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Table 1 Residues of importance for catalytic activity, structure or correct folding. Residues for which the importance has been previously determined are shown in Fig. 2, giving their numbers, their role and the bibliographic reference of the appropriate mutation study.

From: Phylogenetic analysis of condensation domains in NRPS sheds light on their functional evolution

Nb. in Fig. 2 Importance: Position is homologous to: Reference:
1 structure Arg62 (R) in TycB1 [34]
2 folding Arg67 (R) in TycB1 [34]
3 folding His146 in TycB1 (1st His of active site His-motif) [34]
4 catalytic activity His126 (2nd His of the active site His-motif) in VibH [14,33,34]
5 structure Asp130 (D) in VibH [14,33,34]
6 catalytic activity Gly131 (G of the active site His-motif) in VibH [33]
7 folding Trp202 (W) in TycB1 [34]
8 structure Arg263 (R) in VibH = Arg278 (R) in EntF [14,33]
9 catalytic activity Trp264 (W) in VibH according to Keating et al., but absent in LCL, DCL and Starter C domains [14]
10 catalytic activity Asn335 (N) in VibH [33]