SitesBLAST

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, 97% coverage: 3:233/239 of query aligns to 6:236/240 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 (≠ G80) mutation to T: No activity toward PRA. Almost no effect on activity toward ProFAR.
D130 (= D129) mutation to A: Very low activity toward PRA. No activity toward ProFAR.; mutation to Q: No activity.
T166 (= T166) mutation to A: No activity.
D171 (= D171) mutation to A: Low activity toward PRA. No activity toward ProFAR.

2y85A Crystal structure of mycobacterium tuberculosis phosphoribosyl isomerase with bound rcdrp (see paper)
35% identity, 99% coverage: 1:237/239 of query aligns to 3:234/234 of 2y85A

query
sites
2y85A

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active site: D10 (= D8), D120 (= D129)
binding 1-(o-carboxy-phenylamino)-1-deoxy-d-ribulose-5-phosphate: D10 (= D8), H40 (= H48), V42 (= V50), L44 (= L52), A47 (= A55), S71 (≠ G80), R133 (≠ N138), D165 (= D171), G166 (= G172), S190 (= S196), G191 (= G197), G192 (= G198), G216 (= G219), K217 (= K220)

5abtA S.Enterica hisa mutant d7n, g102a, v106m, d176a
29% identity, 97% coverage: 2:233/239 of query aligns to 1:239/246 of 5abtA

query
sites
5abtA

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active site: N7 (≠ D8), D129 (= D129)
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 (= G82), R83 (= R84), V100 (≠ I101), A102 (≠ G103), S103 (≠ T104), D129 (= D129), G144 (= G139), W145 (= W140), G177 (= G172), S202 (= S196), G203 (= G197), I223 (= I217), G225 (= G219), R226 (≠ K220)

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)
31% identity, 93% coverage: 1:222/239 of query aligns to 1:226/241 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 (= R84) mutation to N: Decrease in activity.
D127 (= D129) mutation to N: Almost no activity.
T164 (= T166) mutation to A: Strong decrease in activity.

5ab3A S.Enterica hisa mutant d7n, d10g, dup13-15, q24l, g102a (see paper)
28% identity, 97% coverage: 2:233/239 of query aligns to 1:236/241 of 5ab3A

query
sites
5ab3A

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Y

R

G

G

A

V

I

I

V

V

G
|
G

K
x
R

A

A

I

L

Y

L

S

E

E

G

K

K

I

F

N

T

L

V

K

K

E

E

A

A

I

I

active site: N7 (≠ D8), D132 (= D129)
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 (≠ F22), V52 (= V50), G84 (= G82), A105 (≠ G103), S106 (≠ T104), A130 (≠ G127), D132 (= D129), G174 (= G172), S199 (= S196), G200 (= G197), G201 (= G198), G222 (= G219), R223 (≠ K220)

1h5yB Hisf protein from pyrobaculum aerophilum (see paper)
30% identity, 82% coverage: 3:198/239 of query aligns to 7:206/253 of 1h5yB

query
sites
1h5yB

I

I

L

I

P

P

A

C

I

L

D
|
D

I

I

K

D

Q

G

G

G

K

A

C

K

V

V

R

V

L

V

Y
x
K

Q

G

G

V

R

N

F

F

E

Q

K

G

S

I

S

R

V

E

V

V

A

G

E

D

S

-

P

P

A

V

L

E

T

M

A

A

K

V

S

R

F

Y

E

E

N

E

D

E

G

G

A

A

K

D

Y

E

I

I

H

A

V

I

V

L

D

D

L

I

D

T

G

A

A

A

L

P

E

E

G

G

E

R

I

A

I

T

N

F

L

I

D

D

A

S

V

V

K

K

S

R

I

V

V

A

Q

E

V

A

T

V

S

S

V

I

P

P

I

V

E

L

L

V

G

G

G
|
G

I

V

R

R

N

S

I

L

K

E

V

D

V

A

E

T

K

T

L

L

I

F

N

R

I

A

G

G

V

A

K

D

R

K

I

V

I

S

L

V

G
x
N

T
|
T

A

A

L

V

K

R

D

N

K

P

E

Q

F

L

T

V

R

A

E

L

A

L

I

A

K

R

E

E

Y

F

G

G

-

S

K

Q

S

S

I

T

A

V

V

V

G
x
A

I

I

D
|
D

A

A

K

K

-

W

-

N

-

G

D

E

G

Y

Y

Y

-

E

V

V

A

Y

V

V

N

K

G
|
G

W

G

L

R

N

E

V

A

S

T

K

G

I

L

N

D

Y

A

I

V

E

K

F

W

A

A

K

K

I

E

M

V

E

E

D

E

M

L

G

G

T

A

E

G

D

E

I

I

I

L

L

L

T
|
T

D

S

I

I

S

D

K

R

D
|
D

G
|
G

T

T

L

G

K

L

G

G

P

Y

N

D

F

V

D

E

M

L

L

I

K

R

L

V

Q

A

E

D

N

S

V

V

N

R

C

I

N

P

I

V

T

I

A

A

S

S

G

G

active site: D12 (= D8), D133 (= D129)
binding glycerol: K22 (≠ Y18), N106 (≠ G103), A131 (≠ G127), D133 (= D129), G147 (= G139), T174 (= T166), D179 (= D171)
binding phosphate ion: G84 (= G81), G85 (= G82), N106 (≠ G103), T107 (= T104), D179 (= D171), G180 (= G172)

Sites not aligning to the query:

binding phosphate ion: 226, 227, 228

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)
23% identity, 96% coverage: 3:231/239 of query aligns to 6:243/258 of P60664

query
sites
P60664

I

I

L

I

P

P

A

C

I

L

D

D

I

V

K

R

Q

D

G

G

K

Q

C

V

V

V

R

K

L

G

Y

V

Q

Q

G

-

R

-

F

F

E

R

K

N

S

H

S

E

V

I

A

G

E

D

S

I

P

V

A

P

L

L

T

-

A

A

K

K

S

R

F

Y

E

A

N

E

D

E

G

G

A

A

K

D

Y
x
E

I

L

H

V

V

F

V

Y

D

D

L

I

D

T

G

A

A

S

L

S

E

D

G

G

E

R

I

V

N

D

L

K

D

S

A

W

V

V

K

S

S

R

I

V

V

A

Q

E

V

V

T

I

S

D

V

I

P

P

I

F

E

C

L

V

G

A

G

G

I

I

R

K

N

S

I

L

K

E

V

D

V

A

E

A

K

K

L

I

I

L

N

S

I

F

G

G

V

A

K

D

R

K

I

I

I

S

L

I

G

N

T

S

A

P

A

A

L

L

K

A

D

D

K

P

E

T

F

L

T

I

R

T

E

R

A

L

I

A

K

D

E

R

Y

F

G

G

-

V

K
x
Q

S
x
C

I

I

A

V

V

V

G

G

I

I

-

D

-

T

-

W

-

Y

D

D

A

A

K

E

D

T

G

G

Y

K

V

Y

A

H

V

V

N

N

G

Q

W

Y

-

T

-

G

-

D

-

E

-

S

-

R

L

T

N

R

V

V

S

T

K

Q

I

W

N

E

Y

T

I

L

E

D

F

W

A

V

K

Q

I

E

M

V

E

Q

D

K

M

R

G

G

T

A

E

G

D

E

I

I

I

V

L

L

T

N

D

M

I

M

S

N

K

Q

D

D

G

G

T

V

L

R

K

N

G

G

P

Y

N

D

F

L

D

E

M

Q

L

L

K

K

L

V

Q

R

E

E

N

V

V

C

N

H

C

V

N

P

I

L

T

I

A

A

S

S

G

G

I

A

K

G

D

T

L

M

D

E

D

H

L

F

I

L

K

E

-

A

L

F

K

R

E

D

M

A

N

D

I

V

Y

D

G

G

A

A

I

L

V

A

G

A

K

S

A

V

I

F

Y

H

S

K

E

Q

K

I

I

I

N

N

L

I

K

G

E

E

E46 (≠ Y46) mutation to A: Loss of activity.; mutation to G: Loss of IGP synthase activity. Weak IGP synthase and HisH activities in vitro.
Q123 (≠ K122) mutation to A: Decrease in activity.; mutation to R: Loss of IGP synthase activity. Weak HisH activity in vitro.
C124 (≠ S123) 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.

3zr4E Structural evidence for ammonia tunneling across the (beta-alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex (see paper)
23% identity, 91% coverage: 14:231/239 of query aligns to 9:227/244 of 3zr4E

query
sites
3zr4E

C

C

V

L

R
x
D

L

V

Y

K

Q

D

G

G

R

R

F

V

E

V

K

K

S

S

S

G

V

-

A

-

E

-

S

D

P

P

A

V

L

E

T

L

A

G

K

K

S

F

F

Y

E

S

N

E

D

I

G

G

A

I

K

D

Y

E

I

L

H

V

V

F

V

L

D

D

L

I

D

T

G

A

A

S

L

V

E

E

G

K

E

R

I

K

I

T

N

M

L

L

D

E

A

L

V

V

K

E

S

K

I

V

V

A

Q

E

V

Q

T

I

S

D

V

I

P

P

I

F

E

T

L

V

G

G

I

I

R

H

N

D

I

F

K

E

V

T

V

A

E

S

K

E

L

L

I

I

N

L

I

R

G

G

V

A

K

D

R

K

I

V

I

S

L

I

G

N

T

T

A

A

L

V

K

E

D

N

K

P

E

S

F

L

T

I

R

T

E

Q

A

I

I

A

K

Q

E

T

Y

F

G

G

-

S

K

Q

S

A

I

V

A

V

V

V

G

A

I

I

D
|
D

A

A

K

K

-

R

-

V

D

D

G

G

Y

E

V

F

A

M

V

V

N

F

G

T

W

Y

L

S

N

G

V

K

S

K

K

N

I

T

N

G

Y

I

I

L

-

L

-

R

E

D

F

W

A

V

K

V

I

E

M

V

E

E

D

K

M

R

G

G

T

A

E

G

D

E

I

I

I

L

L

L

T

T

D

S

I

I

S

D

K

R

D

D

G

G

T

T

L

K

K

S

G

G

P

Y

N

D

F

T

D

E

M

M

L

I

K
x
R

K

F

L

V

Q

R

E

P

N

L

V

T

N

T

C

L

N

P

I

I

T

I

A

A

S

S

G

G

I

A

K

G

D

K

L

M

D

E

D

H

L

F

I

L

K

E

L

A

K

F

E
x
L

M

A

N

G

I

A

Y

D

G

A

A

A

I

L

V

A

G

A

K

S

A

V

I

F

Y

H

S

F

E

R

K

E

I

I

N

D

L

V

K

R

E

E

active site: D11 (≠ R16), D121 (= D129)
binding glycerol: R179 (≠ K183), L206 (≠ E210)

7ac8A Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. (see paper)
23% identity, 96% coverage: 3:231/239 of query aligns to 6:236/252 of 7ac8A

query
sites
7ac8A

I

I

L

I

P

A

A

C

I

L

D
|
D

I

V

K

K

Q

D

G

G

K

R

C

V

V

V

R

K

L

-

Y

-

Q

G

G

T

R

N

F

F

E

E

K

N

S

L

S

R

V

D

V

S

A

G

E

D

S

-

P

P

A

V

L

E

T

L

A

G

K

K

S

F

F

Y

E

S

N

E

D

I

G

G

A

I

K

D

Y

E

I

L

H

V

V

F

V
x
L

D

D

L
x
I

D

T

G

A

A

S

L

V

E

E

G

K

E

R

I

K

I

T

N

M

L

L

D

E

A

L

V

V

K

E

S

K

I

V

V

A

Q

E

V

Q

T

I

S

D

V

I

P

P

I

F

E

T

L

V

G

G

G
|
G

I

I

R

H

N

D

I

F

K

E

V

T

V

A

E

S

K

E

L

L

I

I

N

L

I

R

G

G

V

A

K

D

R

K

I

V

I

S

L

I

G
x
N

T
|
T

A

A

L

V

K

E

D

N

K

P

E

S

F

L

T

I

R

T

E

Q

A

I

I

A

K

Q

E

T

Y

F

G

G

-

S

K

Q

S

A

I

V

A

V

V

V

G

A

I

I

D
|
D

A

A

K

K

-

R

-

V

D

D

G

G

Y

E

V

F

A

M

V

V

N

F

G

T

W

Y

L
x
S

N

G

V

K

S

K

K

N

I

T

N

G

Y

I

I

L

-

L

-

R

E

D

F

W

A

V

K

V

I

E

M

V

E

E

D

K

M

R

G

G

T

A

E

G

D

E

I

I

I

L

L

L

T

T

D

S

I

I

S

D

K

R

D
|
D

G
|
G

T

T

L

K

K

S

G

G

P

Y

N

D

F

T

D

E

M

M

L

I

K

R

K

F

L

V

Q

R

E

P

N

L

V

T

N

T

C

L

N

P

I

I

T

I

A

A

S
|
S

G

G

I

A

K

G

D

K

L

M

D

E

D

H

L

F

I

L

K

E

L

A

K

F

E

L

M

A

N

G

I

A

Y

D

G

A

A

A

I

L

V

A

G

A

K
x
S

A

V

I

F

Y

H

S

F

E

R

K

E

I

I

N

D

L

V

K

R

E

E

active site: D11 (= D8), D130 (= D129)
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 (= G82), N103 (≠ G103), T104 (= T104), D130 (= D129), S144 (≠ L141), D176 (= D171), G177 (= G172), S201 (= S196), S225 (≠ K220)

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)
23% identity, 96% coverage: 3:231/239 of query aligns to 6:236/253 of Q9X0C6

query
sites
Q9X0C6

I

I

L

I

P

A

A
x
C

I

L

D
|
D

I

V

K

K

Q

D

G

G

K

R

C

V

V

V

R
x
K

L

-

Y

-

Q

G

G

T

R

N

F

F

E

E

K

N

S

L

S

R

V

D

V

S

A

G

E

D

S

-

P

P

A

V

L

E

T

L

A

G

K

K

S

F

F

Y

E

S

N

E

D

I

G

G

A

I

K

D

Y

E

I

L

H

V

V

F

V

L

D
|
D

L

I

D

T

G

A

A

S

L

V

E

E

G

K

E

R

I

K

I

T

N

M

L

L

D

E

A

L

V

V

K

E

S

K

I

V

V

A

Q

E

V

Q

T

I

S

D

V

I

P

P

I

F

E

T

L

V

G

G

I

I

R

H

N

D

I

F

K

E

V

T

V

A

E

S

K

E

L

L

I

I

N

L

I

R

G

G

V

A

K

D

R

K

I

V

I

S

L

I

G
x
N

T

T

A

A

L

V

K

E

D

N

K

P

E

S

F

L

T

I

R

T

E

Q

A

I

I

A

K

Q

E

T

Y

F

G

G

-

S

K

Q

S

A

I

V

A

V

V

V

G

A

I

I

D
|
D

A

A

K

K

-

R

-

V

D

D

G

G

Y

E

V

F

A

M

V

V

N

F

G

T

W

Y

L

S

N

G

V

K

S

K

K

N

I

T

N

G

Y

I

I

L

-

L

-

R

E

D

F

W

A

V

K

V

I

E

M

V

E

E

D

K

M

R

G

G

T

A

E

G

D

E

I

I

I

L

L

L

T

T

D

S

I

I

S

D

K

R

D
|
D

G

G

T

T

L

K

K

S

G

G

P

Y

N
x
D

F

T

D

E

M

M

L

I

K

R

K

F

L

V

Q

R

E

P

N

L

V

T

N

T

C

L

N

P

I

I

T

I

A

A

S

S

G

G

I

A

K

G

D

K

L

M

D

E

D

H

L

F

I

L

K

E

L

A

K

F

E

L

M

A

N

G

I

A

Y

D

G

A

A

A

I

L

V

A

G

A

K

S

A

V

I

F

Y

H

S

F

E

R

K

E

I

I

N

D

L

V

K

R

E

E

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 (≠ G103) mutation to A: No change in activity.
D130 (= D129) 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 (= D171) mutation to N: Decrease in activity.
D183 (≠ N178) mutation to N: No change in activity.

7qc8A Imidazole glycerol phosphate synthase subunit HisF (see paper)
23% identity, 96% coverage: 3:231/239 of query aligns to 6:236/250 of 7qc8A

query
sites
7qc8A

I

I

L

I

P

A

A

A

I

L

D
x
E

I

V

K

K

Q

D

G

G

K

R

C

V

V

V

R

K

L

-

Y

-

Q

G

G

T

R

N

F

F

E

E

K

N

S

L

S

R

V

D

V

S

A

G

E

D

S

-

P

P

A

A

L

E

T

L

A

G

K

K

S

F

F

Y

E

S

N

E

D

I

G

G

A

I

K

D

Y

E

I

L

H

V

V

F

V
x
H

D

D

L
x
H

D

T

G

A

A

S

L

V

E

E

G

K

E

R

I

K

I

T

N

M

L

L

D

E

A

L

V

V

K

E

S

K

I

V

V

A

Q

E

V

Q

T

I

S

D

V

I

P

P

I

F

E

T

L

V

G

G

I

I

R

H

N

D

I

F

K

E

V

T

V

A

E

S

K

E

L

L

I

I

N

L

I

R

G

G

V

A

K

D

R

K

I

V

I

S

L

I

G

N

T

T

A

A

L

V

K

E

D

N

K

P

E

S

F

L

T

I

R

T

E

Q

A

I

I

A

K

Q

E

T

Y

F

G

G

-

S

K

Q

S

A

I

V

A

V

V

V

G

A

I

I

D

D

A

A

K

K

-

R

-

V

D

D

G

G

Y

E

V

F

A

M

V

V

N

F

G

T

W

Y

L

S

N

G

V

K

S

K

K

N

I

T

N

G

Y

I

I

L

-

L

-

R

E

D

F

W

A

V

K

V

I

E

M

V

E

E

D

K

M

R

G

G

T

A

E

G

D

E

I

I

I

L

L

L

T

T

D

S

I

I

S

D

K

R

D

D

G

G

T

T

L

K

K

S

G

G

P

Y

N

D

F

T

D

E

M

M

L

I

K

R

K

F

L

V

Q

R

E

P

N

L

V

T

N

T

C

L

N

P

I

I

T

I

A

A

S

S

G

G

I

A

K

G

D

K

L

M

D

E

D

H

L

F

I

L

K

E

L

A

K

F

E

L

M

A

N

G

I

A

Y

D

G

A

A

A

I

L

V

A

G

A

K

S

A

V

I

F

Y

H

S

F

E

R

K

E

I

I

N

D

L

V

K

R

E

E

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

1gpwC Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex. (see paper)
22% identity, 96% coverage: 3:231/239 of query aligns to 6:236/253 of 1gpwC

query
sites
1gpwC

I

I

L

I

P

A

A

C

I

L

D
x
N

I

V

K

K

Q

D

G

G

K

R

C

V

V

V

R

K

L

-

Y

-

Q

G

G

T

R

N

F

F

E

E

K

N

S

L

S

R

V

D

V

S

A

G

E

D

S

-

P

P

A

V

L

E

T

L

A

G

K

K

S

F

F

Y

E

S

N

E

D

I

G

G

A

I

K

D

Y

E

I

L

H

V

V

F

V

L

D

D

L

I

D

T

G

A

A

S

L

V

E

E

G

K

E

R

I

K

I

T

N

M

L

L

D

E

A

L

V

V

K

E

S

K

I

V

V

A

Q

E

V

Q

T

I

S

D

V

I

P

P

I

F

E

T

L

V

G

G

G
|
G

I

I

R

H

N

D

I

F

K

E

V

T

V

A

E

S

K

E

L

L

I

I

N

L

I

R

G

G

V

A

K

D

R

K

I

V

I

S

L

I

G
x
N

T
|
T

A

A

L

V

K

E

D

N

K

P

E

S

F

L

T

I

R

T

E

Q

A

I

I

A

K

Q

E

T

Y

F

G

G

-

S

K

Q

S

A

I

V

A

V

V

V

G

A

I

I

D
|
D

A

A

K

K

-

R

-

V

D

D

G

G

Y

E

V

F

A

M

V

V

N

F

G

T

W

Y

L

S

N

G

V

K

S

K

K

N

I

T

N

G

Y

I

I

L

-

L

-

R

E

D

F

W

A

V

K

V

I

E

M

V

E

E

D

K

M

R

G

G

T

A

E

G

D

E

I

I

I

L

L

L

T

T

D

S

I

I

S

D

K

R

D
|
D

G
|
G

T

T

L

K

K

S

G

G

P

Y

N

D

F

T

D

E

M

M

L

I

K

R

K

F

L

V

Q

R

E

P

N

L

V

T

N

T

C

L

N

P

I

I

T

I

A

A

S

S

G

G

I

A

K

G

D

K

L

M

D

E

D

H

L

F

I

L

K

E

L

A

K

F

E

L

M

A

N

G

I

A

Y

D

G

A

A

A

I

L

V

A

G

A

K
x
S

A

V

I

F

Y

H

S

F

E

R

K

E

I

I

N

D

L

V

K

R

E

E

active site: N11 (≠ D8), D130 (= D129)
binding phosphate ion: G82 (= G82), N103 (≠ G103), T104 (= T104), D176 (= D171), G177 (= G172), S225 (≠ K220)

2wjzE Crystal structure of (hish) k181a y138a mutant of imidazoleglycerolphosphate synthase (hish hisf) which displays constitutive glutaminase activity (see paper)
24% identity, 71% coverage: 63:231/239 of query aligns to 49:222/237 of 2wjzE

query
sites
2wjzE

L

L

D

E

A

L

V

V

K

E

S

K

I

V

V

A

Q

E

V

Q

T

I

S

D

V

I

P

P

I

F

E

T

L

V

G

G

G
|
G

I

I

R

H

N

D

I

F

K

E

V

T

V

A

E

S

K

E

L

L

I

I

N

L

I

R

G

G

V

A

K

D

R

K

I

V

I

S

L

I

G
x
N

T
|
T

A

A

L

V

K

E

D

N

K

P

E

S

F

L

T

I

R

T

E

Q

A

I

I

A

K

Q

E

T

Y

F

G

G

-

S

K

Q

S

A

I

V

A

V

V

V

G

A

I

I

D
|
D

A

A

K

K

-

R

-

V

D

D

G

G

Y

E

V

F

A

M

V

V

N

F

G

T

W

Y

L

S

N

G

V

K

S

K

K

N

I

T

N

G

Y

I

I

L

-

L

-

R

E

D

F

W

A

V

K

V

I

E

M

V

E

E

D

K

M

R

G

G

T

A

E

G

D

E

I

I

I

L

L

L

T

T

D

S

I

I

S

D

K

R

D

D

G

G

T

T

L

K

K

S

G

G

P

Y

N

D

F

T

D

E

M

M

L

I

K

R

K

F

L

V

Q

R

E

P

N

L

V

T

N

T

C

L

N

P

I

I

T

I

A

A

S

S

G

G

I

A

K

G

D

K

L

M

D

E

D

H

L

F

I

L

K

E

L

A

K

F

E

L

M

A

N

G

I

A

Y

D

G

A

A

A

I

L

V

A

G

A

K

S

A

V

I

F

Y

H

S

F

E

R

K

E

I

I

N

D

L

V

K

R

E

E

active site: D116 (= D129)
binding phosphate ion: G68 (= G82), N89 (≠ G103), T90 (= T104)

Sites not aligning to the query:

active site: 11

4ewnD Structure of hisf-d130v+d176v with bound rcdrp (see paper)
21% identity, 96% coverage: 3:231/239 of query aligns to 5:229/243 of 4ewnD

query
sites
4ewnD

I

I

L

I

P

A

A

C

I

L

D

D

I

V

K

K

Q

D

G

G

K

R

C

V

V

V

R

K

L

-

Y

-

Q

G

G

T

R

N

F

F

E

E

K

N

S

L

S

R

V

D

V

S

A

G

E

D

S

-

P

P

A

V

L

E

T

L

A

G

K

K

S

F

F

Y

E

S

N

E

D

I

G

G

A

I

K

D

Y

E

I

L

H

V

V

F

V

L

D

D

L

I

D

T

G

K

A

T

L

M

E

-

G

-

E

-

I

-

N

-

L

L

D

E

A

L

V

V

K

E

S

K

I

V

V

A

Q

E

V

Q

T

I

S

D

V

I

P

P

I

F

E

T

L

V

G

G

I

I

R

H

N

D

I

F

K

E

V

T

V

A

E

S

K

E

L

L

I

I

N

L

I

R

G

G

V

A

K

D

R

K

I

V

I

S

L

I

G

N

T

T

A

A

L

V

K

E

D

N

K

P

E

S

F

L

T

I

R

T

E

Q

A

I

I

A

K

Q

E

T

Y

F

G

G

-

S

K

Q

S

A

I

V

A

V

V

V

G

A

I

I

D
x
V

A

A

K

K

-

R

-

V

D

D

G

G

Y

E

V

F

A

M

V

V

N

F

G

T

W

Y

L

S

N

G

V

K

S

K

K

N

I

T

N

G

Y

I

I

L

-

L

-

R

E

D

F

W

A

V

K

V

I

E

M

V

E

E

D

K

M

R

G

G

T

A

E

G

D

E

I

I

I

L

L

L

T

T

D

S

I

I

S

D

K

R

D

V

G
|
G

T

T

L

K

K

S

G

G

P

Y

N

D

F

T

D

E

M

M

L

I

K

R

K

F

L

V

Q

R

E

P

N

L

V

T

N

T

C

L

N

P

I

I

T

I

A

A

S
|
S

G
|
G

I

A

K

G

D

K

L

M

D

E

D

H

L

F

I

L

K

E

L

A

K

F

E

L

M

A

N

G

I

A

Y

D

G

A

A

A

I
x
L

V
x
A

G
x
A

K
x
S

A

V

I

F

Y

H

S

F

E

R

K

E

I

I

N

D

L

V

K

R

E

E

binding 1-(O-carboxy-phenylamino)-1-deoxy-D-ribulose-5-phosphate: V123 (≠ D129), G170 (= G172), S194 (= S196), G195 (= G197), G196 (= G198), L215 (≠ I217), A216 (≠ V218), A217 (≠ G219), S218 (≠ K220)

5d2tA Directed evolutionary changes in kemp eliminase ke07 - crystal 3 wild type
22% identity, 96% coverage: 3:231/239 of query aligns to 4:234/251 of 5d2tA

query
sites
5d2tA

I

I

L

I

P

A

A

A

I

L

D

I

I

V

K

K

Q

D

G

G

K

R

C

V

V

V

R

K

L

-

Y

-

Q

G

G

S

R

N

F

F

E

E

K

N

S

L

S

R

V

D

V

S

A

G

E

D

S

-

P

P

A

V

L

E

T

L

A

G

K

K

S

F

F

Y

E

S

N

E

D

I

G

G

A

I

K

D

Y

E

I

L

H

S

V

F

V
x
W

D

D

L

I

D

T

G

A

A

S

L

V

E

E

G

K

E

R

I

K

I

T

N

M

L

L

D

E

A

L

V

V

K

E

S

K

I

V

V

A

Q

E

V

Q

T

I

S

D

V

I

P

P

I

F

E

T

L

V

G

G

I

I

R

H

N

D

I

F

K

E

V

T

V

A

E

S

K

E

L

L

I

I

N

L

I

R

G

G

V

A

K

D

R

K

I

V

I
x
E

L

I

G

N

T

T

A

A

L

V

K

E

D

N

K

P

E

S

F

L

T

I

R

T

E

Q

A

I

I

A

K

Q

E

T

Y

F

G

G

-

S

K

Q

S

A

I

V

A

V

V

V

G
x
Y

I

I

D

A

A

A

K

K

-

R

-

V

D

D

G

G

Y

E

V

F

A

M

V

V

N

F

G

T

W

Y

L

S

N

G

V

K

S

K

K

N

I

T

N

G

Y

I

I

L

-

L

-

R

E

D

F

W

A

V

K

V

I

E

M

V

E

E

D

K

M

R

G

G

T

A

E

G

D

E

I

I

I

V

L

L

T

G

D

S

I

I

S

D

K

R

D

L

G

G

T

T

L

K

K

S

G

G

P

Y

N

D

F

T

D

E

M

M

L

I

K

R

K

F

L

V

Q

R

E

P

N

L

V

T

N

T

C

L

N

P

I

I

T

I

A

A

S

H

G

G

I

A

K

G

D

K

L

M

D

E

D

H

L

F

I

L

K

-

L

-

K

-

E

E

M

A

N

F

I

L

Y

A

G

G

A

A

I

D

V

A

G

A

K
|
K

A

A

-

N

-

S

-

V

I

L

Y

H

S

F

E

R

K

E

I

I

N

D

L

V

K

R

E

E

binding 5-nitro-2-oxidanyl-benzenecarbonitrile: W48 (≠ V50), E99 (≠ I101), Y126 (≠ G127), K220 (= K220)

3iivB Evolutionary optimization of computationally designed enzymes: kemp eliminases of the ke07 series (see paper)
23% identity, 84% coverage: 32:231/239 of query aligns to 32:235/262 of 3iivB

query
sites
3iivB

P

P

A

V

L

E

T

L

A

G

K

K

S

F

F

Y

E

S

N

E

D

I

G

G

A

I

K

D

Y

E

I

L

H

S

V

F

V

W

D

D

L

I

D

T

G

A

A

S

L

V

E

E

G

K

E

K

I

T

I

M

N

-

L

L

D

E

A

L

V

V

K

E

S

K

I

V

V

A

Q

E

V

Q

T

I

S

D

V

I

P

P

I

I

E

T

L

V

G

G

I

I

R

Y

N

D

I

F

K

E

V

T

V

A

E

S

K

E

L

L

I

I

N

L

I

R

G

G

V

A

K

D

R

K

I

V

I
x
E

L

I

G

N

T

T

A

A

L

V

K

E

D

N

K

P

E

S

F

L

T

I

R

T

E

Q

A

I

I

A

K

Q

E

T

Y

F

G

G

-

S

K

Q

S

A

I

V

A

V

V

V

G

Y

I

I

D

A

A

A

K

K

-

R

-

V

D

D

G

G

Y

E

V

F

A

M

V

V

N

F

G

T

W

Y

L

S

N

G

V

T

S

K

K

N

I

T

N

G

Y

I

I

L

-

L

-

R

E

D

F

W

A

V

K

V

I

E

M

V

E

E

D

K

M

R

G

G

T

A

E

G

D

E

I

I

I

V

L

L

T

G

D

S

I

I

S

D

K

R

D

L

G

G

T

T

L

K

K

S

G

G

P

Y

N

D

F

T

D

E

M

M

L

I

K

R

K

F

L

V

Q

R

E

P

N

L

V

T

N

T

C

L

N

P

I

I

T

I

A

A

S

H

G

R

G

G

I

A

K

G

D

K

L

T

D

E

D

H

L

F

I

L

K

-

L

-

K

-

E

E

M

A

N

F

I

L

Y

A

G

G

A

A

I

D

V

A

G

A

K
|
K

A

A

-

D

-

S

-

V

I

F

Y

H

S

S

E

R

K

E

I

I

N

D

L

V

K

R

E

E

binding magnesium ion: E100 (≠ I101), K221 (= K220)

Query Sequence

>WP_010964258.1 NCBI__GCF_000008765.1:WP_010964258.1
MIILPAIDIKQGKCVRLYQGRFEKSSVVAESPALTAKSFENDGAKYIHVVDLDGALEGEI
INLDAVKSIVQVTSVPIELGGGIRNIKVVEKLINIGVKRIILGTAALKDKEFTREAIKEY
GKSIAVGIDAKDGYVAVNGWLNVSKINYIEFAKIMEDMGTEDIILTDISKDGTLKGPNFD
MLKKLQENVNCNITASGGIKDLDDLIKLKEMNIYGAIVGKAIYSEKINLKEAIAVIEKR

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