Q7V8J0 · Q7V8J0_PROMM
- ProteinMultifunctional fusion protein
- GenetrmD
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids410 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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.
Catalytic activity
- 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Cofactor
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 | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 115 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 134-139 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | |||
Binding site | 256 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 256-258 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | |||
Binding site | 258 | a divalent metal cation (UniProtKB | ChEBI) | |||
Site | 284 | Transition state stabilizer | |||
Binding site | 284-285 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | |||
Binding site | 292 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 306-308 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | |||
Binding site | 382-385 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | |||
Site | 383 | Transition state stabilizer | |||
Binding site | 392 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity | |
Molecular Function | metal ion binding | |
Molecular Function | tRNA (guanine(37)-N1)-methyltransferase activity | |
Biological Process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway | |
Biological Process | terpenoid biosynthetic process | |
Biological Process | tRNA N1-guanine methylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended name2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- EC number
- Short namesMECDP-synthase ; MECPP-synthase ; MECPS
- Recommended nametRNA (guanine-N(1)-)-methyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Synechococcales > Prochlorococcaceae > Prochlorococcus
Accessions
- Primary accessionQ7V8J0
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Homotrimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 27-222 | tRNA methyltransferase TRMD/TRM10-type | |||
Domain | 249-404 | 2-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 statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length410
- Mass (Da)44,893
- Last updated2003-10-01 v1
- MD5 Checksum481BE021DB876BEDE2A046A32D2D1063
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX548175 EMBL· GenBank· DDBJ | CAE20531.1 EMBL· GenBank· DDBJ | Genomic DNA |