A0A3D0FSW3 · A0A3D0FSW3_9BACT
- ProteinMultifunctional fusion protein
- GeneispH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids956 (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.
Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA.
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 | 14 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 42 | substrate | ||||
Sequence: H | ||||||
Binding site | 76 | substrate | ||||
Sequence: H | ||||||
Binding site | 98 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 130 | substrate | ||||
Sequence: H | ||||||
Active site | 132 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 168 | substrate | ||||
Sequence: T | ||||||
Binding site | 203 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 231-233 | substrate | ||||
Sequence: SSN | ||||||
Binding site | 275 | substrate | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | primosome complex | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase activity | |
Molecular Function | ATP binding | |
Molecular Function | DNA binding | |
Molecular Function | DNA helicase activity | |
Molecular Function | hydrolase activity | |
Molecular Function | zinc ion binding | |
Biological Process | dimethylallyl diphosphate biosynthetic process | |
Biological Process | DNA replication, synthesis of primer | |
Biological Process | DNA unwinding involved in DNA replication | |
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 nameMultifunctional fusion protein
Including 2 domains:
- Recommended name4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- EC number
- Short namesHMBPP reductase
- Recommended namePrimosomal protein N'
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales > Rikenellaceae
Accessions
- Primary accessionA0A3D0FSW3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Interaction
Subunit
Component of the primosome.
Structure
Family & Domains
Features
Showing features for domain, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 429-597 | Helicase ATP-binding | ||||
Sequence: KQSFADGKITLLYGVTGSGKSEIYMHLAMEELKKGNNVLFLVPEIAMSRQLGTRLERFFGNSLLIYHSKQSLSERERVRKQLYDHKCPFIVLGTRSSLFLPFTNLSLIIVDEEHDSSYKQSDPAPRYSGRDTALILASLHSANALLGSATPSLESYFNAISGRYSMVEL | ||||||
Zinc finger | 660-672 | C4-type | ||||
Sequence: CMYCEDIPICPHC | ||||||
Zinc finger | 687-703 | C4-type | ||||
Sequence: CHYCNYNIRFNTICTKC | ||||||
Domain | 695-857 | Helicase C-terminal | ||||
Sequence: RFNTICTKCGKPGLRDIGAGTEKVEETLKELFPNAKVERFDLETTRSSTKEMSILKNFSQGKTDILVGTQMLGKGFDFENLSLICILNSEGMLAIQDFRAEERTFQMLTQLAGRVGRRDSAGKVIIQTSRSDHPVYKHLLKTQQKEAGIIIAEEMLREREEYG |
Sequence similarities
Belongs to the IspH family.
Belongs to the helicase family. PriA subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length956
- Mass (Da)108,278
- Last updated2019-01-16 v1
- ChecksumD73D2050982069FA