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Literature summary for 2.8.4.3 extracted from
- MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters (2007), Biochemistry, 46, 5140-5147.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C150/154/157A | mutant lacks the radical-S-adenosyl-L-methionine [4Fe-4S] cluster, inactive in an in vivo assay | Thermotoga maritima |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermotoga maritima | Q9WZC1 | - |
- |
| Thermotoga maritima DSM 3109 | Q9WZC1 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MiaB | - |
Thermotoga maritima |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| [4Fe-4S]-center | presence of two distinct [4Fe-4S]2+,1+ clusters in the protein. One is coordinated by residues Cys150, Cys154, and Cys157 in the radical-AdoMet motif, and the other is proposed to be coordinated by the three N-terminal conserved cysteines Cys10, Cys46, and Cys79. The two [4Fe-4S]2+ clusters have similar UV-visible absorption, resonance Raman, and Moessbauer properties but differ in terms of redox properties and the EPR properties of the reduced [4Fe-4S]1+ clusters | Thermotoga maritima |  |
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