A0A0Q4ESI5 · A0A0Q4ESI5_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.

TypeIDPosition(s)Description
Site19Transition state stabilizer
Site26Transition state stabilizer
Site149Positions MEP for the nucleophilic attack
Site204Positions MEP for the nucleophilic attack
Binding site229a divalent metal cation (UniProtKB | ChEBI)
Binding site229-2314-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site231a divalent metal cation (UniProtKB | ChEBI)
Site255Transition state stabilizer
Binding site255-2564-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site263a divalent metal cation (UniProtKB | ChEBI)
Binding site277-2794-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site353-3564-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site354Transition state stabilizer
Binding site3604-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3634-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
      ASE69_01380

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Leaf208
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingomonas

Accessions

  • Primary accession
    A0A0Q4ESI5

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2222-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain223-3752-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region223-3822-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
    382
  • Mass (Da)
    39,851
  • Last updated
    2016-01-20 v1
  • Checksum
    3C883635DA6C239C
MTQAQRIVAIIVAAGTGVRAGGSVPKQFALIAGRPMIAYSHEAFATHPAIAETIVVVAEGQQGLATAALGDVSIVVGGTTRRESVTNGLATVGEATHVLIHDAARPFLSHAVIDSLAAALKTRDAAIPVLPVTDTLARGSVLLGDIVPRADLNRVQTPQAFAVEALRAAHAVWPADEEATDDAQMVRRLGVGVALVQGSAMLEKVTHPEDFAAAEARVAYETRTAMGFDVHRLETGEELWLGGVLIPHDKGLSGHSDADVALHALTDALLGTIAAGDIGTHFPPSDPQWKGADSAQFLQHAAKLIADKRGRIDFVDLTIMCEAPKIGPHRTAMTARIADLLGLTLDRVSVKATTTERLGFTGRGEGIAAQAVATIRLPGSPL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LMKH01000001
EMBL· GenBank· DDBJ
KQM56351.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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