A0A5B7TCH8 · A0A5B7TCH8_9CLOT
- Protein4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- GeneispH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids654 (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 | 40 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 40 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 40 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 73 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 73 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 73 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 95 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 123 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 123 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 123 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 125 | 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 | |
---|---|---|
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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Caloramator
Accessions
- Primary accessionA0A5B7TCH8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 322-390 | S1 motif | ||||
Sequence: DSIVKGTVLLVNDKEVFFDIGYKSDAILPIEEASNFPVNLKEKFKVGDVYDLQVIKLNDGEGNVLVSRK | ||||||
Domain | 408-476 | S1 motif | ||||
Sequence: EDYIDVIVTKENKGGLECQYGDVKAFMPVSQVGLSKDEDIKEYLGKKLKVKIIDIKEKKNDVEIVVSRK | ||||||
Domain | 497-565 | S1 motif | ||||
Sequence: GQALKGTVKSMIESGVFVSVGDVDVFIPISEISWKRIKTPKEVLNEKDIVEFIVIKVNREDKKITGSIK | ||||||
Domain | 582-651 | S1 motif | ||||
Sequence: DDIVDVKVLRFAEFGAFAEIIPGVDGLIHISKLSEKRINKPQEVVKIGQIVKAKIINIDTASKRVSLSLK |
Sequence similarities
Belongs to the IspH family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length654
- Mass (Da)73,775
- Last updated2019-11-13 v1
- ChecksumC61FEC80BF5E0D9F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP040093 EMBL· GenBank· DDBJ | QCX32616.1 EMBL· GenBank· DDBJ | Genomic DNA |