A0A6V8SGN7 · A0A6V8SGN7_9CLOT
- Protein4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- GeneispH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids636 (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 | 13 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 42 | substrate | ||||
Sequence: H | ||||||
Binding site | 77 | substrate | ||||
Sequence: H | ||||||
Binding site | 99 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 127 | substrate | ||||
Sequence: H | ||||||
Active site | 129 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 163 | substrate | ||||
Sequence: T | ||||||
Binding site | 191 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 219-221 | substrate | ||||
Sequence: SSN | ||||||
Binding site | 265 | substrate | ||||
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 | |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Clostridium
Accessions
- Primary accessionA0A6V8SGN7
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 302-374 | S1 motif | ||||
Sequence: GEILKGEILSIVKNELIVAIDGYKADGVIPNSEISVNDGVKSKLSEHFKVGELVDAKVLRLQNEEGYVVLSRI | ||||||
Domain | 392-459 | S1 motif | ||||
Sequence: GSIVTVKVTEVVNGGVVATFKGLRVFIPASQLDIKYTGEFDNFVGKEIEVKFIEVEKERHIRIVASRR | ||||||
Domain | 480-548 | S1 motif | ||||
Sequence: GDVVEGTVKRFTNFGAFVEVNGIDGLVHISEISWGKINNPSDVLKVGEKVKAKVIALDIEKKKVSLSVK | ||||||
Domain | 565-634 | S1 motif | ||||
Sequence: GSIVLGKVARLNDFGAFLELEPGVDGLAHISKISFNKISHPSEVLKVGELVKARIIKVEKENKRIGLSIK |
Sequence similarities
Belongs to the IspH family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length636
- Mass (Da)70,815
- Last updated2020-12-02 v1
- Checksum24D72975E534357F
Keywords
- Technical term