A0A2Z5UBU9 · A0A2Z5UBU9_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.

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
Site24Transition state stabilizer
Site31Transition state stabilizer
Site158Positions MEP for the nucleophilic attack
Site212Positions MEP for the nucleophilic attack
Binding site241a divalent metal cation (UniProtKB | ChEBI)
Binding site241-2434-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site243a divalent metal cation (UniProtKB | ChEBI)
Site267Transition state stabilizer
Binding site267-2684-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site275a divalent metal cation (UniProtKB | ChEBI)
Binding site289-2914-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site365-3684-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site366Transition state stabilizer
Binding site3724-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3754-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
      SPYCW_1367

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • EG6
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingopyxis

Accessions

  • Primary accession
    A0A2Z5UBU9

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2342-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Region235-3922-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Domain236-3872-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
    392
  • Mass (Da)
    40,697
  • Last updated
    2018-10-10 v1
  • Checksum
    7368D124A2FAB3CF
MTESAPFATPRAMAILLAGGRGSRTGFVMPKQLAMLGGKPVLRWSLDALAGHPAIAGGVVVGNDDVMAALGTLPDGWISAGPGEERQQSVANALAALAHCDDAVRVLVHDAARPGVTADVIDRLLAALDVANAAIPTLPVPDTLVEHAGSEAGEVVDRAALARVQTPQAFHLGTLRRAHGVAAEEAATDDAQLVRRQGLSVATVAGDARLHKLTYAEDMAILSGLLGIKTMTRTAVGMGYDVHRLVAGKPLWIGGIEIAHSHGLEGHSDADVGLHALTDAILGALGDGDIGDHFPPSDPQWRGAASHRFLSFAAARVAARSGRIDHVDLAIIAEAPKIGPHRAAMRARIAEILAIPVERVSVKATTTERLGFTGRREGIAAQAVATLRLPEN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP017603
EMBL· GenBank· DDBJ
BBB08351.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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