A0A6A7K6A2 · A0A6A7K6A2_9FIRM
- Protein2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- GeneispF
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids157 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
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
- 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
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 4/6.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 8 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 8-10 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DVH | ||||||
Binding site | 10 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 34 | Transition state stabilizer | ||||
Sequence: H | ||||||
Binding site | 34-35 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: HS | ||||||
Binding site | 42 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 56-58 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DIG | ||||||
Binding site | 61-65 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: FPDTD | ||||||
Binding site | 100-106 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: AQRPKMA | ||||||
Binding site | 132-135 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TTEE | ||||||
Site | 133 | Transition state stabilizer | ||||
Sequence: T | ||||||
Binding site | 139 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 142 | 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 | 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 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 > Bacillota > Clostridia > Eubacteriales > Eubacteriaceae > Alkalibaculum
Accessions
- Primary accessionA0A6A7K6A2
Proteomes
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-154 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | ||||
Sequence: MKIGIGYDVHELTKGRNLIIGGVKIPYEKGLLGHSDADVLIHAIMDAIIGALGLGDIGKHFPDTDNKYKNIDSLLLLDEVYKILKSKGYKIQNLDGVIIAQRPKMAPYIEGMKKNIANILRSSLEDINIKATTEEGLGFTGREEGIASQVVVLL |
Sequence similarities
Belongs to the IspF family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length157
- Mass (Da)17,169
- Last updated2020-06-17 v1
- Checksum4B78B516F2E97D5D
Keywords
- Technical term