGNGYDVHQLVEGDGVTLCGVFIPHERKLSGHSDADVALHALTDALLATCGAGDIGDHFPPSDPQWKGAPSRIFLEHAAKIVREHGGTITNADISLIAEAPKVGPHRQQMRENLAAMLDIDLDRCSIKATTNENLGFVGRKEGIAAIATATVVYHRGKKN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP023067
EMBL· GenBank· DDBJ
ASY62756.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help