A0A3R7V7K2 · A0A3R7V7K2_9PROT
- ProteinBifunctional enzyme IspD/IspF
- GeneispD
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids393 (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 | 28 | Transition state stabilizer | ||||
Sequence: K | ||||||
Site | 158 | Positions MEP for the nucleophilic attack | ||||
Sequence: R | ||||||
Site | 214 | Positions MEP for the nucleophilic attack | ||||
Sequence: K | ||||||
Binding site | 241 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 241-243 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DTH | ||||||
Binding site | 243 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 267 | Transition state stabilizer | ||||
Sequence: H | ||||||
Binding site | 267-268 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: HS | ||||||
Binding site | 275 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 289-291 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DIG | ||||||
Binding site | 365-368 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TTTE | ||||||
Site | 366 | Transition state stabilizer | ||||
Sequence: T | ||||||
Binding site | 372 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 375 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria
Accessions
- Primary accessionA0A3R7V7K2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 43-60 | Helical | ||||
Sequence: IEIFFSLPYLTYLIVVIS |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-235 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase | ||||
Sequence: MQKKINKSLAGIILASGSGSRMKRTXPKQYLLINDISLLEINIEIFFSLPYLTYLIVVISKKHFRFYKAIKXKYKNVFFIEGGKSRQESAFNALNFLKKFTCEYVMIHDAARPFVSKXLIDNLYGKLLKVRTAVVPVVKIQDTIKFCXKNXVTKDINRNNLFLTQTPQLFEYKTLYKAYLHNEKILNNFTDDAQIFAKGNSIIHTVKGDIDNTKITTNKDWINKINMMKENFTTK | ||||||
Domain | 235-387 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | ||||
Sequence: KIGHGFDTHKLIKGKKITLFGIRIPHKFKLLGHSDADVGVHAIIDALLGSCSLGDIGKHFPDTXXKIKGXNSLXMLSKXQXLXXDAXAXISXIDCTLVGESPKIAKYTXKMCIXXAKTLXTQKEXISIKATTTEGLGFTGRKEGISCYCVATI | ||||||
Region | 235-393 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | ||||
Sequence: KIGHGFDTHKLIKGKKITLFGIRIPHKFKLLGHSDADVGVHAIIDALLGSCSLGDIGKHFPDTXXKIKGXNSLXMLSKXQXLXXDAXAXISXIDCTLVGESPKIAKYTXKMCIXXAKTLXTQKEXISIKATTTEGLGFTGRKEGISCYCVATIKQEKKI |
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.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length393
- Mass (Da)44,355
- Last updated2019-04-10 v1
- ChecksumA94F0F231124EF62