Literature summary extracted from

Hernandez, H.L.; Pierrel, F.; Elleingand, E.; Garcia-Serres, R.; Huynh, B.H.; Johnson, M.K.; Fontecave, M.; Atta, M.
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

EC Number	Protein Variants	Comment	Organism
2.8.4.3	C150/154/157A	mutant lacks the radical-S-adenosyl-L-methionine [4Fe-4S] cluster, inactive in an in vivo assay	Thermotoga maritima

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.8.4.3	Thermotoga maritima	Q9WZC1	-	-
2.8.4.3	Thermotoga maritima DSM 3109	Q9WZC1	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
2.8.4.3	MiaB	-	Thermotoga maritima

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
2.8.4.3	[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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)