Q55643 · ISPH_SYNY3
- Protein4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- GeneispH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids379 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Catalytic activity
- H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H+ + 2 reduced [2Fe-2S]-[ferredoxin]
Cofactor
Note: Binds 1 [4Fe-4S] cluster per subunit.
Pathway
Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 6/6.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 39 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 69 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 69 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 69 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 130 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 158 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 158 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 158 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 160 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 223 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 261 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 290 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 290 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 290 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 291 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 291 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 291 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 292 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 292 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 292 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 352 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 352 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 352 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase activity | |
Molecular Function | metal ion binding | |
Biological Process | dimethylallyl diphosphate biosynthetic process | |
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 name4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- EC number
- Short namesHMBPP reductase
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Synechococcales > Merismopediaceae > Synechocystis
Accessions
- Primary accessionQ55643
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000128880 | 1-379 | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | |||
Sequence: MGVMNTEYQSHLIQEIRQNNYRLERGDVTILLAEAFGFCWGVERAVAMAYETRQHFPGDRLWITNEIIHNPSVNQRLREMEVNFIDVVNGEKDFSGVAKGDVVILPAFGASVEEMQLLNDRECTIVDTTCPWVSKVWNSVEKHKKKEHTSIIHGKYNHEETIATSSFAGTYLIVLNMAEAQKVCDYILHGGDRQEFLDYFANAHSAGFDPDQDLVRLGVANQTTMLKSETEMIGKLFEKTLLQKYGPIELNNHFMSFNTICDATQERQDAMFDLVEEDLSLMVVIGGFNSSNTTHLQEIAVEHGIPSVHIDSGDRIGPGNRVEHKPLGKDLEVLEPWLPAGKITVGVTSGASTPDKVVEEVMKKILAIKEAQPVLEIAG |
Proteomic databases
Structure
Sequence
- Sequence statusComplete
- Length379
- Mass (Da)42,415
- Last updated2000-12-01 v2
- Checksum4CD0167AF5D4957E
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U38915 EMBL· GenBank· DDBJ | AAB72119.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BA000022 EMBL· GenBank· DDBJ | BAA10159.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |