A8F959 · ISPF_BACP2
- Protein2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- GeneispF
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids158 (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 | 9 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 9-11 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DVH | ||||||
Binding site | 11 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 35 | Transition state stabilizer | ||||
Sequence: H | ||||||
Binding site | 35-36 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: HS | ||||||
Binding site | 43 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 57-59 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DIG | ||||||
Binding site | 62-66 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: FPDTD | ||||||
Binding site | 101-107 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: AQKPKMA | ||||||
Binding site | 133-136 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TTTE | ||||||
Site | 134 | Transition state stabilizer | ||||
Sequence: T | ||||||
Binding site | 140 | 4-CDP-2-C-methyl-D-erythritol 2-phosphate (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 143 | 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
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionA8F959
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000057707 | 1-158 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase | |||
Sequence: MLRIGQGFDVHQLTEGRPLIIGGVTIPYEKGLLGHSDADVLLHTVADACLGAIAEGDIGRHFPDTDPEFKDADSFQLLQHVWALVKEKGYTLVNIDCTIMAQKPKMAPYIQPMCEKIAEALEADVTQVNVKATTTEKLGFTGRGEGIASQATVLLQKK |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length158
- Mass (Da)17,145
- Last updated2007-11-13 v1
- ChecksumD6AADDCDCB59883A
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000813 EMBL· GenBank· DDBJ | ABV60776.1 EMBL· GenBank· DDBJ | Genomic DNA |