A0A0Q5WZL6 · A0A0Q5WZL6_9HYPH

  • Protein
    Bifunctional enzyme IspD/IspF
  • Gene
    ispDF
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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
Site38Transition state stabilizer
Site47Transition state stabilizer
Site181Positions MEP for the nucleophilic attack
Site238Positions MEP for the nucleophilic attack
Binding site266a divalent metal cation (UniProtKB | ChEBI)
Binding site266-2684-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site268a divalent metal cation (UniProtKB | ChEBI)
Site292Transition state stabilizer
Binding site292-2934-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site300a divalent metal cation (UniProtKB | ChEBI)
Binding site314-3164-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site390-3934-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site391Transition state stabilizer
Binding site3974-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site4004-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
      ASG58_15950

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Leaf383
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Rhizobiaceae > Rhizobium/Agrobacterium group > Rhizobium

Accessions

  • Primary accession
    A0A0Q5WZL6

Proteomes

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-2592-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain260-4122-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region260-4192-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
    419
  • Mass (Da)
    44,442
  • Last updated
    2016-01-20 v1
  • Checksum
    D36AF39281EF0E2C
MRPGASFEGRQGGVLQQMQRERELSCGVVIVAAGRGERAGASIEGPKQYRRIGGRPVISWTLDAFAAWGKAGPIVVVIHADDEALLETALAACRSRPVVTIVRGGPTRQASVLAGLRALSRQGIRHAMIQDAVRPFVTSDLLDRCLAALSSGVRAVLPAIPVTDTLKRTNISGDVGETVSRDRLFAAQTPQCFDLPSILAAHESAATSGRSDFTDDTSIAEWAGLPVVLVAGSADNVKLTTQQDLRMADERLNGHRIDVRTGNGYDVHQLVPGNGVTLCGIFLPHDQSLLGHSDADVALHALTDALLATCGAGDIGDHFPPSDDRWKGARSRIFLEHAAGIVRQHGGVVMNADISLIAEAPKVGPHRDAMRQALSDMLGISLDRCSVKATTNERIGFVGRREGIAAIATATVSFPDGFR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LMQD01000029
EMBL· GenBank· DDBJ
KQS74463.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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