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Table 2 Key positions in AMP domain binding pocket identified by structural modeling

From: Module evolution and substrate specificity of fungal nonribosomal peptide synthetases involved in siderophore biosynthesis

AMP domaina Positionb Prediction
  2 2 2 2 2 2 2 2 2 2 3 3 3 3 3 3 5  
  2 3 3 3 3 4 4 7 8 9 0 2 2 2 3 3 1  
  9 0 5 6 9 0 3 8 0 9 1 0 2 6 0 1 7  
1AMU_A F A D A W E M T P I A I A T I C K Phe
Spsib1 AMP1 F A D V F E G E T I I V A T I H K G
ChNPS2 AMP1 F A D V F E F E T L I W M T I H K G
FgNPS2 AMP1 F A D V F E F E T L I W M T I H K G
FgNPS1 AMP2 L S D V Q D Y H T T I Y T A V V K G
AnsidC AMP2 F S D V Q D Y H T T I F T A V V K G
Umfer3 AMP2 F S D V Q D W H T T I Y T A V V K G
ChNPS2 AMP3 Y A D M Y D L D T Y I V S T F C K G
Umsid2 AMP1 Y S D L M D Y L T I G L L A L I K G
ChNPS2 AMP2 A C D V F E F S T V A Y G S N I K S
FgNPS2 AMP2 A C D V F E Y S T V A W G S N I K S
AnsidC AMP1 F A D P M E V M T W M V A T I N K S
Umfer3 AMP1 F A D P M E V M T W M A A T V N K S
FgNPS1 AMP1 G A D I F E W N T M G F G T I Y K A
Spsib1 AMP2 T A D C C W G I T Y Y I A L I C K degenerate
Spsib1 AMP3 F A D V L E F D T I G Y F T I G K AHO
ChNPS2 AMP4 F A D V L E W D T I G Y G T I G K AHO
FgNPS2 AMP3 F A D V L E W D T I G Y A T I G K AHO
FgNPS1 AMP3 L T D P T Q V G V T G F F T I G K AHO
AnsidC AMP3 Q A D P L E F S V T G V A T I G K AHO
Umfer3 AMP3 L A D V S Q M S V G G L A T I M K AHO
Umsid2 AMP2 R S D V L E L C V I G L A S I G K AHO
Umsid2 AMP3 L A D V I E M D P M G I A T I G K AHO
  1. a AMP domains in bold within blocks have highly similar residue sets.
  2. b Positions in bold correspond to the proposed 10 AA code. Position 229, in bold italics, corresponds to one of three additional positions (226, 229, 276) predicted by Schwecke et al. [6] to bind AHO. All other sites were identified in this study. Residues D and K at positions 235 and 517 in bold indicate residue conservation. Letters in body of table refer to amino acid residues.