A0A5B7WQ57 · A0A5B7WQ57_9MICC
- ProteinMultifunctional fusion protein
- GeneispDF
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids407 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
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).
Catalytic activity
- 2-C-methyl-D-erythritol 4-phosphate + CTP + H+ = 4-CDP-2-C-methyl-D-erythritol + diphosphate
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 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 | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 21 | Transition state stabilizer | ||||
Sequence: R | ||||||
Site | 28 | Transition state stabilizer | ||||
Sequence: K | ||||||
Site | 162 | Positions MEP for the nucleophilic attack | ||||
Sequence: R | ||||||
Site | 222 | Positions MEP for the nucleophilic attack | ||||
Sequence: K | ||||||
Binding site | 258 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 258-260 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DVH | ||||||
Binding site | 260 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 286 | Transition state stabilizer | ||||
Sequence: H | ||||||
Binding site | 286-287 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: HS | ||||||
Binding site | 294 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 308-310 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DLG | ||||||
Binding site | 381-384 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TTSD | ||||||
Site | 382 | Transition state stabilizer | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity | |
Molecular Function | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity | |
Molecular Function | metal ion binding | |
Biological Process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway | |
Biological Process | terpenoid biosynthetic process |
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 name2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Glutamicibacter
Accessions
- Primary accessionA0A5B7WQ57
Proteomes
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 252-403 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | ||||
Sequence: RIGNAIDVHAVSKDPQRPMWLAGLLFADDVGLDGHSDGDAVAHAACDALFSAAGIGDLGTHFGVDRPEMAGASGTTLLAEAARIVRAAGYQIGNVSVQFVGRRPRFAARREEANQVLSDAAQASVTVTATTSDGLGYEGEGAGITAYATALV |
Sequence similarities
Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.
Belongs to the IspF family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length407
- Mass (Da)42,751
- Last updated2019-11-13 v1
- ChecksumEFCCB17C0693E0D0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP034412 EMBL· GenBank· DDBJ | QCY46198.1 EMBL· GenBank· DDBJ | Genomic DNA |