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 (= H32) mutation to A: 4,5-fold decrease in glutamine affinity.
D34 (= D36) mutation D->N,E: Little effect on the kinetic properties.
H81 (≠ F86) mutation to A: 5-fold decrease in glutamine affinity.
A105 (= A111) mutation to H: Little effect on the kinetic properties.
E349 (≠ D377) 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)
31% identity, 66% coverage: 4:434/649 of query aligns to 3:386/497 of 1ct9A

query
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active site: L50 (= L55), N74 (= N80), G75 (= G81), T305 (≠ S355), R308 (vs. gap), E332 (≠ D377), M366 (≠ L414)
binding adenosine monophosphate: L232 (≠ F275), L233 (≠ I276), S234 (= S277), S239 (= S282), A255 (≠ T301), V256 (≠ I302), D263 (≠ E311), M316 (≠ V362), S330 (= S375), G331 (= G376), E332 (≠ D377)
binding glutamine: R49 (= R54), L50 (= L55), I52 (= I57), V53 (= V58), N74 (= N80), G75 (= G81), E76 (= E82), D98 (= D105)

Sites not aligning to the query:

active site: 1
binding glutamine: 1

P08243 Asparagine synthetase [glutamine-hydrolyzing]; Cell cycle control protein TS11; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Homo sapiens (Human) (see 7 papers)
29% identity, 59% coverage: 1:386/649 of query aligns to 1:374/561 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 (= V234) to E: in dbSNP:rs1049674
F362 (≠ L374) 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)
30% identity, 56% coverage: 22:386/649 of query aligns to 14:361/509 of 6gq3A

query
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6gq3A

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-

S

T

V

V

V

S

I

L

F

S

S

G

G

D

E

G

G

G

S

D

D

E

E

L

L

F

T

A

Q

G

G

Y

Y

active site: L49 (= L55), N74 (= N80), G75 (= G81), T324 (≠ P350), R327 (≠ D353)
binding 5-oxo-l-norleucine: R48 (= R54), V51 (≠ I57), V52 (= V58), Y73 (≠ F79), N74 (= N80), G75 (= G81), E76 (= E82), V95 (≠ S104), D96 (= D105)

Sites not aligning to the query:

active site: 4
binding 5-oxo-l-norleucine: 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: 1:386/649 of query aligns to 1:365/557 of P78753

query
sites
P78753

M

M

C

C

G

G

I

I

T

L

G

A

F

V

W

H

D

H

I

V

S

A

K

E

Q

D

F

I

S

-

G

-

E

E

H

A

L

F

D

K

E

P

T

K

I

A

Q

L

K

H

M

L

S

S

K

K

T

Q

L

L

L

R

H

H

R

R

G

G

P

P

D

D

D

W

G

S

G

G

I

-

W

-

T

K

D

A

V

I

E

R

V

N

G

Q

V

T

A

I

L

L

G

C

H

H

R

E

R

R

L

L

S

A

I

I

V

V

D

G

L

V

S

E

P

S

L

-

G

G

H

A

Q

Q

P

P

M

L

M

V

S

S

A

D

N

D

G

G

R

K

Y

L

M

V

V

L

V

T

F

V

N

N

G

G

E

E

I

I

Y

Y

N

N

F

H

L

L

E

K

L

L

R

R

R

E

E

N

L

L

T

-

Q

K

L

G

G

N

H

Y

N

K

F

F

R

K

G

T

H

Y

S

S

D

D

T

C

E

E

I

V

M

I

L

L

A

Y

G

L

F

Y

S

R

E

E

W

H

G

G

L

P

D

A

K

C

A

A

I

-

R

N

R

M

F

L

N

D

G

G

M

M

F

F

A

S

F

W

A

V

L

L

W

Y

D

D

R

Q

Q

D

K

K

R

D

I

K

L

V

H

V

L

A

G

A

R

R

D

D

R

P

L

I

G

G

E

I

K

T

P

T

L

L

Y

Y

Y

Q

G

G

W

F

Q

S

G

S

-

D

-

S

-

P

S

D

T

T

F

A

L

Y

F

F

T

A

S

S

E

E

L

L

K

K

A

A

L

L

K

-

A

-

H

H

P

P

N

V

F

C

R

-

A

-

E

-

I

-

N

-

R

-

D

D

A

K

L

I

T

I

Q

A

F

F

F

P

R

P

Y

G

S

H

Y

Y

L

Y

P

D

A

S

P

-

Y

-

S

E

I

T

Y

K

Q

Q

G

T

I

V

Y

R

K

Y

L

F

P

K

P

P

G

S

T

W

L

-

S

-

W

W

N

D

G

E

I

N

D

K

A

I

H

P

P

S

D

N

P

P

V

V

T

D

Y

Y

W

K

S

L

A

L

R

R

E

E

V

T

T

-

E

-

L

-

G

-

I

-

A

-

E

-

P

-

F

-

M

-

G

-

S

-

E

-

S

-

E

-

A

-

V

-

I

-

Q

-

L

L

E

E

A

A

L

S

L

V

R

R

E

K

A

-

V

-

G

-

L

-

R

R

M

L

V

M

A

A

D

E

V

V

P

P

L

Y

G

G

A

V

F

L

I

L

S

S

G

G

I

L

D

D

S

S

T

L

I

I

V

A

A

S

L

I

M

A

Q

A

A

R

Q

E

S

T

S

E

Q

K

-

L

-

A

-

N

-

S

-

T

-

S

-

Q

-

S

-

E

-

A

-

R

-

T

-

I

-

T

-

A

-

W

-

P

P

K

V

L

K

H

T

S

F

F

T

A

I

I

G

G

F

L

N

-

E

-

E

P

A

G

Y

S

N

P

E

D

A

L

K

L

H

A

A

A

K

R

A

K

V

V

A

A

K

D

H

F

L

L

G

H

T

T

D

F

H

H

T

H

E

E

L

H

Y

T

V

F

N

T

P

I

K

D

E

E

A

G

L

L

E

D

V

A

I

L

P

R

K

D

L

V

P

-

F

-

L

I

Y

Y

D

H

E

L

P

E

F

T

S

Y

D

D

V

V

S

T

Q

T

I

I

-

R

-

A

-

S

-

T

P

P

T

M

F

Y

L

L

V

L

S

S

Q

R

L

K

A

I

K

K

Q

A

Q

Q

-

G

V

V

T

K

V

M

S

V

L

L

S

S

G

G

D

E

G

G

G

S

D

D

E

E

L

I

F

F

A

G

G

G

Y

Y

Sites not aligning to the query:

391 modified: Phosphoserine
489 modified: Phosphoserine

1jgtB Crystal structure of beta-lactam synthetase (see paper)
30% identity, 41% coverage: 78:341/649 of query aligns to 71:307/500 of 1jgtB

query
sites
1jgtB

V

V

F

L

N
x
A

G
|
G

E

E

I

I

Y

Y

N

N

F

R

L

D

E

E

L

L

R

-

E

-

L

L

T

S

Q

V

L

L

G

P

H

A

N

G

F

P

R

A

G

P

H

E

S

G

D

D

T

A

E

E

I

L

M

V

L

L

A

R

G

L

F

L

S

E

E

R

W

Y

G

D

L

L

D

-

K

H

A

A

I

F

R

R

R

L

F

V

N

N

G

G

M

R

F

F

A

A

F

T

A

V

L

V

W

R

D

T

R

-

Q

G

K

D

R

R

I

V

L

L

H

-

L

L

G

A

R

T

D

D

R

H

L

A

G

G

E

S

K

V

P

P

L

L

Y

Y

Y

T

G

C

W

V

Q

A

G

P

S

G

T

E

F

V

L

R

F

A

T

S

S

T

E

E

L

A

K

K

A

A

L

L

K

A

A

A

H

H

P

R

N

D

F

P

R

K

A

G

E

F

I

P

N

L

R

A

D

D

A

A

L

-

T

-

Q

-

F

-

F

R

R

R

Y

V

S

A

Y

G

L

L

P

-

A

-

P

-

Y

-

S

-

I

-

Y

-

Q

T

G

G

I

V

Y

Y

K

Q

L

V

P

P

P

A

G

G

T

A

L

V

L

M

S

D

W

-

N

-

G

-

I

-

D

-

A

-

H

-

P

-

D

-

P

-

V

I

T

D

Y

L

W

G

S

S

A

G

R

T

E

A

V

V

T

T

E

H

L

R

-

T

-

W

-

T

-

P

G

G

I

L

A

S

E

R

P

R

F

I

M

L

G

-

S

P

E

E

S

G

E

E

A

A

V

V

I

A

Q

A

L

V

E

R

A

A

L

A

L

L

R

E

E

K

A

A

V

V

G

A

L

Q

R

R

M

V

V

T

-

P

A

G

D

D

V

T

P

P

L

L

G

-

A

V

F
x
V

I
x
L

S
|
S

G

G

G
|
G

I
|
I

D
|
D

S
|
S

S

S

T

G

I

V

V

A

A

A

L

C

M

A

Q

H

A

R

Q

A

S

A

S

G

Q

E

P

-

V

-

K

-

T

L

F

D

T

T

I

V

G
x
S

F
x
M

N

G

E

T

E

D

A

T

Y

S

N

N

E

E

A

F

K

R

H

E

A

A

K

R

A

A

V

V

A

V

K

D

H

H

L

L

G

R

T

T

D

R

H

H

T

R

E

E

L

I

Y

T

V

I

N

P

P

T

K

T

E

E

A

L

L

L

E

A

V

Q

I

L

P

P

active site: A73 (≠ N80), G74 (= G81)
binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ F275), L245 (≠ I276), S246 (= S277), G248 (= G279), I249 (= I280), D250 (= D281), S251 (= S282), S269 (≠ G303), M270 (≠ F304)
binding magnesium ion: D250 (= D281)

Sites not aligning to the query:

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

1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
29% identity, 41% coverage: 78:341/649 of query aligns to 67:299/496 of 1mbzA

query
sites
1mbzA

V

V

F

L

N
x
A

G
|
G

E

E

I

I

Y

Y

N

N

F

R

L

D

E

E

L

L

R

-

E

-

L

L

T

S

Q

V

L

L

G

P

H

A

N

G

F

P

R

A

G

P

H

E

S

G

D

D

T

A

E

E

I

L

M

V

L

L

A

R

G

L

F

L

S

E

E

R

W

Y

G

D

L

L

D

-

K

H

A

A

I

F

R

R

R

L

F

V

N

N

G

G

M

R

F

F

A

A

F

T

A

V

L

V

W

R

D

T

R

-

Q

G

K

D

R

R

I

V

L

L

H

-

L

L

G

A

R

T

D

D

R

H

L

A

G

G

E

S

K

V

P

P

L

L

Y

Y

Y

T

G

C

W

V

Q

A

G

P

S

G

T

E

F

V

L

R

F

A

T

S

S

T

E

E

L

A

K

K

A

A

L

L

K

A

A

A

H

H

P

G

N

F

F

P

R

L

A

A

E

D

I

A

N

R

R

R

D

-

A

-

L

-

T

-

Q

-

F

-

R

-

Y

-

S

-

Y

-

L

-

P

-

A

-

P

-

Y

V

S

A

I

G

Y

L

Q

T

G

G

I

V

Y

Y

K

Q

L

V

P

P

P

A

G

G

T

A

L

V

L

M

S

D

W

-

N

-

G

-

I

-

D

-

A

-

H

-

P

-

D

-

P

-

V

I

T

D

Y

L

W

G

S

S

A

G

R

T

E

A

V

V

T

T

E

H

L

R

-

T

-

W

-

T

-

P

G

G

I

L

A

S

E

R

P

R

F

I

M

L

G

-

S

P

E

E

S

G

E

E

A

A

V

V

I

A

Q

A

L

V

E

R

A

A

L

A

L

L

R

E

E

K

A

A

V

V

G

A

L

Q

R

R

M

V

V

T

-

P

A

G

D

D

V

T

P

P

L

L

G

-

A

V

F
x
V

I
x
L

S
|
S

G

G

G
|
G

I

I

D
|
D

S
|
S

S

S

T

G

I

V

V

A

A

A

L

C

M

A

Q

H

A

R

Q

A

S

A

S

G

Q

E

P

-

V

-

K

-

T

L

F

D

T

T

I

V

G
x
S

F
x
M

N

G

E

T

E

D

A

T

Y

S

N

N

E

E

A

F

K

R

H

E

A

A

K

R

A

A

V

V

A

V

K

D

H

H

L

L

G

R

T

T

D

R

H

H

T

R

E

E

L

I

Y

T

V

I

N

P

P

T

K

T

E

E

A

L

L

L

E

A

V

Q

I

L

P

P

active site: A69 (≠ N80), G70 (= G81)
binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ F275), L237 (≠ I276), S238 (= S277), S243 (= S282), S261 (≠ G303), M262 (≠ F304)
binding magnesium ion: D242 (= D281)
binding pyrophosphate 2-: S238 (= S277), G240 (= G279), D242 (= D281), S243 (= S282)

Sites not aligning to the query:

active site: 311, 337, 371, 432
binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: 315, 319, 336, 337, 338, 340, 341, 362, 371, 432, 434, 435
binding magnesium ion: 340
binding pyrophosphate 2-: 340, 412, 432, 433

1mb9A Beta-lactam synthetase complexed with atp (see paper)
29% identity, 41% coverage: 78:341/649 of query aligns to 68:298/485 of 1mb9A

query
sites
1mb9A

V

V

F

L

N
x
A

G
|
G

E

E

I

I

Y

Y

N

N

F

R

L

D

E

E

L

L

R

-

E

-

L

L

T

S

Q

V

L

L

G

P

H

A

N

G

F

P

R

A

G

P

H

E

S

G

D

D

T

A

E

E

I

L

M

V

L

L

A

R

G

L

F

L

S

E

E

R

W

Y

G

D

L

L

D

-

K

H

A

A

I

F

R

R

R

L

F

V

N

N

G

G

M

R

F

F

A

A

F

T

A

V

L

V

W

R

D

T

R

-

Q

G

K

D

R

R

I

V

L

L

H

-

L

L

G

A

R

T

D

D

R

H

L

A

G

G

E

S

K

V

P

P

L

L

Y

Y

Y

T

G

C

W

V

Q

A

G

P

S

G

T

E

F

V

L

R

F

A

T

S

S

T

E

E

L

A

K

K

A

A

L

L

K

A

A

A

H

F

P

P

N

-

F

-

R

-

A

-

E

-

I

-

N

-

R

-

D

-

A

-

L

L

T

A

Q

D

F

A

F

R

R

R

Y

V

S

A

Y

G

L

L

P

-

A

-

P

-

Y

-

S

-

I

-

Y

-

Q

T

G

G

I

V

Y

Y

K

Q

L

V

P

P

P

A

G

G

T

A

L

V

L

M

S

D

W

-

N

-

G

-

I

-

D

-

A

-

H

-

P

-

D

-

P

-

V

I

T

D

Y

L

W

G

S

S

A

G

R

T

E

A

V

V

T

T

E

H

L

R

-

T

-

W

-

T

-

P

G

G

I

L

A

S

E

R

P

R

F

I

M

L

G

-

S

P

E

E

S

G

E

E

A

A

V

V

I

A

Q

A

L

V

E

R

A

A

L

A

L

L

R

E

E

K

A

A

V

V

G

A

L

Q

R

R

M

V

V

T

-

P

A

G

D

D

V

T

P

P

L

L

G

-

A

V

F
x
V

I
x
L

S
|
S

G

G

G
|
G

I

I

D
|
D

S
|
S

S

S

T

G

I

V

V

A

A

A

L

C

M

A

Q

H

A

R

Q

A

S

A

S

G

Q

E

P

-

V

-

K

-

T

L

F

D

T

T

I

V

G
x
S

F
x
M

N

G

E

T

E

D

A

T

Y

S

N

N

E

E

A

F

K

R

H

E

A

A

K

R

A

A

V

V

A

V

K

D

H

H

L

L

G

R

T

T

D

R

H

H

T

R

E

E

L

I

Y

T

V

I

N

P

P

T

K

T

E

E

A

L

L

L

E

A

V

Q

I

L

P

P

active site: A70 (≠ N80), G71 (= G81)
binding adenosine monophosphate: V235 (≠ F275), L236 (≠ I276), S242 (= S282), S260 (≠ G303), M261 (≠ F304)
binding adenosine-5'-triphosphate: V235 (≠ F275), L236 (≠ I276), S237 (= S277), G239 (= G279), D241 (= D281), S242 (= S282), S260 (≠ G303), M261 (≠ F304)
binding magnesium ion: D241 (= D281)
binding pyrophosphate 2-: S237 (= S277), G239 (= G279), D241 (= D281), S242 (= S282)

Sites not aligning to the query:

active site: 310, 336, 370, 431
binding adenosine monophosphate: 314, 318, 335, 336
binding adenosine-5'-triphosphate: 318, 335, 339, 411, 431
binding magnesium ion: 339
binding pyrophosphate 2-: 339, 411, 431

1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
29% identity, 41% coverage: 78:341/649 of query aligns to 63:294/491 of 1mc1A

query
sites
1mc1A

V

V

F

L

N
x
A

G
|
G

E

E

I

I

Y

Y

N

N

F

R

L

D

E

E

L

L

R

-

E

-

L

L

T

S

Q

V

L

L

G

P

H

A

N

G

F

P

R

A

G

P

H

E

S

G

D

D

T

A

E

E

I

L

M

V

L

L

A

R

G

L

F

L

S

E

E

R

W

Y

G

D

L

L

D

-

K

H

A

A

I

F

R

R

R

L

F

V

N

N

G

G

M

R

F

F

A

A

F

T

A

V

L

V

W

R

D

T

R

-

Q

G

K

D

R

R

I

V

L

L

H

-

L

L

G

A

R

T

D

D

R

H

L

A

G

G

E

S

K

V

P

P

L

L

Y

Y

Y

T

G

C

W

V

Q

A

G

P

S

G

T

E

F

V

L

R

F

A

T

S

S

T

E

E

L

A

K

K

A

A

L

L

K

A

A

A

H

-

P

-

N

G

F

F

R

-

A

-

E

-

I

-

N

-

R

-

D

-

A

P

L

L

T

A

Q

D

F

A

F

R

R

R

Y

V

S

A

Y

G

L

L

P

-

A

-

P

-

Y

-

S

-

I

-

Y

-

Q

T

G

G

I

V

Y

Y

K

Q

L

V

P

P

P

A

G

G

T

A

L

V

L

M

S

D

W

-

N

-

G

-

I

-

D

-

A

-

H

-

P

-

D

-

P

-

V

I

T

D

Y

L

W

G

S

S

A

G

R

T

E

A

V

V

T

T

E

H

L

R

-

T

-

W

-

T

-

P

G

G

I

L

A

S

E

R

P

R

F

I

M

L

G

-

S

P

E

E

S

G

E

E

A

A

V

V

I

A

Q

A

L

V

E

R

A

A

L

A

L

L

R

E

E

K

A

A

V

V

G

A

L

Q

R

R

M

V

V

T

-

P

A

G

D

D

V

T

P

P

L

L

G

-

A

V

F
x
V

I

L

S
|
S

G

G

G
|
G

I

I

D
|
D

S
|
S

S

S

T

G

I

V

V

A

A

A

L

C

M

A

Q

H

A

R

Q

A

S

A

S

G

Q

E

P

-

V

-

K

-

T

L

F

D

T

T

I

V

G
x
S

F
x
M

N

G

E

T

E

D

A

T

Y

S

N

N

E

E

A

F

K

R

H

E

A

A

K

R

A

A

V

V

A

V

K

D

H

H

L

L

G

R

T

T

D

R

H

H

T

R

E

E

L

I

Y

T

V

I

N

P

P

T

K

T

E

E

A

L

L

L

E

A

V

Q

I

L

P

P

active site: A65 (≠ N80), G66 (= G81)
binding adenosine monophosphate: V231 (≠ F275), S233 (= S277), S238 (= S282), S256 (≠ G303), M257 (≠ F304)
binding magnesium ion: D237 (= D281)
binding pyrophosphate 2-: S233 (= S277), G235 (= G279), D237 (= D281), S238 (= S282)

Sites not aligning to the query:

active site: 306, 332, 366, 427
binding adenosine monophosphate: 331, 427, 430
binding magnesium ion: 335
binding deoxyguanidinoproclavaminic acid: 310, 332, 333, 336, 357, 366, 427
binding pyrophosphate 2-: 335, 407, 427, 428

1q19A Carbapenam synthetase (see paper)
34% identity, 18% coverage: 272:385/649 of query aligns to 240:352/500 of 1q19A

query
sites
1q19A

L

V

G

G

A

I

F
x
P

I
x
L

S
|
S

G

G

I

L

D
|
D

S
|
S

S

S

T

L

I

V

V

T

A

A

L

L

M

A

Q

-

A

S

Q

R

S

H

S

F

Q

K

P

K

V

L

K

N

T

T

F

Y

T
x
S

I
|
I

G

G

F

-

N

-

E

T

E

E

A

L

Y

S

N

N

E

E

A

F

K

E

H

F

A

S

K

Q

A

Q

V

V

A

A

K

D

H

A

L

L

G

G

T

T

D

H

H

H

T

Q

E

M

L

K

Y

I

V

L

N

S

P

E

K

T

E

E

A

V

L

I

E

N

V

G

I

I

P

I

K

E

L

-

P

S

F

I

L

Y

Y

Y

D

N

E

E

P

I

F

F

S

D

D

G

V
x
L

S

S

-

A

-
x
E

-

I

Q

Q

I

S

P

G

T

L

F

F

L

N

V

V

S

Y

Q

R

L

Q

A

A

K

Q

Q

G

Q

Q

V

V

T

S

V

C

S

M

L

L

S
x
T

G
|
G

D
x
Y

G
|
G

G

S

D
|
D

E
x
L

L

L

F

F

A

G

G

G

active site: L318 (≠ V354), E321 (vs. gap), Y344 (≠ D377)
binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ F275), L244 (≠ I276), S245 (= S277), D249 (= D281), S250 (= S282), S268 (≠ T301), I269 (= I302), T342 (≠ S375), G343 (= G376), D347 (= D380)
binding (2s,5s)-5-carboxymethylproline: Y344 (≠ D377), G345 (= G378), L348 (≠ E381)

Sites not aligning to the query:

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

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)
34% identity, 18% coverage: 272:385/649 of query aligns to 241:353/503 of Q9XB61

query
sites
Q9XB61

L

V

G

G

A

I

F
x
P

I
x
L

S
|
S

G
|
G

I
x
L

D
|
D

S
|
S

S

S

T

L

I

V

V

T

A

A

L

L

M

A

Q

-

A

S

Q

R

S

H

S

F

Q

K

P

K

V

L

K

N

T

T

F

Y

T

S

I
|
I

G

G

F

-

N

-

E

T

E

E

A

L

Y

S

N

N

E

E

A

F

K

E

H

F

A

S

K

Q

A

Q

V

V

A

A

K

D

H

A

L

L

G

G

T

T

D

H

H

H

T

Q

E

M

L

K

Y

I

V

L

N

S

P

E

K

T

E

E

A

V

L

I

E

N

V

G

I

I

P

I

K

E

L

-

P

S

F

I

L

Y

Y

Y

D

N

E

E

P

I

F

F

S

D

D

G

V

L

S

S

-

A

-

E

-

I

Q

Q

I

S

P

G

T

L

F

F

L

N

V

V

S

Y

Q

R

L

Q

A

A

K

Q

Q

G

Q

Q

V

V

T

S

V

C

S

M

L

L

S

T

G
|
G

D
x
Y

G
|
G

G
x
S

D
|
D

E

L

L

L

F

F

A

G

G

G

244:251 (vs. 275:282, 63% identical) binding ATP
I270 (= I302) binding ATP
GYGSD 344:348 (≠ GDGGD 376:380) binding ATP
Y345 (≠ D377) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
G346 (= G378) 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

Query Sequence

>WP_012408102.1 NCBI__GCF_000020025.1:WP_012408102.1
MCGITGFWDISKQFSGEHLDETIQKMSKTLLHRGPDDGGIWTDVEVGVALGHRRLSIVDL
SPLGHQPMMSANGRYMVVFNGEIYNFLELRRELTQLGHNFRGHSDTEIMLAGFSEWGLDK
AIRRFNGMFAFALWDRQKRILHLGRDRLGEKPLYYGWQGSTFLFTSELKALKAHPNFRAE
INRDALTQFFRYSYLPAPYSIYQGIYKLPPGTLLSWNGIDAHPDPVTYWSAREVTELGIA
EPFMGSESEAVIQLEALLREAVGLRMVADVPLGAFISGGIDSSTIVALMQAQSSQPVKTF
TIGFNEEAYNEAKHAKAVAKHLGTDHTELYVNPKEALEVIPKLPFLYDEPFSDVSQIPTF
LVSQLAKQQVTVSLSGDGGDELFAGYNRYLFGRKIWQAIGWIPTTVRKNSARALTSVSPQ
NWNRGFANVNALLPSRIKQPEFGNKLHTFSEIMALPNPTAIYTKLVSHWEDPKALVIDGL
EPPTILSNSQNWPHLLDFTQCMMYFDTVTYLPDDILVKVDRASMGVSLEGRIPFLDHRLV
EFAWRLPLSMKIRNGQGKWLLRQVLYKYVPPTLVERPKVGFGVPINSWLRGPLRDWAEEL
LNENRLKNEGFFNPKPIREKWEEHLSGAASWEYRLWDVLMFQAWLEANH

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