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 (≠ P29) mutation to A: 4,5-fold decrease in glutamine affinity.
D34 (= D33) mutation D->N,E: Little effect on the kinetic properties.
H81 (≠ Y81) mutation to A: 5-fold decrease in glutamine affinity.
A105 (≠ K106) mutation to H: Little effect on the kinetic properties.
E349 (≠ Q371) 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)
26% identity, 84% coverage: 23:526/601 of query aligns to 24:468/557 of P78753

query
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P78753

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S391 (≠ D446) modified: Phosphoserine

Sites not aligning to the query:

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)
25% identity, 94% coverage: 1:563/601 of query aligns to 1:514/561 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 (≠ E231) to E: in dbSNP:rs1049674
F362 (≠ Q368) 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)
25% identity, 91% coverage: 16:563/601 of query aligns to 14:488/509 of 6gq3A

query
sites
6gq3A

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L

G

G

R

R

D

D

R

T

L

Y

G

G

I

V

K

R

P

P

L

L

Y

F

L

K

T

A

R

M

T

T

A

E

D

D

R

G

V

F

R

L

F

A

A

V

S

C

S

S

L

E

P

-

A

-

L

-

A

A

G

K

G

G

E

L

V

V

D

T

T

L

R

K

I

-

D

-

P

-

V

-

A

-

L

-

H

-

Y

-

M

-

T

-

F

-

H

H

S

S

V

A

V

T

P

P

A

F

P

L

R

K

T

-

I

-

L

-

R

-

G

-

V

V

E

E

K

P

L

F

P

L

P

P

A

G

S

H

L

Y

T

E

A

V

I

L

E

D

-

L

-

K

P

P

D

N

G

G

R

K

I

V

T

A

T

S

T

V

T

E

Y

M

W

V

E

K

P

Y

D

H

F

H

S

C

R

R

R

-

E

D

E

V

R

F

A

P

G

G

W

F

S

E

E

I

K

E

D

T

W

V

E

K

D

N

A

N

V

L

L

R

E

I

S

L

L

F

R

N

V

N

A

A

V

V

K

K

R

K

R

R

L

L

V

M

A

T

D

D

V

R

P

R

V

I

G

G

C

C

L

L

S

S

G

G

V

L

D

D

S

S

L

L

I

V

V

A

G

A

L

T

L

L

A

L

E

K

-

Q

-

L

-

K

-

E

-

A

A

Q

G

V

Q

Q

H

Y

G

P

L

L

A

Q

T

T

F

F

S

A

I

I

G

G

F

M

E

E

S

D

V

S

G

P

G

D

V

L

A

L

G

A

D

-

E

-

F

-

K

-

Y

-

S

A

D

R

I

K

I

V

A

A

D

D

R

H

F

I

G

G

T

S

D

E

H

H

H

Y

Q

E

I

V

R

L

I

F

G

N

T

S

E

E

R

E

M

G

L

I

P

Q

A

A

L

L

G

D

G

E

A

V

I

I

G

F

A

S

M

L

S

E

E

T

P

Y

M

D

V

I

S
x
T

-

T

-

V

H
x
R

D

A

C

S

V

V

A

G

F

M

Y

Y

L

L

L

I

S

S

Q

K

E

Y

V

I

A

R

K

K

H

N

V

T

K

D

-

S

-

V

V

V

V

I

Q

F

S

S

G

G

Q

E

G

G

A

S

D

D

E

E

V

L

F

T

A

Q

G

G

Y

Y

H

I

W

Y

Y

F

P

H

P

K

M

A

G

P

E

S

P

P

A

E

A

K

A

A

S

E

V

E

E

E

G

S

S

E

V

R

A

L

S

L

Y

R

R

E

A

L

A

Y

F

L

F

F

D

D

R

-

D

-

R

-

D

-

G

-

Y

-

A

-

D

-

I

-

V

-

S

-

P

-

G

-

Y

-

L

-

A

-

D

-

P

-

S

-

E

-

L

-

F

-

V

-

T

-

E

-

H

-

F

-

A

-

R

-

P

-

G

-

A

-

Q

-

T

-

G

-

V

-

D

-

R

-

A

V

L

L

R

R

L

A

D

D

T

R

T

T

V

-

M

-

L

-

V

-

D

-

P

-

V

-

K

-

R

-

V

-

D

-

N

-

M

-

T

T

M

A

A

A

W

H

G

G

L

L

E

E

G

L

R

R

V

V

P

P

F

F

L

L

D

D

H

H

E

R

L

F

V

S

E

S

L

Y

A

Y

A

L

T

S

C

L

P

P

Q

E

L

M

K

R

T

I

A

P

H

K

D

N

G

G

-

I

-

E

K

K

G

H

V

L

L

L

K

R

Q

E

A

T

A

F

R

E

-

D

-

S

Q

N

V

L

I

I

P

P

S

K

E

E

V

I

I

L

D

W

R

R

P

P

K

-

G

S

Y

W

F

F

P

K

V

I

P

-

A

-

L

-

T

-

H

-

L

L

E

Q

G

E

P

Y

Y

V

L

E

E

H

L

Q

V

V

R

D

D

D

A

A

L

M

Y

M

A

A

P

N

A

A

K

Q

E

K

R

F

G

P

L

F

F

N

R

T

P

P

D

K

A

T

V

K

E

E

active site: L49 (= L50), N74 (= N75), G75 (= G76), T324 (≠ S347), R327 (≠ H348)
binding 5-oxo-l-norleucine: R48 (= R49), V51 (≠ I52), V52 (≠ I53), Y73 (≠ W74), N74 (= N75), G75 (= G76), E76 (≠ C77), V95 (≠ S99), D96 (= D100)

Sites not aligning to the query:

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

1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 52% coverage: 71:381/601 of query aligns to 69:355/500 of 1jgtB

query
sites
1jgtB

T

T

I

A

A

V

W

L

N
x
A

G
|
G

C

E

I

I

Y

Y

N

N

Y

R

E

D

Q

E

L

L

R

L

D

S

E

V

L

L

S

P

G

A

H

G

G

P

Y

A

R

-

F

-

S

P

H

E

S

G

D

D

T

A

E

E

V

L

L

V

L

L

K

R

G

L

Y

L

H

E

H

R

W

Y

G

D

D

L

R

H

F

A

V

F

D

R

H

L

L

V

K

N

G

G

M

R

F

F

A

A

F

T

A

V

I

V

V

-

E

-

R

R

D

T

S

G

G

D

R

R

V

V

L

L

G

A

R

T

D

D

R

H

L

A

G

G

I

S

K

V

P

P

L

L

Y

Y

L

T

T

C

R

V

T

A

A

P

D

G

R

E

V

V

R

R

F

A

A

S

S

T

S

E

L

A

P

K

A

A

L

L

L

A

A

A

G

-

E

H

V

R

D

D

T

P

R

K

I

G

D

F

P

P

V

L

A

A

L

D

H

A

H

R

Y

R

M

V

T

A

F

G

H

-

S

-

V

-

P

-

A

-

P

-

R

-

T

-

I

-

L

L

R

T

G

G

V

V

E

Y

K

Q

L

V

P

P

P

A

A

G

S

A

L

V

T

M

A

D

I

I

E

D

-

L

P

G

D

S

G

G

R

T

I

A

T

V

T

T

T

H

T

R

Y

T

W

W

E

T

P

P

D

G

F

L

S

S

R

R

E

I

E

-

R

-

A

-

G

-

W

L

S

P

E

E

K

G

D

E

W

A

E

V

D

A

A

A

V

V

L

R

E

A

S

A

L

L

R

E

V

K

A

A

V

V

K

A

R

Q

R

R

L

V

V

T

-

P

A

G

D

D

V

T

P

P

V

L

G

-

C

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

V

A

G

A

L

C

L

A

A

H

E

R

A

A

G

A

Q

G

H

E

G

-

L

L

A

D

T

T

F

V

S
|
S

I
x
M

G

G

F

T

E

D

S

T

V

-

G

-

V

-

A

-

G

S

D

N

E

E

F

F

K

R

Y

E

S

A

D

R

I

A

I

V

A

V

D

D

R

H

F

L

G

R

T

T

D

R

H

H

H

R

Q

E

I

I

R

T

I

I

G

P

T

T

E

T

R

E

M

L

L

L

P

A

A

Q

L

L

G

P

G

Y

A

A

I

V

G

W

A

A

M

S

S

E

E

S

P

-

M

-

V

V

S

D

H

P

D
|
D

C

I

V

I

A

E

F
x
Y

Y

L

L

L

-

P

-
x
L

-

T

-

A

L

L

S

Y

Q

R

E

A

V

L

A

D

K

G

H

P

V

E

K

R

V

R

V

I

Q

L

S

T

G
|
G

Q
x
Y

G
|
G

A

A

D
|
D

E
x
I

V

P

F

L

A

G

G

G

Y
x
M

H

H

active site: A73 (≠ N75), G74 (= G76), D319 (= D349), Y345 (≠ Q371)
binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L266), L245 (= L267), S246 (= S268), G248 (= G270), I249 (≠ V271), D250 (= D272), S251 (= S273), S269 (= S292), M270 (≠ I293), L327 (vs. gap), G344 (= G370), Y345 (≠ Q371), D348 (= D374)
binding n2-(carboxyethyl)-l-arginine: Y323 (≠ F353), Y345 (≠ Q371), G346 (= G372), D348 (= D374), I349 (≠ E375), M354 (≠ Y380)
binding magnesium ion: D250 (= D272), D348 (= D374)

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)
27% identity, 52% coverage: 71:381/601 of query aligns to 61:342/491 of 1mc1A

query
sites
1mc1A

T

T

I

A

A

V

W

L

N
x
A

G
|
G

C

E

I

I

Y

Y

N

N

Y

R

E

D

Q

E

L

L

R

L

D

S

E

V

L

L

S

P

G

A

H

G

G

P

Y

A

R

-

F

-

S

P

H

E

S

G

D

D

T

A

E

E

V

L

L

V

L

L

K

R

G

L

Y

L

H

E

H

R

W

Y

G

D

D

L

R

H

F

A

V

F

D

R

H

L

L

V

K

N

G

G

M

R

F

F

A

A

F

T

A

V

I

V

V

-

E

-

R

R

D

T

S

G

G

D

R

R

V

V

L

L

G

A

R

T

D

D

R

H

L

A

G

G

I

S

K

V

P

P

L

L

Y

Y

L

T

T

C

R

V

T

A

A

P

D

G

R

E

V

V

R

R

F

A

A

S

S

T

S

E

L

A

P

K

A

A

L

L

L

A

A

A

G

G

G

F

E

-

V

-

D

-

T

-

R

-

I

-

D

-

P

P

V

L

A

A

L

D

H

A

H

R

Y

R

M

V

T

A

F

G

H

-

S

-

V

-

P

-

A

-

P

-

R

-

T

-

I

-

L

L

R

T

G

G

V

V

E

Y

K

Q

L

V

P

P

P

A

A

G

S

A

L

V

T

M

A

D

I

I

E

D

-

L

P

G

D

S

G

G

R

T

I

A

T

V

T

T

T

H

T

R

Y

T

W

W

E

T

P

P

D

G

F

L

S

S

R

R

E

I

E

-

R

-

A

-

G

-

W

L

S

P

E

E

K

G

D

E

W

A

E

V

D

A

A

A

V

V

L

R

E

A

S

A

L

L

R

E

V

K

A

A

V

V

K

A

R

Q

R

R

L

V

V

T

-

P

A

G

D

D

V

T

P

P

V

L

G

-

C

V

L
x
V

L

L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

S

S

L

G

I

V

V

A

G

A

L

C

L

A

A

H

E

R

A

A

G

A

Q

G

H

E

G

-

L

L

A

D

T

T

F

V

S
|
S

I
x
M

G

G

F

T

E

D

S

T

V

-

G

-

V

-

A

-

G

S

D

N

E

E

F

F

K

R

Y

E

S

A

D

R

I

A

I

V

A

V

D

D

R

H

F

L

G

R

T

T

D

R

H

H

H

R

Q

E

I

I

R

T

I

I

G

P

T

T

E

T

R

E

M

L

L

L

P

A

A

Q

L

L

G

P

G

Y

A

A

I

V

G

W

A

A

M

S

S

E

E

S

P

-

M

-

V

V

S

D

H

P

D
|
D

C

I

V

I

A

E

F
x
Y

Y

L

L

L

-

P

-

L

-

T

-

A

L

L

S

Y

Q

R

E

A

V

L

A

D

K

G

H

P

V

E

K

R

V

R

V

I

Q

L

S

T

G
|
G

Q
x
Y

G
|
G

A

A

D
|
D

E
x
I

V

P

F

L

A

G

G

G

Y

M

H

H

active site: A65 (≠ N75), G66 (= G76), D306 (= D349), Y332 (≠ Q371)
binding adenosine monophosphate: V231 (≠ L266), S233 (= S268), S238 (= S273), S256 (= S292), M257 (≠ I293), G331 (= G370)
binding magnesium ion: D237 (= D272), D335 (= D374)
binding deoxyguanidinoproclavaminic acid: Y310 (≠ F353), Y332 (≠ Q371), G333 (= G372), I336 (≠ E375)
binding pyrophosphate 2-: S233 (= S268), G235 (= G270), D237 (= D272), S238 (= S273), D335 (= D374)

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

1mb9A Beta-lactam synthetase complexed with atp (see paper)
27% identity, 52% coverage: 71:381/601 of query aligns to 66:346/485 of 1mb9A

query
sites
1mb9A

T

T

I

A

A

V

W

L

N
x
A

G
|
G

C

E

I

I

Y

Y

N

N

Y

R

E

D

Q

E

L

L

R

L

D

S

E

V

L

L

S

P

G

A

H

G

G

P

Y

A

R

-

F

-

S

P

H

E

S

G

D

D

T

A

E

E

V

L

L

V

L

L

K

R

G

L

Y

L

H

E

H

R

W

Y

G

D

D

L

R

H

F

A

V

F

D

R

H

L

L

V

K

N

G

G

M

R

F

F

A

A

F

-

A

-

I

T

V

V

E

V

R

R

D

T

S

G

G

D

R

R

V

V

L

L

G

A

R

T

D

D

R

H

L

A

G

G

I

S

K

V

P

P

L

L

Y

Y

L

T

T

C

R

V

T

A

A

P

D

G

R

E

V

V

R

R

F

A

A

S

S

T

S

E

L

A

P

K

A

A

L

L

L

A

A

A

G

F

G

P

E

L

V

A

D

D

T

A

R

R

I

-

D

-

P

-

V

-

A

-

L

-

H

-

Y

-

M

-

T

-

F

-

H

-

S

-

V

-

P

-

A

-

P

-

R

R

T

V

I

A

-

G

L

L

R

T

G

G

V

V

E

Y

K

Q

L

V

P

P

P

A

A

G

S

A

L

V

T

M

A

D

I

I

E

D

-

L

P

G

D

S

G

G

R

T

I

A

T

V

T

T

T

H

T

R

Y

T

W

W

E

T

P

P

D

G

F

L

S

S

R

R

E

I

E

-

R

-

A

-

G

-

W

L

S

P

E

E

K

G

D

E

W

A

E

V

D

A

A

A

V

V

L

R

E

A

S

A

L

L

R

E

V

K

A

A

V

V

K

A

R

Q

R

R

L

V

V

T

-

P

A

G

D

D

V

T

P

P

V

L

G

-

C

V

L
x
V

L
|
L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

S

S

L

G

I

V

V

A

G

A

L

C

L

A

A

H

E

R

A

A

G

A

Q

G

H

E

G

-

L

L

A

D

T

T

F

V

S
|
S

I
x
M

G

G

F

T

E

D

S

T

V

-

G

-

V

-

A

-

G

S

D

N

E

E

F

F

K

R

Y

E

S

A

D

R

I

A

I

V

A

V

D

D

R

H

F

L

G

R

T

T

D

R

H

H

H

R

Q

E

I

I

R

T

I

I

G

P

T

T

E

T

R

E

M

L

L

L

P

A

A

Q

L

L

G

P

G

Y

A

A

I

V

G

W

A

A

M

S

S

E

E

S

P

-

M

-

V

V

S

D

H

P

D
|
D

C

I

V

I

A

E

F
x
Y

Y

L

L

L

-

P

-
x
L

-

T

-

A

L

L

S

Y

Q

R

E

A

V

L

A

D

K

G

H

P

V

E

K

R

V

R

V

I

Q

L

S

T

G
|
G

Q
x
Y

G

G

A

A

D
|
D

E

I

V

P

F

L

A

G

G

G

Y

M

H

H

active site: A70 (≠ N75), G71 (= G76), D310 (= D349), Y336 (≠ Q371)
binding adenosine monophosphate: V235 (≠ L266), L236 (= L267), S242 (= S273), S260 (= S292), M261 (≠ I293), Y314 (≠ F353), L318 (vs. gap), G335 (= G370), Y336 (≠ Q371)
binding adenosine-5'-triphosphate: V235 (≠ L266), L236 (= L267), S237 (= S268), G239 (= G270), D241 (= D272), S242 (= S273), S260 (= S292), M261 (≠ I293), L318 (vs. gap), G335 (= G370), D339 (= D374)
binding magnesium ion: D241 (= D272), D339 (= D374)
binding pyrophosphate 2-: S237 (= S268), G239 (= G270), D241 (= D272), S242 (= S273), D339 (= D374)

Sites not aligning to the query:

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

1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
27% identity, 52% coverage: 71:381/601 of query aligns to 65:347/496 of 1mbzA

query
sites
1mbzA

T

T

I

A

A

V

W

L

N
x
A

G
|
G

C

E

I

I

Y

Y

N

N

Y

R

E

D

Q

E

L

L

R

L

D

S

E

V

L

L

S

P

G

A

H

G

G

P

Y

A

R

-

F

-

S

P

H

E

S

G

D

D

T

A

E

E

V

L

L

V

L

L

K

R

G

L

Y

L

H

E

H

R

W

Y

G

D

D

L

R

H

F

A

V

F

D

R

H

L

L

V

K

N

G

G

M

R

F

F

A

A

F

T

A

V

I

V

V

-

E

-

R

R

D

T

S

G

G

D

R

R

V

V

L

L

G

A

R

T

D

D

R

H

L

A

G

G

I

S

K

V

P

P

L

L

Y

Y

L

T

T

C

R

V

T

A

A

P

D

G

R

E

V

V

R

R

F

A

A

S

S

T

S

E

L

A

P

K

A

A

L

L

L

A

A

A

G

H

G

G

E

F

V

-

D

-

T

-

R

-

I

-

D

-

P

P

V

L

A

A

L

D

H

A

H

R

Y

R

M

V

T

A

F

G

H

-

S

-

V

-

P

-

A

-

P

-

R

-

T

-

I

-

L

L

R

T

G

G

V

V

E

Y

K

Q

L

V

P

P

P

A

A

G

S

A

L

V

T

M

A

D

I

I

E

D

-

L

P

G

D

S

G

G

R

T

I

A

T

V

T

T

T

H

T

R

Y

T

W

W

E

T

P

P

D

G

F

L

S

S

R

R

E

I

E

-

R

-

A

-

G

-

W

L

S

P

E

E

K

G

D

E

W

A

E

V

D

A

A

A

V

V

L

R

E

A

S

A

L

L

R

E

V

K

A

A

V

V

K

A

R

Q

R

R

L

V

V

T

-

P

A

G

D

D

V

T

P

P

V

L

G

-

C

V

L
x
V

L
|
L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

S

S

L

G

I

V

V

A

G

A

L

C

L

A

A

H

E

R

A

A

G

A

Q

G

H

E

G

-

L

L

A

D

T

T

F

V

S
|
S

I
x
M

G

G

F

T

E

D

S

T

V

-

G

-

V

-

A

-

G

S

D

N

E

E

F

F

K

R

Y

E

S

A

D

R

I

A

I

V

A

V

D

D

R

H

F

L

G

R

T

T

D

R

H

H

H

R

Q

E

I

I

R

T

I

I

G

P

T

T

E

T

R

E

M

L

L

L

P

A

A

Q

L

L

G

P

G

Y

A

A

I

V

G

W

A

A

M

S

S

E

E

S

P

-

M

-

V

V

S

D

H

P

D
|
D

C

I

V

I

A

E

F
x
Y

Y

L

L

L

-

P

-
x
L

-

T

-

A

L

L

S

Y

Q

R

E

A

V

L

A

D

K

G

H

P

V

E

K

R

V

R

V

I

Q

L

S

T

G
|
G

Q
x
Y

G
|
G

A

A

D
|
D

E
x
I

V

P

F

L

A

G

G

G

Y

M

H

H

active site: A69 (≠ N75), G70 (= G76), D311 (= D349), Y337 (≠ Q371)
binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L266), L237 (= L267), S238 (= S268), S243 (= S273), S261 (= S292), M262 (≠ I293), Y315 (≠ F353), L319 (vs. gap), G336 (= G370), Y337 (≠ Q371), G338 (= G372), D340 (= D374), I341 (≠ E375)
binding magnesium ion: D242 (= D272), D340 (= D374)
binding pyrophosphate 2-: S238 (= S268), G240 (= G270), D242 (= D272), S243 (= S273), D340 (= D374)

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)
25% identity, 43% coverage: 263:523/601 of query aligns to 241:443/503 of Q9XB61

query
sites
Q9XB61

V

V

G

G

C

I

L
x
P

L
|
L

S
|
S

G
|
G

V
x
L

D
|
D

S
|
S

S

S

L

L

I

V

V

T

G

A

L

L

L

-

A

-

E

-

A

A

G

S

Q

R

H

H

-

F

-

K

G

K

L

L

A

N

T

T

F

Y

S

S

I
|
I

G

G

F

T

E

E

S

-

V

-

G

-

V

-

A

L

G

S

D

N

E

E

F

F

K

E

Y

F

S

S

D

Q

I

Q

I

V

A

A

D

D

R

A

F

L

G

G

T

T

D

-

H

H

Q

Q

I

M

R

K

I

I

G

L

T

S

E

E

R

T

M

-

L

-

P

E

A

V

L

I

G

N

G

G

A

I

I

I

G

E

A

S

M

I

S

Y

E

Y

P

N

M

E

V

I

S

F

H

D

D

G

C

L

V

S

A

A

-

E

-

I

-

Q

-

S

-

G

F

L

Y

F

L

N

L

V

S

Y

Q

R

E

Q

V

A

A

Q

K

G

H

Q

V

V

K

S

V

C

V

M

Q

L

S

T

G
|
G

Q
x
Y

G
|
G

A
x
S

D
|
D

E

L

V

L

F

F

A

G

G

G

Y

-

H

-

W

-

Y

-

P

-

M

I

G

L

E

K

P

P

A

G

A

A

A

Q

S

-

V

-

E

-

G

-

S

-

V

-

A

-

S

-

Y

-

R

-

A

-

F

-

F

Y

D

D

R

-

D

-

R

-

D

-

G

-

Y

-

A

-

D

-

I

-

V

-

S

N

P

P

G

N

Y

Q

L

L

A

L

A

A

D

E

D
x
Q

P

V

S

Y

E
x
R

L

T

F

R

V

W

T

T

E

G

H
x
E

F

F

A

A

R

T

P

H

G

G

A

A

Q

S

T

-

G

-

V

-

D

-

R

-

A

-

L

-

R

-

L

-

D

-

T

-

V

-

M

-

L

-

V

-

D

-

P

-

V

-

K

-

R

-

V

-

D

-

N

-

M

-

T

-

M

-

A

C

W

Y

G

G

L

I

E

D

G

I

R

R

V

H

P

P

F

F

L

W

D

S

H

H

E

S

L

L

V

I

E

S

L

L

A

C

A

H

T

A

C

L

P

H

P

P

Q

D

L

Y

K

K

T

I

A

F

-

D

H

N

D

E

G

V

K
|
K

G

N

V

I

L

L

K

R

Q

E

A

Y

A

A

R

D

-

S

-

L

Q

Q

V

L

I

L

P

P

S

K

E

D

V

I

I

V

D

W

R

R

P

K

K
|
K

244:251 (vs. 266:273, 75% identical) binding ATP
I270 (= I293) binding ATP
GYGSD 344:348 (≠ GQGAD 370:374) binding ATP
Y345 (≠ Q371) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
G346 (= G372) binding substrate
Q371 (≠ D426) binding substrate
R374 (≠ E429) binding substrate
E380 (≠ H435) mutation to A: Loss of activity.; mutation to D: Reduces catalytic efficiency.; mutation to Q: Reduces catalytic efficiency.
K421 (= K503) binding ATP
K443 (= K523) mutation K->A,M: Loss of activity.

Sites not aligning to the query:

444:446 binding ATP

1q19A Carbapenam synthetase (see paper)
25% identity, 43% coverage: 263:523/601 of query aligns to 240:442/500 of 1q19A

query
sites
1q19A

V

V

G

G

C

I

L
x
P

L
|
L

S
|
S

G

G

V

L

D
|
D

S
|
S

S

S

L

L

I

V

V

T

G

A

L

L

L

-

A

-

E

-

A

A

G

S

Q

R

H

H

-

F

-

K

G

K

L

L

A

N

T

T

F

Y

S
|
S

I
|
I

G

G

F

T

E

E

S

-

V

-

G

-

V

-

A

L

G

S

D

N

E

E

F

F

K

E

Y

F

S

S

D

Q

I

Q

I

V

A

A

D

D

R

A

F

L

G

G

T

T

D

-

H

H

Q

Q

I

M

R

K

I

I

G

L

T

S

E

E

R

T

M

-

L

-

P

E

A

V

L

I

G

N

G

G

A

I

I

I

G

E

A

S

M

I

S

Y

E

Y

P

N

M

E

V

I

S

F

H

D

D

G

C
x
L

V

S

A

A

-
x
E

-

I

-

Q

-

S

-

G

F

L

Y

F

L

N

L

V

S

Y

Q

R

E

Q

V

A

A

Q

K

G

H

Q

V

V

K

S

V

C

V

M

Q

L

S
x
T

G
|
G

Q
x
Y

G
|
G

A

S

D
|
D

E
x
L

V

L

F

F

A

G

G

G

Y

-

H

-

W

-

Y

-

P

-

M

I

G

L

E

K

P

P

A

G

A

A

A

Q

S

-

V

-

E

-

G

-

S

-

V

-

A

-

S

-

Y

-

R

-

A

-

F

-

F

Y

D

D

R

-

D

-

R

-

D

-

G

-

Y

-

A

-

D

-

I

-

V

-

S

N

P

P

G

N

Y

Q

L

L

A

L

A

A

D

E

D

Q

P

V

S

Y

E
x
R

L

T

F

R

V

W

T

T

E

G

H
x
E

F

F

A

A

R

T

P

H

G

G

A

A

Q

S

T

-

G

-

V

-

D

-

R

-

A

-

L

-

R

-

L

-

D

-

T

-

V

-

M

-

L

-

V

-

D

-

P

-

V

-

K

-

R

-

V

-

D

-

N

-

M

-

T

-

M

-

A

C

W

Y

G

G

L

I

E

D

G

I

R

R

V

H

P

P

F

F

L

W

D

S

H

H

E

S

L

L

V

I

E

S

L

L

A

C

A

H

T

A

C

L

P

H

P

P

Q

D

L

Y

K

K

T

I

A

F

-

D

H

N

D

E

G

V

K

K

G

N

V

I

L

L

K

R

Q

E

A

Y

A

A

R

D

-

S

-

L

Q

Q

V

L

I

L

P

P

S

K

E

D

V

I

I

V

D

W

R

R

P

K

K
|
K

active site: L318 (≠ C350), E321 (vs. gap), Y344 (≠ Q371), E379 (≠ H435), K442 (= K523)
binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L266), L244 (= L267), S245 (= S268), D249 (= D272), S250 (= S273), S268 (= S292), I269 (= I293), T342 (≠ S369), G343 (= G370), D347 (= D374), K442 (= K523)
binding (2s,5s)-5-carboxymethylproline: Y344 (≠ Q371), G345 (= G372), L348 (≠ E375), R373 (≠ E429), E379 (≠ H435)

Sites not aligning to the query:

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

Query Sequence

>WP_011779502.1 NCBI__GCF_000015305.1:WP_011779502.1
MCGATGEVRLDGTTPNVRAVTAMAEVMVPRGPDSAGVWSQGRVALGHRRLKIIDLSEAGA
QPMVDAELGLTIAWNGCIYNYEQLRDELSGHGYRFFSHSDTEVLLKGYHHWGDRFVDHLK
GMFAFAIVERDSGRVLLGRDRLGIKPLYLTRTADRVRFASSLPALLAGGEVDTRIDPVAL
HHYMTFHSVVPAPRTILRGVEKLPPASLTAIEPDGRITTTTYWEPDFSRREERAGWSEKD
WEDAVLESLRVAVKRRLVADVPVGCLLSGGVDSSLIVGLLAEAGQHGLATFSIGFESVGG
VAGDEFKYSDIIADRFGTDHHQIRIGTERMLPALGGAIGAMSEPMVSHDCVAFYLLSQEV
AKHVKVVQSGQGADEVFAGYHWYPPMGEPAAASVEGSVASYRAAFFDRDRDGYADIVSPG
YLAADDPSELFVTEHFARPGAQTGVDRALRLDTTVMLVDDPVKRVDNMTMAWGLEGRVPF
LDHELVELAATCPPQLKTAHDGKGVLKQAARQVIPSEVIDRPKGYFPVPALTHLEGPYLE
LVRDALYAPAAKERGLFRPDAVERLLADPNGRLTPLRGNELWQIALLELWLQRHGINGPA
A

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