SitesBLAST

Q9X0C6 Imidazole glycerol phosphate synthase subunit HisF; IGP synthase cyclase subunit; IGP synthase subunit HisF; ImGP synthase subunit HisF; IGPS subunit HisF; EC 4.3.2.10 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
50% identity, 99% coverage: 1:250/253 of query aligns to 1:249/253 of Q9X0C6

query
sites
Q9X0C6

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C9 (= C9) mutation to A: No change in activity.
D11 (= D11) mutation to X: Loss of activity.
K19 (= K19) mutation to S: Decrease in activity.
D51 (= D51) mutation to N: No change in activity.
N103 (= N103) mutation to A: No change in activity.
D130 (= D130) mutation D->A,C,F,G,H,I,K,L,M,N,P,Q,R,S,T,V,W,Y: Complete loss of activity.; mutation to E: Weak activity.
D176 (= D176) mutation to N: Decrease in activity.
D183 (= D183) mutation to N: No change in activity.

7ac8A Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. (see paper)
50% identity, 99% coverage: 1:250/253 of query aligns to 1:249/252 of 7ac8A

query
sites
7ac8A

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active site: D11 (= D11), D130 (= D130)
binding [(2R,3S,4R,5R)-5-[4-aminocarbonyl-5-[(E)-[[(2R,3R,4S,5R)-3,4-bis(oxidanyl)-5-(phosphonooxymethyl)oxolan-2-yl]amino]methylideneamino]imidazol-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl dihydrogen phosphate: L50 (= L50), I52 (= I52), G82 (= G82), N103 (= N103), T104 (≠ S104), D130 (= D130), S144 (≠ G144), D176 (= D176), G177 (= G177), S201 (= S201), S225 (= S226)

1gpwC Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex. (see paper)
50% identity, 99% coverage: 1:250/253 of query aligns to 1:249/253 of 1gpwC

query
sites
1gpwC

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active site: N11 (≠ D11), D130 (= D130)
binding phosphate ion: G82 (= G82), N103 (= N103), T104 (≠ S104), D176 (= D176), G177 (= G177), S225 (= S226)

7qc8A Imidazole glycerol phosphate synthase subunit HisF (see paper)
48% identity, 98% coverage: 2:250/253 of query aligns to 2:249/250 of 7qc8A

query
sites
7qc8A

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binding zinc ion: E11 (≠ D11), H50 (≠ L50), H52 (≠ I52)

3zr4E Structural evidence for ammonia tunneling across the (beta-alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex (see paper)
48% identity, 99% coverage: 1:250/253 of query aligns to 1:240/244 of 3zr4E

query
sites
3zr4E

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V

P

N

V

V

R

R

active site: D11 (= D11), D121 (= D130)
binding glycerol: R179 (= R188), L206 (≠ Q216)

4ewnD Structure of hisf-d130v+d176v with bound rcdrp (see paper)
48% identity, 98% coverage: 2:250/253 of query aligns to 1:242/243 of 4ewnD

query
sites
4ewnD

L

L

A

A

S

K

R

R

V

I

I

I

P

A

C

C

L

L

D

D

I

V

D

K

H

D

G

G

R

R

V

V

K

K

G

G

V

T

Q

N

F

F

V

E

A

N

L

L

R

R

D

D

A

S

G

G

D

D

P

P

V

V

E

E

V

L

A

G

K

K

R

F

Y

Y

N

S

D

E

E

I

G

G

A

I

D

D

E

E

I

L

T

V

F

F

L

L

D

D

I

I

S

T

A

K

S

-

Y

-

E

-

R

-

G

-

T

T

L

M

A

L

D

E

M

L

V

V

S

E

A

K

V

V

A

A

A

E

Q

Q

V

I

F

D

I

I

P

P

L

F

T

T

V

V

G

G

V

I

R

H

C

D

V

F

E

E

D

T

I

A

R

S

T

E

L

L

L

I

L

L

A

R

G

G

A

A

D

D

K

K

V

V

S

S

I

I

N

N

S

T

A

A

V

V

N

E

D

N

P

P

E

S

L

L

V

I

R

T

A

Q

A

I

A

A

R

Q

R

T

F

F

G

G

N

S

S

Q

C

A

I

V

V

V

A

A

I

I

D
x
V

A

A

K

K

R

R

V

V

E

D

D

G

H

E

W

F

E

M

V

V

F

F

T

T

H

Y

G

S

G

G

R

K

G

N

T

T

G

G

L

I

D

L

A

L

V

R

A

D

W

W

A

V

Q

V

R

E

M

V

A

E

A

K

Y

R

G

G

A

A

G

G

E

E

I

I

L

L

T

T

S

S

M

I

D

D

R

R

D

V

G
|
G

T

T

G

K

I

S

G

G

F

Y

D

D

L

T

A

E

L

M

T

I

R

R

A

F

I

V

S

R

D

P

A

L

V

T

P

T

V

L

P

P

V

I

I

I

A

A

S
|
S

G
|
G

V

A

G

G

E

K

I

M

R

E

H

H

F

F

V

L

E

E

G

-

I

A

Q

F

Q

L

G

A

R

G

A

A

D

D

A

A

V

A

L
|
L

A
|
A

S
|
S

V

V

F

F

H

H

F

F

G

R

Q

E

F

I

R

D

I

V

S

R

E

E

V

L

K

K

A

E

R

Y

M

L

A

K

A

H

G

G

I

V

P

N

V

V

R

R

binding 1-(O-carboxy-phenylamino)-1-deoxy-D-ribulose-5-phosphate: V123 (≠ D130), G170 (= G177), S194 (= S201), G195 (= G202), G196 (= G203), L215 (= L223), A216 (= A224), A217 (= A225), S218 (= S226)

5d2tA Directed evolutionary changes in kemp eliminase ke07 - crystal 3 wild type
45% identity, 98% coverage: 3:250/253 of query aligns to 1:247/251 of 5d2tA

query
sites
5d2tA

A

A

S

K

R

R

V

I

I

I

P

A

C

A

L

L

D

I

I

V

D

K

H

D

G

G

R

R

V

V

K

K

G

G

V

S

Q

N

F

F

V

E

A

N

L

L

R

R

D

D

A

S

G

G

D

D

P

P

V

V

E

E

V

L

A

G

K

K

R

F

Y

Y

N

S

D

E

E

I

G

G

A

I

D

D

E

E

I

L

T

S

F

F

L
x
W

D

D

I

I

S

T

A

A

S

S

Y

V

E

E

E

K

R

R

G

K

T

T

L

M

A

L

D

E

M

L

V

V

S

E

A

K

V

V

A

A

A

E

Q

Q

V

I

F

D

I

I

P

P

L

F

T

T

V

V

G

G

V

I

R

H

C

D

V

F

E

E

D

T

I

A

R

S

T

E

L

L

L

I

L

L

A

R

G

G

A

A

D

D

K

K

V

V

S
x
E

I

I

N

N

S

T

A

A

V

V

N

E

D

N

P

P

E

S

L

L

V

I

R

T

A

Q

A

I

A

A

R

Q

R

T

F

F

G

G

N

S

S

Q

C

A

I

V

V

V

A
x
Y

I

I

D

A

A

A

K

K

R

R

V

V

E

D

D

G

H

E

W

F

E

M

V

V

F

F

T

T

H

Y

G

S

G

G

R

K

G

N

T

T

G

G

L

I

D

L

A

L

V

R

A

D

W

W

A

V

Q

V

R

E

M

V

A

E

A

K

Y

R

G

G

A

A

G

G

E

E

I

I

L

V

L

L

T

G

S

S

M

I

D

D

R

R

D

L

G

G

T

T

G

K

I

S

G

G

F

Y

D

D

L

T

A

E

L

M

T

I

R

R

A

F

I

V

S

R

D

P

A

L

V

T

P

T

V

L

P

P

V

I

I

I

A

A

S

H

G

G

V

A

G

G

E

K

I

M

R

E

H

H

F

F

V

L

E

E

G

A

I

F

Q

L

Q

A

G

G

R

-

A

A

D

D

A

A

V

A

L
x
K

A

A

A

N

S

S

V

V

F

L

H

H

F

F

G

R

Q

E

F

I

R

D

I

V

S

R

E

E

V

L

K

K

A

E

R

Y

M

L

A

K

A

H

G

G

I

V

P

N

V

V

R

R

binding 5-nitro-2-oxidanyl-benzenecarbonitrile: W48 (≠ L50), E99 (≠ S101), Y126 (≠ A128), K220 (≠ L223)

6dnjA Directed evolutionary changes in kemp eliminase ke07 - crystal 28 round 5 (see paper)
45% identity, 98% coverage: 2:250/253 of query aligns to 1:248/250 of 6dnjA

query
sites
6dnjA

L

L

A

A

S

K

R

R

V

I

I

D

P

A

C

A

L

L

D

I

I

M

D

K

H

D

G

G

R

R

V

V

K

K

G

G

V

S

Q

N

F

F

V

E

A

N

L

L

R

R

D

D

A

S

G

G

D

D

P

P

V

V

E

E

V

L

A

G

K

K

R

F

Y

Y

N

S

D

E

E

I

G

G

A

I

D

D

E

E

I

L

T

S

F

F

L
x
W

D

D

I

I

S

T

A

A

S

S

Y

V

E

E

E

K

R

R

G

K

T

T

L

M

A

L

D

E

M

L

V

V

S

E

A

K

V

V

A

A

A

E

Q

Q

V

I

F

D

I

I

P

P

L

F

T

T

V

V

G
|
G

G

G

V

I

R

H

C

D

V

F

E

E

D

T

I

A

R

S

T

E

L

L

L

I

L

L

A

R

G

G

A

A

D

D

K

K

V

V

S

E

I

I

N
|
N

S

T

A

A

V

V

N

E

D

N

P

P

E

S

L

L

V

I

R

T

A

Q

A

I

A

A

R

Q

R

T

F

F

G

G

N

S

S

Q

C

A

I

V

V

V

A
x
Y

I

I

D

A

A

A

K

K

R

R

V

V

E

D

D

G

H

E

W

F

E

M

V

V

F

F

T

T

H

Y

G

S

G

G

R

K

G

N

T

T

G

G

L

I

D

L

A

L

V

R

A

D

W

W

A

V

Q

V

R

E

M

V

A

E

A

K

Y

R

G

G

A

A

G

G

E

E

I

I

L

V

L

L

T

G

S

S

M

I

D

D

R

R

D

L

G

G

T

T

G

K

I

S

G

G

F

Y

D

D

L

T

A

E

L

M

T

I

R

R

A

F

I

V

S

R

D

P

A

L

V

T

P

T

V

L

P

P

V

I

I

I

A

A

S

H

G

R

G

G

V

A

G

G

E

K

I

M

R

E

H

H

F

F

V

L

E

E

G

A

I

F

Q

L

Q

A

G

G

R

-

A

A

D

D

A

A

V

A

L

K

A

A

A

D

S

S

V

V

F

F

H

H

F

F

G

R

Q

E

F

I

R

D

I

V

S

R

E

E

V

L

K

K

A

E

R

Y

M

L

A

K

A

H

G

G

I

V

P

N

V

V

R

R

binding 5-nitro-1,2-benzoxazole: W49 (≠ L50), G79 (= G80), G80 (= G81), N102 (= N103), Y127 (≠ A128)

2wjzE Crystal structure of (hish) k181a y138a mutant of imidazoleglycerolphosphate synthase (hish hisf) which displays constitutive glutaminase activity (see paper)
47% identity, 99% coverage: 1:250/253 of query aligns to 1:235/237 of 2wjzE

query
sites
2wjzE

M

M

L

L

A

A

S

K

R

R

V

I

I

I

P

A

C

C

L

L

D
|
D

I

V

D

K

H

D

G

G

R

R

V

V

K

-

G

-

V

-

Q

-

F

-

V

-

A

-

L

-

R

-

D

-

A

-

G

G

D

D

P

P

V

V

E

E

V

L

A

G

K

K

R

F

Y

Y

N

S

D

E

E

I

G

G

A

I

D

D

E

E

I

L

T

V

F

F

L

L

D

D

I

I

S

T

A

A

S

-

Y

-

E

-

E

K

R

R

G

K

T

T

L

M

A

L

D

E

M

L

V

V

S

E

A

K

V

V

A

A

A

E

Q

Q

V

I

F

D

I

I

P

P

L

F

T

T

V

V

G

G

G
|
G

V

I

R

H

C

D

V

F

E

E

D

T

I

A

R

S

T

E

L

L

L

I

L

L

A

R

G

G

A

A

D

D

K

K

V

V

S

S

I

I

N
|
N

S
x
T

A

A

V

V

N

E

D

N

P

P

E

S

L

L

V

I

R

T

A

Q

A

I

A

A

R

Q

R

T

F

F

G

G

N

S

S

Q

C

A

I

V

V

V

A

A

I

I

D
|
D

A

A

K

K

R

R

V

V

E

D

D

G

H

E

W

F

E

M

V

V

F

F

T

T

H

Y

G

S

G

G

R

K

G

N

T

T

G

G

L

I

D

L

A

L

V

R

A

D

W

W

A

V

Q

V

R

E

M

V

A

E

A

K

Y

R

G

G

A

A

G

G

E

E

I

I

L

L

T

T

S

S

M

I

D

D

R

R

D

D

G

G

T

T

G

K

I

S

G

G

F

Y

D

D

L

T

A

E

L

M

T

I

R

R

A

F

I

V

S

R

D

P

A

L

V

T

P

T

V

L

P

P

V

I

I

I

A

A

S

S

G

G

V

A

G

G

E

K

I

M

R

E

H

H

F

F

V

L

E

E

G

A

I

F

Q

L

Q

A

G

G

R

A

A

D

D

-

A

A

V

A

L

L

A

A

S

S

V

V

F

F

H

H

F

F

G

R

Q

E

F

I

R

D

I

V

S

R

E

E

V

L

K

K

A

E

R

Y

M

L

A

K

A

H

G

G

I

V

P

N

V

V

R

R

active site: D11 (= D11), D116 (= D130)
binding phosphate ion: G68 (= G82), N89 (= N103), T90 (≠ S104)

P60664 Imidazole glycerol phosphate synthase subunit HisF; IGP synthase cyclase subunit; IGP synthase subunit HisF; ImGP synthase subunit HisF; IGPS subunit HisF; EC 4.3.2.10 from Escherichia coli (strain K12) (see paper)
45% identity, 99% coverage: 1:250/253 of query aligns to 1:256/258 of P60664

query
sites
P60664

M

M

L

L

A

A

S

K

R
|
R

V

I

I

I

P

P

C

C

L

L

D

D

I

V

D

R

H

D

G

G

R

Q

V

V

K

K

G

G

V

V

Q

Q

F

F

V

R

A

N

L

H

R

E

D

I

A

I

G

G

D

D

P

I

V

V

E

P

V

L

A

A

K

K

R

R

Y

Y

N

A

D

E

E

E

G

G

A

A

D

D

E
|
E

I

L

T

V

F

F

L

Y

D

D

I

I

S

T

A

A

S

S

Y

S

E

D

E

G

R

R

G

V

T

V

L

D

A

K

D

S

M

W

V

V

S

S

A

R

V

V

A

A

A

E

Q

V

V

I

F

D

I

I

P

P

L

F

T

C

V

V

G

A

G

G

V

I

R

K

C

S

V

L

E

E

D

D

I

A

R

A

T

K

L

I

L

L

L

S

A

F

G

G

A

A

D

D

K

K

V

I

S

S

I

I

N

N

S

S

A

P

A

A

V

L

N

A

D

D

P

P

E

T

L

L

V

I

R

T

A

R

A

L

A

A

R

D

R

R

F

F

G

G

N

V

S
x
Q

C
|
C

I

I

V

V

A

G

I

I

-

D

-

T

-

W

-

Y

D

D

A

A

K

E

R

T

V

G

E

K

D

Y

H

H

W

V

E

N

V

Q

F

Y

T

T

-

G

-

D

H

E

G

S

G

R

R

T

R

R

G

V

T

T

G

Q

L

W

D

E

A

T

V

L

A

D

W

W

A

V

Q

Q

R

E

M

V

A

Q

A

K

Y

R

G

G

A

A

G

G

E

E

I

I

L

V

L

L

T

N

S

M

M

M

D

N

R

Q

D

D

G

G

T

V

G

R

I

N

G

G

F

Y

D

D

L

L

A

E

L

Q

T

L

R

K

A

K

I

V

S

R

D

E

A

V

V

C

P

H

V

V

P

P

V

L

I

I

A

A

S

S

G

G

V

A

G

G

E

T

I

M

R

E

H

H

F

F

V

L

E

E

G

A

I

F

Q

R

Q

D

G

A

R

D

A

V

D

D

A

G

V

A

L

L

A

A

S

S

V

V

F

F

H

H

F

K

G

Q

Q

I

F

I

R

N

I

I

S

G

E

E

V

L

K

K

A

A

R

Y

M

L

A

A

A

T

A

Q

G

G

I

V

P

E

V

I

R

R

R5 (= R5) mutation to A: Loss of activity.; mutation to H: Loss of IGP synthase activity. Weak IGP synthase activity and reduced HisH activity in vitro.
E46 (= E46) mutation to A: Loss of activity.; mutation to G: Loss of IGP synthase activity. Weak IGP synthase and HisH activities in vitro.
Q123 (≠ S123) mutation to A: Decrease in activity.; mutation to R: Loss of IGP synthase activity. Weak HisH activity in vitro.
C124 (= C124) mutation to A: No change in activity.; mutation to R: Loss of IGP synthase activity. Weak HisH activity in vitro.

3iivB Evolutionary optimization of computationally designed enzymes: kemp eliminases of the ke07 series (see paper)
44% identity, 98% coverage: 2:250/253 of query aligns to 2:248/262 of 3iivB

query
sites
3iivB

L

L

A

A

S

K

R

R

V

I

I

D

P

A

C

A

L

L

D

I

I

L

D

K

H

D

G

G

R

R

V

V

K

K

G

G

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Q

N

F

F

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E

A

N

L

L

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R

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D

A

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G

G

D

D

P

P

V

V

E

E

V

L

A

G

K

K

R

F

Y

Y

N

S

D

E

E

I

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G

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D

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I

L

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F

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A

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K

G

-

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L

M

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V

A

A

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C

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E

L

L

L

I

L

L

A

R

G

G

A

A

D

D

K

K

V

V

S
x
E

I

I

N

N

S

T

A

A

V

V

N

E

D

N

P

P

E

S

L

L

V

I

R

T

A

Q

A

I

A

A

R

Q

R

T

F

F

G

G

N

S

S

Q

C

A

I

V

V

V

A

Y

I

I

D

A

A

A

K

K

R

R

V

V

E

D

D

G

H

E

W

F

E

M

V

V

F

F

T

T

H

Y

G

S

G

G

R

T

R

K

G

N

T

T

G

G

L

I

D

L

A

L

V

R

A

D

W

W

A

V

Q

V

R

E

M

V

A

E

A

K

Y

R

G

G

A

A

G

G

E

E

I

I

L

V

L

L

T

G

S

S

M

I

D

D

R

R

D

L

G

G

T

T

G

K

I

S

G

G

F

Y

D

D

L

T

A

E

L

M

T

I

R

R

A

F

I

V

S

R

D

P

A

L

V

T

P

T

V

L

P

P

V

I

I

I

A

A

S

H

G

R

G

G

V

A

G

G

E

K

I

T

R

E

H

H

F

F

V

L

E

E

G

A

I

F

Q

L

Q

A

G

G

R

-

A

A

D

D

A

A

V

A

L
x
K

A

A

A

D

S

S

V

V

F

F

H

H

F

S

G

R

Q

E

F

I

R

D

I

V

S

R

E

E

V

L

K

K

A

E

R

Y

M

L

A

K

A

H

G

G

I

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P

N

V

V

R

R

binding magnesium ion: E100 (≠ S101), K221 (≠ L223)

P33734 Imidazole glycerol phosphate synthase hisHF; IGP synthase; IGPS; ImGP synthase; EC 4.3.2.10; EC 3.5.1.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
32% identity, 98% coverage: 2:250/253 of query aligns to 236:548/552 of P33734

query
sites
P33734

L

L

A

T

S

R

R
|
R

V

I

I

I

P

A

C

C

L

L

D

D

I

V

-

R

-

T

-

N

D

D

H

Q

G

G

R

D

V

L

V

V

-

V

-

T

K
|
K

G

G

V

D

Q

Q

F

Y

-

D

-

V

-

R

-

E

-

K

-

S

-

D

-

G

V

K

A

G

L

V

R

R

D

N

A

L

G

G

D

K

P

P

V

V

E

Q

V

L

A

A

K

Q

R

K

Y

Y

N

Y

D

Q

E

Q

G

G

A

A

D

D

E

E

I

V

T

T

F

F

L

L

D

N

I

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A

S

S

F

Y

R

E

D

-

C

-

P

-

L

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K

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G

T

T

P

L

M

A

L

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E

M

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A

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A

A

A

A

K

Q

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F

F

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P

L

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G

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C

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E

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D

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-

D

-

G

-

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K

-

I

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P

-

A

-

L

-

E

-

V

-

A

R

S

T

L

L

Y

L

F

L

R

A

S

G

G

A

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D

K
|
K

V

V

S

S

I

I

N

G

S

T

A

D

A

A

V

V

N

Y

D

A

P

A

E

E

L

K

-

Y

-

E

-

L

-

G

-

N

-

R

-

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-

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-

G

-

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-

P

V

I

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A

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A

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R

A

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A

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I

A

S

I

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D

D

A

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K

K

R

R

V

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-

Y

-

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-

S

-

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-

A

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-

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-

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K

-

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-

F

-

E

-

T

-

E

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Y

-

P

-

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-

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-

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-

G

E

E

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H

Y

-

C

-

W

W

Y

E

Q

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T

T

I

H

K

G

G

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R

E

G

S

T

R

G

D

L

L

D

G

A

V

V

W

A

E

W

L

A

T

Q

R

R

A

M

C

A

E

A

A

Y

L

G

G

A

A

G

G

E

E

I

I

L

L

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N

S

C

M

I

D

D

R

K

D

D

G

G

T

S

G

N

I

S

G

G

F

Y

D

D

L

L

A

E

L

L

T

I

R

E

A

H

I

V

S

K

D

D

A

A

V

V

P

K

V

I

P

P

V

V

I

I

A

A

S

S

G

S

G

G

V

A

G

G

E

V

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P

R

E

H

H

F

F

V

E

E

E

G

A

I

F

Q

L

Q

K

G

T

R

R

A

A

D

D

A

A

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C

L

L

A

G

A

A

S

G

V

M

F

F

H

H

F

R

G

G

Q

E

F

F

R

T

I

V

S

N

E

D

V

V

K

K

A

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Y

M

L

A

L

A

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A

H

G

G

I

L

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V

R

R

R239 (= R5) mutation R->A,H,K: 1000-fold decrease in catalytic efficiency. Uncoupling of glutaminase activity from the cyclase activity.
K258 (= K19) mutation to A: No activity. Uncoupling of glutaminase activity from the cyclase activity.; mutation to R: Small reduction of activity.
K360 (= K99) mutation K->A,R: Almost no effect on activity.

1ox4B Towards understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerophosphate synthase (see paper)
33% identity, 98% coverage: 2:250/253 of query aligns to 239:536/538 of 1ox4B

query
sites
1ox4B

L

L

A

T

S

R

R

R

V

I

I

I

P

A

C

C

L

L

D
|
D

I

V

-

R

-

T

-

N

D

D

H

Q

G

G

R

D

V

L

V

V

K

-

G

-

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-

Q

-

F

-

V

V

A

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G

D

D

A

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G

G

D

K

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P

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V

L

A

A

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Y

Y

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D

Q

E

Q

G

G

A

A

D

D

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E

I

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F

F

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I

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-

C

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A

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A

A

A

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A

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G

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K

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D

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W

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R

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L

L

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W

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A

A

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G

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D

D

L

L

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E

L

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K

D

D

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A

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x
S

G

G

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A

G

G

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V

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H

H

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F

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E

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A

I

F

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L

Q

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G

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R

R

A

A

D

D

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C

L

L

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A
|
A

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x
G

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M

F

F

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G

G

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E

F

F

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T

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K

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L

A

L

A

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R

active site: D248 (= D11), D392 (= D130)
binding pyrophosphate 2-: G463 (= G177), S488 (≠ G202), A511 (= A225), G512 (≠ S226)

1ox5A Towards understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerophosphate synthase (see paper)
33% identity, 98% coverage: 2:250/253 of query aligns to 239:530/532 of 1ox5A

query
sites
1ox5A

L

L

A

T

S

R

R

R

V

I

I

I

P

A

C

C

L

L

D
|
D

I

V

-

R

-

T

-

N

D

D

H

Q

G

G

R

D

V

L

V

V

K

-

G

-

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-

Q

-

F

-

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A

-

L

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R

T

D

K

A

L

G

G

D

K

P

P

V

V

E

Q

V

L

A

A

K

Q

R

K

Y

Y

N

Y

D

Q

E

Q

G

G

A

A

D

D

E

E

I

V

T

T

F

F

L
|
L

D

N

I
|
I

S

T

A

C

S

P

Y

L

E

K

E

D

R

T

G

P

T

M

L

L

A

-

D

E

M

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V

L

S

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A

Q

V

A

A

A

A

K

Q

T

V

V

F

F

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P

P

L

L

T

T

V

V

G

G

G
|
G

G

G

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K

C

D

V

I

E

V

D

D

I

V

-

D

-

G

-

T

-

K

-

I

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P

-

A

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L

-

E

-

V

-

A

R

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T

L

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L

F

L

R

A

S

G

G

A

A

D

D

K

K

V

V

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S

I

I

N
x
G

S
x
T

A

D

A

A

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V

N

Y

D

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A

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E

L

K

-

Y

-

E

-

L

-

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-

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-

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-

G

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V

I

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A

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A

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S

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D

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K

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-

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-

K

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-

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-

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G

-

P

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-

G

E

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K

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Y

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W

Y

E

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G

G

G

R

R

R

E

G

S

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R

G

D

L

L

D

G

A

V

V

W

A

E

W

L

A

T

Q

R

R

A

M

C

A

E

A

A

Y

L

G

G

A

A

G

G

E

E

I

I

L

L

T
x
N

S

C

M

I

D

D

R

K

D
|
D

G
|
G

T

S

G

N

I

S

G

G

F

Y

D

D

L

L

A

E

L

L

T

I

R

E

A

H

I

V

S

K

D

D

A

A

V

V

P

K

V

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P

P

V

V

I

I

A

A

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S

G
x
S

G

G

V

A

G

G

E

V

I

P

R

E

H

H

F

F

V

E

E

E

G

A

I

F

Q

L

Q

K

G

T

R

R

A

A

D

D

A

A

V

C

L

L

A

G

A
|
A

S
x
G

V

M

F

F

H

H

F

R

G

G

Q

E

F

F

R

T

I

V

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N

E

D

V

V

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K

A

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M

L

A

L

A

E

A

H

G

G

I

L

P

K

V

V

R

R

active site: D248 (= D11), D386 (= D130)
binding phosphoric acid mono-[5-({[5-carbamoyl-3-(5-phosphonooxy-5-deoxy-ribofuranosyl)- 3h-imidazol-4-ylamino]-methyl}-amino)-2,3,4-trihydroxy-pentyl] ester: L283 (= L50), I285 (= I52), G313 (= G81), G346 (≠ N103), T347 (≠ S104), S384 (≠ A128), D386 (= D130), G424 (= G144), N451 (≠ T171), D456 (= D176), G457 (= G177), S482 (≠ G202), A505 (= A225), G506 (≠ S226)

3tdmA Computationally designed tim-barrel protein, halfflr (see paper)
47% identity, 40% coverage: 123:222/253 of query aligns to 1:99/120 of 3tdmA

query
sites
3tdmA

S

Q

C

A

I

V

V

V

A

A

I

I

D

D

A

A

K

K

R

R

V

V

E

D

D

G

H

E

W

F

E

M

V

V

F

F

T

T

H

Y

G

S

G

G

R

K

G

N

T

T

G

G

L

I

D

L

A

L

V

R

A

D

W

W

A

V

Q

V

R

E

M

V

A

E

A

K

Y

R

G

G

A

A

G

G

E

E

I

I

L

L

T

T

S

S

M

I

D

D

R

R

D
|
D

G
|
G

T

T

G

K

I

S

G

G

F

Y

D

D

L

T

A

E

L

M

T

I

R

R

A

F

I

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S

R

D

P

A

L

V

T

P

T

V

L

P

P

V

I

I

I

A

A

S

S

G

G

V

A

G

G

E

K

I

M

R

E

H

H

F

F

V

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E

E

G

A

I

F

Q

L

Q

R

G

G

R

-

A

A

D

D

A

K

V

V

binding phosphate ion: D54 (= D176), G55 (= G177)

Sites not aligning to the query:

binding phosphate ion: 102, 103

5ab3A S.Enterica hisa mutant d7n, d10g, dup13-15, q24l, g102a (see paper)
31% identity, 80% coverage: 6:207/253 of query aligns to 2:205/241 of 5ab3A

query
sites
5ab3A

V

I

I

I

P

P

C

A

L

L

D
x
N

I

L

D

I

H

G

G

G

R

T

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V

K

R

G

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V

V

Q
x
R

-

L

-

H

-

Q

-

G

-

D

F
x
Y

V

A

A

R

L

L

R

R

D

D

A

Y

G

G

-

N

D

D

P

P

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E

P

V

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A

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R

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Y

Y

N

A

D

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G

A

A

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x
V

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A

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A

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A

I

D

P

M

L

V

I

S

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A

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A

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N

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P

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G
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G

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V

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R

C

T

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E

E

E

D

D

I

V

R

A

T

A

L

L

L

K

A

A

G

G

A

V

D

A

K

R

V

V

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V

I

I

N
x
A

S
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S

A

T

A

A

V

V

N

K

D

S

P

P

E

D

L

V

V

V

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K

A

G

A

W

A

F

R

E

R

R

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F

G

G

N

A

S

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C

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A

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D

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-

R

R

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D

D

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H

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-

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-

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-

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-

H

-

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-

G

G

R

T

R

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G

Q

T

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G

A

L

V

D

S

A

G

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V

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S

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Q

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M

V

A

E

A

T

Y

Y

-

L

-

P

-

V

G

G

A

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G

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E

H

I

V

L

L

L

C

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T

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M

I

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S

R

R

D

D

G
|
G

T

T

G

L

I

A

G

G

F

S

D

N

L

V

A

S

L

L

T

Y

R

E

A

E

I

V

S

C

D

A

A

R

V

Y

P

P

-

Q

V

I

P

A

V

F

I

Q

A

S

S
|
S

G
|
G

V

I

G

G

E

D

I

I

active site: N7 (≠ D11), D132 (= D130)
binding [(2r,3s,4r,5r)-5-[4-aminocarbonyl-5-[[(z)-[(3r,4r)-3,4-dihydroxy-2-oxo-5-phosphonooxy-pentyl]iminomethyl]amino]imidazol-1-yl]-3,4-dihydroxy-oxolan-2-yl]methyl dihydrogen phosphate: N7 (≠ D11), R18 (≠ Q22), Y24 (≠ F23), V52 (≠ L50), G84 (= G82), A105 (≠ N103), S106 (= S104), A130 (= A128), D132 (= D130), G174 (= G177), S199 (= S201), G200 (= G202), G201 (= G203)

Sites not aligning to the query:

binding [(2r,3s,4r,5r)-5-[4-aminocarbonyl-5-[[(z)-[(3r,4r)-3,4-dihydroxy-2-oxo-5-phosphonooxy-pentyl]iminomethyl]amino]imidazol-1-yl]-3,4-dihydroxy-oxolan-2-yl]methyl dihydrogen phosphate: 222, 223

5abtA S.Enterica hisa mutant d7n, g102a, v106m, d176a
30% identity, 80% coverage: 6:207/253 of query aligns to 2:208/246 of 5abtA

query
sites
5abtA

V

I

I

I

P

P

C

A

L

L

D
x
N

I

L

D

I

H

D

G

G

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R

G

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Q

-
x
G

-

D

F

Y

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A

A

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D

A

Y

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G

-

N

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D

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A

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Y

Y

N

A

D

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G

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L

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x
V

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x
L

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A

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P

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G

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R

C

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E

E

E

D

D

I

V

R

A

T

A

L

L

L

K

A

A

G

G

A

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D

A

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x
V

I

I

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x
A

S
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S

A

T

A

A

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M

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S

P

P

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L

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A

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A

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R

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G

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A

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A

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A

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D

A

V

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-

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R

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I

E

D

D

E

H

H

-

G

-

T

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K

E

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A

T

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H

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G
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G

G
x
W

R

Q

R

E

G

N

T

S

G

G

L

V

D

S

A

L

V

E

A

Q

W

L

A

V

Q

E

R

T

M

Y

A

L

A

P

Y

V

G

G

A

L

G

K

E

H

I

V

L

L

L

C

T

T

S

D

M

I

D

S

R

R

D

A

G
|
G

T

T

G

L

I

A

G

G

F

S

D

N

L

V

A

S

L

L

T

Y

R

E

A

E

I

V

S

C

D

A

A

R

V

Y

P

P

-

Q

V

I

P

A

V

F

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A

S

S
|
S

G
|
G

G

G

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I

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G

E

D

I

I

active site: N7 (≠ D11), D129 (= D130)
binding [(2R,3S,4R,5R)-5-[4-aminocarbonyl-5-[(E)-[[(2R,3R,4S,5R)-3,4-bis(oxidanyl)-5-(phosphonooxymethyl)oxolan-2-yl]amino]methylideneamino]imidazol-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl dihydrogen phosphate: N7 (≠ D11), G19 (vs. gap), V49 (≠ L50), L51 (≠ I52), G81 (= G82), R83 (= R84), V100 (≠ S101), A102 (≠ N103), S103 (= S104), D129 (= D130), G144 (= G144), W145 (≠ G145), G177 (= G177), S202 (= S201), G203 (= G202)

Sites not aligning to the query:

binding [(2R,3S,4R,5R)-5-[4-aminocarbonyl-5-[(E)-[[(2R,3R,4S,5R)-3,4-bis(oxidanyl)-5-(phosphonooxymethyl)oxolan-2-yl]amino]methylideneamino]imidazol-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl dihydrogen phosphate: 223, 225, 226

Q9X0C7 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; EC 5.3.1.16 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
27% identity, 79% coverage: 6:204/253 of query aligns to 3:197/241 of Q9X0C7

query
sites
Q9X0C7

V

V

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D

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-

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x
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D

I

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S

A

N

S

A

Y

I

E

E

E

N

R

S

G

G

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E

-

N

-

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L

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E

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F

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I

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-

L

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R

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L

L

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L

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A

L

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G

A

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I

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N

S

S

S

A

K

A

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V

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N

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P

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A

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N

-

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K

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x
D

T

T

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G

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R

-

V

-

A

-

F

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K

G

G

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-

L

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A

-

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T

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G

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D

A

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V

A

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W

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M

L

A

K

A

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Y

Y

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G

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E

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L

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T

S

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M

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R

K

D

D

G

G

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G

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D

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F

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L

L

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T

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K

A

K

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A

A

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A

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G

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I

D8 (= D11) mutation to N: Loss of activity.
H48 (≠ T48) mutation to A: Decrease in activity.
D51 (= D51) mutation to N: Decrease in activity.
R83 (= R84) mutation to N: Decrease in activity.
D127 (≠ F141) mutation to N: Almost no activity.
T164 (= T171) mutation to A: Strong decrease in activity.

3zs4A Crystal structure of mycobacterium tuberculosis phosphoribosyl isomerase with bound prfar
26% identity, 80% coverage: 6:207/253 of query aligns to 5:205/244 of 3zs4A

query
sites
3zs4A

V

L

I

L

P

P

C
x
A

L

V

D
|
D

I

V

D

V

H

E

G

G

R

R

V

A

V

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K
x
R

G

L

V

V

Q

Q

F

G

V

K

A

A

-

G

-

S

L

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R

T

D

E

A

Y

G

G

D

S

P

A

V

V

E

D

V

A

A

A

K

L

R

G

Y

W

N

Q

D

R

E

D

G

G

A

A

D

E

E

W

I

I

T

H

F

L

L

V

D

D

I

L

S

D

A

A

S
x
A

Y
x
F

E

G

E

-

R

R

G

G

T

S

L

N

A

H

D

E

M

L

V

L

S

A

A

E

V

V

A

V

A

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Q

K

V

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F

D

I

V

P

Q

L

V

T

E

V

L

G
x
S

G

G

G
|
G

V

I

R
|
R

C

D

V

D

E

E

D

S

I

L

R

A

T

A

L

A

L

L

L

A

A

T

G

G

A

C

D

A

K

R

V

V

S

N

I

V

N
x
G

S
x
T

A

A

V

L

N

E

D

N

P

P

E

Q

L

W

V

C

R

A

A

R

A

V

A

I

R

G

R

E

F

H

G

G

N

D

S

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C

-

I

V

V

A

V

V

A

G

I

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D
|
D

A

V

K

Q

R

I

V

I

E

D

D

G

H

E

W

H

E

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V

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F

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R

G
|
G

G
x
W

R

E

R

T

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D

T

G

G

G

L

-

D

D

A

L

V

W

A

D

W

V

A

L

Q

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R

R

M

L

A

D

A

S

Y

E

G

G

A

C

G

S

E

R

I

F

L

V

T

T

S

D

M

I

D

T

R

K

D
|
D

G
|
G

T

T

G

L

I

G

G

G

F

P

D

N

L

L

A

D

L

L

T

L

R

A

A

G

I

V

S

A

D

D

A

R

V

T

P

D

V

A

P

P

V

V

I

I

A

A

S

S

G
|
G

V

V

G

S

E

S

I

L

active site: D10 (= D11), D129 (= D130)
binding phosphoric acid mono-[5-({[5-carbamoyl-3-(5-phosphonooxy-5-deoxy-ribofuranosyl)- 3h-imidazol-4-ylamino]-methyl}-amino)-2,3,4-trihydroxy-pentyl] ester: A8 (≠ C9), D10 (= D11), R18 (≠ K19), A56 (≠ S55), F57 (≠ Y56), S80 (≠ G80), G82 (= G82), R84 (= R84), G103 (≠ N103), T104 (≠ S104), D129 (= D130), G143 (= G144), W144 (≠ G145), D174 (= D176), G175 (= G177), G200 (= G202), G201 (= G203)

Sites not aligning to the query:

binding phosphoric acid mono-[5-({[5-carbamoyl-3-(5-phosphonooxy-5-deoxy-ribofuranosyl)- 3h-imidazol-4-ylamino]-methyl}-amino)-2,3,4-trihydroxy-pentyl] ester: 223, 225, 226

Query Sequence

>WP_012537568.1 NCBI__GCF_000021485.1:WP_012537568.1
MLASRVIPCLDIDHGRVVKGVQFVALRDAGDPVEVAKRYNDEGADEITFLDISASYEERG
TLADMVSAVAAQVFIPLTVGGGVRCVEDIRTLLLAGADKVSINSAAVNDPELVRAAARRF
GNSCIVVAIDAKRVEDHWEVFTHGGRRGTGLDAVAWAQRMAAYGAGEILLTSMDRDGTGI
GFDLALTRAISDAVPVPVIASGGVGEIRHFVEGIQQGRADAVLAASVFHFGQFRISEVKA
RMAAAGIPVRTTR

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