SitesBLAST

K135 (≠ S126) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
135:142 (vs. 126:133, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
K142 (≠ R133) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.

2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
36% identity, 93% coverage: 16:258/260 of query aligns to 20:258/260 of 2hw5C

query
sites
2hw5C

V

I

T

Q

L

L

D

N

R

R

P

P

K
|
K

A
|
A

-
x
L

N

N

A
|
A

I

L

D

C

L

D

T

G

T

L

S

I

R

D

L

E

M

L

G

N

E

Q

T

A

F

L

K

K

K

I

F

F

R

E

D

E

D

D

T

P

E

A

L

V

R

G

V

-

A

A

I

I

V

V

Q

L

T

T

E

G

G

G

D

D

K
|
K

F

A

F

F

C

A

A

A

G

G

W
x
A

D

D

L
x
I

K

K

A

E

A
x
M

A

Q

G

N

G

L

D

S

A

F

V

Q

D

D

G

C

D

-

Y

Y

G
x
S

V

S

G

K

G

F

F
x
L

G

K

G

H

L

W

Q

D

E

H

L

L

I

T

D

Q

L

V

N

K

K

K

P

P

V

V

I

I

A

A

V

V

N

N

G

G

M

Y

A

A

V
x
F

G

G

G
|
G

G

G

F

C

E
|
E

L

L

A

A

L

M

S

M

C

C

D

D

L

I

I

I

Y

Y

A

A

S

G

D

E

H

K

S

A

S

Q

F

F

A

A

L

Q

P
|
P

E
|
E

I

I

R

L

A

I

G

G

T
|
T

L

I

A
x
P

D
x
G

A

A

-

G

A

G

T

T

V

Q

K

R

L

L

P

T

K

R

R

A

I

V

P

G

Y

K

H

S

V

L

A

A

M

M

D

E

L

M

L

V

L

L

T

T

G

G

R

D

W

R

M

I

D

S

V

A

T

Q

E

D

A

A

H

K

R

Q

W

A

G

G

L

L

V

V

N

S

E

K

V

I

L

C

P

P

K

V

D

E

K

T

L

L

M

V

E

E

R

E

V

A

W

I

E

Q

I

C

A

A

R

E

M

K

L

I

E

A

S

S

G

N

P

S

P

K

L

I

V

V

F

V

A

A

A

M

I

A

K

K

E

E

V

S

A

V

R

N

E

A

A

A

E

F

S

E

M

M

G

T

F

L

Q

T

E

E

A

G

M

S

N
x
K

W

L

I

E

T

K

K

K

R

L

K

F

F

Y

R

S

T

T

V

-

D

-

T

-

L

-

Y
x
F

A

A

S

T

E

D

D

D

G

R

Q

K

E

E

G

G

F

M

K

T

A

A

F

F

A

V

E

E

K

K

R

R

E

K

P

A

V

N

W

F

K

K

active site: A68 (≠ W64), M73 (≠ A69), S83 (≠ G80), L87 (≠ F84), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), T139 (= T136), P141 (≠ A138), G142 (≠ D139), K227 (≠ N223), F237 (≠ Y237)
binding crotonyl coenzyme a: K26 (= K22), A27 (= A23), L28 (vs. gap), A30 (= A25), K62 (= K58), I70 (≠ L66), F109 (≠ V106)

5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
32% identity, 99% coverage: 3:260/260 of query aligns to 4:259/259 of 5zaiC

query
sites
5zaiC

D

E

V

T

I

I

R

E

T

T

R

K

E

E

G

G

G

N

I

L

L

F

E

W

V

I

T

T

L

L

D

N

R

R

P

P

-

D

K
|
K

A
x
L

N

N

A

A

I

L

D

N

L

A

T

K

T

L

S

L

R

E

L

E

M

L

G

D

E

R

T

A

F

V

K

S

K

Q

F

A

R

E

D

S

D

D

T

P

E

E

L

I

R

R

V

V

A

I

I

I

V

I

Q

T

T

G

E

K

G

G

D

-

K

K

F

A

F

F

C

C

A
|
A

G
|
G

W
x
A

D
|
D

L
x
I

K

T

A

Q

A
x
F

A

N

G

Q

G

L

D

T

A

P

V

A

D

E

G

A

-

W

D

K

Y

F

G
x
S

V

K

G

K

G

G

F
x
R

G

E

G

I

L

M

Q

D

E

K

L

I

I

E

D

A

L

L

N

S

K

K

P

P

V

T

I

I

A

A

A

M

V

I

N

N

G

G

M

Y

A

A

V

L

G

G

G
|
G

G

G

F

L

E
|
E

L

L

A

A

L

L

S

A

C

C

D

D

L

I

I

R

Y

I

A

A

S

A

D

E

H

E

S

A

S

Q

F

L

A

G

L

L

P
|
P

E
|
E

I

I

R

N

A

L

G

G

T
x
I

L

Y

A
x
P

D
x
G

-

Y

A

G

T

T

V

Q

K

R

L

L

P

T

K

R

R

V

I

I

P

G

Y

K

H

G

V

R

A

A

M

L

D

E

L

M

T

T

G

G

R

D

W
x
R

M

I

D

P

V

G

T

K

E

D

A

A

H

E

R

K

W

Y

G

G

L

L

V

V

N

N

E

R

V

V

L

V

P

P

K

L

D

A

K

N

L

L

M

E

E

Q

R

E

V

T

W

R

E

K

I

L

A

A

R

E

M

K

L

I

E

A

S

K

G

K

P

S

P

P

L

I

V

S

F

L

A

A

A

L

I

I

K

K

E

E

V

V

A

V

R

N

E

R

A

G

E

L

S

D

M

S

G

P

F

L

-

L

-

S

-

G

-

L

-
x
A

Q

L

E

E

A

S

M

V

N

G

W

W

I

-

T

-

K

-

R

-

K

-

F

-

R

-

T

-

V

-

D

G

T

V

L

V

Y
x
F

A

S

S

T

E

E

D

D

G

K

Q

K

E

E

G

G

F

V

K

S

A

A

F
|
F

A

L

E

E

K
|
K

R

R

E

E

P

P

V

T

W

F

K

K

G

G

K

K

active site: A65 (≠ W64), F70 (≠ A69), S82 (≠ G80), R86 (≠ F84), G110 (= G108), E113 (= E111), P132 (= P130), E133 (= E131), I138 (≠ T136), P140 (≠ A138), G141 (≠ D139), A226 (vs. gap), F236 (≠ Y237)
binding coenzyme a: K24 (= K22), L25 (≠ A23), A63 (= A62), G64 (= G63), A65 (≠ W64), D66 (= D65), I67 (≠ L66), P132 (= P130), R166 (≠ W163), F248 (= F249), K251 (= K252)

1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
34% identity, 93% coverage: 16:258/260 of query aligns to 20:256/258 of 1mj3A

query
sites
1mj3A

V

I

T

Q

L

L

D

N

R

R

P

P

K
|
K

A
|
A

-
x
L

N

N

A
|
A

I

L

D

C

L

N

T

G

T

L

S

I

R

E

L

E

M

L

G

N

E

Q

T

A

F

L

K

E

K

T

F

F

R

E

D

E

D

D

T

P

E

A

L

V

R

G

V

-

A

A

I

I

V

V

Q

L

T

T

E

G

G

G

D

E

K

K

F

A

F

F

C

A

A
|
A

G
|
G

W
x
A

D
|
D

L
x
I

K

K

A

E

A
x
M

A

Q

G

N

G

R

D

T

A

F

V

Q

D

D

G

C

D

Y

Y
x
S

G

G

V
x
L

G

S

G

H

F

W

G

-

L

-

Q

D

E

H

L

I

I

T

D

R

L

I

N

K

K

K

P

P

V

V

I

I

A

A

V

V

N

N

G

G

M

Y

A

A

V

L

G

G

G
|
G

G

G

F

C

E
|
E

L

L

A

A

L

M

S

M

C

C

D

D

L

I

I

I

Y

Y

A

A

S

G

D

E

H

K

S

A

S

Q

F

F

A

G

L

Q

P
|
P

E
|
E

I

I

R

L

A
x
L

G

G

T
|
T

L

I

A
x
P

D
x
G

A

A

-

G

A

G

T

T

V

Q

K

R

L

L

P

T

K

R

R

A

I

V

P

G

Y

K

H

S

V

L

A

A

M

M

D

E

L

M

L

V

L

L

T

T

G

G

R

D

W

R

M

I

D

S

V

A

T

Q

E

D

A

A

H

K

R

Q

W

A

G

G

L

L

V

V

N

S

E

K

V

I

L

F

P

P

K

V

D

E

K

T

L

L

M

V

E

E

R

E

V

A

W

I

E

Q

I

C

A

A

R

E

M

K

L

I

E

A

S

N

G

N

P

S

P

K

L

I

V

I

F

V

A

A

A

M

I

A

K

K

E

E

V

S

A

V

R

N

E

A

A

A

E

F

S

E

M

M

G

T

F

L

Q

T

E

E

A

G

M

-

N

N

W
x
K

I

L

T

E

K

K

R

K

K

L

F

F

R

Y

T

S

V

T

D

-

T

-

L

-

Y
x
F

A

A

S

T

E

D

D

D

G

R

Q

R

E

E

G

G

F

M

K

S

A

A

F

F

A

V

E

E

K

K

R

R

E

K

P

A

V

N

W

F

K

K

active site: A68 (≠ W64), M73 (≠ A69), S83 (≠ Y79), L85 (≠ V81), G109 (= G108), E112 (= E111), P131 (= P130), E132 (= E131), T137 (= T136), P139 (≠ A138), G140 (≠ D139), K225 (≠ W224), F235 (≠ Y237)
binding hexanoyl-coenzyme a: K26 (= K22), A27 (= A23), L28 (vs. gap), A30 (= A25), A66 (= A62), G67 (= G63), A68 (≠ W64), D69 (= D65), I70 (≠ L66), G109 (= G108), P131 (= P130), E132 (= E131), L135 (≠ A134), G140 (≠ D139)

3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
35% identity, 99% coverage: 3:260/260 of query aligns to 3:256/256 of 3h81A

query
sites
3h81A

D

E

V

T

I

I

R

L

T

V

R

E

R

R

E

D

G

Q

G

R

I

V

L

G

E

I

V

I

T

T

L

L

D

N

R

R

P

P

K

Q

A

A

-

L

N

N

A

A

I

L

D

N

L

-

T

-

S

S

R

Q

L

V

M

M

G

N

E

E

T

V

F

T

K

S

-

A

-

T

K

E

F

L

R

D

D

D

T

P

E

D

L

I

R

G

V

-

A

A

I

I

V

I

Q

I

T

T

E

G

G

S

D

A

K

K

F

A

F

F

C

A

A

A

G

G

W
x
A

D

D

L

I

K

K

A

E

A
x
M

A

A

G

D

-

L

-

T

-

F

G

A

D

D

A

A

V

F

D
x
T

G

A

D

D

Y

F

G

-

V

-

G

-

F
|
F

G

A

G

T

L

W

Q

G

E

K

L

L

I

A

D

A

L

V

N

R

K

T

P

P

V

T

I

I

A

A

V

V

N

A

G

G

M

Y

A

A

V

L

G

G

G
|
G

G

G

F

C

E
|
E

L

L

A

A

L

M

S

M

C

C

D

D

L

V

I

L

Y

I

A

A

S

A

D

D

H

T

S

A

S

K

F

F

A

G

L

Q

P
|
P

E
|
E

I

I

R

K

A

L

G

G

T
x
V

L

L

A
x
P

D
x
G

-

M

A

G

T

S

V

Q

K

R

L

L

P

T

K

R

R

A

I

I

P

G

Y

K

H

A

V

K

A

A

M

M

D

D

L

L

L

I

L

L

T

T

G

G

R

R

W

T

M

M

D

D

V

A

T

A

E

E

A

A

H

E

R

R

W

S

G

G

L

L

V

V

N

S

E

R

V

V

L

V

P

P

K

A

D

D

K

D

L

L

M

L

E

T

R

E

V

-

W

-

E

-

I

-

A

A

R

R

M

A

L

T

E

A

S

T

G

T

P

I

P

S

L

Q

V

M

F

S

A

A

A

S

I

A

K

A

E

R

V

M

A

A

R

K

E

E

A

A

E

V

S

N

M

R

G

A

F

F

Q

E

E

S

A

S

M

L

N

S

W

E

I

G

T

L

K
x
L

R

Y

K

E

F

R

R

R

T

L

V

F

D

H

T

S

L

A

Y
x
F

A

A

S

T

E

E

D

D

G
x
Q

Q

S

E

E

G

G

F

M

K

A

A

A

F

F

A

I

E

E

K

K

R

R

E

A

P

P

V

Q

W

F

K

T

G

H

K

R

active site: A64 (≠ W64), M69 (≠ A69), T79 (≠ D76), F83 (= F84), G107 (= G108), E110 (= E111), P129 (= P130), E130 (= E131), V135 (≠ T136), P137 (≠ A138), G138 (≠ D139), L223 (≠ K227), F233 (≠ Y237)
binding calcium ion: F233 (≠ Y237), Q238 (≠ G242)

3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
35% identity, 98% coverage: 3:257/260 of query aligns to 4:254/255 of 3q0jC

query
sites
3q0jC

D

E

V

T

I

I

R

L

T

V

R

E

R

R

E

D

G

Q

G

R

I

V

L

G

E

I

V

I

T

T

L

L

D

N

R

R

P

P

K
x
Q

A
|
A

-
x
L

N

N

A
|
A

I

L

D

N

L

-

T

-

S

S

R

Q

L

V

M

M

G

N

E

E

T

V

F

T

K

S

-

A

-

T

K

E

F

L

R

D

D

D

T

P

E

D

L

I

R

G

V

-

A

A

I

I

V

I

Q

I

T

T

E

G

G

S

D

A

K

K

F

A

F

F

C

A

A
|
A

G
|
G

W
x
A

D
|
D

L
x
I

K
|
K

A

E

A
x
M

A

A

G

D

-

L

-

T

-

F

G

A

D

D

A

A

V

F

D
x
T

G

A

D

D

Y

F

G

-

V

-

G

-

F
|
F

G

A

G

T

L

W

Q

G

E

K

L

L

I

A

D

A

L

V

N

R

K

T

P

P

V

T

I

I

A

A

V

V

N

A

G

G

M

Y

A

A

V

L

G
|
G

G

G

F

C

E
|
E

L

L

A

A

L

M

S

M

C

C

D

D

L

V

I

L

Y

I

A

A

S

A

D

D

H

T

S

A

S

K

F

F

A

G

L

Q

P
|
P

E
|
E

I

I

R

K

A

L

G

G

T
x
V

L

L

A
x
P

D
x
G

-
x
M

A

G

T

S

V

Q

K

R

L

L

P

T

K

R

R

A

I

I

P

G

Y

K

H

A

V

K

A

A

M

M

D

D

L

L

L

I

L

L

T

T

G

G

R

R

W

T

M

M

D

D

V

A

T

A

E

E

A

A

H

E

R

R

W

S

G

G

L

L

V

V

N

S

E

R

V

V

L

V

P

P

K

A

D

D

K

D

L

L

M

L

E

T

R

E

V

-

W

-

E

-

I

-

A

A

R

R

M

A

L

T

E

A

S

T

G

T

P

I

P

S

L

Q

V

M

F

S

A

A

A

S

I

A

K

A

E

R

V

M

A

A

R

K

E

E

A

A

E

V

S

N

M

R

G

A

F

F

Q

E

E

S

A

S

M

L

N

S

W

E

I

G

T

L

K
x
L

R

Y

K

E

F

R

R

R

T

L

V

F

D

H

T

S

L

A

Y
x
F

A

A

S

T

E

E

D

D

G

Q

Q

S

E

E

G

G

F

M

K

A

A

A

F

F

A

I

E

E

K

K

R

R

E

A

P

P

V

Q

W

F

active site: A65 (≠ W64), M70 (≠ A69), T80 (≠ D76), F84 (= F84), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), V136 (≠ T136), P138 (≠ A138), G139 (≠ D139), L224 (≠ K227), F234 (≠ Y237)
binding acetoacetyl-coenzyme a: Q23 (≠ K22), A24 (= A23), L25 (vs. gap), A27 (= A25), A63 (= A62), G64 (= G63), A65 (≠ W64), D66 (= D65), I67 (≠ L66), K68 (= K67), M70 (≠ A69), F84 (= F84), G107 (= G107), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), P138 (≠ A138), G139 (≠ D139), M140 (vs. gap)

3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 98% coverage: 3:257/260 of query aligns to 4:254/255 of 3q0gC

query
sites
3q0gC

D

E

V

T

I

I

R

L

T

V

R

E

R

R

E

D

G

Q

G

R

I

V

L

G

E

I

V

I

T

T

L

L

D

N

R

R

P

P

K

Q

A

A

-
x
L

N

N

A

A

I

L

D

N

L

-

T

-

S

S

R

Q

L

V

M

M

G

N

E

E

T

V

F

T

K

S

-

A

-

T

K

E

F

L

R

D

D

D

T

P

E

D

L

I

R

G

V

-

A

A

I

I

V

I

Q

I

T

T

E

G

G

S

D

A

K

K

F

A

F

F

C

A

A
|
A

G

G

W
x
A

D

D

L
x
I

K
|
K

A

E

A
x
M

A

A

G

D

-

L

-

T

-

F

G

A

D

D

A

A

V

F

D
x
T

G

A

D

D

Y

F

G

-

V

-

G

-

F
|
F

G

A

G

T

L

W

Q

G

E

K

L

L

I

A

D

A

L

V

N

R

K

T

P

P

V

T

I

I

A

A

V

V

N

A

G

G

M
x
Y

A

A

V

L

G

G

G
|
G

G

G

F

C

E
|
E

L

L

A

A

L

M

S

M

C

C

D

D

L

V

I

L

Y

I

A

A

S

A

D

D

H

T

S

A

S

K

F

F

A

G

L

Q

P
|
P

E
|
E

I

I

R

K

A
x
L

G

G

T
x
V

L

L

A
x
P

D
x
G

-

M

A

G

T

S

V

Q

K

R

L

L

P

T

K

R

R

A

I

I

P

G

Y

K

H

A

V

K

A

A

M

M

D

D

L

L

L

I

L

L

T

T

G

G

R

R

W

T

M

M

D

D

V

A

T

A

E

E

A

A

H

E

R

R

W

S

G

G

L

L

V

V

N

S

E

R

V

V

L

V

P

P

K

A

D

D

K

D

L

L

M

L

E

T

R

E

V

-

W

-

E

-

I

-

A

A

R

R

M

A

L

T

E

A

S

T

G

T

P

I

P

S

L

Q

V

M

F

S

A

A

A

S

I

A

K

A

E

R

V

M

A

A

R

K

E

E

A

A

E

V

S

N

M

R

G

A

F

F

Q

E

E

S

A

S

M

L

N

S

W

E

I

G

T

L

K
x
L

R

Y

K

E

F

R

R

R

T

L

V

F

D

H

T

S

L

A

Y
x
F

A

A

S

T

E

E

D

D

G

Q

Q

S

E

E

G

G

F

M

K

A

A

A

F

F

A

I

E

E

K

K

R

R

E

A

P

P

V

Q

W

F

active site: A65 (≠ W64), M70 (≠ A69), T80 (≠ D76), F84 (= F84), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), V136 (≠ T136), P138 (≠ A138), G139 (≠ D139), L224 (≠ K227), F234 (≠ Y237)
binding coenzyme a: L25 (vs. gap), A63 (= A62), I67 (≠ L66), K68 (= K67), Y104 (≠ M104), P130 (= P130), E131 (= E131), L134 (≠ A134)

1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
34% identity, 93% coverage: 16:258/260 of query aligns to 20:258/260 of 1dubA

query
sites
1dubA

V

I

T

Q

L

L

D

N

R

R

P

P

K
|
K

A
|
A

-
x
L

N

N

A
|
A

I

L

D

C

L

N

T

G

T

L

S

I

R

E

L

E

M

L

G

N

E

Q

T

A

F

L

K

E

K

T

F

F

R

E

D

E

D

D

T

P

E

A

L

V

R

G

V

-

A

A

I

I

V

V

Q

L

T

T

E

G

G

G

D

E

K

K

F

A

F

F

C

A

A
|
A

G

G

W
x
A

D
|
D

L
x
I

K

K

A

E

A
x
M

A

Q

G

N

-

R

-

T

-

F

G

Q

D

D

A

C

V

Y

D
x
S

G

G

D

K

Y

F

G

-

V

-

G

-

F
x
L

G

S

G

H

L

W

Q

D

E

H

L

I

I

T

D

R

L

I

N

K

K

K

P

P

V

V

I

I

A

A

V

V

N

N

G

G

M
x
Y

A

A

V

L

G
|
G

G

G

F

C

E
|
E

L

L

A

A

L

M

S

M

C

C

D

D

L

I

I

I

Y

Y

A

A

S

G

D

E

H

K

S

A

S

Q

F

F

A

G

L

Q

P
|
P

E
|
E

I

I

R

L

A
x
L

G

G

T
|
T

L

I

A
x
P

D
x
G

A

A

-

G

A

G

T

T

V

Q

K

R

L

L

P

T

K

R

R

A

I

V

P

G

Y

K

H

S

V

L

A

A

M

M

D

E

L

M

L

V

L

L

T

T

G

G

R

D

W

R

M

I

D

S

V

A

T

Q

E

D

A

A

H

K

R

Q

W

A

G

G

L

L

V

V

N

S

E

K

V

I

L

F

P

P

K

V

D

E

K

T

L

L

M

V

E

E

R

E

V

A

W

I

E

Q

I

C

A

A

R

E

M

K

L

I

E

A

S

N

G

N

P

S

P

K

L

I

V

I

F

V

A

A

A

M

I

A

K

K

E

E

V

S

A

V

R

N

E

A

A

A

E

F

S

E

M

M

G

T

F

L

Q

T

E

E

A

G

M

-

N

N

W
x
K

I

L

T

E

K

K

R

K

K

L

F
|
F

R

Y

T

S

V

T

D

-

T

-

L

-

Y
x
F

A

A

S

T

E

D

D

D

G

R

Q

R

E

E

G

G

F

M

K

S

A

A

F
|
F

A

V

E

E

K

K

R

R

E

K

P

A

V

N

W

F

K

K

active site: A68 (≠ W64), M73 (≠ A69), S83 (≠ D76), L87 (≠ F84), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), T139 (= T136), P141 (≠ A138), G142 (≠ D139), K227 (≠ W224), F237 (≠ Y237)
binding acetoacetyl-coenzyme a: K26 (= K22), A27 (= A23), L28 (vs. gap), A30 (= A25), A66 (= A62), A68 (≠ W64), D69 (= D65), I70 (≠ L66), Y107 (≠ M104), G110 (= G107), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), L137 (≠ A134), G142 (≠ D139), F233 (= F230), F249 (= F249)

1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
34% identity, 93% coverage: 16:258/260 of query aligns to 18:256/258 of 1ey3A

query
sites
1ey3A

V

I

T

Q

L

L

D

N

R

R

P

P

K
|
K

A

A

-
x
L

N

N

A
|
A

I

L

D

C

L

N

T

G

T

L

S

I

R

E

L

E

M

L

G

N

E

Q

T

A

F

L

K

E

K

T

F

F

R

E

D

E

D

D

T

P

E

A

L

V

R

G

V

-

A

A

I

I

V

V

Q

L

T

T

E

G

G

G

D

E

K

K

F

A

F

F

C

A

A
|
A

G
|
G

W
x
A

D
|
D

L
x
I

K

K

A

E

A
x
M

A

Q

G

N

-

R

-

T

-

F

G

Q

D

D

A

C

V

Y

D
x
S

G

G

D

K

Y

F

G

-

V

-

G

-

F
x
L

G

S

G

H

L
x
W

Q

D

E

H

L

I

I

T

D

R

L

I

N

K

K

K

P

P

V

V

I

I

A

A

V

V

N

N

G

G

M

Y

A

A

V

L

G

G

G
|
G

G

G

F

C

E
|
E

L

L

A

A

L

M

S

M

C

C

D

D

L

I

I

I

Y

Y

A

A

S

G

D

E

H

K

S

A

S

Q

F

F

A

G

L

Q

P
|
P

E
|
E

I

I

R

L

A
x
L

G

G

T
|
T

L

I

A
x
P

D
x
G

A

A

-

G

A

G

T

T

V

Q

K

R

L

L

P

T

K

R

R

A

I

V

P

G

Y

K

H

S

V

L

A

A

M

M

D

E

L

M

L

V

L

L

T

T

G

G

R

D

W

R

M

I

D

S

V

A

T

Q

E

D

A

A

H

K

R

Q

W

A

G

G

L

L

V

V

N

S

E

K

V

I

L

F

P

P

K

V

D

E

K

T

L

L

M

V

E

E

R

E

V

A

W

I

E

Q

I

C

A

A

R

E

M

K

L

I

E

A

S

N

G

N

P

S

P

K

L

I

V

I

F

V

A

A

A

M

I

A

K

K

E

E

V

S

A

V

R

N

E

A

A

A

E

F

S

E

M

M

G

T

F

L

Q

T

E

E

A

G

M

-

N

N

W
x
K

I

L

T

E

K

K

R

K

K

L

F

F

R

Y

T

S

V

T

D

-

T

-

L

-

Y
x
F

A

A

S

T

E

D

D

D

G

R

Q

R

E

E

G

G

F

M

K

S

A

A

F

F

A

V

E

E

K

K

R

R

E

K

P

A

V

N

W

F

K

K

active site: A66 (≠ W64), M71 (≠ A69), S81 (≠ D76), L85 (≠ F84), G109 (= G108), E112 (= E111), P131 (= P130), E132 (= E131), T137 (= T136), P139 (≠ A138), G140 (≠ D139), K225 (≠ W224), F235 (≠ Y237)
binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K22), L26 (vs. gap), A28 (= A25), A64 (= A62), G65 (= G63), A66 (≠ W64), D67 (= D65), I68 (≠ L66), L85 (≠ F84), W88 (≠ L87), G109 (= G108), P131 (= P130), L135 (≠ A134), G140 (≠ D139)

P14604 Enoyl-CoA hydratase, mitochondrial; mECH; mECH1; Enoyl-CoA hydratase 1; ECHS1; Short-chain enoyl-CoA hydratase; SCEH; EC 4.2.1.17; EC 5.3.3.8 from Rattus norvegicus (Rat) (see 3 papers)
34% identity, 93% coverage: 16:258/260 of query aligns to 50:288/290 of P14604

query
sites
P14604

V

I

T

Q

L

L

D

N

R

R

P

P

K

K

A

A

-

L

N

N

A

A

I

L

D

C

L

N

T

G

T

L

S

I

R

E

L

E

M

L

G

N

E

Q

T

A

F

L

K

E

K

T

F

F

R

E

D

E

D

D

T

P

E

A

L

V

R

G

V

-

A

A

I

I

V

V

Q

L

T

T

E

G

G

G

D

E

K

K

F

A

F

F

C

A

A

A

G

G

W

A

D

D

L

I

K

K

A

E

A

M

A

Q

G

N

-

R

-

T

-

F

G

Q

D

D

A

C

V

Y

D

S

G

G

D

K

Y

F

G

-

V

-

G

-

F

L

G

S

G

H

L

W

Q

D

E

H

L

I

I

T

D

R

L

I

N

K

K

K

P

P

V

V

I

I

A

A

V

V

N

N

G

G

M

Y

A

A

V

L

G

G

F

C

E
|
E

L

L

A

A

L

M

S

M

C

C

D

D

L

I

I

I

Y

Y

A

A

S

G

D

E

H

K

S

A

S

Q

F

F

A

G

L

Q

P

P

E
|
E

I

I

R

L

A

L

G

G

T

T

L

I

A

P

D

G

A

A

-

G

A

G

T

T

V

Q

K

R

L

L

P

T

K

R

R

A

I

V

P

G

Y

K

H

S

V

L

A

A

M

M

D

E

L

M

L

V

L

L

T

T

G

G

R

D

W

R

M

I

D

S

V

A

T

Q

E

D

A

A

H

K

R

Q

W

A

G

G

L

L

V

V

N

S

E

K

V

I

L

F

P

P

K

V

D

E

K

T

L

L

M

V

E

E

R

E

V

A

W

I

E

Q

I

C

A

A

R

E

M

K

L

I

E

A

S

N

G

N

P

S

P

K

L

I

V

I

F

V

A

A

A

M

I

A

K

K

E

E

V

S

A

V

R

N

E

A

A

A

E

F

S

E

M

M

G

T

F

L

Q

T

E

E

A

G

M

-

N

N

W

K

I

L

T

E

K

K

R

K

K

L

F

F

R

Y

T

S

V

T

D

-

T

-

L

-

Y

F

A

A

S

T

E

D

D

D

G

R

Q

R

E

E

G

G

F

M

K

S

A

A

F

F

A

V

E

E

K

K

R

R

E

K

P

A

V

N

W

F

K

K

E144 (= E111) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
E164 (= E131) mutation to D: Reduces activity 1250-fold.; mutation to Q: Reduces activity 330000-fold.

Sites not aligning to the query:

1:29 modified: transit peptide, Mitochondrion

Q4WF54 Mevalonyl-coenzyme A hydratase sidH; Siderophore biosynthesis protein H; EC 4.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
34% identity, 95% coverage: 13:258/260 of query aligns to 21:266/270 of Q4WF54

query
sites
Q4WF54

I

I

L

L

E

L

V

L

T

T

L

L

D

N

R

R

P

P

-

E

K

K

A

R

N

N

A

C

I

I

D

S

L

L

T

A

T

T

S

S

R

A

L

E

M

I

G

Q

E

R

T

L

F

W

K

T

K

W

F

F

R

D

D

T

D

Q

T

P

E

A

L

L

R

Y

V

V

A

A

I

I

V

I

Q

T

T

G

E

T

G

G

D

E

K

S

F

F

F

-

C

C

A

A

G

G

W

A

D

D

L

L

K

K

A

E

A

W

A

N

G

D

G

L

D

N

A

A

-

R

-

G

V

I

D

T

G

N

D

E

Y

M

G

T

V

A

G

P

G

G

F

L

G

A

G

G

L

L

Q

P

E

R

L

R

I

R

D

G

L

-

N

S

K

K

P

P

V

I

I

I

A

A

V

V

N

N

G

G

M

Y

A

C

V

L

G

G

F

F

E

E

L

M

A

V

L

A

S

N

C

C

D

D

L

I

I

V

Y

V

A

A

S

S

D

E

H

N

S

A

S

T

F

F

A

G

L

L

P

P

E

E

I

V

R

Q

A

R

G

G

T

I

L

A

A

A

D

V

A

A

A

G

T

S

V

L

-

P

K

R

L

L

P

V

K

R

R

V

I

L

P

G

Y

K

H

Q

V

R

A

A

M

A

D

E

L

I

L

A

L

L

T

S

G

G

R

L

W

S

M

F

D

S

V

A

T

S

E

Q

A

L

H

E

R

R

W

W

G

G

L

L

V

V

N

N

E

R

V

V

L

V

P

E

K

H

D

D

K

Q

L

L

M

L

E

A

R

T

V

A

W

V

E

E

I

I

A

A

R

T

M

A

L

I

E

S

S

R

G

N

P

S

P

P

L

-

V

-

F

-

A

-

I

-

K

D

E

S

V

V

A

R

R

V

E

T

A

M

E

E

S

G

M

L

G

H

F

Y

Q

G

E

W

A

E

M

M

N

A

W

S

I

V

T

E

K

E

R

A

K

S

F

S

R

A

T

L

V

V

D

D

T

Q

L

W

Y

Y

A

A

S

K

-

L

-

M

-

A

-

G

E

E

D

N

G

F

Q

H

E

E

G

G

F

V

K

R

A

A

F

F

A

V

E

E

K

K

R

R

E

K

P

P

V

Q

W

W

K

R

Sites not aligning to the query:

268:270 PTS1-type peroxisomal targeting signal

2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
34% identity, 93% coverage: 16:258/260 of query aligns to 19:252/254 of 2dubA

query
sites
2dubA

V

I

T

Q

L

L

D

N

R

R

P

P

K
|
K

A
|
A

-
x
L

N

N

A
|
A

I

L

D

C

L

N

T

G

T

L

S

I

R

E

L

E

M

L

G

N

E

Q

T

A

F

L

K

E

K

T

F

F

R

E

D

E

D

D

T

P

E

A

L

V

R

G

V

-

A

A

I

I

V

V

Q

L

T

T

E

G

G

G

D

E

K

K

F

A

F

F

C

A

A
|
A

G

G

W
x
A

D
|
D

L
x
I

K
|
K

A

E

A
x
M

A

Q

G

N

G

R

D

T

A

F

V

Q

D

D

G

C

D

-

Y

-

G

-

V

-

G

-

F

Y

G
x
S

G

H

L

W

Q

D

E

H

L

I

I

T

D

R

L

I

N

K

K

K

P

P

V

V

I

I

A

A

V

V

N

N

G

G

M

Y

A

A

V

L

G

G

G
|
G

G

G

F

C

E
|
E

L

L

A

A

L

M

S

M

C

C

D

D

L

I

I

I

Y

Y

A

A

S

G

D

E

H

K

S

A

S

Q

F

F

A

G

L

Q

P
|
P

E
|
E

I

I

R

L

A

L

G

G

T
|
T

L

I

A
x
P

D
x
G

A
|
A

-

G

A

G

T

T

V

Q

K

R

L

L

P

T

K

R

R

A

I

V

P

G

Y

K

H

S

V

L

A

A

M

M

D

E

L

M

L

V

L

L

T

T

G

G

R

D

W

R

M

I

D

S

V

A

T

Q

E

D

A

A

H

K

R

Q

W

A

G

G

L

L

V

V

N

S

E

K

V

I

L

F

P

P

K

V

D

E

K

T

L

L

M

V

E

E

R

E

V

A

W

I

E

Q

I

C

A

A

R

E

M

K

L

I

E

A

S

N

G

N

P

S

P

K

L

I

V

I

F

V

A

A

A

M

I

A

K

K

E

E

V

S

A

V

R

N

E

A

A

A

E

F

S

E

M

M

G

T

F

L

Q

T

E

E

A

G

M

-

N

N

W
x
K

I

L

T

E

K

K

R

K

K

L

F

F

R

Y

T

S

V

T

D

-

T

-

L

-

Y
x
F

A

A

S

T

E

D

D

D

G

R

Q

R

E

E

G

G

F

M

K

S

A

A

F

F

A

V

E

E

K

K

R

R

E

K

P

A

V

N

W

F

K

K

active site: A67 (≠ W64), M72 (≠ A69), S82 (≠ G85), G105 (= G108), E108 (= E111), P127 (= P130), E128 (= E131), T133 (= T136), P135 (≠ A138), G136 (≠ D139), K221 (≠ W224), F231 (≠ Y237)
binding octanoyl-coenzyme a: K25 (= K22), A26 (= A23), L27 (vs. gap), A29 (= A25), A65 (= A62), A67 (≠ W64), D68 (= D65), I69 (≠ L66), K70 (= K67), G105 (= G108), E108 (= E111), P127 (= P130), E128 (= E131), G136 (≠ D139), A137 (= A140)

3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 98% coverage: 3:257/260 of query aligns to 3:249/250 of 3q0gD

query
sites
3q0gD

D

E

V

T

I

I

R

L

T

V

R

E

R

R

E

D

G

Q

G

R

I

V

L

G

E

I

V

I

T

T

L

L

D

N

R

R

P

P

K

Q

A

A

-

L

N

N

A

A

I

L

D

N

L

-

T

-

S

S

R

Q

L

V

M

M

G

N

E

E

T

V

F

T

K

S

-

A

-

T

K

E

F

L

R

D

D

D

T

P

E

D

L

I

R

G

V

-

A

A

I

I

V

I

Q

I

T

T

E

G

G

S

D

A

K

K

F

A

F

F

C

A

A

A

G

G

W
x
A

D

D

L

I

K

K

A

E

A
x
M

A

F

G

A

G

-

D

D

A

A

V

F

D
x
T

G

A

D

D

Y

F

G

-

V

-

G

-

F
|
F

G

A

G

T

L

W

Q

G

E

K

L

L

I

A

D

A

L

V

N

R

K

T

P

P

V

T

I

I

A

A

V

V

N

A

G

G

M

Y

A

A

V

L

G

G

G
|
G

G

G

F

C

E
|
E

L

L

A

A

L

M

S

M

C

C

D

D

L

V

I

L

Y

I

A

A

S

A

D

D

H

T

S

A

S

K

F

F

A

G

L

Q

P
|
P

E
|
E

I

I

R

K

A

L

G

G

T
x
V

L

L

A
x
P

D
x
G

-

M

A

G

T

S

V

Q

K

R

L

L

P

T

K

R

R

A

I

I

P

G

Y

K

H

A

V

K

A

A

M

M

D

D

L

L

L

I

L

L

T

T

G

G

R

R

W

T

M

M

D

D

V

A

T

A

E

E

A

A

H

E

R

R

W

S

G

G

L

L

V

V

N

S

E

R

V

V

L

V

P

P

K

A

D

D

K

D

L

L

M

L

E

T

R

E

V

-

W

-

E

-

I

-

A

A

R

R

M

A

L

T

E

A

S

T

G

T

P

I

P

S

L

Q

V

M

F

S

A

A

A

S

I

A

K

A

E

R

V

M

A

A

R

K

E

E

A

A

E

V

S

N

M

R

G

A

F

F

Q

E

E

S

A

S

M

L

N

S

W

E

I

G

T

L

K
x
L

R

Y

K

E

F

R

R

R

T

L

V
x
F

D

H

T

S

L

A

Y
x
F

A

A

S

T

E

E

D

D

G

Q

Q

S

E

E

G

G

F

M

K

A

A

A

F
|
F

A

I

E

E

K

K

R

R

E

A

P

P

V

Q

W

F

active site: A64 (≠ W64), M69 (≠ A69), T75 (≠ D76), F79 (= F84), G103 (= G108), E106 (= E111), P125 (= P130), E126 (= E131), V131 (≠ T136), P133 (≠ A138), G134 (≠ D139), L219 (≠ K227), F229 (≠ Y237)
binding Butyryl Coenzyme A: F225 (≠ V233), F241 (= F249)

5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
32% identity, 91% coverage: 24:260/260 of query aligns to 27:261/261 of 5jbxB

query
sites
5jbxB

N

N

A
|
A

I

I

D

S

L

R

T

A

T

M

S

L

R

K

L

E

M

L

G

G

E

E

T

L

F

V

K

T

K

R

F

V

R

S

D

S

T

R

E

D

L

V

R

R

V

A

A

V

I

V

V

I

Q

T

T

G

E

A

G

G

D

D

K

K

F

A

F

F

C

C

A
|
A

G

G

W
x
A

D
|
D

L
|
L

K
|
K

A

E

A
x
R

A

A

G

T

G

M

D

A

A

E

V

D

D

E

G

V

D

R

Y

A

G

F

V
x
L

G

D

G

G

F

L

G
x
R

G

R

L

T

Q

F

E

R

L

A

I

I

D

E

L

K

N

S

K

D

P

C

V

V

-

F

I

I

A

A

V

I

N

N

G

G

M

A

A

A

V
x
L

G
|
G

G

G

F

T

E
|
E

L

L

A

A

L

L

S

A

C

C

D

D

L

L

I

R

Y

V

A

A

S

A

D

P

H

A

S

A

S

E

F

L

A

G

L

L

P
x
T

E
|
E

I

V

R

K

A
x
L

G

G

T
x
I

L

I

-
x
P

A
x
G

D

G

A

G

T

T

V

Q

K

R

L

L

P

A

K

R

R

L

I

V

P

G

Y

P

H

G

V

R

A

A

M

K

D

D

L

L

L

I

L

L

T

T

G

A

R

R

W
x
R

M

I

D

N

V

A

T

A

E

E

A

A

H

F

R

S

W

V

G

G

L

L

V

A

N

N

E

R

V

L

L

A

P

P

K

E

D

G

K

H

L

L

M

L

E

A

R

V

V

A

W

Y

E

G

I

L

A

A

R

E

M

S

L

V

E

V

S

E

G

N

P

A

P

P

L

I

V

A

F

V

A

A

A

T

I

A

K

K

E

H

V

A

A

I

R

D

E

E

A

G

E

T

S

G

M

L

G

E

F

L

Q

D

E

D

A

A

M

L

N
x
A

W

L

I

-

T

-

K

-

R

-

K

E

F

L

R

R

T

K

V

Y

D

E

T

E

L

I

Y
x
L

A

K

S

T

E

E

D

D

G

R

Q

L

E

E

G

G

F

L

K

R

A

A

F

F

A

A

E

E

K

K

R

R

E

A

P

P

V

V

W

Y

K

K

G

G

K

R

active site: A67 (≠ W64), R72 (≠ A69), L84 (≠ V81), R88 (≠ G85), G112 (= G108), E115 (= E111), T134 (≠ P130), E135 (= E131), I140 (≠ T136), P142 (vs. gap), G143 (≠ A138), A228 (≠ N223), L238 (≠ Y237)
binding coenzyme a: A28 (= A25), A65 (= A62), D68 (= D65), L69 (= L66), K70 (= K67), L110 (≠ V106), G111 (= G107), T134 (≠ P130), E135 (= E131), L138 (≠ A134), R168 (≠ W163)

Sites not aligning to the query:

binding coenzyme a: 24, 25, 26

6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 99% coverage: 4:260/260 of query aligns to 4:257/257 of 6slbAAA

query
sites
6slbAAA

V

M

I

I

R

L

T

K

R

E

R

R

E

Q

G

D

G

G

I

V

L

L

E

V

V

L

T

T

L

L

D

N

R

R

P

P

-

E

K

K

A

L

N

N

A

A

I

I

D

T

L

G

T

E

T

L

S

L

R

D

L

A

M

L

G

Y

E

A

T

A

F

L

K

K

K

E

F

G

R

E

D

E

D

D

T

R

E

E

L

V

R

R

V

-

A

A

I

L

V

L

Q

L

T

T

E

G

G

A

D

G

K
x
R

F

A

F

F

C

S

A
|
A

G

G

W
x
Q

D
|
D

L
|
L

K

-

A

T

A

E

A
x
F

G

G

G

D

D

R

A

K

V

P

D

D

G
x
Y

D

E

Y

A

G

H

V
x
L

G

R

F

Y

G
x
N

G

R

L

V

Q

V

E

E

-

A

L

L

I

S

D

G

L

L

N

E

K

K

P

P

V

L

I

V

A

V

A

A

V

V

N

N

G

G

M

V

A

A

V

A

G

G

G
x
A

G

G

F

M

E
x
S

L

L

A

A

L

L

S

W

C

G

D

D

L

L

I

R

Y

L

A

A

S

A

D

V

H

G

S

A

S

S

F

F

A

T

L

T

P
x
A

E
x
F

I

V

R

R

A

I

G

G

T
x
L

L

V

A
x
P

D
|
D

A

S

A

G

-

L

T

S

V

F

K

L

L

L

P

P

K

R

R

L

I

V

P

G

Y

L

H

A

V

K

A

A

M

Q

D

E

L

L

T

L

G

S

R

P

W

R

M

L

D

S

V

A

T

E

E

E

A

A

H

L

R

A

W

L

G

G

L

L

V

V

N

H

E

R

V

V

L

V

P

P

K

A

D

E

K

K

L

L

M

M

E

E

R

E

V

A

W

L

E

S

I

L

A

A

R

K

M

E

L

L

E

A

S

Q

G

G

P

P

P

T

L

R

V

A

F

Y

A

A

A

L

I

T

K

K

E

K

V

L

A

L

R

L

E

E

A

T

E

Y

S

R

M

L

G

S

F

L

Q

T

E

E

A

A

M

L

N
x
A

W

L

I

E

T

A

K

V

R

L

K

Q

F

G

R

Q

T

A

V
x
G

D

Q

T

T

L

-

Y

-

A

-

S

-

E

Q

D

D

G

H

Q

E

E

E

G

G

F

V

K

R

A

A

F

F

A

R

E

E

K

K

R

R

E

P

P

P

V

R

W

F

K

Q

G

G

K

R

active site: Q64 (≠ W64), F69 (≠ A70), L80 (≠ V81), N84 (≠ G85), A108 (≠ G108), S111 (≠ E111), A130 (≠ P130), F131 (≠ E131), L136 (≠ T136), P138 (≠ A138), D139 (= D139), A224 (≠ N223), G234 (≠ V233)
binding (~{E})-6-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethylsulfanyl]-6-oxidanylidene-hex-3-enoic acid: R58 (≠ K58), A62 (= A62), Q64 (≠ W64), D65 (= D65), L66 (= L66), Y76 (≠ G77), A108 (≠ G108), F131 (≠ E131), D139 (= D139)

6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
32% identity, 99% coverage: 4:260/260 of query aligns to 1:245/245 of 6slaAAA

query
sites
6slaAAA

V

M

I

I

R

L

T

K

R

E

R

R

E

Q

G

D

G

G

I

V

L

L

E

V

V

L

T

T

L

L

D

N

R

R

P

P

-

E

K

K

A
x
L

N

N

A

A

I

I

D

T

L

G

T

E

T

L

S

L

R

D

L

A

M

L

G

Y

E

A

T

A

F

L

K

K

K

E

F

G

R

E

D

E

D

D

T

R

E

E

L

V

R

R

V

-

A

A

I

L

V

L

Q

L

T

T

E

G

G

A

D

G

K

R

F

A

F

F

C

S

A
|
A

G

G

W
x
Q

D
|
D

L
|
L

K

T

A

E

A

A

A

-

G

-

D

H

A
x
L

V

R

D

R

G
x
Y

D
x
N

Y

R

G

V

V

V

G

E

G

A

F

L

G

S

G

G

L

L

Q

E

E

-

L

-

I

-

D

-

L

-

N

-

K

K

P

P

V

L

I

V

A

V

A

A

V

V

N

N

G

G

M

V

A

A

V
x
A

G
|
G

G
x
A

G

G

F

M

E
x
S

L

L

A

A

L

L

S

W

C

G

D

D

L

L

I

R

Y

L

A

A

S

A

D

V

H

G

S

A

S

S

F

F

A

T

L

T

P
x
A

E
x
F

I

V

R

R

A
x
I

G

G

T
x
L

L

V

A
x
P

D
x
N

A

S

A

G

-

L

T

S

V

F

K

L

L

L

P

P

K

R

R

L

I

V

P

G

Y

L

H

A

V

K

A

A

M

Q

D

E

L

L

T

L

G

S

R

P

W

R

M

L

D

S

V

A

T

E

E

E

A

A

H

L

R

A

W

L

G

G

L

L

V

V

N

H

E

R

V

V

L

V

P

P

K

A

D

E

K

K

L

L

M

M

E

E

R

E

V

A

W

L

E

S

I

L

A

A

R

K

M

E

L

L

E

A

S

Q

G

G

P

P

P

T

L

R

V

A

F

Y

A

A

A

L

I

T

K

K

E

K

V

L

A

L

R

L

E

E

A

T

E

Y

S

R

M

L

G

S

F

L

Q

T

E

E

A

A

M

L

N
x
A

W

L

I

E

T

A

K

V

R

L

K

Q

F

G

R

Q

T

A

V
x
G

D

Q

T

T

L

-

Y

-

A

-

S

-

E

Q

D

D

G

H

Q

E

E

E

G

G

F

V

K

R

A

A

F
|
F

A

R

E

E

K
|
K

R

R

E

P

P

P

V

R

W

F

K

Q

G

G

K

R

active site: Q61 (≠ W64), L68 (≠ A74), N72 (≠ D78), A96 (≠ G108), S99 (≠ E111), A118 (≠ P130), F119 (≠ E131), L124 (≠ T136), P126 (≠ A138), N127 (≠ D139), A212 (≠ N223), G222 (≠ V233)
binding ~{S}-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethyl] 2-(2,5-dihydrooxepin-7-yl)ethanethioate: L21 (≠ A23), A59 (= A62), Q61 (≠ W64), D62 (= D65), L63 (= L66), L68 (≠ A74), Y71 (≠ G77), A94 (≠ V106), G95 (= G107), A96 (≠ G108), F119 (≠ E131), I122 (≠ A134), L124 (≠ T136), N127 (≠ D139), F234 (= F249), K237 (= K252)

A5JTM5 4-chlorobenzoyl coenzyme A dehalogenase; 4-CBA-CoA dehalogenase; 4-CBCoA dehalogenase; 4-chlorobenzoyl-CoA dehalogenase; EC 3.8.1.7 from Pseudomonas sp. (strain CBS-3) (see 7 papers)
28% identity, 90% coverage: 1:233/260 of query aligns to 1:236/269 of A5JTM5

query
sites
A5JTM5

M

M

S

Y

D

E

V

A

I

I

R

G

T

H

R

R

R

V

E

E

G

D

G

G

I

V

L

A

E

E

V

I

T

T

L

I

D

K

R

L

P

P

K

R

A

H

-
x
R

N

N

A

A

I

L

D

S

L

V

T

K

T

A

S

M

R

Q

L
x
E

M

V

G

T

E

D

T

A

F

L

K

N

K

R

F

A

R
x
E

D

E

D
|
D

T
x
D

E

S

L

V

R

G

V

-

A

A

I

V

V

M

Q

I

T

T

E

G

G

A

D

E

K

D

F

A

F

F

C

C

A

A

G
|
G

W
x
F

D
x
Y

L

L

K
x
R

A
x
E

A

I

A

P

G

L

G

D

D

K

A

G

V

V

D

A

G

G

-

V

-

R

-

D

D
x
H

Y
x
F

G

R

V

I

G

G

G

A

F

L

-

W

-
x
W

-
x
H

G

Q

G

M

L

I

Q
x
H

E

K

L

I

I

I

D

R

L

V

N

K

K

R

P

P

V

V

I

L

A

A

V

I

N

N

G

G

M

V

A

A

V
x
A

G
|
G

F

L

E

G

L

I

A

S

L

L

S

A

C

S

D
|
D

L

M

I

A

Y

I

A

C

S

A

D
|
D

H

S

S

A

S

K

F

F

A

V

L

C

P

A

E
x
W

I

H

R

T

A

I

G

G

T

I

L

G

A

N

D
|
D

A

T

A

A

T

T

-

S

V

Y

K

S

L

L

P

A

K

R

R

I

I

V

P

G

Y

M

H

R

V

R

A

A

M

M

D
x
E

L

L

L

M

L

L

T

T

G

N

R

R

W

T

M

L

D

Y

V

P

T

E

E
|
E

A

A

H

K

R

D

W
|
W

G

G

L

L

V

V

N

S

E

R

V

V

L

Y

P

P

K

K

D

D

K

D

L

F

M

R

E

E

R

V

V

A

W

W

E

K

I

V

A

A

R

R

M

E

L

L

E

A

S

A

G

A

P

P

P

-

L

-

V

-

F

-

A

T

A
x
H

I

L

K

Q

E

V

V

M

A

A

R

K

E

E

A
x
R

E

F

S

H

M

A

G

G

F

W

Q

M

E

Q

A

P

M

V

N

E

W

E

I

C

T

T

K

E

R

F

K
x
E

F

I

R

Q

T

N

V

V

R24 (vs. gap) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
E34 (≠ L33) mutation to T: Forms inclusion bodies.
E43 (≠ R42) mutation to A: No effect on catalytic activity.
D45 (= D44) mutation to A: No effect on catalytic activity.
D46 (≠ T45) mutation to A: No effect on catalytic activity.
G63 (= G63) mutation G->A,I,P: Yields insoluble protein.
F64 (≠ W64) mutation to A: 30-fold reduction in catalytic activity, substrate benzoyl group binding is unaffected.; mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to P: Severely reduces catalytic activity. Arylated intermediate does not accumulate.
Y65 (≠ D65) mutation to D: Catalytic activity is almost as efficient as wild type.
R67 (≠ K67) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
E68 (≠ A68) mutation to T: No effect on catalytic activity.
H81 (≠ D78) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
F82 (≠ Y79) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
W89 (vs. gap) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
H90 (vs. gap) active site, Proton acceptor; mutation to Q: Complete loss of catalytic activity (PubMed:8718880, PubMed:9063883). Significantly reduced activity (PubMed:11695894). Substrate binding is not significantly affected. Reduced arylated intermediate formation.
H94 (≠ Q88) mutation to Q: No effect on catalytic activity.
A112 (≠ V106) mutation to G: Yields insoluble protein.; mutation to S: Protein precipitates upon purification.; mutation to V: Catalytic activity is almost as efficient as wild type.
G113 (= G107) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding. Arylated intermediate does not accumulate.; mutation G->N,S: Strongly reduced catalytic activity. Arylated intermediate does not accumulate.; mutation to V: Protein precipitates upon purification.
G114 (= G108) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
G115 (= G109) mutation G->L,N,S,V: Yields insoluble protein.
D123 (= D117) mutation to T: No effect on catalytic activity.
D129 (= D123) mutation to T: No effect on catalytic activity.
W137 (≠ E131) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
D145 (= D139) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
E163 (≠ D156) mutation to T: No effect on catalytic activity.
E175 (= E168) mutation to D: No effect on catalytic activity.
W179 (= W172) mutation to F: No effect on catalytic activity.
H208 (≠ A205) mutation to Q: No effect on catalytic activity.
R216 (≠ A213) mutation R->E,K,L: Yields insoluble protein.
E232 (≠ K229) mutation E->A,N,Q,R: Yields insoluble protein.; mutation to D: Reduced catalytic activity, increased substrate binding.

Sites not aligning to the query:

257 R→K: Retains catalytic activity and substrate CoA binding.; R→L: Significantly reduces catalytic activity and substrate CoA binding.

1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
28% identity, 90% coverage: 1:233/260 of query aligns to 1:236/269 of 1jxzB

query
sites
1jxzB

M

M

S

Y

D

E

V

A

I

I

R

G

T

H

R

R

R

V

E

E

G

D

G

G

I

V

L

A

E

E

V

I

T

T

L

I

D

K

R

L

P

P

K
x
R

A
x
H

-
x
R

N

N

A

A

I

L

D

S

L

V

T

K

T

A

S

M

R

Q

L

E

M

V

G

T

E

D

T

A

F

L

K

N

K

R

F

A

R

E

D

E

D

D

T

D

E

S

L

V

R
x
G

V

-

A

A

I

V

V

M

Q

I

T

T

E

G

G

A

D

E

K

D

F

A

F

F

C
|
C

A
|
A

G

G

W
x
F

D
x
Y

L
|
L

K
x
R

A

E

A

-

G

-

D

-

A

-

V
x
I

D

P

G

L

D

D

Y

K

G

G

V

V

G

A

G

G

F

V

G

R

G

D

-

H

-

F

-

R

-

I

-

A

-
x
A

-

L

-

W

-
x
W

-
x
Q

-

Q

-

M

L

I

Q

H

E

K

L

I

I

I

D

R

L

V

N

K

K

R

P

P

V

V

I

L

A

A

V

I

N

N

G

G

M

V

A

A

V

A

G
|
G

G

G

F

L

E
x
G

L

I

A

S

L

L

S

A

C

S

D

D

L

M

I

A

Y

I

A

C

S

A

D

D

H

S

S

A

S

K

F

F

A

V

L

C

P
x
A

E
x
W

I

H

R

T

A

I

G

G

T
x
I

L

G

A
x
N

D
|
D

A
x
T

A

A

T

T

-

S

V

Y

K

S

L

L

P

A

K

R

R

I

I

V

P

G

Y

M

H

R

V

R

A

A

M

M

D

E

L

L

L

M

L

L

T

T

G

N

R

R

W

T

M

L

D

Y

V

P

T

E

E

E

A

A

H

K

R

D

W

W

G

G

L

L

V

V

N

S

E

R

V

V

L

Y

P

P

K

K

D

D

K

E

L

F

M

R

E

E

R

V

V

A

W

W

E

K

I

V

A

A

R

R

M

E

L
|
L

E
x
A

S

A

G
x
A

P

P

P

-

L

-

V

-

F

-

A
x
T

A

H

I

L

K
x
Q

E

V

V

M

A

A

R

K

E

E

A

R

E

F

S

H

M

A

G

G

F

W

Q

M

E

Q

A

P

M

V

N

E

W

E

I

C

T

T

K
x
E

R

F

K

E

F

I

R

Q

T

N

V

V

active site: C61 (= C61), F64 (≠ W64), I69 (≠ V75), A86 (vs. gap), Q90 (vs. gap), G113 (= G107), G114 (= G108), G117 (≠ E111), A136 (≠ P130), W137 (≠ E131), I142 (≠ T136), N144 (≠ A138), D145 (= D139), E230 (≠ K227)
binding 4-hydroxybenzoyl coenzyme a: R22 (≠ K22), H23 (≠ A23), R24 (vs. gap), A62 (= A62), F64 (≠ W64), Y65 (≠ D65), L66 (= L66), R67 (≠ K67), W89 (vs. gap), G113 (= G107), A136 (≠ P130), W137 (≠ E131), I142 (≠ T136), D145 (= D139), T146 (≠ A140)
binding calcium ion: G49 (≠ R48), L202 (= L195), A203 (≠ E196), A205 (≠ G198), T207 (≠ A204), Q210 (≠ K207)

Sites not aligning to the query:

binding 4-hydroxybenzoyl coenzyme a: 252, 257

3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
32% identity, 88% coverage: 3:232/260 of query aligns to 1:219/224 of 3p85A

query
sites
3p85A

D

E

V

I

I

L

R

L

T

S

R

N

R

T

E

E

G

E

G

R

I

V

L

R

E

T

V

L

T

T

L

L

D

N

R

R

P

P

K

Q

A

A

-

R

N

N

A

A

I

L

D

-

L

-

T

-

T

S

S

A

R

A

L

L

M

R

G

D

E

R

T

F

F

F

K

G

K

A

F

L

R

A

D

D

-

A

-

E

-

T

D
|
D

T

D

E
x
D

L

V

R

D

V

V

A

V

I

I

V

I

Q

-

T

T

E

G

G

A

D

D

K

P

F

V

F

F

C

C

A

A

G

G

W
x
L

D

D

L

L

K

K

A

-

G

-

D

-

A

-

V

-

D

-

G

-

D

-

Y

-

G

-

V

-

G

-

F

-

G

-

L

-

Q

-

E

E

L
|
L

I
x
P

D

D

-

I

-

S

-

P

-

R

-

W

-

P

-

A

L

L

N

T

K

K

P

P

V

V

I

I

A

G

A

A

V

I

N

N

G

G

M

A

A

A

V

V

G

T

G
|
G

G

G

F

L

E
|
E

L

L

A

A

L

L

S

Y

C

C

D

D

L

I

I

L

Y

I

A

A

S

S

D

E

H

N

S

A

S

R

F

F

A

A

L

D

P
x
T

E
x
H

I

A

R

R

A

V

G

G

T
x
L

L

L

A
x
P

D
x
T

-

W

A

G

A

L

T

S

V

V

K

R

L

L

P

P

K

Q

R

K

I

V

P

G

Y

I

H

G

V

L

A

A

M

R

D

R

L

M

L

S

L

L

T

T

G

G

R

D

W

Y

M

L

D

S

V

A

T

A

E

D

A

A

H

L

R

R

W

A

G

G

L

L

V

V

N

T

E

E

V

V

L

V

P

P

K

H

D

D

K

Q

L

L

M

L

E

G

R

A

V

A

W

R

E

A

I

V

A

A

R

A

M

S

L

I

-

V

-

G

-

N

E

Q

S

N

G

A

P

V

P

R

L

A

V

L

F

L

A

T

A

S

I

Y

K

H

E

R

V

I

A

D

R

D

E

A

A

Q

E

T

S

S

M

A

G

G

F

L

-
x
W

Q

Q

E

E

A

A

M

M

N

-

W

-

I

-

T

A

K

A

R

R

K

Q

F

F

R

R

T
|
T

active site: L62 (≠ W64), L67 (= L90), P68 (≠ I91), G92 (= G108), E95 (= E111), T114 (≠ P130), H115 (≠ E131), L120 (≠ T136), P122 (≠ A138), T123 (≠ D139), W208 (vs. gap), T219 (= T232)
binding calcium ion: D43 (= D44), D45 (≠ E46)

1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
28% identity, 90% coverage: 1:233/260 of query aligns to 1:236/269 of 1nzyB

query
sites
1nzyB

M

M

S

Y

D

E

V

A

I

I

R

G

T

H

R

R

R

V

E

E

G

D

G

G

I

V

L

A

E

E

V

I

T

T

L

I

D

K

R

L

P

P

K
x
R

A
x
H

-
x
R

N

N

A

A

I

L

D

S

L

V

T

K

T

A

S

M

R

Q

L

E

M

V

G

T

E

D

T

A

F

L

K

N

K

R

F

A

R

E

D

E

D

D

T

D

E

S

L

V

R
x
G

V

-

A

A

I

V

V

M

Q

I

T

T

E

G

G

A

D
x
E

K

D

F

A

F

F

C
|
C

A
|
A

G

G

W
x
F

D
x
Y

L
|
L

K
x
R

A

E

A

-

G

-

D

-

A

-

V
x
I

D

P

G

L

D

D

Y

K

G

G

V

V

G

A

G

G

-

V

-

R

-

D

-

H

-

F

-

R

-

I

-

A

-
x
A

-

L

-

W

-
x
W

F
x
H

G

Q

G

M

L

I

Q

H

E

K

L

I

I

I

D

R

L

V

N

K

K

R

P

P

V

V

I

L

A

A

V

I

N
|
N

G

G

M

V

A

A

V

A

G
|
G

G

G

F

L

E
x
G

L

I

A

S

L

L

S

A

C

S

D

D

L

M

I

A

Y

I

A

C

S

A

D

D

H

S

S

A

S

K

F

F

A

V

L

C

P
x
A

E
x
W

I

H

R

T

A

I

G

G

T
x
I

L

G

A
x
N

D
|
D

A
x
T

A

A

T

T

-

S

V

Y

K

S

L

L

P

A

K

R

R

I

I

V

P

G

Y

M

H

R

V

R

A

A

M

M

D

E

L

L

L

M

L

L

T

T

G

D

R

R

W

T

M

L

D

Y

V

P

T

E

E

E

A

A

H

K

R

D

W

W

G

G

L

L

V

V

N

S

E

R

V

V

L

Y

P

P

K
|
K

D

D

K

E

L

F

M
x
R

E

E

R

V

V

A

W

W

E

K

I

V

A

A

R

R

M

E

L
|
L

E
x
A

S

A

G
x
A

P

P

P

-

L

-

V

-

F

-

A
x
T

A

H

I

L

K
x
Q

E

V

V

M

A

A

R

K

E

E

A

R

E

F

S

H

M

A

G

G

F

W

Q

M

E

Q

A

P

M

V

N

E

W

E

I

C

T

T

K
x
E

R

F

K

E

F

I

R

Q

T

N

V

V

active site: C61 (= C61), F64 (≠ W64), I69 (≠ V75), A86 (vs. gap), H90 (≠ F84), G114 (= G108), G117 (≠ E111), A136 (≠ P130), W137 (≠ E131), I142 (≠ T136), N144 (≠ A138), D145 (= D139), E230 (≠ K227)
binding 4-hydroxybenzoyl coenzyme a: R22 (≠ K22), H23 (≠ A23), R24 (vs. gap), A62 (= A62), F64 (≠ W64), Y65 (≠ D65), L66 (= L66), R67 (≠ K67), W89 (vs. gap), G113 (= G107), G114 (= G108), A136 (≠ P130), W137 (≠ E131), D145 (= D139), T146 (≠ A140)
binding calcium ion: G49 (≠ R48), L202 (= L195), A203 (≠ E196), A205 (≠ G198), T207 (≠ A204), Q210 (≠ K207)
binding phosphate ion: E57 (≠ D57), N108 (= N102), K188 (= K181), R192 (≠ M185)

Sites not aligning to the query:

binding 4-hydroxybenzoyl coenzyme a: 252, 257

Query Sequence

>WP_106710550.1 NCBI__GCF_003010955.1:WP_106710550.1
MSDVIRTRREGGILEVTLDRPKANAIDLTTSRLMGETFKKFRDDTELRVAIVQTEGDKFF
CAGWDLKAAAGGDAVDGDYGVGGFGGLQELIDLNKPVIAAVNGMAVGGGFELALSCDLIY
ASDHSSFALPEIRAGTLADAATVKLPKRIPYHVAMDLLLTGRWMDVTEAHRWGLVNEVLP
KDKLMERVWEIARMLESGPPLVFAAIKEVAREAESMGFQEAMNWITKRKFRTVDTLYASE
DGQEGFKAFAEKREPVWKGK

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory