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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.