A0A9D1PUB0 · A0A9D1PUB0_9BACT
- ProteinBifunctional enzyme IspD/IspF
- GeneispD
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids445 (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 | 21 | Transition state stabilizer | ||||
Sequence: R | ||||||
Site | 30 | Transition state stabilizer | ||||
Sequence: K | ||||||
Site | 167 | Positions MEP for the nucleophilic attack | ||||
Sequence: R | ||||||
Site | 223 | Positions MEP for the nucleophilic attack | ||||
Sequence: K | ||||||
Binding site | 293 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 293-295 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DVH | ||||||
Binding site | 295 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 319 | Transition state stabilizer | ||||
Sequence: H | ||||||
Binding site | 319-320 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: HS | ||||||
Binding site | 327 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 341-343 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DIG | ||||||
Binding site | 346-350 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: FPDND | ||||||
Binding site | 417-420 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TTEE | ||||||
Site | 418 | Transition state stabilizer | ||||
Sequence: T | ||||||
Binding site | 424 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: F |
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
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
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae > Desulfovibrio
Accessions
- Primary accessionA0A9D1PUB0
Proteomes
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-286 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase | ||||
Sequence: MPYTLDTAPWLILLAAGQGTRLAAAAGCPKQFLTVDSVPLFWLSVRTCSRVARLGGVVFVFPKDTFESSRDLVRELDRLEPCGLNMAFAVGGARRQDSVASGLAVVPQSARFVLVHDAARPFFSPGLVNALLDRLEAGAQAVIPGLAVTDTIKVVNKAGLVCATPDRSTLRAVQTPQGFSRRALAEAHRTLNTPENTVTDDASLMEEAGHEVLVIDGEAGNIKITNPEDLQLLKKKAETGAEDGSSCTKQAAPDQTVPGQAVSGQAGENGSPAAPDNPDTTGCLVP | ||||||
Region | 241-277 | Disordered | ||||
Sequence: AEDGSSCTKQAAPDQTVPGQAVSGQAGENGSPAAPDN | ||||||
Compositional bias | 243-267 | Polar residues | ||||
Sequence: DGSSCTKQAAPDQTVPGQAVSGQAG | ||||||
Region | 287-445 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | ||||
Sequence: CTGFGYDVHRYGGDRPLVLAGVPIPCDFQVRAHSDGDVLLHALMDALLGLFGQGDIGMLFPDNDPRYDGADSAQLLAEVLQRMRQARVRLTHADVTVVAQKPRLSPHKKAMQESLCRLLGLGPEHVNVKATTEEGLGFTGDLSGIKAYATVCGLKSETI | ||||||
Domain | 288-437 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | ||||
Sequence: TGFGYDVHRYGGDRPLVLAGVPIPCDFQVRAHSDGDVLLHALMDALLGLFGQGDIGMLFPDNDPRYDGADSAQLLAEVLQRMRQARVRLTHADVTVVAQKPRLSPHKKAMQESLCRLLGLGPEHVNVKATTEEGLGFTGDLSGIKAYATV |
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
- Length445
- Mass (Da)47,105
- Last updated2023-05-03 v1
- ChecksumD93044E07E856DAE
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 243-267 | Polar residues | ||||
Sequence: DGSSCTKQAAPDQTVPGQAVSGQAG |