SitesBLAST

M1 (= M1) modified: Initiator methionine, Removed
C2 (= C2) mutation C->A,S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity.
H30 (≠ W30) mutation to A: 4,5-fold decrease in glutamine affinity.
D34 (= D34) mutation D->N,E: Little effect on the kinetic properties.
H81 (≠ M83) mutation to A: 5-fold decrease in glutamine affinity.
A105 (≠ V108) mutation to H: Little effect on the kinetic properties.
E349 (= E379) 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.

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)
29% identity, 87% coverage: 1:534/613 of query aligns to 1:468/557 of P78753

query
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P78753

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S391 (≠ M465) modified: Phosphoserine

Sites not aligning to the query:

489 modified: Phosphoserine

1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
28% identity, 87% coverage: 2:534/613 of query aligns to 1:433/497 of 1ct9A

query
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active site: A1 (≠ C2), L50 (= L51), N74 (= N77), G75 (= G78), T305 (= T355), R308 (≠ D358), E332 (= E379), M366 (≠ L461)
binding adenosine monophosphate: L232 (= L263), L233 (= L264), S234 (= S265), S239 (= S270), A255 (≠ S293), V256 (≠ I294), D263 (= D313), M316 (≠ F364), S330 (= S377), G331 (= G378), E332 (= E379)
binding glutamine: A1 (≠ C2), R49 (= R50), L50 (= L51), I52 (= I53), V53 (≠ I54), N74 (= N77), G75 (= G78), E76 (= E79), D98 (= D102)

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)
28% identity, 64% coverage: 1:393/613 of query aligns to 1:379/561 of P08243

query
sites
P08243

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D

R

T

L

Y

G

G

V

V

K

R

P

P

L

L

F

F

Y

K

A

A

P

M

L

T

A

E

S

D

G

G

-

F

L

L

V

A

F

V

A

C

S

S

E

E

L

A

K

K

G

G

L

L

L

V

-

T

-

L

-

K

-

H

-

S

A

A

H

T

P

P

A

F

V

L

R

K

P

V

E

E

V

P

D

F

S

L

E

P

G

G

L

H

A

Y

E

E

I

V

F

L

A

D

M

L

G

K

P

P

G

N

-

G

-

K

-

V

-

A

-

S

-

V

-

E

-

M

-

V

-

K

-

Y

-

H

-

C

-

R

R

D

T
x
V

P

P

G

L

H

H

G

A

V

L

F

Y

R

D

N

N

T

V

C

E

E

K

V

L

K

F

P

P

G

G

W

F

A

-

L

-

F

-

D

-

R

-

G

-

L

-

H

-

R

-

Q

-

Y

-

W

-

K

-

L

-

E

-

S

-

R

-

P

-

H

-

E

-

D

-

D

E

L

I

E

E

T

T

T

V

I

K

A

N

T

N

V

L

R

R

D

I

L

L

L

F

E

N

D

N

T

A

V

V

G

K

R

K

Q

R

L

L

M

M

S

T

D

D

V

R

P

R

V

I

C

G

T

C

L

L

S

S

G

G

L

L

D

D

S

S

A

L

I

V

T

A

A

A

F

T

A

L

R

K

A

Q

F

L

R

K

R

E

-

A

Q

Q

G

V

R

Q

P

Y

P

P

L

L

R

Q

T

T

F

F

S

A

I

I

D

G

Y

M

V

E

D

D

N

-

D

-

V

-

Y

-

F

-

Q

-

P

-

N

-

A

-

F

-

Q

-

P

-

A

S

A

P

D

D

G

L

P

L

W

A

A

A

E

R

R

K

V

V

A

A

D

D

F

H

L

I

Q

G

V

S

D

E

R

H

R

Y

I

E

V

V

T

L

L

F

T

N

P

S

A

E

V

G

A

I

D

Q

A

A

L

L

R

D

E

E

A

V

V

I

R

F

A

S

R

L

D

E

L

T

P

Y

G

D

M

I

T

T

D

T

I

V

D

R

S

A

S

S

-

V

-

G

L

M

L

Y

L

L

F

I

C

S

R

K

E

Y

I

I

K

R

K

K

-

N

-

T

E

D

A

S

T

V

V

V

A

I

L
x
F

S

S

G

G

E

E

C

G

A

S

D

D

E

E

V

L

F

T

G

Q

G

G

Y

Y

P

I

W

Y

F

F

H

H

R

K

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 (≠ I8) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
V210 (≠ T193) to E: in dbSNP:rs1049674
F362 (≠ L376) 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

6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
28% identity, 64% coverage: 2:393/613 of query aligns to 1:366/509 of 6gq3A

query
sites
6gq3A

C
|
C

G

G

I

I

A

-

G

-

W
|
W

I

A

D

L

W

F

N

G

V

S

E

D

M

D

T

C

E

L

Q

S

R

V

P

Q

V

C

L

L

K

S

A

A

M

M

A

K

D

I

V

A

Q

H

Y

-

W

-

R

R

G

G

P

P

D

D

A

A

-

F

-

R

-

F

E

E

G

N

I

V

W

N

M

G

S

Y

R

T

R

N

A

C

G

C

L

F

A

G

H

F

R

H

R
|
R

L
|
L

S

A

I
x
V

D

D

P

P

E

L

G

F

G

G

A

M

Q

Q

P

P

M

-

I

I

R

R

R

V

H

K

G

K

E

Y

R

P

T

Y

L

L

V

W

I

L

V

C

Y
|
Y

N
|
N

G
|
G

E
|
E

L

I

Y

Y

N

N

M

H

A

K

E

K

L

M

Q

Q

R

Q

E

H

L

F

E

E

G

-

L

-

G

-

Y

F

T

E

F

Y

A

Q

T

T

R

K

C
x
V

D
|
D

T

G

E

E

V

I

L

L

V

H

A

L

Y

Y

A

D

H

K

W

G

G

G

-

I

P

E

A

Q

C

T

V

I

E

C

R

M

F

L

N

D

G

G

I

V

Y

F

A

A

I

F

G

V

I

L

W

L

D

D

E

T

Q

A

S

N

Q

K

E

K

L

V

F

F

L

L

A

G

R

R

D

D

R

T

L

Y

G

G

V

V

K

R

P

P

L

L

F

F

Y

K

A

A

P

M

L

T

A

E

S

D

G

G

-

F

L

L

V

A

F

V

A

C

S

S

E

E

L

A

K

K

G

G

L

L

L

V

-

T

-

L

-

K

-

H

-

S

A

A

H

T

P

P

A

F

V

L

R

K

P

V

E

E

V

P

D

F

S

L

E

P

G

G

L

H

A

Y

E

E

I

V

F

L

A

D

M

L

G

K

P

P

-

N

G

G

R

K

T

V

P

A

G

S

H

V

G

E

V

M

-

V

-

K

F

Y

R

H

N

H

T

C

C

R

E

D

V

V

K

F

P

P

G

G

W

F

A

-

L

-

F

-

D

-

R

-

G

-

L

-

H

-

R

-

Q

-

Y

-

W

-

K

-

L

-

E

-

S

-

R

-

P

-

H

-

E

-

D

-

D

E

L

I

E

E

T

T

T

V

I

K

A

N

T

N

V

L

R

R

D

I

L

L

L

F

E

N

D

N

T

A

V

V

G

K

R

K

Q

R

L

L

M

M

S

T

D

D

V

R

P

R

V

I

C

G

T

C

L

L

S

S

G

G

L

L

D

D

S

S

A

L

I

V

T

A

A

A

F

T

A

L

R

K

A

Q

F

L

R

K

R

E

-

A

Q

Q

G

V

R

Q

P

Y

P

P

L

L

R

Q

T

T

F

F

S

A

I

I

D

G

Y

M

V

E

D

D

N

-

D

-

V

-

Y

-

F

-

Q

-

P

-

N

-

A

-

F

-

Q

-

P

-

A

S

A

P

D

D

G

L

P

L

W

A

A

A

E

R

R

K

V

V

A

A

D

D

F

H

L

I

Q

G

V

S

D

E

R

H

R

Y

I

E

V

V

T

L

L

F

T

N

P

S

A

E

V

G

A

I

D

Q

A

A

L

L

R

D

E

E

A

V

V

I

R

F

A

S

R

L

D

E

L

T

P

Y

G

D

M

I

T
|
T

D

T

I

V

D
x
R

S

A

S

S

-

V

-

G

L

M

L

Y

L

L

F

I

C

S

R

K

E

Y

I

I

K

R

K

K

-

N

-

T

E

D

A

S

T

V

V

V

A

I

L

F

S

S

G

G

E

E

C

G

A

S

D

D

E

E

V

L

F

T

G

Q

G

G

Y

Y

P

I

W

Y

F

F

H

H

R

K

active site: W4 (= W7), L49 (= L51), N74 (= N77), G75 (= G78), T324 (= T355), R327 (≠ D358)
binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R50), V51 (≠ I53), V52 (≠ I54), Y73 (= Y76), N74 (= N77), G75 (= G78), E76 (= E79), V95 (≠ C101), D96 (= D102)

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)
23% identity, 32% coverage: 246:442/613 of query aligns to 231:436/503 of Q9XB61

query
sites
Q9XB61

L

L

E

E

D

D

T

L

V

A

G

P

R

R

Q

F

L

D

M

T

S

V

D

G

V

I

P
|
P

V

-

C

-

T

-

L

-

L
|
L

S
|
S

G
|
G

L
|
L

D
|
D

S
|
S

S

S

A

L

I

V

T

T

A

A

F

L

A

A

A

S

R

R

A

H

F

F

R

K

Q

-

G

-

R

-

P

-

L

L

R

N

T

T

F

Y

S

S

I
|
I

D

-

Y

-

V

-

D

-

N

-

D

-

V

-

Y

-

F

-

Q

-

P

-

N

-

A

G

F

T

Q

E

P

L

A

S

A

N

D

E

G

F

P

E

W

F

A

S

E

Q

R

Q

V

V

A

A

D

D

F

A

L

L

Q

G

V

T

D

H

R

H

R

Q

I

M

V

K

T

I

L

L

T

S

P

E

A

T

A

E

V

V

A

I

D

N

A

G

L

I

R

I

E

E

A

S

V

I

R

Y

A

Y

R

N

D

E

L

I

-

F

P

D

G

G

M

L

T

S

-

A

D

E

I

I

D

Q

S

S

S

G

L

L

L

F

L

N

F

V

C

Y

R

R

E

Q

I

A

K

Q

K

G

E

Q

A

V

T

S

V

C

A

M

L

L

S

T

G
|
G

E
x
Y

C
x
G

A
x
S

D
|
D

E

L

V

L

F

F

G

G

Y

I

-

L

-

K

-

P

-

G

-

A

P

Q

W

Y

F

D

H

N

R

P

K

N

E

Q

A

L

L

L

E

A

A

E

D
x
Q

V

V

F

Y

P
x
R

-

T

-

R

-

W

-

T

-

G

-
x
E

-

F

-

A

-

T

-

H

-

G

-

A

-

S

-

C

-

Y

-

G

-

I

-

D

-

I

-

R

-

H

-

P

-

F

W

W

S

S

L

H

K

S

M

L

R

I

E

S

R

L

I

C

S

H

V

A

L

L

H

H

P

P

D

D

F

Y

V

K

D

I

H

F

V

D

Q

N

P

E

E

V

Q
x
K

Y

N

V

I

R

L

R

R

R

E

Y

Y

R

A

E

D

V

S

L

L

D

Q

A

L

V

L

P

P

R

K

244:251 (vs. 259:270, 67% identical) binding ATP
I270 (= I294) binding ATP
GYGSD 344:348 (≠ GECAD 378:382) binding ATP
Y345 (≠ E379) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
G346 (≠ C380) binding substrate
Q371 (≠ D400) binding substrate
R374 (≠ P403) binding substrate
E380 (vs. gap) mutation to A: Loss of activity.; mutation to D: Reduces catalytic efficiency.; mutation to Q: Reduces catalytic efficiency.
K421 (≠ Q427) binding ATP

Sites not aligning to the query:

443 mutation K->A,M: Loss of activity.
444:446 binding ATP

1q19A Carbapenam synthetase (see paper)
23% identity, 32% coverage: 246:442/613 of query aligns to 230:435/500 of 1q19A

query
sites
1q19A

L

L

E

E

D

D

T

L

V

A

G

P

R

R

Q

F

L

D

M

T

S

V

D

G

V

I

P
|
P

V

-

C

-

T

-

L

-

L
|
L

S
|
S

G

G

L

L

D
|
D

S
|
S

S

S

A

L

I

V

T

T

A

A

F

L

A

A

A

S

R

R

A

H

F

F

R

K

Q

-

G

-

R

-

P

-

L

L

R

N

T

T

F

Y

S
|
S

I
|
I

D

-

Y

-

V

-

D

-

N

-

D

-

V

-

Y

-

F

-

Q

-

P

-

N

-

A

G

F

T

Q

E

P

L

A

S

A

N

D

E

G

F

P

E

W

F

A

S

E

Q

R

Q

V

V

A

A

D

D

F

A

L

L

Q

G

V

T

D

H

R

H

R

Q

I

M

V

K

T

I

L

L

T

S

P

E

A

T

A

E

V

V

A

I

D

N

A

G

L

I

R

I

E

E

A

S

V

I

R

Y

A

Y

R

N

D

E

L

I

-

F

P

D

G

G

M
x
L

T

S

-

A

D
x
E

I

I

D

Q

S

S

S

G

L

L

L

F

L

N

F

V

C

Y

R

R

E

Q

I

A

K

Q

K

G

E

Q

A

V

T

S

V

C

A

M

L

L

S
x
T

G
|
G

E
x
Y

C
x
G

A

S

D
|
D

E
x
L

V

L

F

F

G

G

Y

I

-

L

-

K

-

P

-

G

-

A

P

Q

W

Y

F

D

H

N

R

P

K

N

E

Q

A

L

L

L

E

A

A

E

D

Q

V

V

F

Y

P
x
R

-

T

-

R

-

W

-

T

-

G

-
x
E

-

F

-

A

-

T

-

H

-

G

-

A

-

S

-

C

-

Y

-

G

-

I

-

D

-

I

-

R

-

H

-

P

-

F

W

W

S

S

L

H

K

S

M

L

R

I

E

S

R

L

I

C

S

H

V

A

L

L

H

H

P

P

D

D

F

Y

V

K

D

I

H

F

V

D

Q

N

P

E

E

V

Q

K

Y

N

V

I

R

L

R

R

R

E

Y

Y

R

A

E

D

V

S

L

L

D

Q

A

L

V

L

P

P

R

K

active site: L318 (≠ M354), E321 (≠ D356), Y344 (≠ E379), E379 (vs. gap)
binding diphosphomethylphosphonic acid adenosyl ester: P243 (= P259), L244 (= L264), S245 (= S265), D249 (= D269), S250 (= S270), S268 (= S293), I269 (= I294), T342 (≠ S377), G343 (= G378), D347 (= D382)
binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E379), G345 (≠ C380), L348 (≠ E383), R373 (≠ P403), E379 (vs. gap)

Sites not aligning to the query:

active site: 56, 442
binding diphosphomethylphosphonic acid adenosyl ester: 442, 443, 444, 445

1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
28% identity, 20% coverage: 43:163/613 of query aligns to 65:194/465 of 1gph1

query
sites
1gph1

R

K

A

G

G

A

L

I

A

G

H

H

R

V

R

R

L

Y

S

A

I

T

I

A

D

G

P

G

E

G

G

G

-

Y

-

E

G

N

A

V

Q

Q

P

P

M

L

I

L

-

F

R

R

R

S

H

Q

G

N

E

N

R

G

T

S

L

L

V

A

I

L

V

A

Y

H

N

N

G

G

E

N

L

L

Y

V

N

N

M

A

A

T

E

Q

L

L

Q

K

R

Q

E

Q

L

L

E

E

G

N

L

Q

G

G

Y

S

T

I

F

F

A

Q

T

T

R

S

C

S

D

D

T

T

E

E

V

V

V

L

L

A

V

H

A

L

Y

I

A

K

H

R

W

S

G

G

-

H

-

F

-

T

-

L

-

K

-

D

-

Q

-

I

P

K

A

N

C

S

V

L

E

S

R

M

F

L

N

K

G

G

I

A

Y

Y

A

A

I

F

G

L

I

I

W

M

D

T

E

E

Q

-

S

-

Q

T

E

E

L

M

F

I

L

V

A

A

R

L

D

D

R

P

L

N

G

G

V

L

K

R

P

P

L

L

F

S

Y

I

A

G

P

M

L

M

A

G

S

D

G

A

L

Y

V

V

F

V

A

A

S

S

E

E

Sites not aligning to the query:

active site: 300, 305, 315, 423
binding adenosine monophosphate: 242, 242, 244, 245, 246, 282, 283, 283, 304, 305, 307, 345, 346, 347, 349, 350, 353, 388
binding iron/sulfur cluster: 236, 237, 382, 384, 388, 437, 440

P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
28% identity, 20% coverage: 43:163/613 of query aligns to 76:205/476 of P00497

query
sites
P00497

R

K

A

G

G

A

L

I

A

G

H

H

R

V

R

R

L

Y

S

A

I

T

I

A

D

G

P

G

E

G

G

G

-

Y

-

E

G

N

A

V

Q

Q

P

P

M

L

I

L

-

F

R

R

R

S

H

Q

G

N

E

N

R

G

T

S

L

L

V

A

I

L

V

A

Y

H

N

N

G

G

E

N

L

L

Y

V

N

N

M

A

A

T

E

Q

L

L

Q

K

R

Q

E

Q

L

L

E

E

G

N

L

Q

G

G

Y

S

T

I

F

F

A

Q

T

T

R

S

C

S

D

D

T

T

E

E

V

V

V

L

L

A

V

H

A

L

Y

I

A

K

H

R

W

S

G

G

-

H

-

F

-

T

-

L

-

K

-

D

-

Q

-

I

P

K

A

N

C

S

V

L

E

S

R

M

F

L

N

K

G

G

I

A

Y

Y

A

A

I

F

G

L

I

I

W

M

D

T

E

E

Q

-

S

-

Q

T

E

E

L

M

F

I

L

V

A

A

R

L

D

D

R

P

L

N

G

G

V

L

K

R

P

P

L

L

F

S

Y

I

A

G

P

M

L

M

A

G

S

D

G

A

L

Y

V

V

F

V

A

A

S

S

E

E

Sites not aligning to the query:

1:11 modified: propeptide
12 active site, Nucleophile; C→F: Loss of enzyme activity and N-terminal processing.
247 binding [4Fe-4S] cluster
294 binding Mg(2+)
356 binding Mg(2+)
357 binding Mg(2+)
393 binding [4Fe-4S] cluster
394 F→V: Partial loss of activity.
442 D→S: Partial loss of activity.
448 binding [4Fe-4S] cluster; C→S: Loss of activity.
451 binding [4Fe-4S] cluster; C→S: Loss of activity.
452 F→C: Lethal.

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)
33% identity, 17% coverage: 61:167/613 of query aligns to 172:285/561 of Q9STG9

query
sites
Q9STG9

Q

Q

P

P

M

F

I

V

R

A

R

G

H

Y

G

R

E

F

R

G

T

S

L

V

V

G

I

V

V

A

Y
x
H

N

N

G

G

E

N

L

L

Y

V

N

N

M

Y

A

T

E

K

L

L

Q

R

R

A

E

D

L

L

E

E

G

E

L

N

G

G

Y

S

T

I

F

F

A

N

T

T

R

S

C

S

D

D

T

T

E

E

V

V

-

L

-

H

L

L

V

I

A

A

Y

I

A

S

H

K

W

A

G

R

P

P

-

F

-

M

-

R

-

I

-

V

-

D

A

A

C

C

V

-

E

E

R

K

F

L

N

Q

G

G

I

A

Y

Y

A

S

I

M

G

V

I

F

W

V

D

T

E

E

Q

-

S

-

Q

D

E

K

L

L

F

V

L

A

A

V

R

R

D

D

R

P

L

H

G

G

V

F

K
x
R

P
|
P

L

L

F

V

Y

M

A

G

P

R

L

R

A

S

S

N

G

G

-

A

L

V

V

V

F

F

A

A

S

S

E

E

L

T

K

C

G

A

L

L

H187 (≠ Y76) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
R264 (≠ K147) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
P265 (= P148) 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.

6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
33% identity, 17% coverage: 61:167/613 of query aligns to 86:199/460 of 6lbpA

query
sites
6lbpA

Q

Q

P

P

M

F

I

V

R

A

R

G

H

Y

G

R

E

F

R

G

T

S

L

V

V

G

I

V

V

A

Y

H

N
|
N

G
|
G

E

N

L

L

Y

V

N

N

M

Y

A

T

E

K

L

L

Q

R

R

A

E

D

L

L

E

E

G

E

L

N

G

G

Y

S

T

I

F

F

A

N

T

T

R

S

C

S

D

D

T

T

E

E

V

V

-

L

-

H

L

L

V

I

A

A

Y

I

A

S

H

K

W

A

G

R

P

P

-

F

-

M

-

R

-

I

-

V

-

D

A

A

C

C

V

-

E

E

R

K

F

L

N

Q

G

G

I

A

Y

Y

A

S

I

M

G

V

I

F

W

V

D

T

E

E

Q

-

S

-

Q

D

E

K

L

L

F

V

L

A

A

V

R

R

D

D

R

P

L

H

G

G

V

F

K

R

P

P

L

L

F

V

Y

M

A

G

P

R

L

R

A

S

S

N

G

G

-

A

L

V

V

V

F

F

A

A

S

S

E

E

L

T

K

C

G

A

L

L

active site: N102 (= N77), G103 (= G78)

Sites not aligning to the query:

active site: 1, 27, 243, 301, 306, 316, 424
binding iron/sulfur cluster: 237, 239, 383, 385, 434, 436, 437

1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
30% identity, 17% coverage: 61:163/613 of query aligns to 81:190/455 of 1ao0A

query
sites
1ao0A

Q

Q

P

P

M

L

I

L

-

F

R

R

R

S

H

Q

G

N

E

N

R

G

T

S

L

L

V

A

I

L

V

A

Y

H

N
|
N

G
|
G

E

N

L

L

Y

V

N

N

M

A

A

T

E

Q

L

L

Q

K

R

Q

E

Q

L

L

E

E

G

N

L

Q

G

G

Y

S

T

I

F

F

A

Q

T

T

R

S

C

S

D

D

T

T

E

E

V

V

V

L

L

A

V

H

A

L

Y

I

A

K

H

R

W

S

G

G

-

H

-

F

-

T

-

L

-

K

-

D

-

Q

-

I

P

K

A

N

C

S

V

L

E

S

R

M

F

L

N

K

G

G

I

A

Y

Y

A

A

I

F

G

L

I

I

W

M

D

T

E

E

Q

-

S

-

Q

T

E

E

L

M

F

I

L

V

A

A

R

L

D

D

R

P

L

N

G

G

V

L

K

R

P

P

L

L

F

S

Y

I

A

G

P

M

L

M

A

G

S

D

G

A

L

Y

V

V

F

V

A

A

S

S

E

E

active site: N98 (= N77), G99 (= G78)

Sites not aligning to the query:

active site: 1, 27, 238, 296, 301, 311, 419
binding guanosine-5'-monophosphate: 234, 238, 279, 341, 342, 343, 345, 346, 347, 348, 349
binding adenosine-5'-diphosphate: 25, 238, 240, 241, 242, 277, 278, 279, 300, 301, 301, 303
binding magnesium ion: 279, 341, 342
binding iron/sulfur cluster: 232, 233, 234, 378, 380, 433, 436

1jgtB Crystal structure of beta-lactam synthetase (see paper)
30% identity, 34% coverage: 75:280/613 of query aligns to 71:261/500 of 1jgtB

query
sites
1jgtB

V

V

Y

L

N
x
A

G
|
G

E

E

L

I

Y

Y

N

N

M

R

A

D

E

E

L

L

Q

-

R

-

E

-

L

L

E

S

G

V

L

L

G

P

Y

A

T

G

F

P

A

A

T

P

R

E

C

G

D

D

T

A

E

E

V

L

V

V

L

L

V

R

A

L

Y

L

A

E

H

R

W

Y

G

D

P

L

A

H

C

A

V

F

E

R

R

L

F

V

N

N

G

G

I

R

Y

F

A

A

I

T

G

V

I

V

W

-

D

-

E

R

Q

T

S

G

Q

D

E

R

L

V

F

L

L

L

A

A

R

T

D

D

R

H

L

A

G

G

V

S

K

V

P

P

L

L

F

-

Y

Y

A

T

P

C

L

V

A

A

S

P

G

G

L

E

V

V

F

R

A

A

S

S

-

T

E

E

L

A

K

K

G

A

L

L

L

A

A

A

H

H

-

R

-

D

P

P

A

K

V

G

R

F

P

P

E

L

V

A

D

D

S

A

E

R

-

R

-

V

-

A

G

G

L

L

A

T

E

G

I

V

F

Y

A

Q

M

V

G

P

P

A

G

G

R

A

T

V

P

M

G

D

H

I

G

D

V

L

F

G

R

S

N

G

T

T

C

A

E

V

V

T

K

H

P

R

G

T

W

W

A

T

L

P

L

G

F

L

D

S

R

R

G

I

L

L

H

P

H

E

R

G

Q

E

Y

-

W

-

K

-

L

-

E

-

S

-

R

-

P

-

H

-

E

-

D

-

L

-

E

-

T

-

T

A

I

V

A

A

T

A

V

V

R

R

D

A

L

A

L

L

E

E

D

K

T

A

V

V

G

A

R

Q

Q

R

L

V

M

T

-

P

S

G

D

D

V

T

P

P

V

L

C

V

T

-

L
x
V

L
|
L

S
|
S

G

G

G
|
G

L
x
I

D
|
D

S
|
S

S

S

A

G

I

V

T

A

A

A

F

C

A

A

A

H

R

R

A

A

active site: A73 (≠ N77), G74 (= G78)
binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L263), L245 (= L264), S246 (= S265), G248 (= G267), I249 (≠ L268), D250 (= D269), S251 (= S270)
binding magnesium ion: D250 (= D269)

Sites not aligning to the query:

active site: 319, 345, 379, 440
binding diphosphomethylphosphonic acid adenosyl ester: 269, 270, 327, 344, 345, 348, 420, 440
binding n2-(carboxyethyl)-l-arginine: 323, 345, 346, 348, 349, 354, 370, 379
binding magnesium ion: 348

Query Sequence

>WP_013074357.1 NCBI__GCF_000092905.1:WP_013074357.1
MCGIAGWIDWNVEMTEQRPVLKAMADVQYWRGPDAEGIWMSRRAGLAHRRLSIIDPEGGA
QPMIRRHGERTLVIVYNGELYNMAELQRELEGLGYTFATRCDTEVVLVAYAHWGPACVER
FNGIYAIGIWDEQSQELFLARDRLGVKPLFYAPLASGLVFASELKGLLAHPAVRPEVDSE
GLAEIFAMGPGRTPGHGVFRNTCEVKPGWALLFDRRGLHHRQYWKLESRPHEDDLETTIA
TVRDLLEDTVGRQLMSDVPVCTLLSGGLDSSAITAFAARAFRRQGRPPLRTFSIDYVDND
VYFQPNAFQPAADGPWAERVADFLQVDRRIVTLTPAAVADALREAVRARDLPGMTDIDSS
LLLFCREIKKEATVALSGECADEVFGGYPWFHRKEALEADVFPWSLKMRERISVLHPDFV
DHVQPEQYVRRRYREVLDAVPRLTGENPQDARIREMFYLNLFHWMPVLLDRKDRMSMAVG
LEVRVPFCDHRLVEYMWNVPWSIKMAAGREKGLLRLAMKGLLPDDALWRKKSPFPKTHHP
DFARACRSALQEVLVDSSSPLLPLIDVKSIHQWLQAEGEFDIPWFGQLMRLPQLFAYLVQ
VDQWLREYRVQIL

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