N1MTC1 · N1MTC1_9SPHN

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
Site24Transition state stabilizer
Site31Transition state stabilizer
Site161Positions MEP for the nucleophilic attack
Site216Positions MEP for the nucleophilic attack
Binding site243a divalent metal cation (UniProtKB | ChEBI)
Binding site243-2454-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site245a divalent metal cation (UniProtKB | ChEBI)
Site269Transition state stabilizer
Binding site269-2704-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site277a divalent metal cation (UniProtKB | ChEBI)
Binding site291-2934-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site367-3704-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site368Transition state stabilizer
Binding site3744-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site3774-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
      EBBID32_32890

Organism names

  • Taxonomic identifier
  • Strain
    • BiD32
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingobium

Accessions

  • Primary accession
    N1MTC1

Proteomes

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-2362-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Domain236-3892-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Region237-3952-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
    395
  • Mass (Da)
    41,557
  • Last updated
    2013-06-26 v1
  • MD5 Checksum
    01DFDFB1A7E6B97BBF4C59F2D08573E8
MPRAMTDNRHRTVALLVAAGTGSRAGGDIPKQFRVVGGKAVIAHAVDALAAHEDIDAIHLVIGAGQEAQVRALLGGRVVAGMTQGADSRRGSVRAGLEAIAAAGGVDRVLIHDAARPFLPGAVVNRLLAALDDAQGAIPVLPVADTLVRGMGGAMGDGVARDDLFRVQTPQVFRFDTILAAHRGWDESREATDDAQIMKGWGHDVTLVAGDEGLEKLTYKQDFARAEARLASARTVRVGMGYDVHRLAPDEELWLGGVLVPHDRGLAGHSDADVALHAIVDALLGALAEGDIGSHFPPSDAQWRGASSDRFLAYARDRVAARGGTIDHVDLTIICEAPRIGPHRDAMRARIAEILDVPVERVSVKATTTERLGFAGRREGIAAQAVATLSLPALS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CAVK010000155
EMBL· GenBank· DDBJ
CCW18932.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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