SitesBLAST

Q9P4U9 Enoyl-CoA hydratase AKT3-1; AF-toxin biosynthesis protein 3-1; EC 4.2.1.17 from Alternaria alternata (Alternaria rot fungus) (Torula alternata) (see paper)
33% identity, 93% coverage: 17:258/260 of query aligns to 28:268/296 of Q9P4U9

query
sites
Q9P4U9

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Sites not aligning to the query:

294:296 Peroxisomal targeting signal type 1

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)
30% identity, 99% coverage: 2:258/260 of query aligns to 32:287/290 of P14604

query
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P14604

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E144 (≠ S115) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
E164 (≠ F135) 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

1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
30% identity, 99% coverage: 2:258/260 of query aligns to 2:257/260 of 1dubA

query
sites
1dubA

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active site: A68 (≠ Q65), M73 (≠ L74), S83 (≠ R84), L87 (≠ N88), G111 (≠ A112), E114 (≠ S115), P133 (≠ M134), E134 (≠ F135), T139 (≠ L140), P141 (≠ M142), G142 (≠ D143), K227 (≠ E228), F237 (≠ G238)
binding acetoacetyl-coenzyme a: K26 (≠ A23), A27 (≠ V24), L28 (≠ F25), A30 (= A27), A66 (≠ S63), A68 (≠ Q65), D69 (= D66), I70 (≠ L67), Y107 (≠ A108), G110 (= G111), G111 (≠ A112), E114 (≠ S115), P133 (≠ M134), E134 (≠ F135), L137 (≠ I138), G142 (≠ D143), F233 (≠ Q234), F249 (= F250)

1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
31% identity, 98% coverage: 3:258/260 of query aligns to 1:255/258 of 1ey3A

query
sites
1ey3A

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active site: A66 (≠ Q65), M71 (≠ L74), S81 (≠ R84), L85 (≠ N88), G109 (≠ A112), E112 (≠ S115), P131 (≠ M134), E132 (≠ F135), T137 (≠ L140), P139 (≠ M142), G140 (≠ D143), K225 (≠ E228), F235 (≠ G238)
binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A23), L26 (≠ F25), A28 (= A27), A64 (≠ S63), G65 (= G64), A66 (≠ Q65), D67 (= D66), I68 (≠ L67), L85 (≠ N88), W88 (≠ I91), G109 (≠ A112), P131 (≠ M134), L135 (≠ I138), G140 (≠ D143)

2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
30% identity, 99% coverage: 2:258/260 of query aligns to 1:251/254 of 2dubA

query
sites
2dubA

D

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T

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I

M
x
P

D
x
G

A
|
A

G

G

S

G

N

T

Y

Q

F

R

L

L

P

T

K

R

R

A

V

V

G

G

Y

K

P

S

L

L

A

A

F

M

E

E

L

M

A

V

T

L

T

T

G

G

R

D

K

R

V

I

Y

S

A

A

E

Q

E

D

A

A

E

K

R

Q

L

A

G

G

L

L

V

V

N

S

K

K

A

I

I

F

E

P

H

V

S

E

A

T

L

L

D

V

E

E

T

E

V

A

A

I

Q

Q

Y

C

V

A

E

E

V

K

Y

I

V

A

N

N

A

N

S

S

G

K

S

I

A

I

I

V

G

A

M

M

I

A

K

K

E

E

M

S

L

V

R

N

K

A

S

A

N

F

G

E

M

M

S

T

L

L

E

T

E

E

V

G

L

N

E
x
K

M

L

E

E

A

K

V

K

Y

L

Q

F

E

Y

K

S

A

T

G
x
F

S

A

H

T

Q

D

D

D

F

R

K

R

E

E

G

G

V

M

T

S

S

A

F

F

L

V

E

E

K

K

R

R

K

K

P

A

R

N

F

F

active site: A67 (≠ Q65), M72 (≠ L74), S82 (≠ R84), G105 (≠ A112), E108 (≠ S115), P127 (≠ M134), E128 (≠ F135), T133 (≠ L140), P135 (≠ M142), G136 (≠ D143), K221 (≠ E228), F231 (≠ G238)
binding octanoyl-coenzyme a: K25 (≠ A23), A26 (≠ V24), L27 (≠ F25), A29 (= A27), A65 (≠ S63), A67 (≠ Q65), D68 (= D66), I69 (≠ L67), K70 (= K68), G105 (≠ A112), E108 (≠ S115), P127 (≠ M134), E128 (≠ F135), G136 (≠ D143), A137 (= A144)

O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
32% identity, 95% coverage: 13:258/260 of query aligns to 17:263/266 of O53561

query
sites
O53561

H

H

C

T

Q

L

E

I

I

V

A

T

I

M

D

N

R

R

P

P

A

A

V

A

F

R

N

N

A

A

L

L

N

S

F

T

E

E

V

M

L

M

E

R

E

I

L

M

K

V

A

Q

A

A

F

W

D

D

Q

R

A

V

A

D

Q

N

A

D

E

P

T

D

V

I

R

R

C

C

V

C

V

I

L

L

T

T

G

G

G

A

G

G

A

Y

F

F

C

C

S

A

G

G

Q

M

D

D

L

L

K

K

A

A

V

A

G

T

T

Q

D

K

L

P

D

P

G

G

I

D

P

S

F

F

K

K

E

D

I

-

R

-

K

G

Y

S

Y

Y

N

G

P

P

-

S

-

R

-

I

-

D

L

A

I

L

Q

K

M

G

R

R

N

R

L

L

S

T

K

K

P

P

I

L

I

I

C

A

K

A

L

V

N

E

G

G

A

P

A

A

V

I

G

A

A

G

G

G

C

T

S

E

L

I

A

L

L

Q

A

G

T

T

D

D

V

I

I

R

I

V

A

A

S

G

K

E

E

S

A

A

Y
x
K

L
x
F

A
x
G

E
x
I

M
x
S

F
x
E

A
|
A

H
x
K

I

W

G

S

L

L

V

Y

M

P

D

M

A

G

G

G

S

S

N

A

Y

V

F

R

L

L

P

V

K

R

R

Q

V

I

G

P

Y

Y

P

T

L

L

A

A

F

C

E

D

L

L

A

L

T

L

T

T

G

G

R

R

K

H

V

I

Y

T

A

A

E

A

E

E

A

A

E

K

R

E

L

M

G

G

L

L

V

I

N

G

K

H

A

V

I

V

-

P

E

D

H

G

S

Q

A

A

L

L

D

-

E

-

T

T

V

K

A

A

Q

L

Y

E

V

L

E

A

V

D

Y

A

V

I

N

S

A

A

S

N

G

G

S

P

-

L

A

A

I

V

G

Q

M

A

I

I

K

L

E

R

M

S

L

I

R

R

K

E

S

T

N

E

G

C

M

M

S

P

L

E

E

N

E

E

V

A

L

F

E

K

M

I

E

D

A

T

V

Q

Y

I

Q

G

E

I

K

K

A

V

G

F

S

L

H

S

Q

D

D

D

F

A

K

K

E

E

G

G

V

P

T

R

S

A

F

F

L

A

E

E

K

K

R

R

K

A

P

P

R

N

F

F

K135 (≠ Y130) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
135:142 (vs. 130:137, 13% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
K142 (≠ H137) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.

1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
31% identity, 99% coverage: 2:258/260 of query aligns to 2:255/258 of 1mj3A

query
sites
1mj3A

D

N

Y

F

K

Q

Y

Y

I

I

-

I

-

T

-

E

R

K

S

K

S

G

V

K

N

N

N

S

H

S

C

V

Q

G

E

L

I

I

A

Q

I

L

D

N

R

R

P

P

A
x
K

V
x
A

F
x
L

N

N

A
|
A

L

L

N

C

F

N

E

G

V

L

L

I

E

E

L

L

K

N

A

Q

A

A

F

L

D

E

Q

T

A

F

A

E

Q

E

A

D

E

P

T

A

V

V

R

G

C

A

V

I

V

V

L

L

T

T

G

G

G

E

G

K

A

A

F

F

C

A

S
x
A

G
|
G

Q
x
A

D
|
D

L
x
I

K

K

A

-

V

-

G

-

T

-

D

E

L
x
M

D

Q

G

N

I

R

P

T

F

F

K

Q

E

D

I

C

I

-

R

-

K

-

Y

-

Y

Y

N
x
S

P

G

L
|
L

-

S

-

H

I

W

I

D

Q

H

M

I

R

T

N

R

L

I

S

K

K

K

P

P

I

V

I

I

C

A

K

A

L

V

N

N

G

G

A

Y

A

A

V

L

G

G

A
x
G

G

G

C

C

S
x
E

L

L

A

A

L

M

A

M

T

C

D

D

V

I

I

I

I

Y

A

A

S

G

K

E

E

K

A

A

Y

Q

L

F

A

G

E

Q

M
x
P

F
x
E

A

I

H

L

I
x
L

G

G

L
x
T

V

I

M
x
P

D
x
G

A

A

G

G

S

G

N

T

Y

Q

F

R

L

L

P

T

K

R

R

A

V

V

G

G

Y

K

P

S

L

L

A

A

F

M

E

E

L

M

A

V

T

L

T

T

G

G

R

D

K

R

V

I

Y

S

A

A

E

Q

E

D

A

A

E

K

R

Q

L

A

G

G

L

L

V

V

N

S

K

K

A

I

I

F

E

P

H

V

S

E

A

T

L

L

D

V

E

E

T

E

V

A

A

I

Q

Q

Y

C

V

A

E

E

V

K

Y

I

V

A

N

N

A

N

S

S

G

K

S

I

A

I

I

V

G

A

M

M

I

A

K

K

E

E

M

S

L

V

R

N

K

A

S

A

N

F

G

E

M

M

S

T

L

L

E

T

E

E

V

G

L

N

E
x
K

M

L

E

E

A

K

V

K

Y

L

Q

F

E

Y

K

S

A

T

G
x
F

S

A

H

T

Q

D

D

D

F

R

K

R

E

E

G

G

V

M

T

S

S

A

F

F

L

V

E

E

K

K

R

R

K

K

P

A

R

N

F

F

active site: A68 (≠ Q65), M73 (≠ L74), S83 (≠ N88), L85 (= L90), G109 (≠ A112), E112 (≠ S115), P131 (≠ M134), E132 (≠ F135), T137 (≠ L140), P139 (≠ M142), G140 (≠ D143), K225 (≠ E228), F235 (≠ G238)
binding hexanoyl-coenzyme a: K26 (≠ A23), A27 (≠ V24), L28 (≠ F25), A30 (= A27), A66 (≠ S63), G67 (= G64), A68 (≠ Q65), D69 (= D66), I70 (≠ L67), G109 (≠ A112), P131 (≠ M134), E132 (≠ F135), L135 (≠ I138), G140 (≠ D143)

3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
29% identity, 99% coverage: 1:258/260 of query aligns to 1:254/255 of 3q0jC

query
sites
3q0jC

M

M

D

T

Y

Y

K

E

Y

T

I

I

R

L

S

V

S

E

V

R

N

D

N

Q

H

R

C

V

Q

G

E

I

I

I

A

T

I

L

D

N

R

R

P

P

A
x
Q

V
x
A

F
x
L

N

N

A
|
A

L

L

N

N

F

S

E

Q

V

V

L

M

E

N

E

E

L

V

K

T

A

S

A

A

F

A

D

T

Q

E

A

L

A

D

Q

D

A

D

E

P

T

D

V

I

R

G

C

A

V

I

L

I

T

T

G

G

G

S

G

A

G

K

A

A

F

F

C

A

S
x
A

G
|
G

Q
x
A

D
|
D

L
x
I

K
|
K

A

-

V

-

G

-

T

-

D

E

L
x
M

D

A

G

D

I

L

P

T

F

F

K

A

E

D

I

A

I

F

R
x
T

K

A

Y

D

Y

F

N
x
F

P

A

L

T

I

W

I

G

Q

K

M

L

R

A

N

A

L

V

S

R

K

T

P

P

I

T

I

I

C

A

K

A

L

V

N

A

G

G

A

Y

A

A

V

L

G
|
G

A
x
G

G

G

C

C

S
x
E

L

L

A

A

L

M

A

M

T

C

D

D

V

V

I

L

I

I

A

A

S

A

K

D

E

T

A

A

Y

K

L

F

A

G

E

Q

M
x
P

F
x
E

A

I

H

K

I

L

G

G

L
x
V

V

L

M
x
P

D
x
G

A
x
M

G

G

S

G

N

S

Y

Q

F

R

L

L

P

T

K

R

R

A

V

I

G

G

Y

K

P

A

L

K

A

A

F

M

E

D

L

L

A

I

T

L

T

T

G

G

R

R

K

T

V

M

Y

D

A

A

E

A

E

E

A

A

E

E

R

R

L

S

G

G

L

L

V

V

N

S

K

R

A

V

I

V

E

P

H

A

S

D

A

D

L

L

D

L

E

T

T

E

V

A

A

R

Q

A

Y

T

V

A

E

T

V

T

Y

I

V

S

N

Q

A

M

S

S

G

A

S

S

A

A

I

A

G

R

M

M

I

A

K

K

E

E

M

A

L

V

R

N

K

R

S

A

N

F

G

E

M

S

S

S

L

L

E

S

E

E

V

G

L

L

E
x
L

M

Y

E

E

A

R

V

R

Y

L

Q

F

E

H

K

S

A

A

G
x
F

S

A

H

T

Q

E

D

D

F

Q

K

S

E

E

G

G

V

M

T

A

S

A

F

F

L

I

E

E

K

K

R

R

K

A

P

P

R

Q

F

F

active site: A65 (≠ Q65), M70 (≠ L74), T80 (≠ R84), F84 (≠ N88), G108 (≠ A112), E111 (≠ S115), P130 (≠ M134), E131 (≠ F135), V136 (≠ L140), P138 (≠ M142), G139 (≠ D143), L224 (≠ E228), F234 (≠ G238)
binding acetoacetyl-coenzyme a: Q23 (≠ A23), A24 (≠ V24), L25 (≠ F25), A27 (= A27), A63 (≠ S63), G64 (= G64), A65 (≠ Q65), D66 (= D66), I67 (≠ L67), K68 (= K68), M70 (≠ L74), F84 (≠ N88), G107 (= G111), G108 (≠ A112), E111 (≠ S115), P130 (≠ M134), E131 (≠ F135), P138 (≠ M142), G139 (≠ D143), M140 (≠ A144)

3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 99% coverage: 1:258/260 of query aligns to 1:254/255 of 3q0gC

query
sites
3q0gC

M

M

D

T

Y

Y

K

E

Y

T

I

I

R

L

S

V

S

E

V

R

N

D

N

Q

H

R

C

V

Q

G

E

I

I

I

A

T

I

L

D

N

R

R

P

P

A

Q

V

A

F
x
L

N

N

A

A

L

L

N

N

F

S

E

Q

V

V

L

M

E

N

E

E

L

V

K

T

A

S

A

A

F

A

D

T

Q

E

A

L

A

D

Q

D

A

D

E

P

T

D

V

I

R

G

C

A

V

I

L

I

T

T

G

G

G

S

G

A

G

K

A

A

F

F

C

A

S
x
A

G

G

Q
x
A

D

D

L
x
I

K
|
K

A

-

V

-

G

-

T

-

D

E

L
x
M

D

A

G

D

I

L

P

T

F

F

K

A

E

D

I

A

I

F

R
x
T

K

A

Y

D

Y

F

N
x
F

P

A

L

T

I

W

I

G

Q

K

M

L

R

A

N

A

L

V

S

R

K

T

P

P

I

T

I

I

C

A

K

A

L

V

N

A

G

G

A
x
Y

A

A

V

L

G

G

A
x
G

G

G

C

C

S
x
E

L

L

A

A

L

M

A

M

T

C

D

D

V

V

I

L

I

I

A

A

S

A

K

D

E

T

A

A

Y

K

L

F

A

G

E

Q

M
x
P

F
x
E

A

I

H

K

I
x
L

G

G

L
x
V

V

L

M
x
P

D
x
G

A

M

G

G

S

G

N

S

Y

Q

F

R

L

L

P

T

K

R

R

A

V

I

G

G

Y

K

P

A

L

K

A

A

F

M

E

D

L

L

A

I

T

L

T

T

G

G

R

R

K

T

V

M

Y

D

A

A

E

A

E

E

A

A

E

E

R

R

L

S

G

G

L

L

V

V

N

S

K

R

A

V

I

V

E

P

H

A

S

D

A

D

L

L

D

L

E

T

T

E

V

A

A

R

Q

A

Y

T

V

A

E

T

V

T

Y

I

V

S

N

Q

A

M

S

S

G

A

S

S

A

A

I

A

G

R

M

M

I

A

K

K

E

E

M

A

L

V

R

N

K

R

S

A

N

F

G

E

M

S

S

S

L

L

E

S

E

E

V

G

L

L

E
x
L

M

Y

E

E

A

R

V

R

Y

L

Q

F

E

H

K

S

A

A

G
x
F

S

A

H

T

Q

E

D

D

F

Q

K

S

E

E

G

G

V

M

T

A

S

A

F

F

L

I

E

E

K

K

R

R

K

A

P

P

R

Q

F

F

active site: A65 (≠ Q65), M70 (≠ L74), T80 (≠ R84), F84 (≠ N88), G108 (≠ A112), E111 (≠ S115), P130 (≠ M134), E131 (≠ F135), V136 (≠ L140), P138 (≠ M142), G139 (≠ D143), L224 (≠ E228), F234 (≠ G238)
binding coenzyme a: L25 (≠ F25), A63 (≠ S63), I67 (≠ L67), K68 (= K68), Y104 (≠ A108), P130 (≠ M134), E131 (≠ F135), L134 (≠ I138)

3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
29% identity, 98% coverage: 3:258/260 of query aligns to 2:253/256 of 3h81A

query
sites
3h81A

Y

Y

K

E

Y

T

I

I

R

L

S

V

S

E

V

R

N

D

N

Q

H

R

C

V

Q

G

E

I

I

I

A

T

I

L

D

N

R

R

P

P

A

Q

V

A

F

L

N

N

A

A

L

L

N

N

F

S

E

Q

V

V

L

M

E

N

E

E

L

V

K

T

A

S

A

A

F

A

D

T

Q

E

A

L

A

D

Q

D

A

D

E

P

T

D

V

I

R

G

C

A

V

I

L

I

T

T

G

G

G

S

G

A

G

K

A

A

F

F

C

A

S

A

G

G

Q
x
A

D

D

L

I

K

K

A

-

V

-

G

-

T

-

D

E

L
x
M

D

A

G

D

I

L

P

T

F

F

K

A

E

D

I

A

I

F

R
x
T

K

A

Y

D

Y

F

N
x
F

P

A

L

T

I

W

I

G

Q

K

M

L

R

A

N

A

L

V

S

R

K

T

P

P

I

T

I

I

C

A

K

A

L

V

N

A

G

G

A

Y

A

A

V

L

G

G

A
x
G

G

G

C

C

S
x
E

L

L

A

A

L

M

A

M

T

C

D

D

V

V

I

L

I

I

A

A

S

A

K

D

E

T

A

A

Y

K

L

F

A

G

E

Q

M
x
P

F
x
E

A

I

H

K

I

L

G

G

L
x
V

V

L

M
x
P

D
x
G

A

M

G

G

S

G

N

S

Y

Q

F

R

L

L

P

T

K

R

R

A

V

I

G

G

Y

K

P

A

L

K

A

A

F

M

E

D

L

L

A

I

T

L

T

T

G

G

R

R

K

T

V

M

Y

D

A

A

E

A

E

E

A

A

E

E

R

R

L

S

G

G

L

L

V

V

N

S

K

R

A

V

I

V

E

P

H

A

S

D

A

D

L

L

D

L

E

T

T

E

V

A

A

R

Q

A

Y

T

V

A

E

T

V

T

Y

I

V

S

N

Q

A

M

S

S

G

A

S

S

A

A

I

A

G

R

M

M

I

A

K

K

E

E

M

A

L

V

R

N

K

R

S

A

N

F

G

E

M

S

S

S

L

L

E

S

E

E

V

G

L

L

E
x
L

M

Y

E

E

A

R

V

R

Y

L

Q

F

E

H

K

S

A

A

G
x
F

S

A

H

T

Q

E

D

D

F
x
Q

K

S

E

E

G

G

V

M

T

A

S

A

F

F

L

I

E

E

K

K

R

R

K

A

P

P

R

Q

F

F

active site: A64 (≠ Q65), M69 (≠ L74), T79 (≠ R84), F83 (≠ N88), G107 (≠ A112), E110 (≠ S115), P129 (≠ M134), E130 (≠ F135), V135 (≠ L140), P137 (≠ M142), G138 (≠ D143), L223 (≠ E228), F233 (≠ G238)
binding calcium ion: F233 (≠ G238), Q238 (≠ F243)

3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 98% coverage: 3:258/260 of query aligns to 2:249/250 of 3q0gD

query
sites
3q0gD

Y

Y

K

E

Y

T

I

I

R

L

S

V

S

E

V

R

N

D

N

Q

H

R

C

V

Q

G

E

I

I

I

A

T

I

L

D

N

R

R

P

P

A

Q

V

A

F

L

N

N

A

A

L

L

N

N

F

S

E

Q

V

V

L

M

E

N

E

E

L

V

K

T

A

S

A

A

F

A

D

T

Q

E

A

L

A

D

Q

D

A

D

E

P

T

D

V

I

R

G

C

A

V

I

L

I

T

T

G

G

G

S

G

A

G

K

A

A

F

F

C

A

S

A

G

G

Q
x
A

D

D

L

I

K

K

A

E

V
x
M

G

-

T

-

D

-

L

-

D

-

G

-

I

-

P

-

F

F

K

A

E

D

I

A

I

F

R
x
T

K

A

Y

D

Y

F

N
x
F

P

A

L

T

I

W

I

G

Q

K

M

L

R

A

N

A

L

V

S

R

K

T

P

P

I

T

I

I

C

A

K

A

L

V

N

A

G

G

A

Y

A

A

V

L

G

G

A
x
G

G

G

C

C

S
x
E

L

L

A

A

L

M

A

M

T

C

D

D

V

V

I

L

I

I

A

A

S

A

K

D

E

T

A

A

Y

K

L

F

A

G

E

Q

M
x
P

F
x
E

A

I

H

K

I

L

G

G

L
x
V

V

L

M
x
P

D
x
G

A

M

G

G

S

G

N

S

Y

Q

F

R

L

L

P

T

K

R

R

A

V

I

G

G

Y

K

P

A

L

K

A

A

F

M

E

D

L

L

A

I

T

L

T

T

G

G

R

R

K

T

V

M

Y

D

A

A

E

A

E

E

A

A

E

E

R

R

L

S

G

G

L

L

V

V

N

S

K

R

A

V

I

V

E

P

H

A

S

D

A

D

L

L

D

L

E

T

T

E

V

A

A

R

Q

A

Y

T

V

A

E

T

V

T

Y

I

V

S

N

Q

A

M

S

S

G

A

S

S

A

A

I

A

G

R

M

M

I

A

K

K

E

E

M

A

L

V

R

N

K

R

S

A

N

F

G

E

M

S

S

S

L

L

E

S

E

E

V

G

L

L

E
x
L

M

Y

E

E

A

R

V

R

Y

L

Q
x
F

E

H

K

S

A

A

G
x
F

S

A

H

T

Q

E

D

D

F

Q

K

S

E

E

G

G

V

M

T

A

S

A

F
|
F

L

I

E

E

K

K

R

R

K

A

P

P

R

Q

F

F

active site: A64 (≠ Q65), M69 (≠ V70), T75 (≠ R84), F79 (≠ N88), G103 (≠ A112), E106 (≠ S115), P125 (≠ M134), E126 (≠ F135), V131 (≠ L140), P133 (≠ M142), G134 (≠ D143), L219 (≠ E228), F229 (≠ G238)
binding Butyryl Coenzyme A: F225 (≠ Q234), F241 (= F250)

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)
27% identity, 97% coverage: 3:255/260 of query aligns to 2:257/269 of A5JTM5

query
sites
A5JTM5

Y

Y

K

E

Y

A

I

I

R

G

S

H

S

R

V

V

N

E

N

D

H

G

C

V

Q

A

E

E

I

I

A

T

I

I

D

K

R

L

P

P

A

R

V

H

F
x
R

N

N

A

A

L

L

N

S

F

V

E

K

V

A

L

M

E

Q

E
|
E

L

V

K

T

A

D

A

A

F

L

D

N

Q

R

A

A

A
x
E

Q

E

A
x
D

E
x
D

T

S

V

V

R

G

C

A

V

V

V

M

L

I

T

T

G

G

G

A

G

E

G

D

A

A

F

F

C

C

S

A

G
|
G

Q
x
F

D
x
Y

L

L

K
x
R

A
x
E

V

I

G

P

T

L

D

D

L

K

D

G

G

V

I

A

P

G

F

V

K

R

E

D

I
x
H

I
x
F

R

R

-

I

-

G

-

A

K

L

Y

W

Y
x
W

N
x
H

P

Q

L

M

I

I

I
x
H

Q

K

M

I

R

I

N

R

L

V

S

K

K

R

P

P

I

V

I

L

C

A

K

A

L

I

N

N

G

G

A

V

A

A

V
x
A

G
|
G

A
x
G

G
|
G

C

L

S

G

L

I

A

S

L

L

A

A

T

S

D
|
D

V

M

I

A

I

I

A

C

S

A

K
x
D

E

S

A

A

Y

K

L

F

A

V

E

C

M

A

F
x
W

A

H

H

T

I

I

G

G

L

I

V

G

M

N

D
|
D

A

T

G

A

S

T

N

S

Y

Y

F

S

L

L

P

A

K

R

R

I

V

V

G

G

Y

M

P

R

L

R

A

A

F

M

E
|
E

L

L

A

M

T

L

T

T

G

N

R

R

K

T

V

L

Y

Y

A

P

E

E

E
|
E

A

A

E

K

R

D

L
x
W

G

G

L

L

V

V

N

S

K

R

A

V

I

Y

E

P

H

K

S

D

A

D

L

F

D

R

E

E

T

V

V

A

A

W

Q

K

Y

V

V

A

E

R

V

E

Y

L

V

A

N

A

A

A

S

P

G

T

S
x
H

A

L

I

Q

G

V

M

M

I

A

K

K

E

E

M
x
R

L

F

R

H

K

A

S

G

N

W

G

M

M

Q

S

P

L

V

E

E

V

C

L

T

E

E

M

F

E
|
E

A

I

V

Q

Y

N

Q

V

E

I

K

A

A

S

G

V

S

T

H

H

Q

P

D

H

F

F

K

M

E

P

G

C

V

L

T

T

S

E

F

F

L

L

E

D

K

G

R

H

K
x
R

R24 (≠ F25) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
E34 (= E35) mutation to T: Forms inclusion bodies.
E43 (≠ A44) mutation to A: No effect on catalytic activity.
D45 (≠ A46) mutation to A: No effect on catalytic activity.
D46 (≠ E47) mutation to A: No effect on catalytic activity.
G63 (= G64) mutation G->A,I,P: Yields insoluble protein.
F64 (≠ Q65) 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 (≠ D66) mutation to D: Catalytic activity is almost as efficient as wild type.
R67 (≠ K68) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
E68 (≠ A69) mutation to T: No effect on catalytic activity.
H81 (≠ I82) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
F82 (≠ I83) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
W89 (≠ Y87) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
H90 (≠ N88) 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 (≠ I92) mutation to Q: No effect on catalytic activity.
A112 (≠ V110) 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 (= G111) 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 (≠ A112) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
G115 (= G113) mutation G->L,N,S,V: Yields insoluble protein.
D123 (= D121) mutation to T: No effect on catalytic activity.
D129 (≠ K127) mutation to T: No effect on catalytic activity.
W137 (≠ F135) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
D145 (= D143) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
E163 (= E161) mutation to T: No effect on catalytic activity.
E175 (= E173) mutation to D: No effect on catalytic activity.
W179 (≠ L177) mutation to F: No effect on catalytic activity.
H208 (≠ S206) mutation to Q: No effect on catalytic activity.
R216 (≠ M214) mutation R->E,K,L: Yields insoluble protein.
E232 (= E230) mutation E->A,N,Q,R: Yields insoluble protein.; mutation to D: Reduced catalytic activity, increased substrate binding.
R257 (≠ K255) mutation to K: Retains catalytic activity and substrate CoA binding.; mutation to L: Significantly reduces catalytic activity and substrate CoA binding.

1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
27% identity, 97% coverage: 3:255/260 of query aligns to 2:257/269 of 1nzyB

query
sites
1nzyB

Y

Y

K

E

Y

A

I

I

R

G

S

H

S

R

V

V

N

E

N

D

H

G

C

V

Q

A

E

E

I

I

A

T

I

I

D

K

R

L

P

P

A
x
R

V
x
H

F
x
R

N

N

A

A

L

L

N

S

F

V

E

K

V

A

L

M

E

Q

E

E

L

V

K

T

A

D

A

A

F

L

D

N

Q

R

A

A

A

E

Q

E

A

D

E

D

T

S

V

V

R
x
G

C

A

V

V

V

M

L

I

T

T

G

G

G

A

G
x
E

G

D

A

A

F

F

C
|
C

S
x
A

G

G

Q
x
F

D
x
Y

L
|
L

K
x
R

A

E

V
x
I

G

P

T

L

D

D

L

K

D

G

G

V

I

A

P

G

F

V

K

R

E

D

I

H

I

F

R

R

-

I

-

A

-
x
A

K

L

Y

W

Y
x
W

N
x
H

P

Q

L

M

I

I

I

H

Q

K

M

I

R

I

N

R

L

V

S

K

K

R

P

P

I

V

I

L

C

A

K

A

L

I

N
|
N

G

G

A

V

A

A

V

A

G
|
G

A
x
G

G

G

C

L

S
x
G

L

I

A

S

L

L

A

A

T

S

D

D

V

M

I

A

I

I

A

C

S

A

K

D

E

S

A

A

Y

K

L

F

A

V

E

C

M
x
A

F
x
W

A

H

H

T

I

I

G

G

L
x
I

V

G

M
x
N

D
|
D

A
x
T

G

A

S

T

N

S

Y

Y

F

S

L

L

P

A

K

R

R

I

V

V

G

G

Y

M

P

R

L

R

A

A

F

M

E

E

L

L

A

M

T

L

T

T

G

D

R

R

K

T

V

L

Y

Y

A

P

E

E

A

A

E

K

R

D

L

W

G

G

L

L

V

V

N

S

K

R

A

V

I

Y

E

P

H
x
K

S

D

A

E

L

F

D
x
R

E

E

T

V

V

A

A

W

Q

K

Y

V

V

A

E

R

V

E

Y
x
L

V
x
A

N

A

A
|
A

S

P

G
x
T

S

H

A

L

I
x
Q

G

V

M

M

I

A

K

K

E

E

M

R

L

F

R

H

K

A

S

G

N

W

G

M

M

Q

S

P

L

V

E

E

V

C

L

T

E
|
E

M

F

E

E

A

I

V

Q

Y

N

Q

V

E

I

K

A

A

S

G

V

S

T

H

H

Q

P

D

H

F

F

K

M

E

P

G

C

V

L

T

T

S

R

F
|
F

L

L

E

D

K

G

R

H

K
x
R

active site: C61 (= C62), F64 (≠ Q65), I69 (≠ V70), A86 (vs. gap), H90 (≠ N88), G114 (≠ A112), G117 (≠ S115), A136 (≠ M134), W137 (≠ F135), I142 (≠ L140), N144 (≠ M142), D145 (= D143), E230 (= E228)
binding 4-hydroxybenzoyl coenzyme a: R22 (≠ A23), H23 (≠ V24), R24 (≠ F25), A62 (≠ S63), F64 (≠ Q65), Y65 (≠ D66), L66 (= L67), R67 (≠ K68), W89 (≠ Y87), G113 (= G111), G114 (≠ A112), A136 (≠ M134), W137 (≠ F135), D145 (= D143), T146 (≠ A144), F252 (= F250), R257 (≠ K255)
binding calcium ion: G49 (≠ R50), L202 (≠ Y200), A203 (≠ V201), A205 (= A203), T207 (≠ G205), Q210 (≠ I208)
binding phosphate ion: E57 (≠ G58), N108 (= N106), K188 (≠ H186), R192 (≠ D190)

1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
27% identity, 97% coverage: 3:255/260 of query aligns to 2:257/269 of 1jxzB

query
sites
1jxzB

Y

Y

K

E

Y

A

I

I

R

G

S

H

S

R

V

V

N

E

N

D

H

G

C

V

Q

A

E

E

I

I

A

T

I

I

D

K

R

L

P

P

A
x
R

V
x
H

F
x
R

N

N

A

A

L

L

N

S

F

V

E

K

V

A

L

M

E

Q

E

E

L

V

K

T

A

D

A

A

F

L

D

N

Q

R

A

A

A

E

Q

E

A

D

E

D

T

S

V

V

R
x
G

C

A

V

V

V

M

L

I

T

T

G

G

G

A

G

E

G

D

A

A

F

F

C
|
C

S
x
A

G

G

Q
x
F

D
x
Y

L
|
L

K
x
R

A

E

V
x
I

G

P

T

L

D

D

L

K

D

G

G

V

I

A

P

G

F

V

K

R

E

D

I

H

I

F

R

R

-

I

-

A

-
x
A

K

L

Y

W

Y
x
W

N
x
Q

P

Q

L

M

I

I

I

H

Q

K

M

I

R

I

N

R

L

V

S

K

K

R

P

P

I

V

I

L

C

A

K

A

L

I

N

N

G

G

A

V

A

A

V

A

G
|
G

A
x
G

G

G

C

L

S
x
G

L

I

A

S

L

L

A

A

T

S

D

D

V

M

I

A

I

I

A

C

S

A

K

D

E

S

A

A

Y

K

L

F

A

V

E

C

M
x
A

F
x
W

A

H

H

T

I

I

G

G

L
x
I

V

G

M
x
N

D
|
D

A
x
T

G

A

S

T

N

S

Y

Y

F

S

L

L

P

A

K

R

R

I

V

V

G

G

Y

M

P

R

L

R

A

A

F

M

E

E

L

L

A

M

T

L

T

T

G

N

R

R

K

T

V

L

Y

Y

A

P

E

E

A

A

E

K

R

D

L

W

G

G

L

L

V

V

N

S

K

R

A

V

I

Y

E

P

H

K

S

D

A

E

L

F

D

R

E

E

T

V

V

A

A

W

Q

K

Y

V

V

A

E

R

V

E

Y
x
L

V
x
A

N

A

A
|
A

S

P

G
x
T

S

H

A

L

I
x
Q

G

V

M

M

I

A

K

K

E

E

M

R

L

F

R

H

K

A

S

G

N

W

G

M

M

Q

S

P

L

V

E

E

V

C

L

T

E
|
E

M

F

E

E

A

I

V

Q

Y

N

Q

V

E

I

K

A

A

S

G

V

S

T

H

H

Q

P

D

H

F

F

K

M

E

P

G

C

V

L

T

T

S

R

F
|
F

L

L

E

D

K

G

R

H

K
x
R

active site: C61 (= C62), F64 (≠ Q65), I69 (≠ V70), A86 (vs. gap), Q90 (≠ N88), G113 (= G111), G114 (≠ A112), G117 (≠ S115), A136 (≠ M134), W137 (≠ F135), I142 (≠ L140), N144 (≠ M142), D145 (= D143), E230 (= E228)
binding 4-hydroxybenzoyl coenzyme a: R22 (≠ A23), H23 (≠ V24), R24 (≠ F25), A62 (≠ S63), F64 (≠ Q65), Y65 (≠ D66), L66 (= L67), R67 (≠ K68), W89 (≠ Y87), G113 (= G111), A136 (≠ M134), W137 (≠ F135), I142 (≠ L140), D145 (= D143), T146 (≠ A144), F252 (= F250), R257 (≠ K255)
binding calcium ion: G49 (≠ R50), L202 (≠ Y200), A203 (≠ V201), A205 (= A203), T207 (≠ G205), Q210 (≠ I208)

3omeC Crystal structure of a probable enoyl-coa hydratase from mycobacterium smegmatis (see paper)
33% identity, 75% coverage: 5:198/260 of query aligns to 5:194/247 of 3omeC

query
sites
3omeC

Y

Y

I

I

R

D

S

Y

S

G

V

V

N

A

N

D

H

S

C

I

Q

A

E

T

I

I

A

T

I

L

D

N

R

R

P

P

A

E

V

A

F

A

N

N

A

A

L

Q

N

N

F

P

E

E

V

L

L

L

E

D

E

E

L

L

K

D

A

A

F

W

D

T

Q

R

A

A

Q

E

A

D

E

N

T

E

V

V

R

K

C

V

V

I

L

L

T

R

G

A

G

N

G

G

G

K

A

H

F

F

C

S

S

A

G

G

Q
x
H

D

D

L

L

K

R

A

P

V
x
E

G

K

T

I

D

S

L

L

D

E

G

F

I

I

P

-

F

I

K

Q

E

H

I
x
E

I
x
A

R

R

K

R

Y

Y

Y
x
L

N

D

P

-

L

Y

I

T

I

L

Q

R

M

W

R

R

N

N

L

V

S

P

K

K

P

P

I

S

I

I

C

A

K

A

L

V

N

Q

G

G

A

R

A

C

V

I

G

S

A
x
G

G

G

C

L

S
x
L

L

L

A

C

L

W

A

P

T

C

D

D

V

L

I

I

I

L

A

A

S

S

K

D

E

D

A

A

Y

L

L

F

A

S

E

D

M

P

F
x
V

A

A

H

L

I

M

G

G

L
x
I

-
x
G

-

G

V

V

M
x
E

D

Y

A

H

G

G

S

H

N

T

Y

W

F

E

L

L

P

G

K

P

R

R

V

K

G

-

Y

-

P

-

L

-

A

A

F

K

E

E

L

I

A

L

T

F

T

T

G

G

R

R

K

A

V

L

Y

T

A

A

E

E

A

A

E

E

R

R

L

T

G

G

L

M

V

V

N

N

K

R

A

V

I

V

E

A

H

R

S

D

A

E

L

L

D

D

E

A

T

Q

V

T

A

R

Q

E

Y

L

V

A

E

E

active site: H65 (≠ Q65), E70 (≠ V70), A82 (≠ I83), L86 (≠ Y87), G110 (≠ A112), L113 (≠ S115), V133 (≠ F135), I138 (≠ L140), G139 (vs. gap), E142 (≠ M142)
binding zinc ion: E81 (≠ I82), E142 (≠ M142)

Sites not aligning to the query:

active site: 225, 235
binding zinc ion: 231, 235

5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
31% identity, 93% coverage: 19:260/260 of query aligns to 20:259/261 of 5jbxB

query
sites
5jbxB

I

I

D

D

R

G

P

E

A
x
S

V
x
R

F
x
R

N

N

A
|
A

L

I

N

S

F

R

E

A

V

M

L

L

E

K

E

E

L

L

K

G

A

E

A

L

F

V

D

T

Q

R

A

V

A

S

Q

S

A

S

E

R

T

D

V

V

R

R

C

A

V

V

L

I

T

T

G

G

G

A

G

G

G

D

-

K

A

A

F

F

C

C

S
x
A

G

G

Q
x
A

D
|
D

L
|
L

K
|
K

A

E

V
x
R

G

A

T

T

D

M

L

A

D

E

G

-

I

-

P

-

F

-

K

-

E

D

I

E

I

V

R

R

K

A

Y

F

Y
x
L

N

D

P

G

L

L

I
x
R

I

R

Q

T

M

F

R

R

N

A

L

I

S

E

K

K

P

S

-

D

-

C

-

V

I

F

I

I

C

A

K

A

L

I

N

N

G

G

A

A

V
x
L

G
|
G

A
x
G

G

G

C

T

S
x
E

L

L

A

A

L

L

A

A

T

C

D

D

V

L

I

R

I

V

A

A

S

A

K

P

E

A

A

A

Y

E

L

L

A

G

E

L

M
x
T

F
x
E

A

V

H

K

I
x
L

G

G

L
x
I

V

I

M
x
P

D
x
G

A

G

G

G

S

G

N

T

Y

Q

F

R

L

L

P

A

K

R

R

L

V

V

G

G

Y

P

P

G

L

R

A

A

F

K

E

D

L

L

A

I

T

L

T

T

G

A

R

R

K
x
R

V

I

Y

N

A

A

E

A

E

E

A

A

E

F

R

S

L

V

G

G

L

L

V

A

N

N

K

R

A

L

I

A

E

P

H

E

S

G

A

H

L

L

D

L

E

A

T

V

V

A

A

Y

Q

G

Y

L

V

A

E

E

V

S

Y

V

V

V

N

E

A

N

S

A

G

P

S

I

A

A

I

V

G

A

M

T

I

A

K

K

E

H

M

A

L

I

R

D

K

E

S

G

N

T

G

G

M

L

S

E

L

L

E

D

V

A

L

L

E
x
A

M

L

E

E

A

L

V

R

Y

K

Q

Y

E

E

K

E

A

I

G
x
L

S

K

H

T

Q

E

D

D

F

R

K

L

E

E

G

G

V

L

T

R

S

A

F

F

L

A

E

E

K

K

R

R

K

A

P

P

R

-

F

V

Y

Y

K

K

active site: A67 (≠ Q65), R72 (≠ V70), L84 (≠ Y87), R88 (≠ I91), G112 (≠ A112), E115 (≠ S115), T134 (≠ M134), E135 (≠ F135), I140 (≠ L140), P142 (≠ M142), G143 (≠ D143), A228 (≠ E228), L238 (≠ G238)
binding coenzyme a: S24 (≠ A23), R25 (≠ V24), R26 (≠ F25), A28 (= A27), A65 (≠ S63), D68 (= D66), L69 (= L67), K70 (= K68), L110 (≠ V110), G111 (= G111), T134 (≠ M134), E135 (≠ F135), L138 (≠ I138), R168 (≠ K168)

Query Sequence

>Echvi_0069 Echvi_0069 Enoyl-CoA hydratase/carnithine racemase
MDYKYIRSSVNNHCQEIAIDRPAVFNALNFEVLEELKAAFDQAAQAETVRCVVLTGGGGA
FCSGQDLKAVGTDLDGIPFKEIIRKYYNPLIIQMRNLSKPIICKLNGAAVGAGCSLALAT
DVIIASKEAYLAEMFAHIGLVMDAGSNYFLPKRVGYPLAFELATTGRKVYAEEAERLGLV
NKAIEHSALDETVAQYVEVYVNASGSAIGMIKEMLRKSNGMSLEEVLEMEAVYQEKAGSH
QDFKEGVTSFLEKRKPRFYK

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