SitesBLAST

H30 (= H28) mutation to A: 4,5-fold decrease in glutamine affinity.
D34 (= D32) mutation D->N,E: Little effect on the kinetic properties.
H81 (= H82) mutation to A: 5-fold decrease in glutamine affinity.
A105 (= A105) mutation to H: Little effect on the kinetic properties.
E349 (≠ D370) 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.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 mutation C->A,S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity.

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, 62% coverage: 1:386/625 of query aligns to 1:380/561 of P08243

query
sites
P08243

M

M

C
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C

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x
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A

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 (≠ A226) to E: in dbSNP:rs1049674
F362 (≠ L367) 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, 62% coverage: 2:386/625 of query aligns to 1:367/509 of 6gq3A

query
sites
6gq3A

C
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C

G

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A

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H

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R

G

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D

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A

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D

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Y
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Y

N
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Y

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H

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x
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A

active site: W4 (≠ T5), L49 (= L51), N74 (= N76), G75 (= G77), T324 (≠ P343), R327 (≠ D346)
binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R50), V51 (≠ I53), V52 (≠ L54), Y73 (= Y75), N74 (= N76), G75 (= G77), E76 (= E78), V95 (≠ S98), D96 (= D99)

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)
32% identity, 57% coverage: 22:379/625 of query aligns to 24:365/557 of P78753

query
sites
P78753

M

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A

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N

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Y

Sites not aligning to the query:

391 modified: Phosphoserine
489 modified: Phosphoserine

1jgtB Crystal structure of beta-lactam synthetase (see paper)
29% identity, 42% coverage: 74:334/625 of query aligns to 71:307/500 of 1jgtB

query
sites
1jgtB

V

V

Y

L

N
x
A

G
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G

E

E

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Y

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N

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K

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D

D

T

A

E

E

T

L

I

V

L

L

A

R

A

L

V

L

S

E

A

R

W

Y

G

D

V

L

G

-

K

H

A

A

I

F

E

R

K

L

F

V

V

N

G

G

M

R

F

F

A

A

F

T

G

V

L

V

W

-

D

-

K

R

K

T

T

G

R

D

K

R

L

V

T

L

L

L

V

A

R

T

D

D

R

H

L

A

G

G

I

S

K

V

P

P

L

L

Y

Y

Y

T

G

C

I

V

A

A

E

P

D

-

G

G

A

E

W

V

V

R

F

A

G

S

S

T

E

E

L

A

K

K

A

A

L

L

-

A

H

H

R

R

Y

D

P

P

A

K

Y

G

S

F

P

P

S

L

I

A

D

D

R

A

N

R

A

R

L

V

A

A

L

G

F

L

F

T

R

G

H

V

N

Y

Y

Q

I

V

P

P

A

A

P

G

Y

A

S

V

I

M

Y

D

E

-

K

-

T

-

W

-

K

-

L

-

E

-

P

-

G

-

Q

-

M

-

V

I

V

D

L

L

G

G

E

S

E

G

E

T

P

A

E

V

V

T

T

H

R

R

W

T

W

W

D

T

I

P

D

G

A

L

V

S

W

R

R

R

E

-

G

-

F

-

D

-

N

-

P

-

W

-

Q

I

M

L

S

P

D

E

H

G

D

E

A

A

V

V

N

A

E

A

L

V

E

R

S

A

L

A

L

L

S

E

D

K

A

A

V

V

G

A

I

Q

R

R

M

V

L

T

-

P

S

G

D

D

V

T

P

P

L

L

G

-

A

V

F
x
V

L
|
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

K

R

Q

A

A

A

T

G

S

E

P

-

V

L

K

D

T

T

F

V

S
|
S

I
x
M

G

G

F

T

H

D

E

T

A

S

A

-

F

-

N

N

E

E

A

F

K

R

H

E

A

A

R

R

A

A

V

V

A

V

D

D

H

H

L

L

G

R

T

T

D

R

H

H

T

R

E

E

L

I

Y

T

V

I

T

P

S

T

G

T

D

E

L

L

D

A

V

Q

V

L

P

P

active site: A73 (≠ N76), G74 (= G77)
binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ F268), L245 (= L269), S246 (= S270), G248 (= G272), I249 (= I273), D250 (= D274), S251 (= S275), S269 (= S294), M270 (≠ I295)
binding magnesium ion: D250 (= D274)

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

6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
29% identity, 24% coverage: 44:196/625 of query aligns to 67:250/460 of 6lbpA

query
sites
6lbpA

V

I

A

A

L

I

G

G

H

H

R

V

R

R

L

Y

S

S

I

T

L

A

D

G

L

S

S

S

P

M

L

L

G

K

R

N

-

V

Q

Q

P

P

M

F

V

V

S

A

A

G

-

Y

-

R

C

F

G

G

R

S

Y

V

V

G

I

V

V

A

Y

H

N
|
N

G
|
G

E

N

V

L

Y

V

N

N

H

Y

L

T

T

K

L

L

R

R

N

A

E

D

L

L

-

E

H

N

S

G

Y

S

P

I

F

F

K

N

S

T

S

S

D

D

T

T

E

E

T

V

I

V

L

L

A

H

A

L

V

I

S

A

A

I

-

S

-

K

-

A

-

R

-

P

-

F

W

M

G

R

V

I

G

V

K

D

A

A

I

C

E

E

K

K

F

L

V

Q

G

G

M

A

F

Y

A

S

F

M

G

V

L

F

W

V

D

T

K

E

K

D

T

-

R

-

K

K

L

L

T

V

L

A

V

V

R

R

D

D

R

P

L

H

G

G

I

F

K

R

P

P

L

L

Y

V

Y

M

G

G

I

R

A

R

E

S

D

N

G

G

A

A

W

V

V

V

F

F

G

A

S

S

E

E

L

T

K

C

A

A

L

L

-

D

-

L

-

I

-

E

-

A

-

T

-

Y

-

E

-

R

H

E

R

V

Y

Y

P

P

A

G

Y

E

S

V

P

L

S

V

I

V

D

D

R

K

N

D

A

G

L

V

A

K

-

C

-

Q

-

C

-

L

-

M

-

P

-

H

-

P

-

E

-

P

-

K

-

Q

L
x
C

F

I

F
|
F

R

E

H

H

N

I

Y
|
Y

I

F

P

S

A

L

P

P

Y

N

S

S

I

I

active site: N102 (= N76), G103 (= G77), Y243 (= Y189)
binding iron/sulfur cluster: C237 (≠ L183), F239 (= F185)

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)
29% identity, 24% coverage: 44:196/625 of query aligns to 153:336/561 of Q9STG9

query
sites
Q9STG9

V

I

A

A

L

I

G

G

H

H

R

V

R

R

L

Y

S

S

I

T

L

A

D

G

L

S

S

S

P

M

L

L

G

K

R

N

-

V

Q

Q

P

P

M

F

V

V

S

A

A

G

-

Y

-

R

C

F

G

G

R

S

Y

V

V

G

I

V

V

A

Y
x
H

N

N

G

G

E

N

V

L

Y

V

N

N

H

Y

L

T

T

K

L

L

R

R

N

A

E

D

L

L

-

E

H

N

S

G

Y

S

P

I

F

F

K

N

S

T

S

S

D

D

T

T

E

E

T

V

I

V

L

L

A

H

A

L

V

I

S

A

A

I

-

S

-

K

-

A

-

R

-

P

-

F

W

M

G

R

V

I

G

V

K

D

A

A

I

C

E

E

K

K

F

L

V

Q

G

G

M

A

F

Y

A

S

F

M

G

V

L

F

W

V

D

T

K

E

K

D

T

-

R

-

K

K

L

L

T

V

L

A

V

V

R

R

D

D

R

P

L

H

G

G

I

F

K
x
R

P
|
P

L

L

Y

V

Y

M

G

G

I

R

A

R

E

S

D

N

G

G

A

A

W

V

V

V

F

F

G

A

S

S

E

E

L

T

K

C

A

A

L

L

-

D

-

L

-

I

-

E

-

A

-

T

-

Y

-

E

-

R

H

E

R

V

Y

Y

P

P

A

G

Y

E

S

V

P

L

S

V

I

V

D

D

R

K

N

D

A

G

L

V

A

K

-

C

-

Q

-

C

-

L

-

M

-

P

-

H

-

P

-

E

-

P

-

K

-

Q

L

C

F

I

F

F

R

E

H

H

N

I

Y

Y

I

F

P

S

A

L

P

P

Y

N

S

S

I

I

H187 (≠ Y75) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
R264 (≠ K145) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
P265 (= P146) 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.

1mb9A Beta-lactam synthetase complexed with atp (see paper)
29% identity, 42% coverage: 74:334/625 of query aligns to 68:298/485 of 1mb9A

query
sites
1mb9A

V

V

Y

L

N
x
A

G
|
G

E

E

V

I

Y

Y

N

N

H

R

L

D

T

E

L

L

R

L

N

S

E

V

L

L

H

P

S

A

Y

G

P

P

F

-

K

A

S

P

S

E

S

G

D

D

T

A

E

E

T

L

I

V

L

L

A

R

A

L

V

L

S

E

A

R

W

Y

G

D

V

L

G

-

K

H

A

A

I

F

E

R

K

L

F

V

V

N

G

G

M

R

F

F

A

A

F

T

G

V

L

V

W

-

D

-

K

R

K

T

T

G

R

D

K

R

L

V

T

L

L

L

V

A

R

T

D

D

R

H

L

A

G

G

I

S

K

V

P

P

L

L

Y

Y

Y

T

G

C

I

V

A

A

E

P

D

-

G

G

A

E

W

V

V

R

F

A

G

S

S

T

E

E

L

A

K

K

A

A

L

L

H

A

R

A

Y

F

P

P

A

-

Y

-

S

-

P

-

S

-

I

-

D

-

R

-

N

-

A

-

L

L

A

A

L

D

F

A

F

R

R

R

H

V

N

A

Y

G

I

L

P

T

A

G

P

V

Y

Y

S

Q

I

V

Y

-

E

-

K

-

T

-

W

-

K

-

L

-

E

-

P

P

G

A

Q

G

M

A

V

V

V

M

-

D

-

I

-

D

L

L

G

G

E

S

E

G

E

T

P

A

E

V

V

T

T

H

R

R

W

T

W

W

D

T

I

P

D

G

A

L

V

S

W

R

R

R

E

-

G

-

F

-

D

-

N

-

P

-

W

-

Q

I

M

L

S

P

D

E

H

G

D

E

A

A

V

V

N

A

E

A

L

V

E

R

S

A

L

A

L

L

S

E

D

K

A

A

V

V

G

A

I

Q

R

R

M

V

L

T

-

P

S

G

D

D

V

T

P

P

L

L

G

-

A

V

F
x
V

L
|
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

K

R

Q

A

A

A

T

G

S

E

P

-

V

L

K

D

T

T

F

V

S
|
S

I
x
M

G

G

F

T

H

D

E

T

A

S

A

-

F

-

N

N

E

E

A

F

K

R

H

E

A

A

R

R

A

A

V

V

A

V

D

D

H

H

L

L

G

R

T

T

D

R

H

H

T

R

E

E

L

I

Y

T

V

I

T

P

S

T

G

T

D

E

L

L

D

A

V

Q

V

L

P

P

active site: A70 (≠ N76), G71 (= G77)
binding adenosine monophosphate: V235 (≠ F268), L236 (= L269), S242 (= S275), S260 (= S294), M261 (≠ I295)
binding adenosine-5'-triphosphate: V235 (≠ F268), L236 (= L269), S237 (= S270), G239 (= G272), D241 (= D274), S242 (= S275), S260 (= S294), M261 (≠ I295)
binding magnesium ion: D241 (= D274)
binding pyrophosphate 2-: S237 (= S270), G239 (= G272), D241 (= D274), S242 (= S275)

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

1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
29% identity, 42% coverage: 74:334/625 of query aligns to 67:299/496 of 1mbzA

query
sites
1mbzA

V

V

Y

L

N
x
A

G
|
G

E

E

V

I

Y

Y

N

N

H

R

L

D

T

E

L

L

R

L

N

S

E

V

L

L

H

P

S

A

Y

G

P

P

F

-

K

A

S

P

S

E

S

G

D

D

T

A

E

E

T

L

I

V

L

L

A

R

A

L

V

L

S

E

A

R

W

Y

G

D

V

L

G

-

K

H

A

A

I

F

E

R

K

L

F

V

V

N

G

G

M

R

F

F

A

A

F

T

G

V

L

V

W

-

D

-

K

R

K

T

T

G

R

D

K

R

L

V

T

L

L

L

V

A

R

T

D

D

R

H

L

A

G

G

I

S

K

V

P

P

L

L

Y

Y

Y

T

G

C

I

V

A

A

E

P

D

-

G

G

A

E

W

V

V

R

F

A

G

S

S

T

E

E

L

A

K

K

A

A

L

L

-

A

H

H

R

G

Y

F

P

P

A

-

Y

-

S

-

P

-

S

-

I

-

D

-

R

-

N

-

A

-

L

L

A

A

L

D

F

A

F

R

R

R

H

V

N

A

Y

G

I

L

P

T

A

G

P

V

Y

Y

S

Q

I

V

Y

-

E

-

K

-

T

-

W

-

K

-

L

-

E

-

P

P

G

A

Q

G

M

A

V

V

V

M

-

D

-

I

-

D

L

L

G

G

E

S

E

G

E

T

P

A

E

V

V

T

T

H

R

R

W

T

W

W

D

T

I

P

D

G

A

L

V

S

W

R

R

R

E

-

G

-

F

-

D

-

N

-

P

-

W

-

Q

I

M

L

S

P

D

E

H

G

D

E

A

A

V

V

N

A

E

A

L

V

E

R

S

A

L

A

L

L

S

E

D

K

A

A

V

V

G

A

I

Q

R

R

M

V

L

T

-

P

S

G

D

D

V

T

P

P

L

L

G

-

A

V

F
x
V

L
|
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

K

R

Q

-

A

A

T

A

S

G

P

E

V

L

K

D

T

T

F

V

S
|
S

I
x
M

G

G

F

T

H

D

E

T

A

S

A

-

F

-

N

N

E

E

A

F

K

R

H

E

A

A

R

R

A

A

V

V

A

V

D

D

H

H

L

L

G

R

T

T

D

R

H

H

T

R

E

E

L

I

Y

T

V

I

T

P

S

T

G

T

D

E

L

L

D

A

V

Q

V

L

P

P

active site: A69 (≠ N76), G70 (= G77)
binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ F268), L237 (= L269), S238 (= S270), S243 (= S275), S261 (= S294), M262 (≠ I295)
binding magnesium ion: D242 (= D274)
binding pyrophosphate 2-: S238 (= S270), G240 (= G272), D242 (= D274), S243 (= S275)

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

1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
29% identity, 42% coverage: 74:334/625 of query aligns to 63:294/491 of 1mc1A

query
sites
1mc1A

V

V

Y

L

N
x
A

G
|
G

E

E

V

I

Y

Y

N

N

H

R

L

D

T

E

L

L

R

L

N

S

E

V

L

L

H

P

S

A

Y

G

P

P

F

-

K

A

S

P

S

E

S

G

D

D

T

A

E

E

T

L

I

V

L

L

A

R

A

L

V

L

S

E

A

R

W

Y

G

D

V

L

G

-

K

H

A

A

I

F

E

R

K

L

F

V

V

N

G

G

M

R

F

F

A

A

F

T

G

V

L

V

W

-

D

-

K

R

K

T

T

G

R

D

K

R

L

V

T

L

L

L

V

A

R

T

D

D

R

H

L

A

G

G

I

S

K

V

P

P

L

L

Y

Y

Y

T

G

C

I

V

A

A

E

P

D

-

G

G

A

E

W

V

V

R

F

A

G

S

S

T

E

E

L

A

K

K

A

A

L

L

H

-

R

-

Y

-

P

A

A

A

Y

G

S

F

P

P

S

L

I

A

D

D

R

A

N

R

A

R

L

V

A

A

L

G

F

L

F

T

R

G

H

V

N

Y

Y

Q

I

V

P

P

A

A

P

G

Y

A

S

V

I

M

Y

D

E

-

K

-

T

-

W

-

K

-

L

-

E

-

P

-

G

-

Q

-

M

-

V

I

V

D

L

L

G

G

E

S

E

G

E

T

P

A

E

V

V

T

T

H

R

R

W

T

W

W

D

T

I

P

D

G

A

L

V

S

W

R

R

R

E

-

G

-

F

-

D

-

N

-

P

-

W

-

Q

I

M

L

S

P

D

E

H

G

D

E

A

A

V

V

N

A

E

A

L

V

E

R

S

A

L

A

L

L

S

E

D

K

A

A

V

V

G

A

I

Q

R

R

M

V

L

T

-

P

S

G

D

D

V

T

P

P

L

L

G

-

A

V

F
x
V

L

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

K

R

Q

-

A

A

T

A

S

G

P

E

V

L

K

D

T

T

F

V

S
|
S

I
x
M

G

G

F

T

H

D

E

T

A

S

A

-

F

-

N

N

E

E

A

F

K

R

H

E

A

A

R

R

A

A

V

V

A

V

D

D

H

H

L

L

G

R

T

T

D

R

H

H

T

R

E

E

L

I

Y

T

V

I

T

P

S

T

G

T

D

E

L

L

D

A

V

Q

V

L

P

P

active site: A65 (≠ N76), G66 (= G77)
binding adenosine monophosphate: V231 (≠ F268), S233 (= S270), S238 (= S275), S256 (= S294), M257 (≠ I295)
binding magnesium ion: D237 (= D274)
binding pyrophosphate 2-: S233 (= S270), G235 (= G272), D237 (= D274), S238 (= S275)

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)
32% identity, 18% coverage: 265:378/625 of query aligns to 240:352/500 of 1q19A

query
sites
1q19A

L

V

G

G

A

I

F
x
P

L
|
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

S

K

R

Q

H

A

-

T

F

S

K

P

K

V

L

K

N

T

T

F

Y

S
|
S

I
|
I

G

G

F

T

H

E

E

L

A

S

A

-

F

-

N

N

E

E

A

F

K

E

H

F

A

S

R

Q

A

Q

V

V

A

A

D

D

H

A

L

L

G

G

T

T

D

H

H

H

T

Q

E

M

L

K

Y

I

V

L

T

S

S

E

G

T

D

E

L

V

L

I

D

N

-

G

V

I

P

E

S

S

M

I

P

-

Q

-

C

Y

W

Y

D

N

E

E

P

I

F

F

A

D

D

G

L
|
L

S

S

-

A

-
x
E

-

I

Q

Q

I

S

P

G

T

L

Y

F

I

N

L

V

S

Y

K

R

L

Q

T

A

R

Q

E

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

S

G

G

G

active site: L318 (= L347), E321 (vs. gap), Y344 (≠ D370)
binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ F268), L244 (= L269), S245 (= S270), D249 (= D274), S250 (= S275), S268 (= S294), I269 (= I295), T342 (≠ S368), G343 (= G369), D347 (= D373)
binding (2s,5s)-5-carboxymethylproline: Y344 (≠ D370), G345 (= G371), L348 (≠ E374)

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)
32% identity, 18% coverage: 265:378/625 of query aligns to 241:353/503 of Q9XB61

query
sites
Q9XB61

L

V

G

G

A

I

F
x
P

L
|
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

S

K

R

Q

H

A

-

T

F

S

K

P

K

V

L

K

N

T

T

F

Y

S

S

I
|
I

G

G

F

T

H

E

E

L

A

S

A

-

F

-

N

N

E

E

A

F

K

E

H

F

A

S

R

Q

A

Q

V

V

A

A

D

D

H

A

L

L

G

G

T

T

D

H

H

H

T

Q

E

M

L

K

Y

I

V

L

T

S

S

E

G

T

D

E

L

V

L

I

D

N

-

G

V

I

P

E

S

S

M

I

P

-

Q

-

C

Y

W

Y

D

N

E

E

P

I

F

F

A

D

D

G

L

L

S

S

-

A

-

E

-

I

Q

Q

I

S

P

G

T

L

Y

F

I

N

L

V

S

Y

K

R

L

Q

T

A

R

Q

E

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

S

G

G

G

244:251 (vs. 268:275, 75% identical) binding ATP
I270 (= I295) binding ATP
GYGSD 344:348 (≠ GDGGD 369:373) binding ATP
Y345 (≠ D370) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
G346 (= G371) 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_026167556.1 NCBI__GCF_000375485.1:WP_026167556.1
MCGITGFISSGSGSDSHCIERMVESLSHRGPDQFGVWNDGAAGVALGHRRLSILDLSPLG
RQPMVSACGRYVIVYNGEVYNHLTLRNELHSYPFKSSSDTETILAAVSAWGVGKAIEKFV
GMFAFGLWDKKTRKLTLVRDRLGIKPLYYGIAEDGAWVFGSELKALHRYPAYSPSIDRNA
LALFFRHNYIPAPYSIYEKTWKLEPGQMVVLGEEEPEVTRWWDIDAVWREGFDNPWQMSD
HDAVNELESLLSDAVGIRMLSDVPLGAFLSGGIDSSTIVALMQKQATSPVKTFSIGFHEA
AFNEAKHARAVADHLGTDHTELYVTSGDLLDVVPSMPQCWDEPFADLSQIPTYILSKLTR
EQVTVSLSGDGGDELFSGYARYFYASKWDTLTKLPVAFRRIIMGALKVSPPSLFKLLGSF
GPKLRWRLDLLGMREFCEFYRYILSHFKHPDEFVLGAQEWPTPLTDGNPVMSDRFAYMAL
KDLQMYLPGDILTKVDRASMAVGLEARVPLLDHRVVEFAARTPVSSKIRVGEGKWLLRQV
LYRHVPQKIVDRPKMGFGVPIEGWMRNELREWCEDMLSPEAIARQGFIDPKMVERMWNEF
LGGETDWNYYLWDILMFQSWLEEWA

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