Q7V8J0 · Q7V8J0_PROMM

Function

function

Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. 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).
Specifically methylates guanosine-37 in various tRNAs.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

a divalent metal cation (UniProtKB | Rhea| CHEBI:60240 )

Note: Binds 1 divalent metal cation per subunit.

Pathway

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.

Features

Showing features for binding site, site.

Type
IDPosition(s)Description
Binding site115S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site134-139S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site256a divalent metal cation (UniProtKB | ChEBI)
Binding site256-2584-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site258a divalent metal cation (UniProtKB | ChEBI)
Site284Transition state stabilizer
Binding site284-2854-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site292a divalent metal cation (UniProtKB | ChEBI)
Binding site306-3084-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Binding site382-3854-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)
Site383Transition state stabilizer
Binding site3924-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity
Molecular Functionmetal ion binding
Molecular FunctiontRNA (guanine(37)-N1)-methyltransferase activity
Biological Processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
Biological Processterpenoid biosynthetic process
Biological ProcesstRNA N1-guanine methylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
  • EC number
  • Short names
    MECDP-synthase
    ; MECPP-synthase
    ; MECPS
  • Recommended name
    tRNA (guanine-N(1)-)-methyltransferase
  • EC number
  • Alternative names
    • M1G-methyltransferase
    • tRNA [GM37] methyltransferase

Gene names

    • Name
      trmD
    • Synonyms
      ispF
    • Ordered locus names
      PMT_0356

Organism names

Accessions

  • Primary accession
    Q7V8J0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.
Homotrimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain27-222tRNA methyltransferase TRMD/TRM10-type
Domain249-4042-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase

Sequence similarities

Belongs to the IspF family.
Belongs to the RNA methyltransferase TrmD family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    410
  • Mass (Da)
    44,893
  • Last updated
    2003-10-01 v1
  • MD5 Checksum
    481BE021DB876BEDE2A046A32D2D1063
MAPFRLDVVTLVPQAFTPLGELGVIGRAFASGIAVLHTHNPRDYTTDRYHKVDDQPYGGGAGMVLKPEPVFAAVEAIPVQARRRVLLLTPQGKPLCQKDLHRWVEDHDQLVLICGHYEGFDERIRGLADEEVSVGDFVLTGGELPAMTVINGVVRLLPGTVGTAESLQDESHSDVLLEHPHYTRPANFRGMVVPDVLRSGDHGAIALWRQQQRQLRTQMRRPDLYVRWSDQQQSSTLTMESHGSTSMQFRIGNGYDIHRLVPGRPLILGGVTLDHPDGLGLDGHSDADVLVHALMDALLGALALGDIGKYFPPDDPRWKGADSLMLLEQVVALVRDRGWQILNVDAVVVAERPKLKPHINAMRSNLAQRLGVELDAVGVKATTNEGLGPEGREEGMSSQAVALLQQIGLT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX548175
EMBL· GenBank· DDBJ
CAE20531.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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