SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing HSERO_RS21020 FitnessBrowser__HerbieS:HSERO_RS21020 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)

1gpwC Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex. (see paper)
42% identity, 82% coverage: 1:208/253 of query aligns to 1:207/253 of 1gpwC

query
sites
1gpwC

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active site: N11 (≠ L11), D130 (= D130)
binding phosphate ion: G82 (= G82), N103 (= N103), T104 (= T104), D176 (≠ E177), G177 (= G178)

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)
42% identity, 82% coverage: 1:208/253 of query aligns to 1:207/253 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 (= K19) mutation to S: Decrease in activity.
D51 (= D51) mutation to N: No change in activity.
N103 (= N103) mutation to A: No change in activity.
D130 (= D130) mutation D->A,C,F,G,H,I,K,L,M,N,P,Q,R,S,T,V,W,Y: Complete loss of activity.; mutation to E: Weak activity.
D176 (≠ E177) mutation to N: Decrease in activity.
D183 (= D184) mutation to N: No change in activity.

7ac8A Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. (see paper)
42% identity, 82% coverage: 1:208/253 of query aligns to 1:207/252 of 7ac8A

query
sites
7ac8A

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active site: D11 (≠ L11), D130 (= D130)
binding [(2R,3S,4R,5R)-5-[4-aminocarbonyl-5-[(E)-[[(2R,3R,4S,5R)-3,4-bis(oxidanyl)-5-(phosphonooxymethyl)oxolan-2-yl]amino]methylideneamino]imidazol-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl dihydrogen phosphate: L50 (= L50), I52 (= I52), G82 (= G82), N103 (= N103), T104 (= T104), D130 (= D130), S144 (= S145), D176 (≠ E177), G177 (= G178), S201 (≠ H202)

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

1h5yB Hisf protein from pyrobaculum aerophilum (see paper)
42% identity, 81% coverage: 5:208/253 of query aligns to 6:210/253 of 1h5yB

query
sites
1h5yB

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active site: D12 (≠ L11), D133 (= D130)
binding glycerol: K22 (= K19), N106 (= N103), A131 (≠ S128), D133 (= D130), G147 (≠ S145), T174 (= T172), D179 (≠ E177)
binding phosphate ion: G84 (= G81), G85 (= G82), N106 (= N103), T107 (= T104), D179 (≠ E177), G180 (= G178)

Sites not aligning to the query:

binding phosphate ion: 226, 227, 228

3zr4E Structural evidence for ammonia tunneling across the (beta-alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex (see paper)
42% identity, 82% coverage: 1:208/253 of query aligns to 1:198/244 of 3zr4E

query
sites
3zr4E

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active site: D11 (≠ L11), D121 (= D130)
binding glycerol: R179 (≠ K189)

Sites not aligning to the query:

binding glycerol: 206

7qc8A Imidazole glycerol phosphate synthase subunit HisF (see paper)
42% identity, 82% coverage: 2:208/253 of query aligns to 2:207/250 of 7qc8A

query
sites
7qc8A

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L

V

E

E

N

N

P

P

S

S

L

L

I

I

S

T

E

Q

I

I

A

A

T

Q

E

T

Y

F

G

G

S

S

Q

Q

A

A

V

V

S

A

V

I

D

D

V

A

K

K

G

-

G

R

V

V

L

D

G

G

G

E

Q

F

T

M

V

V

R

F

S

T

H

Y

S

S

G

G

R

K

H

K

N

N

T

T

G

G

R

I

D

L

P

L

V

R

A

D

W

W

A

V

Q

V

E

E

A

V

E

E

R

K

L

R

G

G

A

A

G

G

E

E

L

I

F

L

L

L

T

T

A

S

I

I

D

D

R

R

E

D

G

G

T

T

W

K

S

S

G

G

F

Y

D

D

I

T

D

E

L

M

V

I

K

R

K

F

V

V

T

R

D

P

A

L

V

T

S

T

I

L

P

P

V

I

I

I

A

A

H

S

G

G

A

A

G

G

S

K

L

M

binding zinc ion: E11 (≠ L11), H50 (≠ L50), H52 (≠ I52)

5d2tA Directed evolutionary changes in kemp eliminase ke07 - crystal 3 wild type
39% identity, 91% coverage: 5:233/253 of query aligns to 3:229/251 of 5d2tA

query
sites
5d2tA

R

R

V

I

I

I

P

A

A

A

L

L

L

I

L

V

Q

K

H

D

E

G

S

R

L

V

V

V

K

K

T

G

Q

S

R

N

F

F

S

E

T

N

F

L

D

R

Y

D

V

S

G

G

D

D

P

P

C

V

N

E

T

L

V

G

R

K

I

F

F

Y

N

S

E

E

L

I

E

G

V

I

D

D

E

E

L

L

F

S

F

F

L
x
W

D

D

I

I

A

T

A

A

S

S

R

V

E

E

K

K

K

R

G

K

P

T

N

M

L

L

Q

E

L

L

L

V

A

E

D

K

I

V

A

A

N

E

E

Q

C

I

F

D

M

I

P

P

L

F

G

T

Y

V

G

G

I

I

R

H

S

D

L

F

D

E

D

T

A

A

R

S

S

E

V

L

F

I

S

L

I

R

G

G

F

A

E

D

K

K

V

V

A
x
E

V

I

N

N

T

T

H

A

A

A

L

V

E

E

N

N

P

P

S

S

L

L

I

I

S

T

E

Q

I

I

A

A

T

Q

E

T

Y

F

G

G

S

S

Q

Q

A

A

V

V

S
x
Y

V

I

D

A

V

A

K

K

G

-

G

R

V

V

L

D

G

G

G

E

Q

F

T

M

V

V

R

F

S

T

H

Y

S

S

G

G

R

K

H

K

N

N

T

T

G

G

R

I

D

L

P

L

V

R

A

D

W

W

A

V

Q

V

E

E

A

V

E

E

R

K

L

R

G

G

A

A

G

G

E

E

L

I

F

V

L

L

T

G

A

S

I

I

D

D

R

R

E

L

G

G

T

T

W

K

S

S

G

G

F

Y

D

D

I

T

D

E

L

M

V

I

K

R

K

F

V

V

T

R

D

P

A

L

V

T

S

T

I

L

P

P

V

I

I

I

A

A

H

H

G

G

A

A

G

G

S

K

L

M

S

E

D

H

I

F

R

L

K

E

V

A

V

F

K

-

Q

L

A

A

G

G

A

A

S

D

A

A

V

A

A
x
K

L

A

G

N

S

S

M

V

V

L

V

H

Y

F

Q

R

K

E

binding 5-nitro-2-oxidanyl-benzenecarbonitrile: W48 (≠ L50), E99 (≠ A101), Y126 (≠ S128), K220 (≠ A224)

6dnjA Directed evolutionary changes in kemp eliminase ke07 - crystal 28 round 5 (see paper)
38% identity, 92% coverage: 2:233/253 of query aligns to 1:230/250 of 6dnjA

query
sites
6dnjA

L

L

R

A

T

K

R

R

V

I

I

D

P

A

A

A

L

L

L

I

L

M

Q

K

H

D

E

G

S

R

L

V

V

V

K

K

T

G

Q

S

R

N

F

F

S

E

T

N

F

L

D

R

Y

D

V

S

G

G

D

D

P

P

C

V

N

E

T

L

V

G

R

K

I

F

F

Y

N

S

E

E

L

I

E

G

V

I

D

D

E

E

L

L

F

S

F

F

L
x
W

D

D

I

I

A

T

A

A

S

S

R

V

E

E

K

K

K

R

G

K

P

T

N

M

L

L

Q

E

L

L

L

V

A

E

D

K

I

V

A

A

N

E

E

Q

C

I

F

D

M

I

P

P

L

F

G

T

Y

V

G
|
G

G

G

I

I

R

H

S

D

L

F

D

E

D

T

A

A

R

S

S

E

V

L

F

I

S

L

I

R

G

G

F

A

E

D

K

K

V

V

A

E

V

I

N
|
N

T

T

H

A

A

A

L

V

E

E

N

N

P

P

S

S

L

L

I

I

S

T

E

Q

I

I

A

A

T

Q

E

T

Y

F

G

G

S

S

Q

Q

A

A

V

V

S
x
Y

V

I

D

A

V

A

K

K

G

-

G

R

V

V

L

D

G

G

G

E

Q

F

T

M

V

V

R

F

S

T

H

Y

S

S

G

G

R

K

H

K

N

N

T

T

G

G

R

I

D

L

P

L

V

R

A

D

W

W

A

V

Q

V

E

E

A

V

E

E

R

K

L

R

G

G

A

A

G

G

E

E

L

I

F

V

L

L

T

G

A

S

I

I

D

D

R

R

E

L

G

G

T

T

W

K

S

S

G

G

F

Y

D

D

I

T

D

E

L

M

V

I

K

R

K

F

V

V

T

R

D

P

A

L

V

T

S

T

I

L

P

P

V

I

I

I

A

A

H

H

G

R

G

G

A

A

G

G

S

K

L

M

S

E

D

H

I

F

R

L

K

E

V

A

V

F

K

-

Q

L

A

A

G

G

A

A

S

D

A

A

V

A

A

K

L

A

G

D

S

S

M

V

V

F

V

H

Y

F

Q

R

K

E

binding 5-nitro-1,2-benzoxazole: W49 (≠ L50), G79 (= G80), G80 (= G81), N102 (= N103), Y127 (≠ S128)

2wjzE Crystal structure of (hish) k181a y138a mutant of imidazoleglycerolphosphate synthase (hish hisf) which displays constitutive glutaminase activity (see paper)
44% identity, 71% coverage: 29:208/253 of query aligns to 18:193/237 of 2wjzE

query
sites
2wjzE

V

V

G

G

D

D

P

P

C

V

N

E

T

L

V

G

R

K

I

F

F

Y

N

S

E

E

L

I

E

G

V

I

D

D

E

E

L

L

F

V

F

F

L

L

D

D

I

I

A

T

A

A

S

K

R

R

E

K

K

-

G

-

P

T

N

M

L

L

Q

E

L

L

L

V

A

E

D

K

I

V

A

A

N

E

E

Q

C

I

F

D

M

I

P

P

L

F

G

T

Y

V

G

G

G
|
G

I

I

R

H

S

D

L

F

D

E

D

T

A

A

R

S

S

E

V

L

F

I

S

L

I

R

G

G

F

A

E

D

K

K

V

V

A

S

V

I

N
|
N

T
|
T

H

A

A

A

L

V

E

E

N

N

P

P

S

S

L

L

I

I

S

T

E

Q

I

I

A

A

T

Q

E

T

Y

F

G

G

S

S

Q

Q

A

A

V

V

S

A

V

I

D
|
D

V

A

K

K

G

R

G

-

V

V

L

D

G

G

G

E

Q

F

T

M

V

V

R

F

S

T

H

Y

S

S

G

G

R

K

H

K

N

N

T

T

G

G

R

I

D

L

P

L

V

R

A

D

W

W

A

V

Q

V

E

E

A

V

E

E

R

K

L

R

G

G

A

A

G

G

E

E

L

I

F

L

L

L

T

T

A

S

I

I

D

D

R

R

E

D

G

G

T

T

W

K

S

S

G

G

F

Y

D

D

I

T

D

E

L

M

V

I

K

R

K

F

V

V

T

R

D

P

A

L

V

T

S

T

I

L

P

P

V

I

I

I

A

A

H

S

G

G

A

A

G

G

S

K

L

M

active site: D116 (= D130)
binding phosphate ion: G68 (= G82), N89 (= N103), T90 (= T104)

Sites not aligning to the query:

active site: 11

3iivB Evolutionary optimization of computationally designed enzymes: kemp eliminases of the ke07 series (see paper)
42% identity, 81% coverage: 2:206/253 of query aligns to 2:204/262 of 3iivB

query
sites
3iivB

L

L

R

A

T

K

R

R

V

I

I

D

P

A

A

A

L

L

L

I

L

L

Q

K

H

D

E

G

S

R

L

V

V

V

K

K

T

G

Q

S

R

N

F

F

S

E

T

N

F

L

D

R

Y

D

V

S

G

G

D

D

P

P

C

V

N

E

T

L

V

G

R

K

I

F

F

Y

N

S

E

E

L

I

E

G

V

I

D

D

E

E

L

L

F

S

F

F

L

W

D

D

I

I

A

T

A

A

S

S

R

V

E

E

K

K

G

-

P

T

N

M

L

L

Q

E

L

L

L

V

A

E

D

K

I

V

A

A

N

E

E

Q

C

I

F

D

M

I

P

P

L

I

G

T

Y

V

G

G

I

I

R

Y

S

D

L

F

D

E

D

T

A

A

R

S

S

E

V

L

F

I

S

L

I

R

G

G

F

A

E

D

K

K

V

V

A
x
E

V

I

N

N

T

T

H

A

A

A

L

V

E

E

N

N

P

P

S

S

L

L

I

I

S

T

E

Q

I

I

A

A

T

Q

E

T

Y

F

G

G

S

S

Q

Q

A

A

V

V

S

Y

V

I

D

A

V

A

K

K

G

-

G

R

V

V

L

D

G

G

G

E

Q

F

T

M

V

V

R

F

S

T

H

Y

S

S

G

G

R

T

H

K

N

N

T

T

G

G

R

I

D

L

P

L

V

R

A

D

W

W

A

V

Q

V

E

E

A

V

E

E

R

K

L

R

G

G

A

A

G

G

E

E

L

I

F

V

L

L

T

G

A

S

I

I

D

D

R

R

E

L

G

G

T

T

W

K

S

S

G

G

F

Y

D

D

I

T

D

E

L

M

V

I

K

R

K

F

V

V

T

R

D

P

A

L

V

T

S

T

I

L

P

P

V

I

I

I

A

A

H

H

G

R

G

G

A

A

G

G

binding magnesium ion: E100 (≠ A101)

Sites not aligning to the query:

binding magnesium ion: 221

4ewnD Structure of hisf-d130v+d176v with bound rcdrp (see paper)
40% identity, 82% coverage: 2:208/253 of query aligns to 1:200/243 of 4ewnD

query
sites
4ewnD

L

L

R

A

T

K

R

R

V

I

I

I

P

A

A

C

L

L

L

D

L

V

Q

K

H

D

E

G

S

R

L

V

V

V

K

K

T

G

Q

T

R

N

F

F

S

E

T

N

F

L

D

R

Y

D

V

S

G

G

D

D

P

P

C

V

N

E

T

L

V

G

R

K

I

F

F

Y

N

S

E

E

L

I

E

G

V

I

D

D

E

E

L

L

F

V

F

F

L

L

D

D

I

I

A

T

A

K

S

T

R

M

E

-

K

-

G

-

P

-

N

-

L

L

Q

E

L

L

L

V

A

E

D

K

I

V

A

A

N

E

E

Q

C

I

F

D

M

I

P

P

L

F

G

T

Y

V

G

G

I

I

R

H

S

D

L

F

D

E

D

T

A

A

R

S

S

E

V

L

F

I

S

L

I

R

G

G

F

A

E

D

K

K

V

V

A

S

V

I

N

N

T

T

H

A

A

A

L

V

E

E

N

N

P

P

S

S

L

L

I

I

S

T

E

Q

I

I

A

A

T

Q

E

T

Y

F

G

G

S

S

Q

Q

A

A

V

V

S

A

V

I

D

-

V
|
V

K

A

G

K

G

R

V

V

L

D

G

G

G

E

Q

F

T

M

V

V

R

F

S

T

H

Y

S

S

G

G

R

K

H

K

N

N

T

T

G

G

R

I

D

L

P

L

V

R

A

D

W

W

A

V

Q

V

E

E

A

V

E

E

R

K

L

R

G

G

A

A

G

G

E

E

L

I

F

L

L

L

T

T

A

S

I

I

D

D

R

R

E

V

G
|
G

T

T

W

K

S

S

G

G

F

Y

D

D

I

T

D

E

L

M

V

I

K

R

K

F

V

V

T

R

D

P

A

L

V

T

S

T

I

L

P

P

V

I

I

I

A

A

H
x
S

G
|
G

A

A

G

G

S

K

L

M

binding 1-(O-carboxy-phenylamino)-1-deoxy-D-ribulose-5-phosphate: V123 (= V131), G170 (= G178), S194 (≠ H202), G195 (= G203), G196 (= G204)

Sites not aligning to the query:

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

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)
30% identity, 99% coverage: 1:251/253 of query aligns to 1:250/258 of P60664

query
sites
P60664

M

M

L

L

R

A

T

K

R
|
R

V

I

I

I

P

P

A

C

L

L

L

D

L

V

Q

R

H

D

E

G

S

Q

L

V

V

V

K

K

T

G

Q

V

R

Q

F

F

S

R

T

N

F

H

D

E

Y

I

V

I

G

G

D

D

P

I

C

V

N

P

T

L

V

A

R

K

I

R

F

Y

N

A

E

E

L

E

E

G

V

A

D

D

E
|
E

L

L

F

V

F

F

L

Y

D

D

I

I

A

T

A

A

S

S

R

S

E

D

K

G

K

R

G

V

P

V

N

D

L

K

Q

S

L

W

L

V

A

S

D

R

I

V

A

A

N

E

E

V

C

I

F

D

M

I

P

P

L

F

G

C

Y

V

G

A

G

G

I

I

R

K

S

S

L

L

D

E

D

D

A

A

R

A

S

K

V

I

F

L

S

S

I

F

G

G

F

A

E

D

K

K

V

I

A

S

V

I

N

N

T

S

H

P

A

A

L

L

E

A

N

D

P

P

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T

L

L

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Q

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x
C

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Y

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G

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E

N

S

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G

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R

-

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-

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-

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W

A

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Q

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A

V

E

Q

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K

L

R

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G

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A

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A

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I

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A

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A

A

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D

A

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D

A

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V

A

A

L

L

A

G

A

S

S

M

-

V

-

V

V

Y

F

Q

H

K

K

Q

Q

G

-

N

-

G

-

I

-

L

I

V

I

H

N

F

I

P

G

E

E

T

L

K

K

E

A

L

Y

E

L

A

A

T

T

R5 (= R5) mutation to A: Loss of activity.; mutation to H: Loss of IGP synthase activity. Weak IGP synthase activity and reduced HisH activity in vitro.
E46 (= E46) mutation to A: Loss of activity.; mutation to G: Loss of IGP synthase activity. Weak IGP synthase and HisH activities in vitro.
Q123 (= Q123) mutation to A: Decrease in activity.; mutation to R: Loss of IGP synthase activity. Weak HisH activity in vitro.
C124 (≠ A124) mutation to A: No change in activity.; mutation to R: Loss of IGP synthase activity. Weak HisH activity in vitro.

P33734 Imidazole glycerol phosphate synthase hisHF; IGP synthase; IGPS; ImGP synthase; EC 4.3.2.10; EC 3.5.1.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
32% identity, 70% coverage: 29:206/253 of query aligns to 276:503/552 of P33734

query
sites
P33734

V

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-

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Y

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G

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K
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K

V

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A

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D

A

A

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V

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Y

-

A

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-

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Y

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D

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P

K

K

G

R

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H

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-

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-

F

-

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-

T

-

E

-

Y

-

P

-

G

-

P

-

N

-

G

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E

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K

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Y

-

C

-

W

-

Y

-

Q

-

C

-

T

-

I

-

K

-

G

G

G

R

R

H

E

N

S

T

-

G

-

R

R

D

D

P

L

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G

A

V

W

W

-

E

-

L

A

T

Q

R

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A

A

C

E

E

R

A

L

L

G

G

A

A

G

G

E

E

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F

L

L

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N

A

C

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I

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D

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K

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D

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N

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Y

D

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I

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L

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D

A

A

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P

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V

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I

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A

H

S

G

S

G

G

A

A

G

G

K360 (= K99) 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.

1ox4B Towards understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerophosphate synthase (see paper)
32% identity, 70% coverage: 29:206/253 of query aligns to 264:491/538 of 1ox4B

query
sites
1ox4B

V

L

G

G

D

K

P

P

C

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A

A

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D

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K

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G

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W

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A

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C

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A

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x
S

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G

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A

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G

active site: D392 (= D130)
binding pyrophosphate 2-: G463 (= G178), S488 (≠ G203)

Sites not aligning to the query:

active site: 248
binding pyrophosphate 2-: 511, 512

1ox5A Towards understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerophosphate synthase (see paper)
32% identity, 70% coverage: 29:206/253 of query aligns to 262:485/532 of 1ox5A

query
sites
1ox5A

V

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S

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D

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x
G

G

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A

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G

G

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x
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C

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x
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G
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G

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N

S

S

G

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Y

D

D

I

L

D

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L

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x
S

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A

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G

active site: D386 (= D130)
binding phosphoric acid mono-[5-({[5-carbamoyl-3-(5-phosphonooxy-5-deoxy-ribofuranosyl)- 3h-imidazol-4-ylamino]-methyl}-amino)-2,3,4-trihydroxy-pentyl] ester: L283 (= L50), I285 (= I52), G313 (= G81), G346 (≠ N103), T347 (= T104), S384 (= S128), D386 (= D130), G424 (vs. gap), N451 (≠ T172), D456 (≠ E177), G457 (= G178), S482 (≠ G203)

Sites not aligning to the query:

3tdmA Computationally designed tim-barrel protein, halfflr (see paper)
47% identity, 34% coverage: 123:208/253 of query aligns to 1:85/120 of 3tdmA

query
sites
3tdmA

Q

Q

A

A

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V

S

A

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I

D

D

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K

K

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N

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x
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G

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G

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M

binding phosphate ion: D54 (≠ E177), G55 (= G178)

Sites not aligning to the query:

binding phosphate ion: 102, 103

5dn1A Crystal structure of phosphoribosyl isomerase a from streptomyces coelicolor (see paper)
27% identity, 85% coverage: 1:214/253 of query aligns to 1:208/240 of 5dn1A

query
sites
5dn1A

M

M

L

S

R

K

T

L

R

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A

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x
D

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R

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G

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x
G

Q

E

R

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F

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F

T

D

S

Y

Y

V

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G

G

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x
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D

N

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x
S

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G

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R

S

D

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D

D

D

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A

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G

T
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T

H

A

A

A

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L

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A

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E

Y

H

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G

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D

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K

A

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I

V

A

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D
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D

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K

R

G

G

G

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T

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L

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G

Q

R

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V

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R

-

S

-

H

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S

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G
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G

R
x
W

H

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N

R

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D

G

G

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G

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D

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A

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R

K

L

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G

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G

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L

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D

A

A

A

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D

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V

I

V

A

A

H

S

G

G

A

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G

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S

S

L

L

S

D

D

D

I

L

R

R

K

A

V

I

active site: D11 (≠ L11), D130 (= D130)
binding aminoimidazole 4-carboxamide ribonucleotide: G23 (≠ T20), L54 (≠ I52), F58 (≠ R56), S81 (≠ G80), G83 (= G82), R85 (= R84), G104 (≠ N103), T105 (= T104), G140 (= G146), W141 (≠ R147)

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)
27% identity, 85% coverage: 1:214/253 of query aligns to 1:208/240 of P16250

query
sites
P16250

M

M

L

S

R

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T

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R

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L

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P

A

A

L

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L
x
D

L

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Q

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A

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x
R

L

L

V

V

K

H

T

G

Q

E

R

S

F

G

S

T

T

E

F

T

D

S

Y

Y

V

-

G

G

D

S

P

P

C

L

N

E

T

A

V

A

R

L

I

A

F

W

N

Q

E

R

L

S

E

G

V

A

D

E

E

W

L

L

F

H

F

L

L

V

D

D

I

L

A

D

A

A

S

A

R

F

E

-

K

G

K

T

G

G

P

D

N

N

L

R

Q

A

L

L

L

I

A

A

D

E

I

V

A

A

N

Q

E

A

C

M

F

D

M

I

P

K

L

V

G

E

Y

L

G
x
S

G

G

I

I

R

R

S

D

L

D

D

D

D

T

A

L

R

A

S

A

V

A

F

L

S

A

I

T

G

G

F

C

E

T

K

R

V

V

A

N

V

L

N

G

T

T

H

A

A

A

L

L

E

E

N

T

P

P

S

E

L

W

I

V

S

A

E

K

I

V

A

I

T

A

E

E

Y

H

G

G

S

D

Q

K

A

-

V

I

V

A

V

V

S

G

V

L

D
|
D

V

V

K

R

G

G

G

T

V

T

L

L

G

R

G

G

Q

R

T

-

V

-

R

-

S

-

H

-

S

-

G

G

R

W

H

T

N

R

T

D

G

G

R

G

D

D

P

L

V

Y

A

E

W

T

A

L

Q

D

E

R

A

L

E

N

R

K

L

E

G

G

A

C

G

A

E

R

L

Y

F

V

L

V

T
|
T

A

D

I

I

D

A

R

K

E
x
D

G

G

T

T

W

L

S

Q

G

G

F

P

D

N

I

L

D

E

L

L

V

L

K

K

K

N

V

V

T

C

D

A

A

A

V

T

S

D

I

R

P

P

V

V

I

V

A

A

H

S

G

G

A

V

G

S

S

S

L

L

S

D

D

D

I

L

R

R

K

A

V

I

D11 (≠ L11) mutation to A: No activity.
R19 (≠ S16) 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 (= T172) mutation to A: No activity.
D171 (≠ E177) mutation to A: Low activity toward PRA. No activity toward ProFAR.

2y85A Crystal structure of mycobacterium tuberculosis phosphoribosyl isomerase with bound rcdrp (see paper)
31% identity, 62% coverage: 59:214/253 of query aligns to 50:202/234 of 2y85A

query
sites
2y85A

K

R

G

G

P

S

N

N

L

H

Q

E

L

L

A

A

D

E

I

V

A

V

N

G

E

K

C

L

F

D

M

V

P

Q

L

V

G

E

Y

L

G
x
S

G

G

I

I

R

R

S

D

L

D

D

E

D

S

A

L

R

A

S

A

V

A

F

L

S

A

I

T

G

G

F

C

E

A

K

R

V

V

A

N

V

V

N

G

T

T

H

A

A

A

L

L

E

E

N

N

P

P

S

Q

L

W

I

C

S

A

E

R

I

V

A

I

T

G

E

E

Y

H

G

G

S

D

Q

Q

A

-

V

V

V

A

V

V

S

G

V

L

D
|
D

V

V

K

Q

G

-

V

I

L

I

G

D

G

G

Q

E

T

H

V

R

R

L

S

R

H

G

S
x
R

G

G

R

W

H

E

N

T

T

D

G

G

R

G

D

D

P

L

V

W

A

D

W

V

A

L

Q

E

E

R

A

L

E

D

R

S

L

E

G

G

A

C

G

S

E

R

L

F

F

V

L

V

T

T

A

D

I

I

D

T

R

K

E
x
D

G
|
G

T

T

W

L

S

G

G

G

F

P

D

N

I

L

D

D

L

L

V

L

K

A

K

G

V

V

T

A

D

D

A

R

V

T

S

D

I

A

P

P

V

V

I

I

A

A

H
x
S

G
|
G

A

V

G

S

S

S

L

L

S

D

D

D

I

L

R

R

K

A

V

I

active site: D120 (= D130)
binding 1-(o-carboxy-phenylamino)-1-deoxy-d-ribulose-5-phosphate: S71 (≠ G80), R133 (≠ S145), D165 (≠ E177), G166 (= G178), S190 (≠ H202), G191 (= G203), G192 (= G204)

Sites not aligning to the query:

active site: 10
binding 1-(o-carboxy-phenylamino)-1-deoxy-d-ribulose-5-phosphate: 10, 40, 42, 44, 47, 216, 217

3zs4A Crystal structure of mycobacterium tuberculosis phosphoribosyl isomerase with bound prfar
31% identity, 62% coverage: 59:214/253 of query aligns to 59:211/244 of 3zs4A

query
sites
3zs4A

K

R

G

G

P

S

N

N

L

H

Q

E

L

L

A

A

D

E

I

V

A

V

N

G

E

K

C

L

F

D

M

V

P

Q

L

V

G

E

Y

L

G
x
S

G

G

G
|
G

I

I

R
|
R

S

D

L

D

D

E

D

S

A

L

R

A

S

A

V

A

F

L

S

A

I

T

G

G

F

C

E

A

K

R

V

V

A

N

V

V

N
x
G

T
|
T

H

A

A

A

L

L

E

E

N

N

P

P

S

Q

L

W

I

C

S

A

E

R

I

V

A

I

T

G

E

E

Y

H

G

G

S

D

Q

Q

A

-

V

V

V

A

V

V

S

G

V

L

D
|
D

V

V

K

Q

G

-

V

I

L

I

G

D

G

G

Q

E

T

H

V

R

R

L

S

R

H

G

S

R

G
|
G

R
x
W

H

E

N

T

T

D

G

G

R

G

D

D

P

L

V

W

A

D

W

V

A

L

Q

E

E

R

A

L

E

D

R

S

L

E

G

G

A

C

G

S

E

R

L

F

F

V

L

V

T

T

A

D

I

I

D

T

R

K

E
x
D

G
|
G

T

T

W

L

S

G

G

G

F

P

D

N

I

L

D

D

L

L

V

L

K

A

K

G

V

V

T

A

D

D

A

R

V

T

S

D

I

A

P

P

V

V

I

I

A

A

H

S

G
|
G

A

V

G

S

S

S

L

L

S

D

D

D

I

L

R

R

K

A

V

I

active site: 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: S80 (≠ G80), G82 (= G82), R84 (= R84), G103 (≠ N103), T104 (= T104), D129 (= D130), G143 (= G146), W144 (≠ R147), D174 (≠ E177), G175 (= G178), G200 (= G203), G201 (= G204)

Sites not aligning to the query:

Query Sequence

>HSERO_RS21020 FitnessBrowser__HerbieS:HSERO_RS21020
MLRTRVIPALLLQHESLVKTQRFSTFDYVGDPCNTVRIFNELEVDELFFLDIAASREKKG
PNLQLLADIANECFMPLGYGGGIRSLDDARSVFSIGFEKVAVNTHALENPSLISEIATEY
GSQAVVVSVDVKGGVLGGQTVRSHSGRHNTGRDPVAWAQEAERLGAGELFLTAIDREGTW
SGFDIDLVKKVTDAVSIPVIAHGGAGSLSDIRKVVKQAGASAVALGSMVVYQKQGNGILV
HFPETKELEATLA

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