A0AA37WY51 · A0AA37WY51_9RHOB

  • 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
Site15Transition state stabilizer
Site22Transition state stabilizer
Site144Positions MEP for the nucleophilic attack
Site197Positions MEP for the nucleophilic attack
Binding site225a divalent metal cation (UniProtKB | ChEBI)
Binding site225-2274-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site227a divalent metal cation (UniProtKB | ChEBI)
Site251Transition state stabilizer
Binding site251-2524-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site259a divalent metal cation (UniProtKB | ChEBI)
Binding site273-2754-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site349-3524-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site350Transition state stabilizer
Binding site3564-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3594-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

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
      GCM10010873_00860

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NBRC 111766
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Paracoccaceae > Cypionkella

Accessions

  • Primary accession
    A0AA37WY51

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-2182-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain218-3712-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region219-3742-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
    374
  • Mass (Da)
    38,972
  • Last updated
    2024-01-24 v1
  • Checksum
    3E393531FB82D8A1
MTTAAIITAAGRGLRAGGDVPKQWQMLAGQPVVAQALAAFDGMLRVLVVHPDDTARAEALGLDVLIVAGGATRSASVRNALEALAGRNIARVLIHDGARPLVSAAVIARVIAALDHAKAAAPALAVTDALWRGADGMVAGTVARDGLFRAQTPQGFCFETILSAHRAHLGDAADDVAVARAFGVEVAIVAGDEDNLKLTYPGDFARAEAILRGRQMDLRVGNGFDVHAFCDGDGVWLCGVKVPHGRGLLGHSDADVGMHALTDAIYGALAEGDIGRHFPPSDPQWKGADSKIFLAHAMRLARARGFALANCDVTLICERPKIGPYAEAMRSALAAIMDVALERISVKATTSERLGFTGREEGIAAMATCALVRA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BSPP01000001
EMBL· GenBank· DDBJ
GLS85113.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp