SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing CA265_RS19260 FitnessBrowser__Pedo557:CA265_RS19260 to proteins with known functional sites using BLASTp with E ≤ 0.001.

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

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

7ac8A Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. (see paper)
33% identity, 82% coverage: 1:210/255 of query aligns to 1:208/252 of 7ac8A

query
sites
7ac8A

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active site: D11 (≠ L11), D130 (= D131)
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 (= L51), I52 (= I53), G82 (= G83), N103 (≠ Q104), T104 (= T105), D130 (= D131), S144 (= S146), D176 (= D178), G177 (= G179), S201 (≠ L203)

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

1gpwC Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex. (see paper)
33% identity, 82% coverage: 1:210/255 of query aligns to 1:208/253 of 1gpwC

query
sites
1gpwC

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active site: N11 (≠ L11), D130 (= D131)
binding phosphate ion: G82 (= G83), N103 (≠ Q104), T104 (= T105), D176 (= D178), G177 (= G179)

Sites not aligning to the query:

binding phosphate ion: 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)
33% identity, 82% coverage: 1:210/255 of query aligns to 1:208/253 of Q9X0C6

query
sites
Q9X0C6

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C9 (≠ A9) mutation to A: No change in activity.
D11 (≠ L11) mutation to X: Loss of activity.
K19 (= K20) mutation to S: Decrease in activity.
D51 (= D52) mutation to N: No change in activity.
N103 (≠ Q104) mutation to A: No change in activity.
D130 (= D131) 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 (= D178) mutation to N: Decrease in activity.
D183 (= D185) mutation to N: No change in activity.

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)
31% identity, 90% coverage: 1:229/255 of query aligns to 1:234/258 of P60664

query
sites
P60664

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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 (= E47) mutation to A: Loss of activity.; mutation to G: Loss of IGP synthase activity. Weak IGP synthase and HisH activities in vitro.
Q123 (≠ S124) mutation to A: Decrease in activity.; mutation to R: Loss of IGP synthase activity. Weak HisH activity in vitro.
C124 (≠ A125) mutation to A: No change in activity.; mutation to R: Loss of IGP synthase activity. Weak HisH activity in vitro.

1h5yB Hisf protein from pyrobaculum aerophilum (see paper)
31% identity, 81% coverage: 5:210/255 of query aligns to 6:211/253 of 1h5yB

query
sites
1h5yB

R

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E

active site: D12 (≠ L11), D133 (= D131)
binding glycerol: K22 (= K20), N106 (≠ Q104), A131 (≠ S129), D133 (= D131), G147 (≠ E147), T174 (≠ N173), D179 (= D178)
binding phosphate ion: G84 (= G82), G85 (= G83), N106 (≠ Q104), T107 (= T105), D179 (= D178), G180 (= G179)

Sites not aligning to the query:

binding phosphate ion: 226, 227, 228

7qc8A Imidazole glycerol phosphate synthase subunit HisF (see paper)
32% identity, 82% coverage: 2:210/255 of query aligns to 2:208/250 of 7qc8A

query
sites
7qc8A

L

L

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I

S

G

G

D

D

P

P

L

A

N

E

A

L

M

G

R

K

I

F

F

Y

N

S

T

E

K

I

E

G

V

I

D

D

E

E

L

L

M

V

V

F

L
x
H

D

D

I
x
H

D

T

A

A

S

S

K

V

L

E

K

K

R

R

E

K

P

T

N

M

Y

L

G

E

L

L

I

V

E

E

Q

K

F

V

A

A

G

E

E

Q

C

I

F

D

M

I

P

P

L

F

C

T

Y

V

G

G

I

I

K

H

T

D

I

F

D

E

Q

T

A

A

Y

S

K

E

I

L

F

I

K

L

L

R

G

G

V

A

E

D

K

K

I

V

C

S

L

I

Q

N

T

T

A

A

V

A

L

V

E

E

D

N

L

P

D

S

L

L

V

I

R

T

D

Q

L

I

V

A

A

Q

R

T

F

F

G

G

S

S

S

Q

A

A

I

V

V

V

S

A

V

I

D

D

V

A

K

K

K

R

-

V

-

D

-

G

D

E

W

F

L

M

Q

-

R

-

P

-

K

-

L

V

F

F

K

T

S

Y

S

S

E

G

G

K

K

K

N

N

A

T

N

G

-

I

-

L

E

R

N

D

W

W

I

V

S

V

Y

E

I

V

K

E

Q

K

A

-

V

-

D

-

A

R

G

G

A

A

G

G

E

E

I

I

L

L

N

T

A

S

V

I

D

D

K

R

D

D

G

G

T

T

L

K

Q

S

G

G

S

Y

D

D

L

T

T

E

L

M

I

I

K

R

Q

F

A

V

S

R

G

P

E

L

I

T

S

T

A

L

P

P

L

I

I

I

A

A

L

S

G

G

I

A

G

G

S

K

L

M

K

E

binding zinc ion: E11 (≠ L11), H50 (≠ L51), H52 (≠ I53)

5d2tA Directed evolutionary changes in kemp eliminase ke07 - crystal 3 wild type
31% identity, 89% coverage: 5:231/255 of query aligns to 3:227/251 of 5d2tA

query
sites
5d2tA

R

R

V

I

I

I

P

A

A

A

L

L

L

I

L

V

N

-

Q

K

H

D

G

G

G

R

L

V

V

V

K

K

T

G

T

S

K

N

F

F

A

E

A

N

P

L

K

R

Y

D

I

S

G

G

D

D

P

P

L

V

N

E

A

L

M

G

R

K

I

F

F

Y

N

S

T

E

K

I

E

G

V

I

D

D

E

E

L

L

M

S

V

F

L
x
W

D

D

I

I

D

T

A

A

S

S

K

V

L

E

K

K

R

R

E

K

P

T

N

M

Y

L

G

E

L

L

I

V

E

E

Q

K

F

V

A

A

G

E

E

Q

C

I

F

D

M

I

P

P

L

F

C

T

Y

V

G

G

I

I

K

H

T

D

I

F

D

E

Q

T

A

A

Y

S

K

E

I

L

F

I

K

L

L

R

G

G

V

A

E

D

K

K

I

V

C
x
E

L

I

Q

N

T

T

A

A

V

A

L

V

E

E

D

N

L

P

D

S

L

L

V

I

R

T

D

Q

L

I

V

A

A

Q

R

T

F

F

G

G

S

S

S

Q

A

A

I

V

V

V

S
x
Y

V

I

D

A

V

A

K

K

K

R

-

V

-

D

-

G

D

E

W

F

L

M

Q

-

R

-

P

-

K

-

L

V

F

F

K

T

S

Y

S

S

E

G

G

K

K

K

N

N

A

T

N

G

-

I

-

L

E

R

N

D

W

W

I

V

S

V

Y

E

I

V

K

E

Q

K

A

-

V

-

D

-

A

R

G

G

A

A

G

G

E

E

I

I

L

V

L

L

N

G

A

S

V

I

D

D

K

R

D

L

G

G

T

T

L

K

Q

S

G

G

S

Y

D

D

L

T

T

E

L

M

I

I

K

R

Q

F

A

V

S

R

G

P

E

L

I

T

S

T

A

L

P

P

L

I

I

I

A

A

L

H

G

G

I

A

G

G

S

K

L

M

K

E

D

H

I

F

K

L

D

E

A

A

V

F

D

L

A

A

G

G

A

A

S

D

A

A

V

A

A
x
K

A

A

G

N

A

S

F

V

F

L

V

H

F

F

binding 5-nitro-2-oxidanyl-benzenecarbonitrile: W48 (≠ L51), E99 (≠ C102), Y126 (≠ S129), K220 (≠ A224)

3zr4E Structural evidence for ammonia tunneling across the (beta-alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex (see paper)
32% identity, 82% coverage: 1:210/255 of query aligns to 1:199/244 of 3zr4E

query
sites
3zr4E

M

M

L

L

K

A

H

K

R

R

V

I

I

I

P

A

A

C

L

L

L
x
D

L

V

N

-

Q

K

H

D

G

G

G

R

L

V

V

V

K

K

T

S

T

-

K

-

F

-

A

-

P

-

K

-

Y

-

I

-

G

G

D

D

P

P

L

V

N

E

A

L

M

G

R

K

I

F

F

Y

N

S

T

E

K

I

E

G

V

I

D

D

E

E

L

L

M

V

V

F

L

L

D

D

I

I

D

T

A

A

S

S

K

V

L

E

K

K

R

R

E

K

P

T

N

M

Y

L

G

E

L

L

I

V

E

E

Q

K

F

V

A

A

G

E

E

Q

C

I

F

D

M

I

P

P

L

F

C

T

Y

V

G

G

I

I

K

H

T

D

I

F

D

E

Q

T

A

A

Y

S

K

E

I

L

F

I

K

L

L

R

G

G

V

A

E

D

K

K

I

V

C

S

L

I

Q

N

T

T

A

A

V

A

L

V

E

E

D

N

L

P

D

S

L

L

V

I

R

T

D

Q

L

I

V

A

A

Q

R

T

F

F

G

G

S

S

S

Q

A

A

I

V

V

V

S

A

V

I

D
|
D

V

A

K

K

K

R

-

V

-

D

-

G

D

E

W

F

L

M

Q

-

R

-

P

-

K

-

L

V

F

F

K

T

S

Y

S

S

E

G

G

K

K

K

N

N

A

T

N

G

-

I

-

L

E

R

N

D

W

W

I

V

S

V

Y

E

I

V

K

E

Q

K

A

-

V

-

D

-

A

R

G

G

A

A

G

G

E

E

I

I

L

L

N

T

A

S

V

I

D

D

K

R

D

D

G

G

T

T

L

K

Q

S

G

G

S

Y

D

D

L

T

T

E

L

M

I

I

K
x
R

Q

F

A

V

S

R

G

P

E

L

I

T

S

T

A

L

P

P

L

I

I

I

A

A

L

S

G

G

I

A

G

G

S

K

L

M

K

E

active site: D11 (≠ L11), D121 (= D131)
binding glycerol: R179 (≠ K190)

Sites not aligning to the query:

binding glycerol: 206

6dnjA Directed evolutionary changes in kemp eliminase ke07 - crystal 28 round 5 (see paper)
31% identity, 89% coverage: 7:232/255 of query aligns to 5:229/250 of 6dnjA

query
sites
6dnjA

I

I

P

D

A

A

L

A

L

L

L

I

N

M

Q

K

H

D

G

G

G

R

L

V

V

V

K

K

T

G

T

S

K

N

F

F

A

E

A

N

P

L

K

R

Y

D

I

S

G

G

D

D

P

P

L

V

N

E

A

L

M

G

R

K

I

F

F

Y

N

S

T

E

K

I

E

G

V

I

D

D

E

E

L

L

M

S

V

F

L
x
W

D

D

I

I

D

T

A

A

S

S

K

V

L

E

K

K

R

R

E

K

P

T

N

M

Y

L

G

E

L

L

I

V

E

E

Q

K

F

V

A

A

G

E

E

Q

C

I

F

D

M

I

P

P

L

F

C

T

Y

V

G
|
G

G

G

I

I

K

H

T

D

I

F

D

E

Q

T

A

A

Y

S

K

E

I

L

F

I

K

L

L

R

G

G

V

A

E

D

K

K

I

V

C

E

L

I

Q
x
N

T

T

A

A

V

A

L

V

E

E

D

N

L

P

D

S

L

L

V

I

R

T

D

Q

L

I

V

A

A

Q

R

T

F

F

G

G

S

S

S

Q

A

A

I

V

V

V

S
x
Y

V

I

D

A

V

A

K

K

K

R

-

V

-

D

-

G

D

E

W

F

L

M

Q

-

R

-

P

-

K

-

L

V

F

F

K

T

S

Y

S

S

E

G

G

K

K

K

N

N

A

T

N

G

-

I

-

L

E

R

N

D

W

W

I

V

S

V

Y

E

I

V

K

E

Q

K

A

-

V

-

D

-

A

R

G

G

A

A

G

G

E

E

I

I

L

V

L

L

N

G

A

S

V

I

D

D

K

R

D

L

G

G

T

T

L

K

Q

S

G

G

S

Y

D

D

L

T

T

E

L

M

I

I

K

R

Q

F

A

V

S

R

G

P

E

L

I

T

S

T

A

L

P

P

L

I

I

I

A

A

L

H

G

R

G

G

I

A

G

G

S

K

L

M

K

E

D

H

I

F

K

L

D

E

A

A

V

F

D

L

A

A

G

G

A

A

S

D

A

A

V

A

A

K

A

A

G

D

A

S

F

V

F

F

V

H

F

F

H

R

binding 5-nitro-1,2-benzoxazole: W49 (≠ L51), G79 (= G81), G80 (= G82), N102 (≠ Q104), Y127 (≠ S129)

2wjzE Crystal structure of (hish) k181a y138a mutant of imidazoleglycerolphosphate synthase (hish hisf) which displays constitutive glutaminase activity (see paper)
32% identity, 72% coverage: 28:210/255 of query aligns to 16:194/237 of 2wjzE

query
sites
2wjzE

K

R

Y

V

I

V

G

G

D

D

P

P

L

V

N

E

A

L

M

G

R

K

I

F

F

Y

N

S

T

E

K

I

E

G

V

I

D

D

E

E

L

L

M

V

V

F

L

L

D

D

I

I

D

T

A

A

S

-

K

-

L

-

K

K

R

R

E

K

P

T

N

M

Y

L

G

E

L

L

I

V

E

E

Q

K

F

V

A

A

G

E

E

Q

C

I

F

D

M

I

P

P

L

F

C

T

Y

V

G

G

G
|
G

I

I

K

H

T

D

I

F

D

E

Q

T

A

A

Y

S

K

E

I

L

F

I

K

L

L

R

G

G

V

A

E

D

K

K

I

V

C

S

L

I

Q
x
N

T
|
T

A

A

V

A

L

V

E

E

D

N

L

P

D

S

L

L

V

I

R

T

D

Q

L

I

V

A

A

Q

R

T

F

F

G

G

S

S

S

Q

A

A

I

V

V

V

S

A

V

I

D
|
D

V

A

K

K

K

R

-

V

-

D

-

G

D

E

W

F

L

M

Q

-

R

-

P

-

K

-

L

V

F

F

K

T

S

Y

S

S

E

G

G

K

K

K

N

N

A

T

N

G

-

I

-

L

E

R

N

D

W

W

I

V

S

V

Y

E

I

V

K

E

Q

K

A

R

V

-

D

-

A

-

G

G

A

A

G

G

E

E

I

I

L

L

N

T

A

S

V

I

D

D

K

R

D

D

G

G

T

T

L

K

Q

S

G

G

S

Y

D

D

L

T

T

E

L

M

I

I

K

R

Q

F

A

V

S

R

G

P

E

L

I

T

S

T

A

L

P

P

L

I

I

I

A

A

L

S

G

G

I

A

G

G

S

K

L

M

K

E

active site: D116 (= D131)
binding phosphate ion: G68 (= G83), N89 (≠ Q104), T90 (= T105)

Sites not aligning to the query:

active site: 11

3iivB Evolutionary optimization of computationally designed enzymes: kemp eliminases of the ke07 series (see paper)
30% identity, 91% coverage: 2:232/255 of query aligns to 2:227/262 of 3iivB

query
sites
3iivB

L

L

K

A

H

K

R

R

V

I

I

D

P

A

A

A

L

L

L

I

L

L

N

-

Q

K

H

D

G

G

G

R

L

V

V

V

K

K

T

G

T

S

K

N

F

F

A

E

A

N

P

L

K

R

Y

D

I

S

G

G

D

D

P

P

L

V

N

E

A

L

M

G

R

K

I

F

F

Y

N

S

T

E

K

I

E

G

V

I

D

D

E

E

L

L

M

S

V

F

L

W

D

D

I

I

D

T

A

A

S

S

K

-

L

V

K

E

R

K

E

K

P

T

N

M

Y

L

G

E

L

L

I

V

E

E

Q

K

F

V

A

A

G

E

E

Q

C

I

F

D

M

I

P

P

L

I

C

T

Y

V

G

G

I

I

K

Y

T

D

I

F

D

E

Q

T

A

A

Y

S

K

E

I

L

F

I

K

L

L

R

G

G

V

A

E

D

K

K

I

V

C
x
E

L

I

Q

N

T

T

A

A

V

A

L

V

E

E

D

N

L

P

D

S

L

L

V

I

R

T

D

Q

L

I

V

A

A

Q

R

T

F

F

G

G

S

S

S

Q

A

A

I

V

V

V

S

Y

V

I

D

A

V

A

K

K

K

R

-

V

-

D

-

G

D

E

W

F

L

M

Q

-

R

-

P

-

K

-

L

V

F

F

K

T

S

Y

S

S

E

G

G

T

K

K

N

N

A

T

N

G

-

I

-

L

E

R

N

D

W

W

I

V

S

V

Y

E

I

V

K

E

Q

K

A

-

V

-

D

-

A

R

G

G

A

A

G

G

E

E

I

I

L

V

L

L

N

G

A

S

V

I

D

D

K

R

D

L

G

G

T

T

L

K

Q

S

G

G

S

Y

D

D

L

T

T

E

L

M

I

I

K

R

Q

F

A

V

S

R

G

P

E

L

I

T

S

T

A

L

P

P

L

I

I

I

A

A

L

H

G

R

G

G

I

A

G

G

S

K

L

T

K

E

D

H

I

F

K

L

D

E

A

A

V

F

D

L

A

A

G

G

A

A

S

D

A

A

V

A

A
x
K

A

A

G

D

A

S

F

-

V

V

F

F

H

H

binding magnesium ion: E100 (≠ C102), K221 (≠ A224)

4ewnD Structure of hisf-d130v+d176v with bound rcdrp (see paper)
31% identity, 82% coverage: 2:210/255 of query aligns to 1:201/243 of 4ewnD

query
sites
4ewnD

L

L

K

A

H

K

R

R

V

I

I

I

P

A

A

C

L

L

L

D

L

V

N

-

Q

K

H

D

G

G

G

R

L

V

V

V

K

K

T

G

T

T

K

N

F

F

A

E

A

N

P

L

K

R

Y

D

I

S

G

G

D

D

P

P

L

V

N

E

A

L

M

G

R

K

I

F

F

Y

N

S

T

E

K

I

E

G

V

I

D

D

E

E

L

L

M

V

V

F

L

L

D

D

I

I

D

T

A

K

S

T

K

M

L

L

K

E

R

-

E

-

P

-

N

-

Y

-

G

-

L

L

I

V

E

E

Q

K

F

V

A

A

G

E

E

Q

C

I

F

D

M

I

P

P

L

F

C

T

Y

V

G

G

I

I

K

H

T

D

I

F

D

E

Q

T

A

A

Y

S

K

E

I

L

F

I

K

L

L

R

G

G

V

A

E

D

K

K

I

V

C

S

L

I

Q

N

T

T

A

A

V

A

L

V

E

E

D

N

L

P

D

S

L

L

V

I

R

T

D

Q

L

I

V

A

A

Q

R

T

F

F

G

G

S

S

S

Q

A

A

I

V

V

V

S

A

V

I

D

-

V
|
V

K

A

K

K

D

R

W

V

L

D

Q

G

R

E

P

F

K

M

L

V

F

F

K

T

S

Y

S

S

E

G

G

K

K

K

N

N

A

T

N

G

-

I

-

L

E

R

N

D

W

W

I

V

S

V

Y

E

I

V

K

E

Q

K

A

R

V

-

D

-

A

-

G

G

A

A

G

G

E

E

I

I

L

L

N

T

A

S

V

I

D

D

K

R

D

V

G
|
G

T

T

L

K

Q

S

G

G

S

Y

D

D

L

T

T

E

L

M

I

I

K

R

Q

F

A

V

S

R

G

P

E

L

I

T

S

T

A

L

P

P

L

I

I

I

A

A

L
x
S

G
|
G

I

A

G

G

S

K

L

M

K

E

binding 1-(O-carboxy-phenylamino)-1-deoxy-D-ribulose-5-phosphate: V123 (= V132), G170 (= G179), S194 (≠ L203), G195 (= G204), G196 (= G205)

Sites not aligning to the query:

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

1ox5A Towards understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerophosphate synthase (see paper)
27% identity, 84% coverage: 2:215/255 of query aligns to 239:493/532 of 1ox5A

query
sites
1ox5A

L

L

K

T

H

R

R

R

V

I

I

I

P

A

A

C

L

L

-
x
D

-

V

L

R

L

T

N

N

Q

D

H

Q

G

G

G

D

L

L

V

V

K

V

T

T

T

K

K

-

F

-

A

-

P

-

K

-

Y

-

I

L

G

G

D

K

P

P

L

V

N

Q

A

L

M

A

R

Q

I

K

F

Y

N

Y

T

Q

K

Q

E

G

V

A

D

D

E

E

L

V

M

T

V

F

L
|
L

D

N

I
|
I

D

-

A

T

S

C

K

P

L

L

K

K

R

D

E

T

P

P

N

M

Y

L

G

E

L

V

I

L

E

K

Q

Q

F

A

A

A

G

K

E

T

C

V

F

F

M

V

P

P

L

L

C

T

Y

V

G

G

G
|
G

G

G

I

I

K

K

T

D

I

I

-

V

-

D

-

V

-

D

-

G

-

T

-

K

-

I

-

P

-

A

-

L

D

E

Q

V

A

A

Y

S

K

L

I

Y

F

F

K

R

L

S

G

G

V

A

E

D

K

K

I

V

C

S

L

I

Q
x
G

T
|
T

A

D

V

A

L

V

E

Y

D

A

L

A

D

E

L

K

V

Y

R

Y

D

E

L

L

V

G

A

N

R

R

-

G

-

D

-

G

-

T

-

S

-

P

-

I

-

E

-

T

-

I

-

S

-

K

-

A

F

Y

G

G

S

A

S

Q

A

A

I

V

V

V

V

I

S
|
S

V

V

D
|
D

V

P

K

K

K

R

D

V

W

Y

L

V

Q

N

-

S

-

Q

-

A

-

D

-

T

R

K

P

N

K

K

L

V

F

F

K

E

S

T

S

E

E

Y

G

P

K

G

N

P

A

N

N

G

E

E

N

K

W

Y

I

C

S

W

Y

Y

-

Q

-

C

-

T

-

I

-

K

-
x
G

-

G

-

R

-

E

-

S

-

R

-

D

-

L

-

G

-

V

-

W

-

E

I

L

K

T

Q

R

A

A

V

C

D

E

A

A

-

L

G

G

A

A

G

G

E

E

I

I

L

L

N
|
N

A

C

V

I

D

D

K

K

D
|
D

G
|
G

T

S

L

N

Q

S

G

G

S

Y

D

D

L

L

T

E

L

L

I

I

K

E

Q

H

A

V

S

K

G

D

E

A

I

V

S

K

A

I

P

P

L

V

I

I

A

A

L

S

G
x
S

G

G

I

A

G

G

S

V

L

P

K

E

D

H

I

F

K

E

D

E

A

A

active site: D248 (vs. gap), D386 (= D131)
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 (= L51), I285 (= I53), G313 (= G82), G346 (≠ Q104), T347 (= T105), S384 (= S129), D386 (= D131), G424 (vs. gap), N451 (= N173), D456 (= D178), G457 (= G179), S482 (≠ G204)

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: 505, 506

1ox4B Towards understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerophosphate synthase (see paper)
27% identity, 84% coverage: 2:215/255 of query aligns to 239:499/538 of 1ox4B

query
sites
1ox4B

L

L

K

T

H

R

R

R

V

I

I

I

P

A

A

C

L

L

-
x
D

-

V

L

R

L

T

N

N

Q

D

H

Q

G

G

G

D

L

L

V

V

K

V

T

T

T

K

K

G

F

-

A

-

P

-

K

-

Y

D

I

L

G

G

D

K

P

P

L

V

N

Q

A

L

M

A

R

Q

I

K

F

Y

N

Y

T

Q

K

Q

E

G

V

A

D

D

E

E

L

V

M

T

V

F

L

L

D

N

I

I

D

T

A

S

S

F

K

R

-

D

-

C

-

P

L

L

K

K

R

D

E

T

P

P

N

M

Y

L

G

E

L

V

I

L

E

K

Q

Q

F

A

A

A

G

K

E

T

C

V

F

F

M

V

P

P

L

L

C

T

Y

V

G

G

I

I

K

K

T

D

I

I

-

V

-

D

-

V

-

D

-

G

-

T

-

K

-

I

-

P

-

A

-

L

D

E

Q

V

A

A

Y

S

K

L

I

Y

F

F

K

R

L

S

G

G

V

A

E

D

K

K

I

V

C

S

L

I

Q

G

T

T

A

D

V

A

L

V

E

Y

D

A

L

A

D

E

L

K

V

Y

R

Y

D

E

L

L

V

G

A

N

R

R

-

G

-

D

-

G

-

T

-

S

-

P

-

I

-

E

-

T

-

I

-

S

-

K

-

A

F

Y

G

G

S

A

S

Q

A

A

I

V

V

V

V

I

S

S

V

V

D
|
D

V

P

K

K

K

R

D

V

W

Y

L

V

Q

N

-

S

-

Q

-

A

-

D

-

T

R

K

P

N

K

K

L

V

F

F

K

E

S

T

S

E

E

Y

G

P

K

G

N

P

A

N

N

G

E

E

N

K

W

Y

I

C

S

W

Y

Y

-

Q

-

C

-

T

-

I

-

K

-

G

-

R

-

E

-

S

-

R

-

D

-

L

-

G

-

V

-

W

-

E

I

L

K

T

Q

R

A

A

V

C

D

E

A

A

-

L

G

G

A

A

G

G

E

E

I

I

L

L

N

N

A

C

V

I

D

D

K

K

D

D

G
|
G

T

S

L

N

Q

S

G

G

S

Y

D

D

L

L

T

E

L

L

I

I

K

E

Q

H

A

V

S

K

G

D

E

A

I

V

S

K

A

I

P

P

L

V

I

I

A

A

L

S

G
x
S

G

G

I

A

G

G

S

V

L

P

K

E

D

H

I

F

K

E

D

E

A

A

active site: D248 (vs. gap), D392 (= D131)
binding pyrophosphate 2-: G463 (= G179), S488 (≠ G204)

Sites not aligning to the query:

binding pyrophosphate 2-: 511, 512

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)
26% identity, 74% coverage: 28:215/255 of query aligns to 274:511/552 of P33734

query
sites
P33734

K

R

Y

N

I

L

G

G

D

K

P

P

L

V

N

Q

A

L

M

A

R

Q

I

K

F

Y

N

Y

T

Q

K

Q

E

G

V

A

D

D

E

E

L

V

M

T

V

F

L

L

D

N

I

I

D

T

A

S

S

F

K

R

-

D

-

C

-

P

L

L

K

K

R

D

E

T

P

P

N

M

Y

L

G

E

L

V

I

L

E

K

Q

Q

F

A

A

A

G

K

E

T

C

V

F

F

M

V

P

P

L

L

C

T

Y

V

G

G

I

I

K

K

T

D

I

I

-

V

-

D

-

V

-

D

-

G

-

T

-

K

-

I

-

P

-

A

-

L

D

E

Q

V

A

A

Y

S

K

L

I

Y

F

F

K

R

L

S

G

G

V

A

E

D

K
|
K

I

V

C

S

L

I

Q

G

T

T

A

D

V

A

L

V

E

Y

D

A

L

A

D

E

L

K

V

Y

R

Y

D

E

L

L

V

G

A

N

R

R

-

G

-

D

-

G

-

T

-

S

-

P

-

I

-

E

-

T

-

I

-

S

-

K

-

A

F

Y

G

G

S

A

S

Q

A

A

I

V

V

V

V

I

S

S

V

V

D

D

V

P

K

K

K

R

D

V

W

Y

L

V

Q

N

-

S

-

Q

-

A

-

D

-

T

R

K

P

N

K

K

L

V

F

F

K

E

S

T

S

E

E

Y

G

P

K

G

N

P

A

N

N

G

E

E

N

K

W

Y

I

C

S

W

Y

Y

-

Q

-

C

-

T

-

I

-

K

-

G

-

R

-

E

-

S

-

R

-

D

-

L

-

G

-

V

-

W

-

E

I

L

K

T

Q

R

A

A

V

C

D

E

A

A

-

L

G

G

A

A

G

G

E

E

I

I

L

L

N

N

A

C

V

I

D

D

K

K

D

D

G

G

T

S

L

N

Q

S

G

G

S

Y

D

D

L

L

T

E

L

L

I

I

K

E

Q

H

A

V

S

K

G

D

E

A

I

V

S

K

A

I

P

P

L

V

I

I

A

A

L

S

G

S

G

G

I

A

G

G

S

V

L

P

K

E

D

H

I

F

K

E

D

E

A

A

K360 (= K100) mutation K->A,R: Almost no effect on activity.

Sites not aligning to the query:

239 mutation R->A,H,K: 1000-fold decrease in catalytic efficiency. Uncoupling of glutaminase activity from the cyclase activity.
258 K→A: No activity. Uncoupling of glutaminase activity from the cyclase activity.; K→R: Small reduction of activity.

5abtA S.Enterica hisa mutant d7n, g102a, v106m, d176a
24% identity, 78% coverage: 29:226/255 of query aligns to 27:225/246 of 5abtA

query
sites
5abtA

Y

Y

I

G

G

N

D

D

P

P

L

L

N

P

A

R

M

L

R

Q

I

D

F

Y

N

A

T

A

K

Q

E

G

V

A

D

G

E

V

L

L

M

H

V

L

L
x
V

D

D

I
x
L

D

T

A

G

S

A

K

K

L

D

K

P

R

A

E

K

P

R

N

Q

Y

I

G

P

L

L

I

I

E

K

Q

T

F

L

A

V

G

A

E

G

C

V

F

N

M

V

P

P

L

V

C

Q

Y

V

G

G

G
|
G

I

V

K
x
R

T

T

I

E

D

E

Q

D

A

V

Y

A

K

A

I

L

F

L

K

K

L

A

G

G

V

V

E

A

K

R

I

V

C
x
V

L

I

Q
x
A

T
x
S

A

T

V

A

L

M

E

K

D

S

L

P

D

D

L

V

V

V

R

K

D

G

L

W

V

F

A

E

R

R

F

F

G

G

S

A

S

Q

A

A

I

L

V

V

V

L

S

A

V

L

D
|
D

V

V

K

R

K

I

D

D

W

E

L

H

Q

G

R

T

P

K

K

Q

L

V

F

A

K

V

S

S

S
x
G

E
x
W

G

Q

K

E

N

N

A

S

N

G

E

V

N

S

W

L

I

E

S

Q

Y

L

I

V

K

E

Q

T

A

Y

V

L

D

P

A

V

G

G

A

L

G

K

E

H

I

V

L

L

L

C

N

T

A

D

V

I

D

S

K

R

D

A

G
|
G

T

T

L

L

Q

A

G

G

S

S

D

N

L

V

T

S

L

L

I

Y

K

E

Q

E

A

V

S

C

G

A

E

R

I

Y

S

-

A

-

P

P

L

Q

I

I

A

A

L

F

-

Q

-

S

-
x
S

G
|
G

G

G

I

I

G

G

S

D

L

I

K

D

D

D

I

I

K

A

D

A

A

L

V

R

D

G

A

T

G

G

A

V

S

R

A

G

V

V

A
x
I

A

V

G
|
G

active site: D129 (= D131)
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: V49 (≠ L51), L51 (≠ I53), G81 (= G83), R83 (≠ K85), V100 (≠ C102), A102 (≠ Q104), S103 (≠ T105), D129 (= D131), G144 (≠ S146), W145 (≠ E147), G177 (= G179), S202 (vs. gap), G203 (= G204), I223 (≠ A224), G225 (= G226)

Sites not aligning to the query:

5ab3A S.Enterica hisa mutant d7n, d10g, dup13-15, q24l, g102a (see paper)
25% identity, 87% coverage: 6:226/255 of query aligns to 2:222/241 of 5ab3A

query
sites
5ab3A

V

I

I

I

P

P

A

A

L

L

L
x
N

L

L

N

I

Q

-

H

G

G

G

G

T

L

V

V

V

K

R

T

V

K
x
R

F

L

A

H

A

Q

P

G

K

D

Y
|
Y

I

A

-

R

-

L

-

R

-

D

-

Y

-

G

G

N

D

D

P

P

L

L

N

P

A

R

M

L

R

Q

I

D

F

Y

N

A

T

A

K

Q

E

G

V

A

D

G

E

V

L

L

M

H

V

L

L
x
V

D

D

I

L

D

T

A

G

S

A

K

K

L

D

K

P

R

A

E

K

P

R

N

Q

Y

I

G

P

L

L

I

I

E

K

Q

T

F

L

A

V

G

A

E

G

C

V

F

N

M

V

P

P

L

V

C

Q

Y

V

G

G

G
|
G

I

V

K

R

T

T

I

E

D

E

Q

D

A

V

Y

A

K

A

I

L

F

L

K

K

L

A

G

G

V

V

E

A

K

R

I

V

C

V

L

I

Q
x
A

T
x
S

A

T

V

A

L

V

E

K

D

S

L

P

D

D

L

V

V

V

R

K

D

G

L

W

V

F

A

E

R

R

F

F

G

G

S

A

S

Q

A

A

I

L

V

V

V

L

S
x
A

V

L

D
|
D

V

V

K

R

K

I

D

D

W

E

L

H

Q

G

R

T

P

K

K

Q

L

V

F

A

K

V

S

S

S

-

E

-

G

G

K

V

N

S

A

L

N

E

E

Q

N

L

W

V

I

E

S

T

Y

Y

I

L

K

P

Q

-

A

-

V

-

D

-

A

V

G

G

A

L

G

K

E

H

I

V

L

L

L

C

N

T

A

D

V

I

D

S

K

R

D

D

G
|
G

T

T

L

L

Q

A

G

G

S

S

D

N

L

V

T

S

L

L

I

Y

K

E

Q

E

A

V

S

C

G

A

E

R

I

Y

S

-

A

-

P

P

L

Q

I

I

A

A

L

F

-

Q

-

S

-
x
S

G
|
G

I

I

G

G

S

D

L

I

K

D

D

D

I

I

K

A

D

A

A

L

V

R

D

G

A

T

G

G

A

V

S

R

A

G

V

V

A

I

A

V

G
|
G

active site: N7 (≠ L11), D132 (= D131)
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 (≠ L11), R18 (≠ K23), Y24 (= Y29), V52 (≠ L51), G84 (= G83), A105 (≠ Q104), S106 (≠ T105), A130 (≠ S129), D132 (= D131), G174 (= G179), S199 (vs. gap), G200 (= G204), G201 (= G205), G222 (= G226)

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: 223

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, 82% coverage: 6:215/255 of query aligns to 3:206/241 of Q9X0C7

query
sites
Q9X0C7

V

V

I

V

P

P

A

A

-

I

-
x
D

L

L

L

F

L

R

N

G

Q

K

H

V

G

A

G

R

L

M

V

I

K

K

T

G

T

R

K

K

F

E

A

N

A

T

P

I

K

F

Y

Y

I

E

G

K

D

D

P

P

L

V

N

E

A

L

M

V

R

E

I

K

F

L

N

I

T

E

K

E

E

G

V

F

D

T

E

L

L

I

M
x
H

V

V

L

V

D
|
D

I

L

D

S

A

N

S

A

K

I

L

E

K

N

R

S

E

G

P

E

N

N

Y

L

G

P

L

V

I

L

E

E

Q

K

F

L

A

S

G

-

E

E

C

F

F

A

M

E

P

H

L

I

C

Q

Y

I

G

G

I

I

K
x
R

T

S

I

L

D

D

Q

Y

A

A

Y

E

K

K

I

L

F

R

K

K

L

L

G

G

V

Y

E

R

K

R

I

Q

C

I

L

V

Q

S

T

S

A

K

V

V

L

L

E

E

D

D

L

P

D

S

L

F

V

L

R

K

D

S

L

L

V

-

A

-

R

R

F

E

G

I

S

D

S

V

A

E

I

P

V

V

V

F

S

S

V

L

D
|
D

V

T

K

R

-

G

-

R

-

V

-

A

-

F

K

K

D

G

W

W

L

L

Q

A

R

E

P

E

K

E

L

I

F

-

K

-

S

-

E

-

G

-

K

-

N

-

A

-

N

-

E

-

N

D

W

P

I

V

S

S

Y

L

I

L

K

K

Q

R

A

L

V

K

D

E

A

Y

G

G

A

L

G

E

E

E

I

I

L

V

L

H

N
x
T

A

E

V

I

D

E

K

K

D

D

G

G

T

T

L

L

Q

Q

G

E

S

H

D

D

L

F

T

S

L

L

I

T

K

K

Q

K

A

I

S

A

G

I

E

E

I

A

S

E

A

V

P

K

L

V

I

L

A

A

L

A

G

G

I

I

G

S

S

S

L

E

K

N

D

S

I

L

K

K

D

T

A

A

D8 (vs. gap) mutation to N: Loss of activity.
H48 (≠ M49) mutation to A: Decrease in activity.
D51 (= D52) mutation to N: Decrease in activity.
R83 (≠ K85) mutation to N: Decrease in activity.
D127 (= D131) mutation to N: Almost no activity.
T164 (≠ N173) mutation to A: Strong decrease in activity.

5dn1A Crystal structure of phosphoribosyl isomerase a from streptomyces coelicolor (see paper)
28% identity, 72% coverage: 31:213/255 of query aligns to 32:206/240 of 5dn1A

query
sites
5dn1A

G

G

D

S

P

P

L

L

N

E

A

A

M

A

R

L

I

A

F

W

N

Q

T

R

K

S

E

G

V

A

D

E

E

W

L

L

M

H

V

L

L

V

D

D

I
x
L

D

D

A

A

S

A

K

-

L
x
F

K

G

R

T

E

G

P

D

N

N

Y

R

G

A

L

L

I

I

E

A

Q

E

F

V

A

A

G

Q

E

A

C

M

F

D

M

I

P

K

L

V

C

E

Y

L

G
x
S

G

G

G
|
G

I

I

K
x
R

T

D

I

D

D

D

Q

T

A

L

Y

A

K

A

I

A

F

L

K

A

L

T

G

G

V

C

E

T

K

R

I

V

C

N

L

L

Q
x
G

T
|
T

A

A

V

A

L

L

E

E

D

T

L

P

D

E

L

W

V

V

R

A

D

K

L

V

V

I

A

A

R

E

F

H

G

G

S

D

S

K

A

-

I

I

V

A

V

V

S

G

V

L

D
|
D

V

V

K

R

K

G

D

T

W

T

L

L

Q

R

R

G

P

R

K
x
G

L
x
W

F

T

K

R

S

-

E

D

G

G

K

G

N

D

A

L

N

Y

E

E

N

T

W

L

I

D

S

R

Y

L

I

N

K

K

Q

E

A

-

V

-

D

-

A

-

G

G

A

C

G

A

E

R

I

Y

L

V

N

T

A

D

V

I

D

A

K

K

D

D

G

G

T

T

L

L

Q

Q

G

G

S

P

D

N

L

L

T

E

L

L

I

L

K

K

Q

N

A

V

S

C

G

A

E

A

I

T

S

D

A

R

P

P

L

V

I

V

A

A

L

S

G

G

I

V

G

S

S

S

L

L

K

D

D

D

I

L

K

R

active site: D130 (= D131)
binding aminoimidazole 4-carboxamide ribonucleotide: L54 (≠ I53), F58 (≠ L58), S81 (≠ G81), G83 (= G83), R85 (≠ K85), G104 (≠ Q104), T105 (= T105), G140 (≠ K141), W141 (≠ L142)

Sites not aligning to the query:

active site: 11
binding aminoimidazole 4-carboxamide ribonucleotide: 23

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)
28% identity, 72% coverage: 31:213/255 of query aligns to 32:206/240 of P16250

query
sites
P16250

G

G

D

S

P

P

L

L

N

E

A

A

M

A

R

L

I

A

F

W

N

Q

T

R

K

S

E

G

V

A

D

E

E

W

L

L

M

H

V

L

L

V

D

D

I

L

D

D

A

A

S

A

K

-

L

F

K

G

R

T

E

G

P

D

N

N

Y

R

G

A

L

L

I

I

E

A

Q

E

F

V

A

A

G

Q

E

A

C

M

F

D

M

I

P

K

L

V

C

E

Y

L

G
x
S

G

G

I

I

K

R

T

D

I

D

D

D

Q

T

A

L

Y

A

K

A

I

A

F

L

K

A

L

T

G

G

V

C

E

T

K

R

I

V

C

N

L

L

Q

G

T

T

A

A

V

A

L

L

E

E

D

T

L

P

D

E

L

W

V

V

R

A

D

K

L

V

V

I

A

A

R

E

F

H

G

G

S

D

S

K

A

-

I

I

V

A

V

V

S

G

V

L

D
|
D

V

V

K

R

K

G

D

T

W

T

L

L

Q

R

R

G

P

R

K

G

L

W

F

T

K

R

S

-

E

D

G

G

K

G

N

D

A

L

N

Y

E

E

N

T

W

L

I

D

S

R

Y

L

I

N

K

K

Q

E

A

-

V

-

D

-

A

-

G

G

A

C

G

A

E

R

I

Y

L

V

N
x
T

A

D

V

I

D

A

K

K

D
|
D

G

G

T

T

L

L

Q

Q

G

G

S

P

D

N

L

L

T

E

L

L

I

L

K

K

Q

N

A

V

S

C

G

A

E

A

I

T

S

D

A

R

P

P

L

V

I

V

A

A

L

S

G

G

I

V

G

S

S

S

L

L

K

D

D

D

I

L

K

R

S81 (≠ G81) mutation to T: No activity toward PRA. Almost no effect on activity toward ProFAR.
D130 (= D131) mutation to A: Very low activity toward PRA. No activity toward ProFAR.; mutation to Q: No activity.
T166 (≠ N173) mutation to A: No activity.
D171 (= D178) mutation to A: Low activity toward PRA. No activity toward ProFAR.

Sites not aligning to the query:

11 D→A: No activity.
19 R→A: No effect on activity toward PRA. No activity toward ProFAR.

Query Sequence

>CA265_RS19260 FitnessBrowser__Pedo557:CA265_RS19260
MLKHRVIPALLLNQHGGLVKTTKFAAPKYIGDPLNAMRIFNTKEVDELMVLDIDASKLKR
EPNYGLIEQFAGECFMPLCYGGGIKTIDQAYKIFKLGVEKICLQTAVLEDLDLVRDLVAR
FGSSAIVVSVDVKKDWLQRPKLFKSSEGKNANENWISYIKQAVDAGAGEILLNAVDKDGT
LQGSDLTLIKQASGEISAPLIALGGIGSLKDIKDAVDAGASAVAAGAFFVFHGPHRAVLI
TYPQYQELLTLFNTK

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