Q8RI52 · ISPH_FUSNN
- Protein4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- GeneispH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids827 (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
- 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 | 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 | 79 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 79 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 79 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 101 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 129 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 129 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 129 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 131 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 168 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 196 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 224 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 224 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 224 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 225 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 225 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 225 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 226 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 226 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 226 | isopentenyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 268 | (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 268 | dimethylallyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 268 | 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 > Fusobacteriota > Fusobacteriia > Fusobacteriales > Fusobacteriaceae > Fusobacterium
Accessions
- Primary accessionQ8RI52
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000128909 | 1-827 | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | |||
Sequence: MEIIRAKHMGFCFGVLEAINVCNSLVEEKGRKYILGMLVHNKQVVEDMERKGFKLVTEDELLNDMDELKEDDIVVIRAHGTSKSVHEKLKERKVKVFDATCIFVNKIRQEIEIANENGYSILFMGDKNHPEVKGVISFADDIQIFESFEEAKKLKIDLDKTYLLSTQTTLNKKKFEEIKKYFKENYKNVVIFDKICGATAVRQKAVEDLAVKVEVMIIVGDTKSSNTKKLYEISKKLNDNSYLVENEEQLDLSIFRGKEVVGITAGASTPEETIMNIEKKVRGIYKMSNVNENQNEFSLMLEEFLPNQEKRVEGVIESMDQNFSYLDVPGERTAVRVRTDELKDYKVGDTVEVLITGLSEEDDDQEYITASRRKIEVEKNWEKIEDSFKNKTILDAKVTKKIKGGYLVEAFLYPGFLPNSLSEISDSEEKVNGKKIQVIVKDIKMDPKDKKNRKITYSVKDIRLAEQEKEFAGLAVGQIVDCVVTEVLDFGLAVDINTLKGFIHISEVSWKRLDKLSDNYKVGDKIKAVVVSLDEAKRNVKLSIKKLEEDPWATVANEFKVDDEIEGIVTKVLPYGAFVEIKPGVEGLVHISDFSWTKKKVNVADYVKEREKIKVRITDLHPEDRKLKLGIKQLVANPWETAEKDFAIDTVIKGKVVEVKPFGIFVEIADGIDAFVHSSDYNWVGEEIPKFEIGNEVELKITELDLNNKKIKGSLKALRKSPWEHAMEEYKVGTTVEKKIKTVADFGLFIELIKGIDGFIPTQFASKEFIKNIRDKFSEGDVVKAQVVEVNKETQKIKLSIKKIEIEEEKREEREQIEKYSTSSSEE |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-284 | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase | ||||
Sequence: MEIIRAKHMGFCFGVLEAINVCNSLVEEKGRKYILGMLVHNKQVVEDMERKGFKLVTEDELLNDMDELKEDDIVVIRAHGTSKSVHEKLKERKVKVFDATCIFVNKIRQEIEIANENGYSILFMGDKNHPEVKGVISFADDIQIFESFEEAKKLKIDLDKTYLLSTQTTLNKKKFEEIKKYFKENYKNVVIFDKICGATAVRQKAVEDLAVKVEVMIIVGDTKSSNTKKLYEISKKLNDNSYLVENEEQLDLSIFRGKEVVGITAGASTPEETIMNIEKKVRGI | ||||||
Domain | 477-545 | S1 motif 1 | ||||
Sequence: GQIVDCVVTEVLDFGLAVDINTLKGFIHISEVSWKRLDKLSDNYKVGDKIKAVVVSLDEAKRNVKLSIK | ||||||
Domain | 562-632 | S1 motif 2 | ||||
Sequence: DDEIEGIVTKVLPYGAFVEIKPGVEGLVHISDFSWTKKKVNVADYVKEREKIKVRITDLHPEDRKLKLGIK | ||||||
Domain | 649-716 | S1 motif 3 | ||||
Sequence: DTVIKGKVVEVKPFGIFVEIADGIDAFVHSSDYNWVGEEIPKFEIGNEVELKITELDLNNKKIKGSLK | ||||||
Domain | 733-802 | S1 motif 4 | ||||
Sequence: GTTVEKKIKTVADFGLFIELIKGIDGFIPTQFASKEFIKNIRDKFSEGDVVKAQVVEVNKETQKIKLSIK |
Sequence similarities
In the N-terminal section; belongs to the IspH family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length827
- Mass (Da)94,508
- Last updated2002-06-01 v1
- Checksum23B71DCED082A35E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE009951 EMBL· GenBank· DDBJ | AAL93880.1 EMBL· GenBank· DDBJ | Genomic DNA |