A0A2A5KVI4 · A0A2A5KVI4_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.

TypeIDPosition(s)Description
Site24Transition state stabilizer
Site33Transition state stabilizer
Site167Positions MEP for the nucleophilic attack
Site224Positions MEP for the nucleophilic attack
Binding site253a divalent metal cation (UniProtKB | ChEBI)
Binding site253-2554-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site255a divalent metal cation (UniProtKB | ChEBI)
Site279Transition state stabilizer
Binding site279-2804-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site287a divalent metal cation (UniProtKB | ChEBI)
Binding site301-3034-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site377-3804-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site378Transition state stabilizer
Binding site3844-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3874-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
      CPT34_10210
      , EFR00_03515

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • L101
    • CCBAU 03470
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Rhizobiaceae > Rhizobium/Agrobacterium group > Rhizobium

Accessions

  • Primary accession
    A0A2A5KVI4

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2462-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain247-3992-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region247-4052-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
    405
  • Mass (Da)
    43,198
  • Last updated
    2017-12-20 v1
  • Checksum
    B33BB196403DC9CF
MLQMPSKQLISAGIVIVAAGRGERAGSSKDGPKQYRPIGGTPVIVHTLENFMTWELATEIVVVIHPDDEALFAKALRHIISATPIQTVHGGPTRQQSVLAGLRYLKDKHVSHVLIHDAVRPFFDHALLDRIAESLGNGAAAVLPAMPVTDTLKRADGAGTVLTTVSREQLYSAQTPQSFAFETILDAHEKAAASGRSDFTDDASIAEWLGIPVTIVEGTGDNVKLTVKSDIVMADDKLSASLLPDVRTGNGYDVHQLEAGDGVTLCGVFIPHDQKLKGHSDADVALHALTDALLATCGAGDIGDHFPPSDPQWKGAASRIFIEHAARIVRERGGTIMNADVSLIAEAPKVGPHREAMRANLSEYLGIDLERCSVKATTNETIGFVGRREGIAAIATATVVYRGRK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NXDM01000008
EMBL· GenBank· DDBJ
PCK81068.1
EMBL· GenBank· DDBJ
Genomic DNA
RQIH01000002
EMBL· GenBank· DDBJ
RSC20607.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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