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)
31% identity, 97% coverage: 1:233/241 of query aligns to 4:234/240 of P16250

query
sites
P16250

M

L

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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 (= 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)
33% identity, 97% coverage: 1:233/241 of query aligns to 9:239/246 of 4tx9A

query
sites
4tx9A

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active site: D16 (= D8), D135 (= D130)
binding aminoimidazole 4-carboxamide ribonucleotide: G28 (= G20), V57 (= V50), L59 (= L52), S86 (≠ G80), G88 (= G82), R90 (≠ K84), G109 (= G103), T110 (≠ S104), D135 (= D130), G145 (= G140), W146 (= W141)

3zs4A Crystal structure of mycobacterium tuberculosis phosphoribosyl isomerase with bound prfar
31% identity, 96% coverage: 3:233/241 of query aligns to 5:237/244 of 3zs4A

query
sites
3zs4A

I

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active site: D10 (= D8), 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 (= A6), D10 (= D8), R18 (= R16), A56 (= A55), F57 (≠ K56), S80 (≠ G80), G82 (= G82), R84 (≠ K84), G103 (= G103), T104 (≠ S104), D129 (= D130), G143 (= G140), W144 (= W141), D174 (= D172), G175 (= G173), G200 (= G199), G201 (= G200), I223 (= I219), G225 (= G221), K226 (= K222)

2y88A Crystal structure of mycobacterium tuberculosis phosphoribosyl isomerase (variant d11n) with bound prfar (see paper)
30% identity, 96% coverage: 3:233/241 of query aligns to 5:237/244 of 2y88A

query
sites
2y88A

I

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active site: N10 (≠ D8), D129 (= 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: A8 (= A6), N10 (≠ D8), R18 (= R16), G22 (= G20), L53 (= L52), A56 (= A55), S80 (≠ G80), G81 (= G81), G82 (= G82), R84 (≠ K84), G103 (= G103), T104 (≠ S104), D129 (= D130), G143 (= G140), W144 (= W141), D174 (= D172), G175 (= G173), S199 (= S198), G200 (= G199), G225 (= G221), K226 (= K222)

2y85A Crystal structure of mycobacterium tuberculosis phosphoribosyl isomerase with bound rcdrp (see paper)
30% identity, 96% coverage: 3:233/241 of query aligns to 5:228/234 of 2y85A

query
sites
2y85A

I

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x
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L

L

P

R

K

A

L

I

A

A

E

T

L

L

-

T

-

H

-

R

G

G

C

V

E

E

G

G

V

A

I

I

I

V

G
|
G

K
|
K

A

A

I

L

Y

Y

E

A

N

R

R

R

I

F

S

T

L

L

K

P

Q

Q

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 (≠ G80), R133 (≠ S139), D165 (= D172), G166 (= G173), S190 (= S198), G191 (= G199), G192 (= G200), G216 (= G221), K217 (= K222)

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)
26% identity, 98% coverage: 1:237/241 of query aligns to 1:239/241 of Q9X0C7

query
sites
Q9X0C7

M

M

R

L

I

V

P

P

A

A

I

I

D
|
D

I

L

I

F

D

R

G

G

K

K

C

V

V

A

R

R

L

M

S

I

K

K

G

G

D

R

Y

K

N

E

T

N

K

T

K

I

I

F

Y

Y

N

E

E

K

S

D

P

P

L

V

E

E

V

L

A

V

K

E

S

K

F

L

E

I

G

E

A

E

G

G

I

F

Q

T

Y

L

L

I

H
|
H

V

V

D
|
D

L

L

D

S

G

N

A

A

K

I

A

E

K

N

H

S

I

G

I

E

N

N

H

L

K

P

V

V

L

L

E

E

Q

K

I

L

A

S

T

E

K

F

T

A

N

E

L

-

K

H

I

I

D

Q

F

I

G

G

L

I

K
x
R

T

S

N

L

E

D

D

Y

L

A

K

E

I

K

A

L

F

R

N

K

S

L

G

G

A

Y

S

R

Q

R

I

Q

T

I

G

V

G

S

S

S

I

K

A

V

V

L

K

E

N

D

P

P

K

S

I

-

F

F

Q

L

E

K

W

S

L

L

T

R

K

E

F

I

G

D

S

V

D

E

K

P

I

-

I

V

L

F

G

S

A

L

D
|
D

C

T

N

R

N

G

E

G

N

R

I

V

A

A

I

F

S

K

G

G

W

W

L

L

E

A

E

E

S

E

D

E

L

I

K

D

V

P

I

V

P

S

F

L

I

L

Q

K

D

R

Y

L

Q

K

T

E

K

Y

G

G

A

L

S

E

Y

E

V

I

I

V

C

H

T
|
T

D

E

I

I

S

E

K

K

D

D

G

G

M

T

L

L

E

Q

G

E

P

H

S

D

F

F

E

S

L

L

Y

T

E

K

R

K

I

I

L

A

K

I

E

E

T

A

K

E

N

-

L

V

N

K

L

V

I

L

A

A

S

A

G

G

I

I

S

S

T

S

F

E

D

N

E

S

L

L

P

K

K

T

L

A

A

Q

E

K

L

V

G

H

C

T

E

E

-

T

-

N

-

G

-

L

-

K

G

G

V

V

I

I

I

V

G

G

K

R

A

A

I

F

Y

L

E

E

N

G

R

I

I

L

S

T

L

V

K

E

Q

V

L

M

E

K

N

R

Y

Y

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 (≠ K84) mutation to N: Decrease in activity.
D127 (= D130) mutation to N: Almost no activity.
T164 (= T167) mutation to A: Strong decrease in activity.

1h5yB Hisf protein from pyrobaculum aerophilum (see paper)
27% identity, 83% coverage: 1:200/241 of query aligns to 5:206/253 of 1h5yB

query
sites
1h5yB

M

L

R

R

I

I

P

P

A

C

I

L

D
|
D

I

I

I

-

D

D

G

G

K

G

C

A

V

K

R

V

L

V

S

V

K
|
K

G

G

D

-

Y

V

N

N

T

F

K

Q

K

G

I

I

Y

R

N

E

E

V

S

G

-

D

P

P

L

V

E

E

V

M

A

A

K

V

S

R

F

Y

E

E

G

E

A

E

G

G

I

A

Q

D

Y

E

L

I

H

A

V

I

V

L

D

D

L

I

D

T

G

A

A

A

K

P

A

E

K

G

H

R

I

A

I

T

N

F

H

I

K

D

V

S

L

V

E

K

Q

R

I

V

A

A

T

E

K

A

T

V

N

S

L

I

K

P

I

V

D

L

F

V

G

G

G
|
G

L

V

K

R

T

S

N

L

E

E

D

D

L

A

K

T

I

T

A

L

F

F

N

R

S

A

G

G

A

A

S

D

Q

K

I

V

T

S

G

V

G
x
N

S
x
T

I

A

A

A

V

V

K

R

N

N

P

P

K

Q

I

L

F

V

Q

A

E

L

W

L

L

A

T

R

K

E

F

F

G

G

S

S

D

Q

K

S

I

T

I

V

L

V

G
x
A

A

I

D
|
D

C

A

-

K

-

W

N

N

N

G

E

E

-

Y

N

E

I

V

A

Y

I

V

S

K

G
|
G

W

G

L

R

E

E

E

A

S

T

D

G

L

L

K

D

V

A

I

V

P

K

F

W

I

A

Q

K

D

E

Y

V

Q

E

T

E

K

L

G

G

A

A

S

G

Y

E

V

I

I

L

C

L

T
|
T

D

S

I

I

S

D

K

R

D
|
D

G
|
G

M

T

L

G

E

L

G

G

P

Y

S

D

F

V

E

E

L

L

Y

I

E

R

R

R

I

V

L

-

K

A

E

D

T

S

K

V

N

R

L

I

N

P

L

V

I

I

A

A

S

S

G

G

active site: D12 (= D8), D133 (= D130)
binding glycerol: K22 (= K19), N106 (≠ G103), A131 (≠ G128), D133 (= D130), G147 (= G140), T174 (= T167), D179 (= D172)
binding phosphate ion: G84 (= G81), G85 (= G82), N106 (≠ G103), T107 (≠ S104), D179 (= D172), G180 (= G173)

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)
22% identity, 100% coverage: 2:241/241 of query aligns to 5:251/258 of P60664

query
sites
P60664

R
|
R

I

I

P

P

A

C

I

L

D

D

I

V

I

R

D

D

G

G

K

Q

C

V

V

V

R

K

L

G

S

V

K

Q

G

F

D

-

Y

R

N

N

T

H

K

E

K

I

I

I

Y

G

N

D

E

I

S

V

P

P

L

L

E

-

V

-

A

A

K

K

S

R

F

Y

E

A

G

E

A

E

G

G

I

A

Q

D

Y
x
E

L

L

H

V

V

F

V

Y

D

D

L

I

D

T

G

A

A

S

K

S

A

D

K

G

H

R

I

V

N

D

H

K

K

S

V

W

L

V

E

S

Q

R

I

V

A

A

T

E

K

V

T

I

N

D

L

I

K

P

I

F

D

C

F

V

G

A

G

G

L

I

K

K

T

S

N

L

E

E

D

D

L

A

K

A

I

K

A

I

F

L

N

S

S

F

G

G

A

A

S

D

Q

K

I

I

T

S

G

I

G

N

S

S

I

P

A

A

V

L

K

A

N

D

P

P

K

T

I

L

F

I

Q

T

E

R

W

L

L

A

T

D

K

R

F

F

G

G

S

V

D
x
Q

K
x
C

I

I

I

V

L

V

G

G

A

I

D

D

C

T

-

W

-

Y

-

D

-

A

-

E

-

T

-

G

-

K

-

Y

-

H

N

V

N

N

E

Q

N

Y

I

T

A

G

I

D

S

E

G

S

W

R

L

T

E

R

E

V

S

T

D

Q

L

W

K

E

V

T

I

L

P

D

F

W

I

V

Q

Q

D

E

Y

V

Q

Q

T

K

K

R

G

G

A

A

S

G

Y

E

V

I

I

V

C

L

T

N

D

M

I

M

S

N

K

Q

D

D

G

G

M

V

L

R

E

N

G

G

P

Y

S

D

F

L

E

E

L

Q

Y

L

E

K

R

K

I

V

L

-

K

R

E

E

T

V

K

C

N

H

L

V

N

P

L

L

I

I

A

A

S

S

G

G

I

A

S

G

T

T

F

M

D

E

E

H

-

F

L

L

P

E

K

A

L

F

A

R

E

D

L

A

G

D

C

V

E

D

G

G

V

A

I

L

I

A

G

A

K

S

A

V

I

F

Y

H

E

K

N

Q

R

I

I

I

S

N

L

I

K

G

Q

E

L

L

E

K

N

A

Y

Y

I

L

I

A

N

T

K

Q

R5 (= R2) 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 (≠ Y46) mutation to A: Loss of activity.; mutation to G: Loss of IGP synthase activity. Weak IGP synthase and HisH activities in vitro.
Q123 (≠ D123) mutation to A: Decrease in activity.; mutation to R: Loss of IGP synthase activity. Weak HisH activity in vitro.
C124 (≠ K124) mutation to A: No change in activity.; mutation to R: Loss of IGP synthase activity. Weak 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)
22% identity, 98% coverage: 2:238/241 of query aligns to 5:232/244 of 3zr4E

query
sites
3zr4E

R

R

I

I

P

A

A

C

I

L

D
|
D

I

V

I

K

D

D

G

G

K

R

C

V

V

V

R

K

L

-

S

-

K

S

G

G

D

D

Y

-

N

-

T

-

K

-

I

-

Y

-

N

-

E

-

S

-

P

P

L

V

E

E

V

L

A

G

K

K

S

F

F

Y

E

S

G

E

A

I

G

G

I

I

Q

D

Y

E

L

L

H

V

V

F

V

L

D

D

L

I

D

T

G

A

A

S

K

V

A

E

K

K

H

R

I

K

I

T

N

M

H

L

K

E

V

L

L

V

E

E

Q

K

I

V

A

A

T

E

K

Q

T

I

N

D

L

I

K

P

I

F

D

T

F

V

G

G

L

I

K

H

T

D

N

F

E

E

D

T

L

A

K

S

I

E

A

L

F

I

N

L

S

R

G

G

A

A

S

D

Q

K

I

V

T

S

G

I

G

N

S

T

I

A

A

A

V

V

K

E

N

N

P

P

K

S

I

L

F

I

Q

T

E

Q

W

I

L

A

T

Q

K

T

F

F

G

G

S

S

D

Q

K

A

I

V

L

V

G

A

A

I

D
|
D

C

A

-

K

-

R

-

V

-

D

-

G

-

E

-

F

-

M

-

V

-

F

-

T

-

Y

-

S

-

G

-

K

N

K

N

N

E

T

N

G

I

I

A

L

I

L

S

R

G

D

W

W

L

V

E

V

E

E

S

-

D

-

L

-

K

-

V

-

I

-

P

-

F

-

I

-

Q

-

D

-

Y

V

Q

E

T

K

K

R

G

G

A

A

S

G

Y

E

V

I

I

L

C

L

T

T

D

S

I

I

S

D

K

R

D

D

G

G

M

T

L

K

E

S

G

G

P

Y

S

D

F

T

E

E

L

M

Y

I

E

-

R
|
R

I

F

L

V

K

R

E

P

T

L

K

T

N

T

L

L

N

P

L

I

I

I

A

A

S

S

G

G

I

A

S

G

T

K

F

M

D

E

E

H

L

F

P

L

K

E

L

A

A

F

E
x
L

L

A

G

G

C

A

E

D

G

A

V

A

I

L

I

A

G

A

K

S

A

V

I

F

Y

H

E

F

N

R

R

E

I

I

S

D

L

V

K

R

Q

E

L

L

E

K

N

E

Y

Y

I

L

active site: D11 (= D8), D121 (= D130)
binding glycerol: R179 (= R185), L206 (≠ E212)

7ac8A Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. (see paper)
22% identity, 98% coverage: 2:238/241 of query aligns to 5:241/252 of 7ac8A

query
sites
7ac8A

R

R

I

I

P

A

A

C

I

L

D
|
D

I

V

I

K

D

D

G

G

K

R

C

V

V

V

R

K

L

G

S

T

K

-

G

-

D

-

Y

-

N

N

T

F

K

E

K

N

I

L

Y

R

N

D

E

S

-

G

S

D

P

P

L

V

E

E

V

L

A

G

K

K

S

F

F

Y

E

S

G

E

A

I

G

G

I

I

Q

D

Y

E

L

L

H

V

V

F

V
x
L

D

D

L
x
I

D

T

G

A

A

S

K

V

A

E

K

K

H

R

I

K

I

T

N

M

H

L

K

E

V

L

L

V

E

E

Q

K

I

V

A

A

T

E

K

Q

T

I

N

D

L

I

K

P

I

F

D

T

F

V

G

G

G
|
G

L

I

K

H

T

D

N

F

E

E

D

T

L

A

K

S

I

E

A

L

F

I

N

L

S

R

G

G

A

A

S

D

Q

K

I

V

T

S

G

I

G
x
N

S
x
T

I

A

A

A

V

V

K

E

N

N

P

P

K

S

I

L

F

I

Q

T

E

Q

W

I

L

A

T

Q

K

T

F

F

G

G

S

S

D

Q

K

A

I

V

L

V

G

A

A

I

D
|
D

C

A

-

K

-

R

-

V

-

D

-

G

-

E

-

F

-

M

-

V

-

F

-

T

-

Y

-
x
S

-

G

-

K

N

K

N

N

E

T

N

G

I

I

A

L

I

L

S

R

G

D

W

W

L

V

E

V

E

E

S

-

D

-

L

-

K

-

V

-

I

-

P

-

F

-

I

-

Q

-

D

-

Y

V

Q

E

T

K

K

R

G

G

A

A

S

G

Y

E

V

I

I

L

C

L

T

T

D

S

I

I

S

D

K

R

D
|
D

G
|
G

M

T

L

K

E

S

G

G

P

Y

S

D

F

T

E

E

L

M

Y

I

E

-

R

R

I

F

L

V

K

R

E

P

T

L

K

T

N

T

L

L

N

P

L

I

I

I

A

A

S
|
S

G

G

I

A

S

G

T

K

F

M

D

E

E

H

L

F

P

L

K

E

L

A

A

F

E

L

L

A

G

G

C

A

E

D

G

A

V

A

I

L

I

A

G

A

K
x
S

A

V

I

F

Y

H

E

F

N

R

R

E

I

I

S

D

L

V

K

R

Q

E

L

L

E

K

N

E

Y

Y

I

L

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 (= G82), N103 (≠ G103), T104 (≠ S104), D130 (= D130), S144 (vs. gap), D176 (= D172), G177 (= G173), S201 (= S198), S225 (≠ K222)

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)
22% identity, 98% coverage: 2:238/241 of query aligns to 5:241/253 of Q9X0C6

query
sites
Q9X0C6

R

R

I

I

P

A

A
x
C

I

L

D
|
D

I

V

I

K

D

D

G

G

K

R

C

V

V

V

R
x
K

L

G

S

T

K

-

G

-

D

-

Y

-

N

N

T

F

K

E

K

N

I

L

Y

R

N

D

E

S

-

G

S

D

P

P

L

V

E

E

V

L

A

G

K

K

S

F

F

Y

E

S

G

E

A

I

G

G

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I

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D

Y

E

L

L

H

V

V

F

V

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D
|
D

L

I

D

T

G

A

A

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K

V

A

E

K

K

H

R

I

K

I

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N

M

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K

E

V

L

L

V

E

E

Q

K

I

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A

A

T

E

K

Q

T

I

N

D

L

I

K

P

I

F

D

T

F

V

G

G

L

I

K

H

T

D

N

F

E

E

D

T

L

A

K

S

I

E

A

L

F

I

N

L

S

R

G

G

A

A

S

D

Q

K

I

V

T

S

G

I

G
x
N

S

T

I

A

A

A

V

V

K

E

N

N

P

P

K

S

I

L

F

I

Q

T

E

Q

W

I

L

A

T

Q

K

T

F

F

G

G

S

S

D

Q

K

A

I

V

L

V

G

A

A

I

D
|
D

C

A

-

K

-

R

-

V

-

D

-

G

-

E

-

F

-

M

-

V

-

F

-

T

-

Y

-

S

-

G

-

K

N

K

N

N

E

T

N

G

I

I

A

L

I

L

S

R

G

D

W

W

L

V

E

V

E

E

S

-

D

-

L

-

K

-

V

-

I

-

P

-

F

-

I

-

Q

-

D

-

Y

V

Q

E

T

K

K

R

G

G

A

A

S

G

Y

E

V

I

I

L

C

L

T

T

D

S

I

I

S

D

K

R

D
|
D

G

G

M

T

L

K

E

S

G

G

P

Y

S
x
D

F

T

E

E

L

M

Y

I

E

-

R

R

I

F

L

V

K

R

E

P

T

L

K

T

N

T

L

L

N

P

L

I

I

I

A

A

S

S

G

G

I

A

S

G

T

K

F

M

D

E

E

H

L

F

P

L

K

E

L

A

A

F

E

L

L

A

G

G

C

A

E

D

G

A

V

A

I

L

I

A

G

A

K

S

A

V

I

F

Y

H

E

F

N

R

R

E

I

I

S

D

L

V

K

R

Q

E

L

L

E

K

N

E

Y

Y

I

L

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 (= 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 (≠ S179) mutation to N: No change in activity.

1gpwC Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex. (see paper)
21% identity, 98% coverage: 2:238/241 of query aligns to 5:241/253 of 1gpwC

query
sites
1gpwC

R

R

I

I

P

A

A

C

I

L

D
x
N

I

V

I

K

D

D

G

G

K

R

C

V

V

V

R

K

L

G

S

T

K

-

G

-

D

-

Y

-

N

N

T

F

K

E

K

N

I

L

Y

R

N

D

E

S

-

G

S

D

P

P

L

V

E

E

V

L

A

G

K

K

S

F

F

Y

E

S

G

E

A

I

G

G

I

I

Q

D

Y

E

L

L

H

V

V

F

V

L

D

D

L

I

D

T

G

A

A

S

K

V

A

E

K

K

H

R

I

K

I

T

N

M

H

L

K

E

V

L

L

V

E

E

Q

K

I

V

A

A

T

E

K

Q

T

I

N

D

L

I

K

P

I

F

D

T

F

V

G

G

G
|
G

L

I

K

H

T

D

N

F

E

E

D

T

L

A

K

S

I

E

A

L

F

I

N

L

S

R

G

G

A

A

S

D

Q

K

I

V

T

S

G

I

G
x
N

S
x
T

I

A

A

A

V

V

K

E

N

N

P

P

K

S

I

L

F

I

Q

T

E

Q

W

I

L

A

T

Q

K

T

F

F

G

G

S

S

D

Q

K

A

I

V

L

V

G

A

A

I

D
|
D

C

A

-

K

-

R

-

V

-

D

-

G

-

E

-

F

-

M

-

V

-

F

-

T

-

Y

-

S

-

G

-

K

N

K

N

N

E

T

N

G

I

I

A

L

I

L

S

R

G

D

W

W

L

V

E

V

E

E

S

-

D

-

L

-

K

-

V

-

I

-

P

-

F

-

I

-

Q

-

D

-

Y

V

Q

E

T

K

K

R

G

G

A

A

S

G

Y

E

V

I

I

L

C

L

T

T

D

S

I

I

S

D

K

R

D
|
D

G
|
G

M

T

L

K

E

S

G

G

P

Y

S

D

F

T

E

E

L

M

Y

I

E

-

R

R

I

F

L

V

K

R

E

P

T

L

K

T

N

T

L

L

N

P

L

I

I

I

A

A

S

S

G

G

I

A

S

G

T

K

F

M

D

E

E

H

L

F

P

L

K

E

L

A

A

F

E

L

L

A

G

G

C

A

E

D

G

A

V

A

I

L

I

A

G

A

K
x
S

A

V

I

F

Y

H

E

F

N

R

R

E

I

I

S

D

L

V

K

R

Q

E

L

L

E

K

N

E

Y

Y

I

L

active site: N11 (≠ D8), D130 (= D130)
binding phosphate ion: G82 (= G82), N103 (≠ G103), T104 (≠ S104), D176 (= D172), G177 (= G173), S225 (≠ K222)

2wjzE Crystal structure of (hish) k181a y138a mutant of imidazoleglycerolphosphate synthase (hish hisf) which displays constitutive glutaminase activity (see paper)
23% identity, 98% coverage: 2:238/241 of query aligns to 5:227/237 of 2wjzE

query
sites
2wjzE

R

R

I

I

P

A

A

C

I

L

D
|
D

I

V

I

K

D

D

G

G

K

R

C

V

V

V

R

-

L

-

S

-

K

-

G

G

D

D

Y

-

N

-

T

-

K

-

I

-

Y

-

N

-

E

-

S

-

P

P

L

V

E

E

V

L

A

G

K

K

S

F

F

Y

E

S

G

E

A

I

G

G

I

I

Q

D

Y

E

L

L

H

V

V

F

V

L

D

D

L

I

D

T

G

-

A

A

K

K

A

R

K

K

H

T

I

M

I

L

N

-

H

-

K

E

V

L

L

V

E

E

Q

K

I

V

A

A

T

E

K

Q

T

I

N

D

L

I

K

P

I

F

D

T

F

V

G

G

G
|
G

L

I

K

H

T

D

N

F

E

E

D

T

L

A

K

S

I

E

A

L

F

I

N

L

S

R

G

G

A

A

S

D

Q

K

I

V

T

S

G

I

G
x
N

S
x
T

I

A

A

A

V

V

K

E

N

N

P

P

K

S

I

L

F

I

Q

T

E

Q

W

I

L

A

T

Q

K

T

F

F

G

G

S

S

D

Q

K

A

I

V

L

V

G

A

A

I

D
|
D

C

A

-

K

-

R

-

V

-

D

-

G

-

E

-

F

-

M

-

V

-

F

-

T

-

Y

-

S

-

G

-

K

N

K

N

N

E

T

N

G

I

I

A

L

I

L

S

R

G

D

W

W

L

V

E

V

E

E

S

-

D

-

L

-

K

-

V

-

I

-

P

-

F

-

I

-

Q

-

D

-

Y

V

Q

E

T

K

K

R

G

G

A

A

S

G

Y

E

V

I

I

L

C

L

T

T

D

S

I

I

S

D

K

R

D

D

G

G

M

T

L

K

E

S

G

G

P

Y

S

D

F

T

E

E

L

M

Y

I

E

-

R

R

I

F

L

V

K

R

E

P

T

L

K

T

N

T

L

L

N

P

L

I

I

I

A

A

S

S

G

G

I

A

S

G

T

K

F

M

D

E

E

H

L

F

P

L

K

E

L

A

A

F

E

L

L

A

G

G

C

A

E

D

G

A

V

A

I

L

I

A

G

A

K

S

A

V

I

F

Y

H

E

F

N

R

R

E

I

I

S

D

L

V

K

R

Q

E

L

L

E

K

N

E

Y

Y

I

L

active site: D11 (= D8), D116 (= D130)
binding phosphate ion: G68 (= G82), N89 (≠ G103), T90 (≠ S104)

7qc8A Imidazole glycerol phosphate synthase subunit HisF (see paper)
22% identity, 98% coverage: 2:238/241 of query aligns to 5:241/250 of 7qc8A

query
sites
7qc8A

R

R

I

I

P

A

A

A

I

L

D
x
E

I

V

I

K

D

D

G

G

K

R

C

V

V

V

R

K

L

G

S

T

K

-

G

-

D

-

Y

-

N

N

T

F

K

E

K

N

I

L

Y

R

N

D

E

S

-

G

S

D

P

P

L

A

E

E

V

L

A

G

K

K

S

F

F

Y

E

S

G

E

A

I

G

G

I

I

Q

D

Y

E

L

L

H

V

V

F

V
x
H

D

D

L
x
H

D

T

G

A

A

S

K

V

A

E

K

K

H

R

I

K

I

T

N

M

H

L

K

E

V

L

L

V

E

E

Q

K

I

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A

A

T

E

K

Q

T

I

N

D

L

I

K

P

I

F

D

T

F

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G

G

L

I

K

H

T

D

N

F

E

E

D

T

L

A

K

S

I

E

A

L

F

I

N

L

S

R

G

G

A

A

S

D

Q

K

I

V

T

S

G

I

G

N

S

T

I

A

A

A

V

V

K

E

N

N

P

P

K

S

I

L

F

I

Q

T

E

Q

W

I

L

A

T

Q

K

T

F

F

G

G

S

S

D

Q

K

A

I

V

L

V

G

A

A

I

D

D

C

A

-

K

-

R

-

V

-

D

-

G

-

E

-

F

-

M

-

V

-

F

-

T

-

Y

-

S

-

G

-

K

N

K

N

N

E

T

N

G

I

I

A

L

I

L

S

R

G

D

W

W

L

V

E

V

E

E

S

-

D

-

L

-

K

-

V

-

I

-

P

-

F

-

I

-

Q

-

D

-

Y

V

Q

E

T

K

K

R

G

G

A

A

S

G

Y

E

V

I

I

L

C

L

T

T

D

S

I

I

S

D

K

R

D

D

G

G

M

T

L

K

E

S

G

G

P

Y

S

D

F

T

E

E

L

M

Y

I

E

-

R

R

I

F

L

V

K

R

E

P

T

L

K

T

N

T

L

L

N

P

L

I

I

I

A

A

S

S

G

G

I

A

S

G

T

K

F

M

D

E

E

H

L

F

P

L

K

E

L

A

A

F

E

L

L

A

G

G

C

A

E

D

G

A

V

A

I

L

I

A

G

A

K

S

A

V

I

F

Y

H

E

F

N

R

R

E

I

I

S

D

L

V

K

R

Q

E

L

L

E

K

N

E

Y

Y

I

L

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

5d2tA Directed evolutionary changes in kemp eliminase ke07 - crystal 3 wild type
20% identity, 98% coverage: 2:238/241 of query aligns to 3:239/251 of 5d2tA

query
sites
5d2tA

R

R

I

I

P

A

A

A

I

L

D

I

I

V

I

K

D

D

G

G

K

R

C

V

V

V

R

K

L

G

S

S

K

-

G

-

D

-

Y

-

N

N

T

F

K

E

K

N

I

L

Y

R

N

D

E

S

-

G

S

D

P

P

L

V

E

E

V

L

A

G

K

K

S

F

F

Y

E

S

G

E

A

I

G

G

I

I

Q

D

Y

E

L

L

H

S

V

F

V
x
W

D

D

L

I

D

T

G

A

A

S

K

V

A

E

K

K

H

R

I

K

I

T

N

M

H

L

K

E

V

L

L

V

E

E

Q

K

I

V

A

A

T

E

K

Q

T

I

N

D

L

I

K

P

I

F

D

T

F

V

G

G

L

I

K

H

T

D

N

F

E

E

D

T

L

A

K

S

I

E

A

L

F

I

N

L

S

R

G

G

A

A

S

D

Q

K

I

V

T
x
E

G

I

G

N

S

T

I

A

A

A

V

V

K

E

N

N

P

P

K

S

I

L

F

I

Q

T

E

Q

W

I

L

A

T

Q

K

T

F

F

G

G

S

S

D

Q

K

A

I

V

-

V

-
x
Y

L

I

G

A

A

A

D

K

C

R

N

V

N

D

E

G

N

E

I

F

A

M

I

V

S

F

G

T

W

Y

L

S

E

G

E

K

S

K

D

N

L

T

K

G

V

I

I

L

-

L

-

R

P

D

F

W

I

V

Q

V

D

E

Y

V

Q

E

T

K

K

R

G

G

A

A

S

G

Y

E

V

I

I

V

C

L

T

G

D

S

I

I

S

D

K

R

D

L

G

G

M

T

L

K

E

S

G

G

P

Y

S

D

F

T

E

E

L

M

Y

I

E

-

R

R

I

F

L

V

K

R

E

P

T

L

K

T

N

T

L

L

N

P

L

I

I

I

A

A

S

H

G

G

I

A

S

G

T

K

F

M

D

E

E

H

L

F

P

L

K

E

L

A

A

F

E

L

L

A

G

G

C

A

E

D

G

A

V

A

I
x
K

I

A

G

N

K

S

A

V

I

L

Y

H

E

F

N

R

R

E

I

I

S

D

L

V

K

R

Q

E

L

L

E

K

N

E

Y

Y

I

L

binding 5-nitro-2-oxidanyl-benzenecarbonitrile: W48 (≠ V50), E99 (≠ T101), Y126 (vs. gap), K220 (≠ I219)

4ewnD Structure of hisf-d130v+d176v with bound rcdrp (see paper)
21% identity, 98% coverage: 2:238/241 of query aligns to 4:234/243 of 4ewnD

query
sites
4ewnD

R

R

I

I

P

A

A

C

I

L

D

D

I

V

I

K

D

D

G

G

K

R

C

V

V

V

R

K

L

G

S

T

K

-

G

-

D

-

Y

-

N

N

T

F

K

E

K

N

I

L

Y

R

N

D

E

S

-

G

S

D

P

P

L

V

E

E

V

L

A

G

K

K

S

F

F

Y

E

S

G

E

A

I

G

G

I

I

Q

D

Y

E

L

L

H

V

V

F

V

L

D

D

L

I

D

-

G

-

A

-

K

-

A

T

K

K

H

T

I

M

I

L

N

-

H

-

K

E

V

L

L

V

E

E

Q

K

I

V

A

A

T

E

K

Q

T

I

N

D

L

I

K

P

I

F

D

T

F

V

G

G

L

I

K

H

T

D

N

F

E

E

D

T

L

A

K

S

I

E

A

L

F

I

N

L

S

R

G

G

A

A

S

D

Q

K

I

V

T

S

G

I

G

N

S

T

I

A

A

A

V

V

K

E

N

N

P

P

K

S

I

L

F

I

Q

T

E

Q

W

I

L

A

T

Q

K

T

F

F

G

G

S

S

D

Q

K

A

I

V

L

V

G

A

-

I

-
x
V

-

A

-

K

-

R

A

V

D

D

C

G

N

E

N

F

E

M

N

V

I

F

A

T

I

Y

S

S

G

G

W

K

L

-

E

K

E

N

S

T

D

G

L

I

K

L

V

L

I

R

P

D

F

W

I

V

Q

V

D

E

Y

V

Q

E

T

K

K

R

G

G

A

A

S

G

Y

E

V

I

I

L

C

L

T

T

D

S

I

I

S

D

K

R

D

V

G
|
G

M

T

L

K

E

S

G

G

P

Y

S

D

F

T

E

E

L

M

Y

I

E

-

R

R

I

F

L

V

K

R

E

P

T

L

K

T

N

T

L

L

N

P

L

I

I

I

A

A

S
|
S

G
|
G

I

A

S

G

T

K

F

M

D

E

E

H

L

F

P

L

K

E

L

A

A

F

E

L

L

A

G

G

C

A

E

D

G

A

V

A

I
x
L

I
x
A

G
x
A

K
x
S

A

V

I

F

Y

H

E

F

N

R

R

E

I

I

S

D

L

V

K

R

Q

E

L

L

E

K

N

E

Y

Y

I

L

binding 1-(O-carboxy-phenylamino)-1-deoxy-D-ribulose-5-phosphate: V123 (vs. gap), G170 (= G173), S194 (= S198), G195 (= G199), G196 (= G200), L215 (≠ I219), A216 (≠ I220), A217 (≠ G221), S218 (≠ K222)

6dnjA Directed evolutionary changes in kemp eliminase ke07 - crystal 28 round 5 (see paper)
19% identity, 98% coverage: 2:238/241 of query aligns to 4:240/250 of 6dnjA

query
sites
6dnjA

R

R

I

I

I

D

P

A

A

A

I

L

D

I

I

M

I

K

D

D

G

G

K

R

C

V

V

V

R

K

L

G

S

S

K

-

G

-

D

-

Y

-

N

N

T

F

K

E

K

N

I

L

Y

R

N

D

E

S

-

G

S

D

P

P

L

V

E

E

V

L

A

G

K

K

S

F

F

Y

E

S

G

E

A

I

G

G

I

I

Q

D

Y

E

L

L

H

S

V

F

V
x
W

D

D

L

I

D

T

G

A

A

S

K

V

A

E

K

K

H

R

I

K

I

T

N

M

H

L

K

E

V

L

L

V

E

E

Q

K

I

V

A

A

T

E

K

Q

T

I

N

D

L

I

K

P

I

F

D

T

F

V

G
|
G

G

G

L

I

K

H

T

D

N

F

E

E

D

T

L

A

K

S

I

E

A

L

F

I

N

L

S

R

G

G

A

A

S

D

Q

K

I

V

T

E

G

I

G
x
N

S

T

I

A

A

A

V

V

K

E

N

N

P

P

K

S

I

L

F

I

Q

T

E

Q

W

I

L

A

T

Q

K

T

F

F

G

G

S

S

D

Q

K

A

I

V

-

V

-
x
Y

L

I

G

A

A

A

D

K

C

R

N

V

N

D

E

G

N

E

I

F

A

M

I

V

S

F

G

T

W

Y

L

S

E

G

E

K

S

K

D

N

L

T

K

G

V

I

I

L

-

L

-

R

P

D

F

W

I

V

Q

V

D

E

Y

V

Q

E

T

K

K

R

G

G

A

A

S

G

Y

E

V

I

I

V

C

L

T

G

D

S

I

I

S

D

K

R

D

L

G

G

M

T

L

K

E

S

G

G

P

Y

S

D

F

T

E

E

L

M

Y

I

E

-

R

R

I

F

L

V

K

R

E

P

T

L

K

T

N

T

L

L

N

P

L

I

I

I

A

A

S

H

G

R

G

G

I

A

S

G

T

K

F

M

D

E

E

H

L

F

P

L

K

E

L

A

A

F

E

L

L

A

G

G

C

A

E

D

G

A

V

A

I

K

I

A

G

D

K

S

A

V

I

F

Y

H

E

F

N

R

R

E

I

I

S

D

L

V

K

R

Q

E

L

L

E

K

N

E

Y

Y

I

L

binding 5-nitro-1,2-benzoxazole: W49 (≠ V50), G79 (= G80), G80 (= G81), N102 (≠ G103), Y127 (vs. gap)

Query Sequence

>WP_055437260.1 NCBI__GCF_001418085.1:WP_055437260.1
MRIIPAIDIIDGKCVRLSKGDYNTKKIYNESPLEVAKSFEGAGIQYLHVVDLDGAKAKHI
INHKVLEQIATKTNLKIDFGGGLKTNEDLKIAFNSGASQITGGSIAVKNPKIFQEWLTKF
GSDKIILGADCNNENIAISGWLEESDLKVIPFIQDYQTKGASYVICTDISKDGMLEGPSF
ELYERILKETKNLNLIASGGISTFDELPKLAELGCEGVIIGKAIYENRISLKQLENYIIN
K

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