SitesBLAST

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)
33% identity, 95% coverage: 1:233/245 of query aligns to 1:233/241 of Q9X0C7

query
sites
Q9X0C7

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D8 (= D8) mutation to N: Loss of activity.
H48 (= H48) mutation to A: Decrease in activity.
D51 (= D51) mutation to N: Decrease in activity.
R83 (= R85) mutation to N: Decrease in activity.
D127 (= D130) mutation to N: Almost no activity.
T164 (= T167) mutation to A: Strong decrease in activity.

5dn1A Crystal structure of phosphoribosyl isomerase a from streptomyces coelicolor (see paper)
35% identity, 96% coverage: 3:236/245 of query aligns to 6:235/240 of 5dn1A

query
sites
5dn1A

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active site: D11 (= D8), D130 (= D130)
binding aminoimidazole 4-carboxamide ribonucleotide: G23 (= G20), L54 (= L52), F58 (= F56), S81 (≠ G81), G83 (= G83), R85 (= R85), G104 (= G104), T105 (= T105), G140 (= G140), W141 (= W141)

P16250 Phosphoribosyl isomerase A; 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; N-(5'-phosphoribosyl)anthranilate isomerase; PRAI; Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; EC 5.3.1.16; EC 5.3.1.24 from Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) (see paper)
35% identity, 96% coverage: 3:236/245 of query aligns to 6:235/240 of P16250

query
sites
P16250

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D11 (= D8) mutation to A: No activity.
R19 (= R16) mutation to A: No effect on activity toward PRA. No activity toward ProFAR.
S81 (≠ G81) mutation to T: No activity toward PRA. Almost no effect on activity toward ProFAR.
D130 (= D130) mutation to A: Very low activity toward PRA. No activity toward ProFAR.; mutation to Q: No activity.
T166 (= T167) mutation to A: No activity.
D171 (= D172) mutation to A: Low activity toward PRA. No activity toward ProFAR.

4tx9A Crystal structure of hisap from streptomyces sviceus with degraded profar (see paper)
35% identity, 96% coverage: 3:236/245 of query aligns to 11:240/246 of 4tx9A

query
sites
4tx9A

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A

active site: D16 (= D8), D135 (= D130)
binding aminoimidazole 4-carboxamide ribonucleotide: G28 (= G20), V57 (= V50), L59 (= L52), S86 (≠ G81), G88 (= G83), R90 (= R85), G109 (= G104), T110 (= T105), D135 (= D130), G145 (= G140), W146 (= W141)

2y85A Crystal structure of mycobacterium tuberculosis phosphoribosyl isomerase with bound rcdrp (see paper)
34% identity, 97% coverage: 1:238/245 of query aligns to 3:231/234 of 2y85A

query
sites
2y85A

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A

active site: D10 (= D8), D120 (= D130)
binding 1-(o-carboxy-phenylamino)-1-deoxy-d-ribulose-5-phosphate: D10 (= D8), H40 (= H48), V42 (= V50), L44 (= L52), A47 (= A55), S71 (≠ G81), R133 (≠ D139), D165 (= D172), G166 (= G173), S190 (= S197), G191 (= G198), G192 (= G199), G216 (= G223), K217 (≠ R224)

5abtA S.Enterica hisa mutant d7n, g102a, v106m, d176a
35% identity, 96% coverage: 2:236/245 of query aligns to 1:238/246 of 5abtA

query
sites
5abtA

L

M

I

I

P

P

A

A

I

L

D
x
N

L

L

K

I

D

D

G

G

K

T

C

V

V

V

R

R

L

L

R

H

Q

Q

G
|
G

R

D

M

Y

D

A

D

R

S

Q

T

R

V

D

F

Y

G

G

D

N

D

D

P

P

V

L

D

P

M

R

A

L

T

Q

R

D

W

Y

V

A

E

A

A

Q

G

G

A

A

R

G

R

V

L

L

H

H

L

L

V
|
V

D

D

L
|
L

N

T

G

G

A

A

F

K

A

D

G

P

E

A

P

K

V

R

N

Q

G

I

E

P

I

L

V

I

Q

K

A

T

I

L

A

V

R

A

K

G

Y

V

P

-

D

N

L

V

P

P

I

V

Q

Q

I

V

G

G

G
|
G

I

V

R
|
R

S

T

A

E

E

E

T

D

I

V

E

A

A

A

Y

L

L

L

K

K

A

A

G

G

V

V

Q

A

W

R

V

V

I
x
V

I

I

G
x
A

T
x
S

K

T

A

A

V

M

K

K

E

S

P

P

E

D

F

V

V

V

T

K

E

G

M

W

C

F

K

E

K

R

F

F

P

G

G

A

H

Q

-

A

I

L

I

V

V

L

G

A

L

L

D
|
D

A

V

K

R

-

I

-

D

-

E

-

H

-

G

D

T

G

K

R

Q

V

V

A

A

T

V

D

S

G
|
G

W
|
W

A

Q

E

E

V

N

S

S

E

G

V

V

M

S

A

L

T

E

D

Q

L

L

A

V

K

E

R

T

F

Y

A

L

N

P

D

V

G

G

V

L

D

K

A

H

I

V

V

L

Y

C

T

T

D

D

I

I

S

S

R

R

D

A

G
|
G

M

T

M

L

Q

A

G

G

V

S

N

N

V

V

E

S

A

L

T

Y

A

E

L

V

-

C

A

A

E

R

E

Y

G

P

G

Q

I

I

P

A

V

F

I

Q

A

S

S
|
S

G
|
G

G

G

V

I

T

G

N

D

M

I

D

D

L

-

K

-

R

-

L

I

A

A

T

A

V

L

A

R

D

G

K

T

G

G

I

V

L

R

G

G

A

V

I
|
I

T

V

G
|
G

R
|
R

A

A

I

L

Y

L

E

E

G

G

T

K

L

F

D

T

V

V

A

K

E

E

A

A

active site: N7 (≠ D8), 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 (≠ D8), G19 (= G20), V49 (= V50), L51 (= L52), G81 (= G83), R83 (= R85), V100 (≠ I102), A102 (≠ G104), S103 (≠ T105), D129 (= D130), G144 (= G140), W145 (= W141), G177 (= G173), S202 (= S197), G203 (= G198), I223 (= I221), G225 (= G223), R226 (= R224)

5ab3A S.Enterica hisa mutant d7n, d10g, dup13-15, q24l, g102a (see paper)
35% identity, 96% coverage: 2:236/245 of query aligns to 1:235/241 of 5ab3A

query
sites
5ab3A

L

M

I

I

P

P

A

A

I

L

D
x
N

L

L

K

I

D

G

G

G

-

T

-

V

K

R

C

V

V

V

R
|
R

L

L

R

H

Q

Q

G

G

R

D

M
x
Y

D

A

D

R

S

L

T

R

V

D

F

Y

G

G

D

N

D

D

P

P

V

L

D

P

M

R

A

L

T

Q

R

D

W

Y

V

A

E

A

A

Q

G

G

A

A

R

G

R

V

L

L

H

H

L

L

V
|
V

D

D

L

L

N

T

G

G

A

A

F

K

A

D

G

P

E

A

P

K

V

R

N

Q

G

I

E

P

I

L

V

I

Q

K

A

T

I

L

A

V

R

A

K

G

Y

V

P

-

D

N

L

V

P

P

I

V

Q

Q

I

V

G

G

G
|
G

I

V

R

R

S

T

A

E

E

E

T

D

I

V

E

A

A

A

Y

L

L

L

K

K

A

A

G

G

V

V

Q

A

W

R

V

V

I

V

I

I

G
x
A

T
x
S

K

T

A

A

V

V

K

K

E

S

P

P

E

D

F

V

V

V

T

K

E

G

M

W

C

F

K

E

K

R

F

F

P

G

G

A

H

Q

-

A

I

L

I

V

V

L

G
x
A

L

L

D
|
D

A

V

K

R

D

I

G

D

R

E

V

H

A

G

T

T

D

K

G

Q

W

V

A

A

E

-

V

V

S

S

E

G

V

V

M

S

A

L

T

E

D

Q

L

L

A

V

K

E

R

T

F

Y

A

L

N

P

D

V

G

G

V

L

D

K

A

H

I

V

V

L

Y

C

T

T

D

D

I

I

S

S

R

R

D

D

G
|
G

M

T

M

L

Q

A

G

G

V

S

N

N

V

V

E

S

A

L

T

Y

A

E

L

V

-

C

A

A

E

R

E

Y

G

P

G

Q

I

I

P

A

V

F

I

Q

A

S

S
|
S

G
|
G

V

I

T

G

N

D

M

I

D

D

L

-

K

-

R

-

L

I

A

A

T

A

V

L

A

R

D

G

K

T

G

G

I

V

L

R

G

G

A

V

I

I

T

V

G
|
G

R
|
R

A

A

I

L

Y

L

E

E

G

G

T

K

L

F

D

T

V

V

A

K

E

E

A

A

active site: N7 (≠ D8), 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 (≠ D8), R18 (= R16), Y24 (≠ M22), V52 (= V50), G84 (= G83), A105 (≠ G104), S106 (≠ T105), A130 (≠ G128), D132 (= D130), G174 (= G173), S199 (= S197), G200 (= G198), G201 (= G199), G222 (= G223), R223 (= R224)

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)
27% identity, 97% coverage: 3:239/245 of query aligns to 6:247/258 of P60664

query
sites
P60664

I

I

P

P

A

C

I

L

D

D

L

V

K

R

D

D

G

G

K

Q

C

V

V

V

R

K

L

G

R

V

Q

Q

G

F

R

R

M

-

D

-

D

N

S

H

T

E

V

I

F

I

G

G

D

D

D

-

P

I

V

V

D

P

M

L

A

A

T

K

R

R

W

Y

V

A

E

E

A

E

G

G

A

A

R

D

R
x
E

L

L

H

V

L

F

V

Y

D

D

L

I

N

T

G

A

A

S

F

S

A

D

G

G

E

R

P

V

V

V

N

D

G

K

E

S

I

W

V

V

Q

S

A

R

I

V

A

A

R

-

K

E

Y

V

P

I

D

D

L

I

P

P

I

F

Q

C

I

V

G

A

G

G

I

I

R

K

S

S

A

L

E

E

T

D

I

A

E

A

A

K

Y

I

L

L

K

S

A

F

G

G

V

A

Q

D

W

K

V

I

I

S

I

I

G

N

T

S

K

P

A

A

V

L

K

A

E

D

P

P

E

T

F

L

V

I

T

T

E

R

M

L

C

A

K

D

K

R

F

F

P

G

G

V

H
x
Q

-
x
C

I

I

I

V

V

V

G

G

L

I

-

D

-

T

-

W

-

Y

D

D

A

A

K

E

D

T

G

G

R

K

V

Y

A

H

T

V

D

N

G

Q

W

Y

-

T

-

G

-

D

-

E

-

S

-

R

A

T

E

R

V

V

S

T

E

Q

V

W

M

E

A

T

T

L

D

D

L

W

A

V

K

Q

R

E

F

V

A

Q

N

K

D

R

G

G

V

A

D

G

A

E

I

I

V

V

Y

L

T

N

D

M

I

M

S

N

R

Q

D

D

G

G

M

V

M

R

Q

N

G

G

V

Y

N

D

V

L

E

E

A

Q

T

L

A

K

L

V

A

R

E

E

E

V

G

C

G

H

I

V

P

P

V

L

I

I

A

A

S

S

G

G

V

A

T

G

N

T

M

M

D

E

D

H

L

F

K

-

R

-

L

L

A

E

T

A

V

F

A

R

D

D

K

A

G

D

I

V

L

D

G

G

A

A

I

L

T

A

G

A

R

S

A

V

I

F

Y

H

E

K

G

Q

T

I

L

I

D

N

V

I

A

G

E

E

A

L

Q

K

A

A

F

Y

E46 (≠ R46) mutation to A: Loss of activity.; mutation to G: Loss of IGP synthase activity. Weak IGP synthase and HisH activities in vitro.
Q123 (≠ H124) mutation to A: Decrease in activity.; mutation to R: Loss of IGP synthase activity. Weak HisH activity in vitro.
C124 (vs. gap) mutation to A: No change in activity.; mutation to R: Loss of IGP synthase activity. Weak HisH activity in vitro.

Sites not aligning to the query:

5 R→A: Loss of activity.; R→H: Loss of IGP synthase activity. Weak IGP synthase activity and reduced HisH activity in vitro.

1h5yB Hisf protein from pyrobaculum aerophilum (see paper)
32% identity, 84% coverage: 1:206/245 of query aligns to 5:213/253 of 1h5yB

query
sites
1h5yB

M

L

L

R

I

I

P

P

A

C

I

L

D
|
D

L

I

K

D

D

G

G

G

K

A

C

K

V

V

R

V

L

V

R
x
K

Q

G

G

V

R

N

M

F

D

Q

D

G

S

I

T

R

V

E

F

V

G

G

D

D

D

-

P

P

V

V

D

E

M

M

A

A

T

V

R

R

W

Y

V

E

E

E

A

E

G

G

A

A

R

D

R

E

L

I

H

A

L

I

V

L

D

D

L

I

N

T

G

A

A

A

F

P

A

E

G

G

E

R

P

A

V

T

N

F

G

I

E

D

I

S

V

V

Q

K

A

R

I

V

A

A

R

E

K

A

Y

V

P

-

D

S

L

I

P

P

I

V

Q

L

I

V

G

G

G
|
G

I

V

R

R

S

S

A

L

E

E

T

D

I

A

E

T

A

T

Y

L

L

F

K

R

A

A

G

G

V

A

Q

D

W

K

V

V

I

S

I

V

G
x
N

T
|
T

K

A

A

A

V

V

K

R

E

N

P

P

E

Q

F

L

V

V

T

A

E

L

M

L

C

A

K

R

K

E

F

F

P

G

G

S

H

Q

-

S

I

T

I

V

V

V

G
x
A

L

I

D
|
D

A

A

K

K

-

W

D

N

G

G

R

E

-

Y

-

E

V

V

A

Y

T

V

D

K

G
|
G

W

G

A

R

E

E

V

A

S

T

E

G

V

L

M

D

A

A

T

V

D

K

L

W

A

A

K

K

R

E

F

V

A

E

N

E

D

L

G

G

V

A

D

G

A

E

I

I

V

L

Y

L

T
|
T

D

S

I

I

S

D

R

R

D
|
D

G
|
G

M

T

M

G

Q

L

G

G

V

Y

N

D

V

V

E

E

A

L

T

I

A

R

L

V

A

A

E

D

E

S

G

V

G

R

I

I

P

P

V

V

I

I

A

A

S

S

G

G

V

A

T

G

N

R

M

V

D

E

D

H

L

F

active site: D12 (= D8), D133 (= D130)
binding glycerol: K22 (≠ R18), N106 (≠ G104), A131 (≠ G128), D133 (= D130), G147 (= G140), T174 (= T167), D179 (= D172)
binding phosphate ion: G84 (= G82), G85 (= G83), N106 (≠ G104), T107 (= T105), D179 (= D172), G180 (= G173)

Sites not aligning to the query:

binding phosphate ion: 226, 227, 228

7ac8A Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. (see paper)
29% identity, 83% coverage: 3:206/245 of query aligns to 6:210/252 of 7ac8A

query
sites
7ac8A

I

I

P

A

A

C

I

L

D
|
D

L

V

K

K

D

D

G

G

K

R

C

V

V

V

R

K

L

-

R

-

Q

-

G

G

R

T

M

N

D

F

D

E

S

N

T

L

V

R

F

D

G

S

D

G

D

D

P

P

V

V

D

E

M

L

A

G

T

K

R

F

W

Y

V

S

E

E

A

I

G

G

A

I

R

D

R

E

L

L

H

V

L

F

V
x
L

D

D

L
x
I

N

T

G

A

A

S

F

V

A

E

G

K

E

R

P

K

V

T

N

M

G

L

E

E

I

L

V

V

Q

E

A

K

I

V

A

A

R

E

K

Q

Y

I

P

-

D

D

L

I

P

P

I

F

Q

T

I

V

G

G

G
|
G

I

I

R

H

S

D

A

F

E

E

T

T

I

A

E

S

A

E

Y

L

L

I

K

L

A

R

G

G

V

A

Q

D

W

K

V

V

I

S

I

I

G
x
N

T
|
T

K

A

A

A

V

V

K

E

E

N

P

P

E

S

F

L

V

I

T

T

E

Q

M

I

C

A

K

Q

K

T

F

F

P

G

G

S

H

Q

-

A

I

V

V

V

G

A

L

I

D
|
D

A

A

K

K

-

R

-

V

D

D

G

G

R

E

-

F

-

M

V

V

A

F

T

T

D

Y

G
x
S

W

G

A

K

E

K

V

N

S

T

E

G

V

I

M

L

A

L

T

R

D

D

L

W

A

V

K

V

R

E

F

V

A

E

N

K

D

R

G

G

V

A

D

G

A

E

I

I

V

L

Y

L

T

T

D

S

I

I

S

D

R

R

D
|
D

G
|
G

M

T

M

K

Q

S

G

G

V

Y

N

D

V

T

E

E

A

M

T

I

A

R

A

F

L

V

A

R

E

P

E

L

G

T

I

L

P

P

V

I

I

I

A

A

S
|
S

G

G

V

A

T

G

N

K

M

M

D

E

D

H

L

F

active site: D11 (= D8), 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 (≠ V50), I52 (≠ L52), G82 (= G83), N103 (≠ G104), T104 (= T105), D130 (= D130), S144 (≠ G140), D176 (= D172), G177 (= G173), S201 (= S197)

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: 225

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)
29% identity, 83% coverage: 3:206/245 of query aligns to 6:210/253 of Q9X0C6

query
sites
Q9X0C6

I

I

P

A

A
x
C

I

L

D
|
D

L

V

K

K

D

D

G

G

K

R

C

V

V

V

R
x
K

L

-

R

-

Q

-

G

G

R

T

M

N

D

F

D

E

S

N

T

L

V

R

F

D

G

S

D

G

D

D

P

P

V

V

D

E

M

L

A

G

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K

R

F

W

Y

V

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E

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I

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G

A

I

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R

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L

L

H

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L

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V

L

D
|
D

L

I

N

T

G

A

A

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F

V

A

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G

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K

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V

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A

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-

D

D

L

I

P

P

I

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Q

T

I

V

G

G

I

I

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D

A

F

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E

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T

I

A

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A

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Y

L

L

I

K

L

A

R

G

G

V

A

Q

D

W

K

V

V

I

S

I

I

G
x
N

T

T

K

A

A

A

V

V

K

E

E

N

P

P

E

S

F

L

V

I

T

T

E

Q

M

I

C

A

K

Q

K

T

F

F

P

G

G

S

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Q

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A

I

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G

A

L

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D

A

A

K

K

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R

-

V

D

D

G

G

R

E

-

F

-

M

V

V

A

F

T

T

D

Y

G

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W

G

A

K

E

K

V

N

S

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E

G

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M

L

A

L

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R

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D

L

W

A

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K

V

R

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F

V

A

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K

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R

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G

V

A

D

G

A

E

I

I

V

L

Y

L

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T

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S

I

I

S

D

R

R

D
|
D

G

G

M

T

M

K

Q

S

G

G

V

Y

N
x
D

V

T

E

E

A

M

T

I

A

R

A

F

L

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A

R

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P

E

L

G

T

I

L

P

P

V

I

I

I

A

A

S

S

G

G

V

A

T

G

N

K

M

M

D

E

D

H

L

F

C9 (≠ A6) mutation to A: No change in activity.
D11 (= D8) mutation to X: Loss of activity.
K19 (≠ R16) mutation to S: Decrease in activity.
D51 (= D51) mutation to N: No change in activity.
N103 (≠ G104) 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 (= D172) mutation to N: Decrease in activity.
D183 (≠ N179) mutation to N: No change in activity.

3zr4E Structural evidence for ammonia tunneling across the (beta-alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex (see paper)
28% identity, 83% coverage: 3:206/245 of query aligns to 6:201/244 of 3zr4E

query
sites
3zr4E

I

I

P

A

A

C

I

L

D
|
D

L

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K

K

D

D

G

G

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-

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Q

-

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M

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G

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D

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D

E

M

L

A

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E

A

I

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G

A

I

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L

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L

F

V

L

D

D

L

I

N

T

G

A

A

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K

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T

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M

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E

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A

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I

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A

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K

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Y

I

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-

D

D

L

I

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P

I

F

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T

I

V

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G

I

I

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S

D

A

F

E

E

T

T

I

A

E

S

A

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Y

L

L

I

K

L

A

R

G

G

V

A

Q

D

W

K

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V

I

S

I

I

G

N

T

T

K

A

A

A

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V

K

E

E

N

P

P

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F

L

V

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T

T

E

Q

M

I

C

A

K

Q

K

T

F

F

P

G

G

S

H

Q

-

A

I

V

V

V

G

A

L

I

D
|
D

A

A

K

K

-

R

-

V

D

D

G

G

R

E

-

F

-

M

V

V

A

F

T

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Y

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S

W

G

A

K

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V

N

S

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G

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M

L

A

L

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D

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W

A

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V

R

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F

V

A

E

N

K

D

R

G

G

V

A

D

G

A

E

I

I

V

L

Y

L

T

T

D

S

I

I

S

D

R

R

D

D

G

G

M

T

M

K

Q

S

G

G

V

Y

N

D

V

T

E

E

A

M

T

I

A
x
R

A

F

L

V

A

R

E

P

E

L

G

T

I

L

P

P

V

I

I

I

A

A

S

S

G

G

V

A

T

G

N

K

M

M

D

E

D

H

L

F

active site: D11 (= D8), D121 (= D130)
binding glycerol: R179 (≠ A184)

Sites not aligning to the query:

binding glycerol: 206

1gpwC Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex. (see paper)
28% identity, 83% coverage: 3:206/245 of query aligns to 6:210/253 of 1gpwC

query
sites
1gpwC

I

I

P

A

A

C

I

L

D
x
N

L

V

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K

D

D

G

G

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V

R

K

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Q

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G

G

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M

N

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S

N

T

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G

A

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M

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E

A

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V

A

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K

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D

D

L

I

P

P

I

F

Q

T

I

V

G

G

G
|
G

I

I

R

H

S

D

A

F

E

E

T

T

I

A

E

S

A

E

Y

L

L

I

K

L

A

R

G

G

V

A

Q

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W

K

V

V

I

S

I

I

G
x
N

T
|
T

K

A

A

A

V

V

K

E

E

N

P

P

E

S

F

L

V

I

T

T

E

Q

M

I

C

A

K

Q

K

T

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F

P

G

G

S

H

Q

-

A

I

V

V

V

G

A

L

I

D
|
D

A

A

K

K

-

R

-

V

D

D

G

G

R

E

-

F

-

M

V

V

A

F

T

T

D

Y

G

S

W

G

A

K

E

K

V

N

S

T

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G

V

I

M

L

A

L

T

R

D

D

L

W

A

V

K

V

R

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F

V

A

E

N

K

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R

G

G

V

A

D

G

A

E

I

I

V

L

Y

L

T

T

D

S

I

I

S

D

R

R

D
|
D

G
|
G

M

T

M

K

Q

S

G

G

V

Y

N

D

V

T

E

E

A

M

T

I

A

R

A

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L

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A

R

E

P

E

L

G

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L

P

P

V

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I

I

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A

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S

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G

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A

T

G

N

K

M

M

D

E

D

H

L

F

active site: N11 (≠ D8), D130 (= D130)
binding phosphate ion: G82 (= G83), N103 (≠ G104), T104 (= T105), D176 (= D172), G177 (= G173)

Sites not aligning to the query:

binding phosphate ion: 225

7qc8A Imidazole glycerol phosphate synthase subunit HisF (see paper)
28% identity, 83% coverage: 3:206/245 of query aligns to 6:210/250 of 7qc8A

query
sites
7qc8A

I

I

P

A

A

A

I

L

D
x
E

L

V

K

K

D

D

G

G

K

R

C

V

V

V

R

K

L

-

R

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Q

-

G

G

R

T

M

N

D

F

D

E

S

N

T

L

V

R

F

D

G

S

D

G

D

D

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P

V

A

D

E

M

L

A

G

T

K

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F

W

Y

V

S

E

E

A

I

G

G

A

I

R

D

R

E

L

L

H

V

L

F

V
x
H

D

D

L
x
H

N

T

G

A

A

S

F

V

A

E

G

K

E

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P

K

V

T

N

M

G

L

E

E

I

L

V

V

Q

E

A

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A

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R

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K

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I

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-

D

D

L

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D

A

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L

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T

T

K

A

A

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L

V

I

T

T

E

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M

I

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K

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K

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F

P

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G

S

H

Q

-

A

I

V

V

V

G

A

L

I

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D

A

A

K

K

-

R

-

V

D

D

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E

-

F

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M

V

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F

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Y

G

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A

K

E

K

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N

S

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M

L

A

L

T

R

D

D

L

W

A

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K

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A

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N

K

D

R

G

G

V

A

D

G

A

E

I

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L

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T

D

S

I

I

S

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R

R

D

D

G

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K

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S

G

G

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Y

N

D

V

T

E

E

A

M

T

I

A

R

A

F

L

V

A

R

E

P

E

L

G

T

I

L

P

P

V

I

I

I

A

A

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S

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G

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A

T

G

N

K

M

M

D

E

D

H

L

F

binding zinc ion: E11 (≠ D8), H50 (≠ V50), H52 (≠ L52)

2wjzE Crystal structure of (hish) k181a y138a mutant of imidazoleglycerolphosphate synthase (hish hisf) which displays constitutive glutaminase activity (see paper)
29% identity, 83% coverage: 3:206/245 of query aligns to 6:196/237 of 2wjzE

query
sites
2wjzE

I

I

P

A

A

C

I

L

D
|
D

L

V

K

K

D

D

G

G

K

R

C

V

V

V

R

-

L

-

R

-

Q

-

G

-

R

-

M

-

D

-

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-

T

-

V

-

F

-

G

-

D

G

D

D

P

P

V

V

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M

L

A

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A

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G

A

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E

L

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H

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F

V

L

D

D

L

I

N

T

G

-

A

-

F

-

A

A

G

K

E

R

P

K

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N

M

G

L

E

E

I

L

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V

Q

E

A

K

I

V

A

A

R

E

K

Q

Y

I

P

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D

D

L

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P

I

F

Q

T

I

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G

G

G
|
G

I

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H

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D

A

F

E

E

T

T

I

A

E

S

A

E

Y

L

L

I

K

L

A

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G

G

V

A

Q

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W

K

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V

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S

I

I

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x
N

T
|
T

K

A

A

A

V

V

K

E

E

N

P

P

E

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F

L

V

I

T

T

E

Q

M

I

C

A

K

Q

K

T

F

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G

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Q

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A

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V

G

A

L

I

D
|
D

A

A

K

K

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R

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D

G

G

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E

-

F

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M

V

V

A

F

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T

D

Y

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G

A

K

E

K

V

N

S

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M

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A

L

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D

L

W

A

V

K

V

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G

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A

D

G

A

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L

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T

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I

S

D

R

R

D

D

G

G

M

T

M

K

Q

S

G

G

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Y

N

D

V

T

E

E

A

M

T

I

A

R

A

F

L

V

A

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E

L

G

T

I

L

P

P

V

I

I

I

A

A

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S

G

G

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A

T

G

N

K

M

M

D

E

D

H

L

F

active site: D11 (= D8), D116 (= D130)
binding phosphate ion: G68 (= G83), N89 (≠ G104), T90 (= T105)

4ewnD Structure of hisf-d130v+d176v with bound rcdrp (see paper)
28% identity, 83% coverage: 3:206/245 of query aligns to 5:203/243 of 4ewnD

query
sites
4ewnD

I

I

P

A

A

C

I

L

D

D

L

V

K

K

D

D

G

G

K

R

C

V

V

V

R

K

L

-

R

-

Q

-

G

G

R

T

M

N

D

F

D

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N

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D

G

D

D

P

P

V

V

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M

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E

E

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G

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L

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V

L

D

D

L

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N

T

G

K

A

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M

A

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G

-

E

-

P

-

V

-

N

-

G

-

E

E

I

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E

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A

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K

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Y

I

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L

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A

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G

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A

I

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V

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A

L

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x
V

A

A

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K

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D

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E

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M

V

V

A

F

T

T

D

Y

G

S

W

G

A

K

E

K

V

N

S

T

E

G

V

I

M

L

A

L

T

R

D

D

L

W

A

V

K

V

R

E

F

V

A

E

N

K

D

R

G

G

V

A

D

G

A

E

I

I

V

L

Y

L

T

T

D

S

I

I

S

D

R

R

D

V

G
|
G

M

T

M

K

Q

S

G

G

V

Y

N

D

V

T

E

E

A

M

T

I

A

R

A

F

L

V

A

R

E

P

E

L

G

T

I

L

P

P

V

I

I

I

A

A

S
|
S

G
|
G

V

A

T

G

N

K

M

M

D

E

D

H

L

F

binding 1-(O-carboxy-phenylamino)-1-deoxy-D-ribulose-5-phosphate: V123 (≠ D130), G170 (= G173), S194 (= S197), G195 (= G198), G196 (= G199)

Sites not aligning to the query:

binding 1-(O-carboxy-phenylamino)-1-deoxy-D-ribulose-5-phosphate: 215, 216, 217, 218

5d2tA Directed evolutionary changes in kemp eliminase ke07 - crystal 3 wild type
27% identity, 83% coverage: 3:206/245 of query aligns to 4:208/251 of 5d2tA

query
sites
5d2tA

I

I

P

A

A

A

I

L

D

I

L

V

K

K

D

D

G

G

K

R

C

V

V

V

R

K

L

-

R

-

Q

-

G

G

R

S

M

N

D

F

D

E

S

N

T

L

V

R

F

D

G

S

D

G

D

D

P

P

V

V

D

E

M

L

A

G

T

K

R

F

W

Y

V

S

E

E

A

I

G

G

A

I

R

D

R

E

L

L

H

S

L

F

V
x
W

D

D

L

I

N

T

G

A

A

S

F

V

A

E

G

K

E

R

P

K

V

T

N

M

G

L

E

E

I

L

V

V

Q

E

A

K

I

V

A

A

R

E

K

Q

Y

I

P

-

D

D

L

I

P

P

I

F

Q

T

I

V

G

G

I

I

R

H

S

D

A

F

E

E

T

T

I

A

E

S

A

E

Y

L

L

I

K

L

A

R

G

G

V

A

Q

D

W

K

V

V

I
x
E

I

I

G

N

T

T

K

A

A

A

V

V

K

E

E

N

P

P

E

S

F

L

V

I

T

T

E

Q

M

I

C

A

K

Q

K

T

F

F

P

G

G

S

H

Q

-

A

I

V

V

V

G
x
Y

L

I

D

A

A

A

K

K

-

R

-

V

D

D

G

G

R

E

-

F

-

M

V

V

A

F

T

T

D

Y

G

S

W

G

A

K

E

K

V

N

S

T

E

G

V

I

M

L

A

L

T

R

D

D

L

W

A

V

K

V

R

E

F

V

A

E

N

K

D

R

G

G

V

A

D

G

A

E

I

I

V

V

Y

L

T

G

D

S

I

I

S

D

R

R

D

L

G

G

M

T

M

K

Q

S

G

G

V

Y

N

D

V

T

E

E

A

M

T

I

A

R

A

F

L

V

A

R

E

P

E

L

G

T

I

L

P

P

V

I

I

I

A

A

S

H

G

G

V

A

T

G

N

K

M

M

D

E

D

H

L

F

binding 5-nitro-2-oxidanyl-benzenecarbonitrile: W48 (≠ V50), E99 (≠ I102), Y126 (≠ G128)

Sites not aligning to the query:

binding 5-nitro-2-oxidanyl-benzenecarbonitrile: 220

6dnjA Directed evolutionary changes in kemp eliminase ke07 - crystal 28 round 5 (see paper)
26% identity, 82% coverage: 6:206/245 of query aligns to 8:209/250 of 6dnjA

query
sites
6dnjA

A

A

I

L

D

I

L

M

K

K

D

D

G

G

K

R

C

V

V

V

R

K

L

-

R

-

Q

-

G

G

R

S

M

N

D

F

D

E

S

N

T

L

V

R

F

D

G

S

D

G

D

D

P

P

V

V

D

E

M

L

A

G

T

K

R

F

W

Y

V

S

E

E

A

I

G

G

A

I

R

D

R

E

L

L

H

S

L

F

V
x
W

D

D

L

I

N

T

G

A

A

S

F

V

A

E

G

K

E

R

P

K

V

T

N

M

G

L

E

E

I

L

V

V

Q

E

A

K

I

V

A

A

R

E

K

Q

Y

I

P

-

D

D

L

I

P

P

I

F

Q

T

I

V

G
|
G

G

G

I

I

R

H

S

D

A

F

E

E

T

T

I

A

E

S

A

E

Y

L

L

I

K

L

A

R

G

G

V

A

Q

D

W

K

V

V

I

E

I

I

G
x
N

T

T

K

A

A

A

V

V

K

E

E

N

P

P

E

S

F

L

V

I

T

T

E

Q

M

I

C

A

K

Q

K

T

F

F

P

G

G

S

H

Q

-

A

I

V

V

V

G
x
Y

L

I

D

A

A

A

K

K

-

R

-

V

D

D

G

G

R

E

-

F

-

M

V

V

A

F

T

T

D

Y

G

S

W

G

A

K

E

K

V

N

S

T

E

G

V

I

M

L

A

L

T

R

D

D

L

W

A

V

K

V

R

E

F

V

A

E

N

K

D

R

G

G

V

A

D

G

A

E

I

I

V

V

Y

L

T

G

D

S

I

I

S

D

R

R

D

L

G

G

M

T

M

K

Q

S

G

G

V

Y

N

D

V

T

E

E

A

M

T

I

A

R

A

F

L

V

A

R

E

P

E

L

G

T

I

L

P

P

V

I

I

I

A

A

S

H

G

R

G

G

V

A

T

G

N

K

M

M

D

E

D

H

L

F

binding 5-nitro-1,2-benzoxazole: W49 (≠ V50), G79 (= G81), G80 (= G82), N102 (≠ G104), Y127 (≠ G128)

Query Sequence

>GFF3066 FitnessBrowser__Marino:GFF3066
MLIIPAIDLKDGKCVRLRQGRMDDSTVFGDDPVDMATRWVEAGARRLHLVDLNGAFAGEP
VNGEIVQAIARKYPDLPIQIGGGIRSAETIEAYLKAGVQWVIIGTKAVKEPEFVTEMCKK
FPGHIIVGLDAKDGRVATDGWAEVSEVMATDLAKRFANDGVDAIVYTDISRDGMMQGVNV
EATAALAEEGGIPVIASGGVTNMDDLKRLATVADKGILGAITGRAIYEGTLDVAEAQAFC
DGLKG

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