SitesBLAST

E189 (= E273) binding Mg(2+)
V190 (= V274) mutation to A: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant partially relieves expression of the glnRA-lacZ fusion, but has no effect on the TnrA-dependent regulation of amtB-lacZ fusion. Resistant to inhibition by MetSox.
E196 (= E280) binding Mg(2+)
G241 (= G325) binding L-glutamate
H245 (= H329) binding Mg(2+)

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
59 G→R: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion.
62 Important for inhibition by glutamine; R→A: Highly resistant to inhibition by glutamine and AMP. Regulation by TnrA and GlnR is abolished. Only small differences (less than 2-fold) in its steady-state kinetic constants compared with the wild-type. Similar sensitivity to Met-Sox that compared to the wild-ytpe.
132 binding Mg(2+)
134 binding Mg(2+)
302 G→E: Unable to form stable complex with TnrA. In the presence of glutamine, amtB-lacZ fusion is only 4-fold regulated by TnrA, whereas glnRA-lacZ fusion is derepressed. This mutant retains enzymatic specific activity with a 2-fold decrease of the affinity for glutamate and glutamine compared to the wild-type. Slightly less sensitive to inhibition by glutamine.
304 E→A: Highly resistant to Met-Sox inhibition. 8- and 2-fold increase of the affinity for glutamate and ATP, respectively. Strong decrease of the affinity for ammonium.
306 P→H: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant completely derepresses glnRA-lacZ fusion, whereas amtB-lacZ fusion expression is only partially derepresses.
333 binding Mg(2+)
424 E→K: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion. Although it is defective in regulation, this mutant retains enzymatic specific activity and similar affinity for ATP, glutamate and glutamine compared to the wild-type. Slightly less sensitive to inhibition by glutamine.

4lnkA B. Subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of gs-glutamate-amppcp complex (see paper)
34% identity, 12% coverage: 254:341/714 of query aligns to 169:255/443 of 4lnkA

query
sites
4lnkA

Q

R

D

D

V

I

E

V

H

L

E

E

L

L

Y

E

L

E

L

M

G

G

I

F

P

E

A

I

K

E

T

A

R

S

H

H

N

H

E
|
E

V
|
V

A

A

P

P

H

G

Q

Q

F

H

E
|
E

I

I

A

D

P
x
F

I

K

F
x
Y

E

A

E

G

A

A

N

V

I

R

A

S

V

C

D

D

H

D

N

I

L

Q

L

T

V

F

M

K

E

L

V

V

M

V

R

K

K

T

V

I

A

A

D

R

K

K

K

H

G

G

F

L

A

H

L

A

L

T

L

F

T

M

E

P

K

K

P

P

F

L

A

F

G

G

I

V

N
|
N

G
|
G

S

S

G
|
G

K

M

H
|
H

N

C

N
|
N

W

L

S
|
S

I

L

G

F

T

K

D

N

T

-

G

G

I

V

N

N

active site: E188 (= E273), E195 (= E280), H244 (= H329)
binding adenosine-5'-diphosphate: F198 (≠ P283), Y200 (≠ F285), N246 (= N331), S248 (= S333)
binding glutamic acid: E188 (= E273), V189 (= V274), N239 (= N324), G240 (= G325), G242 (= G327)
binding magnesium ion: E188 (= E273), E195 (= E280), H244 (= H329)

Sites not aligning to the query:

active site: 52, 131, 133, 315, 332, 334
binding adenosine-5'-diphosphate: 43, 50, 324, 328, 330
binding glutamic acid: 133, 303
binding magnesium ion: 131, 332

4lniA B. Subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of the transition state complex (see paper)
34% identity, 12% coverage: 254:341/714 of query aligns to 169:255/443 of 4lniA

query
sites
4lniA

Q

R

D

D

V

I

E

V

H

L

E

E

L

L

Y

E

L

E

L

M

G

G

I

F

P

E

A

I

K
x
E

T

A

R

S

H

H

N

H

E
|
E

V

V

A

A

P

P

H

G

Q

Q

F

H

E
|
E

I

I

A
x
D

P

F

I

K

F
x
Y

E

A

E

G

A

A

N

V

I

R

A

S

V

C

D

D

H

D

N

I

L

Q

L

T

V

F

M

K

E

L

V

V

M

V

R

K

K

T

V

I

A

A

D

R

K

K

K

H

G

G

F

L

A

H

L

A

L

T

L

F

T

M

E

P

K

K

P

P

F

L

A

F

G

G

I

V

N

N

G

G

S

S

G

G

K

M

H
|
H

N

C

N
|
N

W

L

S
|
S

I

L

G

F

T

K

D

N

T

-

G

G

I

V

N

N

active site: E188 (= E273), E195 (= E280), H244 (= H329)
binding adenosine-5'-diphosphate: E183 (≠ K268), D197 (≠ A282), Y200 (≠ F285), N246 (= N331), S248 (= S333)
binding magnesium ion: E188 (= E273), E195 (= E280), E195 (= E280), H244 (= H329)
binding l-methionine-s-sulfoximine phosphate: E188 (= E273), H244 (= H329)

Sites not aligning to the query:

active site: 52, 131, 133, 315, 332, 334
binding adenosine-5'-diphosphate: 131, 320, 330
binding magnesium ion: 131, 131, 133, 332
binding l-methionine-s-sulfoximine phosphate: 133, 297, 303, 315, 334

Query Sequence

>WP_150081556.1 NCBI__GCF_000020465.1:WP_150081556.1
MNMESKVPVSSYFGAMTFDQKAMRARLPKDEFKALQDTIRAGKKITGEIAGVVAHGMKEW
AMEQGATHYTHWFQPMTGSTAEKHDAFLSIDRDGTPIERFSGEQLIQGEPDASSFPSGGM
RTTFEARGYTAWDPSSPAFLMKGGTGLTLCIPTVFISYHGEALDSKTPLLRSMDAVSNSA
IRLLNVLGTTGISRVKTFAGCEQEYFLIDKKFYSERPDLIMCGRTLLGALPPKGQQLEDH
YFGSIPDRVLEFMQDVEHELYLLGIPAKTRHNEVAPHQFEIAPIFEEANIAVDHNLLVME
VMRKVADKKGFALLLTEKPFAGINGSGKHNNWSIGTDTGINLLDPGDTPTENINFLVFLV
AVLKGVYKRADVLRMSIASTGNDHRLGANEAPPAVVTVFLGEQLETVLDAIESGKVDLKT
EKQVLNLGLSQVPLLNKDYTDRNRTSPFAFTGNKFEFRAVGSSQAASVPNMVLNTLMAEA
LDELTDAIEAKIAAGKDRDSAVLEAIREGITATKDIRYPGDNYSEALQQAAKERGLPNLK
NTPQALRTLEKSDVKAMFVKYGVLTEQEIESRLNIRLERYVKGIDIEARTLQLMLKTLVI
PDVSEYQGDIGNSFNNLLAASEAIGLSEGAIASQANHFKNLAENLSSLIDLTAELDEAVE
KIETIEGEFGKADFCADELLPLMNAVRAVADRLELMVDRSRWQLPTYSEMLFEH

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