SitesBLAST

H143 (= H135) active site, Proton donor/acceptor; mutation to A: Loss of dehydratase activity.
H146 (≠ S138) mutation to A: It retains full catalytic activity.
K170 (= K162) active site, Schiff-base intermediate with substrate; mutation to A: Loss of dehydratase activity, but it is still able to bind substrate.
M205 (= M195) mutation to L: It has little effect on the catalytic efficiency and affinity for 3-dehydroquinate.

1l9wA Crystal structure of 3-dehydroquinase from salmonella typhi complexed with reaction product (see paper)
35% identity, 87% coverage: 32:242/242 of query aligns to 39:250/252 of 1l9wA

query
sites
1l9wA

E

E

K

A

G

T

A

F

D

D

I

I

L

L

E
|
E

V

W

R
|
R

L

V

D

D

-

H

L

F

L

M

G

D

I

I

R

A

N

S

P

T

E

Q

S

S

-

V

-

L

-

T

A

A

K

R

I

V

I

I

R

R

E

D

I

A

K

M

S

P

E

D

T

-

G

-

L

I

P

P

V

L

L

L

V

F

T

T

N

F

R
|
R

S

S

V

A

A

K

E
|
E

G

G

K

-

W

-

E

E

G

Q

K

T

E

I

V

T

D

T

R

Q

T

H

E

Y

L

L

L

T

V

L

A

N

L

R

L

A

S

A

L

I

K

D

D

S

G

G

-

L

P

V

D

D

A

M

V

I

D

D

I

L

E

E

L

L

S

F

A

T

S

G

R

D

E

A

D

D

R

V

D

K

K

A

V

T

I

V

K

D

A

Y

A

A

K

H

A

A

H

H

G

N

K

V

T

Y

V

V

I

V

I

M

S

S

S

N

H
|
H

D

D

F

F

S

H

K

Q

T

T

P

P

S

S

P

A

Q

E

E

E

M

M

T

V

A

S

T

R

L

L

A

R

E

K

M

M

F

Q

L

A

A

L

E

G

A

A

D

D

I

I

A

P

K
|
K

I

I

A

A

V

V

M

M

P

P

G

Q

S

S

M

K

E

H

D

D

V

V

L

L

N

T

L

L

K

T

V

A

T

T

L

L

E

E

F

M

K

Q

N

Q

-

H

-

Y

T

A

G

D

K

R

T

P

V

V

C

I

T

T

I

M

A

S

M

M

G

A

K

K

P

E

G

G

K

V

H

I

T

S

R
|
R

V

L

V

A

A

G

P

E

L

V

Y

F

G

G

S

S

V

A

L

A

T

T

Y
x
F

A

G

S

A

I

V

E

K

S

Q

N

-

A

-

V

A

A
x
S

A
|
A

P

P

G

G

Q
|
Q

L

I

P

A

V

V

D

N

E

D

V

L

K

R

K

S

I

V

M

L

E

M

M

I

L

L

K

H

active site: E86 (= E77), H143 (= H135), K170 (= K162)
binding 3-amino-4,5-dihydroxy-cyclohex-1-enecarboxylate: E46 (= E39), R48 (= R41), R82 (= R73), H143 (= H135), K170 (= K162), R213 (= R203), F225 (≠ Y215), S232 (≠ A224), A233 (= A225), Q236 (= Q228)

8b2cAAA 3-dehydroquinate dehydratase (see paper)
35% identity, 87% coverage: 32:242/242 of query aligns to 39:250/252 of 8b2cAAA

query
sites
8b2cAAA

E

E

K

A

G

T

A

F

D

D

I

I

L

L

E
|
E

V

W

R
|
R

L

V

D

D

-

H

L

F

L

M

G

D

I

I

R

A

N

S

P

T

E

Q

S

S

-

V

-

L

-

T

A

A

K

R

I

V

I

I

R

R

E

D

I

A

K

M

S

P

E

D

T

-

G

-

L

I

P

P

V

L

L

L

V

F

T

T

N

F

R

R

S

S

V

A

A

K

E

E

G

G

K

-

W

-

E

E

G

Q

K

T

E

I

V

T

D

T

R

Q

T

H

E

Y

L

L

L

T

V

L

A

N

L

R

L

A

S

A

L

I

K

D

D

S

G

G

-

L

P

V

D

D

A

M

V

I

D

D

I

L

E

E

L

L

S

F

A

T

S

G

R

D

E

A

D

D

R

V

D

K

K

A

V

T

I

V

K

D

A

Y

A

A

K

H

A

A

H

H

G

N

K

V

T

Y

V

V

I

V

I

M

S

S

S

N

H
|
H

D

D

F

F

S

H

K

Q

T

T

P

P

S

S

P

A

Q

E

E

E

M

M

T

V

A

L

T

R

L

L

A

R

E

K

M

M

F

Q

L

A

A

L

E

G

A

A

D

D

I

I

A

P

K
|
K

I

I

A

A

V

V

M

M

P

P

G

Q

S

S

M

K

E

H

D

D

V

V

L

L

N

T

L

L

K

T

V

A

T

T

L

L

E

E

F

M

K

Q

N

Q

-

H

-

Y

T

A

G

D

K

R

T

P

V

V

C

I

T

T

I

M

A

S

M
|
M

G

A

K

K

P

E

G

G

K

V

H

I

T

S

R
|
R

V

L

V

A

A

G

P

E

L

V

Y

F

G

G

S

S

V

A

L

A

T

T

Y
x
F

A

G

S

A

I

V

E

K

S

Q

N

-

A

-

V

A

A

S

A
|
A

P

P

G

G

Q
|
Q

L

I

P

A

V

V

D

N

E

D

V

L

K

R

K

S

I

V

M

L

E

M

M

I

L

L

K

H

binding (1~{S},2~{R},4~{R},5~{S},6~{S})-2,4,5-trihydroxy-7-oxabicyclo[4.1.0]heptane-2-carboxylic acid: E46 (= E39), R48 (= R41), H143 (= H135), K170 (= K162), M205 (= M195), R213 (= R203), F225 (≠ Y215), A233 (= A225), Q236 (= Q228)

8b2bAAA 3-dehydroquinate dehydratase (see paper)
35% identity, 87% coverage: 32:242/242 of query aligns to 39:250/252 of 8b2bAAA

query
sites
8b2bAAA

E

E

K

A

G

T

A

F

D

D

I

I

L

L

E
|
E

V

W

R
|
R

L

V

D

D

-

H

L

F

L

M

G

D

I

I

R

A

N

S

P

T

E

Q

S

S

-

V

-

L

-

T

A

A

K

R

I

V

I

I

R

R

E

D

I

A

K

M

S

P

E

D

T

-

G

-

L

I

P

P

V

L

L

L

V

F

T

T

N

F

R

R

S

S

V

A

A

K

E

E

G

G

K

-

W

-

E

E

G

Q

K

T

E

I

V

T

D

T

R

Q

T

H

E

Y

L

L

L

T

V

L

A

N

L

R

L

A

S

A

L

I

K

D

D

S

G

G

-

L

P

V

D

D

A

M

V

I

D

D

I

L

E

E

L

L

S

F

A

T

S

G

R

D

E

A

D

D

R

V

D

K

K

A

V

T

I

V

K

D

A

Y

A

A

K

H

A

A

H

H

G

N

K

V

T

Y

V

V

I

V

I

M

S

S

S

N

H
|
H

D

D

F

F

S

H

K

Q

T

T

P

P

S

S

P

A

Q

E

E

E

M

M

T

V

A

L

T

R

L

L

A

R

E

K

M

M

F

Q

L

A

A

L

E

G

A

A

D

D

I

I

A

P

K
|
K

I

I

A

A

V

V

M

M

P

P

G

Q

S

S

M

K

E

H

D

D

V

V

L

L

N

T

L

L

K

T

V

A

T

T

L

L

E

E

F

M

K

Q

N

Q

-

H

-

Y

T

A

G

D

K

R

T

P

V

V

C

I

T

T

I

M

A

S

M

M

G

A

K

K

P

E

G

G

K

V

H

I

T

S

R
|
R

V

L

V

A

A

G

P

E

L

V

Y

F

G

G

S

S

V

A

L

A

T

T

Y
x
F

A

G

S

A

I

V

E

K

S

Q

N

-

A

-

V

A

A
x
S

A
|
A

P

P

G

G

Q
|
Q

L

I

P

A

V

V

D

N

E

D

V

L

K

R

K

S

I

V

M

L

E

M

M

I

L

L

K

H

binding (4R,5R)-3-amino-4,5-dihydroxy-cyclohexene-1-carboxylic acid: E46 (= E39), R48 (= R41), H143 (= H135), K170 (= K162), R213 (= R203), F225 (≠ Y215), S232 (≠ A224), A233 (= A225), Q236 (= Q228)

6sfeA Crystal structure of dhq1 from salmonella typhi covalently modified by compound 7 (see paper)
35% identity, 87% coverage: 32:242/242 of query aligns to 39:250/252 of 6sfeA

query
sites
6sfeA

E

E

K

A

G

T

A

F

D

D

I

I

L

L

E
|
E

V

W

R
|
R

L

V

D

D

-

H

L

F

L

M

G

D

I

I

R

A

N

S

P

T

E

Q

S

S

-

V

-

L

-

T

A

A

K

R

I

V

I

I

R

R

E

D

I

A

K

M

S

P

E

D

T

-

G

-

L

I

P

P

V

L

L

L

V

F

T

T

N

F

R
|
R

S

S

V

A

A

K

E
|
E

G

G

K

-

W

-

E

E

G

Q

K

T

E

I

V

T

D

T

R

Q

T

H

E

Y

L

L

L

T

V

L

A

N

L

R

L

A

S

A

L

I

K

D

D

S

G

G

-

L

P

V

D

D

A

M

V

I

D

D

I

L

E

E

L

L

S

F

A

T

S

G

R

D

E

A

D

D

R

V

D

K

K

A

V

T

I

V

K

D

A

Y

A

A

K

H

A

A

H

H

G

N

K

V

T

Y

V

V

I

V

I

M

S

S

S

N

H
|
H

D

D

F

F

S

H

K

Q

T

T

P

P

S

S

P

A

Q

E

E

E

M

M

T

V

A

L

T

R

L

L

A

R

E

K

M

M

F

Q

L

A

A

L

E

G

A

A

D

D

I

I

A

P

K
|
K

I

I

A

A

V

V

M

M

P

P

G

Q

S

S

M

K

E

H

D

D

V

V

L

L

N

T

L

L

K

T

V

A

T

T

L

L

E

E

F

M

K

Q

N

Q

-

H

-

Y

T

A

G

D

K

R

T

P

V

V

C

I

T

T

I

M

A

S

M

M

G

A

K

K

P

E

G

G

K

V

H

I

T

S

R
|
R

V

L

V

A

A

G

P

E

L

V

Y

F

G

G

S

S

V

A

L

A

T

T

Y
x
F

A

G

S

A

I

V

E

K

S

Q

N

-

A

-

V

A

A
x
S

A
|
A

P

P

G

G

Q
|
Q

L

I

P

A

V

V

D

N

E

D

V

L

K

R

K

S

I

V

M

L

E

M

M

I

L

L

K

H

active site: E86 (= E77), H143 (= H135), K170 (= K162)
binding (1~{S},3~{S},4~{S},5~{R})-3-(aminomethyl)-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E46 (= E39), R48 (= R41), R82 (= R73), H143 (= H135), K170 (= K162), R213 (= R203), F225 (≠ Y215), S232 (≠ A224), A233 (= A225), Q236 (= Q228)

6h5jA Crystal structure of dhq1 from salmonella typhi covalently modified by ligand 4
35% identity, 87% coverage: 32:242/242 of query aligns to 39:250/252 of 6h5jA

query
sites
6h5jA

E

E

K

A

G

T

A

F

D

D

I

I

L

L

E
|
E

V

W

R
|
R

L

V

D

D

-

H

L

F

L

M

G

D

I

I

R

A

N

S

P

T

E

Q

S

S

-

V

-

L

-

T

A

A

K

R

I

V

I

I

R

R

E

D

I

A

K

M

S

P

E

D

T

-

G

-

L

I

P

P

V

L

L

L

V

F

T

T

N

F

R
|
R

S

S

V

A

A

K

E
|
E

G

G

K

-

W

-

E

E

G

Q

K

T

E

I

V

T

D

T

R

Q

T

H

E

Y

L

L

L

T

V

L

A

N

L

R

L

A

S

A

L

I

K

D

D

S

G

G

-

L

P

V

D

D

A

M

V

I

D

D

I

L

E

E

L

L

S

F

A

T

S

G

R

D

E

A

D

D

R

V

D

K

K

A

V

T

I

V

K

D

A

Y

A

A

K

H

A

A

H

H

G

N

K

V

T

Y

V

V

I

V

I

M

S

S

S

N

H
|
H

D

D

F

F

S

H

K

Q

T

T

P

P

S

S

P

A

Q

E

E

E

M

M

T

V

A

L

T

R

L

L

A

R

E

K

M

M

F

Q

L

A

A

L

E

G

A

A

D

D

I

I

A

P

K
|
K

I

I

A

A

V

V

M

M

P

P

G

Q

S

S

M

K

E

H

D

D

V

V

L

L

N

T

L

L

K

T

V

A

T

T

L

L

E

E

F

M

K

Q

N

Q

-

H

-

Y

T

A

G

D

K

R

T

P

V

V

C

I

T

T

I

M

A

S

M

M

G

A

K

K

P

E

G

G

K

V

H

I

T

S

R
|
R

V

L

V

A

A

G

P

E

L

V

Y

F

G

G

S

S

V

A

L

A

T

T

Y
x
F

A

G

S

A

I

V

E

K

S

Q

N

-

A

-

V

A

A
x
S

A
|
A

P

P

G

G

Q
|
Q

L

I

P

A

V

V

D

N

E

D

V

L

K

R

K

S

I

V

M

L

E

M

M

I

L

L

K

H

active site: E86 (= E77), H143 (= H135), K170 (= K162)
binding (3~{R})-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E46 (= E39), R48 (= R41), R82 (= R73), H143 (= H135), K170 (= K162), R213 (= R203), F225 (≠ Y215), S232 (≠ A224), A233 (= A225), Q236 (= Q228)

6h5gA Crystal structure of dhq1 from salmonella typhi covalently modified by ligand 3
35% identity, 87% coverage: 32:242/242 of query aligns to 39:250/252 of 6h5gA

query
sites
6h5gA

E

E

K

A

G

T

A

F

D

D

I

I

L

L

E
|
E

V

W

R
|
R

L

V

D

D

-

H

L

F

L

M

G

D

I

I

R

A

N

S

P

T

E

Q

S

S

-

V

-

L

-

T

A

A

K

R

I

V

I

I

R

R

E

D

I

A

K

M

S

P

E

D

T

-

G

-

L

I

P

P

V

L

L

L

V

F

T

T

N

F

R
|
R

S

S

V

A

A

K

E
|
E

G

G

K

-

W

-

E

E

G

Q

K

T

E

I

V

T

D

T

R

Q

T

H

E

Y

L

L

L

T

V

L

A

N

L

R

L

A

S

A

L

I

K

D

D

S

G

G

-

L

P

V

D

D

A

M

V

I

D

D

I

L

E

E

L

L

S

F

A

T

S

G

R

D

E

A

D

D

R

V

D

K

K

A

V

T

I

V

K

D

A

Y

A

A

K

H

A

A

H

H

G

N

K

V

T

Y

V

V

I

V

I

M

S

S

S

N

H
|
H

D

D

F

F

S

H

K

Q

T

T

P

P

S

S

P

A

Q

E

E

E

M

M

T

V

A

L

T

R

L

L

A

R

E

K

M

M

F

Q

L

A

A

L

E

G

A

A

D

D

I

I

A

P

K
|
K

I

I

A

A

V

V

M

M

P

P

G

Q

S

S

M

K

E

H

D

D

V

V

L

L

N

T

L

L

K

T

V

A

T

T

L

L

E

E

F

M

K

Q

N

Q

-

H

-

Y

T

A

G

D

K

R

T

P

V

V

C

I

T

T

I
x
M

A

S

M

M

G

A

K

K

P

E

G

G

K

V

H

I

T

S

R
|
R

V

L

V

A

A

G

P

E

L

V

Y

F

G

G

S

S

V

A

L

A

T

T

Y
x
F

A

G

S

A

I

V

E

K

S

Q

N

-

A

-

V

A

A
x
S

A
|
A

P

P

G

G

Q
|
Q

L

I

P

A

V

V

D

N

E

D

V

L

K

R

K

S

I

V

M

L

E

M

M

I

L

L

K

H

active site: E86 (= E77), H143 (= H135), K170 (= K162)
binding (1~{R},3~{S},4~{R},5~{R})-3-methyl-4,5-bis(hydroxyl)cyclohexane-1-carboxylic acid: E46 (= E39), R48 (= R41), R82 (= R73), K170 (= K162), M203 (≠ I193), R213 (= R203), F225 (≠ Y215), S232 (≠ A224), A233 (= A225), Q236 (= Q228)

6h5cA Crystal structure of dhq1 from salmonella typhi covalently modified by ligand 1
35% identity, 87% coverage: 32:242/242 of query aligns to 39:250/252 of 6h5cA

query
sites
6h5cA

E

E

K

A

G

T

A

F

D

D

I

I

L

L

E
|
E

V

W

R
|
R

L

V

D

D

-

H

L

F

L

M

G

D

I

I

R

A

N

S

P

T

E

Q

S

S

-

V

-

L

-

T

A

A

K

R

I

V

I

I

R

R

E

D

I

A

K

M

S

P

E

D

T

-

G

-

L

I

P

P

V

L

L

L

V

F

T

T

N

F

R
|
R

S

S

V

A

A

K

E
|
E

G

G

K

-

W

-

E

E

G

Q

K

T

E

I

V

T

D

T

R

Q

T

H

E

Y

L

L

L

T

V

L

A

N

L

R

L

A

S

A

L

I

K

D

D

S

G

G

-

L

P

V

D

D

A

M

V

I

D

D

I

L

E

E

L

L

S

F

A

T

S

G

R

D

E

A

D

D

R

V

D

K

K

A

V

T

I

V

K

D

A

Y

A

A

K

H

A

A

H

H

G

N

K

V

T

Y

V

V

I

V

I

M

S

S

S

N

H
|
H

D

D

F

F

S

H

K

Q

T

T

P

P

S

S

P

A

Q

E

E

E

M

M

T

V

A

L

T

R

L

L

A

R

E

K

M

M

F

Q

L

A

A

L

E

G

A

A

D

D

I

I

A

P

K
|
K

I

I

A

A

V

V

M

M

P

P

G

Q

S

S

M

K

E

H

D

D

V

V

L

L

N

T

L

L

K

T

V

A

T

T

L

L

E

E

F

M

K

Q

N

Q

-

H

-

Y

T

A

G

D

K

R

T

P

V

V

C

I

T

T

I

M

A

S

M

M

G

A

K

K

P

E

G

G

K

V

H

I

T

S

R
|
R

V

L

V

A

A

G

P

E

L

V

Y

F

G

G

S

S

V

A

L

A

T

T

Y
x
F

A

G

S

A

I

V

E

K

S

Q

N

-

A

-

V

A

A
x
S

A
|
A

P

P

G

G

Q
|
Q

L

I

P

A

V

V

D

N

E

D

V

L

K

R

K

S

I

V

M

L

E

M

M

I

L

L

K

H

active site: E86 (= E77), H143 (= H135), K170 (= K162)
binding (1~{S},3~{R},4~{S},5~{R})-3-methyl-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic Acid: E46 (= E39), R48 (= R41), R82 (= R73), H143 (= H135), K170 (= K162), R213 (= R203), F225 (≠ Y215), S232 (≠ A224), A233 (= A225), Q236 (= Q228)

4cnpA Structure of the salmonella typhi type i dehydroquinase inhibited by a 3-epiquinic acid derivative
35% identity, 87% coverage: 32:242/242 of query aligns to 39:250/252 of 4cnpA

query
sites
4cnpA

E

E

K

A

G

T

A

F

D

D

I

I

L

L

E
|
E

V

W

R
|
R

L

V

D

D

-

H

L

F

L

M

G

D

I

I

R

A

N

S

P

T

E

Q

S

S

-

V

-

L

-

T

A

A

K

R

I

V

I

I

R

R

E

D

I

A

K

M

S

P

E

D

T

-

G

-

L

I

P

P

V

L

L

L

V

F

T

T

N

F

R
|
R

S

S

V

A

A

K

E
|
E

G

G

K

-

W

-

E

E

G

Q

K

T

E

I

V

T

D

T

R

Q

T

H

E

Y

L

L

L

T

V

L

A

N

L

R

L

A

S

A

L

I

K

D

D

S

G

G

-

L

P

V

D

D

A

M

V

I

D

D

I

L

E

E

L

L

S

F

A

T

S

G

R

D

E

A

D

D

R

V

D

K

K

A

V

T

I

V

K

D

A

Y

A

A

K

H

A

A

H

H

G

N

K

V

T

Y

V

V

I

V

I

M

S

S

S

N

H
|
H

D

D

F

F

S

H

K

Q

T

T

P

P

S

S

P

A

Q

E

E

E

M

M

T

V

A

L

T

R

L

L

A

R

E

K

M

M

F

Q

L

A

A

L

E

G

A

A

D

D

I

I

A

P

K
|
K

I

I

A

A

V

V

M

M

P

P

G

Q

S

S

M

K

E

H

D

D

V

V

L

L

N

T

L

L

K

T

V

A

T

T

L

L

E

E

F

M

K

Q

N

Q

-

H

-

Y

T

A

G

D

K

R

T

P

V

V

C

I

T

T

I
x
M

A

S

M

M

G

A

K

K

P

E

G

G

K

V

H

I

T

S

R
|
R

V

L

V

A

A

G

P

E

L

V

Y

F

G

G

S

S

V

A

L

A

T

T

Y
x
F

A

G

S

A

I

V

E

K

S

Q

N

-

A

-

V

A

A
x
S

A
|
A

P

P

G

G

Q
|
Q

L

I

P

A

V

V

D

N

E

D

V

L

K

R

K

S

I

V

M

L

E

M

M

I

L

L

K

H

active site: E86 (= E77), H143 (= H135), K170 (= K162)
binding (2s)-2-hydroxy-3-epiquinic acid: E46 (= E39), R48 (= R41), R82 (= R73), K170 (= K162), M203 (≠ I193), R213 (= R203), F225 (≠ Y215), S232 (≠ A224), A233 (= A225), Q236 (= Q228)

P24670 3-dehydroquinate dehydratase; 3-dehydroquinase; Type I DHQase; Type I dehydroquinase; DHQ1; EC 4.2.1.10 from Salmonella typhi (see 3 papers)
35% identity, 87% coverage: 32:242/242 of query aligns to 39:250/252 of P24670

query
sites
P24670

E

E

K

A

G

T

A

F

D

D

I

I

L

L

E
|
E

V
x
W

R
|
R

L

V

D

D

-

H

L

F

L

M

G

D

I

I

R

A

N

S

P

T

E

Q

S

S

-

V

-

L

-

T

A

A

K

R

I

V

I

I

R

R

E

D

I

A

K

M

S

P

E

D

T

-

G

-

L

I

P

P

V

L

L

L

V

F

T

T

N

F

R
|
R

S

S

V

A

A

K

E

E

G

G

K

-

W

-

E

E

G

Q

K

T

E

I

V

T

D

T

R

Q

T

H

E

Y

L

L

L

T

V

L

A

N

L

R

L

A

S

A

L

I

K

D

D

S

G

G

-

L

P

V

D

D

A

M

V

I

D

D

I

L

E

E

L

L

S

F

A

T

S

G

R

D

E

A

D

D

R

V

D

K

K

A

V

T

I

V

K

D

A

Y

A

A

K

H

A

A

H

H

G

N

K

V

T

Y

V

V

I

V

I

M

S

S

S

N

H

H

D

D

F

F

S

H

K

Q

T

T

P

P

S

S

P

A

Q

E

E

E

M

M

T

V

A

L

T

R

L

L

A

R

E

K

M

M

F

Q

L

A

A

L

E

G

A

A

D

D

I

I

A

P

K
|
K

I

I

A

A

V

V

M

M

P

P

G

Q

S

S

M

K

E

H

D

D

V

V

L

L

N

T

L

L

K

T

V

A

T

T

L

L

E

E

F

M

K

Q

N

Q

-

H

-

Y

T

A

G

D

K

R

T

P

V

V

C

I

T

T

I

M

A

S

M

M

G

A

K

K

P

E

G

G

K

V

H

I

T

S

R
|
R

V

L

V

A

A

G

P

E

L

V

Y

F

G

G

S

S

V

A

L

A

T

T

Y

F

A

G

S

A

I

V

E

K

S

Q

N

-

A

-

V

A

A
x
S

A

A

P

P

G

G

Q
|
Q

L

I

P

A

V

V

D

N

E

D

V

L

K

R

K

S

I

V

M

L

E

M

M

I

L

L

K

H

EWR 46:48 (≠ EVR 39:41) binding
R82 (= R73) binding
K170 (= K162) active site, Schiff-base intermediate with substrate
R213 (= R203) binding
S232 (≠ A224) binding
Q236 (= Q228) binding

Sites not aligning to the query:

21 binding

4clmB Structure of salmonella typhi type i dehydroquinase irreversibly inhibited with a 1,3,4-trihydroxyciclohexane-1-carboxylic acid derivative (see paper)
35% identity, 87% coverage: 32:242/242 of query aligns to 38:249/251 of 4clmB

query
sites
4clmB

E

E

K

A

G

T

A

F

D

D

I

I

L

L

E
|
E

V

W

R
|
R

L

V

D

D

-

H

L

F

L

M

G

D

I

I

R

A

N

S

P

T

E

Q

S

S

-

V

-

L

-

T

A

A

K

R

I

V

I

I

R

R

E

D

I

A

K

M

S

P

E

D

T

-

G

-

L

I

P

P

V

L

L

L

V

F

T

T

N

F

R
|
R

S

S

V

A

A

K

E
|
E

G

G

K

-

W

-

E

E

G

Q

K

T

E

I

V

T

D

T

R

Q

T

H

E

Y

L

L

L

T

V

L

A

N

L

R

L

A

S

A

L

I

K

D

D

S

G

G

-

L

P

V

D

D

A

M

V

I

D

D

I

L

E

E

L

L

S

F

A

T

S

G

R

D

E

A

D

D

R

V

D

K

K

A

V

T

I

V

K

D

A

Y

A

A

K

H

A

A

H

H

G

N

K

V

T

Y

V

V

I

V

I

M

S

S

S

N

H
|
H

D

D

F

F

S

H

K

Q

T

T

P

P

S

S

P

A

Q

E

E

E

M

M

T

V

A

L

T

R

L

L

A

R

E

K

M

M

F

Q

L

A

A

L

E

G

A

A

D

D

I

I

A

P

K
|
K

I

I

A

A

V

V

M

M

P

P

G

Q

S

S

M

K

E

H

D

D

V

V

L

L

N

T

L

L

K

T

V

A

T

T

L

L

E

E

F

M

K

Q

N

Q

-

H

-

Y

T

A

G

D

K

R

T

P

V

V

C

I

T

T

I

M

A

S

M
|
M

G

A

K

K

P

E

G

G

K

V

H

I

T

S

R
|
R

V

L

V

A

A

G

P

E

L

V

Y

F

G

G

S

S

V

A

L

A

T

T

Y
x
F

A

G

S

A

I

V

E

K

S

Q

N

-

A

-

V

A

A
x
S

A
|
A

P

P

G

G

Q
|
Q

L

I

P

A

V

V

D

N

E

D

V

L

K

R

K

S

I

V

M

L

E

M

M

I

L

L

K

H

active site: E85 (= E77), H142 (= H135), K169 (= K162)
binding (1~{S},3~{S},4~{R},5~{R})-3-methyl-1,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E45 (= E39), R47 (= R41), R81 (= R73), K169 (= K162), M204 (= M195), R212 (= R203), F224 (≠ Y215), S231 (≠ A224), A232 (= A225), Q235 (= Q228)

4uioA Structure of the salmonella typhi type i dehydroquinase covalently inhibited by a 3-dehydroquinic acid derivative (see paper)
35% identity, 87% coverage: 32:242/242 of query aligns to 37:248/250 of 4uioA

query
sites
4uioA

E

E

K

A

G

T

A

F

D

D

I

I

L

L

E
|
E

V

W

R
|
R

L

V

D

D

-

H

L

F

L

M

G

D

I

I

R

A

N

S

P

T

E

Q

S

S

-

V

-

L

-

T

A

A

K

R

I

V

I

I

R

R

E

D

I

A

K

M

S

P

E

D

T

-

G

-

L

I

P

P

V

L

L

L

V

F

T

T

N

F

R
|
R

S

S

V

A

A

K

E
|
E

G

G

K

-

W

-

E

E

G

Q

K

T

E

I

V

T

D

T

R

Q

T

H

E

Y

L

L

L

T

V

L

A

N

L

R

L

A

S

A

L

I

K

D

D

S

G

G

-

L

P

V

D

D

A

M

V

I

D

D

I

L

E

E

L

L

S

F

A

T

S

G

R

D

E

A

D

D

R

V

D

K

K

A

V

T

I

V

K

D

A

Y

A

A

K

H

A

A

H

H

G

N

K

V

T

Y

V

V

I

V

I

M

S

S

S

N

H
|
H

D

D

F

F

S

H

K

Q

T

T

P

P

S

S

P

A

Q

E

E

E

M

M

T

V

A

L

T

R

L

L

A

R

E

K

M

M

F

Q

L

A

A

L

E

G

A

A

D

D

I

I

A

P

K
|
K

I

I

A

A

V

V

M

M

P

P

G

Q

S

S

M

K

E

H

D

D

V

V

L

L

N

T

L

L

K

T

V

A

T

T

L

L

E

E

F

M

K

Q

N

Q

-

H

-

Y

T

A

G

D

K

R

T

P

V

V

C

I

T

T

I

M

A

S

M
|
M

G

A

K

K

P

E

G

G

K

V

H

I

T

S

R
|
R

V

L

V

A

A

G

P

E

L

V

Y

F

G

G

S

S

V

A

L

A

T

T

Y
x
F

A

G

S

A

I

V

E

K

S

Q

N

-

A

-

V

A

A

S

A
|
A

P

P

G

G

Q
|
Q

L

I

P

A

V

V

D

N

E

D

V

L

K

R

K

S

I

V

M

L

E

M

M

I

L

L

K

H

active site: E84 (= E77), H141 (= H135), K168 (= K162)
binding (1~{R},3~{R},4~{S},5~{R})-3-methyl-1,3,4,5-tetrakis(oxidanyl)cyclohexane-1-carboxylic acid: E44 (= E39), R46 (= R41), R80 (= R73), H141 (= H135), K168 (= K162), M203 (= M195), R211 (= R203), F223 (≠ Y215), A231 (= A225), Q234 (= Q228)

4cnoA Structure of the salmonella typhi type i dehydroquinase inhibited by a 3-dehydroquinic acid derivative (see paper)
35% identity, 87% coverage: 32:242/242 of query aligns to 38:245/247 of 4cnoA

query
sites
4cnoA

E

E

K

A

G

T

A

F

D

D

I

I

L

L

E
|
E

V

W

R
|
R

L

V

D

D

-

H

L

F

L

M

G

D

I

I

R

A

N

S

P

T

E

Q

S

S

-

V

-

L

-

T

A

A

K

R

I

V

I

I

R

R

E

D

I

A

K

M

S

P

E

D

T

-

G

-

L

I

P

P

V

L

L

L

V

F

T

T

N

F

R

R

S

S

V

A

A

K

E
|
E

G

G

K

-

W

-

E

E

G

Q

K

T

E

I

V

T

D

T

R

Q

T

H

E

Y

L

L

L

T

V

L

A

N

L

R

L

A

S

A

L

I

K

D

D

S

G

G

-

L

P

V

D

D

A

M

V

I

D

D

I

L

E

E

L

L

S

F

A

T

S

G

R

D

E

A

D

D

R

V

D

K

K

A

V

T

I

V

K

D

A

Y

A

A

K

H

A

A

H

H

G

N

K

V

T

Y

V

V

I

V

I

M

S

S

S

N

H
|
H

D

D

F

F

S

H

K

Q

T

T

P

P

S

S

P

A

Q

E

E

E

M

M

T

V

A

L

T

R

L

L

A

R

E

K

M

M

F

Q

L

A

A

L

E

G

A

A

D

D

I

I

A

P

K
|
K

I

I

A

A

V

V

M

M

P

P

G

Q

S

S

M

K

E

H

D

D

V

V

L

L

N

T

L

L

K

T

V

A

T

T

L

L

E

E

F

M

K

Q

N

Q

-

H

-

Y

T

A

G

D

K

R

T

P

V

V

C

I

T

T

I

M

A

S

M

M

G

A

K

K

P

E

G

G

K

V

H

I

T

S

R
|
R

V

L

V

A

A

G

P

E

L

V

Y

F

G

G

S

S

V

A

L

A

T

T

Y
x
F

A

G

S

A

I

V

E

K

S

-

N

-

A

-

V

-

A

-

P

P

G

G

Q
|
Q

L

I

P

A

V

V

D

N

E

D

V

L

K

R

K

S

I

V

M

L

E

M

M

I

L

L

K

H

active site: E85 (= E77), H142 (= H135), K169 (= K162)
binding (2r)-2-methyl-3-dehydroquinic acid: E45 (= E39), R47 (= R41), R212 (= R203), F224 (≠ Y215), Q231 (= Q228)

Sites not aligning to the query:

binding (2r)-2-methyl-3-dehydroquinic acid: 20

Q9SQT8 Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic; DHQ-SDH protein; DHQase-SORase; Protein EMBRYO DEFECTIVE 3004; EC 4.2.1.10; EC 1.1.1.25 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
35% identity, 93% coverage: 3:228/242 of query aligns to 83:304/603 of Q9SQT8

query
sites
Q9SQT8

Q

E

I

I

G

G

P

S

F

H

D

D

L

I

E

V

K

K

K

N

-

P

-

S

-

L

-

I

-

C

A

A

A

P

V

V

V

M

A

A

V

D

I

S

L

I

E

D

K

K

P

M

L

V

E

I

T

E

S

T

K

S

K

K

A

A

A

H

E

E

K

L

G

G

A

A

D

D

I

L

L

V

E
|
E

V

I

R
|
R

L

L

D

D

L

W

L

L

G

K

I

D

R

F

N

N

P

P

E

L

S

E

A

D

A

L

K

K

I

T

I

I

R

-

E

-

I

I

K

K

S

-

E

K

T

S

G

P

L

L

P

P

V

T

L

L

V

F

T

T

N

Y

R
|
R

S

P

V

K

A

W

E

E

G

G

K

Q

W

Y

E

E

G

G

K

D

E

E

V

N

D

E

R

R

T

R

E

D

L

V

L

L

V

-

A

-

L

R

L

L

S

A

L

M

K

E

D

L

G

G

P

A

D

D

A

Y

V

I

D

D

I

V

E

E

L

L

S

Q

A

V

S

A

R

S

E

E

D

-

R

F

D

I

K

K

V

S

I

I

K

D

A

G

A

K

K

K

A

P

H

G

G

K

K

F

T

K

V

V

I

I

I

V

S

S

H

H

D

N

F

Y

S

Q

K

N

T

T

P

P

S

S

P

V

Q

E

E

D

M

L

T

D

A

G

T

L

L

V

A

A

E

R

M

I

F

Q

L

Q

A

T

E

G

A

A

D

D

I

I

A

V

K
|
K

I

I

A

A

V

T

M

T

P

A

G

V

S

D

M

I

E

A

D

D

V

V

L

A

N

R

L

M

L

F

K

H

V

I

T

T

L

-

E

-

F

-

K

-

N

-

T

S

G

K

K

A

T

Q

V

V

C

P

T

T

I

I

A

G

-

L

-

V

M

M

G

G

K

E

P

R

G

G

K

L

H

M

T

S

R
|
R

V

I

V

L

A

C

P

S

L

K

Y

F

G

G

S

G

V

Y

L

L

T

T

Y

F

A

G

S

T

I

L

E

D

S

S

N

S

A

K

V

V

A
x
S

A

A

P

P

G

G

Q
|
Q

E124 (= E39) binding
R126 (= R41) binding
R155 (= R73) binding
K241 (= K162) binding
R279 (= R203) binding
S300 (≠ A224) binding
Q304 (= Q228) binding

Sites not aligning to the query:

336 binding ; S→A: 13-fold decrease in substrate affinity but almost no change in activity.
338 binding ; S→A: 10-fold decrease in activity, and 9-fold decrease in substrate affinity.
381 binding
385 binding ; K→A: Strongly reduced shikimate dehydrogenase activity, but minor change in substrate affinity.; K→N: Strongly reduced shikimate dehydrogenase activity, but no change in substrate affinity.
406 binding
423 binding ; D→A: Loss of shikimate dehydrogenase activity.; D→N: Reduced shikimate dehydrogenase activity, but no change in substrate affinity.
461 binding
463 binding
464 binding
483 binding
485 binding
488 binding
525 binding
548 binding
550 binding ; mutation Y->F,A: 100-fold decrease in activity, and 2-fold decrease in substrate affinity.
571 binding
578 binding
582 binding

6bmqA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase (t381g mutant) in complex with tartrate and shikimate (see paper)
35% identity, 89% coverage: 13:228/242 of query aligns to 9:215/498 of 6bmqA

query
sites
6bmqA

A

A

A

P

V

V

V

M

A

A

V

D

I

S

L

I

E

D

K

K

P

M

L

V

E

I

T

E

S

T

K

S

K

K

A

A

A

H

E

E

K

L

G

G

A

A

D

D

I

L

L

V

E

E

V

I

R

R

L

L

D

D

L

W

L

L

G

K

I

D

R

F

N

N

P

P

-

L

E

E

S

D

A

L

A

K

K

T

I

I

R

K

E

K

I

-

K

-

S

-

E

-

T

S

G

P

L

L

P

P

V

T

L

L

V

F

T

T

N

Y

R

R

S

P

V

K

A

W

E
|
E

G

G

K

Q

W

Y

E

E

G

G

K

D

E

E

V

N

D

E

R

R

T

R

E

D

L

V

L

L

V

-

A

-

L

R

L

L

S

A

L

M

K

E

D

L

G

G

P

A

D

D

A

Y

V

I

D

D

I

V

E

E

L

L

S

Q

A

V

S

A

R

S

E

E

D

-

R

F

D

I

K

K

V

S

I

I

K

D

A

G

A

K

K

K

A

P

H

G

G

K

K

F

T

K

V

V

I

I

I

V

S

S

H
|
H

D

N

F

Y

S

Q

K

N

T

T

P

P

S

S

P

V

Q

E

E

D

M

L

T

D

A

G

T

L

L

V

A

A

E

R

M

I

F

Q

L

Q

A

T

E

G

A

A

D

D

I

I

A

V

K
|
K

I

I

A

A

V

T

M

T

P

A

G

V

S

D

M

I

E

A

D

D

V

V

L

A

N

R

L

M

L

F

K

H

V

I

T

T

L

-

E

-

F

-

K

-

N

-

T

S

G

K

K

A

T

Q

V

V

C

P

T

T

I

I

A

G

-

L

-

V

M

M

G

G

K

E

P

R

G

G

K

L

H

M

T

S

R

R

V

I

V

L

A

C

P

S

L

K

Y

F

G

G

S

G

V

Y

L

L

T

T

Y

F

A

G

S

T

I

L

E

D

S

S

N

S

A

K

V

V

A

S

A

A

P

P

G

G

Q

Q

active site: E70 (= E77), H125 (= H135), K152 (= K162)

Sites not aligning to the query:

binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: 247, 249, 291, 296, 317, 334, 436, 464

2gptA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (see paper)
35% identity, 89% coverage: 13:228/242 of query aligns to 9:215/498 of 2gptA

query
sites
2gptA

A

A

A

P

V

V

V

M

A

A

V

D

I

S

L

I

E

D

K

K

P

M

L

V

E

I

T

E

S

T

K

S

K

K

A

A

A

H

E

E

K

L

G

G

A

A

D

D

I

L

L

V

E

E

V

I

R

R

L

L

D

D

L

W

L

L

G

K

I

D

R

F

N

N

P

P

-

L

E

E

S

D

A

L

A

K

K

T

I

I

R

K

E

K

I

-

K

-

S

-

E

-

T

S

G

P

L

L

P

P

V

T

L

L

V

F

T

T

N

Y

R

R

S

P

V

K

A

W

E
|
E

G

G

K

Q

W

Y

E

E

G

G

K

D

E

E

V

N

D

E

R

R

T

R

E

D

L

V

L

L

V

-

A

-

L

R

L

L

S

A

L

M

K

E

D

L

G

G

P

A

D

D

A

Y

V

I

D

D

I

V

E

E

L

L

S

Q

A

V

S

A

R

S

E

E

D

-

R

F

D

I

K

K

V

S

I

I

K

D

A

G

A

K

K

K

A

P

H

G

G

K

K

F

T

K

V

V

I

I

I

V

S

S

H
|
H

D

N

F

Y

S

Q

K

N

T

T

P

P

S

S

P

V

Q

E

E

D

M

L

T

D

A

G

T

L

L

V

A

A

E

R

M

I

F

Q

L

Q

A

T

E

G

A

A

D

D

I

I

A

V

K
|
K

I

I

A

A

V

T

M

T

P

A

G

V

S

D

M

I

E

A

D

D

V

V

L

A

N

R

L

M

L

F

K

H

V

I

T

T

L

-

E

-

F

-

K

-

N

-

T

S

G

K

K

A

T

Q

V

V

C

P

T

T

I

I

A

G

-

L

-

V

M

M

G

G

K

E

P

R

G

G

K

L

H

M

T

S

R

R

V

I

V

L

A

C

P

S

L

K

Y

F

G

G

S

G

V

Y

L

L

T

T

Y

F

A

G

S

T

I

L

E

D

S

S

N

S

A

K

V

V

A

S

A

A

P

P

G

G

Q

Q

active site: E70 (= E77), H125 (= H135), K152 (= K162)

Sites not aligning to the query:

binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: 239, 247, 249, 292, 296, 317, 334, 436, 464, 468

2o7qA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
35% identity, 89% coverage: 13:228/242 of query aligns to 9:215/501 of 2o7qA

query
sites
2o7qA

A

A

A

P

V

V

V

M

A

A

V

D

I

S

L

I

E

D

K

K

P

M

L

V

E

I

T

E

S

T

K

S

K

K

A

A

A

H

E

E

K

L

G

G

A

A

D

D

I

L

L

V

E
|
E

V

I

R

R

L

L

D

D

L

W

L

L

G

K

I

D

R

F

N

N

P

P

-

L

E

E

S

D

A

L

A

K

K

T

I

I

R

K

E

K

I

-

K

-

S

-

E

-

T

S

G

P

L

L

P

P

V

T

L

L

V

F

T

T

N

Y

R

R

S

P

V

K

A

W

E
|
E

G

G

K

Q

W

Y

E

E

G

G

K

D

E

E

V

N

D

E

R

R

T

R

E

D

L

V

L

L

V

-

A

-

L

R

L

L

S

A

L

M

K

E

D

L

G

G

P

A

D

D

A

Y

V

I

D

D

I

V

E

E

L

L

S

Q

A

V

S

A

R

S

E

E

D

-

R

F

D

I

K

K

V

S

I

I

K

D

A

G

A

K

K

K

A

P

H

G

G

K

K

F

T

K

V

V

I

I

I

V

S

S

H
|
H

D

N

F

Y

S

Q

K

N

T

T

P

P

S

S

P

V

Q

E

E

D

M

L

T

D

A

G

T

L

L

V

A

A

E

R

M

I

F

Q

L

Q

A

T

E

G

A

A

D

D

I

I

A

V

K
|
K

I

I

A

A

V

T

M

T

P

A

G

V

S

D

M

I

E

A

D

D

V

V

L

A

N

R

L

M

L

F

K

H

V

I

T

T

L

-

E

-

F

-

K

-

N

-

T

S

G

K

K

A

T

Q

V

V

C

P

T

T

I

I

A

G

-

L

-

V

M

M

G

G

K

E

P

R

G

G

K

L

H

M

T

S

R
|
R

V

I

V

L

A

C

P

S

L

K

Y

F

G

G

S

G

V

Y

L

L

T

T

Y
x
F

A

G

S

T

I

L

E

D

S

S

N

S

A

K

V

V

A
x
S

A
|
A

P

P

G

G

Q
|
Q

active site: E70 (= E77), H125 (= H135), K152 (= K162)
binding 3-dehydroshikimate: E35 (= E39), K152 (= K162), R190 (= R203), F202 (≠ Y215), S211 (≠ A224), A212 (= A225), Q215 (= Q228)

Sites not aligning to the query:

binding 3-dehydroshikimate: 239, 247, 249, 292, 296, 334, 439, 464, 467, 471

2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
35% identity, 89% coverage: 13:228/242 of query aligns to 9:215/500 of 2o7sA

query
sites
2o7sA

A

A

A

P

V

V

V

M

A

A

V

D

I

S

L

I

E

D

K

K

P

M

L

V

E

I

T

E

S

T

K

S

K

K

A

A

A

H

E

E

K

L

G

G

A

A

D

D

I

L

L

V

E
|
E

V

I

R

R

L

L

D

D

L

W

L

L

G

K

I

D

R

F

N

N

P

P

-

L

E

E

S

D

A

L

A

K

K

T

I

I

R

K

E

K

I

-

K

-

S

-

E

-

T

S

G

P

L

L

P

P

V

T

L

L

V

F

T

T

N

Y

R

R

S

P

V

K

A

W

E
|
E

G

G

K

Q

W

Y

E

E

G

G

K

D

E

E

V

N

D

E

R

R

T

R

E

D

L

V

L

L

V

-

A

-

L

R

L

L

S

A

L

M

K

E

D

L

G

G

P

A

D

D

A

Y

V

I

D

D

I

V

E

E

L

L

S

Q

A

V

S

A

R

S

E

E

D

-

R

F

D

I

K

K

V

S

I

I

K

D

A

G

A

K

K

K

A

P

H

G

G

K

K

F

T

K

V

V

I

I

I

V

S

S

H
|
H

D

N

F

Y

S

Q

K

N

T

T

P

P

S

S

P

V

Q

E

E

D

M

L

T

D

A

G

T

L

L

V

A

A

E

R

M

I

F

Q

L

Q

A

T

E

G

A

A

D

D

I

I

A

V

K
|
K

I

I

A

A

V

T

M

T

P

A

G

V

S

D

M

I

E

A

D

D

V

V

L

A

N

R

L

M

L

F

K

H

V

I

T

T

L

-

E

-

F

-

K

-

N

-

T

S

G

K

K

A

T

Q

V

V

C

P

T

T

I

I

A

G

-

L

-

V

M

M

G

G

K

E

P

R

G

G

K

L

H

M

T

S

R
|
R

V

I

V

L

A

C

P

S

L

K

Y

F

G

G

S

G

V

Y

L

L

T

T

Y
x
F

A

G

S

T

I

L

E

D

S

S

N

S

A

K

V

V

A
x
S

A
|
A

P

P

G

G

Q
|
Q

active site: E70 (= E77), H125 (= H135), K152 (= K162)
binding 3-dehydroshikimate: E35 (= E39), K152 (= K162), R190 (= R203), F202 (≠ Y215), S211 (≠ A224), A212 (= A225), Q215 (= Q228)

Sites not aligning to the query:

binding 3-dehydroshikimate: 239, 247, 249, 292, 296, 317, 334, 438, 466, 470
binding nadp nicotinamide-adenine-dinucleotide phosphate: 293, 294, 296, 334, 354, 355, 356, 374, 375, 376, 379, 409, 410, 411, 436, 462, 463

Q186A6 3-dehydroquinate dehydratase; 3-dehydroquinase; Type I DHQase; Type I dehydroquinase; DHQ1; EC 4.2.1.10 from Clostridioides difficile (strain 630) (Peptoclostridium difficile) (see paper)
33% identity, 90% coverage: 24:241/242 of query aligns to 32:250/255 of Q186A6

query
sites
Q186A6

L

I

E

K

T

E

S

A

K

K

K

E

A

L

A

K

E

D

K

A

G

C

A

L

D

D

I

I

L

I

E
|
E

V
x
W

R
|
R

L

V

D

D

L

F

-

E

G

N

I

V

R

E

N

N

P

I

E

K

S

E

A

V

A

K

K

E

I

V

I

L

R

Y

E

E

I

L

K

R

S

S

E

Y

T

I

-

H

G

D

L

I

P

P

V

L

L

L

V

F

T

T

N

F

R
|
R

S

S

V

V

A

V

E

E

G

G

K

E

-

K

-

L

-

I

-

S

-

R

-

D

-

Y

-

T

W

T

E

L

G

N

K

K

E

E

V

I

D

S

R

N

T

T

E

G

L

L

L

V

V

-

A

-

L

-

S

-

L

-

K

-

D

-

G

-

P

-

D

D

A

L

V

I

D

D

I

V

E

E

L

L

S

F

A

M

S

G

R

D

E

E

D

V

R

I

D

D

K

E

V

V

I

V

K

N

A

F

A

A

K

H

A

K

H

K

G

E

K

V

T

K

V

V

I

I

S

S

S

N

H
|
H

D

D

F

F

S

N

K

K

T

T

P

P

S

K

P

K

Q

E

E

E

M

I

T

V

A

S

T

R

L

L

A

C

E

R

M

M

F

Q

L

E

A

L

E

G

A

A

D

D

I

L

A

P

K
|
K

I

I

A

A

V

V

M

M

P

P

G

Q

S

N

M

E

E

K

D

D

V

V

L

L

N

V

L

L

K

E

V

A

T

T

L

N

E

E

-

M

F

F

K

K

-

I

N

Y

T

A

G

D

K

R

T

P

V

I

C

I

T

T

I

M

A

S

M

M

G

S

K

G

P

M

G

G

K

V

H

I

T

S

R
|
R

V

L

V

C

A

G

P

E

L

I

Y

F

G

G

S

S

V

A

L

L

T

T

Y

F

A

G

S

A

I

A

E

K

S

S

N

-

A

-

V

V

A
x
S

A

A

P

P

G

G

Q
|
Q

L

I

P

S

V

F

D

K

E

E

V

L

K

N

K

S

I

V

M

L

E

N

M

L

L

L

EWR 47:49 (≠ EVR 39:41) binding
R83 (= R73) binding
H144 (= H135) active site, Proton donor/acceptor
K171 (= K162) active site, Schiff-base intermediate with substrate
R214 (= R203) binding
S233 (≠ A224) binding
Q237 (= Q228) binding

4h3dB 1.95 angstrom crystal structure of of type i 3-dehydroquinate dehydratase (arod) from clostridium difficile with covalent modified comenic acid.
33% identity, 90% coverage: 24:241/242 of query aligns to 32:250/254 of 4h3dB

query
sites
4h3dB

L

I

E

K

T

E

S

A

K

K

K

E

A

L

A

K

E

D

K

A

G

C

A

L

D

D

I

I

L

I

E

E

V

W

R

R

L

V

D

D

L

F

-

E

G

N

I

V

R

E

N

N

P

I

E

K

S

E

A

V

A

K

K

E

I

V

I

L

R

Y

E

E

I

L

K

R

S

S

E

Y

T

I

-

H

G

D

L

I

P

P

V

L

L

L

V

F

T

T

N

F

R

R

S

S

V

V

A

V

E
|
E

G

G

K

E

-

K

-

L

-

I

-

S

-

R

-

D

-

Y

-

T

W

T

E

L

G

N

K

K

E

E

V

I

D

S

R

N

T

T

E

G

L

L

L

V

V

-

A

-

L

-

S

-

L

-

K

-

D

-

G

-

P

-

D

D

A

L

V

I

D

D

I

V

E

E

L

L

S

F

A

M

S

G

R

D

E

E

D

V

R

I

D

D

K

E

V

V

I

V

K

N

A

F

A

A

K

H

A

K

H

K

G

E

K

V

T

K

V

V

I

I

S

S

S

N

H
|
H

D

D

F

F

S

N

K

K

T

T

P

P

S

K

P

K

Q

E

E

E

M

I

T

V

A

S

T

R

L

L

A

C

E

R

M

M

F

Q

L

E

A

L

E

G

A

A

D

D

I

L

A

P

K
|
K

I

I

A

A

V

V

M

M

P

P

G

Q

S

N

M

E

E

K

D

D

V

V

L

L

N

V

L

L

K

E

V

A

T

T

L

N

E

E

-

M

F

F

K

K

-

I

N

Y

T

A

G

D

K

R

T

P

V

I

C

I

T

T

I
x
M

A

S

M

M

G

S

K

G

P

M

G

G

K

V

H

I

T

S

R
|
R

V

L

V

C

A

G

P

E

L

I

Y

F

G

G

S

S

V

A

L

L

T

T

Y
x
F

A

G

S

A

I

A

E

K

S

S

N

-

A

-

V

V

A

S

A

A

P

P

G

G

Q

Q

L

I

P

S

V

F

D

K

E

E

V

L

K

N

K

S

I

V

M

L

E

N

M

L

L

L

active site: E87 (= E77), H144 (= H135), K171 (= K162)
binding 5-hydroxy-6-methyl-4-oxo-4H-pyran-2-carboxylic acid: H144 (= H135), K171 (= K162), M204 (≠ I193), R214 (= R203), F226 (≠ Y215)

Query Sequence

>WP_011024466.1 NCBI__GCF_000007345.1:WP_011024466.1
MTQIGPFDLEKKAAVVAVILEKPLETSKKAAEKGADILEVRLDLLGIRNPESAAKIIREI
KSETGLPVLVTNRSVAEGGKWEGKEVDRTELLVALLSLKDGPDAVDIELSASREDRDKVI
KAAKAHGKTVIISSHDFSKTPSPQEMTATLAEMFLAEADIAKIAVMPGSMEDVLNLLKVT
LEFKNTGKTVCTIAMGKPGKHTRVVAPLYGSVLTYASIESNAVAAPGQLPVDEVKKIMEM
LK

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