SitesBLAST

P24058 Argininosuccinate lyase; ASAL; Arginosuccinase; Delta crystallin II; Delta-2 crystallin; EC 4.3.2.1 from Anas platyrhynchos (Mallard) (Anas boschas) (see 4 papers)
43% identity, 98% coverage: 2:431/437 of query aligns to 9:438/468 of P24058

query
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P24058

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W11 (= W4) mutation to A: 98% decrease in catalytic efficiency.; mutation to F: 90% decrease in catalytic efficiency.; mutation to M: 99% decrease in catalytic efficiency.; mutation to R: 97% decrease in catalytic efficiency.; mutation to Y: 50% decrease in catalytic efficiency.
S29 (= S22) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
D33 (= D26) mutation to N: 99% decrease in catalytic efficiency.
D89 (= D82) mutation to N: Loss of activity.
N116 (= N109) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
D117 (= D110) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
T161 (= T153) binding in chain C; mutation to A: Loss of activity.; mutation to D: Loss of activity.; mutation to S: 30% decrease in catalytic efficiency.; mutation to V: Loss of activity.
H162 (= H154) mutation to E: Loss of activity.
R238 (= R230) mutation to Q: Loss of activity.
T281 (= T273) mutation to V: 80% decrease in catalytic efficiency.
S283 (= S275) mutation to A: Loss of activity.; mutation to C: Loss of activity.; mutation to D: Loss of activity.; mutation to H: Loss of activity.; mutation to T: Loss of activity.
N291 (= N283) binding in chain B; mutation to L: Loss of activity.
D293 (= D285) mutation to N: 99% decrease in catalytic efficiency.
E296 (= E288) mutation to D: Loss of activity.
Y323 (= Y315) binding in chain A
K325 (= K317) mutation to N: 99% decrease in catalytic efficiency.
Q328 (= Q320) binding in chain A
D330 (= D322) mutation to N: Loss of activity.
K331 (= K323) binding in chain A; mutation to Q: Loss of activity.

P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
41% identity, 98% coverage: 2:431/437 of query aligns to 7:436/464 of P04424

query
sites
P04424

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R12 (= R7) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
D31 (= D26) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
K51 (= K46) mutation to N: 2-fold reduction in activity.
K69 (≠ S64) modified: N6-acetyllysine
E73 (≠ D68) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
D87 (= D82) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
H89 (= H84) mutation to Q: 10-fold reduction in activity.
R94 (≠ V89) to C: in ARGINSA; severe; dbSNP:rs374304304
R95 (≠ N90) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
R113 (= R108) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
D120 (= D115) to E: in ARGINSA; severe
V178 (≠ S172) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
T181 (≠ N175) to S: in a breast cancer sample; somatic mutation
R182 (= R176) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
R186 (= R180) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
G200 (= G194) to V: in a breast cancer sample; somatic mutation
R236 (= R230) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
D237 (= D231) to N: in ARGINSA; severe; dbSNP:rs552951774
Q286 (= Q280) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
K288 (= K282) modified: N6-acetyllysine; mutation to R: Refractory to inhibition by TSA and NAM and by addition of extra amino acids. No effect on protein structure.
R297 (= R291) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
R306 (≠ D300) to W: in ARGINSA; severe; dbSNP:rs868834862
Q326 (= Q320) to L: in ARGINSA; severe
V335 (≠ S329) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
M360 (= M354) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
M382 (≠ V377) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
R385 (= R380) to L: in ARGINSA; severe
H388 (= H383) to Q: in ARGINSA; severe
A398 (≠ C393) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity

Sites not aligning to the query:

456 R → W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688

1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
42% identity, 96% coverage: 11:431/437 of query aligns to 1:421/450 of 1k7wD

query
sites
1k7wD

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L

L

G

E

F

F

S

A

K

S

P

I

V

S

D

L

N

N

F

S

L

M

D

D

G

A

V

I

S

S

D

E

R

R

D

D

Y

F

I

V

E

E

V

F

L

L

S

S

A

F

F

A

S

T

I

L

C

L

M

M

M

I

H

H

L

L

S

S

R

K

L

M

S

A

E

E

E

D

L

L

I

I

W

Y

S

S

T

T

K

S

E

E

F

F

S

G

F

F

I

L

Q

T

M

L

D

S

D

D

K

A

F

F

S

S

T

T

G

G

S
x
A

S
|
S

I

L

M

M

P

P

Q

Q

K
|
K

K

K

N

N

P

P

D

D

A

S

A

L

E
|
E

L

L

I

I

R

R

G

S

K

K

T

A

G

G

R

R

V

V

Y

F

G

G

D

R

L

L

I

A

A

S

M

I

L

L

T

M

I

V

M

L

K

K

G

G

I

L

P

P

L

S

A

T

Y
|
Y

N

N

K

K

D

D

M

L

Q
|
Q

E

E

D

D

K
|
K

E

E

Q

A

F

V

F

F

D

D

S

V

F

V

D

D

T

T

L

L

K

T

M

A

C

V

I

L

L

Q

V

V

M

A

D

T

G

G

M

V

I

I

A

S

T

T

M

L

T

Q

V

I

K

S

K

K

E

E

A

N

M

M

K

E

E

K

A

A

V

L

K

T

G

P

G

E

F

M

L

L

N

-

A

A

T

T

D

D

V

L

A

A

D

L

Y

Y

L

L

V

V

N

R

K

K

G

G

V

V

A

P

F

F

R

R

D

Q

A

A

H

H

K

T

I

A

S

S

G

G

E

K

L

A

V

V

I

H

Y

L

C

A

E

E

N

T

N

K

D

G

K

I

A

T

I

I

E

N

E

K

L

L

N

S

I

L

N

E

E

D

F

L

K

K

N

S

F

I

C

S

N

P

L

Q

F

F

D

S

E

S

D

D

V

V

Y

S

E

Q

F

V

I

F

N

N

Y

F

N

V

N

N

V

S

I

V

K

E

K

Q

active site: E71 (= E81), T144 (= T153), H145 (= H154), A266 (≠ S275), S267 (= S276), K272 (= K281), E279 (= E288)
binding argininosuccinate: R98 (= R108), N99 (= N109), V102 (= V112), T144 (= T153), H145 (= H154), Y306 (= Y315), Q311 (= Q320), K314 (= K323)

1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
42% identity, 95% coverage: 15:431/437 of query aligns to 3:419/447 of 1hy0A

query
sites
1hy0A

L

I

M

M

E

Q

E

M

F

L

N

S

A

T

S

S

L

I

S

S

F

T

D

E

K

Q

K

R

L

L

Y

S

E

E

E

V

D

D

I

I

E

Q

G

A

S

S

I

I

A

A

H

Y

V

A

K

K

M

A

L

L

N

E

K

K

C

A

K

G

I

I

I

L

N

T

N

K

E

T

E

E

C

L

E

E

E

K

I

I

L

L

S

S

G

G

L

L

K

E

S

K

L

I

Y

S

K

E

D

E

I

L

R

S

S

K

G

G

K

V

L

I

K

V

I

V

E

T

G

Q

D

S

Y

D

E
|
E

D

D

I

I

H

Q

S

T

F

A

V

N

E

E

V

R

N

R

L

L

I

K

D

E

R

L

I

I

G

G

A

D

V

I

G

A

K

G

K

K

L

L

H

H

T

T

A

G

R

R

S

S

R

R

N

N

D

E

Q

Q

V

V

A

V

V

T

D

D

M

L

K

K

M

L

Y

F

V

M

K

K

K

N

S

S

S

L

Y

S

I

I

I

S

E

T

C

H

I

L

N

L

K

Q

L

L

M

I

E

K

T

T

I

L

K

V

D

E

K

R

A

A

E

A

N

I

N

E

-

I

H

D

F

V

I

I

M

L

P

P

G

G

Y

Y

T
|
T

H
|
H

M

L

Q

Q

R

K

A

A

Q

Q

V

P

V

I

T

R

F

W

T

S

H

Q

H

F

M

L

A

S

Y

H

Y

A

S

V

M

A

F

L

N

T

R

R

D

D

K

S

K

E

R

R

I

L

D

G

N

E

A

V

I

K

S

K

N

R

L

I

N

N

E

V

S

L

P

P

L

L

G

G

C

S

C

G

A

A

L

L

A

A

G

G

T

N

T

P

Y

L

D

D

T

I

D

D

R

R

E

E

M

M

T

L

S

R

K

S

E

E

L

L

G

E

F

F

S

A

K

S

P

I

V

S

D

L

N

N

F

S

L

M

D

D

G

A

V

I

S

S

D

E

R

R

D

D

Y

F

I

V

E

E

V

F

L

L

S

S

A

V

F

A

S

T

I

L

C

L

M

L

M

I

H

H

L

L

S

S

R

K

L

M

S

A

E

E

E

D

L

L

I

I

W

Y

S

S

T

T

K

S

E

E

F

F

S

G

F

F

I

L

Q

T

M

L

D

S

D

D

K

A

F

F

S

S

T

T

G

G

S
|
S

I

L

M
|
M

P

P

Q

Q

K
|
K

K

K

N
|
N

P

P

D

D

A

S

A

L

E
|
E

L

L

I

I

R

R

G

S

K

K

T

S

G

G

R

R

V

V

Y

F

G

G

D

R

L

L

I

A

A

S

M

I

L

L

T

M

I

V

M

L

K

K

G

G

I

L

P

P

L

S

A

T

Y

Y

N

N

K

K

D

D

M

L

Q

Q

E

E

D

D

K

K

E

E

Q

A

F

V

F

I

D

D

S

V

F

V

D

D

T

T

L

L

K

T

M

A

C

V

I

L

L

Q

V

V

M

A

D

T

G

G

M

V

I

I

A

S

T

T

M

L

T

Q

V

I

K

S

K

K

E

E

A

N

M

M

K

E

E

K

A

A

V

L

K

T

G

P

G

E

F

M

L

L

N

-

A

A

T

T

D

D

V

L

A

A

D

L

Y

Y

L

L

V

V

N

R

K

K

G

G

V

M

A

P

F

F

R

R

D

Q

A

A

H

H

K

T

I

A

S

S

G

G

E

K

L

A

V

V

I

H

Y

L

C

A

E

E

N

T

N

K

D

G

K

I

A

A

I

I

E

N

L

L

N

T

I

L

N

E

E

D

F

L

K

K

N

S

F

I

C

S

N

P

L

L

F

F

D

S

E

S

D

D

V

V

Y

S

E

Q

F

V

I

F

N

N

Y

F

N

V

N

N

V

S

I

V

K

E

K

Q

active site: E69 (= E81), T142 (= T153), H143 (= H154), S264 (= S275), S265 (= S276), K270 (= K281), E277 (= E288)
binding sulfate ion: S264 (= S275), M267 (= M278), N272 (= N283)

P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
40% identity, 98% coverage: 2:431/437 of query aligns to 7:436/466 of P02521

query
sites
P02521

K

K

L

L

W

L

G

G

R

R

F

F

R

V

E

G

S

S

E

T

S

D

E

P

L

I

M

M

E

E

E

I

F

L

N

S

A

S

S

S

L

I

S

S

F

T

D

E

K

Q

K

R

L

L

Y

T

E

E

E

V

D

D

I

I

E

Q

G

A

S

S

I

M

A

A

H

Y

V

A

K

K

M

A

L

L

N

E

K

K

C

A

K

S

I

I

I

L

N

T

N

K

E

T

E

E

C

L

E

E

E

K

I

I

L

L

S

S

G

G

L

L

K

E

S

K

L

I

Y

S

K

E

D

E

I

S

R

S

S

K

G

G

K

V

L

L

K

V

I

M

E

T

G

Q

D

S

Y

D

E

E

D

D

I

I

H

Q

S

T

F

A

V

I

E

E

V

R

N

R

L

L

I

K

D

E

R

L

I

I

G

G

A

D

V

I

G

A

K

G

K

K

L

L

H

Q

T

T

A

G

R

R

S

S

R

R

N

N

D

E

Q

Q

V

V

A

V

V

T

D

D

M

L

K

K

M

L

Y

L

V

L

K

K

K

S

S

S

S

I

Y

S

I

V

I

I

I

S

E

T

C

H

I

L

N

L

K

Q

L

L

M

I

E

K

T

T

I

L

K

V

D

E

K

R

A

A

E

A

N

I

N

E

-

I

H

D

F

I

I

I

M

M

P

P

G

G

Y

Y

T

T

H

H

M

L

Q

Q

R

K

A

A

Q

L

V

P

V

I

T

R

F

W

T

S

H

Q

H

F

M

L

A

S

Y

H

Y

A

S

V

M

A

F

L

N

T

R

R

D

D

K

S

K

E

R

R

I

L

D

G

N

E

A

V

I

K

S

K

N

R

L

I

N

T

E

V

S

L

P

P

L

L

G

G

C

S

C

G

A

A

L

L

A

A

G

G

T

N

T

P

Y

L

D

E

T

I

D

D

R

R

E

E

M

L

T

L

S

R

K

S

E

E

L

L

G

D

F

M

S

T

K

S

P

I

V

T

D

L

N

N

F

S

L

I

D

D

G

A

V

I

S

S

D

E

R

R

D

D

Y

F

I

V

E

E

V

L

L

I

S

S

A

V

F

A

S

T

I

L

C

L

M

M

M

I

H

H

L

L

S

S

R

K

L

L

S

A

E

E

E

D

L

L

I

I

W

F

S

S

T

T

K

T

E

E

F

F

S

G

F

F

I

V

Q

T

M

L

D

S

D

D

K

A

F

Y

S

S

T

T

G

G

S

S

I

L

M

L

P

P

Q

Q

K

K

N

N

P

P

D

D

A

S

A

L

E

E

L

L

I

I

R

R

G

S

K

K

T

A

G

G

R

R

V

V

Y

F

G

G

D

R

L

L

I

A

A

A

M

I

L

L

T

M

I

V

M

L

K

K

G

G

I

I

P

P

L

S

A

T

Y

F

N

S

K

K

D

D

M

L

Q

Q

E

E

D

D

K

K

E

E

Q

A

F

V

F

L

D

D

S

V

F

V

D

D

T

T

L

L

K

T

M

A

C

V

I

L

L

Q

V

V

M

A

D

T

G

G

M

V

I

I

A

S

T

T

M

L

T

Q

V

V

K

N

K

K

E

E

A

N

M

M

K

E

E

K

A

A

V

L

K

T

G

P

G

E

F

L

L

L

N

S

A

-

T

T

D

D

V

L

A

A

D

L

Y

Y

L

L

V

V

N

R

K

K

G

G

V

M

A

P

F

I

R

R

D

Q

A

A

H

Q

K

T

I

A

S

S

G

G

E

K

L

A

V

V

I

H

Y

L

C

A

E

E

N

T

N

K

D

G

K

I

A

T

I

I

E

N

L

L

N

T

I

L

N

E

E

D

F

L

K

K

N

S

F

I

C

S

N

P

L

L

F

F

D

A

E

S

D

D

V

V

Y

S

E

Q

F

V

I

F

N

S

Y

V

N

V

N

N

V

S

I

V

K

E

K

Q

Sites not aligning to the query:

2 modified: Blocked amino end (Ala)

6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
37% identity, 96% coverage: 13:430/437 of query aligns to 2:421/454 of 6ienB

query
sites
6ienB

S

S

E

D

L

A

M

L

E

A

F

L

N

S

A

K

S

S

L

T

S

H

F

F

D

D

K

W

K

V

L

L

Y

A

E

P

E

Y

D

D

I

L

E

T

G

A

S

S

I

R

A

A

H

H

V

T

K

M

M

V

L

L

N

F

K

R

C

A

K

G

I

L

N

T

N

E

E

E

E

Q

C

R

E

D

E

G

I

L

L

L

S

A

G

G

L

L

K

D

S

S

L

L

Y

A

K

Q

D

D

I

V

R

A

S

D

G

G

K

S

L

F

K

G

I

P

E

L

G

V

D

T

Y

D

E

E

D

D

I

V

H

H

S

A

F

A

V

L

E

E

V

R

N

G

L

L

I

I

D

D

R

R

I

V

G

G

A

P

-

D

V

L

G

G

K

G

K

R

L

L

H

R

T

A

A

G

R

R

S
|
S

R
|
R

N
|
N

D

D

Q

Q

V

V

A

A

V

A

D

L

M

F

K

R

M

M

Y

W

-

L

-

R

-

D

-

A

V

V

K

R

S

V

S

A

Y

T

I

G

I

V

I

L

E

D

C

V

I

V

N

G

K

A

L

L

M

A

E

E

T

-

I

-

K

-

D

Q

K

A

A

A

E

A

N

H

N

P

H

S

F

A

I

I

M

M

P

P

G

G

Y

K

T
|
T

H
|
H

M

L

Q

Q

R

S

A

A

Q

Q

V

P

V

I

T

L

F

L

T

A

H

H

M

L

A

A

Y

H

Y

A

S

H

M

P

F

L

N

L

R

R

D

D

K

L

K

D

R

R

I

I

D

V

N

D

A

F

I

D

S

K

N

R

L

A

N

A

E

V

S

S

P

P

L

Y

G

G

C

S

C

G

A

A

L

L

A

A

G

G

T

S

Y

L

D

G

T

L

D

D

R

P

E

D

M

A

T

I

S

A

K

A

E

D

L

L

G

G

F

F

S

S

K

A

P

A

V

A

D

D

N

N

F

S

L

V

D

D

G

A

V

T

S

A

D

A

R

R

D

D

Y

F

I

A

E

E

V

A

L

A

S

F

A

V

F

F

S

A

I

M

C

I

M

A

M

V

H

D

L

L

S

S

R

R

L

L

S

A

E

E

E

D

L

I

I

I

I

V

W

W

S

S

T

S

K

T

E

E

F

F

S

G

F

Y

I

V

Q

T

M

L

D

H

D

D

K

S

F

W

S

S

T

T

G

G

S
|
S

I

I

M
|
M

P

P

Q

Q

K
|
K

K

K

N

N

P

P

D

D

A

I

A

A

E

E

L

L

I

A

R

R

G

G

K

K

T

S

G

G

R

R

V

L

Y

I

G

G

D

N

L

L

I

A

A

G

M

L

L

L

T

A

I

T

M

L

K

K

G

A

I

Q

P

P

L

L

A

A

Y
|
Y

N

N

K

R

D

D

M

L

Q
|
Q

E

E

D

D

K
|
K

E

E

Q

P

F

V

F

F

D

D

S

S

F

V

D

A

T

Q

L

L

K

E

M

L

C

L

I

L

L

P

V

A

M

M

D

A

G

G

M

L

I

V

A

A

T

S

M

L

T

T

V

F

K

N

K

V

E

Q

A

R

M

M

K

A

E

E

A

L

V

A

K

P

G

A

G

G

F

Y

L

T

N

L

A

A

T

T

D

D

V

L

A

A

D

E

Y

W

L

L

V

V

N

R

K

Q

G

G

V

V

A

P

F

F

R

R

D

S

A

A

H

H

K

E

I

A

S

A

G

G

E

A

L

A

V

V

I

R

Y

A

C

A

E

E

N

Q

N

R

D

G

K

V

A

G

I

L

E

Q

E

E

L

L

N

T

I

D

N

D

E

E

F

L

K

A

N

A

F

I

C

S

N

P

L

E

F

L

D

T

E

P

D

Q

V

V

Y

R

E

E

F

V

I

L

N

T

Y

I

N

E

N

G

V

S

I

V

K

S

binding argininosuccinate: S97 (= S107), R98 (= R108), N99 (= N109), T144 (= T153), H145 (= H154), S266 (= S275), S267 (= S276), M269 (= M278), K272 (= K281), Y306 (= Y315), Q311 (= Q320), K314 (= K323)

6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
39% identity, 85% coverage: 12:384/437 of query aligns to 1:375/418 of 6ienC

query
sites
6ienC

E

P

S

S

E

D

L

A

M

L

E

A

F

L

N

S

A

K

S

S

L

T

S

H

F

F

D

D

K

W

K

V

L

L

Y

A

E

P

E

Y

D

D

I

L

E

T

G

A

S

S

I

R

A

A

H

H

V

T

K

M

M

V

L

L

N

F

K

R

C

A

K

G

I

L

N

T

N

E

E

E

E

Q

C

R

E

D

E

G

I

L

L

L

S

A

G

G

L

L

K

D

S

S

L

L

Y

A

K

Q

D

D

I

V

R

A

S

D

G

G

K

S

L

F

K

G

I

P

E

L

G

V

D

T

Y

D

E

E

D

D

I

V

H

H

S

A

F

A

V

L

E

E

V

R

N

G

L

L

I

I

D

D

R

R

I

V

G

G

A

P

-

D

V

L

G

G

K

G

K

R

L

L

H

R

T

A

A

G

R

R

S
|
S

R
|
R

N
|
N

D

D

Q

Q

V
|
V

A

A

V

A

D

L

M

F

K

R

M

M

Y

W

-

L

-

R

-

D

-

A

V

V

K

R

S

V

S

A

Y

T

I

G

I

V

I

L

E

D

C

V

I

V

N

G

K

A

L

L

M

A

E

E

T

-

I

-

K

-

D

Q

K

A

A

A

E

A

N

H

N

P

H

S

F

A

I

I

M

M

P

P

G

G

Y

K

T
|
T

H
|
H

M

L

Q

Q

R

S

A

A

Q

Q

V

P

V

I

T

L

F

L

T

A

H

H

M

L

A

A

Y

H

Y

A

S

H

M

P

F

L

N

L

R

R

D

D

K

L

K

D

R

R

I

I

D

V

N

D

A

F

I

D

S

K

N

R

L

A

N

A

E

V

S

S

P

P

L

Y

G

G

C

S

C

G

A

A

L

L

A

A

G

G

T

S

Y

L

D

G

T

L

D

D

R

P

E

D

M

A

T

I

S

A

K

A

E

D

L

L

G

G

F

F

S

S

K

A

P

A

V

A

D

D

N

N

F

S

L

V

D

D

G

A

V

T

S

A

D

A

R

R

D

D

Y

F

I

A

E

E

V

A

L

A

S

F

A

V

F

F

S

A

I

M

C

I

M

A

M

V

H

D

L

L

S

S

R

R

L

L

S

A

E

E

E

D

L

I

I

I

I

V

W

W

S

S

T

S

K

T

E

E

F

F

S

G

F

Y

I

V

Q

T

M

L

D

H

D

D

K

S

F

W

S

S

T

T

G

G

S
|
S

I

I

M
|
M

P

P

Q

Q

K
|
K

K

K

N

N

P

P

D

D

A

I

A

A

E

E

L

L

I

A

R

R

G

G

K

K

T

S

G

G

R

R

V

L

Y

I

G

G

D

N

L

L

I

A

A

G

M

L

L

L

T

A

I

T

M

L

K

K

G

A

I

Q

P

P

L

L

A

A

Y
|
Y

N

N

K

R

D

D

M

L

Q
|
Q

E

E

D

D

K
|
K

E

E

Q

P

F

V

F

F

D

D

S

S

F

V

D

A

T

Q

L

L

K

E

M

L

C

L

I

L

L

P

V

A

M

M

D

A

G

G

M

L

I

V

A

A

T

S

M

L

T

T

V

F

K

N

K

V

E

Q

A

R

M

M

K

A

E

E

A

L

V

A

K

P

G

A

G

G

F

Y

L

T

N

L

A

A

T

T

D

D

V

L

A

A

D

E

Y

W

L

L

V

V

N

R

K

Q

G

G

V

V

A

P

F

F

R

R

D

S

A

A

H

H

K

R

binding arginine: R98 (= R108), N99 (= N109), V102 (= V112), Y306 (= Y315), Q311 (= Q320), K314 (= K323)
binding argininosuccinate: T144 (= T153), H145 (= H154), S266 (= S275), S267 (= S276), M269 (= M278), K272 (= K281)
binding fumaric acid: S97 (= S107), R98 (= R108), N99 (= N109)

6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
36% identity, 96% coverage: 13:430/437 of query aligns to 2:419/452 of 6ienA

query
sites
6ienA

S

S

E

D

L

A

M

L

E

A

F

L

N

S

A

K

S

S

L

T

S

H

F

F

D

D

K

W

K

V

L

L

Y

A

E

P

E

Y

D

D

I

L

E

T

G

A

S

S

I

R

A

A

H

H

V

T

K

M

M

V

L

L

N

F

K

R

C

A

K

G

I

L

N

T

N

E

E

E

E

Q

C

R

E

D

E

G

I

L

L

L

S

A

G

G

L

L

K

D

S

S

L

L

Y

A

K

Q

D

D

I

V

R

A

S

D

G

G

K

S

L

F

K

G

I

P

E

L

G

V

D

T

Y

D

E

E

D

D

I

V

H

H

S

A

F

A

V

L

E

E

V

R

N

G

L

L

I

I

D

D

R

R

I

V

G

G

A

P

-

D

V

L

G

G

K

G

K

R

L

L

H

R

T

A

A

G

R

R

S

S

R
|
R

N
|
N

D

D

Q

Q

V
|
V

A

A

V

A

D

L

M

F

K

R

M

M

Y

W

-

L

-

R

-

D

-

A

V

V

K

R

S

V

S

A

Y

T

I

G

I

V

I

L

E

D

C

V

I

V

N

G

K

A

L

L

M

A

E

E

T

-

I

-

K

-

D

Q

K

A

A

A

E

A

N

H

N

P

H

S

F

A

I

I

M

M

P

P

G

G

Y

K

T
|
T

H
|
H

M

L

Q

Q

R

S

A

A

Q

Q

V

P

V

I

T

L

F

L

T

A

H

H

M

L

A

A

Y

H

Y

A

S

H

M

P

F

L

N

L

R

R

D

D

K

L

K

D

R

R

I

I

D

V

N

D

A

F

I

D

S

K

N

R

L

A

N

A

E

V

S

S

P

P

L

Y

G

G

C

S

C

G

A

A

L

L

A

A

G

G

T

S

Y

L

D

G

T

L

D

D

R

P

E

D

M

A

T

I

S

A

K

A

E

D

L

L

G

G

F

F

S

S

K

A

P

A

V

A

D

D

N

N

F

S

L

V

D

D

G

A

V

T

S

A

D

A

R

R

D

D

Y

F

I

A

E

E

V

A

L

A

S

F

A

V

F

F

S

A

I

M

C

I

M

A

M

V

H

D

L

L

S

S

R

R

L

L

S

A

E

E

E

D

L

I

I

I

I

V

W

W

S

S

T

S

K

T

E

E

F

F

S

G

F

Y

I

V

Q

T

M

L

D

H

D

D

K

S

F

W

S

S

T

T

G

G

S
|
S

I

-

M

-

P

P

Q

Q

K
|
K

K

K

N
|
N

P

P

D

D

A

I

A

A

E

E

L

L

I

A

R

R

G

G

K

K

T

S

G

G

R

R

V

L

Y

I

G

G

D

N

L

L

I

A

A

G

M

L

L

L

T

A

I

T

M

L

K

K

G

A

I

Q

P

P

L

L

A

A

Y
|
Y

N

N

K

R

D

D

M

L

Q
|
Q

E

E

D

D

K
|
K

E

E

Q

P

F

V

F

F

D

D

S

S

F

V

D

A

T

Q

L

L

K

E

M

L

C

L

I

L

L

P

V

A

M

M

D

A

G

G

M

L

I

V

A

A

T

S

M

L

T

T

V

F

K

N

K

V

E

Q

A

R

M

M

K

A

E

E

A

L

V

A

K

P

G

A

G

G

F

Y

L

T

N

L

A

A

T

T

D

D

V

L

A

A

D

E

Y

W

L

L

V

V

N

R

K

Q

G

G

V

V

A

P

F

F

R

R

D

S

A

A

H

H

K

E

I

A

S

A

G

G

E

A

L

A

V

V

I

R

Y

A

C

A

E

E

N

Q

N

R

D

G

K

V

A

G

I

L

E

Q

E

E

L

L

N

T

I

D

N

D

E

E

F

L

K

A

N

A

F

I

C

S

N

P

L

E

F

L

D

T

E

P

D

Q

V

V

Y

R

E

E

F

V

I

L

N

T

Y

I

N

E

N

G

V

S

I

V

K

S

binding argininosuccinate: R98 (= R108), N99 (= N109), V102 (= V112), T144 (= T153), H145 (= H154), Y304 (= Y315), Q309 (= Q320), K312 (= K323)
binding fumaric acid: S266 (= S275), S267 (= S276), K270 (= K281), N272 (= N283)

6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
30% identity, 95% coverage: 21:434/437 of query aligns to 27:442/497 of 6g3hA

query
sites
6g3hA

A

A

S

A

L

L

S

T

F

L

D

T

K

S

K

A

L

V

Y

F

E

P

E

Y

D

D

I

S

E

Q

G

I

S

H

I

R

A

A

H

H

V

V

K

V

M

M

L

L

N

T

K

E

C

Q

K

G

I

I

I

L

N

T

N

V

E

E

C

S

E

A

E

T

I

I

L

L

S

S

G

G

L

L

K

A

S

Q

L

V

Y

D

K

E

D

L

I

A

R

A

S

T

-

D

G

G

K

S

L

L

K

R

I

T

E

Y

G

L

D

P

Y

Y

E

E

D

-

I

-

H

-

S

-

F

-

V

-

E

-

V

A

N

A

L

L

I

K

D

R

R

T

I

I

G

G

A

S

V

V

G

A

K

G

K

K

L

M

H

H

T

I

A

G

R

R

S

S

R

R

N

N

D

D

Q

L

V

A

A

N

V

A

D

G

M

K

K

R

M

M

Y

F

V

L

K

R

K

D

S

Q

S

L

Y

L

I

R

I

T

I

I

E

E

C

A

I

V

N

I

K

G

L

Y

M

R

E

E

T

A

I

V

K

V

D

H

K

K

A

A

E

A

N

D

N

H

-

L

H

D

F

T

I

V

M

M

P

V

G

V

Y

Y

T

T

H

Q

M

R

Q

K

R

E

A

A

Q

Q

V

P

V

I

T

T

F

L

T

G

H

H

H

Y

M

L

M

M

A

A

Y

I

Y

S

S

E

M

N

F

L

N

A

R

K

D

N

K

L

K

D

R

R

I

Y

D

R

N

E

A

L

I

Y

S

A

N

R

L

I

N

N

E

L

S

C

P

P

L

L

G

G

C

A

A

A

L

T

A

A

G

G

T

T

T

G

Y

W

D

P

T

L

D

N

R

R

E

D

M

R

T

T

S

S

K

A

E

L

L

L

G

G

F

F

S

D

K

G

P

L

V

V

D

V

N

N

F

S

L

I

D

E

G

G

V

V

S

A

D

G

R

W

D

D

Y

H

I

V

I

A

E

E

V

H

L

A

S

F

A

V

F

N

S

A

I

V

C

F

M

L

M

S

H

G

L

L

S

S

R

R

L

L

S

A

E

S

E

E

L

I

I

Q

I

L

W

W

S

S

T

T

K

D

E

E

F

Y

S

Q

F

V

I

A

Q

E

M

L

D

D

D

A

K

S

F

F

S

A

T

G

G

T

S
|
S

I

I

M
|
M

P

P

Q

Q

K
|
K

K

K

N
|
N

P

P

D
|
D

A

S

A

L

E

E

L
x
R

I

S

R

R

G

K

K

A

T

A

G

F

R

A

V

A

Y

M

G

G

D

P

L

L

I

V

A

G

M

I

L

L

T

T

I

S

M

L

K

N

G

A

I

I

P

E

L

Y

A

Q

Y

Y

N

S

K

A

D

A

M

R

Q

V

E

E

D

L

K

E

E

P

Q

R

F

-

D

-

S

S

F

I

D

D

T

A

L

L

K

I

M

A

C

A

I

T

L

H

V

A

M

M

D

T

G

G

M

V

I

V

A

R

T

T

M

L

T

H

V

P

K

N

K

K

E

E

A

R

M

M

K

R

E

Q

A

Y

V

A

K

A

G

E

G

N

F

Y

L

S

N

T

A

M

T

T

D

D

V

L

A

T

D

D

Y

M

L

L

V

V

N

R

K

R

-

V

G

G

V

I

A

D

F

Y

R

R

D

E

A

A

H

H

K

E

I

I

S

V

G

A

E

H

L

V

V

V

I

I

Y

T

C

A

-

I

E

E

N

K

N

G

D

I

K

K

A

A

-

N

-

K

-

I

-

G

-

L

-

D

-

L

I

V

E

Q

E

E

L

A

N

A

I

V

N

A

E

Q

F

T

K

G

N

A

F

G

C

I

N

N

L

V

F

S

D

A

E

D

D

D

V

I

Y

K

E

D

F

A

I

L

N

D

-

P

Y

W

N

Q

N

N

V

V

I

L

K

R

G

E

N

G

K

K

binding (2~{S})-2-[2-[[(2~{S})-1,4-bis(oxidanyl)-1,4-bis(oxidanylidene)butan-2-yl]amino]ethylamino]butanedioic acid: S276 (= S275), S277 (= S276), M279 (= M278), K282 (= K281), N284 (= N283), D286 (= D285), R290 (≠ L289)

Sites not aligning to the query:

binding (2~{S})-2-[2-[[(2~{S})-1,4-bis(oxidanyl)-1,4-bis(oxidanylidene)butan-2-yl]amino]ethylamino]butanedioic acid: 22

6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
30% identity, 95% coverage: 21:434/437 of query aligns to 27:442/497 of 6g3gA

query
sites
6g3gA

A

A

S

A

L

L

S

T

F

L

D

T

K

S

K

A

L

V

Y

F

E

P

E

Y

D

D

I

S

E

Q

G

I

S

H

I

R

A

A

H

H

V

V

K

V

M

M

L

L

N

T

K

E

C

Q

K

G

I

I

I

L

N

T

N

V

E

E

C

S

E

A

E

T

I

I

L

L

S

S

G

G

L

L

K

A

S

Q

L

V

Y

D

K

E

D

L

I

A

R

A

S

T

-

D

G

G

K

S

L

L

K

R

I

T

E

Y

G

L

D

P

Y

Y

E

E

D

-

I

-

H

-

S

-

F

-

V

-

E

-

V

A

N

A

L

L

I

K

D

R

R

T

I

I

G

G

A

S

V

V

G

A

K

G

K

K

L

M

H

H

T

I

A

G

R

R

S

S

R

R

N

N

D

D

Q

L

V

A

A

N

V

A

D

G

M

K

K

R

M

M

Y

F

V

L

K

R

K

D

S

Q

S

L

Y

L

I

R

I

T

I

I

E

E

C

A

I

V

N

I

K

G

L

Y

M

R

E

E

T

A

I

V

K

V

D

H

K

K

A

A

E

A

N

D

N

H

-

L

H

D

F

T

I

V

M

M

P

V

G

V

Y

Y

T

T

H

Q

M

R

Q

K

R

E

A

A

Q

Q

V

P

V

I

T

T

F

L

T

G

H

H

H

Y

M

L

M

M

A

A

Y

I

Y

S

S

E

M

N

F

L

N

A

R

K

D

N

K

L

K

D

R

R

I

Y

D

R

N

E

A

L

I

Y

S

A

N

R

L

I

N

N

E

L

S

C

P

P

L

L

G

G

C

A

A

A

L

T

A

A

G

G

T

T

T

G

Y

W

D

P

T

L

D

N

R

R

E

D

M

R

T

T

S

S

K

A

E

L

L

L

G

G

F

F

S

D

K

G

P

L

V

V

D

V

N

N

F

S

L

I

D

E

G

G

V

V

S

A

D

G

R

W

D

D

Y

H

I

V

I

A

E

E

V

H

L

A

S

F

A

V

F

N

S

A

I

V

C

F

M

L

M

S

H

G

L

L

S

S

R

R

L

L

S

A

E

S

E

E

L

I

I

Q

I

L

W

W

S

S

T

T

K

D

E

E

F

Y

S

Q

F

V

I

A

Q

E

M

L

D

D

D

A

K

S

F

F

S

A

T

G

G

T

S
|
S

I

I

M
|
M

P

P

Q

Q

K
|
K

K

K

N
|
N

P

P

D

D

A

S

A

L

E

E

L

R

I

S

R

R

G

K

K

A

T

A

G

F

R

A

V

A

Y

M

G

G

D

P

L

L

I

V

A

G

M

I

L

L

T

T

I

S

M

L

K

N

G

A

I

I

P

E

L

Y

A

Q

Y

Y

N

S

K

A

D

A

M

R

Q

V

E

E

D

L

K

E

E

P

Q

R

F

-

D

-

S

S

F

I

D

D

T

A

L

L

K

I

M

A

C

A

I

T

L

H

V

A

M

M

D

T

G

G

M

V

I

V

A

R

T

T

M

L

T

H

V

P

K

N

K

K

E

E

A

R

M

M

K

R

E

Q

A

Y

V

A

K

A

G

E

G

N

F

Y

L

S

N

T

A

M

T

T

D

D

V

L

A

T

D

D

Y

M

L

L

V

V

N

R

K

R

-

V

G

G

V

I

A

D

F

Y

R

R

D

E

A

A

H

H

K

E

I

I

S

V

G

A

E

H

L

V

V

V

I

I

Y

T

C

A

-

I

E

E

N

K

N

G

D

I

K

K

A

A

-

N

-

K

-

I

-

G

-

L

-

D

-

L

I

V

E

Q

E

E

L

A

N

A

I

V

N

A

E

Q

F

T

K

G

N

A

F

G

C

I

N

N

L

V

F

S

D

A

E

D

D

D

V

I

Y

K

E

D

F

A

I

L

N

D

-

P

Y

W

N

Q

N

N

V

V

I

L

K

R

G

E

N

G

K

K

binding succinic acid: S276 (= S275), S277 (= S276), M279 (= M278), K282 (= K281), N284 (= N283)

6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
30% identity, 95% coverage: 21:434/437 of query aligns to 27:442/497 of 6g3fA

query
sites
6g3fA

A

A

S

A

L

L

S

T

F

L

D

T

K

S

K

A

L

V

Y

F

E

P

E

Y

D

D

I

S

E

Q

G

I

S

H

I

R

A

A

H

H

V

V

K

V

M

M

L

L

N

T

K

E

C

Q

K

G

I

I

I

L

N

T

N

V

E

E

C

S

E

A

E

T

I

I

L

L

S

S

G

G

L

L

K

A

S

Q

L

V

Y

D

K

E

D

L

I

A

R

A

S

T

-

D

G

G

K

S

L

L

K

R

I

T

E

Y

G

L

D

P

Y

Y

E

E

D

-

I

-

H

-

S

-

F

-

V

-

E

-

V

A

N

A

L

L

I

K

D

R

R

T

I

I

G

G

A

S

V

V

G

A

K

G

K

K

L

M

H

H

T

I

A

G

R

R

S

S

R

R

N

N

D

D

Q

L

V

A

A

N

V

A

D

G

M

K

K

R

M

M

Y

F

V

L

K

R

K

D

S

Q

S

L

Y

L

I

R

I

T

I

I

E

E

C

A

I

V

N

I

K

G

L

Y

M

R

E

E

T

A

I

V

K

V

D

H

K

K

A

A

E

A

N

D

N

H

-

L

H

D

F

T

I

V

M

M

P

V

G

V

Y

Y

T

T

H

Q

M

R

Q

K

R

E

A

A

Q

Q

V

P

V

I

T

T

F

L

T

G

H

H

H

Y

M

L

M

M

A

A

Y

I

Y

S

S

E

M

N

F

L

N

A

R

K

D

N

K

L

K

D

R

R

I

Y

D

R

N

E

A

L

I

Y

S

A

N

R

L

I

N

N

E

L

S

C

P

P

L

L

G

G

C

A

A

A

L

T

A

A

G

G

T

T

T

G

Y

W

D

P

T

L

D

N

R

R

E

D

M

R

T

T

S

S

K

A

E

L

L

L

G

G

F

F

S

D

K

G

P

L

V

V

D

V

N

N

F

S

L

I

D

E

G

G

V

V

S

A

D

G

R

W

D

D

Y

H

I

V

I

A

E

E

V

H

L

A

S

F

A

V

F

N

S

A

I

V

C

F

M

L

M

S

H

G

L

L

S

S

R

R

L

L

S

A

E

S

E

E

L

I

I

Q

I

L

W

W

S

S

T

T

K

D

E

E

F

Y

S

Q

F

V

I

A

Q

E

M

L

D

D

D

A

K

S

F

F

S

A

T

G

G

T

S
|
S

I

I

M
|
M

P

P

Q

Q

K
|
K

K

K

N
|
N

P

P

D

D

A

S

A

L

E

E

L

R

I

S

R

R

G

K

K

A

T

A

G

F

R

A

V

A

Y

M

G

G

D

P

L

L

I

V

A

G

M

I

L

L

T

T

I

S

M

L

K

N

G

A

I

I

P

E

L

Y

A

Q

Y

Y

N

S

K

A

D

A

M

R

Q

V

E

E

D

L

K

E

E

P

Q

R

F

-

D

-

S

S

F

I

D

D

T

A

L

L

K

I

M

A

C

A

I

T

L

H

V

A

M

M

D

T

G

G

M

V

I

V

A

R

T

T

M

L

T

H

V

P

K

N

K

K

E

E

A

R

M

M

K

R

E

Q

A

Y

V

A

K

A

G

E

G

N

F

Y

L

S

N

T

A

M

T

T

D

D

V

L

A

T

D

D

Y

M

L

L

V

V

N

R

K

R

-

V

G

G

V

I

A

D

F

Y

R

R

D

E

A

A

H

H

K

E

I

I

S

V

G

A

E

H

L

V

V

V

I

I

Y

T

C

A

-

I

E

E

N

K

N

G

D

I

K

K

A

A

-

N

-

K

-

I

-

G

-

L

-

D

-

L

I

V

E

Q

E

E

L

A

N

A

I

V

N

A

E

Q

F

T

K

G

N

A

F

G

C

I

N

N

L

V

F

S

D

A

E

D

D

D

V

I

Y

K

E

D

F

A

I

L

N

D

-

P

Y

W

N

Q

N

N

V

V

I

L

K

R

G

E

N

G

K

K

binding fumaric acid: S276 (= S275), S277 (= S276), M279 (= M278), K282 (= K281), N284 (= N283)

6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
30% identity, 95% coverage: 21:434/437 of query aligns to 27:442/496 of 6g3iA

query
sites
6g3iA

A

A

S

A

L

L

S

T

F

L

D

T

K

S

K

A

L

V

Y

F

E

P

E

Y

D

D

I

S

E

Q

G

I

S

H

I

R

A

A

H

H

V

V

K

V

M

M

L

L

N

T

K

E

C

Q

K

G

I

I

I

L

N

T

N

V

E

E

C

S

E

A

E

T

I

I

L

L

S

S

G

G

L

L

K

A

S

Q

L

V

Y

D

K

E

D

L

I

A

R

A

S

T

-

D

G

G

K

S

L

L

K

R

I

T

E

Y

G

L

D

P

Y

Y

E

E

D

-

I

-

H

-

S

-

F

-

V

-

E

-

V

A

N

A

L

L

I

K

D

R

R

T

I

I

G

G

A

S

V

V

G

A

K

G

K

K

L

M

H

H

T

I

A

G

R

R

S

S

R

R

N

N

D

D

Q

L

V

A

A

N

V

A

D

G

M

K

K

R

M

M

Y

F

V

L

K

R

K

D

S

Q

S

L

Y

L

I

R

I

T

I

I

E

E

C

A

I

V

N

I

K

G

L

Y

M

R

E

E

T

A

I

V

K

V

D

H

K

K

A

A

E

A

N

D

N

H

-

L

H

D

F

T

I

V

M

M

P

V

G

V

Y

Y

T

T

H

Q

M

R

Q

K

R

E

A

A

Q

Q

V

P

V

I

T

T

F

L

T

G

H

H

H

Y

M

L

M

M

A

A

Y

I

Y

S

S

E

M

N

F

L

N

A

R

K

D

N

K

L

K

D

R

R

I

Y

D

R

N

E

A

L

I

Y

S

A

N

R

L

I

N

N

E

L

S

C

P

P

L

L

G

G

C

A

A

A

L

T

A

A

G

G

T

T

T

G

Y

W

D

P

T

L

D

N

R

R

E

D

M

R

T

T

S

S

K

A

E

L

L

L

G

G

F

F

S

D

K

G

P

L

V

V

D

V

N

N

F

S

L

I

D

E

G

G

V

V

S

A

D

G

R

W

D

D

Y

H

I

V

I

A

E

E

V

H

L

A

S

F

A

V

F

N

S

A

I

V

C

F

M

L

M

S

H

G

L

L

S

S

R

R

L

L

S

A

E

S

E

E

L

I

I

Q

I

L

W

W

S

S

T

T

K

D

E

E

F

Y

S

Q

F

V

I

A

Q

E

M

L

D

D

D

A

K

S

F

F

S

A

T

G

G

T

S
|
S

I

I

M
|
M

P

P

Q

Q

K
|
K

K

K

N
|
N

P

P

D
|
D

A

S

A

L

E

E

L
x
R

I

S

R

R

G

K

K

A

T

A

G

F

R

A

V

A

Y

M

G

G

D

P

L

L

I

V

A

G

M

I

L

L

T

T

I

S

M

L

K

N

G

A

I

I

P

E

L

Y

A

Q

Y

Y

N

S

K

A

D

A

M

R

Q

V

E

E

D

L

K

E

E

P

Q

R

F

-

D

-

S

S

F

I

D

D

T

A

L

L

K

I

M

A

C

A

I

T

L

H

V

A

M

M

D

T

G

G

M

V

I

V

A

R

T

T

M

L

T

H

V

P

K

N

K

K

E

E

A

R

M

M

K

R

E

Q

A

Y

V

A

K

A

G

E

G

N

F

Y

L

S

N

T

A

M

T

T

D

D

V

L

A

T

D

D

Y

M

L

L

V

V

N

R

K

R

-

V

G

G

V

I

A

D

F

Y

R

R

D

E

A

A

H

H

K

E

I

I

S

V

G

A

E

H

L

V

V

V

I

I

Y

T

C

A

-

I

E

E

N

K

N

G

D

I

K

K

A

A

-

N

-

K

-

I

-

G

-

L

-

D

-

L

I

V

E

Q

E

E

L

A

N

A

I

V

N

A

E

Q

F

T

K

G

N

A

F

G

C

I

N

N

L

V

F

S

D

A

E

D

D

D

V

I

Y

K

E

D

F

A

I

L

N

D

-

P

Y

W

N

Q

N

N

V

V

I

L

K

R

G

E

N

G

K

K

binding (2~{S})-2-(2-azanylethylamino)butanedioic acid: S276 (= S275), S277 (= S276), M279 (= M278), K282 (= K281), N284 (= N283), D286 (= D285)
binding fumaric acid: R290 (≠ L289)

Sites not aligning to the query:

binding fumaric acid: 22

Q9X0I0 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
23% identity, 73% coverage: 82:398/437 of query aligns to 69:387/431 of Q9X0I0

query
sites
Q9X0I0

D

D

I

V

H

V

S

A

F

F

V

V

E

E

V

-

N

G

L

I

I

G

D

S

R

M

I

I

G

G

A

E

V

D

G

S

K

R

K

F

L

F

H

H

T

Y

A

G

R

L

S

T

R

S

N

S

D

D

Q

V

V

L

A

D

V

T

D

A

M

N

K

S

M

L

Y

A

V

L

K

V

K

E

S

A

S

G

Y

K

I

I

I

L

E

E

C

S

I

L

N

K

K

E

L

F

M

C

E

D

T

V

I

L

K

W

D

E

K

V

A

A

E

N

N

R

-

Y

N

K

H

H

F

T

I

P

M

T

P

I

G

G

Y

R

T

T

H
|
H

M

G

Q

V

R

H

A

A

Q

E

V

P

V

T

T

S

F

F

T

G

H

L

H

K

M

V

M

L

A

G

Y

W

Y

Y

S

S

M

E

F

M

N

K

R

R

D

N

K

V

K

Q

R

R

I

L

D

E

N

R

A

A

I

I

S

E

N

E

L

V

N

S

E

Y

S

G

P

K

L

I

G

S

C

G

C

A

A

V

L

-

A

-

G

G

T

N

T

Y

Y

A

D

N

T

V

D

P

R

P

E

E

M

V

T

E

S

E

K

K

E

A

L

L

G

S

F

Y

-

L

-

G

-

L

-

K

S

P

K

E

P

P

V

V

D

S

N

T

F

-

L

-

D

-

G

Q

V

V

S

V

D

P

R

R

D

D

Y

R

I

H

I

A

E

F

V

Y

L

L

S

S

A

T

F

L

S

A

I

I

C

V

M

A

H

G

L

I

S

E

R

R

L

I

S

A

E

V

E

E

L

-

I

-

I

I

W

R

S

H

T

L

K

Q

E

R

F

T

S

E

F

V

I

L

Q

E

M

V

D

E

K

P

F

F

-

R

-

K

-

G

S

Q

T

R

G

G

S

S

I

A

M

M

P

P

Q

H

K

K

N

N

P

P

D

I

A

T

A

C

E

E

L

R

I

L

R

T

G

G

-

L

-

S

K

R

T

M

G

M

R

R

V

A

Y

Y

G

V

D

D

L

-

I

-

A

-

M

-

L

-

T

P

I

S

M

L

K

E

G

N

I

I

P

A

L

L

A

W

Y

H

N

E

K

R

D

D

M

I

Q

S

E

H

-

S

-

V

D

E

K

R

E

Y

Q

V

F

F

F

P

D

D

S

A

F

T

D

Q

T

T

L

L

K

Y

M

Y

C

M

I

I

L

V

V

T

M

A

D

T

G

N

M

V

I

V

A

R

T

N

M

M

T

K

V

V

K

N

K

E

E

E

A

R

M

M

K

K

E

K

A

N

V

I

-

D

-

L

K

T

G

K

G

G

F

L

L

V

N

F

A

S

T

Q

D

R

V

V

A

L

D

L

Y

K

L

L

V

I

N

E

K

K

G

G

V

L

A

T

F

R

R

K

D

E

A

A

H

Y

K

D

I

I

S

V

G

Q

E

R

L

N

V

A

I

L

Y

K

C

T

E

W

N

N

N

S

D

E

K

K

H141 (= H154) active site, Proton donor/acceptor

3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
28% identity, 40% coverage: 127:300/437 of query aligns to 149:339/462 of 3r6qA

query
sites
3r6qA

I

V

I

L

E

S

C

L

I

L

N

N

K

Q

L

L

M

I

E

E

T

T

-

T

-

K

-

Y

-

M

-

Q

-

E

-

F

I

M

K

K

D

K

K

A

A

D

E

E

N

F

N

A

H

G

F

V

I

I

M

K

P

M

G

G

Y

R

T

T

H
|
H

M

L

Q

Q

R

D

A

A

Q

V

V

P

V

I

T

L

F

L

T

G

H

Q

H

E

M

F

M

E

A

A

Y

Y

Y

A

S

R

M

V

F

I

N

A

R

R

D

D

K

I

K

E

R

R

I

I

D

A

N

N

A

T

I

R

S

N

N

N

L

L

N

Y

E

D

S

I

P

N

L

M

G

G

C

A

C

T

A

A

L

V

A

-

G

G

T

T

T

G

Y

L

D

N

T

A

D

D

R

P

E

E

-

Y

-

I

-

S

-

I

M

V

T

T

S

E

K

H

E

L

L

A

G

K

F

F

S

S

-

G

-

H

-

P

-

L

K

R

P

S

V

A

D

Q

N

H

F

L

L

V

D

D

G

A

V

T

S

Q

D

N

R

T

D

D

Y

C

I

Y

I

T

E

E

V

V

L

S

S

S

A

A

F

L

S

K

I

V

C

C

M

M

M

I

H

N

L

M

S

S

R

K

L

I

S

A

E

N

E

D

L

L

I

R

I

L

W

M

S

A

T

S

K

G

E

P

-

R

-

A

-

G

F

L

S

S

F

E

I

I

Q

V

M

L

D

P

D

A

K

R

F

-

S

Q

T

P

G

G

S
|
S

S

S

I

I

M

M

P

P

Q

G

K
|
K

K

V

N

N

P

P

D

V

A

M

A

P

E
|
E

L

V

I

M

R

N

G

Q

K

V

T

A

G

F

R

Q

V

V

Y

F

G

G

D

N

active site: H184 (= H154), S314 (= S275), K320 (= K281), E327 (= E288)

Sites not aligning to the query:

binding calcium ion: 389, 391

Q9LCC6 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Bacillus sp. (see 3 papers)
28% identity, 40% coverage: 127:300/437 of query aligns to 153:343/468 of Q9LCC6

query
sites
Q9LCC6

I

V

I

L

E

S

C

L

I

L

N

N

K

Q

L

L

M

I

E

E

T

T

-

T

-

K

-

Y

-

M

-

Q

-

E

-

F

I

M

K

K

D

K

K

A

A

D

E

E

N

F

N

A

H

G

F

V

I

I

M
x
K

P

M

G

G

Y

R

T
|
T

H
|
H

M

L

Q

Q

R

D

A

A

Q

V

V

P

V

I

T

L

F

L

T

G

H

Q

H

E

M

F

M

E

A

A

Y

Y

Y

A

S

R

M

V

F

I

N

A

R

R

D

D

K

I

K

E

R

R

I

I

D

A

N

N

A

T

I

R

S

N

N

N

L

L

N

Y

E

D

S

I

P

N

L

M

G

G

C

A

C

T

A

A

L

V

A

-

G

G

T

T

T

G

Y

L

D

N

T

A

D

D

R

P

E

E

-

Y

-

I

-

S

-

I

M

V

T

T

S

E

K

H

E

L

L

A

G

K

F

F

S

S

-

G

-

H

-

P

-

L

K

R

P

S

V

A

D

Q

N

H

F

L

L

V

D

D

G

A

V

T

S

Q

D

N

R

T

D

D

Y

C

I

Y

I

T

E

E

V

V

L

S

S

S

A

A

F

L

S

K

I

V

C

C

M

M

M

I

H

N

L

M

S

S

R

K

L

I

S

A

E

N

E

D

L

L

I

R

I

L

W

M

S

A

T

S

K

G

E

P

-

R

-

A

-

G

F

L

S

S

F

E

I

I

Q

V

M

L

D

P

D

A

K

R

F

-

S

Q

T

P

G

G

S
|
S

I
|
I

M
|
M

P
|
P

Q

G

K
|
K

K

V

N
|
N

P

P

D

V

A

M

A

P

E

E

L

V

I

M

R

N

G

Q

K

V

T

A

G

F

R

Q

V

V

Y

F

G

G

D

N

K183 (≠ M149) mutation to A: Loss of activity. Does not affect tertiary structure.
T187 (= T153) binding L-aspartate; mutation to A: 6280-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to S: 2.3-fold decrease in catalytic efficiency.
H188 (= H154) binding L-aspartate; mutation to A: 100-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation H->K,Q,R: Loss of activity.
S318 (= S275) mutation to A: Loss of activity.
S319 (= S276) binding L-aspartate; mutation to A: Almost no change in catalytic efficiency.
I320 (= I277) mutation to A: 50-fold decrease in catalytic efficiency.
M321 (= M278) mutation to A: 338-fold decrease in catalytic efficiency.
P322 (= P279) mutation to A: Almost no change in catalytic efficiency.
K324 (= K281) binding L-aspartate; mutation to A: Loss of activity. Does not result in any major conformational changes.; mutation K->D,H,R,S,V: Loss of activity.
N326 (= N283) mutation to A: 22500-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to Q: 168750-fold decrease in catalytic efficiency.

Sites not aligning to the query:

101 binding L-aspartate; T→A: 7100-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; T→S: 80-fold decrease in catalytic efficiency.
134 H→A: Retains full activity. Shows a slightly stronger affinity for L-aspartate. Does not affect tertiary structure.
140 binding L-aspartate; S→A: 27-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation S->K,R: Loss of activity.
141 binding L-aspartate; T→A: 15-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; T→K: 40000-fold decrease in catalytic efficiency.; mutation T->V,R: Loss of activity.
142 binding L-aspartate; N→A: Loss of activity. Does not result in any major conformational changes.; N→Q: 3000-fold decrease in catalytic efficiency.

3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
28% identity, 40% coverage: 127:300/437 of query aligns to 150:340/463 of 3r6vG

query
sites
3r6vG

I

V

I

L

E

S

C

L

I

L

N

N

K

Q

L

L

M

I

E

E

T

T

-

T

-

K

-

Y

-

M

-

Q

-

E

-

F

I

M

K

K

D

K

K

A

A

D

E

E

N

F

N

A

H

G

F

V

I

I

M

K

P

M

G

G

Y

R

T

T

H
|
H

M

L

Q

Q

R

D

A

A

Q

V

V

P

V

I

T

L

F

L

T

G

H

Q

H

E

M

F

M

E

A

A

Y

Y

Y

A

S

R

M

V

F

I

N

A

R

R

D

D

K

I

K

E

R

R

I

I

D

A

N

N

A

T

I

R

S

N

N

N

L

L

N

Y

E

D

S

I

P

N

L

M

G

G

C

A

C

T

A

A

L

V

A

-

G

G

T

T

T

G

Y

L

D

N

T

A

D

D

R

P

E

E

-

Y

-

I

-

S

-

I

M

V

T

T

S

E

K

H

E

L

L

A

G

K

F

F

S

S

-

G

-

H

-

P

-

L

K

R

P

S

V

A

D

Q

N

H

F

L

L

V

D

D

G

A

V

T

S

Q

D

N

R

T

D

D

Y

C

I

Y

I

T

E

E

V

V

L

S

S

S

A

A

F

L

S

K

I

V

C

C

M

M

M

I

H

N

L

M

S

S

R

K

L

I

S

A

E

N

E

D

L

L

I

R

I

L

W

M

S

A

T

S

K

G

E

P

-

R

-

A

-

G

F

L

S

S

F

E

I

I

Q

V

M

L

D

P

D

A

K

R

F

-

S

Q

T

P

G
|
G

S
|
S

I

I

M

M

P

P

Q

G

K
|
K

K

V

N

N

P

P

D

V

A

M

A

P

E
|
E

L

V

I

M

R

N

G

Q

K

V

T

A

G

F

R

Q

V

V

Y

F

G

G

D

N

active site: H185 (= H154), S315 (= S275), K321 (= K281), E328 (= E288)
binding aspartic acid: G314 (= G274), S315 (= S275), S316 (= S276)

P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
21% identity, 82% coverage: 74:430/437 of query aligns to 60:419/431 of P12047

query
sites
P12047

L

L

K

E

I

I

E

E

G

K

D

D

Y

T

E

R

-

H

D

D

I

V

H

V

S

A

F

F

V

T

E

R

V

A

N

-

L

V

I

S

D

E

R

S

I

L

G

G

A

E

V

E

G

R

K

K

K

W

L

V

H
|
H

T

Y

A

G

R

L

S

T

R

S

N

T

D

D

Q

V

V

V

A

D

V

T

D

A

M

L

K

S

M

Y

Y

L

V

L

K

K

K

Q

S

A

S

N

Y

D

I

I

I

L

E

K

C

D

I

L

N

E

K

R

L

F

M

V

E

D

T

I

I

I

K

K

D

E

K

K

A

A

-

K

E

E

N

H

N

K

H

Y

F

T

I

V

M

M

P

M

G

G

Y

R

T

T

H
|
H

M

G

Q

V

R

H

A

A

Q

E

V

P

V

T

T

T

F

F

T

G

H

L

H

K

M

L

M

A

A

L

Y

W

Y

H

S

E

M

E

F

M

N

K

R

R

D

N

K

L

K

E

R

R

I

F

D

K

N

Q

A

A

I

K

S

A

N

G

L

I

N

E

E

V

S

G

P

K

L

I

G

S

C

G

C

A

A

V

L

-

A

-

G

G

T

T

T

Y

Y

A

D

N

T

I

D

D

-

P

-

F

-

V

R

E

E

Q

M

Y

T

V

S

C

K

E

E

K

L

L

G

G

F

L

-

K

S

A

K

A

P

P

V

I

D

S

N

T

F

-

L

-

D

-

G
x
Q

V

T

S

L

D

Q

R

R

D

D

Y

R

I

H

I

A

E

D

V

Y

L

M

S

A

A

T

F

L

S

A

I

L

C

I

M

A

M

T

H

S

L

I

S

E

R

K

L

F

S

A

E

V

E

E

L

I

I

R

I

G

W

L

S

Q

T

K

K

S

E

E

F

T

S

R

F

E

I

V

Q

E

-

E

M

F

D

F

D

A

K

K

F

G

S

Q

T

K

G

G

S

S

I

A

M

M

P

P

Q

H

K

K

K

R

N
|
N

P

P

D

I

A

G

A

S

E

E

L

N

I

M

R

T

G

G

K

M

T

A

G

R

R

V

V

I

Y

R

G

G

D

-

L

-

I

-

A

Y

M

M

L

M

T

T

I

A

M

Y

K

E

G

N

I

V

P

P

L

L

A

W

Y

H

N

E

K
x
R

D

D

M

I

Q

S

E

H

D

S

K

S

E

A

Q

E

-

R

-

I

F

L

F

P

D

D

S

A

F

T

D

I

T

A

L

L

K

N

M

Y

C

M

I

L

L

N

V

R

M

F

D

S

G

N

M

I

I

V

A

K

T

N

M

L

T

T

V

V

K

F

K

P

E

E

A

N

M

M

K

K

E

R

A

N

V

M

K

D

G

R

-

T

-

L

G

G

F

L

L

I

N

Y

A

S

T

Q

D

R

V

V

A

L

D

L

Y

A

L

L

V

I

N

D

K

T

G

G

V

L

A

T

F

R

R

E

D

E

A

A

H

Y

K

D

I

T

S

V

G

Q

E

P

L

K

V

A

I

M

Y

E

C

A

E

W

N

E

N

K

D

Q

K

V

A

P

I

F

E

R

E

E

L

L

N

V

I

E

N

A

E

E

F

E

K

K

N

I

F

T

C

S

N

R

L

L

F

S

D

P

E

E

D

K

V

I

Y

A

E

D

F

C

I

F

N

D

Y

Y

N

N

N

Y

V

H

I

L

K

K

H89 (= H103) mutation to Q: Abolishes enzyme activity.
H141 (= H154) mutation to Q: Abolishes enzyme activity.
Q212 (≠ G226) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
N270 (= N283) mutation N->D,L: Abolishes enzyme activity.
R301 (≠ K317) mutation R->K,Q: Abolishes enzyme activity.

2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
22% identity, 69% coverage: 95:395/437 of query aligns to 80:384/427 of 2x75A

query
sites
2x75A

I

L

G

G

A

E

V

E

G

R

K

K

K

W

L

V

H

H

T

Y

A

G

R

L

S

T

R

S

N

T

D

D

Q

V

V

V

A

D

V

T

D

A

M

L

K

S

M

F

Y

V

V

I

K

K

K

Q

S

A

S

N

Y

D

I

I

I

E

E

K

C

D

I

L

N

E

K

R

L

F

M

I

E

D

T

V

I

L

K

A

D

E

K

K

A

A

E

K

N

N

N

Y

H

K

F

Y

-

T

I

L

M

M

P

M

G

G

Y

R

T
|
T

H
|
H

M

G

Q

V

R

H

A

A

Q

E

V

P

V

T

T

T

F

F

T

G

H

V

H

K

M

M

M

A

A

L

Y

W

Y

Y

S

T

M

E

F

M

N

Q

R

R

D

N

K

L

K

Q

R

R

I

F

D

K

N

Q

A

V

I

R

S

E

N

E

L

I

N

E

E

V

S

G

P

K

L

M

G

S

C

G

C

A

A

V

L

-

A

-

G

G

T

T

T

F

Y

A

D

N

T

I

D

P

R

P

E

E

M

I

T

E

S

S

-

Y

-

V

-

C

K

K

E

H

L

L

G

G

F

I

-

G

S

T

K

A

P

P

V

V

D

S

N

T

F

Q

L

T

D

L

G

Q

V

R

S

D

D

R

R

H

D

A

Y

Y

I

Y

I

I

E

A

V

T

L

L

S

A

A

L

F

I

S

A

I

T

C

S

M

L

M

E

H

K

L

F

S

A

R

V

L

E

S

I

E

R

E

N

L

L

I

Q

I

K

W

T

S

E

T

T

K

R

E

E

F

V

S

E

F

-

I

-

Q

E

M

A

D

F

D

A

K

K

F

G

S

Q

T

K

G

G

S
|
S

I

A

M

M

P

P

Q

H

K
|
K

K

R

N

N

P

P

D

I

A

G

A

S

E
|
E

L
x
N

I

I

R

T

G

G

K

I

T

S

G

R

R

V

V

I

Y

R

G

G

D

-

L

-

I

-

A

Y

M

I

L

T

T

T

I

A

M

Y

K

E

G

N

I

V

P

P

L

L

A

W

Y

H

N

E

K

R

D

D

M

I

Q

S

E

H

D

S

K

S

E

A

Q

E

-

R

-

I

-

M

F

L

F

P

D

D

S

V

F

T

D

I

T

A

L

L

K

D

M

Y

C

A

I

L

L

N

V

R

M

F

D

T

G

N

M

I

I

V

A

D

T

R

M

L

T

T

V

V

K

F

K

E

E

D

A

N

M

M

K

R

E

N

A

N

V

I

K

D

G

K

-

T

-

F

G

G

F

L

L

I

N

F

A

S

T

Q

D

R

V

V

A

L

D

L

Y

A

L

L

V

I

N

N

K

K

G

G

V

M

A

V

F

R

R

E

D

E

A

A

H

Y

-

D

K

K

I

V

S

Q

G

P

E

K

L

A

V

M

I

I

Y

S

C

W

E

E

N

T

active site: T139 (= T153), H140 (= H154), S261 (= S275), S262 (= S276), K267 (= K281), E274 (= E288)
binding adenosine monophosphate: N275 (≠ L289)

Sites not aligning to the query:

active site: 67
binding adenosine monophosphate: 3, 4

Query Sequence

>WP_010964292.1 NCBI__GCF_000008765.1:WP_010964292.1
MKLWGGRFRESESELMEEFNASLSFDKKLYEEDIEGSIAHVKMLNKCKIINNEECEEILS
GLKSLYKDIRSGKLKIEGDYEDIHSFVEVNLIDRIGAVGKKLHTARSRNDQVAVDMKMYV
KKSSYIIIECINKLMETIKDKAENNHFIMPGYTHMQRAQVVTFTHHMMAYYSMFNRDKKR
IDNAISNLNESPLGCCALAGTTYDTDREMTSKELGFSKPVDNFLDGVSDRDYIIEVLSAF
SICMMHLSRLSEELIIWSTKEFSFIQMDDKFSTGSSIMPQKKNPDAAELIRGKTGRVYGD
LIAMLTIMKGIPLAYNKDMQEDKEQFFDSFDTLKMCILVMDGMIATMTVKKEAMKEAVKG
GFLNATDVADYLVNKGVAFRDAHKISGELVIYCENNDKAIEELNINEFKNFCNLFDEDVY
EFINYNNVIKKGNKKIM

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