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Literature summary extracted from
- Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus (2008), J. Mol. Biol., 379, 1063-1074.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.8.99.5 | - |
Archaeoglobus fulgidus |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.8.7.1 | hanging-drop method, crystal structure of the dSir (alphabeta)2 core complex at 2.0 A resolution | Archaeoglobus fulgidus |
| 1.8.99.5 | crystal structure at 2 A resolution and comparison with that of the phylogenetically related assimilatory sulfite reductase aSir. Dissimilatory sulfite reductase dSir is organized as a heterotetrameric complex composed of two catalytically independent alphabeta heterodimers. aSir is a monomeric protein built of two fused modules. aSir binds one siroheme-[4Fe-4S] center, dSir harbors two of them within each alphabeta heterodimer. Only one siroheme-[4Fe-4S] center in each alphabeta heterodimer is catalytically active, whereas access to the second one is blocked by a tryptophan residue | Archaeoglobus fulgidus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.7.1 | Archaeoglobus fulgidus | - |
DSM 4304T | - |
| 1.8.99.5 | Archaeoglobus fulgidus | Q59109 and Q59110 | Q59109 i.e. subunit DsrA, Q59110 i.e. subunit DsrB | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.8.7.1 | - |
Archaeoglobus fulgidus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.8.7.1 | dissimilatory sulfite reductase | - |
Archaeoglobus fulgidus |
| 1.8.7.1 | dSiR | - |
Archaeoglobus fulgidus |
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Release 2023.1 (January 2023)
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