A0A0S6U309 · A0A0S6U309_CLOBO
- Protein4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- GeneispH
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids638 (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
- 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 | 12 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 41 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 41 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 41 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 76 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 76 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 76 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 98 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 126 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 126 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 126 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 128 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 162 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 190 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 218 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 218 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 218 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 219 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 219 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 219 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 220 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 220 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 220 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 262 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 262 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 262 | 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 | |
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 > Eubacteriales > Clostridiaceae > Clostridium
Accessions
- Primary accessionA0A0S6U309
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 303-372 | S1 motif | ||||
Sequence: GKVVKGTIVSLNENELFVDLNYKSEGIIPKEEVTLNEEAILKEAFKVGDEIEAKIVRIKNEDGYVVLSLK | ||||||
Domain | 390-458 | S1 motif | ||||
Sequence: KETIKVIVKDAVDAGLICIYNGVRVFIPASHIELSHVDNLEKYKGSELEVNIIEFIKDRYKTKIVGSRR | ||||||
Domain | 479-547 | S1 motif | ||||
Sequence: DTIVEGEVKRFTNFGAFVEINGVDGLLHVSEISWGRVEKPEDALKIGDKIKVYILDIDKENKKLALSIK | ||||||
Domain | 564-633 | S1 motif | ||||
Sequence: GNIVLGKVVRFASFGAFIELEPGVDGLVHISKISNKRIDKPEEELTLGKEVKAKILEVNSAEKRIALSIK |
Sequence similarities
Belongs to the IspH family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length638
- Mass (Da)71,814
- Last updated2016-02-17 v1
- Checksum53F3251805427D64