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 (= H29) mutation to A: 4,5-fold decrease in glutamine affinity.
D34 (= D33) mutation D->N,E: Little effect on the kinetic properties.
H81 (≠ F82) mutation to A: 5-fold decrease in glutamine affinity.
A105 (≠ H107) mutation to H: Little effect on the kinetic properties.
E349 (≠ V367) 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.

1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
33% identity, 58% coverage: 3:376/642 of query aligns to 2:341/497 of 1ct9A

query
sites
1ct9A

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S

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active site: L50 (= L52), N74 (= N76), G75 (= G77), T305 (≠ D343), R308 (≠ F346), E332 (≠ V367)
binding adenosine monophosphate: L232 (≠ F262), L233 (= L263), S234 (= S264), S239 (= S269), A255 (= A288), V256 (≠ I289), D263 (≠ E302), M316 (≠ V352), S330 (= S365), G331 (= G366), E332 (≠ V367)
binding glutamine: R49 (= R51), L50 (= L52), I52 (= I54), V53 (≠ I55), N74 (= N76), G75 (= G77), E76 (= E78), D98 (= D101)

Sites not aligning to the query:

active site: 1, 366
binding glutamine: 1

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)
30% identity, 59% coverage: 1:376/642 of query aligns to 1:365/557 of P78753

query
sites
P78753

M

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Sites not aligning to the query:

391 modified: Phosphoserine
489 modified: Phosphoserine

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)
30% identity, 59% coverage: 1:376/642 of query aligns to 1:374/561 of P08243

query
sites
P08243

M

M

C
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C

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x
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x
F

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Y

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 (≠ W219) to E: in dbSNP:rs1049674
F362 (≠ L364) 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)
31% identity, 58% coverage: 2:376/642 of query aligns to 1:361/509 of 6gq3A

query
sites
6gq3A

C
|
C

G

G

I

I

H
x
W

G

A

F

L

Y

F

R

G

F

S

D

D

G

D

R

-

A

C

V

L

E

S

R

V

A

Q

H

C

L

L

S

S

A

A

M

M

G

K

D

-

V

-

T

I

R

A

H

H

R

R

G

G

P

P

D

D

D

A

-

F

E

R

G

F

Q

E

H

N

I

V

E

N

P

G

G

Y

G

T

R

N

C

C

G

C

I

F

A

G

M

F

R

H

R
|
R

L
|
L

S

A

I
x
V

D

D

L

P

A

L

G

F

G

G

H

M

Q

Q

P

P

I

I

S

R

-

V

N

K

A

K

D

Y

D

P

T

Y

L

L

W

W

V

L

V

C

C
x
Y

N
|
N

G
|
G

E
|
E

I

I

Y

Y

N

N

F

H

R

K

E

K

L

M

R

Q

Q

Q

E

H

L

F

Q

E

A

-

R

-

G

-

Y

F

R

E

F

Y

K

Q

T

T

G

K

S
x
V

D
|
D

S

G

E

E

V

I

L

I

L

L

H

H

L

L

Y

Y

D

D

L

K

H

G

G

G

-

I

D

E

D

Q

F

T

V

I

H

C

R

M

L

L

D

D

G

G

M

V

F

F

N

A

F

F

A

V

L

L

W

L

D

D

A

T

R

A

R

N

Q

K

R

K

L

V

L

F

I

L

G

G

R

R

D

D

H

T

L

Y

G

G

V

V

K

R

P

P

L

L

Y

F

V

K

H

A

Q

M

S

T

A

E

-

D

S

G

L

F

L

L

A

A

F

V

A

C

T

S

E

E

A

A

K

K

A

G

L

L

L

V

A

T

L

L

P

K

-

H

G

S

M

A

Q

T

P

P

A

F

L

L

N

K

R

V

E

E

V

-

L

-

G

-

D

-

Y

-

L

-

H

-

L

-

G

P

Y

F

V

L

P

P

A

G

P

H

H

Y

S

E

M

V

F

-

A

-

G

-

I

L

R

D

K

L

L

K

P

P

P

N

A

G

T

K

L

V

L

A

S

S

V

V

D

E

A

M

Q

V

G

K

V

Y

R

H

E

H

W

C

R

R

Y

-

W

-

R

-

L

-

P

-

Q

-

T

-

V

-

D

D

R

V

T

F

V

P

G

G

-

F

E

E

A

I

E

E

W

T

V

V

E

K

-

N

R

N

I

L

R

R

A

I

G

L

M

F

E

N

A

N

A

A

V

V

Q

K

R

K

Q

R

M

L

V

M

A

T

D

D

V

R

P

R

I

I

G

G

A

C

F

L

L

L

S

S

G

G

V

L

D

D

S

S

A

L

V

V

V

A

A

A

Y

T

M

L

A

L

R

K

H

Q

S

L

D

K

Q

E

-

A

-

Q

-

V

-

Q

-

Y

P

P

I

L

R

Q

T

T

Y

F

A

A

I

I

G

G

F

M

E

E

G

D

G

S

E

P

A

-

E

-

Q

-

L

-

Y

-

N

-

E

D

L

L

P

L

Y

A

A

A

R

R

Q

K

V

V

A

A

G

D

L

H

F

I

G

G

T

S

E

E

H

H

R

Y

E

E

I

V

V

L

V

F

R

N

P

S

D

E

V

E

-

G

V

I

G

Q

L

A

L

L

P

D

R

E

L

V

L

I

W

F

H

S

M

L

D

E

-

T

-

Y

E

D

P

I

V
x
T

A

T

D

V

S
x
R

A

A

F

S

I

V

T

G

T

M

Y

Y

L

L

V

I

S

S

E

K

F

Y

A

I

R

R

R

K

-

N

-

T

D

D

V

S

K

V

V

V

I

I

L

F

S

S

G

G

V

E

G

G

G

S

D

D

E

E

L

L

F

T

G

Q

G

G

Y

Y

active site: W4 (≠ H5), L49 (= L52), N74 (= N76), G75 (= G77), T324 (≠ V341), R327 (≠ S344)
binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R51), V51 (≠ I54), V52 (≠ I55), Y73 (≠ C75), N74 (= N76), G75 (= G77), E76 (= E78), V95 (≠ S100), D96 (= D101)

1mb9A Beta-lactam synthetase complexed with atp (see paper)
31% identity, 54% coverage: 74:418/642 of query aligns to 68:378/485 of 1mb9A

query
sites
1mb9A

V

V

C

L

N
x
A

G
|
G

E

E

I

I

Y

Y

N

N

F

R

R

D

E

E

L

L

R

L

Q

S

E

V

L

L

Q

P

A

A

R

G

G

P

Y

-

R

-

F

-

K

A

T

P

G

E

S

G

D

D

S

A

E

E

V

L

L

V

L

L

H

R

L

L

-

L

-

E

-

R

Y

Y

D

D

L

L

H

H

G

A

D

F

D

R

F

L

V

V

H

N

R

-

L

-

D

-

G

-

M

-

F

G

N

R

F

F

A

A

L

T

W

V

D

V

A

R

R

T

R

G

Q

D

R

R

L

V

L

L

I

L

G

A

R

T

D

D

H

H

L

A

G

G

V

S

K

V

P

P

L

L

Y

Y

V

T

H

C

Q

V

S

A

A

P

S

G

L

E

L

V

A

R

F

A

A

S

T

T

E

E

A

A

K

K

A

A

L

L

L

A

A

A

L

F

P

P

G

-

M

-

Q

-

P

L

A

A

L

D

N

A

R

R

E

R

V

V

L

A

G

G

D

-

Y

-

L

-

H

-

L

-

G

-

Y

-

V

-

P

-

A

-

P

-

H

-

S

-

M

-

F

L

A

T

G

G

I

V

R

Y

K

Q

L

V

P

P

P

A

A

G

T

A

L

V

L

M

S

D

V

I

D

D

-

L

-

G

A

S

Q

G

G

T

V

A

R

V

E

T

W

H

R

R

Y

T

W

W

R

-

L

T

P

P

Q

G

T

L

V

S

D

R

R

R

T

I

V

L

G

P

E

E

A

G

E

E

W

A

V

V

E

A

R

A

I

V

R

R

A

A

G

A

M

L

E

E

A

K

A

A

V

V

-

A

Q

Q

R

R

Q

V

M

T

V

P

A

G

D

D

V

T

P

P

I

L

G

-

A

V

F
x
V

L
|
L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

S

S

A

G

V

V

V

A

A

A

Y

C

M

A

A

H

R

R

H

A

S

A

D

G

Q

E

P

-

I

L

R

D

T

T

Y

V

A
x
S

I
x
M

G

G

F

T

E

D

G

-

E

-

A

-

E

-

Q

-

L

T

Y

S

N

N

E

E

L

F

P

R

Y

E

A

A

R

R

Q

A

V

V

A

V

G

D

L

H

F

L

G

R

T

T

E

R

H

H

R

R

E

E

I

I

V

T

V

I

-

P

R

T

P

T

D

E

V

L

G

A

L

Q

L

L

P

P

R

Y

L

A

L

V

W

W

H

A

M

S

D

E

E

S

P

V

V

D

A

P

D
|
D

S

-

A

-

F

-

I

I

T

I

T

E

Y
|
Y

L

L

V

L

S

P

E
x
L

F

T

A

A

R

L

R

Y

D

R

V

A

-

L

-

D

-

G

-

P

-

E

K

R

V

R

I

I

L

L

S

T

G
|
G

V
x
Y

G

G

G

A

D
|
D

E

I

L

P

F

L

G

G

Y

M

R

-

Y

-

L

-

G

-

H

H

Y

R

L

E

D

D

K

R

L

L

A

P

R

A

L

L

P

D

L

T

W

V

S

L

R

A

R

H

L

D

M

M

A

A

R

T

T

F

A

D

G

G

L

L

L

-

P

-

S

-

D

N

R
x
E

H

M

S

S

K

P

V

V

L

L

N

S

T

T

L

L

active site: A70 (≠ N76), G71 (= G77), D310 (= D343), Y336 (≠ V367), E370 (≠ R410)
binding adenosine monophosphate: V235 (≠ F262), L236 (= L263), S242 (= S269), S260 (≠ A288), M261 (≠ I289), Y314 (= Y350), L318 (≠ E354), G335 (= G366), Y336 (≠ V367)
binding adenosine-5'-triphosphate: V235 (≠ F262), L236 (= L263), S237 (= S264), G239 (= G266), D241 (= D268), S242 (= S269), S260 (≠ A288), M261 (≠ I289), L318 (≠ E354), G335 (= G366), D339 (= D370)
binding magnesium ion: D241 (= D268), D339 (= D370)
binding pyrophosphate 2-: S237 (= S264), G239 (= G266), D241 (= D268), S242 (= S269), D339 (= D370)

Sites not aligning to the query:

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

1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
31% identity, 54% coverage: 74:418/642 of query aligns to 63:374/491 of 1mc1A

query
sites
1mc1A

V

V

C

L

N
x
A

G
|
G

E

E

I

I

Y

Y

N

N

F

R

R

D

E

E

L

L

R

L

Q

S

E

V

L

L

Q

P

A

A

R

G

G

P

Y

-

R

-

F

-

K

A

T

P

G

E

S

G

D

D

S

A

E

E

V

L

L

V

L

L

H

R

L

L

-

L

-

E

-

R

Y

Y

D

D

L

L

H

H

G

A

D

F

D

R

F

L

V

V

H

N

R

-

L

-

D

-

G

-

M

-

F

G

N

R

F

F

A

A

L

T

W

V

D

V

A

R

R

T

R

G

Q

D

R

R

L

V

L

L

I

L

G

A

R

T

D

D

H

H

L

A

G

G

V

S

K

V

P

P

L

L

Y

Y

V

T

H

C

Q

V

S

A

A

P

S

G

L

E

L

V

A

R

F

A

A

S

T

T

E

E

A

A

K

K

A

A

L

L

L

A

A

A

L

-

P

-

G

G

M

F

Q

P

P

L

A

A

L

D

N

A

R

R

E

R

V

V

L

A

G

G

D

-

Y

-

L

-

H

-

L

-

G

-

Y

-

V

-

P

-

A

-

P

-

H

-

S

-

M

-

F

L

A

T

G

G

I

V

R

Y

K

Q

L

V

P

P

P

A

A

G

T

A

L

V

L

M

S

D

V

I

D

D

-

L

-

G

A

S

Q

G

G

T

V

A

R

V

E

T

W

H

R

R

Y

T

W

W

R

-

L

T

P

P

Q

G

T

L

V

S

D

R

R

R

T

I

V

L

G

P

E

E

A

G

E

E

W

A

V

V

E

A

R

A

I

V

R

R

A

A

G

A

M

L

E

E

A

K

A

A

V

V

-

A

Q

Q

R

R

Q

V

M

T

V

P

A

G

D

D

V

T

P

P

I

L

G

-

A

V

F
x
V

L

L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

S

S

A

G

V

V

V

A

A

A

Y

C

M

A

A

H

R

R

H

A

S

A

D

G

Q

E

P

-

I

L

R

D

T

T

Y

V

A
x
S

I
x
M

G

G

F

T

E

D

G

-

E

-

A

-

E

-

Q

-

L

T

Y

S

N

N

E

E

L

F

P

R

Y

E

A

A

R

R

Q

A

V

V

A

V

G

D

L

H

F

L

G

R

T

T

E

R

H

H

R

R

E

E

I

I

V

T

V

I

-

P

R

T

P

T

D

E

V

L

G

A

L

Q

L

L

P

P

R

Y

L

A

L

V

W

W

H

A

M

S

D

E

E

S

P

V

V

D

A

P

D
|
D

S

-

A

-

F

-

I

I

T

I

T

E

Y
|
Y

L

L

V

L

S

P

E

L

F

T

A

A

R

L

R

Y

D

R

V

A

-

L

-

D

-

G

-

P

-

E

K

R

V

R

I

I

L

L

S

T

G
|
G

V
x
Y

G
|
G

G

A

D
|
D

E
x
I

L

P

F

L

G

G

Y

M

R

-

Y

-

L

-

G

-

H

H

Y

R

L

E

D

D

K

R

L

L

A

P

R

A

L

L

P

D

L

T

W

V

S

L

R

A

R

H

L
x
D

M

M

A

A

R

T

T

F

A

D

G

G

L

L

L

-

P

-

S

-

D

N

R
x
E

H

M

S

S

K

P

V

V

L

L

N

S

T

T

L

L

active site: A65 (≠ N76), G66 (= G77), D306 (= D343), Y332 (≠ V367), E366 (≠ R410)
binding adenosine monophosphate: V231 (≠ F262), S233 (= S264), S238 (= S269), S256 (≠ A288), M257 (≠ I289), G331 (= G366)
binding magnesium ion: D237 (= D268), D335 (= D370)
binding deoxyguanidinoproclavaminic acid: Y310 (= Y350), Y332 (≠ V367), G333 (= G368), I336 (≠ E371), D357 (≠ L398), E366 (≠ R410)
binding pyrophosphate 2-: S233 (= S264), G235 (= G266), D237 (= D268), S238 (= S269), D335 (= D370)

Sites not aligning to the query:

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

1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
31% identity, 54% coverage: 74:418/642 of query aligns to 67:379/496 of 1mbzA

query
sites
1mbzA

V

V

C

L

N
x
A

G
|
G

E

E

I

I

Y

Y

N

N

F

R

R

D

E

E

L

L

R

L

Q

S

E

V

L

L

Q

P

A

A

R

G

G

P

Y

-

R

-

F

-

K

A

T

P

G

E

S

G

D

D

S

A

E

E

V

L

L

V

L

L

H

R

L

L

-

L

-

E

-

R

Y

Y

D

D

L

L

H

H

G

A

D

F

D

R

F

L

V

V

H

N

R

-

L

-

D

-

G

-

M

-

F

G

N

R

F

F

A

A

L

T

W

V

D

V

A

R

R

T

R

G

Q

D

R

R

L

V

L

L

I

L

G

A

R

T

D

D

H

H

L

A

G

G

V

S

K

V

P

P

L

L

Y

Y

V

T

H

C

Q

V

S

A

A

P

S

G

L

E

L

V

A

R

F

A

A

S

T

T

E

E

A

A

K

K

A

A

L

L

L

A

A

A

L

H

P

-

G

G

M

F

Q

P

P

L

A

A

L

D

N

A

R

R

E

R

V

V

L

A

G

G

D

-

Y

-

L

-

H

-

L

-

G

-

Y

-

V

-

P

-

A

-

P

-

H

-

S

-

M

-

F

L

A

T

G

G

I

V

R

Y

K

Q

L

V

P

P

P

A

A

G

T

A

L

V

L

M

S

D

V

I

D

D

-

L

-

G

A

S

Q

G

G

T

V

A

R

V

E

T

W

H

R

R

Y

T

W

W

R

-

L

T

P

P

Q

G

T

L

V

S

D

R

R

R

T

I

V

L

G

P

E

E

A

G

E

E

W

A

V

V

E

A

R

A

I

V

R

R

A

A

G

A

M

L

E

E

A

K

A

A

V

V

-

A

Q

Q

R

R

Q

V

M

T

V

P

A

G

D

D

V

T

P

P

I

L

G

-

A

V

F
x
V

L
|
L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

S

S

A

G

V

V

V

A

A

A

Y

C

M

A

A

H

R

R

H

A

S

A

D

G

Q

E

P

-

I

L

R

D

T

T

Y

V

A
x
S

I
x
M

G

G

F

T

E

D

G

-

E

-

A

-

E

-

Q

-

L

T

Y

S

N

N

E

E

L

F

P

R

Y

E

A

A

R

R

Q

A

V

V

A

V

G

D

L

H

F

L

G

R

T

T

E

R

H

H

R

R

E

E

I

I

V

T

V

I

-

P

R

T

P

T

D

E

V

L

G

A

L

Q

L

L

P

P

R

Y

L

A

L

V

W

W

H

A

M

S

D

E

E

S

P

V

V

D

A

P

D
|
D

S

-

A

-

F

-

I

I

T

I

T

E

Y
|
Y

L

L

V

L

S

P

E
x
L

F

T

A

A

R

L

R

Y

D

R

V

A

-

L

-

D

-

G

-

P

-

E

K

R

V

R

I

I

L

L

S

T

G
|
G

V
x
Y

G
|
G

G

A

D
|
D

E
x
I

L

P

F

L

G

G

Y

M

R

-

Y

-

L

-

G

-

H

H

Y

R

L

E

D

D

K

R

L

L

A

P

R

A

L

L

P

D

L

T

W

V

S

L

R

A

R

H

L
x
D

M

M

A

A

R

T

T

F

A

D

G

G

L

L

L

-

P

-

S

-

D

N

R
x
E

H

M

S

S

K

P

V

V

L

L

N

S

T

T

L

L

active site: A69 (≠ N76), G70 (= G77), D311 (= D343), Y337 (≠ V367), E371 (≠ R410)
binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ F262), L237 (= L263), S238 (= S264), S243 (= S269), S261 (≠ A288), M262 (≠ I289), Y315 (= Y350), L319 (≠ E354), G336 (= G366), Y337 (≠ V367), G338 (= G368), D340 (= D370), I341 (≠ E371), D362 (≠ L398), E371 (≠ R410)
binding magnesium ion: D242 (= D268), D340 (= D370)
binding pyrophosphate 2-: S238 (= S264), G240 (= G266), D242 (= D268), S243 (= S269), D340 (= D370)

Sites not aligning to the query:

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

1jgtB Crystal structure of beta-lactam synthetase (see paper)
31% identity, 54% coverage: 74:418/642 of query aligns to 71:387/500 of 1jgtB

query
sites
1jgtB

V

V

C

L

N
x
A

G
|
G

E

E

I

I

Y

Y

N

N

F

R

R

D

E

E

L

L

R

L

Q

S

E

V

L

L

Q

P

A

A

R

G

G

P

Y

-

R

-

F

-

K

A

T

P

G

E

S

G

D

D

S

A

E

E

V

L

L

V

L

L

H

R

L

L

-

L

-

E

-

R

Y

Y

D

D

L

L

H

H

G

A

D

F

D

R

F

L

V

V

H

N

R

-

L

-

D

-

G

-

M

-

F

G

N

R

F

F

A

A

L

T

W

V

D

V

A

R

R

T

R

G

Q

D

R

R

L

V

L

L

I

L

G

A

R

T

D

D

H

H

L

A

G

G

V

S

K

V

P

P

L

L

Y

Y

V

T

H

C

Q

V

S

A

A

P

S

G

L

E

L

V

A

R

F

A

A

S

T

T

E

E

A

A

K

K

A

A

L

L

L

A

A

A

-

H

-

R

-

D

L

P

P

K

G

G

M

F

Q

P

P

L

A

A

L

D

N

A

R

R

E

R

V

V

L

A

G

G

D

-

Y

-

L

-

H

-

L

-

G

-

Y

-

V

-

P

-

A

-

P

-

H

-

S

-

M

-

F

L

A

T

G

G

I

V

R

Y

K

Q

L

V

P

P

P

A

A

G

T

A

L

V

L

M

S

D

V

I

D

D

-

L

-

G

A

S

Q

G

G

T

V

A

R

V

E

T

W

H

R

R

Y

T

W

W

R

-

L

T

P

P

Q

G

T

L

V

S

D

R

R

R

T

I

V

L

G

P

E

E

A

G

E

E

W

A

V

V

E

A

R

A

I

V

R

R

A

A

G

A

M

L

E

E

A

K

A

A

V

V

-

A

Q

Q

R

R

Q

V

M

T

V

P

A

G

D

D

V

T

P

P

I

L

G

-

A

V

F
x
V

L
|
L

S
|
S

G

G

G
|
G

V
x
I

D
|
D

S
|
S

S

S

A

G

V

V

V

A

A

A

Y

C

M

A

A

H

R

R

H

A

S

A

D

G

Q

E

P

-

I

L

R

D

T

T

Y

V

A
x
S

I
x
M

G

G

F

T

E

D

G

-

E

-

A

-

E

-

Q

-

L

T

Y

S

N

N

E

E

L

F

P

R

Y

E

A

A

R

R

Q

A

V

V

A

V

G

D

L

H

F

L

G

R

T

T

E

R

H

H

R

R

E

E

I

I

V

T

V

I

-

P

R

T

P

T

D

E

V

L

G

A

L

Q

L

L

P

P

R

Y

L

A

L

V

W

W

H

A

M

S

D

E

E

S

P

V

V

D

A

P

D
|
D

S

-

A

-

F

-

I

I

T

I

T

E

Y
|
Y

L

L

V

L

S

P

E
x
L

F

T

A

A

R

L

R

Y

D

R

V

A

-

L

-

D

-

G

-

P

-

E

K

R

V

R

I

I

L

L

S

T

G
|
G

V
x
Y

G
|
G

G

A

D
|
D

E
x
I

L

P

F

L

G

G

Y
x
M

R

-

Y

-

L

-

G

-

H

H

Y

R

L

E

D

D

K

R

L

L

A

P

R

A

L

L

P

D

L

T

W

V

S

L

R

A

R

H

L
x
D

M

M

A

A

R

T

T

F

A

D

G

G

L

L

L

-

P

-

S

-

D

N

R
x
E

H

M

S

S

K

P

V

V

L

L

N

S

T

T

L

L

active site: A73 (≠ N76), G74 (= G77), D319 (= D343), Y345 (≠ V367), E379 (≠ R410)
binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ F262), L245 (= L263), S246 (= S264), G248 (= G266), I249 (≠ V267), D250 (= D268), S251 (= S269), S269 (≠ A288), M270 (≠ I289), L327 (≠ E354), G344 (= G366), Y345 (≠ V367), D348 (= D370)
binding n2-(carboxyethyl)-l-arginine: Y323 (= Y350), Y345 (≠ V367), G346 (= G368), D348 (= D370), I349 (≠ E371), M354 (≠ Y376), D370 (≠ L398), E379 (≠ R410)
binding magnesium ion: D250 (= D268), D348 (= D370)

Sites not aligning to the query:

active site: 440
binding diphosphomethylphosphonic acid adenosyl ester: 420, 440

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)
29% identity, 33% coverage: 259:467/642 of query aligns to 241:457/503 of Q9XB61

query
sites
Q9XB61

I

V

G

G

A

I

F
x
P

L
|
L

S
|
S

G
|
G

V
x
L

D
|
D

S
|
S

S

S

A

L

V

V

V

T

A

A

Y

L

M

A

A

S

R

R

H

H

S

F

D

-

Q

K

P

K

I

L

R

N

T

T

Y

Y

A

S

I
|
I

G

G

F

T

E

E

G

-

E

-

A

-

E

-

Q

-

L

L

Y

S

N

N

E

E

L

F

P

E

Y

F

A

S

R

Q

Q

Q

V

V

A

A

G

D

L

A

F

L

G

G

T

T

E

H

H

H

R

Q

-

M

E

K

I

I

V

L

V

S

R

E

P

T

D

E

V

V

V

I

G

N

L

G

L

I

P

I

R

E

L

S

L

I

W

Y

H

Y

M

N

D

E

E

I

P

F

V

D

A

G

D

L

S

S

A

A

F

E

I

I

T

Q

T

S

Y

G

L

L

V

F

S

N

E

V

F

Y

-

R

-

Q

A

A

R

Q

R

G

D

Q

V

V

K

S

V

C

I

M

L

L

S

T

G
|
G

V
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

-

D

-

N

-

P

-

N

-

Q

-

L

-

A

-

E

-
x
Q

-

V

Y

Y

R
|
R

R

T

Y

R

L

W

G

T

G

G

H
x
E

Y

F

L

A

D

T

K

H

L

G

A

A

-

S

-

C

-

Y

-

G

-

I

-

D

-

I

R

R

L

H

P

P

L

F

W

W

S

S

R

H

R

S

L

L

M

I

A

S

R

L

T

C

A

H

G

A

L

L

L

H

P

P

S

D

D

Y

R

K

-

I

-

F

H

D

S

N

K

E

V

V

L
x
K

N

N

T

I

L

L

R

R

L

-

A

-

R

-

G

-

L

-

A

-

S

-

E

-

L

-

A

-

P

-

D

-

R

E

Y

Y

R

A

H

D

Y

S

L

L

Q

Q

V

L

L

L

P

P

R

K

D

D

D

I

V

V

A

W

A

R

L

K

T
x
K

R
x
I

G
|
G

Q
x
I

P

H

G

E

G

G

S

S

D

-

A

S

L

V

A

N

A

Q

A

A

F

F

A

A

244:251 (vs. 262:269, 75% identical) binding ATP
I270 (= I289) binding ATP
GYGSD 344:348 (≠ GVGGD 366:370) binding ATP
Y345 (≠ V367) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
G346 (= G368) binding substrate
Q371 (vs. gap) binding substrate
R374 (= R377) binding substrate
E380 (≠ H383) mutation to A: Loss of activity.; mutation to D: Reduces catalytic efficiency.; mutation to Q: Reduces catalytic efficiency.
K421 (≠ L415) binding ATP
K443 (≠ T452) mutation K->A,M: Loss of activity.
IGI 444:446 (≠ RGQ 453:455) binding ATP

1q19A Carbapenam synthetase (see paper)
29% identity, 33% coverage: 259:467/642 of query aligns to 240:456/500 of 1q19A

query
sites
1q19A

I

V

G

G

A

I

F
x
P

L
|
L

S
|
S

G

G

V

L

D
|
D

S
|
S

S

S

A

L

V

V

V

T

A

A

Y

L

M

A

A

S

R

R

H

H

S

F

D

-

Q

K

P

K

I

L

R

N

T

T

Y

Y

A
x
S

I
|
I

G

G

F

T

E

E

G

-

E

-

A

-

E

-

Q

-

L

L

Y

S

N

N

E

E

L

F

P

E

Y

F

A

S

R

Q

Q

Q

V

V

A

A

G

D

L

A

F

L

G

G

T

T

E

H

H

H

R

Q

-

M

E

K

I

I

V

L

V

S

R

E

P

T

D

E

V

V

V

I

G

N

L

G

L

I

P

I

R

E

L

S

L

I

W

Y

H

Y

M

N

D

E

E

I

P

F

V

D

A

G

D
x
L

S

S

A

A

F
x
E

I

I

T

Q

T

S

Y

G

L

L

V

F

S

N

E

V

F

Y

-

R

-

Q

A

A

R

Q

R

G

D

Q

V

V

K

S

V

C

I

M

L

L

S
x
T

G
|
G

V
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

-

D

-

N

-

P

-

N

-

Q

-

L

-

A

-

E

-

Q

-

V

Y

Y

R
|
R

R

T

Y

R

L

W

G

T

G

G

H
x
E

Y

F

L

A

D

T

K

H

L

G

A

A

-

S

-

C

-

Y

-

G

-

I

-

D

-

I

R

R

L

H

P

P

L

F

W

W

S

S

R

H

R

S

L

L

M

I

A

S

R

L

T

C

A

H

G

A

L

L

L

H

P

P

S

D

D

Y

R

K

-

I

-

F

H

D

S

N

K

E

V

V

L

K

N

N

T

I

L

L

R

R

L

-

A

-

R

-

G

-

L

-

A

-

S

-

E

-

L

-

A

-

P

-

D

-

R

E

Y

Y

R

A

H

D

Y

S

L

L

Q

Q

V

L

L

L

P

P

R

K

D

D

D

I

V

V

A

W

A

R

L

K

T
x
K

R
x
I

G
|
G

Q
x
I

P

H

G

E

G

G

S

S

D

-

A

S

L

V

A

N

A

Q

A

A

F

F

A

A

active site: L318 (≠ D343), E321 (≠ F346), Y344 (≠ V367), E379 (≠ H383), K442 (≠ T452)
binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ F262), L244 (= L263), S245 (= S264), D249 (= D268), S250 (= S269), S268 (≠ A288), I269 (= I289), T342 (≠ S365), G343 (= G366), D347 (= D370), K442 (≠ T452), I443 (≠ R453), G444 (= G454), I445 (≠ Q455)
binding (2s,5s)-5-carboxymethylproline: Y344 (≠ V367), G345 (= G368), L348 (≠ E371), R373 (= R377), E379 (≠ H383)

Sites not aligning to the query:

active site: 56

6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
25% identity, 29% coverage: 70:258/642 of query aligns to 96:282/460 of 6lbpA

query
sites
6lbpA

T

S

L

V

W

G

V

V

V

A

C

H

N
|
N

G
|
G

E

N

I

L

Y

V

N

N

F

Y

R

T

E

K

L

L

R

R

Q

A

E

D

L

L

Q

E

A

E

R

N

G

G

Y

S

R

I

F

F

K

N

T

T

G

S

S

S

D

D

S

T

E

E

V

V

L

V

L

L

H

H

L

L

-

I

-

A

-

I

-

S

-

K

-

A

-

R

-

P

Y

F

D

F

L

M

H

R

G

I

D

V

D

D

F

A

V

C

H

E

R

K

L

L

D

Q

G

G

M

A

F

Y

N

S

F

M

A

V

L

F

W

-

D

-

A

V

R

T

R

E

Q

D

R

K

L

L

L

V

I

A

G

V

R

R

D

D

H

P

L

H

G

G

V

F

K

R

P

P

L

L

Y

V

V

M

-

G

H

R

Q

R

S

S

A

N

S

G

L

A

L

V

A

V

F

F

A

A

T

S

E

E

A

T

K

C

A

A

L

L

L

-

A

-

L

-

P

-

G

-

M

-

Q

-

P

-

A

-

L

-

N

-

R

-

E

-

V

-

L

-

G

-

D

D

Y

L

L

I

H

E

L

A

G

T

Y

Y

V

E

P

-

A

-

P

-

H

-

S

-

M

-

F

-

A

-

G

-

I

-

R

R

K

E

L

V

P

Y

P

P

A

G

T

E

L

V

L

L

S

V

V

V

D

D

A

K

Q

D

G

G

V

V

R

K

-

C

-

Q

-

C

-

L

-

M

-

P

-

H

-

P

-

E

-

P

-

K

-

Q

-
x
C

-

I

-
x
F

E

E

W

H

R

I

Y
|
Y

W

F

R

S

L

L

P

P

Q

N

T

S

V

I

-

V

-

F

D

G

R

R

T

S

V

V

G

Y

E

E

A

S

E

R

W

H

V

V

E

F

R

G

I

E

R

I

A

L

G

A

M

T

E

E

A

S

A

P

V

V

Q

D

R

C

Q

D

M

V

V

V

A

I

D

A

V

V

P

P

active site: N102 (= N76), G103 (= G77), Y243 (= Y221)
binding iron/sulfur cluster: C237 (vs. gap), F239 (vs. gap)

Sites not aligning to the query:

active site: 1, 27, 301, 306, 316, 424
binding iron/sulfur cluster: 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)
25% identity, 29% coverage: 70:258/642 of query aligns to 182:368/561 of Q9STG9

query
sites
Q9STG9

T

S

L

V

W

G

V

V

V

A

C
x
H

N

N

G

G

E

N

I

L

Y

V

N

N

F

Y

R

T

E

K

L

L

R

R

Q

A

E

D

L

L

Q

E

A

E

R

N

G

G

Y

S

R

I

F

F

K

N

T

T

G

S

S

S

D

D

S

T

E

E

V

V

L

V

L

L

H

H

L

L

-

I

-

A

-

I

-

S

-

K

-

A

-

R

-

P

Y

F

D

F

L

M

H

R

G

I

D

V

D

D

F

A

V

C

H

E

R

K

L

L

D

Q

G

G

M

A

F

Y

N

S

F

M

A

V

L

F

W

-

D

-

A

V

R

T

R

E

Q

D

R

K

L

L

L

V

I

A

G

V

R

R

D

D

H

P

L

H

G

G

V

F

K
x
R

P
|
P

L

L

Y

V

V

M

-

G

H

R

Q

R

S

S

A

N

S

G

L

A

L

V

A

V

F

F

A

A

T

S

E

E

A

T

K

C

A

A

L

L

L

-

A

-

L

-

P

-

G

-

M

-

Q

-

P

-

A

-

L

-

N

-

R

-

E

-

V

-

L

-

G

-

D

D

Y

L

L

I

H

E

L

A

G

T

Y

Y

V

E

P

-

A

-

P

-

H

-

S

-

M

-

F

-

A

-

G

-

I

-

R

R

K

E

L

V

P

Y

P

P

A

G

T

E

L

V

L

L

S

V

V

V

D

D

A

K

Q

D

G

G

V

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R

K

-

C

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Q

-

C

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L

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M

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P

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P

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C

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-

F

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E

W

H

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Y

W

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L

L

P

P

Q

N

T

S

V

I

-

V

-

F

D

G

R

R

T

S

V

V

G

Y

E

E

A

S

E

R

W

H

V

V

E

F

R

G

I

E

R

I

A

L

G

A

M

T

E

E

A

S

A

P

V

V

Q

D

R

C

Q

D

M

V

V

V

A

I

D

A

V

V

P

P

H187 (≠ C75) 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

>WP_011766994.1 NCBI__GCF_000061505.1:WP_011766994.1
MCGIHGFYRFDGRAVERAHLSAMGDVTRHRGPDDEGQHIEPGGRCGIAMRRLSIIDLAGG
HQPISNADDTLWVVCNGEIYNFRELRQELQARGYRFKTGSDSEVLLHLYDLHGDDFVHRL
DGMFNFALWDARRQRLLIGRDHLGVKPLYVHQSASLLAFATEAKALLALPGMQPALNREV
LGDYLHLGYVPAPHSMFAGIRKLPPATLLSVDAQGVREWRYWRLPQTVDRTVGEAEWVER
IRAGMEAAVQRQMVADVPIGAFLSGGVDSSAVVAYMARHSDQPIRTYAIGFEGGEAEQLY
NELPYARQVAGLFGTEHREIVVRPDVVGLLPRLLWHMDEPVADSAFITTYLVSEFARRDV
KVILSGVGGDELFGGYRRYLGGHYLDKLARLPLWSRRLMARTAGLLPSDRHSKVLNTLRL
ARGLLASSELAPDDRYRHYLQVLPRDDVAALTRGQPGGSDALAAAFAAAGNDDALNRMFA
VDAETQLPDDLLLLTDKMSMAVSLECRVPLLDRALVELAASIPESLKVRNGRLKHLMKSA
LADVLPPDILDRRKRGFGTPMGAWLKQQLAPVLRRLLAADVVRDRGLFDPAVVARLVADH
EAARIDGTDALLALMNLEIWSRVHLDRHSVDDVTAELKSLIA

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