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 (≠ R29) 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)
29% identity, 81% coverage: 4:498/610 of query aligns to 1:434/557 of P78753

query
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P78753

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S391 (≠ P420) 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)
24% identity, 85% coverage: 1:521/610 of query aligns to 1:470/561 of P08243

query
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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 (vs. gap) to E: in dbSNP:rs1049674
F362 (≠ L368) 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)
24% identity, 81% coverage: 5:497/610 of query aligns to 1:429/509 of 6gq3A

query
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6gq3A

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-

P

-

R

-

T

-

I

-

L

-

K

-

G

-

V

-

R

-

K

-

L

-

G

G

P

H

A

Y

T

E

T

V

M

L

T

D

I

L

N

K

G

P

S

N

G

G

H

K

I

V

E

A

E

S

A

V

I

E

Y

M

W

V

K

K

L

Y

D

H

A

H

T

C

R

R

P

D

A

V

Q

F

A

P

L

G

S

F

E

E

A

I

Q

E

W

T

L

V

A

K

A

N

T

N

R

L

E

R

V

I

L

L

V

F

R

N

A

N

V

A

E

V

R

K

H

K

R

R

L

L

A

M

A

T

D

D

V

R

P

R

V

I

G

G

V

C

L

L

S

S

G

G

L

L

D

D

S

S

L

L

L

V

V

A

G

A

L

T

L

L

A

L

D

K

H

Q

V

L

D

K

D

E

L

A

Q

Q

T

V

F

-

S

Q

M

Y

G

P

F

L

E

Q

T

T

L

F

G

A

E

I

G

G

G

M

E

E

K

D

A

S

D

P

E

D

F

L

E

L

F

A

S

A

D

R

Q

K

V

V

A

A

E

D

Q

H

F

I

G

G

T

S

R

E

H

H

H

Y

K

E

Y

V

L

L

I

F

P

N

Y

S

D

E

E

E

V

G

L

I

R

Q

R

A

L

L

P

D

E

E

A

V

V

I

-

F

-

S

L

L

Q

E

M

T

S

Y

E

D

P

I

M
x
T

V

T

S

V

Q
x
R

D

A

V

S

I

V

A

G

F

M

Y

Y

L

L

L

I

G

S

E

K

R

Y

V

I

S

R

K

K

Q

N

V

T

K

D

-

S

-

V

V

V

V

I

L

F

S

S

G

G

Q

E

G

G

A

S

D

D

E

E

V

L

F

T

G

Q

G

G

Y

Y

F

I

W

Y

Y

F

P

H

R

K

M

A

D

P

A

S

A

P

K

E

G

K

S

A

A

E

L

E

A

E

R

S

F

E

S

R

A

L

H

-

Y

-

F

-

D

-

R

-

D

-

H

-

D

-

E

-

Y

-

L

-

E

-

M

-

V

-

T

-

P

-

A

-

Y

-

H

-

L

-

P

-

D

-

V

-

T

-

A

-

L

-

V

-

A

-

K

-

A

-

L

-

A

-

Q

-

P

-

Q

L

A

R

D

E

T

L

F

Y

I

L

D

F

Q

D

V

V

L

L

R

R

F

A

D

D

A

R

T

T

L

-

V

-

D

-

P

-

V

-

K

-

R

-

V

-

D

-

N

-

M

-

A

-

M

A

A

A

W

H

G

G

L

L

E

E

A

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

R

S

M

L

P

P

E

E

L

M

K

R

L

I

R

P

Q

K

G

N

G

G

active site: W4 (≠ L8), L49 (= L50), N74 (= N75), G75 (= G76), T324 (≠ M345), R327 (≠ Q348)
binding 5-oxo-l-norleucine: C1 (= C5), R48 (= R49), V51 (≠ I52), V52 (≠ I53), Y73 (≠ F74), N74 (= N75), G75 (= G76), E76 (≠ T77), V95 (≠ S99), D96 (= D100)

1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
30% identity, 52% coverage: 73:388/610 of query aligns to 67:354/496 of 1mbzA

query
sites
1mbzA

V

V

F

L

N
x
A

G
|
G

T

E

I

I

Y

Y

N

N

Y

R

K

D

E

E

L

L

R

L

A

S

E

V

L

L

I

P

A

A

M

G

G

P

Y

A

R

-

F

-

S

P

E

E

S

G

D

D

S

A

E

E

V

L

I

V

L

L

K

R

A

L

Y

L

H

E

A

R

W

Y

G

D

A

L

Q

H

C

A

V

F

Q

R

R

L

F

V

F

N

G

G

M

R

F

F

A

A

F

T

A

V

V

V

W

-

D

-

Q

R

R

T

D

G

A

D

R

R

L

V

F

L

M

L

A

A

R

T

D

D

R

H

F

A

G

G

I

S

K

V

P

P

L

L

Y

Y

Y

T

T

C

M

V

D

A

G

P

S

G

R

E

L

V

R

R

F

A

A

S

S

T

S

E

L

A

Q

K

A

A

L

L

L

A

A

A

A

-

G

-

V

-

D

-

T

-

G

-

I

-

D

-

P

-

V

-

A

-

L

-

H

-

H

H

H

G

F

F

T

P

L

L

H

-

A

-

V

-

V

A

P

D

A

A

P

R

R

R

T

V

I

A

-

G

L

L

K

T

G

G

V

V

R

Y

K

Q

L

V

G

P

P

A

A

G

T

A

T

V

M

M

T

D

I

I

N

D

-

L

G

G

S

S

G

G

H

T

I

A

E

V

E

T

A

H

I

R

Y

T

W

W

K

T

L

P

D

G

A

L

T

S

R

R

P

-

A

-

Q

R

A

I

L

L

S

P

E

E

A

G

Q

E

W

A

L

V

A

A

T

V

R

R

E

A

V

A

L

L

V

E

R

K

A

A

V

V

E

A

R

Q

H

R

R

V

L

T

A

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

L

I

D
|
D

S
|
S

S

S

L

G

L

V

V

A

G

A

L

C

L

A

A

H

D

R

H

A

V

A

D

G

D

E

L

L

Q

D

T

T

F

V

S
|
S

M
|
M

G

G

F

T

E

D

T

T

L

-

G

-

E

-

G

-

E

-

K

-

A

S

D

N

E

E

F

F

E

R

F

E

S

A

D

R

Q

A

V

V

A

V

E

D

Q

H

F

L

G

R

T

T

R

R

H

H

H

R

K

E

Y

I

L

T

I

I

P

P

Y

T

D

T

E

E

V

L

L

L

R

A

R

Q

L

L

P

P

E

Y

A

A

V

V

L

-

Q

-

M

W

S

A

E

S

P

E

M

S

V

V

S

D

Q

P

D
|
D

V

I

I

I

A

E

F
x
Y

Y

L

L

L

-

P

-
x
L

-

T

-

A

L

L

G

Y

E

R

R

A

V

L

S

D

K

G

Q

P

V

E

K

R

V

R

V

I

L

L

S

T

G
|
G

Q
x
Y

G
|
G

A

A

D
|
D

E
x
I

V

P

F

L

G

G

Y

M

F

H

W

R

Y

E

P

D

R

R

M

L

D

P

A

A

active site: A69 (≠ N75), G70 (= G76), D311 (= D349), Y337 (≠ Q371)
binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L265), L237 (= L266), S238 (= S267), S243 (= S272), S261 (= S290), M262 (= M291), Y315 (≠ F353), L319 (vs. gap), G336 (= G370), Y337 (≠ Q371), G338 (= G372), D340 (= D374), I341 (≠ E375)
binding magnesium ion: D242 (= D271), D340 (= D374)
binding pyrophosphate 2-: S238 (= S267), G240 (= G269), D242 (= D271), S243 (= S272), 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

1jgtB Crystal structure of beta-lactam synthetase (see paper)
29% identity, 52% coverage: 73:388/610 of query aligns to 71:362/500 of 1jgtB

query
sites
1jgtB

V

V

F

L

N
x
A

G
|
G

T

E

I

I

Y

Y

N

N

Y

R

K

D

E

E

L

L

R

L

A

S

E

V

L

L

I

P

A

A

M

G

G

P

Y

A

R

-

F

-

S

P

E

E

S

G

D

D

S

A

E

E

V

L

I

V

L

L

K

R

A

L

Y

L

H

E

A

R

W

Y

G

D

A

L

Q

H

C

A

V

F

Q

R

R

L

F

V

F

N

G

G

M

R

F

F

A

A

F

T

A

V

V

V

W

-

D

-

Q

R

R

T

D

G

A

D

R

R

L

V

F

L

M

L

A

A

R

T

D

D

R

H

F

A

G

G

I

S

K

V

P

P

L

L

Y

Y

Y

T

T

C

M

V

D

A

G

P

S

G

R

E

L

V

R

R

F

A

A

S

S

T

S

E

L

A

Q

K

A

A

L

L

L

A

A

A

A

-

G

-

V

-

D

-

T

-

G

-

I

-

D

-

P

-

V

-

A

-

L

-

H

H

H

R

H

D

F

P

T

K

L

G

H

F

A

P

V

L

V

A

P

D

A

A

P

R

R

R

T

V

I

A

-

G

L

L

K

T

G

G

V

V

R

Y

K

Q

L

V

G

P

P

A

A

G

T

A

T

V

M

M

T

D

I

I

N

D

-

L

G

G

S

S

G

G

H

T

I

A

E

V

E

T

A

H

I

R

Y

T

W

W

K

T

L

P

D

G

A

L

T

S

R

R

P

-

A

-

Q

R

A

I

L

L

S

P

E

E

A

G

Q

E

W

A

L

V

A

A

T

V

R

R

E

A

V

A

L

L

V

E

R

K

A

A

V

V

E

A

R

Q

H

R

R

V

L

T

A

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

L
x
I

D
|
D

S
|
S

S

S

L

G

L

V

V

A

G

A

L

C

L

A

A

H

D

R

H

A

V

A

D

G

D

E

L

L

Q

D

T

T

F

V

S
|
S

M
|
M

G

G

F

T

E

D

T

T

L

-

G

-

E

-

G

-

E

-

K

-

A

S

D

N

E

E

F

F

E

R

F

E

S

A

D

R

Q

A

V

V

A

V

E

D

Q

H

F

L

G

R

T

T

R

R

H

H

H

R

K

E

Y

I

L

T

I

I

P

P

Y

T

D

T

E

E

V

L

L

L

R

A

R

Q

L

L

P

P

E

Y

A

A

V

V

L

-

Q

-

M

W

S

A

E

S

P

E

M

S

V

V

S

D

Q

P

D
|
D

V

I

I

I

A

E

F
x
Y

Y

L

L

L

-

P

-
x
L

-

T

-

A

L

L

G

Y

E

R

R

A

V

L

S

D

K

G

Q

P

V

E

K

R

V

R

V

I

L

L

S

T

G
|
G

Q
x
Y

G
|
G

A

A

D
|
D

E
x
I

V

P

F

L

G

G

Y
x
M

F

H

W

R

Y

E

P

D

R

R

M

L

D

P

A

A

active site: A73 (≠ N75), G74 (= G76), D319 (= D349), Y345 (≠ Q371)
binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L265), L245 (= L266), S246 (= S267), G248 (= G269), I249 (≠ L270), D250 (= D271), S251 (= S272), S269 (= S290), M270 (= M291), 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 (= D271), 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)
30% identity, 52% coverage: 73:388/610 of query aligns to 63:349/491 of 1mc1A

query
sites
1mc1A

V

V

F

L

N
x
A

G
|
G

T

E

I

I

Y

Y

N

N

Y

R

K

D

E

E

L

L

R

L

A

S

E

V

L

L

I

P

A

A

M

G

G

P

Y

A

R

-

F

-

S

P

E

E

S

G

D

D

S

A

E

E

V

L

I

V

L

L

K

R

A

L

Y

L

H

E

A

R

W

Y

G

D

A

L

Q

H

C

A

V

F

Q

R

R

L

F

V

F

N

G

G

M

R

F

F

A

A

F

T

A

V

V

V

W

-

D

-

Q

R

R

T

D

G

A

D

R

R

L

V

F

L

M

L

A

A

R

T

D

D

R

H

F

A

G

G

I

S

K

V

P

P

L

L

Y

Y

Y

T

T

C

M

V

D

A

G

P

S

G

R

E

L

V

R

R

F

A

A

S

S

T

S

E

L

A

Q

K

A

A

L

L

L

-

A

A

G

G

G

-

V

-

D

-

T

-

G

-

I

-

D

-

P

-

V

-

A

-

L

-

H

-

F

F

T

P

L

L

H

-

A

-

V

-

V

A

P

D

A

A

P

R

R

R

T

V

I

A

-

G

L

L

K

T

G

G

V

V

R

Y

K

Q

L

V

G

P

P

A

A

G

T

A

T

V

M

M

T

D

I

I

N

D

-

L

G

G

S

S

G

G

H

T

I

A

E

V

E

T

A

H

I

R

Y

T

W

W

K

T

L

P

D

G

A

L

T

S

R

R

P

-

A

-

Q

R

A

I

L

L

S

P

E

E

A

G

Q

E

W

A

L

V

A

A

T

V

R

R

E

A

V

A

L

L

V

E

R

K

A

A

V

V

E

A

R

Q

H

R

R

V

L

T

A

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

L

I

D
|
D

S
|
S

S

S

L

G

L

V

V

A

G

A

L

C

L

A

A

H

D

R

H

A

V

A

D

G

D

E

L

L

Q

D

T

T

F

V

S
|
S

M
|
M

G

G

F

T

E

D

T

T

L

-

G

-

E

-

G

-

E

-

K

-

A

S

D

N

E

E

F

F

E

R

F

E

S

A

D

R

Q

A

V

V

A

V

E

D

Q

H

F

L

G

R

T

T

R

R

H

H

H

R

K

E

Y

I

L

T

I

I

P

P

Y

T

D

T

E

E

V

L

L

L

R

A

R

Q

L

L

P

P

E

Y

A

A

V

V

L

-

Q

-

M

W

S

A

E

S

P

E

M

S

V

V

S

D

Q

P

D
|
D

V

I

I

I

A

E

F
x
Y

Y

L

L

L

-

P

-

L

-

T

-

A

L

L

G

Y

E

R

R

A

V

L

S

D

K

G

Q

P

V

E

K

R

V

R

V

I

L

L

S

T

G
|
G

Q
x
Y

G
|
G

A

A

D
|
D

E
x
I

V

P

F

L

G

G

Y

M

F

H

W

R

Y

E

P

D

R

R

M

L

D

P

A

A

active site: A65 (≠ N75), G66 (= G76), D306 (= D349), Y332 (≠ Q371)
binding adenosine monophosphate: V231 (≠ L265), S233 (= S267), S238 (= S272), S256 (= S290), M257 (= M291), G331 (= G370)
binding magnesium ion: D237 (= D271), D335 (= D374)
binding deoxyguanidinoproclavaminic acid: Y310 (≠ F353), Y332 (≠ Q371), G333 (= G372), I336 (≠ E375)
binding pyrophosphate 2-: S233 (= S267), G235 (= G269), D237 (= D271), S238 (= S272), 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)
28% identity, 52% coverage: 73:388/610 of query aligns to 68:353/485 of 1mb9A

query
sites
1mb9A

V

V

F

L

N
x
A

G
|
G

T

E

I

I

Y

Y

N

N

Y

R

K

D

E

E

L

L

R

L

A

S

E

V

L

L

I

P

A

A

M

G

G

P

Y

A

R

-

F

-

S

P

E

E

S

G

D

D

S

A

E

E

V

L

I

V

L

L

K

R

A

L

Y

L

H

E

A

R

W

Y

G

D

A

L

Q

H

C

A

V

F

Q

R

R

L

F

V

F

N

G

G

M

R

F

F

A

A

F

T

A

V

V

V

W

-

D

-

Q

R

R

T

D

G

A

D

R

R

L

V

F

L

M

L

A

A

R

T

D

D

R

H

F

A

G

G

I

S

K

V

P

P

L

L

Y

Y

Y

T

T

C

M

V

D

A

G

P

S

G

R

E

L

V

R

R

F

A

A

S

S

T

S

E

L

A

Q

K

A

A

L

L

L

A

A

A

A

F

G

P

G

L

V

A

D

D

T

A

G

-

I

-

D

-

P

-

V

-

A

-

L

-

H

-

F

-

T

-

L

-

H

-

A

-

V

-

P

-

A

-

P

-

R

R

T

R

I

V

-

A

-

G

L

L

K

T

G

G

V

V

R

Y

K

Q

L

V

G

P

P

A

A

G

T

A

T

V

M

M

T

D

I

I

N

D

-

L

G

G

S

S

G

G

H

T

I

A

E

V

E

T

A

H

I

R

Y

T

W

W

K

T

L

P

D

G

A

L

T

S

R

R

P

-

A

-

Q

R

A

I

L

L

S

P

E

E

A

G

Q

E

W

A

L

V

A

A

T

V

R

R

E

A

V

A

L

L

V

E

R

K

A

A

V

V

E

A

R

Q

H

R

R

V

L

T

A

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

L

I

D
|
D

S
|
S

S

S

L

G

L

V

V

A

G

A

L

C

L

A

A

H

D

R

H

A

V

A

D

G

D

E

L

L

Q

D

T

T

F

V

S
|
S

M
|
M

G

G

F

T

E

D

T

T

L

-

G

-

E

-

G

-

E

-

K

-

A

S

D

N

E

E

F

F

E

R

F

E

S

A

D

R

Q

A

V

V

A

V

E

D

Q

H

F

L

G

R

T

T

R

R

H

H

H

R

K

E

Y

I

L

T

I

I

P

P

Y

T

D

T

E

E

V

L

L

L

R

A

R

Q

L

L

P

P

E

Y

A

A

V

V

L

-

Q

-

M

W

S

A

E

S

P

E

M

S

V

V

S

D

Q

P

D
|
D

V

I

I

I

A

E

F
x
Y

Y

L

L

L

-

P

-
x
L

-

T

-

A

L

L

G

Y

E

R

R

A

V

L

S

D

K

G

Q

P

V

E

K

R

V

R

V

I

L

L

S

T

G
|
G

Q
x
Y

G

G

A

A

D
|
D

E

I

V

P

F

L

G

G

Y

M

F

H

W

R

Y

E

P

D

R

R

M

L

D

P

A

A

active site: A70 (≠ N75), G71 (= G76), D310 (= D349), Y336 (≠ Q371)
binding adenosine monophosphate: V235 (≠ L265), L236 (= L266), S242 (= S272), S260 (= S290), M261 (= M291), Y314 (≠ F353), L318 (vs. gap), G335 (= G370), Y336 (≠ Q371)
binding adenosine-5'-triphosphate: V235 (≠ L265), L236 (= L266), S237 (= S267), G239 (= G269), D241 (= D271), S242 (= S272), S260 (= S290), M261 (= M291), L318 (vs. gap), G335 (= G370), D339 (= D374)
binding magnesium ion: D241 (= D271), D339 (= D374)
binding pyrophosphate 2-: S237 (= S267), G239 (= G269), D241 (= D271), S242 (= S272), D339 (= D374)

Sites not aligning to the query:

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

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)
26% identity, 50% coverage: 76:379/610 of query aligns to 57:353/503 of Q9XB61

query
sites
Q9XB61

G

G

T

S

I

L

Y

Y

N

N

Y

-

K

-

E

-

L

-

R

R

A

T

E

F

L

L

I

I

A

G

M

L

G

A

Y

G

R

V

F

W

F

E

S

G

E

E

-

A

-

Y

-

L

-

A

S

N

D

D

S

A

E

E

V

L

I

L

L

A

K

L

A

L

Y

F

H

T

A

R

W

L

G

G

A

A

Q

N

C

A

V

L

Q

A

R

L

F

A

F

E

G

G

M

D

F

F

A

C

F

F

A

F

V

I

W

-

D

D

Q

E

R

P

D

N

A

G

R

E

L

L

F

T

M

V

A

I

R

T

D

E

R

S

F

R

G

G

I

F

K

S

P

P

L

V

Y

H

Y

-

T

V

M

V

D

Q

G

G

S

K

R

K

L

A

R

W

F

M

A

T

S

N

S

S

L

L

Q

K

A

L

L

V

L

T

A

A

G

E

G

G

V

E

D

G

T

A

-

L

G

W

I

F

D

E

P

E

V

E

A

A

L

L

H

V

H

C

H

Q

F

S

T

L

L

M

H

R

A

A

V

D

V

T

P

Y

A

T

P

P

R

-

T

-

I

-

L

V

K

K

G

N

V

A

R

Q

K

R

L

L

G

K

P

P

A

G

T

A

T

V

M

H

T

V

I

L

N

T

G

-

S

-

G

-

H

H

I

D

E

S

E

E

A

G

I

-

Y

-

W

Y

K

S

L

F

D

V

A

E

T

S

R

R

P

T

A

L

Q

T

A

T

L

P

S

A

E

S

A

N

Q

Q

W

L

L

L

A

A

A

L

T

P

R

R

E

E

V

P

L

L

V

L

R

A

A

L

V

I

E

D

R

R

H

Y

R

L

L

N

A

A

-

P

-

L

A

E

D

D

V

L

-

A

-

P

-

R

-

F

-

D

P

T

V

V

G

G

V

I

L
x
P

L
|
L

S
|
S

G
|
G

L
|
L

D
|
D

S
|
S

S

S

L

L

L

V

V

T

G

A

L

L

L

A

A

S

D

R

H

H

V

F

D

K

L

L

Q

N

T

T

F

Y

S

S

M
x
I

G

G

F

T

E

E

T

L

L

-

G

-

E

-

G

-

E

-

K

-

A

S

D

N

E

E

F

F

E

E

F

F

S

S

D

Q

Q

Q

V

V

A

A

E

D

Q

A

F

L

G

G

T

T

R

H

H

H

H

Q

K

M

Y

K

L

I

I

L

P

S

Y

E

D

T

E

E

V

V

L

I

R

N

R

G

L

I

P

I

E

E

A

S

V

I

L

Y

-

Y

-

N

Q

E

M

I

S

F

E

D

P

G

M

L

V

S

S

A

Q

E

D

I

V

Q

I

S

A

G

F

L

Y

F

L

N

L

V

G

Y

E

R

R

Q

V

A

S

Q

K

G

Q

Q

V

V

K

S

V

C

V

M

L

L

S

T

G
|
G

Q
x
Y

G
|
G

A
x
S

D
|
D

E

L

V

L

F

F

G

G

244:251 (vs. 265:272, 88% identical) binding ATP
I270 (≠ M291) 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

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)
26% identity, 50% coverage: 76:379/610 of query aligns to 56:352/500 of 1q19A

query
sites
1q19A

G
|
G

T

S

I

L

Y

Y

N

N

Y

-

K

-

E

-

L

-

R

R

A

T

E

F

L

L

I

I

A

G

M

L

G

A

Y

G

R

V

F

W

F

E

S

G

E

E

-

A

-

Y

-

L

-

A

S

N

D

D

S

A

E

E

V

L

I

L

L

A

K

L

A

L

Y

F

H

T

A

R

W

L

G

G

A

A

Q

N

C

A

V

L

Q

A

R

L

F

A

F

E

G

G

M

D

F

F

A

C

F

F

A

F

V

I

W

-

D

D

Q

E

R

P

D

N

A

G

R

E

L

L

F

T

M

V

A

I

R

T

D

E

R

S

F

R

G

G

I

F

K

S

P

P

L

V

Y

H

Y

-

T

V

M

V

D

Q

G

G

S

K

R

K

L

A

R

W

F

M

A

T

S

N

S

S

L

L

Q

K

A

L

L

V

L

T

A

A

G

E

G

G

V

E

D

G

T

A

-

L

G

W

I

F

D

E

P

E

V

E

A

A

L

L

H

V

H

C

H

Q

F

S

T

L

L

M

H

R

A

A

V

D

V

T

P

Y

A

T

P

P

R

-

T

-

I

-

L

V

K

K

G

N

V

A

R

Q

K

R

L

L

G

K

P

P

A

G

T

A

T

V

M

H

T

V

I

L

N

T

G

-

S

-

G

-

H

H

I

D

E

S

E

E

A

G

I

-

Y

-

W

Y

K

S

L

F

D

V

A

E

T

S

R

R

P

T

A

L

Q

T

A

T

L

P

S

A

E

S

A

N

Q

Q

W

L

L

L

A

A

A

L

T

P

R

R

E

E

V

P

L

L

V

L

R

A

A

L

V

I

E

D

R

R

H

Y

R

L

L

N

A

A

-

P

-

L

A

E

D

D

V

L

-

A

-

P

-

R

-

F

-

D

P

T

V

V

G

G

V

I

L
x
P

L
|
L

S
|
S

G

G

L

L

D
|
D

S
|
S

S

S

L

L

L

V

V

T

G

A

L

L

L

A

A

S

D

R

H

H

V

F

D

K

L

L

Q

N

T

T

F

Y

S
|
S

M
x
I

G

G

F

T

E

E

T

L

L

-

G

-

E

-

G

-

E

-

K

-

A

S

D

N

E

E

F

F

E

E

F

F

S

S

D

Q

Q

Q

V

V

A

A

E

D

Q

A

F

L

G

G

T

T

R

H

H

H

H

Q

K

M

Y

K

L

I

I

L

P

S

Y

E

D

T

E

E

V

V

L

I

R

N

R

G

L

I

P

I

E

E

A

S

V

I

L

Y

-

Y

-

N

Q

E

M

I

S

F

E

D

P

G

M
x
L

V

S

S

A

Q
x
E

D

I

V

Q

I

S

A

G

F

L

Y

F

L

N

L

V

G

Y

E

R

R

Q

V

A

S

Q

K

G

Q

Q

V

V

K

S

V

C

V

M

L

L

S
x
T

G
|
G

Q
x
Y

G
|
G

A

S

D
|
D

E
x
L

V

L

F

F

G

G

active site: G56 (= G76), L318 (≠ M345), E321 (≠ Q348), Y344 (≠ Q371)
binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ L265), L244 (= L266), S245 (= S267), D249 (= D271), S250 (= S272), S268 (= S290), I269 (≠ M291), T342 (≠ S369), G343 (= G370), D347 (= D374)
binding (2s,5s)-5-carboxymethylproline: Y344 (≠ Q371), G345 (= G372), L348 (≠ E375)

Sites not aligning to the query:

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

Query Sequence

>WP_011798198.1 NCBI__GCF_000015505.1:WP_011798198.1
MCGICGELRFDGSTVDMSAIERMSDRIARRGPDHAGIFSDGALALGHRRLAIIDLSADGD
QPMIDEELKLVLVFNGTIYNYKELRAELIAMGYRFFSESDSEVILKAYHAWGAQCVQRFF
GMFAFAVWDQRDARLFMARDRFGIKPLYYTMDGSRLRFASSLQALLAAGGVDTGIDPVAL
HHHFTLHAVVPAPRTILKGVRKLGPATTMTINGSGHIEEAIYWKLDATRPAQALSEAQWL
AATREVLVRAVERHRLAADVPVGVLLSGGLDSSLLVGLLADHVDDLQTFSMGFETLGEGG
EKADEFEFSDQVAEQFGTRHHKYLIPYDEVLRRLPEAVLQMSEPMVSQDVIAFYLLGERV
SKQVKVVLSGQGADEVFGGYFWYPRMDAAKGSALARFSAHYFDRDHDEYLEMVTPAYHLP
DVTAALVAKALAQPQADTFIDQVLRFDATTLVVDDPVKRVDNMAMAWGLEARVPFLDHEL
VELAARMPPELKLRQGGKFPLKAISRGLISDAVIDRPKGYFPVPVLKHVSGEFLAFMRGI
LNSDACIRRGLYQRAYVEKLLAAPEAWFTRIQGSKLWHLALLELWLQLNVDEPYGSASST
GPSQARTETP

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