SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_013537267.1 NCBI__GCF_000185805.1:WP_013537267.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

O66440 3-dehydroquinate dehydratase; 3-dehydroquinase; Type I DHQase; Type I dehydroquinase; DHQ1; EC 4.2.1.10 from Aquifex aeolicus (strain VF5) (see paper)
37% identity, 88% coverage: 14:233/249 of query aligns to 3:217/219 of O66440

query
sites
O66440

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R61 (= R72) binding
H116 (= H131) active site, Proton donor/acceptor
K142 (= K158) active site, Schiff-base intermediate with substrate
R180 (= R196) binding

6bmqA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase (t381g mutant) in complex with tartrate and shikimate (see paper)
36% identity, 81% coverage: 28:228/249 of query aligns to 24:224/498 of 6bmqA

query
sites
6bmqA

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active site: E70 (= E76), H125 (= H131), K152 (= K158)

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

2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
36% identity, 81% coverage: 28:228/249 of query aligns to 24:224/500 of 2o7sA

query
sites
2o7sA

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active site: E70 (= E76), H125 (= H131), K152 (= K158)
binding 3-dehydroshikimate: E35 (= E39), K152 (= K158), R190 (= R196), F202 (≠ Y208), S211 (≠ V215), A212 (= A216), Q215 (= Q219)

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

2o7qA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
36% identity, 81% coverage: 28:228/249 of query aligns to 24:224/501 of 2o7qA

query
sites
2o7qA

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active site: E70 (= E76), H125 (= H131), K152 (= K158)
binding 3-dehydroshikimate: E35 (= E39), K152 (= K158), R190 (= R196), F202 (≠ Y208), S211 (≠ V215), A212 (= A216), Q215 (= Q219)

Sites not aligning to the query:

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

2gptA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (see paper)
36% identity, 81% coverage: 28:228/249 of query aligns to 24:224/498 of 2gptA

query
sites
2gptA

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active site: E70 (= E76), H125 (= H131), K152 (= K158)

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

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)
36% identity, 81% coverage: 28:228/249 of query aligns to 113:313/603 of Q9SQT8

query
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Q9SQT8

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G

L

L

F

V

K

A

A

R

C

I

L

Q

K

Q

K

T

Q

G

A

A

D

D

I

I

V

V

K
|
K

L

I

A

A

F

T

A

T

G

A

K

V

T

D

H

I

A

A

D

D

A

V

A

A

R

R

V

M

C

F

C

H

T

I

L

T

S

S

K

K

F

A

K

Q

E

V

P

P

K

T

V

I

F

G

M

L

V

V

M

M

G

G

E

E

A

R

G

G

K

L

F

M

T

S

R
|
R

V

I

V

L

G

C

F

S

S

K

F

F

G

G

S

G

L

Y

L

L

T

T

Y

F

T

G

F

T

F

L

-

D

-

S

G

S

R

K

P

V

V
x
S

A

A

P

P

G

G

Q
|
Q

I

P

E

T

A

I

E

K

E

D

L

L

V

L

R

D

L

L

E124 (= E39) binding
R126 (= R41) binding
R155 (= R72) binding
K241 (= K158) binding
R279 (= R196) binding
S300 (≠ V215) binding
Q304 (= Q219) 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

1sfjA 2.4a crystal structure of staphylococcus aureus type i 3- dehydroquinase, with 3-dehydroquinate bound (see paper)
29% identity, 77% coverage: 35:225/249 of query aligns to 25:220/227 of 1sfjA

query
sites
1sfjA

I

I

D

D

L

V

V

L

E
|
E

A

L

R
|
R

L

I

D

D

L

Q

L

F

E

E

E

N

V

V

K

T

P

V

E

D

T

Q

V

V

R

A

E

E

F

M

L

I

D

T

T

K

V

L

A

S

D

-

Y

-

G

-

F

F

Y

K

A

L

V

L

T

V

T

T

L

Y

R
|
R

P

T

V

K

W

L

E
x
Q

G

G

R

Y

F

G

E

Q

G

F

S

T

E

N

E

D

E

S

R

Y

L

L

K

N

L

L

L

I

E

S

L

D

A

L

V

A

N

N

H

I

P

N

A

G

T

I

A

D

A

M

V

I

D

D

V

I

E

E

L

W

R

Q

S

A

K

D

L

I

T

D

-

I

-

E

E

K

P

H

V

Q

R

R

Q

I

I

I

T

T

-

H

-

L

K

Q

E

Q

A

Y

G

N

K

K

K

E

L

V

I

I

V

I

S

S

Y

H

H
|
H

D

N

F

F

E

E

K

S

T

T

P

P

R

P

E

L

E

D

E

E

I

L

E

Q

E

F

L

I

F

F

K

F

A

K

C

M

L

Q

K

K

K

F

Q

N

A

P

D

E

I

Y

V

V

K
|
K

L

L

A

A

F

V

A

M

G

P

K

H

T

N

H

K

A

N

D

D

A

V

A

L

R

N

V

L

C

L

C

Q

T

A

L

M

S

S

K

T

F

F

K

S

E

D

P

T

K

M

-

D

-

C

-

K

-

V

V

V

F

G

M

I

V

S

M

M

G

S

E

K

A

L

G

G

K

L

F

I

T

S

R
|
R

V

T

V

A

G

Q

F

G

S

V

F

F

G

G

S

G

L

A

L

L

T

T

Y
|
Y

T

G

F

C

F

I

G

G

R

E

P

P

V

Q

A
|
A

P

P

G

G

Q
|
Q

I

I

E

D

A

V

E

T

E

D

L

L

active site: Q63 (≠ E76), H122 (= H131), K149 (= K158)
binding 3-dehydroshikimate: E29 (= E39), R31 (= R41), R59 (= R72), K149 (= K158), R191 (= R196), Y203 (= Y208), A211 (= A216), Q214 (= Q219)

Q6GII7 3-dehydroquinate dehydratase; 3-dehydroquinase; Type I DHQase; Type I dehydroquinase; DHQ1; EC 4.2.1.10 from Staphylococcus aureus (strain MRSA252) (see paper)
29% identity, 77% coverage: 35:225/249 of query aligns to 31:231/238 of Q6GII7

query
sites
Q6GII7

I

I

D

D

L

V

V

L

E

E

A

L

R

R

L

I

D

D

L

Q

L

F

E

E

E

N

V

V

K

T

P

V

E

D

T

Q

V

V

R

A

E

E

F

M

L

I

D

T

T

K

-

L

-

K

V

V

A

M

D

Q

Y

D

G

S

F

F

Y

K

A

L

V

L

T

V

T

T

L

Y

R
|
R

P

T

V

K

W

L

E

Q

G

G

R

Y

F

G

E

Q

G

F

S

T

E

N

E

D

E

S

R

Y

L

L

K

N

L

L

L

I

E

S

L

D

A

L

V

A

N

N

H

I

P

N

A

G

T

I

A

D

A

M

V

I

D

D

V

I

E

E

L

W

R

Q

S

A

K

D

L

I

T

D

-

I

-

E

E

K

P

H

V

Q

R

R

Q

I

I

I

T

T

-

H

-

L

K

Q

E

Q

A

Y

G

N

K

K

K

E

L

V

I

I

V

I

S

S

Y

H

H
|
H

D

N

F

F

E

E

K

S

T

T

P

P

R

P

E

L

E

D

E

E

I

L

E

Q

E

F

L

I

F

F

K

F

A

K

C

M

L

Q

K

K

K

F

Q

N

A

P

D

E

I

Y

V

V

K
|
K

L

L

A

A

F

V

A

M

G

P

K

H

T

N

H

K

A

N

D

D

A

V

A

L

R

N

V

L

C

L

C

Q

T

A

L

M

S

S

K

T

F

F

K

S

E

D

P

T

K

M

-

D

-

C

-

K

-

V

V

V

F

G

M

I

V

S

M

M

G

S

E

K

A

L

G

G

K

L

F

I

T

S

R
|
R

V

T

V

A

G

Q

F

G

S

V

F

F

G

G

S

G

L

A

L

L

T

T

Y

Y

T

G

F

C

F

I

G

G

R

E

P

P

V

Q

A

A

P

P

G

G

Q
|
Q

I

I

E

D

A

V

E

T

E

D

L

L

R70 (= R72) binding
H133 (= H131) active site, Proton donor/acceptor
K160 (= K158) active site, Schiff-base intermediate with substrate
R202 (= R196) binding
Q225 (= Q219) binding

8b2aBBB 3-dehydroquinate dehydratase (see paper)
28% identity, 77% coverage: 35:225/249 of query aligns to 31:231/238 of 8b2aBBB

query
sites
8b2aBBB

I

I

D

D

L

V

V

L

E
|
E

A

L

R
|
R

L

I

D

D

L

Q

L

I

E

E

E

N

V

V

K

T

P

V

E

N

T

Q

V

V

R

A

E

E

F

M

L

I

D

T

T

K

-

L

-

K

V

V

A

M

D

Q

Y

D

G

S

F

F

Y

K

A

L

V

L

T

V

T

T

L

Y

R

R

P

T

V

K

W

L

E

Q

G

G

R

Y

F

G

E

Q

G

F

S

T

E

N

E

D

E

L

R

Y

L

L

K

N

L

L

L

I

E

S

L

D

A

L

V

A

N

N

H

I

P

N

A

G

T

I

A

D

A

M

V

I

D

D

V

I

E

E

L

W

R

Q

S

A

K

D

L

I

T

D

-

I

-

E

E

K

P

H

V

Q

R

R

Q

I

I

I

T

T

-

H

-

L

K

Q

E

Q

A

Y

G

N

K

K

K

E

L

V

I

V

V

I

S

S

Y

H

H

H

D

N

F

F

E

E

K

S

T

T

P

P

R

P

E

L

E

D

E

E

I

L

E

Q

E

F

L

I

F

F

K

F

A

K

C

M

L

Q

K

K

K

F

Q

N

A

P

D

E

I

Y

V

V

K
|
K

L

L

A

A

F

V

A

M

G

P

K

H

T

N

H

K

A

N

D

D

A

V

A

L

R

N

V

L

C

L

C

Q

T

A

L

M

S

S

K

T

F

F

K

S

E

D

P

T

K

M

-

D

-

C

-

K

-

V

V

V

F

G

M
x
I

V

S

M

M

G

S

E

K

A

L

G

G

K

L

F

I

T

S

R
|
R

V

T

V

A

G

Q

F

G

S

V

F

F

G

G

S

G

L

A

L

L

T

T

Y
|
Y

T

G

F

C

F

I

G

G

R

E

P

P

V

Q

A
|
A

P

P

G

G

Q
|
Q

I

I

E

D

A

V

E

T

E

D

L

L

binding (4R,5R)-3-amino-4,5-dihydroxy-cyclohexene-1-carboxylic acid: E35 (= E39), R37 (= R41), K160 (= K158), I192 (≠ M186), R202 (= R196), Y214 (= Y208), A222 (= A216), Q225 (= Q219)

6sfhA Crystal structure of dhq1 from staphylococcus aureus covalently modified by ligand 7 (see paper)
28% identity, 77% coverage: 35:225/249 of query aligns to 30:230/237 of 6sfhA

query
sites
6sfhA

I

I

D

D

L

V

V

L

E
|
E

A

L

R
|
R

L

I

D

D

L

Q

L

I

E

E

E

N

V

V

K

T

P

V

E

N

T

Q

V

V

R

A

E

E

F

M

L

I

D

T

T

K

-

L

-

K

V

V

A

M

D

Q

Y

D

G

S

F

F

Y

K

A

L

V

L

T

V

T

T

L

Y

R
|
R

P

T

V

K

W

L

E
x
Q

G

G

R

Y

F

G

E

Q

G

F

S

T

E

N

E

D

E

L

R

Y

L

L

K

N

L

L

L

I

E

S

L

D

A

L

V

A

N

N

H

I

P

N

A

G

T

I

A

D

A

M

V

I

D

D

V

I

E

E

L

W

R

Q

S

A

K

D

L

I

T

D

-

I

-

E

E

K

P

H

V

Q

R

R

Q

I

I

I

T

T

-

H

-

L

K

Q

E

Q

A

Y

G

N

K

K

K

E

L

V

I

V

V

I

S

S

Y

H

H
|
H

D

N

F

F

E

E

K

S

T

T

P

P

R

P

E

L

E

D

E

E

I

L

E

Q

E

F

L

I

F

F

K

F

A

K

C

M

L

Q

K

K

K

F

Q

N

A

P

D

E

I

Y

V

V

K
|
K

L

L

A

A

F

V

A

M

G

P

K

H

T

N

H

K

A

N

D

D

A

V

A

L

R

N

V

L

C

L

C

Q

T

A

L

M

S

S

K

T

F

F

K

S

E

D

P

T

K

M

-

D

-

C

-

K

-

V

V

V

F

G

M

I

V

S

M

M

G

S

E

K

A

L

G

G

K

L

F

I

T

S

R
|
R

V

T

V

A

G

Q

F

G

S

V

F

F

G

G

S

G

L

A

L

L

T

T

Y
|
Y

T

G

F

C

F

I

G

G

R

E

P

P

V

Q

A
|
A

P

P

G

G

Q
|
Q

I

I

E

D

A

V

E

T

E

D

L

L

active site: Q73 (≠ E76), H132 (= H131), K159 (= K158)
binding (1~{S},3~{S},4~{S},5~{R})-3-(aminomethyl)-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E34 (= E39), R36 (= R41), R69 (= R72), H132 (= H131), K159 (= K158), R201 (= R196), Y213 (= Y208), A221 (= A216), Q224 (= Q219)

4h3dB 1.95 angstrom crystal structure of of type i 3-dehydroquinate dehydratase (arod) from clostridium difficile with covalent modified comenic acid.
29% identity, 88% coverage: 12:230/249 of query aligns to 17:248/254 of 4h3dB

query
sites
4h3dB

P

P

R

K

V

I

I

C

V

V

A

P

L

I

N

I

G

G

K

K

N

N

L

K

K

K

E

D

N

I

L

I

E

K

R

E

A

A

R

K

R

E

L

L

R

K

-

D

-

A

-

C

I

L

D

D

L

I

V

I

E

E

A

W

R

R

L

V

D

D

L

F

E

E

E

N

V

V

K

-

P

-

E

E

T

N

V

I

R

K

E

E

F

V

L

K

D

E

T

V

V

L

A

Y

D

E

Y

L

G

R

F

S

Y

Y

A

I

-

H

-

D

-

I

-

P

-

L

V

L

T

F

T

T

L

F

R

R

P

S

V

V

W

V

E
|
E

G

G

R

E

F

K

E

L

G

I

S

S

E

R

E

D

E

Y

R

Y

L

T

K

T

L

L

L

N

E

K

L

E

A

I

V

S

N

N

H

T

P

G

A

L

T

V

A

D

A

L

V

I

D

D

V

V

E

E

L

L

-

F

-

M

R

G

S

D

K

E

L

V

T

I

E

D

P

E

V

V

R

V

Q

N

I

F

T

A

K

H

E

K

A

K

G

E

K

V

K

K

L

V

I

I

V

I

S

S

Y

N

H
|
H

D

D

F

F

E

N

K

K

T

T

P

P

R

K

E

K

E

E

I

I

E

V

E

S

L

R

F

L

K

C

A

R

C

M

L

Q

K

E

K

L

Q

G

A

A

D

D

I

L

V

P

K
|
K

L

I

A

A

F

V

A

M

G

P

K

Q

T

N

H

E

A

K

D

D

A

V

A

L

R

V

V

L

C

L

-

E

C

A

T

T

L

N

S

E

K

M

F

F

K

K

-

I

-

Y

-

A

-

D

E

R

P

P

K

I

V

I

F

T

M
|
M

V

S

M

M

G

S

E

G

A

M

G

G

K

V

F

I

T

S

R
|
R

V

L

V

C

G

G

F

E

S

I

F

F

G

G

S

S

L

A

L

L

T

T

Y
x
F

T

G

F

A

G

K

R

S

P

V

V

S

A

A

P

P

G

G

Q

Q

I

I

E

S

A

F

E

K

E

E

L

L

V

N

R

S

L

V

I

L

S

N

active site: E87 (= E76), H144 (= H131), K171 (= K158)
binding 5-hydroxy-6-methyl-4-oxo-4H-pyran-2-carboxylic acid: H144 (= H131), K171 (= K158), M204 (= M186), R214 (= R196), F226 (≠ Y208)

3js3A Crystal structure of type i 3-dehydroquinate dehydratase (arod) from clostridium difficile with covalent reaction intermediate (see paper)
29% identity, 88% coverage: 12:230/249 of query aligns to 17:248/253 of 3js3A

query
sites
3js3A

P

P

R

K

V

I

I

C

V

V

A

P

L

I

N

I

G

G

K

K

N

N

L

K

K

K

E

D

N

I

L

I

E

K

R

E

A

A

R

K

R

E

L

L

R

K

-

D

-

A

-

C

I

L

D

D

L

I

V

I

E
|
E

A

W

R
|
R

L

V

D

D

L

F

E

E

E

N

V

V

K

-

P

-

E

E

T

N

V

I

R

K

E

E

F

V

L

K

D

E

T

V

V

L

A

Y

D

E

Y

L

G

R

F

S

Y

Y

A

I

-

H

-

D

-

I

-

P

-

L

V

L

T

F

T

T

L

F

R

R

P

S

V

V

W

V

E
|
E

G

G

R

E

F

K

E

L

G

I

S

S

E

R

E

D

E

Y

R

Y

L

T

K

T

L

L

L

N

E

K

L

E

A

I

V

S

N

N

H

T

P

G

A

L

T

V

A

D

A

L

V

I

D

D

V

V

E

E

L

L

-

F

-

M

R

G

S

D

K

E

L

V

T

I

E

D

P

E

V

V

R

V

Q

N

I

F

T

A

K

H

E

K

A

K

G

E

K

V

K

K

L

V

I

I

V

I

S

S

Y

N

H
|
H

D

D

F

F

E

N

K

K

T

T

P

P

R

K

E

K

E

E

I

I

E

V

E

S

L

R

F

L

K

C

A

R

C

M

L

Q

K

E

K

L

Q

G

A

A

D

D

I

L

V

P

K
|
K

L

I

A

A

F

V

A

M

G

P

K

Q

T

N

H

E

A

K

D

D

A

V

A

L

R

V

V

L

C

L

-

E

C

A

T

T

L

N

S

E

K

M

F

F

K

K

-

I

-

Y

-

A

-

D

E

R

P

P

K

I

V

I

F

T

M
|
M

V

S

M

M

G

S

E

G

A

M

G

G

K

V

F

I

T

S

R
|
R

V

L

V

C

G

G

F

E

S

I

F

F

G

G

S

S

L

A

L

L

T

T

Y
x
F

T

G

F

A

G

K

R

S

P

V

V
x
S

A
|
A

P

P

G

G

Q

Q

I

I

E

S

A

F

E

K

E

E

L

L

V

N

R

S

L

V

I

L

S

N

active site: E87 (= E76), H144 (= H131), K171 (= K158)
binding 3-amino-4,5-dihydroxy-cyclohex-1-enecarboxylate: E47 (= E39), R49 (= R41), K171 (= K158), M204 (= M186), R214 (= R196), F226 (≠ Y208), S233 (≠ V215), A234 (= A216)

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)
29% identity, 88% coverage: 12:230/249 of query aligns to 17:248/255 of Q186A6

query
sites
Q186A6

P

P

R

K

V

I

I

C

V

V

A

P

L

I

N

I

G

G

K

K

N

N

L

K

K

K

E

D

N

I

L

I

E

K

R

E

A

A

R

K

R

E

L

L

R

K

-

D

-

A

-

C

I

L

D

D

L

I

V

I

E
|
E

A
x
W

R
|
R

L

V

D

D

L

F

E

E

E

N

V

V

K

-

P

-

E

E

T

N

V

I

R

K

E

E

F

V

L

K

D

E

T

V

V

L

A

Y

D

E

Y

L

G

R

F

S

Y

Y

A

I

-

H

-

D

-

I

-

P

-

L

V

L

T

F

T

T

L

F

R
|
R

P

S

V

V

W

V

E

E

G

G

R

E

F

K

E

L

G

I

S

S

E

R

E

D

E

Y

R

Y

L

T

K

T

L

L

L

N

E

K

L

E

A

I

V

S

N

N

H

T

P

G

A

L

T

V

A

D

A

L

V

I

D

D

V

V

E

E

L

L

-

F

-

M

R

G

S

D

K

E

L

V

T

I

E

D

P

E

V

V

R

V

Q

N

I

F

T

A

K

H

E

K

A

K

G

E

K

V

K

K

L

V

I

I

V

I

S

S

Y

N

H
|
H

D

D

F

F

E

N

K

K

T

T

P

P

R

K

E

K

E

E

I

I

E

V

E

S

L

R

F

L

K

C

A

R

C

M

L

Q

K

E

K

L

Q

G

A

A

D

D

I

L

V

P

K
|
K

L

I

A

A

F

V

A

M

G

P

K

Q

T

N

H

E

A

K

D

D

A

V

A

L

R

V

V

L

C

L

-

E

C

A

T

T

L

N

S

E

K

M

F

F

K

K

-

I

-

Y

-

A

-

D

E

R

P

P

K

I

V

I

F

T

M

M

V

S

M

M

G

S

E

G

A

M

G

G

K

V

F

I

T

S

R
|
R

V

L

V

C

G

G

F

E

S

I

F

F

G

G

S

S

L

A

L

L

T

T

Y

F

T

G

F

A

G

K

R

S

P

V

V
x
S

A

A

P

P

G

G

Q
|
Q

I

I

E

S

A

F

E

K

E

E

L

L

V

N

R

S

L

V

I

L

S

N

EWR 47:49 (≠ EAR 39:41) binding
R83 (= R72) binding
H144 (= H131) active site, Proton donor/acceptor
K171 (= K158) active site, Schiff-base intermediate with substrate
R214 (= R196) binding
S233 (≠ V215) binding
Q237 (= Q219) binding

4gujA 1.50 angstrom crystal structure of the salmonella enterica 3- dehydroquinate dehydratase (arod) in complex with shikimate (see paper)
28% identity, 86% coverage: 12:225/249 of query aligns to 15:241/251 of 4gujA

query
sites
4gujA

P

P

R

K

V

I

I

I

V

V

A

S

L

L

N

M

G

G

K

K

N

T

L

I

K

T

E

D

N

V

L

K

E

S

R

E

A

A

-

L

-

A

-

Y

R

R

R

E

L

A

R

D

I

F

D

D

L

I

V

L

E
|
E

A

W

R
|
R

L

V

D

D

L

H

L

F

E

A

E

N

V

V

K

T

-

T

P

A

E

E

T

S

V

V

R

L

E

E

-

A

-

G

-

A

F

I

L

R

D

E

T

I

V

I

A

T

D

D

Y

K

G

P

F

L

Y

-

A

-

V

L

T

F

T

T

L

F

R
|
R

P

S

V

A

W

K

E
|
E

G

G

R

E

F

Q

E

A

G

L

S

T

E

T

E

G

E

Q

R

Y

L

I

K

D

L

L

L

N

E

R

L

A

A

A

V

V

N

D

H

S

P

G

A

L

T

V

A

D

A

M

V

I

D

D

V

L

E

E

L

L

R

F

S

T

K

G

L

D

T

D

E

E

P

V

V

K

R

A

Q

T

I

V

-

G

-

Y

T

A

K

H

E

Q

A

H

G

N

K

V

K

A

L

V

I

I

V

M

S

S

Y

N

H
|
H

D

D

F

F

E

H

K

K

T

T

P

P

R

A

E

A

E

E

I

I

E

V

E

Q

L

R

F

L

K

R

A

K

C

M

L

Q

K

E

K

L

Q

G

A

A

D

D

I

I

V

P

K
|
K

L

I

A

A

F

V

A

M

G

P

K

Q

T

T

H

K

A

A

D

D

A

V

A

L

R

T

V

L

C

L

C

T

T

A

L

T

S

V

K

E

F

M

K

Q

E

E

-

R

-

Y

-

A

-

D

-

R

P

P

K

I

V

I

F

T

M

M

V

S

M

M

G

S

E

K

A

T

G

G

K

V

F

I

T

S

R
|
R

V

L

V

A

G

G

F

E

S

V

F

F

G

G

S

S

L

A

T

T

Y
x
F

T

G

F

A

F

V

G

K

R

K

P

A

V
x
S

A
|
A

P

P

G

G

Q
|
Q

I

I

E

S

A

V

E

A

E

D

L

L

active site: E85 (= E76), H142 (= H131), K169 (= K158)
binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: E45 (= E39), R47 (= R41), R81 (= R72), H142 (= H131), R212 (= R196), F224 (≠ Y208), S231 (≠ V215), A232 (= A216), Q235 (= Q219)

4guiA 1.78 angstrom crystal structure of the salmonella enterica 3- dehydroquinate dehydratase (arod) in complex with quinate (see paper)
28% identity, 86% coverage: 12:225/249 of query aligns to 15:241/251 of 4guiA

query
sites
4guiA

P

P

R

K

V

I

I

I

V

V

A

S

L

L

N

M

G

G

K

K

N

T

L

I

K

T

E

D

N

V

L

K

E

S

R

E

A

A

-

L

-

A

-

Y

R

R

R

E

L

A

R

D

I

F

D

D

L

I

V

L

E
|
E

A

W

R
|
R

L

V

D

D

L

H

L

F

E

A

E

N

V

V

K

T

-

T

P

A

E

E

T

S

V

V

R

L

E

E

-

A

-

G

-

A

F

I

L

R

D

E

T

I

V

I

A

T

D

D

Y

K

G

P

F

L

Y

-

A

-

V

L

T

F

T

T

L

F

R
|
R

P

S

V

A

W

K

E
|
E

G

G

R

E

F

Q

E

A

G

L

S

T

E

T

E

G

E

Q

R

Y

L

I

K

D

L

L

L

N

E

R

L

A

A

A

V

V

N

D

H

S

P

G

A

L

T

V

A

D

A

M

V

I

D

D

V

L

E

E

L

L

R

F

S

T

K

G

L

D

T

D

E

E

P

V

V

K

R

A

Q

T

I

V

-

G

-

Y

T

A

K

H

E

Q

A

H

G

N

K

V

K

A

L

V

I

I

V

M

S

S

Y

N

H
|
H

D

D

F

F

E

H

K

K

T

T

P

P

R

A

E

A

E

E

I

I

E

V

E

Q

L

R

F

L

K

R

A

K

C

M

L

Q

K

E

K

L

Q

G

A

A

D

D

I

I

V

P

K
|
K

L

I

A

A

F

V

A

M

G

P

K

Q

T

T

H

K

A

A

D

D

A

V

A

L

R

T

V

L

C

L

C

T

T

A

L

T

S

V

K

E

F

M

K

Q

E

E

-

R

-

Y

-

A

-

D

-

R

P

P

K

I

V

I

F

T

M

M

V

S

M
|
M

G

S

E

K

A

T

G

G

K

V

F

I

T

S

R
|
R

V

L

V

A

G

G

F

E

S

V

F

F

G

G

S

S

L

A

T

T

Y
x
F

T

G

F

A

F

V

G

K

R

K

P

A

V

S

A
|
A

P

P

G

G

Q
|
Q

I

I

E

S

A

V

E

A

E

D

L

L

active site: E85 (= E76), H142 (= H131), K169 (= K158)
binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: E45 (= E39), R47 (= R41), R81 (= R72), H142 (= H131), K169 (= K158), M204 (= M188), R212 (= R196), F224 (≠ Y208), A232 (= A216), Q235 (= Q219)

3m7wA Crystal structure of type i 3-dehydroquinate dehydratase (arod) from salmonella typhimurium lt2 in covalent complex with dehydroquinate (see paper)
28% identity, 86% coverage: 12:225/249 of query aligns to 15:241/251 of 3m7wA

query
sites
3m7wA

P

P

R

K

V

I

I

I

V

V

A

S

L

L

N

M

G

G

K

K

N

T

L

I

K

T

E

D

N

V

L

K

E

S

R

E

A

A

-

L

-

A

-

Y

R

R

R

E

L

A

R

D

I

F

D

D

L

I

V

L

E
|
E

A

W

R
|
R

L

V

D

D

L

H

L

F

E

A

E

N

V

V

K

T

-

T

P

A

E

E

T

S

V

V

R

L

E

E

-

A

-

G

-

A

F

I

L

R

D

E

T

I

V

I

A

T

D

D

Y

K

G

P

F

L

Y

-

A

-

V

L

T

F

T

T

L

F

R

R

P

S

V

A

W

K

E
|
E

G

G

R

E

F

Q

E

A

G

L

S

T

E

T

E

G

E

Q

R

Y

L

I

K

D

L

L

L

N

E

R

L

A

A

A

V

V

N

D

H

S

P

G

A

L

T

V

A

D

A

M

V

I

D

D

V

L

E

E

L

L

R

F

S

T

K

G

L

D

T

D

E

E

P

V

V

K

R

A

Q

T

I

V

-

G

-

Y

T

A

K

H

E

Q

A

H

G

N

K

V

K

A

L

V

I

I

V

M

S

S

Y

N

H
|
H

D

D

F

F

E

H

K

K

T

T

P

P

R

A

E

A

E

E

I

I

E

V

E

Q

L

R

F

L

K

R

A

K

C

M

L

Q

K

E

K

L

Q

G

A

A

D

D

I

I

V

P

K
|
K

L

I

A

A

F

V

A

M

G

P

K

Q

T

T

H

K

A

A

D

D

A

V

A

L

R

T

V

L

C

L

C

T

T

A

L

T

S

V

K

E

F

M

K

Q

E

E

-

R

-

Y

-

A

-

D

-

R

P

P

K

I

V

I

F

T

M
|
M

V

S

M
|
M

G

S

E

K

A

T

G

G

K

V

F

I

T

S

R
|
R

V

L

V

A

G

G

F

E

S

V

F

F

G

G

S

S

L

A

T

T

Y
x
F

T

G

F

A

F

V

G

K

R

K

P

A

V

S

A
|
A

P

P

G

G

Q
|
Q

I

I

E

S

A

V

E

A

E

D

L

L

active site: E85 (= E76), H142 (= H131), K169 (= K158)
binding 1,3,4-trihydroxy-5-oxo-cyclohexanecarboxylic acid: E45 (= E39), R47 (= R41), H142 (= H131), K169 (= K158), M202 (= M186), M204 (= M188), R212 (= R196), F224 (≠ Y208), A232 (= A216), Q235 (= Q219)

P58687 3-dehydroquinate dehydratase; 3-dehydroquinase; DHQD; Type I DHQase; Type I dehydroquinase; DHQ1; EC 4.2.1.10 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
28% identity, 86% coverage: 12:225/249 of query aligns to 16:242/252 of P58687

query
sites
P58687

P

P

R

K

V

I

I

I

V

V

A
x
S

L

L

N

M

G

G

K

K

N

T

L

I

K

T

E

D

N

V

L

K

E

S

R

E

A

A

-

L

-

A

-

Y

R

R

R

E

L

A

R

D

I

F

D

D

L

I

V

L

E
|
E

A
x
W

R
|
R

L

V

D

D

L

H

L

F

E

A

E

N

V

V

K

T

-

T

P

A

E

E

T

S

V

V

R

L

E

E

-

A

-

G

-

A

F

I

L

R

D

E

T

I

V

I

A

T

D

D

Y

K

G

P

F

L

Y

-

A

-

V

L

T

F

T

T

L

F

R
|
R

P

S

V

A

W

K

E
|
E

G

G

R

E

F

Q

E

A

G

L

S

T

E

T

E

G

E

Q

R

Y

L

I

K

D

L

L

L

N

E

R

L

A

A

A

V

V

N

D

H

S

P

G

A

L

T

V

A

D

A

M

V

I

D

D

V

L

E

E

L

L

R

F

S

T

K

G

L

D

T

D

E

E

P

V

V

K

R

A

Q

T

I

V

-

G

-

Y

T

A

K

H

E

Q

A

H

G

N

K

V

K

A

L

V

I

I

V

M

S

S

Y

N

H
|
H

D

D

F

F

E

H

K

K

T

T

P

P

R

A

E

A

E

E

I

I

E

V

E

Q

L

R

F

L

K

R

A

K

C

M

L

Q

K

E

K

L

Q

G

A

A

D

D

I

I

V

P

K
|
K

L

I

A

A

F

V

A

M

G

P

K

Q

T

T

H

K

A

A

D

D

A

V

A

L

R

T

V

L

C

L

C

T

T

A

L

T

S

V

K

E

F

M

K

Q

E

E

-

R

-

Y

-

A

-

D

-

R

P

P

K

I

V

I

F

T

M

M

V

S

M

M

G

S

E

K

A

T

G

G

K

V

F

I

T

S

R
|
R

V

L

V

A

G

G

F

E

S

V

F

F

G

G

S

S

L

A

T

T

Y

F

T

G

F

A

F

V

G

K

R

K

P

A

V
x
S

A

A

P

P

G

G

Q
|
Q

I

I

E

S

A

V

E

A

E

D

L

L

S21 (≠ A17) binding
EWR 46:48 (≠ EAR 39:41) binding
R82 (= R72) binding
E86 (= E76) mutation to A: Very strong reduction of the catalytic efficiency and almost the same affinity for 3-dehydroquinate.; mutation to Q: Strong reduction of the catalytic efficiency and slight increase of the affinity for 3-dehydroquinate.
H143 (= H131) active site, Proton donor/acceptor
K170 (= K158) active site, Schiff-base intermediate with substrate; mutation to M: Abolishes enzyme activity and 1.5-fold reduction of the affinity for 3-dehydroquinate.
R213 (= R196) binding
S232 (≠ V215) binding ; mutation to A: Reduces enzyme activity 50-fold.
Q236 (= Q219) binding ; mutation to A: Nearly abolishes enzyme activity.

4guhB 1.95 angstrom crystal structure of the salmonella enterica 3- dehydroquinate dehydratase (arod) e86a mutant in complex with dehydroshikimate (crystal form #2) (see paper)
28% identity, 86% coverage: 12:225/249 of query aligns to 29:255/265 of 4guhB

query
sites
4guhB

P

P

R

K

V

I

I

I

V

V

A

S

L

L

N

M

G

G

K

K

N

T

L

I

K

T

E

D

N

V

L

K

E

S

R

E

A

A

-

L

-

A

-

Y

R

R

R

E

L

A

R

D

I

F

D

D

L

I

V

L

E
|
E

A

W

R
|
R

L

V

D

D

L

H

L

F

E

A

E

N

V

V

K

T

-

T

P

A

E

E

T

S

V

V

R

L

E

E

-

A

-

G

-

A

F

I

L

R

D

E

T

I

V

I

A

T

D

D

Y

K

G

P

F

L

Y

-

A

-

V

L

T

F

T

T

L

F

R
|
R

P

S

V

A

W

K

E
x
A

G

G

R

E

F

Q

E

A

G

L

S

T

E

T

E

G

E

Q

R

Y

L

I

K

D

L

L

L

N

E

R

L

A

A

A

V

V

N

D

H

S

P

G

A

L

T

V

A

D

A

M

V

I

D

D

V

L

E

E

L

L

R

F

S

T

K

G

L

D

T

D

E

E

P

V

V

K

R

A

Q

T

I

V

-

G

-

Y

T

A

K

H

E

Q

A

H

G

N

K

V

K

A

L

V

I

I

V

M

S

S

Y

N

H
|
H

D

D

F

F

E

H

K

K

T

T

P

P

R

A

E

A

E

E

I

I

E

V

E

Q

L

R

F

L

K

R

A

K

C

M

L

Q

K

E

K

L

Q

G

A

A

D

D

I

I

V

P

K
|
K

L

I

A

A

F

V

A

M

G

P

K

Q

T

T

H

K

A

A

D

D

A

V

A

L

R

T

V

L

C

L

C

T

T

A

L

T

S

V

K

E

F

M

K

Q

E

E

-

R

-

Y

-

A

-

D

-

R

P

P

K

I

V

I

F

T

M
|
M

V

S

M

M

G

S

E

K

A

T

G

G

K

V

F

I

T

S

R
|
R

V

L

V

A

G

G

F

E

S

V

F

F

G

G

S

S

L

A

T

T

Y
x
F

T

G

F

A

F

V

G

K

R

K

P

A

V

S

A
|
A

P

P

G

G

Q
|
Q

I

I

E

S

A

V

E

A

E

D

L

L

active site: A99 (≠ E76), H156 (= H131), K183 (= K158)
binding (4S,5R)-4,5-dihydroxy-3-oxocyclohex-1-ene-1-carboxylic acid: E59 (= E39), R61 (= R41), R95 (= R72), K183 (= K158), M216 (= M186), R226 (= R196), F238 (≠ Y208), A246 (= A216), Q249 (= Q219)

P05194 3-dehydroquinate dehydratase; 3-dehydroquinase; Type I DHQase; Type I dehydroquinase; DHQ1; EC 4.2.1.10 from Escherichia coli (strain K12) (see 3 papers)
27% identity, 86% coverage: 12:225/249 of query aligns to 16:242/252 of P05194

query
sites
P05194

P

P

R

K

V

I

I

I

V

V

A

S

L

L

N

M

G

A

K

K

N

D

L

I

K

A

E

S

N

V

L

K

E

S

R

E

A

A

-

L

-

A

-

Y

R

R

R

E

L

A

R

D

I

F

D

D

L

I

V

L

E

E

A

W

R

R

L

V

D

D

-

H

-

Y

-

A

-

D

-

L

-

S

-

N

-

V

-

E

-

S

-

V

-

M

-

A

-

K

L

I

L

L

E

R

E

E

V

T

K

M

P

P

E

E

T

K

V

P

R

L

E

L

F

F

L

-

D

-

T

-

V

-

A

-

D

-

Y

-

G

-

F

-

Y

-

A

-

V

-

T

-

T

T

L

F

R

R

P

S

V

A

W

K

E

E

G

G

R

E

F

Q

E

A

G

I

S

S

E

T

E

E

E

A

R

Y

L

I

K

A

L

L

L

N

E

R

L

A

A

A

V

I

N

D

H

S

P

G

A

L

T

V

A

D

A

M

V

I

D

D

V

L

E

E

L

L

R

F

S

T

K

G

L

-

T

D

E

D

P

Q

V

V

R

K

Q

E

I

T

T

V

K

A

E

Y

A

A

G

H

K

A

-

H

-

D

-

V

K

K

L

V

I

V

V

M

S

S

Y

N

H
|
H

D

D

F

F

E
x
H

K

K

T

T

P

P

R

E

E

A

E

E

I

I

E

I

E

A

L

R

F

L

K

R

A

K

C

M

L

Q

K

S

K

F

Q

D

A

A

D

D

I

I

V

P

K
|
K

L

I

A

A

F

L

A

M

G

P

K

Q

T

S

H

T

A

S

D

D

A

V

A

L

R

T

V

L

C

L

C

A

T

A

L

T

S

L

K

E

F

M

K

Q

E

E

-

Q

-

Y

-

A

-

D

-

R

P

P

K

I

V

I

F

T

M

M

V

S

M
|
M

G

A

E

K

A

T

G

G

K

V

F

I

T

S

R

R

V

L

V

A

G

G

F

E

S

V

F

F

G

G

S

S

L

A

T

T

Y

F

T

G

F

A

F

V

G

K

R

K

P

A

V

S

A

A

P

P

G

G

Q

Q

I

I

E

S

A

V

E

N

E

D

L

L

H143 (= H131) active site, Proton donor/acceptor; mutation to A: Loss of dehydratase activity.
H146 (≠ E134) mutation to A: It retains full catalytic activity.
K170 (= K158) active site, Schiff-base intermediate with substrate; mutation to A: Loss of dehydratase activity, but it is still able to bind substrate.
M205 (= M188) 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)
24% identity, 88% coverage: 8:225/249 of query aligns to 11:242/252 of 1l9wA

query
sites
1l9wA

L

I

G

G

E

E

-

G

I

M

P

P

R

K

V

I

I

I

V

V

A

S

L

L

N

M

G

G

K

R

N

D

L

I

K

N

E

S

N

V

L

K

E

A

R

E

A

A

-

L

-

A

-

Y

R

R

R

E

L

A

R

T

I

F

D

D

L

I

V

L

E
|
E

A

W

R
|
R

L

V

D

D

L

H

L

F

E

M

E

D

V

I

K

A

P

S

E

T

-

Q

-

S

-

V

-

L

-

T

T

A

V

A

R

R

E

V

F

I

L

R

D

D

T

A

V

M

A

P

D

D

Y

I

G

P

F

L

Y

-

A

-

V

L

T

F

T

T

L

F

R
|
R

P

S

V

A

W

K

E
|
E

G

G

R

E

F

Q

E

T

G

I

S

T

E

T

E

Q

E

H

R

Y

L

L

K

T

L

L

L

N

E

R

L

A

A

A

V

I

N

D

H

S

P

G

A

L

T

V

A

D

A

M

V

I

D

D

V

L

E

E

L

L

R

F

S

T

K

G

L

D

T

A

E

D

P

V

V

K

R

A

Q

T

I

V

T

D

K

Y

E

A

A

H

G

A

K

H

K

N

L

V

-

Y

-

V

I

V

V

M

S

S

Y

N

H
|
H

D

D

F

F

E

H

K

Q

T

T

P

P

R

S

E

A

E

E

I

M

E

V

E

S

L

R

F

L

K

R

A

K

C

M

L

Q

K

A

K

L

Q

G

A

A

D

D

I

I

V

P

K
|
K

L

I

A

A

F

V

A

M

G

P

K

Q

T

S

H

K

A

H

D

D

A

V

A

L

R

T

V

L

C

L

C

T

T

A

L

T

S

L

K

E

F

M

K

Q

E

Q

-

H

-

Y

-

A

-

D

-

R

P

P

K

V

V

I

F

T

M

M

V

S

M

M

G

A

E

K

A

E

G

G

K

V

F

I

T

S

R
|
R

V

L

V

A

G

G

F

E

S

V

F

F

G

G

S

S

L

A

T

T

Y
x
F

T

G

F

A

F

V

G

K

R

Q

P

A

V
x
S

A
|
A

P

P

G

G

Q
|
Q

I

I

E

A

A

V

E

N

E

D

L

L

active site: E86 (= E76), H143 (= H131), K170 (= K158)
binding 3-amino-4,5-dihydroxy-cyclohex-1-enecarboxylate: E46 (= E39), R48 (= R41), R82 (= R72), H143 (= H131), K170 (= K158), R213 (= R196), F225 (≠ Y208), S232 (≠ V215), A233 (= A216), Q236 (= Q219)

Query Sequence

>WP_013537267.1 NCBI__GCF_000185805.1:WP_013537267.1
MLLGTVKLGEIPRVIVALNGKNLKENLERARRLRIDLVEARLDLLEEVKPETVREFLDTV
ADYGFYAVTTLRPVWEGGRFEGSEEERLKLLELAVNHPATAAVDVELRSKLTEPVRQITK
EAGKKLIVSYHDFEKTPREEEIEELFKACLKKQADIVKLAFAGKTHADAARVCCTLSKFK
EPKVFMVMGEAGKFTRVVGFSFGSLLTYTFFGRPVAPGQIEAEELVRLISDFYPDYAKEK
LKLQAEPVI

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