SitesBLAST

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)
33% identity, 10% coverage: 278:353/724 of query aligns to 177:252/443 of 4lnkA

query
sites
4lnkA

K

E

L

M

G

G

I

F

P

E

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I

K

E

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A

R

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E

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V

A

A

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Q

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E

C

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A

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x
F

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Y
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Y

E

A

E

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A

N

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R

A

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D

D

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D

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I

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Q

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D

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K

K

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A

A

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R

R

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A

L

T

L

F

H

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K

K

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P

Y

L

A

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G

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N
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N

G
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G

S

S

G
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G

K

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H
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H

N

C

N
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N

W

L

S
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S

L

L

I

F

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K

D

N

active site: E188 (= E289), E195 (= E296), H244 (= H345)
binding adenosine-5'-diphosphate: F198 (≠ P299), Y200 (= Y301), N246 (= N347), S248 (= S349)
binding glutamic acid: E188 (= E289), V189 (= V290), N239 (= N340), G240 (= G341), G242 (= G343)
binding magnesium ion: E188 (= E289), E195 (= E296), H244 (= H345)

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)
33% identity, 10% coverage: 278:353/724 of query aligns to 177:252/443 of 4lniA

query
sites
4lniA

K

E

L

M

G

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K
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E

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A

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L

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L

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K

K

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Y

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A

F

G

G

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V

N

N

G

G

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S

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G

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M

H
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H

N

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N
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N

W

L

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S

L

L

I

F

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K

D

N

active site: E188 (= E289), E195 (= E296), H244 (= H345)
binding adenosine-5'-diphosphate: E183 (≠ K284), D197 (≠ A298), Y200 (= Y301), N246 (= N347), S248 (= S349)
binding magnesium ion: E188 (= E289), E195 (= E296), E195 (= E296), H244 (= H345)
binding l-methionine-s-sulfoximine phosphate: E188 (= E289), H244 (= H345)

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

P12425 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I alpha; GSI alpha; EC 6.3.1.2 from Bacillus subtilis (strain 168) (see 5 papers)
33% identity, 10% coverage: 278:353/724 of query aligns to 178:253/444 of P12425

query
sites
P12425

K

E

L

M

G

G

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F

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K

E

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A

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A

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E

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Y

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D

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K

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R

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L

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L

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Y

L

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F

G

G

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V

N

N

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G

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H

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N

E189 (= E289) binding
V190 (= V290) 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 (= E296) binding
G241 (= G341) binding
H245 (= H345) binding

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
134 binding
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
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.

4s0rD Structure of gs-tnra complex (see paper)
33% identity, 10% coverage: 278:353/724 of query aligns to 181:256/447 of 4s0rD

query
sites
4s0rD

K

E

L

M

G

G

I

F

P

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K

E

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A

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A

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E

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Y

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G

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H

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N

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N

active site: E192 (= E289), E199 (= E296), H248 (= H345)
binding glutamine: E192 (= E289)
binding magnesium ion: E199 (= E296), H248 (= H345), H248 (= H345)
binding : G241 (= G338), V242 (≠ I339), N243 (= N340)

Sites not aligning to the query:

active site: 56, 135, 137, 319, 336, 338
binding glutamine: 137, 301, 307
binding magnesium ion: 66, 135, 135, 336, 419
binding : 63, 64, 65, 66, 161, 305, 306, 376, 426, 430

Query Sequence

>CA265_RS05180 FitnessBrowser__Pedo557:CA265_RS05180
MKSLRTIALKEAQNRISPEVKSPSAKISDFFGANVFDKRKMRDFLSKDVYEKLISSINQG
ELINAEDANQIATAMKSWAMAAGATHYTHWFQPLTGTTAEKHDSFFEPSGEGAIEKFAGS
ALVQQEPDASSFPNGGIRNTFEARGYTAWDPSSPAFIMESKAGKTLCIPTVFVSYTGEAL
DYKAPLLKALASLDKAAVDVCQYFDKSITKVNASLGIEQEYFLVDESLFNARPDLLLTGR
ALFGHMSAKGQQLEDHYFGSIPERVFSYMVDFENEALKLGIPLKTRHNEVAPSQFECAPI
YEEINLAIDHNQLLMDLMEKVARRHHFRVLLHEKPYAGINGSGKHNNWSLITDTGKNLLA
PGKTPKNNLMFLAFFVNTIKAVSEHADLLRASIASVSNDHRLGANEAPPAIISIFLGSQL
NDVLDEIEHSRISKKIKEDNALWLGIPKIPQILLDNTDRNRTSPFAFTGNKFELRAVGSS
ANSSAPMTILNAIMAEQLVKFKVEVDKLIKKGDKKDIALLTVIKKYIKESKNIRFEGNGY
SQEWEDEAATRGLSNIKTTPKALDAYLTEKSAELFASTGIYSAREIHARHEIMLENFYKK
LQIEARVMGEVANTAIIPAAIAYQNSLIENVKGLKELGVDSKSSLDIVKKLSEHLDIVKT
NIDAMLEERKLTNKIEDTREKAIAYDEKVKSYFDTIRYHADKLEQIVDDSVWPLPKFREL
LFMK

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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