CATH Classification
Domain Context
CATH Clusters
| Superfamily | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, catalytic domain |
| Functional Family | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase |
Enzyme Information
| 1.17.7.4 |
4-hydroxy-3-methylbut-2-enyl diphosphate reductase.
based on mapping to UniProt P62623
(1) Isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+). (2) Dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+).
-!- Forms a system with a ferredoxin or a flavodoxin and an NAD(P)H-dependent reductase. -!- This is the last enzyme in the non-mevalonate pathway for isoprenoid biosynthesis. -!- This pathway, also known as the 1-deoxy-D-xylulose 5-phosphate (DOXP) or as the 2-C-methyl-D-erythritol-4-phosphate (MEP) pathway, is found in most bacteria and in plant chloroplasts. -!- The enzyme acts in the reverse direction, producing a 5:1 mixture of isopentenyl diphosphate and dimethylallyl diphosphate. -!- Formerly EC 1.17.1.2.
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UniProtKB Entries (1)
| P62623 |
ISPH_ECOLI
Escherichia coli K-12
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
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PDB Structure
| PDB | 3UV7 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Discovery of acetylene hydratase activity of the iron-sulphur protein IspH.
Nat Commun
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