A0A1B9VKT8 · A0A1B9VKT8_9PROT
- ProteinBifunctional enzyme IspD/IspF
- GeneispDF
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids397 (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 | 17 | Transition state stabilizer | ||||
Sequence: R | ||||||
Site | 24 | Transition state stabilizer | ||||
Sequence: K | ||||||
Site | 154 | Positions MEP for the nucleophilic attack | ||||
Sequence: R | ||||||
Site | 208 | Positions MEP for the nucleophilic attack | ||||
Sequence: K | ||||||
Binding site | 246 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 246-248 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DVH | ||||||
Binding site | 248 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 272 | Transition state stabilizer | ||||
Sequence: H | ||||||
Binding site | 272-273 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: HS | ||||||
Binding site | 280 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 294-296 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DIG | ||||||
Binding site | 370-373 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TTTE | ||||||
Site | 371 | Transition state stabilizer | ||||
Sequence: T | ||||||
Binding site | 377 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 380 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R |
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 > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Thalassospiraceae > Thalassospira
Accessions
- Primary accessionA0A1B9VKT8
Proteomes
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-234 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase | ||||
Sequence: MTKKIAVVIVAAGSGSRFGDPIPKQYHLLGAKTLLRHCIESFAKYVPSELIRVIYNPDHQDLYDNSVKGLSLDAPVPGGVTRQQSVLNGLRSLENENPDHVLIHDAARPGISDDVIDRVISALATYQGAIPTLPVLDTIKQTESTGIIRRTIPREQLHRAQTPQGFHFKTILDAHQRFEGHEFTDDAALLEQLGLDVVCVEGAGSNDKITRPDDIERARDWINPVPASEKDSDM | ||||||
Domain | 239-392 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | ||||
Sequence: FRAGTGFDVHRFAPGDHCILCGVKVPHSARLEGHSDADVGLHTLTDALLGSIGAGDIGQHFPPSDMKWKGAASDQFVLHAVNLIRERGGRIVNADITLICERPKIGPHTQAMREKVAEILGIEVDRVNVKATTTERLGFTGREEGIAAQAAVSV | ||||||
Region | 240-397 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | ||||
Sequence: RAGTGFDVHRFAPGDHCILCGVKVPHSARLEGHSDADVGLHTLTDALLGSIGAGDIGQHFPPSDMKWKGAASDQFVLHAVNLIRERGGRIVNADITLICERPKIGPHTQAMREKVAEILGIEVDRVNVKATTTERLGFTGREEGIAAQAAVSVALPVK |
Sequence similarities
Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.
Belongs to the IspF family.
In the C-terminal section; belongs to the IspF family.
In the N-terminal section; belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length397
- Mass (Da)43,226
- Last updated2016-11-02 v1
- Checksum03BF9F365F24948F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MAJC01000002 EMBL· GenBank· DDBJ | OCK09050.1 EMBL· GenBank· DDBJ | Genomic DNA |