SitesBLAST

H30 (= H28) mutation to A: 4,5-fold decrease in glutamine affinity.
D34 (= D32) mutation D->N,E: Little effect on the kinetic properties.
H81 (≠ F82) mutation to A: 5-fold decrease in glutamine affinity.
A105 (= A107) mutation to H: Little effect on the kinetic properties.
E349 (≠ D365) mutation E->A,Q: Loss of glutamine- and ammonia-dependent synthetase activity, but still exhibits glutaminase activity.; mutation to D: 5-fold increase in affinity for aspartate when assaying both the glutamine- and ammonia-dependent synthetase reactions, and 2-fold decrease in kcat for these reactions. Modifies the product glutamate/asparagine stoichiometry.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 mutation C->A,S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity.

P78753 Probable asparagine synthetase [glutamine-hydrolyzing]; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
31% identity, 61% coverage: 1:377/616 of query aligns to 1:368/557 of P78753

query
sites
P78753

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Sites not aligning to the query:

391 modified: Phosphoserine
489 modified: Phosphoserine

6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
27% identity, 57% coverage: 28:379/616 of query aligns to 25:366/509 of 6gq3A

query
sites
6gq3A

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active site: L49 (= L51), N74 (= N76), G75 (= G77), T324 (≠ P338), R327 (≠ D341)
binding 5-oxo-l-norleucine: R48 (= R50), V51 (≠ I53), V52 (≠ I54), Y73 (≠ F75), N74 (= N76), G75 (= G77), E76 (= E78), V95 (≠ S100), D96 (= D101)

Sites not aligning to the query:

active site: 4
binding 5-oxo-l-norleucine: 1

P08243 Asparagine synthetase [glutamine-hydrolyzing]; Cell cycle control protein TS11; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Homo sapiens (Human) (see 7 papers)
26% identity, 62% coverage: 1:379/616 of query aligns to 1:379/561 of P08243

query
sites
P08243

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C2 (= C2) active site, For GATase activity; mutation to A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected.
A6 (≠ G6) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
V210 (≠ L211) to E: in dbSNP:rs1049674
F362 (≠ L362) to V: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122973

Sites not aligning to the query:

550 R → C: in ASNSD; increases level of protein abundance; dbSNP:rs398122974

1mb9A Beta-lactam synthetase complexed with atp (see paper)
28% identity, 51% coverage: 72:383/616 of query aligns to 66:354/485 of 1mb9A

query
sites
1mb9A

S

T

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A

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x
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L

A

R

A

L

Y

L

A

E

Q

R

W

Y

G

D

I

L

G

H

C

A

L

F

T

R

R

L

L

V

N

N

G

G

M

R

F

F

A

A

F

T

A

V

I

V

F

R

D

T

A

G

R

-

A

-

N

D

K

R

V

V

Y

L

F

L

A

A

R

T

D

D

R

H

A

A

G

G

E

S

K

V

P

P

L

L

F

Y

Y

T

H

C

A

V

A

A

N

P

G

G

T

E

I

V

H

R

F

A

A

S

S

T

E

E

L

A

K

K

T

A

L

L

L

A

A

A

D

F

P

P

T

L

L

A

P

-

R

-

V

-

I

-

D

-

P

-

A

-

L

-

D

D

G

A

Y

R

L

R

L

V

T

A

G

G

Y

-

V

-

P

-

G

-

D

-

G

-

C

-

I

-

L

L

A

T

G

G

Y

V

R

Y

K

Q

L

V

P

P

P

A

G

G

H

A

A

V

M

M

E

D

L

I

D

D

L

L

S

G

S

S

G

G

A

T

H

A

R

V

V

T

W

H

R

R

Y

T

W

W

N

T

L

-

P

P

D

G

Y

L

A

S

P

R

V

R

E

I

D

L

D

P

D

E

A

G

G

E

L

A

L

V

G

A

E

A

L

V

E

R

A

A

L

A

L

L

E

E

D

K

A

A

V

V

G

A

R

Q

Q

R

L

V

V

T

-

P

A

G

D

D

V

T

P

P

V

L

G

-

V

V

L
x
V

L
|
L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

S

S

L

G

I

V

T

A

A

A

M

C

A

A

V

H

R

R

N

A

A

A

A

G

K

E

V

L

R

D

T

T

F

V

T
x
S

I
x
M

G

G

F

T

A

D

G

T

A

S

G

-

P

-

L

-

N

N

E

E

I

F

E

R

H

E

A

A

R

R

L

A

I

V

A

V

D

D

H

H

F

L

G

R

T

T

E

R

Q

H

V

R

E

E

L

I

M

T

A

I

E

P

P

T

T

T

V

-

A

-

E

E

L

L

P

A

R

Q

L

L

-

P

-

Y

-

A

-

V

-

W

A

A

A

S

Q

E

F

S

D

V

E

D

P

P

M
x
D

A

I

D

I

S

E

S
x
Y

M

L

F

L

P

P

T
x
L

F

T

M

A

V

L

S

Y

E

R

L

A

V

L

R

D

Q

G

H

P

C

E

T

R

V

R

A

I

L

L

G

T

G
|
G

D
x
Y

G

G

G

A

D
|
D

E

I

L

P

F

L

G

G

Y

M

G

H

H

R

Y

E

S

D

Q

R

L

L

L

P

A

A

L

L

active site: A70 (≠ N76), G71 (= G77), D310 (≠ M339), Y336 (≠ D365)
binding adenosine monophosphate: V235 (≠ L264), L236 (= L265), S242 (= S271), S260 (≠ T289), M261 (≠ I290), Y314 (≠ S343), L318 (≠ T347), G335 (= G364), Y336 (≠ D365)
binding adenosine-5'-triphosphate: V235 (≠ L264), L236 (= L265), S237 (= S266), G239 (= G268), D241 (= D270), S242 (= S271), S260 (≠ T289), M261 (≠ I290), L318 (≠ T347), G335 (= G364), D339 (= D368)
binding magnesium ion: D241 (= D270), D339 (= D368)
binding pyrophosphate 2-: S237 (= S266), G239 (= G268), D241 (= D270), S242 (= S271), D339 (= D368)

Sites not aligning to the query:

active site: 370, 431
binding adenosine-5'-triphosphate: 411, 431
binding pyrophosphate 2-: 411, 431

1jgtB Crystal structure of beta-lactam synthetase (see paper)
28% identity, 51% coverage: 72:383/616 of query aligns to 69:363/500 of 1jgtB

query
sites
1jgtB

S

T

V

A

V

V

F

L

N
x
A

G
|
G

E

E

I

I

Y

Y

N

N

F

R

R

D

D

E

L

L

R

-

A

-

E

-

L

L

E

S

G

V

L

L

G

P

H

A

V

G

F

P

R

A

S

P

H

E

S

G

D

D

T

A

E

E

V

L

L

V

L

L

A

R

A

L

Y

L

A

E

Q

R

W

Y

G

D

I

L

G

H

C

A

L

F

T

R

R

L

L

V

N

N

G

G

M

R

F

F

A

A

F

T

A

V

I

V

F

R

D

T

A

G

R

-

A

-

N

D

K

R

V

V

Y

L

F

L

A

A

R

T

D

D

R

H

A

A

G

G

E

S

K

V

P

P

L

L

F

Y

Y

T

H

C

A

V

A

A

N

P

G

G

T

E

I

V

H

R

F

A

A

S

S

T

E

E

L

A

K

K

T

A

L

L

L

A

A

A

-

H

-

R

D

D

P

P

T

K

L

G

P

F

R

P

V

L

I

A

D

D

P

A

A

R

L

V

D

A

G

G

Y

-

L

-

T

-

G

-

Y

-

V

-

P

-

G

-

D

-

G

-

C

-

I

-

L

L

A

T

G

G

Y

V

R

Y

K

Q

L

V

P

P

P

A

G

G

H

A

A

V

M

M

E

D

L

I

D

D

L

L

S

G

S

S

G

G

A

T

H

A

R

V

V

T

W

H

R

R

Y

T

W

W

N

T

L

-

P

P

D

G

Y

L

A

S

P

R

V

R

E

I

D

L

D

P

D

E

A

G

G

E

L

A

L

V

G

A

E

A

L

V

E

R

A

A

L

A

L

L

E

E

D

K

A

A

V

V

G

A

R

Q

Q

R

L

V

V

T

-

P

A

G

D

D

V

T

P

P

V

L

G

-

V

V

L
x
V

L
|
L

S
|
S

G

G

G
|
G

V
x
I

D
|
D

S
|
S

S

S

L

G

I

V

T

A

A

A

M

C

A

A

V

H

R

R

N

A

A

A

A

G

K

E

V

L

R

D

T

T

F

V

T
x
S

I
x
M

G

G

F

T

A

D

G

T

A

S

G

-

P

-

L

-

N

N

E

E

I

F

E

R

H

E

A

A

R

R

L

A

I

V

A

V

D

D

H

H

F

L

G

R

T

T

E

R

Q

H

V

R

E

E

L

I

M

T

A

I

E

P

P

T

T

T

V

-

A

-

E

E

L

L

P

A

R

Q

L

L

-

P

-

Y

-

A

-

V

-

W

A

A

A

S

Q

E

F

S

D

V

E

D

P

P

M
x
D

A

I

D

I

S

E

S
x
Y

M

L

F

L

P

P

T
x
L

F

T

M

A

V

L

S

Y

E

R

L

A

V

L

R

D

Q

G

H

P

C

E

T

R

V

R

A

I

L

L

G

T

G
|
G

D
x
Y

G
|
G

G

A

D
|
D

E
x
I

L

P

F

L

G

G

Y
x
M

G

H

H

R

Y

E

S

D

Q

R

L

L

L

P

A

A

L

L

active site: A73 (≠ N76), G74 (= G77), D319 (≠ M339), Y345 (≠ D365)
binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L264), L245 (= L265), S246 (= S266), G248 (= G268), I249 (≠ V269), D250 (= D270), S251 (= S271), S269 (≠ T289), M270 (≠ I290), L327 (≠ T347), G344 (= G364), Y345 (≠ D365), D348 (= D368)
binding n2-(carboxyethyl)-l-arginine: Y323 (≠ S343), Y345 (≠ D365), G346 (= G366), D348 (= D368), I349 (≠ E369), M354 (≠ Y374)
binding magnesium ion: D250 (= D270), D348 (= D368)

Sites not aligning to the query:

active site: 379, 440
binding diphosphomethylphosphonic acid adenosyl ester: 420, 440
binding n2-(carboxyethyl)-l-arginine: 370, 379

1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
28% identity, 51% coverage: 72:383/616 of query aligns to 61:350/491 of 1mc1A

query
sites
1mc1A

S

T

V

A

V

V

F

L

N
x
A

G
|
G

E

E

I

I

Y

Y

N

N

F

R

R

D

D

E

L

L

R

-

A

-

E

-

L

L

E

S

G

V

L

L

G

P

H

A

V

G

F

P

R

A

S

P

H

E

S

G

D

D

T

A

E

E

V

L

L

V

L

L

A

R

A

L

Y

L

A

E

Q

R

W

Y

G

D

I

L

G

H

C

A

L

F

T

R

R

L

L

V

N

N

G

G

M

R

F

F

A

A

F

T

A

V

I

V

F

R

D

T

A

G

R

-

A

-

N

D

K

R

V

V

Y

L

F

L

A

A

R

T

D

D

R

H

A

A

G

G

E

S

K

V

P

P

L

L

F

Y

Y

T

H

C

A

V

A

A

N

P

G

G

T

E

I

V

H

R

F

A

A

S

S

T

E

E

L

A

K

K

T

A

L

L

L

A

A

A

D

G

P

F

T

P

L

L

P

A

R

-

V

-

I

-

D

-

P

-

A

-

L

-

D

D

G

A

Y

R

L

R

L

V

T

A

G

G

Y

-

V

-

P

-

G

-

D

-

G

-

C

-

I

-

L

L

A

T

G

G

Y

V

R

Y

K

Q

L

V

P

P

P

A

G

G

H

A

A

V

M

M

E

D

L

I

D

D

L

L

S

G

S

S

G

G

A

T

H

A

R

V

V

T

W

H

R

R

Y

T

W

W

N

T

L

-

P

P

D

G

Y

L

A

S

P

R

V

R

E

I

D

L

D

P

D

E

A

G

G

E

L

A

L

V

G

A

E

A

L

V

E

R

A

A

L

A

L

L

E

E

D

K

A

A

V

V

G

A

R

Q

Q

R

L

V

V

T

-

P

A

G

D

D

V

T

P

P

V

L

G

-

V

V

L
x
V

L

L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

S

S

L

G

I

V

T

A

A

A

M

C

A

A

V

H

R

R

N

A

A

A

A

G

K

E

V

L

R

D

T

T

F

V

T
x
S

I
x
M

G

G

F

T

A

D

G

T

A

S

G

-

P

-

L

-

N

N

E

E

I

F

E

R

H

E

A

A

R

R

L

A

I

V

A

V

D

D

H

H

F

L

G

R

T

T

E

R

Q

H

V

R

E

E

L

I

M

T

A

I

E

P

P

T

T

T

V

-

A

-

E

E

L

L

P

A

R

Q

L

L

-

P

-

Y

-

A

-

V

-

W

A

A

A

S

Q

E

F

S

D

V

E

D

P

P

M
x
D

A

I

D

I

S

E

S
x
Y

M

L

F

L

P

P

T

L

F

T

M

A

V

L

S

Y

E

R

L

A

V

L

R

D

Q

G

H

P

C

E

T

R

V

R

A

I

L

L

G

T

G
|
G

D
x
Y

G
|
G

G

A

D
|
D

E
x
I

L

P

F

L

G

G

Y

M

G

H

H

R

Y

E

S

D

Q

R

L

L

L

P

A

A

L

L

active site: A65 (≠ N76), G66 (= G77), D306 (≠ M339), Y332 (≠ D365)
binding adenosine monophosphate: V231 (≠ L264), S233 (= S266), S238 (= S271), S256 (≠ T289), M257 (≠ I290), G331 (= G364)
binding magnesium ion: D237 (= D270), D335 (= D368)
binding deoxyguanidinoproclavaminic acid: Y310 (≠ S343), Y332 (≠ D365), G333 (= G366), I336 (≠ E369)
binding pyrophosphate 2-: S233 (= S266), G235 (= G268), D237 (= D270), S238 (= S271), D335 (= D368)

Sites not aligning to the query:

active site: 366, 427
binding adenosine monophosphate: 427, 430
binding deoxyguanidinoproclavaminic acid: 357, 366, 427
binding pyrophosphate 2-: 407, 427, 428

1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
28% identity, 51% coverage: 72:383/616 of query aligns to 65:355/496 of 1mbzA

query
sites
1mbzA

S

T

V

A

V

V

F

L

N
x
A

G
|
G

E

E

I

I

Y

Y

N

N

F

R

R

D

D

E

L

L

R

-

A

-

E

-

L

L

E

S

G

V

L

L

G

P

H

A

V

G

F

P

R

A

S

P

H

E

S

G

D

D

T

A

E

E

V

L

L

V

L

L

A

R

A

L

Y

L

A

E

Q

R

W

Y

G

D

I

L

G

H

C

A

L

F

T

R

R

L

L

V

N

N

G

G

M

R

F

F

A

A

F

T

A

V

I

V

F

R

D

T

A

G

R

-

A

-

N

D

K

R

V

V

Y

L

F

L

A

A

R

T

D

D

R

H

A

A

G

G

E

S

K

V

P

P

L

L

F

Y

Y

T

H

C

A

V

A

A

N

P

G

G

T

E

I

V

H

R

F

A

A

S

S

T

E

E

L

A

K

K

T

A

L

L

L

A

A

A

D

H

P

-

T

-

L

-

P

-

R

-

V

-

I

-

D

-

P

-

A

-

L

-

D

-

G

G

Y

F

L

P

L

L

T

A

G

D

Y

A

V

R

P

R

G

V

D

A

G

G

C

-

I

-

L

L

A

T

G

G

Y

V

R

Y

K

Q

L

V

P

P

P

A

G

G

H

A

A

V

M

M

E

D

L

I

D

D

L

L

S

G

S

S

G

G

A

T

H

A

R

V

V

T

W

H

R

R

Y

T

W

W

N

T

L

-

P

P

D

G

Y

L

A

S

P

R

V

R

E

I

D

L

D

P

D

E

A

G

G

E

L

A

L

V

G

A

E

A

L

V

E

R

A

A

L

A

L

L

E

E

D

K

A

A

V

V

G

A

R

Q

Q

R

L

V

V

T

-

P

A

G

D

D

V

T

P

P

V

L

G

-

V

V

L
x
V

L
|
L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

S

S

L

G

I

V

T

A

A

A

M

C

A

A

V

H

R

R

N

A

A

A

A

G

K

E

V

L

R

D

T

T

F

V

T
x
S

I
x
M

G

G

F

T

A

D

G

T

A

S

G

-

P

-

L

-

N

N

E

E

I

F

E

R

H

E

A

A

R

R

L

A

I

V

A

V

D

D

H

H

F

L

G

R

T

T

E

R

Q

H

V

R

E

E

L

I

M

T

A

I

E

P

P

T

T

T

V

-

A

-

E

E

L

L

P

A

R

Q

L

L

-

P

-

Y

-

A

-

V

-

W

A

A

A

S

Q

E

F

S

D

V

E

D

P

P

M
x
D

A

I

D

I

S

E

S
x
Y

M

L

F

L

P

P

T
x
L

F

T

M

A

V

L

S

Y

E

R

L

A

V

L

R

D

Q

G

H

P

C

E

T

R

V

R

A

I

L

L

G

T

G
|
G

D
x
Y

G
|
G

G

A

D
|
D

E
x
I

L

P

F

L

G

G

Y

M

G

H

H

R

Y

E

S

D

Q

R

L

L

L

P

A

A

L

L

active site: A69 (≠ N76), G70 (= G77), D311 (≠ M339), Y337 (≠ D365)
binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L264), L237 (= L265), S238 (= S266), S243 (= S271), S261 (≠ T289), M262 (≠ I290), Y315 (≠ S343), L319 (≠ T347), G336 (= G364), Y337 (≠ D365), G338 (= G366), D340 (= D368), I341 (≠ E369)
binding magnesium ion: D242 (= D270), D340 (= D368)
binding pyrophosphate 2-: S238 (= S266), G240 (= G268), D242 (= D270), S243 (= S271), D340 (= D368)

Sites not aligning to the query:

active site: 371, 432
binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: 362, 371, 432, 434, 435
binding pyrophosphate 2-: 412, 432, 433

Q9XB61 Carbapenam-3-carboxylate synthase; Carbapenam-3-carboxylate ligase; EC 6.3.3.6 from Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora) (see 3 papers)
33% identity, 20% coverage: 261:382/616 of query aligns to 241:369/503 of Q9XB61

query
sites
Q9XB61

V

V

G

G

V

I

L
x
P

L
|
L

S
|
S

G
|
G

V
x
L

D
|
D

S
|
S

S

S

L

L

I

V

T

T

A

A

M

L

A

A

V

S

R

R

N

H

A

F

A

K

K

K

V

L

R

N

T

T

F

Y

T

S

I
|
I

G

G

F

T

A

E

G

L

A

S

G

-

P

-

L

-

N

N

E

E

I

F

E

E

H

F

A

S

R

Q

L

Q

I

V

A

A

D

D

H

A

F

L

G

G

T

T

-

H

E

H

Q

Q

V

M

E

K

L

I

M

L

A

S

E

E

P

T

T

E

V

V

A

I

-

N

-

G

-

I

-

E

-

S

-

I

-

Y

-

N

E

E

L

I

L

F

P

D

R

G

L

L

A

S

A

A

Q

E

F

I

D

Q

E

S

P

G

M

L

A

-

D

-

S

-

M

-

F

-

P

-

T

-

F

F

M

N

V

V

S

Y

E

R

L

Q

V

A

R

Q

Q

G

H

Q

C

V

T

S

V

C

A

M

L

L

G

T

G
|
G

D
x
Y

G
|
G

G
x
S

D
|
D

E

L

L

L

F

F

G

G

-

I

-

L

-

K

-

P

-

G

-

A

-

Q

Y

Y

G

D

H

N

Y

P

S

N

Q

Q

L

L

A

A

244:251 (vs. 264:271, 75% identical) binding ATP
I270 (= I290) binding ATP
GYGSD 344:348 (≠ GDGGD 364:368) binding ATP
Y345 (≠ D365) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
G346 (= G366) binding substrate

Sites not aligning to the query:

371 binding substrate
374 binding substrate
380 E→A: Loss of activity.; E→D: Reduces catalytic efficiency.; E→Q: Reduces catalytic efficiency.
421 binding ATP
443 mutation K->A,M: Loss of activity.
444:446 binding ATP

1q19A Carbapenam synthetase (see paper)
33% identity, 20% coverage: 261:382/616 of query aligns to 240:368/500 of 1q19A

query
sites
1q19A

V

V

G

G

V

I

L
x
P

L
|
L

S
|
S

G

G

V

L

D
|
D

S
|
S

S

S

L

L

I

V

T

T

A

A

M

L

A

A

V

S

R

R

N

H

A

F

A

K

K

K

V

L

R

N

T

T

F

Y

T
x
S

I
|
I

G

G

F

T

A

E

G

L

A

S

G

-

P

-

L

-

N

N

E

E

I

F

E

E

H

F

A

S

R

Q

L

Q

I

V

A

A

D

D

H

A

F

L

G

G

T

T

-

H

E

H

Q

Q

V

M

E

K

L

I

M

L

A

S

E

E

P

T

T

E

V

V

A

I

-

N

-

G

-

I

-

E

-

S

-

I

-

Y

-

N

E

E

L

I

L

F

P

D

R

G

L
|
L

A

S

A

A

Q
x
E

F

I

D

Q

E

S

P

G

M

L

A

-

D

-

S

-

M

-

F

-

P

-

T

-

F

F

M

N

V

V

S

Y

E

R

L

Q

V

A

R

Q

Q

G

H

Q

C

V

T

S

V

C

A

M

L

L

G
x
T

G
|
G

D
x
Y

G
|
G

G

S

D
|
D

E
x
L

L

L

F

F

G

G

-

I

-

L

-

K

-

P

-

G

-

A

-

Q

Y

Y

G

D

H

N

Y

P

S

N

Q

Q

L

L

A

A

active site: L318 (= L331), E321 (≠ Q334), Y344 (≠ D365)
binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L264), L244 (= L265), S245 (= S266), D249 (= D270), S250 (= S271), S268 (≠ T289), I269 (= I290), T342 (≠ G363), G343 (= G364), D347 (= D368)
binding (2s,5s)-5-carboxymethylproline: Y344 (≠ D365), G345 (= G366), L348 (≠ E369)

Sites not aligning to the query:

active site: 56, 379, 442
binding diphosphomethylphosphonic acid adenosyl ester: 442, 443, 444, 445
binding (2s,5s)-5-carboxymethylproline: 373, 379

6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
27% identity, 29% coverage: 2:181/616 of query aligns to 1:215/460 of 6lbpA

query
sites
6lbpA

C
|
C

G

G

I

V

A

V

G

G

V

I

A

Y

S

G

R

D

H

S

E

E

L

A

P

S

R

R

S

L

G

C

W

Y

L

L

G

-

D

-

A

A

V

L

G

H

A

A

L

L

H

Q

H

H

R

R

G
|
G

P

Q

D

E

D

G

T

A

G

G

Q

I

W

V

W

T

S

V

P

S

D

K

G

D

R

K

V

V

-

L

-

Q

-

T

-

I

-

T

-

G

-

V

G

G

L

L

A

V

Q

S

A

E

R

V

L

F

A

S

-

E

-

S

I

K

I

L

D

D

L

Q

S

L

P

P

G

G

-

D

-

I

-

A

-

I

G

G

H

H

-

V

-

R

-

Y

-

S

-

T

-

A

-

G

Q

S

P

S

M

M

H

L

R

K

E

N

A

V

D

Q

-

P

-

F

-

V

-

A

-

G

-

Y

-

R

-

F

-

G

R

S

L

V

S

G

V

V

V

A

F

H

N
|
N

G
|
G

E

N

I

L

Y

V

N

N

F

Y

R

T

D

K

L

L

R

R

A

A

E

D

L

L

E

E

G

E

L

N

G

G

H

S

V

I

F

F

R

N

S

T

H

S

S

S

D

D

T

T

E

E

V

V

L

V

L

L

A

H

A

L

Y

I

A

A

Q

I

W

S

G

K

-

A

-

R

-

P

-

F

-

M

-

R

-

I

I

V

G

D

C

A

L

C

T

E

R

K

L

L

N

Q

G

G

M

-

F

-

A

A

F

Y

A

S

I

M

F

V

D

F

A

V

R

T

A

E

N

D

K

K

V

L

Y

V

F

A

A

V

R

R

D

D

R

P

A

H

G

G

E

F

K

R

P

P

L

L

F

V

Y

M

-

G

H

R

A

R

A

S

N

N

G

G

T

A

I

V

H

V

F

F

A

A

S

S

E

E

L

T

K

C

T

A

L

L

-

D

L

L

A

I

D

E

P

A

T

T

L

Y

P

E

R

R

V

E

I

V

D

Y

P

P

A

G

A

E

L

V

active site: C1 (= C2), G27 (= G30), N102 (= N76), G103 (= G77)

Sites not aligning to the query:

active site: 243, 301, 306, 316, 424
binding iron/sulfur cluster: 237, 239, 383, 385, 434, 436, 437

Q9STG9 Amidophosphoribosyltransferase 2, chloroplastic; AtATase2; AtPURF2; PRPP2; Glutamine phosphoribosylpyrophosphate amidotransferase 2; AtGPRAT2; Protein CHLOROPLAST IMPORT APPARATUS 1; Protein DIFFERENTIAL DEVELOPMENT OF VASCULAR ASSOCIATED CELLS; EC 2.4.2.14 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 29% coverage: 2:181/616 of query aligns to 87:301/561 of Q9STG9

query
sites
Q9STG9

C

C

G

G

I

V

A

V

G

G

V

I

A

Y

S

G

R

D

H

S

E

E

L

A

P

S

R

R

S

L

G

C

W

Y

L

L

G

-

D

-

A

A

V

L

G

H

A

A

L

L

H

Q

H

H

R

R

G

G

P

Q

D

E

D

G

T

A

G

G

Q

I

W

V

W

T

S

V

P

S

D

K

G

D

R

K

V

V

-

L

-

Q

-

T

-

I

-

T

-

G

-

V

G

G

L

L

A

V

Q

S

A

E

R

V

L

F

A

S

-

E

-

S

I

K

I

L

D

D

L

Q

S

L

P

P

G

G

-

D

-

I

-

A

-

I

G

G

H

H

-

V

-

R

-

Y

-

S

-

T

-

A

-

G

Q

S

P

S

M

M

H

L

R

K

E

N

A

V

D

Q

-

P

-

F

-

V

-

A

-

G

-

Y

-

R

-

F

-

G

R

S

L

V

S

G

V

V

V

A

F
x
H

N

N

G

G

E

N

I

L

Y

V

N

N

F

Y

R

T

D

K

L

L

R

R

A

A

E

D

L

L

E

E

G

E

L

N

G

G

H

S

V

I

F

F

R

N

S

T

H

S

S

S

D

D

T

T

E

E

V

V

L

V

L

L

A

H

A

L

Y

I

A

A

Q

I

W

S

G

K

-

A

-

R

-

P

-

F

-

M

-

R

-

I

I

V

G

D

C

A

L

C

T

E

R

K

L

L

N

Q

G

G

M

-

F

-

A

A

F

Y

A

S

I

M

F

V

D

F

A

V

R

T

A

E

N

D

K

K

V

L

Y

V

F

A

A

V

R

R

D

D

R

P

A

H

G

G

E

F

K
x
R

P
|
P

L

L

F

V

Y

M

-

G

H

R

A

R

A

S

N

N

G

G

T

A

I

V

H

V

F

F

A

A

S

S

E

E

L

T

K

C

T

A

L

L

-

D

L

L

A

I

D

E

P

A

T

T

L

Y

P

E

R

R

V

E

I

V

D

Y

P

P

A

G

A

E

L

V

H187 (≠ F75) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
R264 (≠ K146) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
P265 (= P147) mutation to S: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with F-494.

Sites not aligning to the query:

371 G→S: Low resistance to the bleaching herbicides DAS073 and DAS734.
476 P→S: Resistance to the bleaching herbicides DAS073 and DAS734.
494 Y→F: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with S-265.

Query Sequence

>Ga0059261_3119 FitnessBrowser__Korea:Ga0059261_3119
MCGIAGVASRHELPRSGWLGDAVGALHHRGPDDTGQWWSPDGRVGLAQARLAIIDLSPGG
HQPMHREADRLSVVFNGEIYNFRDLRAELEGLGHVFRSHSDTEVLLAAYAQWGIGCLTRL
NGMFAFAIFDARANKVYFARDRAGEKPLFYHAANGTIHFASELKTLLADPTLPRVIDPAA
LDGYLLTGYVPGDGCILAGYRKLPPGHAMELDLSSGAHRVWRYWNLPDYAPVEDDDAGLL
GELEALLEDAVGRQLVADVPVGVLLSGGVDSSLITAMAVRNAAKVRTFTIGFAGAGPLNE
IEHARLIADHFGTEQVELMAEPTVAELLPRLAAQFDEPMADSSMFPTFMVSELVRQHCTV
ALGGDGGDELFGGYGHYSQLLALRAKVGAVPGPLRSLAARTAETLLPLGFRGRNWLKGLD
VDFRHGLPLPSGFFDAASRRKLLGGAHPITAEADYRSRIPAMDDLLQRATRTDFGTYLSE
DILVKVDRTSMLTSLEVRAPFLDHRLIEFAFGKVPSRLKATASDKKILLKQLAARVLPPQ
FDRQRKQGFSIPLADWLKAGPFREMFWSVLTDCDCLFDRRAVQALLDGQDAGRSNGDRLF
ALAQFELWRRAYGIGG

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