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)
34% identity, 12% coverage: 267:356/729 of query aligns to 169:257/443 of 4lnkA

query
sites
4lnkA

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active site: E188 (= E286), E195 (= E293), H244 (= H342)
binding adenosine-5'-diphosphate: F198 (≠ P296), Y200 (≠ F298), N246 (= N344), S248 (= S346)
binding glutamic acid: E188 (= E286), V189 (= V287), N239 (= N337), G240 (= G338), G242 (= G340)
binding magnesium ion: E188 (= E286), E195 (= E293), H244 (= H342)

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: 267:356/729 of query aligns to 169:257/443 of 4lniA

query
sites
4lniA

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active site: E188 (= E286), E195 (= E293), H244 (= H342)
binding adenosine-5'-diphosphate: E183 (≠ K281), D197 (≠ A295), Y200 (≠ F298), N246 (= N344), S248 (= S346)
binding magnesium ion: E188 (= E286), E195 (= E293), E195 (= E293), H244 (= H342)
binding l-methionine-s-sulfoximine phosphate: E188 (= E286), H244 (= H342)

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

4s0rD Structure of gs-tnra complex (see paper)
34% identity, 12% coverage: 267:356/729 of query aligns to 173:261/447 of 4s0rD

query
sites
4s0rD

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active site: E192 (= E286), E199 (= E293), H248 (= H342)
binding glutamine: E192 (= E286)
binding magnesium ion: E199 (= E293), H248 (= H342), H248 (= H342)
binding : G241 (≠ S335), V242 (= V336), N243 (= N337)

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

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)
34% identity, 12% coverage: 267:356/729 of query aligns to 170:258/444 of P12425

query
sites
P12425

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E189 (= E286) binding
V190 (= V287) 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 (= E293) binding
G241 (= G338) binding
H245 (= H342) 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.

3ng0A Crystal structure of glutamine synthetase from synechocystis sp. Pcc 6803
29% identity, 26% coverage: 212:398/729 of query aligns to 127:321/465 of 3ng0A

query
sites
3ng0A

L

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active site: E130 (= E215), E132 (= E217), E213 (= E286), E221 (= E293), H270 (= H342)
binding phosphoaminophosphonic acid-adenylate ester: E130 (= E215), K209 (≠ T282), I224 (≠ P296), F226 (= F298), H272 (≠ N344), S274 (= S346)
binding manganese (ii) ion: E130 (= E215), E132 (= E217), E213 (= E286), E221 (= E293), H270 (= H342)

Sites not aligning to the query:

active site: 51, 340, 359, 361
binding phosphoaminophosphonic acid-adenylate ester: 126, 340, 345, 357
binding manganese (ii) ion: 359, 361

8tfkA Glutamine synthetase (see paper)
29% identity, 21% coverage: 211:362/729 of query aligns to 124:260/440 of 8tfkA

query
sites
8tfkA

N

N

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binding adenosine-5'-diphosphate: E128 (= E215), D194 (≠ A295), F195 (≠ P296), F197 (= F298), N243 (= N344)
binding magnesium ion: E128 (= E215), E128 (= E215), E130 (= E217), E185 (= E286), E192 (= E293), E192 (= E293), H241 (= H342)
binding l-methionine-s-sulfoximine phosphate: E128 (= E215), E130 (= E217), E185 (= E286), E192 (= E293), G237 (= G338), H241 (= H342)

Sites not aligning to the query:

P77961 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Synechocystis sp. (strain PCC 6803 / Kazusa)
28% identity, 26% coverage: 212:398/729 of query aligns to 129:323/473 of P77961

query
sites
P77961

L

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E134 (= E217) binding
E215 (= E286) binding
E223 (= E293) binding

Sites not aligning to the query:

361 binding

8ufjB Glutamine synthetase (see paper)
30% identity, 13% coverage: 267:362/729 of query aligns to 170:264/444 of 8ufjB

query
sites
8ufjB

K

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N

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H
|
H

N

S

N

N

W

Q

S

S

L

L

C

F

T

K

D

D

T

-

G

G

I

K

N

N

L

V

F

F

A

Y

P

D

G

P

K

D

N

T

P

P

binding magnesium ion: E189 (= E286), E196 (= E293), H245 (= H342)

Sites not aligning to the query:

binding magnesium ion: 132, 134, 333

Query Sequence

>353865 FitnessBrowser__Btheta:353865
MSKMRFYALQELSNRKPLEVTAPSNKLSDYYGSHVFDRKKMQEYLPKEAYKAVTDAIEKG
TPISREIADLIANGMKSWAKSLNVTHYTHWFQPLTDGTAEKHDGFIEFGEDGGVIERFSG
KLLIQQEPDASSFPNGGIRNTFEARGYTAWDVSSPAFVVDTTLCIPTIFISYTGEALDYK
TPLLKALAAVDKAATEVCQLFDKNVTRVFTNLGWEQEYFLVDSSLYNARPDLCLTGRTLM
GHSSAKDQQLEDHYFGSIPPRVTAFMKELEIECHKLGIPAKTRHNEVAPNQFELAPIFEN
CNLANDHNQLVMDLMKRIARKHHFNVLLHEKPYSSVNGSGKHNNWSLCTDTGINLFAPGK
NPKGNMLFLTFLVNVLMMVYKNQDLLRASIMSASNSYRLGANEAPPAILSCFLGSQLSAT
LDEIVRQVGNEKMTPEEKTTLKLGIGRIPEILLDTTDRNRTSPFAFTGNRFEFRAAGSSS
NCAAAMIAINAAMANQLNEFRASVEKLMEEGVGKDEAIFRLLKETIIASEAIRFEGDGYS
EEWRQEAARRGLTNICHVPEALMHYVDNQSKSVLIGERIFNETELNSRLEVELEKYTMKV
QIEGRVLGDLAINHIVPTAVTYQNRLLENLCKMKEIFSPEEYEVLSADRKELIREISHRV
TSIKVLVREMTEARKVANHKDNYKERAFEYEEKVRPYLDKIRDHIDHLEMEVDDEIWPLP
KYRELLFTK

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