M5E1P8 · M5E1P8_9FIRM
- Protein4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- GeneispH
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids753 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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
- isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] + H2O = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 reduced [2Fe-2S]-[ferredoxin] + 2 H+
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 | 15 | [4Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 45 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 45 | dimethylallyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 45 | isopentenyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 77 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 77 | dimethylallyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 77 | isopentenyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 99 | [4Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 127 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 127 | dimethylallyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 127 | isopentenyl diphosphate (UniProtKB | ChEBI) | |||
Active site | 129 | Proton donor | |||
Binding site | 165 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 193 | [4Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 221 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 221 | dimethylallyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 221 | isopentenyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 223 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 223 | dimethylallyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 223 | isopentenyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 265 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 265 | dimethylallyl diphosphate (UniProtKB | ChEBI) | |||
Binding site | 265 | isopentenyl diphosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | ribosome | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleic acid 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
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Halanaerobiales > Halanaerobiaceae > Halanaerobium
Accessions
- Primary accessionM5E1P8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 283-363 | Disordered | |||
Compositional bias | 295-358 | Acidic residues | |||
Domain | 371-440 | S1 motif | |||
Domain | 458-523 | S1 motif | |||
Domain | 544-612 | S1 motif | |||
Domain | 629-698 | S1 motif | |||
Region | 698-753 | Disordered | |||
Compositional bias | 710-740 | Polar residues | |||
Sequence similarities
Belongs to the IspH family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length753
- Mass (Da)83,313
- Last updated2013-05-29 v1
- MD5 Checksum17FD242AAAFA216DB6F4E58DE605432E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 295-358 | Acidic residues | |||
Compositional bias | 710-740 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CAUI01000015 EMBL· GenBank· DDBJ | CCU79483.1 EMBL· GenBank· DDBJ | Genomic DNA |