SitesBLAST

K7 (= K16) mutation to A: Loss of aspartokinase activity.; mutation to M: Loss of aspartokinase activity.
G9 (= G18) mutation to M: Loss of aspartokinase activity.
G10 (= G19) mutation to A: Significant decrease in the catalytic efficiency.
S41 (= S58) mutation to A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
A42 (= A59) mutation to S: Loss of aspartokinase activity.
T47 (= T64) mutation to A: Significant decrease in the affinity for aspartic acid. Requires higher concentration of magnesium ion than wild-type.
E74 (= E91) mutation to A: Loss of aspartokinase activity.; mutation to Q: Loss of aspartokinase activity.
G135 (= G153) mutation to A: Very low catalytic efficiency.; mutation to S: Loss of aspartokinase activity.
R150 (= R168) mutation to A: Significant decrease in the catalytic efficiency.
D154 (= D172) mutation to A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.; mutation to N: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type.
D174 (= D192) mutation to A: Significant decrease in the catalytic efficiency.
D182 (= D200) mutation to A: Significant decrease in the catalytic efficiency.Requires higher concentration of magnesium ion than wild-type.

P41398 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Corynebacterium flavescens (see paper)
34% identity, 56% coverage: 12:248/421 of query aligns to 3:231/421 of P41398

query
sites
P41398

V

L

V

V

L

Q

K

K

F

Y

G

G

A

S

F

L

A

E

A

S

P

A

G

E

A

R

H

-

Q

-

G

-

I

-

A

I

R

R

H

N

V

V

A

A

D

E

R

R

L

I

R

V

A

A

G

-

S

-

A

T

S

K

P

K

G

A

G

G

A

N

R

D

A

V

I

V

V

V

V

C

S

S

A

A

V

M

A

G

G

D

E

T

T

T

D

D

R

E

L

L

G

L

T

E

A

L

L

A

R

A

A

A

V

V

S

N

P

P

A

V

P

P

D

P

R

A

D

R

L

E

L

M

A

D

A

M

A

L

L

L

M

T

T

A

G

G

E

E

T

R

V

I

N

S

V

N

A

A

L

L

M

V

T

A

A

M

A

A

L

I

R

E

D

S

A

L

G

G

L

A

A

E

A

A

V

Q

A

S

L

F

T

T

A

G

A

S

D

Q

T

A

G

G

F

V

V

L

G

T

A

T

G

-

E

E

P

R

H

H

C

-

A

G

D

N

L

A

R

R

R

I

I

V

D

D

-

V

-

T

-

P

G

G

S

R

V

V

L

R

A

E

S

A

L

L

V

D

E

E

P

-

A

-

G

G

T

K

V

I

L

C

V

I

V

V

P

A

G

G

G

F

Q

Q

A

G

V

V

D

N

G

K

D

E

G

T

R

R

P

D

I

V

M

T

-

T

L

L

G

G

R

R

N

G

S

G

S

S

D

D

L

T

S

T

A

A

I

V

A

A

A

L

A

A

I

A

A

A

V

L

G

N

A

A

R

D

A

V

C

C

E

E

I

I

F

Y

S

S

D

D

S

V

P

D

G

G

I

V

C

Y

T

T

A

A

D

D

P

P

R

R

L

I

V

V

P

P

D

N

A

A

R

Q

T

K

L

L

A

E

A

K

V

L

D

S

Y

F

D

E

T

E

M

M

I

L

T

E

M

L

S

A

R

A

H

V

G

G

A

S

K

K

V

I

L

L

H

V

H

L

S

R

A

S

V

V

A

E

W

Y

A

A

Q

R

R

A

H

F

G

N

V

V

E

P

I

L

R

R

C

V

R

R

S

S

Sites not aligning to the query:

345 D→G: Decreased sensitivity of AK activity to concerted feedback inhibition by lysine and threonine.

P26512 Aspartokinase; Aspartate kinase; EC 2.7.2.4 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see 2 papers)
34% identity, 56% coverage: 12:248/421 of query aligns to 3:231/421 of P26512

query
sites
P26512

V

L

V

V

L

Q

K

K

F

Y

G

G

A

S

F

L

A

E

A

S

P

A

G

E

A

R

H

-

Q

-

G

-

I

-

A

I

R

R

H

N

V

V

A

A

D

E

R

R

L

I

R

V

A

A

G

-

S

-

A

T

S

K

P

K

G

A

G

G

A

N

R

D

A

V

I

V

V

V

V

C

S

S

A

A

V

M

A

G

G

D

E

T

T

T

D

D

R

E

L

L

G

L

T

E

A

L

L

A

R

A

A

A

V

V

S

N

P

P

A

V

P

P

D

P

R

A

D

R

L

E

L

M

A

D

A

M

A

L

L

L

M

T

T

A

G

G

E

E

T

R

V

I

N

S

V

N

A

A

L

L

M

V

T

A

A

M

A

A

L

I

R

E

D

S

A

L

G

G

L

A

A

E

A

A

V

Q

A

S

L

F

T

T

A

G

A

S

D

Q

T

A

G

G

F

V

V

L

G

T

A

T

G

-

E

E

P

R

H

H

C

-

A

G

D

N

L

A

R

R

R

I

I

V

D

D

-

V

-

T

-

P

G

G

S

R

V

V

L

R

A

E

S

A

L

L

V

D

E

E

P

-

A

-

G

G

T

K

V

I

L

C

V

I

V

V

P

A

G

G

G

F

Q

Q

A

G

V

V

D

N

G

K

D

E

G

T

R

R

P

D

I

V

M

T

-

T

L

L

G

G

R

R

N

G

S

G

S

S

D

D

L

T

S

T

A

A

I

V

A

A

A

L

A

A

I

A

A

A

V

L

G

N

A

A

R

D

A

V

C

C

E

E

I

I

F

Y

S

S

D

D

S

V

P

D

G

G

I

V

C

Y

T

T

A

A

D

D

P

P

R

R

L

I

V

V

P

P

D

N

A

A

R

Q

T

K

L

L

A

E

A

K

V

L

D

S

Y

F

D

E

T

E

M

M

I

L

T

E

M

L

S

A

R

A

H

V

G

G

A

S

K

K

V

I

L

L

H

V

H

L

S

R

A

S

V

V

A

E

W

Y

A

A

Q

R

R

A

H

F

G

N

V

V

E

P

I

L

R

R

C

V

R

R

S

S

Sites not aligning to the query:

277 G→A: Change in the inhibitory profile upon addition of threonine.
279 A→V: Absence of inhibition upon addition of threonine and lysine or lysine alone.
298 Q→A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
301 S→F: Absence of inhibition upon addition of threonine and lysine or lysine alone.; S→Y: Feedback-resistant and enhanced expression of the asd gene.
360 V→A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.
361 T→A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
363 E→A: Change in the inhibitory profile and absence of dimerization upon addition of threonine.
364 F→A: Change in the inhibitory profile and shows an different oligomer state upon addition of threonine.

3aawC Crystal structure of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
32% identity, 56% coverage: 12:248/421 of query aligns to 3:214/392 of 3aawC

query
sites
3aawC

V

L

V

V

L

Q

K
|
K

F

Y

G

G

A

S

F

L

A

E

A

S

P

A

G

E

A

R

H

-

Q

-

G

-

I

-

A

I

R

R

H

N

V

V

A

A

D

E

R

R

L

I

R

V

A

A

G

-

S

-

A

T

S

K

P

K

G

A

G

G

A

N

R

D

A

V

I

V

V

V

V

C

S
|
S

A

A

V

M

A

G

G

D

E

T

T

T

D

D

R

E

L

L

G

L

T

E

A

L

L

A

R

A

A

A

V

V

S

N

P

P

A

V

P

P

D

P

R

A

D

R

L

E

L

M

A

D

A

M

A

L

L

L

M

T

T

A

G

G

E

E

T

R

V

I

N

S

V

N

A

A

L

L

M

V

T

A

A

M

A

A

L

I

R

E

D

S

A

L

G

G

L

A

A

E

A

A

V

Q

A

S

L

F

T

T

A

G

A

S

D

Q

T

-

G

-

F

-

V

-

G

-

A

-

G

-

E

-

P

-

H

-

C

-

A

-

D

D

L

V

R

-

I

T

D

P

G

G

S

R

V

V

L

R

A

E

S

A

L

L

V

D

E

E

P

-

A

-

G

G

T

K

V

I

L

C

V

I

V

V

P

A

G

G

G

F

Q

Q

A

G

V

V

D

N

G

K

D

-

G

-

R

R

P

D

I

V

M

T

-

T

L

L

G

G

R

R

N

G

S
x
G

S
|
S

D
|
D

L

T

S

T

A

A

I

V

A

A

A

L

A

A

I

A

A

A

V

L

G

N

A

A

R

D

A

V

C

C

E

E

I

I

F

Y

S

S

D

D

S

V

P

D

G

G

I

V

C

Y

T

T

A

A

D

D

P

P

R

R

L

I

V

V

P

P

D

N

A

A

R

Q

T

K

L

L

A

E

A

K

V

L

D

S

Y

F

D

E

T

E

M

M

I

L

T

E

M

L

S

A

R

A

H

V

G

G

A

S

K

K

V

I

L

L

H

V

H

L

S

R

A

S

V

V

A

E

W

Y

A

A

Q

R

R

A

H

F

G

N

V

V

E

P

I

L

R

R

C

V

R

R

S

S

binding lysine: K7 (= K16), S41 (= S58), G136 (≠ S170), S137 (= S171), D138 (= D172)

Sites not aligning to the query:

binding lysine: 337, 340, 344, 364
binding threonine: 258, 260, 261, 262, 281, 357, 358

3c1nA Crystal structure of allosteric inhibition threonine-sensitive aspartokinase from methanococcus jannaschii with l-threonine (see paper)
30% identity, 41% coverage: 80:251/421 of query aligns to 120:288/458 of 3c1nA

query
sites
3c1nA

R

R

D

D

L

Y

L

I

A

-

L

L

M

S

T

F

G

G

E

E

T

R

V

L

N

S

V

S

A

P

L

I

M

L

T

S

A

G

A

A

L

I

R

R

D

D

A

L

G

G

L

E

A

K

A

S

V

I

A

A

L

L

T

E

A

G

D

E

T

A

G

G

F

I

V

I

G

T

A

D

G

N

E

N

P

F

H

G

C

S

A

A

D

R

L

V

R

K

R

R

I

L

D

E

-

V

-

K

G

E

S

R

V

L

L

L

A

P

S

L

L

L

V

K

E

E

P

-

A

-

G

G

T

I

V

I

L

P

V

V

P

T

G

G

G

F

Q

I

A

G

V

T

D

T

G

E

D

E

G

G

R

Y

P

I

I

T

M

T

L

L

G

G

R

R

N

G

S

G

S

S

D

D

L

Y

S

S

A

A

I

A

A

L

A

I

A

G

I

Y

A

G

V

L

G

D

A

A

R

D

A

I

C

I

E

E

I

I

F
x
W

S
x
T

D
|
D

S

V

P

S

G

G

I

V

C

Y

T

T

A

T

D

D

P

P

R

R

L

L

V

V

P

P

D

T

A

A

R

R

T

R

L

I

A

P

A

K

V

L

D

S

Y

Y

D

I

T

E

M

A

I

M

T

E

M

L

S

A

R

Y

H

F

G

G

A

A

K

K

V

V

L

L

H

H

H

P

S

R

A

T

V

I

A

E

W

P

A

A

Q

M

R

E

H

K

G

G

V

I

E

P

I

I

R

L

C

V

R

K

S

N

L

T

L

F

P

E

binding threonine: W227 (≠ F190), T228 (≠ S191), D229 (= D192)

Sites not aligning to the query:

binding threonine: 7, 8, 9, 10, 406, 409, 410, 423, 424, 429, 433

3c1mC Cyrstal structure of threonine-sensitive aspartokinase from methanococcus jannaschii with mgamp-pnp and l-aspartate (see paper)
30% identity, 41% coverage: 80:251/421 of query aligns to 121:289/468 of 3c1mC

query
sites
3c1mC

R

R

D

D

L

Y

L

I

A

-

L

L

M

S

T

F

G

G

E
|
E

T

R

V

L

N

S

V

S

A

P

L

I

M

L

T

S

A

G

A

A

L

I

R

R

D

D

A

L

G

G

L

E

A

K

A

S

V

I

A

A

L

L

T

E

A

G

D

E

T

A

G

G

F

I

V

I

G

T

A

D

G

N

E

N

P

F

H

G

C

S

A

A

D

R

L

V

R

K

R

R

I

L

D

E

-

V

-

K

G

E

S

R

V

L

L

L

A

P

S

L

L

L

V

K

E

E

P

-

A

-

G

G

T

I

V

I

L

P

V

V

P

T

G

G

G
x
F

Q

I

A

G

V

T

D

T

G

E

D

E

G

G

R

Y

P

I

I

T

M

T

L

L

G

G

R
|
R

N
x
G

S

G

S
|
S

D

D

L

Y

S

S

A

A

I

A

A

L

A

I

A

G

I

Y

A

G

V

L

G

D

A

A

R

D

A

I

C

I

E

E

I

I

F

W

S
x
T

D
|
D

S

V

P

S

G

G

I

V

C
x
Y

T

T

A

T

D
|
D

P
|
P

R
|
R

L

L

V

V

P

P

D

T

A

A

R

R

T

R

L

I

A

P

A

K

V

L

D

S

Y

Y

D

I

T

E

M

A

I

M

T

E

M

L

S

A

R

Y

H

F

G

G

A

A

K
|
K

V
|
V

L

L

H

H

H

P

S

R

A

T

V

I

A

E

W

P

A

A

Q

M

R

E

H

K

G

G

V

I

E

P

I

I

R

L

C

V

R

K

S

N

L

T

L

F

P

E

binding phosphoaminophosphonic acid-adenylate ester: T229 (≠ S191), D230 (= D192), Y235 (≠ C197), D238 (= D200), P239 (= P201), R240 (= R202), K265 (= K227), V266 (= V228)
binding aspartic acid: E129 (= E91), F192 (≠ G154), R206 (= R168), G207 (≠ N169), S209 (= S171)

Sites not aligning to the query:

2hmfA Structure of a threonine sensitive aspartokinase from methanococcus jannaschii complexed with mg-adp and aspartate (see paper)
30% identity, 41% coverage: 80:251/421 of query aligns to 121:289/464 of 2hmfA

query
sites
2hmfA

R

R

D

D

L

Y

L

I

A

-

L

L

M

S

T

F

G

G

E

E

T

R

V

L

N

S

V

S

A

P

L

I

M

L

T

S

A

G

A

A

L

I

R

R

D

D

A

L

G

G

L

E

A

K

A

S

V

I

A

A

L

L

T

E

A

G

D

E

T

A

G

G

F

I

V

I

G

T

A

D

G

N

E

N

P

F

H

G

C

S

A

A

D

R

L

V

R

K

R

R

I

L

D

E

-

V

-

K

G

E

S

R

V

L

L

L

A

P

S

L

L

L

V

K

E

E

P

-

A

-

G

G

T

I

V

I

L

P

V

V

P

T

G

G

G
x
F

Q

I

A

G

V

T

D

T

G

E

D

E

G

G

R

Y

P

I

I

T

M

T

L

L

G

G

R
|
R

N
x
G

S

G

S
|
S

D

D

L

Y

S

S

A

A

I

A

A

L

A

I

A

G

I

Y

A

G

V

L

G

D

A

A

R

D

A

I

C

I

E

E

I

I

F

W

S
x
T

D
|
D

S
x
V

P

S

G

G

I

V

C
x
Y

T

T

A
x
T

D
|
D

P
|
P

R
|
R

L

L

V

V

P

P

D

T

A

A

R

R

T

R

L

I

A

P

A

K

V

L

D

S

Y

Y

D

I

T

E

M

A

I

M

T

E

M

L

S

A

R

Y

H

F

G

G

A

A

K
|
K

V
|
V

L

L

H

H

H

P

S

R

A

T

V

I

A

E

W

P

A

A

Q

M

R

E

H

K

G

G

V

I

E

P

I

I

R

L

C

V

R

K

S

N

L

T

L

F

P

E

binding adenosine-5'-diphosphate: T229 (≠ S191), D230 (= D192), V231 (≠ S193), Y235 (≠ C197), T237 (≠ A199), D238 (= D200), P239 (= P201), R240 (= R202), K265 (= K227), V266 (= V228)
binding aspartic acid: F192 (≠ G154), R206 (= R168), G207 (≠ N169), S209 (= S171)

Sites not aligning to the query:

3ab4A Crystal structure of feedback inhibition resistant mutant of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine (see paper)
30% identity, 56% coverage: 12:248/421 of query aligns to 2:195/370 of 3ab4A

query
sites
3ab4A

V

L

V

V

L

Q

K

K

F

Y

G

G

A

S

F

L

A

E

A

S

P

A

G

E

A

R

H

-

Q

-

G

-

I

-

A

I

R

R

H

N

V

V

A

A

D

E

R

R

L

I

R

V

A

A

G

-

S

-

A

T

S

K

P

K

G

A

G

G

A

N

R

D

A

V

I

V

V

V

V

C

S

S

A

A

V

M

A

G

G

D

E

T

T

T

D

D

R

E

L

L

G

L

T

E

A

L

L

A

R

A

A

A

V

V

S

N

P

P

A

V

P

P

D

P

R

A

D

R

L

E

L

M

A

D

A

M

A

L

L

L

M

T

T

A

G

G

E

E

T

R

V

I

N

S

V

N

A

A

L

L

M

V

T

A

A

M

A

A

L

I

R

E

D

S

A

L

G

G

L

A

A

E

A

A

V

-

A

-

L

-

T

-

A

-

D

-

T

Q

G

S

F

F

V

T

G

G

A

S

G

V

E

T

P

P

H

-

C

-

A

-

D

-

L

-

R

-

I

-

D

-

G

G

S

R

V

V

L

R

A

E

S

A

L

L

V

D

E

E

P

-

A

-

G

G

T

K

V

I

L

C

V

I

V

V

P

G

G

G

G

-

Q

-

A

-

V

-

D

-

G

-

D

-

G

-

R

-

P

-

I

-

M

-

L

-

G

-

R

-

N

-

S

-

S

S

D

D

L

T

S

T

A

A

I

V

A

A

A

L

A

A

I

A

A

A

V

L

G

N

A

A

R

D

A

V

C

C

E

E

I

I

F

Y

S

S

D

D

S

V

P

D

G

G

I

V

C

Y

T

T

A

A

D

D

P

P

R

R

L

I

V

V

P

P

D

N

A

A

R

Q

T

K

L

L

A

E

A

K

V

L

D

S

Y

F

D

E

T

E

M

M

I

L

T

E

M

L

S

A

R

A

H

V

G

G

A

S

K

K

V

I

L

L

H

V

H

L

S

R

A

S

V

V

A

E

W

Y

A

A

Q

R

R

A

H

F

G

N

V

V

E

P

I

L

R

R

C

V

R

R

S

S

Sites not aligning to the query:

binding lysine: 316, 319, 320, 322, 323, 343, 344
binding threonine: 239, 241, 242, 243, 262, 336, 337

O81852 Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic; AK-HD 2; AK-HSDH 2; Beta-aspartyl phosphate homoserine 2; EC 2.7.2.4; EC 1.1.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
25% identity, 54% coverage: 90:318/421 of query aligns to 211:464/916 of O81852

query
sites
O81852

G

G

E

E

T

L

V

W

N

S

V

A

A

Q

L

M

M

L

T

S

A

Y

A

V

L

V

R

R

D

K

A

T

G

G

L

L

A

E

A

C

V

K

A

W

L

M

T

D

A

T

A

R

D

D

T

V

G

L

F

I

V

V

G

N

A

P

G

T

E

S

P

S

H

N

C

Q

A

V

D

D

-

P

-

D

-

F

-

G

-

E

-

S

L

E

R

K

R

R

I

L

D

D

G

K

S

W

V

F

L

S

A

-

S

-

L

-

V

L

E

N

P

P

A

S

G

-

T

K

V

I

L

I

V

I

V

A

P

T

G

G

G

F

Q

I

A

A

V

S

D

T

G

P

D

Q

G

N

R

I

P

P

I

T

M

T

L

L

G

K

R

R

N

D

S

G

S

S

D

D

L

F

S

S

A

A

I

A

A

I

A

M

A

G

I

A

A

L

V

L

G

R

A

A

R

R

A

Q

C

V

E

T

I

I

F

W

S

T

D

D

S

V

P

D

G

G

I

V

C

Y

T

S

A

A

D

D

P

P

R

R

L

K

V

V

P

N

D

E

A

A

R

V

T

I

L

L

A

Q

A

T

V

L

D

S

Y

Y

D

Q

T

E

M

A

I

W

T

E

M

M

S

S

R

Y

H

F

G

G

A

A

K

N

V

V

L

L

H

H

H

P

S

R

A

T

V

I

A

I

W

P

A

V

Q

M

R

R

H

Y

G

N

V

I

E

P

I

I

R

V

C

I

R

R

S

N

L

I

L

F

P

N

-

L

-

S

-

A

-

P

-

G

-

T

-

I

-

C

-

Q

-

P

-

E

-

D

-

Y

D

D

G

L

A

K

V

L

Y

T

S

T

V

P

V

V

R

K

A

G

G

F

R

A

T

T

S

I

A

D

A

N

A

L

V

A

L

L

V

I

H

N

G

V

T

E

G

G

T

T

V

G

W

M

A

A

G

G

D

V

P

P

D

G

L

T

-

A

-

S

-

D

V

I

R

F

A

G

T

C

L

V

A

K

E

D

L

V

G

G

S

A

D

N

A

V

V

I

A

M

I
|
I

P

S

E
x
Q

A

A

A

S

-

S

-

E

-

H

-

S

-

V

-

C

-

F

A

A

V

V

P

P

E

E

V

-

A

-

V

-

T

K

E

E

V

V

A

N

A

A

V

V

P

S

E

E

I441 (= I299) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.
Q443 (≠ E301) mutation to A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine.

Sites not aligning to the query:

522 I→A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.
524 Q→A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine.

O60163 Probable aspartokinase; Aspartate kinase; EC 2.7.2.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 58% coverage: 63:308/421 of query aligns to 119:363/519 of O60163

query
sites
O60163

E

E

T

L

D

E

R

Q

L

Y

G

L

T

N

A

A

L

I

R

R

A

V

V

L

S

S

P

E

A

V

P

S

-

P

-

R

D

T

R

R

D

D

L

L

L

V

A

I

A

G

A

-

L

-

M

-

T

M

G

G

E

E

T

R

V

L

N

S

V

C

A

R

L

F

M

M

T

A

A

A

A

V

L

L

R

K

D

D

A

Q

G

G

L

I

A

-

V

-

A

-

L

-

T

-

A

-

D

D

T

S

G

E

F

F

V

I

G

D

A

M

G

S

E

-

P

-

H

H

C

I

A

I

D

D

-

E

-

Q

-

R

-

E

L

W

R

R

R

N

I

L

D

D

G

A

S

S

V

F

-

Y

-

A

-

Y

-

L

-

A

-

S

-

Q

L

L

A

A

S

S

L

K

V

V

E

T

P

A

A

V

G

G

T

N

-

K

V

V

L

P

V

V

P

T

G

G

G

F

Q

F

A

G

V

M

D

V

G

P

D

G

G

G

R

L

P

L

I

S

M

Q

L

I

G

G

R

R

N

G

S

Y

S

T

D

D

L

F

S

C

A

A

I

A

A

L

A

A

I

V

A

G

V

L

G

N

A

A

R

D

A

E

C

L

E

Q

I

I

F

W

S

K

D

E

S

V

P

D

G

G

I

I

C

F

T

T

A

A

D

D

P

P

R

R

L

K

V

V

P

P

D

T

A

A

R

R

T

L

L

L

A

P

A

L

V

I

D

T

Y

P

D

E

T

E

M

A

I

A

T

E

M

L

S

T

R

Y

H

Y

G

G

A

S

K

E

V

V

L

I

H

H

H

P

S

F

A

T

V

M

A

S

W

Q

A

V

Q

V

R

H

H

A

G

R

V

I

E

P

I

I

R

R

C

I

R

K

S

N

-

V

-

G

-

N

-

P

-

R

-

G

-

K

-

G

-

T

-

V

L

I

L

F

P

P

D

D

G

-

A

-

V

-

Y

-

S

T

V

I

V

S

R

R

A

H

G

G

R

-

T

-

S

-

A

-

A
x
S

A

A

V
x
T

L

P

V

P

H

H

G

P

T

P

G

K

T

I

V

M

W

-

A

-

G

-

D

-

P

P

D

D

L

D

V

I

R

S

A

A

T

S

L

L

A

A

E

N

L

K

G

G

S

A

D

T

A

A

V

V

A

T

I

I

P

K

E

D

A

T

A

I

A

M

V

V

P

I

E

N

V

I

S326 (≠ A267) modified: Phosphoserine
T328 (≠ V269) modified: Phosphothreonine

3tviE Crystal structure of clostridium acetobutylicum aspartate kinase (caak): an important allosteric enzyme for industrial amino acids production (see paper)
30% identity, 24% coverage: 150:248/421 of query aligns to 166:264/439 of 3tviE

query
sites
3tviE

V

V

V

I

P

P

G

G

-
x
F

-

Y

G

G

Q

S

A

S

V

F

D

N

G

G

D

D

G

V

R

K

P

T

I

-

M

-

L

F

G

S

R

R

N

G

S
x
G

S
|
S

D

D

L

V

S

T

A

G

I

S

A

I

A

S

I

A

A

G

V

V

G

N

A

A

R

D

A

L

C

Y

E

E

I

N

F

W

S

T

D

D

S

V

P

S

G

G

I

F

C

L

T

M

A

A

D

D

P

P

R

R

L

I

V

V

P

E

D

N

A

P

R

K

T

T

L

I

A

S

A

K

V

I

D

S

Y

Y

D

K

T

E

M

L

I

R

T

E

M

L

S

S

R

Y

H

M

G

G

A

A

K

T

V

V

L

L

H

H

H

E

S

E

A

A

V

I

A

F

W

P

A

V

Q

K

R

D

H

S

G

G

V

I

E

P

I

I

R

N

C

I

R

K

S

N

binding aspartic acid: F170 (vs. gap), G186 (≠ S170), S187 (= S171)

Sites not aligning to the query:

binding aspartic acid: 51, 116

2j0xA Crystal structure of e. Coli aspartokinase iii in complex with lysine and aspartate (t-state) (see paper)
36% identity, 20% coverage: 148:230/421 of query aligns to 176:258/447 of 2j0xA

query
sites
2j0xA

V

L

L

V

V

I

V

T

P

Q

G

G

G
x
F

Q

I

A

G

V

S

D

E

G

N

D

K

G

G

R

R

P

T

I

T

M

T

L

L

G

G

R

R

N
x
G

S
x
G

S
|
S

D
|
D

L

Y

S

T

A

A

I

A

A

L

A

A

I

E

A

A

V

L

G

H

A

A

R

S

A

R

C

V

E

D

I

I

F

W

S

T

D

D

S

V

P

P

G

G

I

I

C

Y

T

T

A

T

D

D

P

P

R

R

L

V

V

V

P

S

D

A

A

A

R

K

T

R

L

I

A

D

A

E

V

I

D

A

Y

F

D

A

T

E

M

A

I

A

T

E

M

M

S

A

R

T

H

F

G

G

A

A

K

K

V

V

L

L

H

H

binding aspartic acid: F182 (≠ G154), G197 (≠ N169), G198 (≠ S170), S199 (= S171), D200 (= D172)

Sites not aligning to the query:

binding lysine: 316, 319, 322, 323, 336, 337, 338, 343, 344

2j0wA Crystal structure of e. Coli aspartokinase iii in complex with aspartate and adp (r-state) (see paper)
36% identity, 20% coverage: 148:230/421 of query aligns to 176:258/447 of 2j0wA

query
sites
2j0wA

V

L

L

V

V

I

V

T

P

Q

G

G

G
x
F

Q

I

A

G

V

S

D

E

G

N

D

K

G

G

R

R

P

T

I

T

M

T

L

L

G

G

R
|
R

N
x
G

S

G

S
|
S

D

D

L

Y

S

T

A

A

I

A

A

L

A

A

I

E

A

A

V

L

G

H

A

A

R

S

A

R

C

V

E

D

I

I

F

W

S
x
T

D
|
D

S

V

P

P

G

G

I
|
I

C
x
Y

T

T

A

T

D
|
D

P

P

R
|
R

L

V

V

V

P

S

D

A

A

A

R

K

T

R

L

I

A

D

A

E

V

I

D

A

Y

F

D

A

T

E

M

A

I

A

T

E

M

M

S

A

R

T

H

F

G

G

A

A

K
|
K

V
|
V

L

L

H

H

binding adenosine-5'-diphosphate: T219 (≠ S191), D220 (= D192), I224 (= I196), Y225 (≠ C197), D228 (= D200), R230 (= R202), K255 (= K227), V256 (= V228)
binding aspartic acid: F182 (≠ G154), R196 (= R168), G197 (≠ N169), S199 (= S171)

Sites not aligning to the query:

binding aspartic acid: 37, 43, 117

P08660 Lysine-sensitive aspartokinase 3; Aspartate kinase III; AKIII; Lysine-sensitive aspartokinase III; EC 2.7.2.4 from Escherichia coli (strain K12) (see paper)
36% identity, 20% coverage: 148:230/421 of query aligns to 178:260/449 of P08660

query
sites
P08660

V

L

L

V

V

I

V

T

P

Q

G

G

G

F

Q

I

A

G

V

S

D

E

G

N

D

K

G

G

R

R

P

T

I

T

M

T

L

L

G

G

R
|
R

N

G

S

G

S

S

D
|
D

L

Y

S

T

A

A

I

A

A

L

A

A

I

E

A

A

V

L

G

H

A

A

R

S

A

R

C

V

E

D

I

I

F

W

S

T

D

D

S

V

P

P

G

G

I

I

C

Y

T

T

A

T

D

D

P

P

R

R

L

V

V

V

P

S

D

A

A

A

R

K

T

R

L

I

A

D

A

E

V

I

D

A

Y

F

D

A

T

E

M

A

I

A

T

E

M

M

S

A

R

T

H

F

G

G

A

A

K

K

V

V

L

L

H

H

R198 (= R168) mutation to K: Increases KM for aspartate about 200-fold.
D202 (= D172) mutation to E: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.

Sites not aligning to the query:

8 K→R: Reduces activity about 98%. Increases KM for aspartate about 40-fold, enzyme is less sensitive to lysine inhibition.
119 E→D: Increases KM for aspartate about 3000-fold.

2cdqA Crystal structure of arabidopsis thaliana aspartate kinase complexed with lysine and s- adenosylmethionine (see paper)
22% identity, 45% coverage: 80:270/421 of query aligns to 116:308/470 of 2cdqA

query
sites
2cdqA

R

R

D

D

L

Y

L

L

A

V

A

S

A

F

L

-

M

-

T

-

G

G

E
|
E

T

C

V

L

N

S

V

T

A

R

L

I

M

F

T

A

A

A

A

Y

L

L

R

N

D

T

A

I

G

G

L

V

A

K

A

A

V

R

A

Q

L

Y

T

D

A

A

A

F

D

E

T

I

G

G

F

F

V

I

G

T

A

T

G

D

E

D

P

F

H

T

C

N

A

G

D

D

L

I

-

L

-

E

-

A

-

T

-

Y

-

P

-

A

-

V

-

A

R

K

R

R

I

L

D

Y

G

D

S

D

V

W

L

M

A

H

S

D

L

P

V

A

E

V

P

P

A

I

G

V

T

T

V

G

L

F

V

L

V

G

P

K

G

G

G

W

Q

K

A

T

V

-

D

-

G

-

D

-

G

G

R

A

P

V

I

T

M

T

L

L

G

G

R

R

N

G

S

G

S

S

D

D

L

L

S

T

A

A

I

T

A

T

A

I

A

G

I

K

A

A

V

L

G

G

A

L

R

K

A

E

C

I

E

Q

I

V

F

W

S

K

D

D

S

V

P

D

G

G

I

V

C

L

T

T

A

C

D

D

P

P

R

T

L

I

V

Y

P

K

D

R

A

A

R

T

T

P

L

V

A

P

A

Y

V

L

D

T

Y

F

D

D

T

E

M

A

I

A

T

E

M

L

S

A

R

Y

H

F

G

G

A

A

K

Q

V

V

L

L

H

H

H

P

S

Q

A

S

V

M

A

R

W

P

A

A

Q

R

R

E

H

G

G

E

V

I

E

P

I

V

R

R

C

V

R

K

S

N

L

S

L

Y

P

N

D

P

G

K

A

A

V

P

Y

G

S

T

V

I

R

T

A

K

G

T

R

R

T

D

S

M

A

T

A

K

A

S

V

I

L

L

binding lysine: E124 (= E91)

Sites not aligning to the query:

binding lysine: 40, 41, 46, 327, 330, 333, 334, 347, 348, 349
binding s-adenosylmethionine: 345, 346, 347, 368, 369, 370, 372, 376

Query Sequence

>WP_083866752.1 NCBI__GCF_000058485.1:WP_083866752.1
MGPADVPVAGDVVVLKFGGAAFAAPGAHQGIARHVADRLRAGGSSASPGGARAIVVVSAV
AGETDRLGTALRAVSPAPDRDLLAAALMTGETVNVALMTAALRDAGLAAVALTAADTGFV
GAGEPHCADLRRIDGSVLASLVEPAGTVLVVPGGQAVDGDGRPIMLGRNSSDLSAIAAAI
AVGARACEIFSDSPGICTADPRLVPDARTLAAVDYDTMITMSRHGAKVLHHSAVAWAQRH
GVEIRCRSLLPDGAVYSVVRAGRTSAAAVLVHGTGTVWAGDPDLVRATLAELGSDAVAIP
EAAAVPEVAVTEVAAVPEVAAVPDVAVTDVAVTEVAVTEVAAAAATAGIAGTAAVGEPVG
GTVAHLVLADAARDLRPRGLRHRADLRLVTTLFPDGRLQHRLVPAAEAPTVARAQHDVVV
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