SitesBLAST

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)
34% identity, 96% coverage: 6:208/212 of query aligns to 6:209/552 of P33734

query
sites
P33734

V

V

V

I

D

D

Y

V

G

E

M

S

G

G

N

N

L

L

R

Q

S

S

V

L

A

T

Q

N

A

A

L

I

R

E

H

H

V

L

A

G

P

Y

E

E

A

V

D

Q

V

L

R

V

I

K

S

S

G

P

E

K

V

D

A

F

D

N

I

I

R

S

A

G

A

T

D

S

R

R

V

L

V

I

L

L

P

P

G

G

Q

V

G

G

A

N

M

Y

P

G

D

H

C

F

M

V

R

D

S

N

L

L

R

F

E

N

S

R

G

G

V

F

Q

E

D

K

A

P

V

I

I

R

E

E

A

Y

S

I

R

E

T

S

-

G

K

K

P

P

L

I

F

M

G

G

V

I

C

C

V

V

G

G

E

L

Q

Q

M

A

L

L

F

F

D

A

W

G

S

S

-

V

E

E

E

S

G

P

D

K

T

S

P

T

G

G

L

L

G

N

L

Y

L

I

P

D

G

F

K

K

V

L

V

S

R

R

F

F

D

D

L

-

E

-

G

-

M

-

R

-

Q

-

D

-

G

D

S

S

L

E

F

K

K

P

V

V

P

P

Q

E

M

I

G

G

W

W

N

N

H

S

V

C

H

I

Q

P

T

S

S

E

R

N

H

-

P

-

L

L

W

F

E

F

G

G

I

L

A

D

D

P

N

Y

A

K

F

R

F

Y

Y

Y

F

F

V

V

H

H

S

S

Y

F

Y

A

A

A

V

I

P

L

A

N

E

S

S

E

A

K

H

K

V

K

-

N

-

L

-

E

-

N

-

D

-

G

-

W

-

K

V

I

G

A

Q

K

T

A

P

K

Y

Y

G

G

-

S

R

E

D

E

F

F

A

I

C

A

A

A

V

V

A

N

R

K

D

N

N

N

I

I

F

F

A

A

T

T

Q

Q

F

F

H

H

P

P

E

E

K

K

S

S

A

G

S

K

A

A

G

G

L

L

Q

N

L

V

Y

I

R

E

N

N

F

F

V

L

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.
360 mutation K->A,R: Almost no effect on activity.

1ox5A Towards understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerophosphate synthase (see paper)
34% identity, 96% coverage: 6:208/212 of query aligns to 9:212/532 of 1ox5A

query
sites
1ox5A

V

V

V

I

D

D

Y

V

G

E

M

S

G

G

N

N

L

L

R

Q

S

S

V

L

A

T

Q

N

A

A

L

I

R

E

H

H

V

L

A

G

P

Y

E

E

A

V

D

Q

V

L

R

V

I

K

S

S

G

P

E

K

V

D

A

F

D

N

I

I

R

S

A

G

A

T

D

S

R

R

V

L

V

I

L

L

P

P

G

G

Q

V

G

G

A

N

M

Y

P

G

D

H

C

F

M

V

R

D

S

N

L

L

R

F

E

N

S

R

G

G

V

F

Q

E

D

K

A

P

V

I

I

R

E

E

A

Y

S

I

R

E

T

S

-

G

K

K

P

P

L

I

F

M

G

G

V

I

C

C

V

V

G

G

E

L

Q

Q

M

A

L

L

F

F

D

A

W

G

S

S

-

V

E

E

E

S

G

P

D

K

T

S

P

T

G

G

L

L

G

N

L

Y

L

I

P

D

G

F

K

K

V

L

V

S

R

R

F

F

D

D

L

-

E

-

G

-

M

-

R

-

Q

-

D

-

G

D

S

S

L

E

F

K

K

P

V

V

P

P

Q

E

M

I

G

G

W

W

N

N

H

S

V

C

H

I

Q

P

T

S

S

E

R

N

H

-

P

-

L

L

W

F

E

F

G

G

I

L

A

D

D

P

N

Y

A

K

F

R

F

Y

Y

Y

F

F

V

V

H

H

S

S

Y

F

Y

A

A

A

V

I

P

L

A

N

E

S

S

E

A

K

H

K

V

K

-

N

-

L

-

E

-

N

-

D

-

G

-

W

-

K

V

I

G

A

Q

K

T

A

P

K

Y

Y

G

G

-

S

R

E

D

E

F

F

A

I

C

A

A

A

V

V

A

N

R

K

D

N

N

N

I

I

F

F

A

A

T

T

Q

Q

F

F

H

H

P

P

E

E

K

K

S

S

A

G

S

K

A

A

G

G

L

L

Q

N

L

V

Y

I

R

E

N

N

F

F

V

L

Sites not aligning to the query:

active site: 248, 386
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: 283, 285, 313, 346, 347, 384, 386, 424, 451, 456, 457, 482, 505, 506

7ac8B Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex. (see paper)
33% identity, 97% coverage: 3:208/212 of query aligns to 4:196/202 of 7ac8B

query
sites
7ac8B

K

R

I

I

V

G

V

I

D

S

Y

V

G

G

M

P

G

G

N

N

L

I

R

M

S

N

V

L

A

Y

Q

R

A

G

L

V

R

K

H

R

V

A

A

S

P

E

E

N

-

F

A

E

D

D

V

V

R

S

I

I

S

E

-

L

G

V

E

E

V

S

A

P

D

R

I

N

R

D

A

L

A

Y

D

D

R

L

V

L

V

F

L

I

P

P

G

G

Q

V

G
|
G

A

H

M

F

P

G

D

E

C

G

M

M

R

R

S

R

L

L

R

R

E

E

S

N

G

D

V

L

Q

I

D

D

A

F

V

V

-

R

-

K

-

H

I

V

E

E

A

D

S

E

R

R

T

Y

K

-

P

-

L

V

F

V

G

G

V

V

C

A

V

L

G

G

E

M

Q
|
Q

M

L

L

L

F

F

D

E

W

E

S

S

E

E

E
|
E

G

A

-

P

D

G

T

V

P

K

G

G

L

L

G

S

L

L

L

I

P

E

G

G

K

N

V

V

R

K

F

L

D

R

L

S

E

R

G

-

M

-

R

-

Q

-

D

-

G

-

S

-

L

-

F

-

K

R

V

L

P

P

Q

H

M

M

G

G

W

W

N

N

H

E

V

V

H

-

Q

-

T

-

S

-

R

-

H

-

P

-

L

I

W

F

E

K

G

D

I

T

A

F

D

P

N

N

A

G

F

Y

Y

Y

F

F

V
|
V

H
|
H

S
x
T

Y
|
Y

Y

R

A

A

V

V

P

-

A

C

E

E

S

E

A

E

H

H

V

V

V

L

G

G

Q

T

T

T

P

E

Y

Y

-

D

G

G

R

E

D

I

F

F

A

P

C

S

A

A

V

V

A

R

R

K

D

G

N

R

I

I

F

L

A

G

T

F

Q

Q

F

F

H

H

P

P

E

E

K

K

S

S

A

S

S

K

A

I

G

G

L

R

Q

K

L

L

Y

L

R

E

N

K

F

V

V

I

binding glutamine: G54 (= G51), Q90 (= Q86), E98 (= E94), V142 (= V154), H143 (= H155), T144 (≠ S156), Y145 (= Y157)

Query Sequence

>HSERO_RS20325 FitnessBrowser__HerbieS:HSERO_RS20325
MNKIVVVDYGMGNLRSVAQALRHVAPEADVRISGEVADIRAADRVVLPGQGAMPDCMRSL
RESGVQDAVIEASRTKPLFGVCVGEQMLFDWSEEGDTPGLGLLPGKVVRFDLEGMRQDDG
SLFKVPQMGWNHVHQTSRHPLWEGIADNAFFYFVHSYYAVPAESAHVVGQTPYGRDFACA
VARDNIFATQFHPEKSASAGLQLYRNFVHWKP

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