A0A0M3AUI7 · A0A0M3AUI7_9SPHN

  • 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
Site17Transition state stabilizer
Site24Transition state stabilizer
Site154Positions MEP for the nucleophilic attack
Site209Positions MEP for the nucleophilic attack
Binding site236a divalent metal cation (UniProtKB | ChEBI)
Binding site236-2384-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site238a divalent metal cation (UniProtKB | ChEBI)
Site262Transition state stabilizer
Binding site262-2634-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site270a divalent metal cation (UniProtKB | ChEBI)
Binding site284-2864-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site360-3634-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site361Transition state stabilizer
Binding site3674-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3704-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
      YP76_06555

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DJ77
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingobium

Accessions

  • Primary accession
    A0A0M3AUI7

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-2292-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain230-3822-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region230-3882-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
    388
  • Mass (Da)
    40,962
  • Last updated
    2015-11-11 v1
  • Checksum
    12CD4F1A459AF0D4
MTEKTVALLVAAGQGNRAGGGTPKQFRMIGGKPVLAHAVDALIAHPGIDSVTVVVGAGQEAAAMTALAGRPIAAIVEGADSRRGSVRAGLEQIASSGGAGRILIHDAARPFLPAAVIDRLLSALDEAAGAIPVLPVADTLVRHQDGRAGDTVDRDTLARVQTPQAFHFDTLLSAHRAWDSQREATDDAQIVRHQGHDVLLVTGDERLEKLTYPEDFVRAERGLGVTRSTRVGMGYDVHRLADREELWLGGIRMPHDRGLSGHSDADVALHAIVDALLGALAEGDIGSHFPPSDPQWRGVASARFLEYAADRVAKRDGIIEHIDLTIICEAPKIGPHRDAMRARIAEILALSLDRVSVKATTTERLGFAGRGEGIAAQAVATLSLPALS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LBIC01000003
EMBL· GenBank· DDBJ
KKW92596.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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