A0A2W5HH12 · A0A2W5HH12_9BACT
- ProteinBifunctional enzyme IspD/IspF
- GeneispDF
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids377 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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).
Catalytic activity
- 2-C-methyl-D-erythritol 4-phosphate + CTP + H+ = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Cofactor
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 | 16 | Transition state stabilizer | |||
Site | 23 | Transition state stabilizer | |||
Site | 153 | Positions MEP for the nucleophilic attack | |||
Site | 206 | Positions MEP for the nucleophilic attack | |||
Binding site | 228 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 228-230 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | |||
Binding site | 230 | a divalent metal cation (UniProtKB | ChEBI) | |||
Site | 255 | Transition state stabilizer | |||
Binding site | 255-256 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | |||
Binding site | 263 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 277-279 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | |||
Binding site | 353-356 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | |||
Site | 354 | Transition state stabilizer | |||
Binding site | 360 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | |||
Binding site | 363 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | |||
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 nameBifunctional enzyme IspD/IspF
Including 2 domains:
- Recommended name2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- EC number
- Alternative names
- Recommended name2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- EC number
- Short namesMECDP-synthase ; MECPP-synthase ; MECPS
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bdellovibrionota > Bdellovibrionia > Bdellovibrionales > Pseudobdellovibrionaceae > Micavibrio
Accessions
- Primary accessionA0A2W5HH12
Proteomes
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-221 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase | |||
Domain | 222-375 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | |||
Region | 222-377 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | |||
Sequence similarities
Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.
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 statusComplete
- Length377
- Mass (Da)41,245
- Last updated2018-09-12 v1
- Checksum026FBFBF8848453F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
QFOT01000101 EMBL· GenBank· DDBJ | PZP54912.1 EMBL· GenBank· DDBJ | Genomic DNA |