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)
45% identity, 99% coverage: 3:459/461 of query aligns to 8:463/468 of P24058

query
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P24058

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W11 (= W6) 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 (= S24) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
D33 (= D28) mutation to N: 99% decrease in catalytic efficiency.
D89 (= D84) mutation to N: Loss of activity.
N116 (= N111) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
D117 (= D112) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
T161 (= T156) 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 (= H157) mutation to E: Loss of activity.
R238 (= R233) mutation to Q: Loss of activity.
T281 (= T276) mutation to V: 80% decrease in catalytic efficiency.
S283 (= S278) 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 (= N286) binding in chain B; mutation to L: Loss of activity.
D293 (= D288) mutation to N: 99% decrease in catalytic efficiency.
E296 (= E291) mutation to D: Loss of activity.
Y323 (= Y318) binding in chain A
K325 (= K320) mutation to N: 99% decrease in catalytic efficiency.
Q328 (= Q323) binding in chain A
D330 (= D325) mutation to N: Loss of activity.
K331 (= K326) 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)
44% identity, 99% coverage: 2:458/461 of query aligns to 5:460/464 of P04424

query
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P04424

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R12 (= R9) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
D31 (= D28) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
K51 (= K48) mutation to N: 2-fold reduction in activity.
K69 (≠ Q66) modified: N6-acetyllysine
E73 (= E70) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
D87 (= D84) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
H89 (= H86) mutation to Q: 10-fold reduction in activity.
R94 (≠ K91) to C: in ARGINSA; severe; dbSNP:rs374304304
R95 (= R92) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
R113 (= R110) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
D120 (= D117) to E: in ARGINSA; severe
V178 (≠ Q175) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
T181 (≠ K178) to S: in a breast cancer sample; somatic mutation
R182 (= R179) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
R186 (= R183) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
G200 (= G197) to V: in a breast cancer sample; somatic mutation
R236 (= R233) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
D237 (= D234) to N: in ARGINSA; severe; dbSNP:rs552951774
Q286 (= Q283) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
K288 (= K285) 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 (= R294) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
R306 (≠ S303) to W: in ARGINSA; severe; dbSNP:rs868834862
Q326 (= Q323) to L: in ARGINSA; severe
V335 (≠ A332) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
M360 (= M357) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
M382 (≠ V380) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
R385 (= R383) to L: in ARGINSA; severe
H388 (= H386) to Q: in ARGINSA; severe
A398 (= A396) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
R456 (≠ K454) to 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)
44% identity, 97% coverage: 14:459/461 of query aligns to 2:446/450 of 1k7wD

query
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1k7wD

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F

W

A

S

H

Q

W

F

A

L

M

L

A

S

Y

H

F

A

Q

V

M

A

I

L

K

T

R

R

D

D

F

S

S

E

R

R

F

L

A

G

D

E

C

V

L

K

E

K

R

R

M

I

D

N

F

V

C

L

P

P

L

L

G

G

A

S

G

G

A

A

L

L

A

A

G

G

T

N

T

P

F

L

N

D

I

I

D

D

R

R

H

E

F

M

T

L

A

R

A

S

E

E

L

L

G

E

F

F

K

A

A

S

P

I

T

S

E

L

N

N

S

S

L

M

D

D

S

A

V

I

S

S

D

E

R

R

D

D

F

F

A

V

L

V

E

E

F

F

L

L

A

S

A

F

C

A

S

T

I

L

C

L

Q

M

M

I

H

H

L

L

S

S

R

K

F

M

S

A

E

E

E

D

L

L

I

I

Y

Y

S

S

A

T

S

S

E

E

F

F

S

G

F

F

I

L

E

T

L

L

S

S

D

D

D

A

F

F

C

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

M

S

P

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

S

R

L

L

I

A

S

S

L

I

L

L

T

M

T

V

M

L

K

K

G

G

L

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

P

A

V

V

F

F

D

D

A

V

V

V

D

D

T

T

I

L

K

T

A

A

S

V

L

L

K

Q

I

V

F

A

S

T

P

G

M

V

V

I

E

S

K

T

M

L

T

Q

L

I

R

S

K

K

D

E

K

N

M

M

E

E

K

K

S

-

A

A

G

L

N

T

G

P

Y

E

S

M

T

L

A

A

T

T

D

D

L

L

A

A

D

L

Y

Y

L

L

V

V

R

R

K

K

G

G

V

V

P

P

F

F

R

R

Q

Q

S

A

H

H

H

T

I

A

V

S

G

G

S

K

A

A

V

V

A

H

Y

L

A

A

I

E

E

T

K

K

G

G

V

I

D

T

L

I

S

N

E

K

L

L

S

S

M

L

D

E

E

D

F

L

A

K

R

S

F

I

T

S

D

P

V

Q

I

F

T

S

D

S

D

D

I

V

Y

S

Q

Q

Y

V

I

F

T

N

V

F

R

V

A

N

S

S

V

V

N

E

S

Q

R

Y

V

T

A

A

Y

L

G

G

T

T

A

A

E

K

S

S

V

V

K

T

E

T

Q

Q

I

I

K

E

S

Q

A

L

K

R

K

E

F

L

L

M

N

K

E

K

active site: E71 (= E83), T144 (= T156), H145 (= H157), A266 (≠ S278), S267 (= S279), K272 (= K284), E279 (= E291)
binding argininosuccinate: R98 (= R110), N99 (= N111), V102 (= V114), T144 (= T156), H145 (= H157), Y306 (= Y318), Q311 (= Q323), K314 (= K326)

1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
42% identity, 97% coverage: 15:459/461 of query aligns to 1:444/447 of 1hy0A

query
sites
1hy0A

D

D

K

P

F

I

V

M

E

Q

E

M

F

L

N

S

A

T

S

S

V

I

H

S

F

T

D

E

N

Q

R

R

F

L

Y

S

K

E

Y

V

D

D

I

I

K

Q

G

A

S

S

I

I

A

A

H

Y

A

A

K

K

M

A

L

L

A

E

K

K

Q

A

E

G

I

I

I

L

S

T

T

K

E

T

D

E

R

L

D

E

S

K

I

I

I

L

K

S

G

G

L

L

N

E

Q

K

V

I

L

S

Q

E

E

E

I

L

E

S

T

K

G

G

K

V

L

I

E

V

W

V

K

T

T

Q

E

S

D

D

E
|
E

D

D

I

I

H

Q

M

T

A

A

V

N

E

E

K

R

R

R

L

L

T

K

E

E

L

L

V

I

G

G

D

D

A

I

G

A

K

G

R

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

F

L

R

K

M

L

Y

F

L

M

K

K

A

N

E

S

I

L

I

S

E

I

I

I

Q

S

A

T

L

H

I

L

A

L

E

Q

L

L

L

I

N

K

T

T

L

L

M

V

K

E

K

R

A

A

E

A

A

I

E

E

H

I

E

D

V

V

M

I

M

L

P

P

G

G

F

Y

T
|
T

H
|
H

L

L

Q

Q

T

K

A

A

Q

Q

P

P

I

I

L

R

F

W

A

S

H

Q

W

F

A

L

M

L

A

S

Y

H

F

A

Q

V

M

A

I

L

K

T

R

R

D

D

F

S

S

E

R

R

F

L

A

G

D

E

C

V

L

K

E

K

R

R

M

I

D

N

F

V

C

L

P

P

L

L

G

G

A

S

G

G

A

A

L

L

A

A

G

G

T

N

T

P

F

L

N

D

I

I

D

D

R

R

H

E

F

M

T

L

A

R

A

S

E

E

L

L

G

E

F

F

K

A

A

S

P

I

T

S

E

L

N

N

S

S

L

M

D

D

S

A

V

I

S

S

D

E

R

R

D

D

F

F

A

V

L

V

E

E

F

F

L

L

A

S

A

V

C

A

S

T

I

L

C

L

Q

L

M

I

H

H

L

L

S

S

R

K

F

M

S

A

E

E

E

D

L

L

I

I

Y

Y

S

S

A

T

S

S

E

E

F

F

S

G

F

F

I

L

E

T

L

L

S

S

D

D

D

A

F

F

C

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

M

S

P

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

S

R

L

L

I

A

S

S

L

I

L

L

T

M

T

V

M

L

K

K

G

G

L

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

P

A

V

V

F

I

D

D

A

V

V

V

D

D

T

T

I

L

K

T

A

A

S

V

L

L

K

Q

I

V

F

A

S

T

P

G

M

V

V

I

E

S

K

T

M

L

T

Q

L

I

R

S

K

K

D

E

K

N

M

M

E

E

K

K

S

-

A

A

G

L

N

T

G

P

Y

E

S

M

T

L

A

A

T

T

D

D

L

L

A

A

D

L

Y

Y

L

L

V

V

R

R

K

K

G

G

V

M

P

P

F

F

R

R

Q

Q

S

A

H

H

H

T

I

A

V

S

G

G

S

K

A

A

V

V

A

H

Y

L

A

A

I

E

E

T

K

K

G

G

V

I

D

A

L

I

S

N

E

N

L

L

S

T

M

L

D

E

E

D

F

L

A

K

R

S

F

I

T

S

D

P

V

L

I

F

T

S

D

S

D

D

I

V

Y

S

Q

Q

Y

V

I

F

T

N

V

F

R

V

A

N

S

S

V

V

N

E

S

Q

R

Y

V

T

A

A

Y

L

G

G

T

T

A

A

E

K

S

S

V

V

K

T

E

T

Q

Q

I

I

K

E

S

Q

A

L

K

R

K

E

F

L

L

M

N

K

E

K

active site: E69 (= E83), T142 (= T156), H143 (= H157), S264 (= S278), S265 (= S279), K270 (= K284), E277 (= E291)
binding sulfate ion: S264 (= S278), M267 (= M281), N272 (= N286)

P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
40% identity, 99% coverage: 3:459/461 of query aligns to 6:461/466 of P02521

query
sites
P02521

E

D

K

K

M

L

W

L

G

G

R

R

F

F

S

V

L

G

P

S

T

T

D

D

K

P

F

I

V

M

E

E

E

I

F

L

N

S

A

S

S

S

V

I

H

S

F

T

D

E

N

Q

R

R

F

L

Y

T

K

E

Y

V

D

D

I

I

K

Q

G

A

S

S

I

M

A

A

H

Y

A

A

K

K

M

A

L

L

A

E

K

K

Q

A

E

S

I

I

I

L

S

T

T

K

E

T

D

E

R

L

D

E

S

K

I

I

I

L

K

S

G

G

L

L

N

E

Q

K

V

I

L

S

Q

E

E

E

I

S

E

S

T

K

G

G

K

V

L

L

E

V

W

M

K

T

T

Q

E

S

D

D

E

E

D

D

I

I

H

Q

M

T

A

A

V

I

E

E

K

R

R

R

L

L

T

K

E

E

L

L

V

I

G

G

D

D

A

I

G

A

K

G

R

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

F

L

R

K

M

L

Y

L

L

L

K

K

A

S

E

S

I

I

I

S

E

V

I

I

Q

S

A

T

L

H

I

L

A

L

E

Q

L

L

L

I

N

K

T

T

L

L

M

V

K

E

K

R

A

A

E

A

A

I

E

E

H

I

E

D

V

I

M

I

M

M

P

P

G

G

F

Y

T

T

H

H

L

L

Q

Q

T

K

A

A

Q

L

P

P

I

I

L

R

F

W

A

S

H

Q

W

F

A

L

M

L

A

S

Y

H

F

A

Q

V

M

A

I

L

K

T

R

R

D

D

F

S

S

E

R

R

F

L

A

G

D

E

C

V

L

K

E

K

R

R

M

I

D

T

F

V

C

L

P

P

L

L

G

G

A

S

G

G

A

A

L

L

A

A

G

G

T

N

T

P

F

L

N

E

I

I

D

D

R

R

H

E

F

L

T

L

A

R

A

S

E

E

L

L

G

D

F

M

K

T

A

S

P

I

T

T

E

L

N

N

S

S

L

I

D

D

S

A

V

I

S

S

D

E

R

R

D

D

F

F

A

V

L

V

E

E

F

L

L

I

A

S

A

V

C

A

S

T

I

L

C

L

Q

M

M

I

H

H

L

L

S

S

R

K

F

L

S

A

E

E

E

D

L

L

I

I

Y

F

S

S

A

T

S

T

E

E

F

F

S

G

F

F

I

V

E

T

L

L

S

S

D

D

D

A

F

Y

C

S

T

T

G

G

S

S

I

L

M

L

P

P

Q

Q

K

K

N

N

P

P

D

D

M

S

P

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

S

R

L

L

I

A

S

A

L

I

L

L

T

M

T

V

M

L

K

K

G

G

L

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

P

A

V

V

F

L

D

D

A

V

V

V

D

D

T

T

I

L

K

T

A

A

S

V

L

L

K

Q

I

V

F

A

S

T

P

G

M

V

V

I

E

S

K

T

M

L

T

Q

L

V

R

N

K

K

D

E

K

N

M

M

E

E

K

K

S

-

A

A

G

L

N

T

G

P

Y

E

S

L

T

L

A

S

T

T

D

D

L

L

A

A

D

L

Y

Y

L

L

V

V

R

R

K

K

G

G

V

M

P

P

F

I

R

R

Q

Q

S

A

H

Q

H

T

I

A

V

S

G

G

S

K

A

A

V

V

A

H

Y

L

A

A

I

E

E

T

K

K

G

G

V

I

D

T

L

I

S

N

E

N

L

L

S

T

M

L

D

E

E

D

F

L

A

K

R

S

F

I

T

S

D

P

V

L

I

F

T

A

D

S

D

D

I

V

Y

S

Q

Q

Y

V

I

F

T

S

V

V

R

V

A

N

S

S

V

V

N

E

S

Q

R

Y

V

T

A

A

Y

V

G

G

T

T

A

A

E

K

S

S

V

V

K

T

E

A

Q

Q

I

I

K

E

S

Q

A

L

K

R

K

E

F

L

L

L

N

K

E

K

Sites not aligning to the query:

2 modified: Blocked amino end (Ala)

6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
42% identity, 95% coverage: 13:452/461 of query aligns to 1:440/454 of 6ienB

query
sites
6ienB

P

P

T

S

D

D

K

A

F

L

V

A

E

A

E

-

F

L

N

S

A

K

S

S

V

T

H

H

F

F

D

D

N

W

R

V

F

L

Y

A

K

P

Y

Y

D

D

I

L

K

T

G

A

S

S

I

R

A

A

H

H

A

T

K

M

M

V

L

L

A

F

K

R

Q

A

E

G

I

L

S

T

T

E

E

E

D

Q

R

R

D

D

S

G

I

L

K

A

G

G

L

L

N

D

Q

S

V

L

L

A

Q

Q

E

D

I

V

E

A

T

D

G

G

K

S

L

F

E

G

W

P

K

L

T

V

E

T

D

D

E

E

D

D

I

V

H

H

M

A

A

A

V

L

E

E

K

R

R

G

L

L

T

I

E

D

L

R

V

V

G

G

-

P

D

D

A

L

G

G

K

G

R

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

F

F

R

R

M

M

Y

W

L

L

K

R

A

D

E

A

I

V

I

R

E

R

I

V

Q

A

A

T

L

G

I

V

A

L

E

D

L

V

N

G

T

A

L

L

M

A

K

E

K

Q

A

A

E

A

A

A

E

H

H

P

E

S

V

A

M

I

M

M

P

P

G

G

F

K

T
|
T

H
|
H

L

L

Q

Q

T

S

A

A

Q

Q

P

P

I

I

L

L

F

L

A

A

H

H

W

H

A

L

M

L

A

A

Y

H

F

A

Q

H

M

P

I

L

K

L

R

R

D

D

F

L

S

D

R

R

F

I

A

V

D

D

C

F

L

D

E

K

R

R

M

A

D

A

F

V

C

S

P

P

L

Y

G

G

A

S

G

G

A

A

L

L

A

A

G

G

T

S

F

L

N

G

I

L

D

D

R

P

H

D

F

A

T

I

A

A

E

D

L

L

G

G

F

F

K

S

A

A

P

A

T

A

E

D

N

N

S

S

L

V

D

D

S

A

V

T

S

A

D

A

R

R

D

D

F

F

A

A

L

A

E

E

F

A

L

A

A

F

A

V

C

F

S

A

I

M

C

I

Q

A

M

V

H

D

L

L

S

S

R

R

F

L

S

A

E

E

E

D

L

I

I

I

I

V

Y

W

S

S

A

S

S

T

E

E

F

F

S

G

F

Y

I

V

E

T

L

L

S

H

D

D

D

S

F

W

C

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

M

I

P

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

S

N

L

L

I

A

S

G

L

L

T

A

T

T

M

L

K

K

G

A

L

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

P

P

V

V

F

F

D

D

A

S

V

V

D

A

T

Q

I

L

K

E

A

L

S

L

L

L

K

P

I

A

F

M

S

A

P

G

M

L

V

V

E

A

K

S

M

L

T

T

L

F

R

N

K

V

D

Q

K

R

M

M

E

A

K

E

S

L

A

A

G

P

N

A

G

G

Y

Y

S

T

T

L

A

A

T

T

D

D

L

L

A

A

D

E

Y

W

L

L

V

V

R

R

K

Q

G

G

V

V

P

P

F

F

R

R

Q

S

S

A

H

H

H

E

I

A

V

A

G

G

S

A

A

A

V

V

A

R

Y

A

A

A

I

E

E

Q

K

R

G

G

V

V

D

G

L

L

S

Q

E

E

L

L

S

T

M

D

D

D

E

E

F

L

A

A

R

A

F

I

T

S

D

P

V

E

I

L

T

T

D

P

D

Q

I

V

Y

R

Q

E

Y

V

I

L

T

T

V

I

R

E

A

G

S

S

V

V

N

S

S

A

R

R

V

D

A

C

Y

R

G

G

T

T

A

A

E

P

S

G

S

R

V

V

K

A

E

E

Q

Q

I

L

K

N

S

A

binding argininosuccinate: S97 (= S109), R98 (= R110), N99 (= N111), T144 (= T156), H145 (= H157), S266 (= S278), S267 (= S279), M269 (= M281), K272 (= K284), Y306 (= Y318), Q311 (= Q323), K314 (= K326)

6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
42% identity, 95% coverage: 13:452/461 of query aligns to 1:438/452 of 6ienA

query
sites
6ienA

P

P

T

S

D

D

K

A

F

L

V

A

E

A

E

-

F

L

N

S

A

K

S

S

V

T

H

H

F

F

D

D

N

W

R

V

F

L

Y

A

K

P

Y

Y

D

D

I

L

K

T

G

A

S

S

I

R

A

A

H

H

A

T

K

M

M

V

L

L

A

F

K

R

Q

A

E

G

I

L

S

T

T

E

E

E

D

Q

R

R

D

D

S

G

I

L

K

A

G

G

L

L

N

D

Q

S

V

L

L

A

Q

Q

E

D

I

V

E

A

T

D

G

G

K

S

L

F

E

G

W

P

K

L

T

V

E

T

D

D

E

E

D

D

I

V

H

H

M

A

A

A

V

L

E

E

K

R

R

G

L

L

T

I

E

D

L

R

V

V

G

G

-

P

D

D

A

L

G

G

K

G

R

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

F

F

R

R

M

M

Y

W

L

L

K

R

A

D

E

A

I

V

I

R

E

R

I

V

Q

A

A

T

L

G

I

V

A

L

E

D

L

V

N

G

T

A

L

L

M

A

K

E

K

Q

A

A

E

A

A

A

E

H

H

P

E

S

V

A

M

I

M

M

P

P

G

G

F

K

T
|
T

H
|
H

L

L

Q

Q

T

S

A

A

Q

Q

P

P

I

I

L

L

F

L

A

A

H

H

W

H

A

L

M

L

A

A

Y

H

F

A

Q

H

M

P

I

L

K

L

R

R

D

D

F

L

S

D

R

R

F

I

A

V

D

D

C

F

L

D

E

K

R

R

M

A

D

A

F

V

C

S

P

P

L

Y

G

G

A

S

G

G

A

A

L

L

A

A

G

G

T

S

F

L

N

G

I

L

D

D

R

P

H

D

F

A

T

I

A

A

E

D

L

L

G

G

F

F

K

S

A

A

P

A

T

A

E

D

N

N

S

S

L

V

D

D

S

A

V

T

S

A

D

A

R

R

D

D

F

F

A

A

L

A

E

E

F

A

L

A

A

F

A

V

C

F

S

A

I

M

C

I

Q

A

M

V

H

D

L

L

S

S

R

R

F

L

S

A

E

E

E

D

L

I

I

I

I

V

Y

W

S

S

A

S

S

T

E

E

F

F

S

G

F

Y

I

V

E

T

L

L

S

H

D

D

D

S

F

W

C

S

T

T

G

G

S
|
S

I

-

M

-

P

P

Q

Q

K
|
K

K

K

N
|
N

P

P

D

D

M

I

P

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

S

N

L

L

I

A

S

G

L

L

T

A

T

T

M

L

K

K

G

A

L

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

P

P

V

V

F

F

D

D

A

S

V

V

D

A

T

Q

I

L

K

E

A

L

S

L

L

L

K

P

I

A

F

M

S

A

P

G

M

L

V

V

E

A

K

S

M

L

T

T

L

F

R

N

K

V

D

Q

K

R

M

M

E

A

K

E

S

L

A

A

G

P

N

A

G

G

Y

Y

S

T

T

L

A

A

T

T

D

D

L

L

A

A

D

E

Y

W

L

L

V

V

R

R

K

Q

G

G

V

V

P

P

F

F

R

R

Q

S

S

A

H

H

H

E

I

A

V

A

G

G

S

A

A

A

V

V

A

R

Y

A

A

A

I

E

E

Q

K

R

G

G

V

V

D

G

L

L

S

Q

E

E

L

L

S

T

M

D

D

D

E

E

F

L

A

A

R

A

F

I

T

S

D

P

V

E

I

L

T

T

D

P

D

Q

I

V

Y

R

Q

E

Y

V

I

L

T

T

V

I

R

E

A

G

S

S

V

V

N

S

S

A

R

R

V

D

A

C

Y

R

G

G

T

T

A

A

E

P

S

G

S

R

V

V

K

A

E

E

Q

Q

I

L

K

N

S

A

binding argininosuccinate: R98 (= R110), N99 (= N111), V102 (= V114), T144 (= T156), H145 (= H157), Y304 (= Y318), Q309 (= Q323), K312 (= K326)
binding fumaric acid: S266 (= S278), S267 (= S279), K270 (= K284), N272 (= N286)

6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
39% identity, 95% coverage: 13:452/461 of query aligns to 1:404/418 of 6ienC

query
sites
6ienC

P

P

T

S

D

D

K

A

F

L

V

A

E

A

E

-

F

L

N

S

A

K

S

S

V

T

H

H

F

F

D

D

N

W

R

V

F

L

Y

A

K

P

Y

Y

D

D

I

L

K

T

G

A

S

S

I

R

A

A

H

H

A

T

K

M

M

V

L

L

A

F

K

R

Q

A

E

G

I

L

S

T

T

E

E

E

D

Q

R

R

D

D

S

G

I

L

K

A

G

G

L

L

N

D

Q

S

V

L

L

A

Q

Q

E

D

I

V

E

A

T

D

G

G

K

S

L

F

E

G

W

P

K

L

T

V

E

T

D

D

E

E

D

D

I

V

H

H

M

A

A

A

V

L

E

E

K

R

R

G

L

L

T

I

E

D

L

R

V

V

G

G

-

P

D

D

A

L

G

G

K

G

R

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

F

F

R

R

M

M

Y

W

L

L

K

R

A

D

E

A

I

V

I

R

E

R

I

V

Q

A

A

T

L

G

I

V

A

L

E

D

L

V

N

G

T

A

L

L

M

A

K

E

K

Q

A

A

E

A

A

A

E

H

H

P

E

S

V

A

M

I

M

M

P

P

G

G

F

K

T
|
T

H
|
H

L

L

Q

Q

T

S

A

A

Q

Q

P

P

I

I

L

L

F

L

A

A

H

H

W

H

A

L

M

L

A

A

Y

H

F

A

Q

H

M

P

I

L

K

L

R

R

D

D

F

L

S

D

R

R

F

I

A

V

D

D

C

F

L

D

E

K

R

R

M

A

D

A

F

V

C

S

P

P

L

Y

G

G

A

S

G

G

A

A

L

L

A

A

G

G

T

S

F

L

N

G

I

L

D

D

R

P

H

D

F

A

T

I

A

A

E

D

L

L

G

G

F

F

K

S

A

A

P

A

T

A

E

D

N

N

S

S

L

V

D

D

S

A

V

T

S

A

D

A

R

R

D

D

F

F

A

A

L

A

E

E

F

A

L

A

A

F

A

V

C

F

S

A

I

M

C

I

Q

A

M

V

H

D

L

L

S

S

R

R

F

L

S

A

E

E

E

D

L

I

I

I

I

V

Y

W

S

S

A

S

S

T

E

E

F

F

S

G

F

Y

I

V

E

T

L

L

S

H

D

D

D

S

F

W

C

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

M

I

P

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

S

N

L

L

I

A

S

G

L

L

T

A

T

T

M

L

K

K

G

A

L

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

P

P

V

V

F

F

D

D

A

S

V

V

D

A

T

Q

I

L

K

E

A

L

S

L

L

L

K

P

I

A

F

M

S

A

P

G

M

L

V

V

E

A

K

S

M

L

T

T

L

F

R

N

K

V

D

Q

K

R

M

M

E

A

K

E

S

L

A

A

G

P

N

A

G

G

Y

Y

S

T

T

L

A

A

T

T

D

D

L

L

A

A

D

E

Y

W

L

L

V

V

R

R

K

Q

G

G

V

V

P

P

F

F

R

R

Q

S

S

A

H

H

H

R

I

-

V

-

G

-

S

-

A

-

V

-

A

-

Y

-

A

-

I

-

E

-

K

-

G

-

V

-

D

-

L

-

S

-

E

-

L

-

S

-

M

-

D

-

E

-

F

-

A

-

R

-

F

-

T

-

D

-

V

-

I

-

T

-

D

-

I

-

Y

-

Q

E

Y

V

I

L

T

T

V

I

R

E

A

G

S

S

V

V

N

S

S

A

R

R

V

D

A

C

Y

R

G

G

T

T

A

A

E

P

S

G

S

R

V

V

K

A

E

E

Q

Q

I

L

K

N

S

A

binding arginine: R98 (= R110), N99 (= N111), V102 (= V114), Y306 (= Y318), Q311 (= Q323), K314 (= K326)
binding argininosuccinate: T144 (= T156), H145 (= H157), S266 (= S278), S267 (= S279), M269 (= M281), K272 (= K284)
binding fumaric acid: S97 (= S109), R98 (= R110), N99 (= N111)

6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
30% identity, 95% coverage: 23:459/461 of query aligns to 27:463/496 of 6g3iA

query
sites
6g3iA

A

A

S

A

V

L

H

T

F

L

D

T

N

S

R

A

F

V

Y

F

K

P

Y

Y

D

D

I

S

K

Q

G

I

S

H

I

R

A

A

H

H

A

V

K

V

M

M

L

L

A

T

K

E

Q

Q

E

G

I

I

I

L

S

T

T

V

E

E

D

E

R

S

D

A

S

T

I

I

I

L

K

S

G

G

L

L

N

A

Q

Q

V

V

L

D

Q

E

E

L

I

A

E

A

T

T

-

D

G

G

K

S

L

L

E

R

W

-

K

-

T

-

E

-

D

-

E

-

D

-

I

T

H

Y

M

L

A

P

V

Y

E

E

K

A

R

A

L

L

T

K

E

R

L

T

V

I

G

G

D

S

A

V

G

A

K

G

R

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

F

K

R

R

M

M

Y

F

L

L

K

R

A

D

E

Q

I

L

E

R

I

T

Q

I

A

E

L

A

I

V

A

I

E

G

L

Y

L

R

N

E

T

A

L

V

M

V

K

H

K

K

A

A

E

A

A

D

E

H

H

L

E

D

V

T

M

V

M

M

P

V

G

V

F

Y

T

T

H

Q

L

R

Q

K

T

E

A

A

Q

Q

P

P

I

I

L

T

F

L

A

G

H

H

W

Y

A

L

M

M

A

A

Y

I

F

S

Q

E

M

N

I

L

K

A

R

K

D

N

F

L

S

D

R

R

F

Y

A

R

D

E

C

L

L

Y

E

A

R

R

M

I

D

N

F

L

C

C

P

P

L

L

G

G

A

A

G

A

A

A

L

T

A

A

G

G

T

T

T

G

F

W

N

P

I

L

D

N

R

R

H

D

F

R

T

T

A

S

A

A

E

L

L

L

G

G

F

F

K

D

A

G

P

L

T

V

E

V

N

N

S

S

L

I

D

E

S

G

V

V

S

A

D

G

R

W

D

D

F

H

A

V

L

A

E

E

F

H

L

A

A

F

A

V

C

N

S

A

I

V

C

F

Q

L

M

S

H

G

L

L

S

S

R

R

F

L

S

A

E

S

E

E

L

I

I

Q

I

L

Y

W

S

S

A

T

S

D

E

E

F

Y

S

Q

F

V

I

A

E

E

L

L

S

D

D

A

D

S

F

F

C

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

M

S

P

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

S

P

L

L

I

V

S

G

L

I

L

L

T

T

T

S

M

L

K

N

G

A

L

I

P

E

L

Y

A

Q

Y

Y

N

S

K

A

D

A

M

R

Q

V

E

E

D

-

K

L

E

E

P

P

V

-

F

-

D

R

A

S

V

I

D

D

T

A

I

L

K

I

A

A

S

A

L

T

K

H

I

A

F

M

S

T

P

G

M

V

V

V

E

R

K

T

M

L

T

H

L

P

R

N

K

K

D

E

K

R

M

M

E

R

K

Q

S

Y

A

A

G

A

N

E

G

N

Y

Y

S

S

T

T

A

M

T

T

D

D

L

L

A

T

D

D

Y

M

L

L

V

V

R

R

K

R

-

V

G

G

V

I

P

D

F

Y

R

R

Q

E

S

A

H

H

H

E

I

I

V

V

G

A

S

H

A

V

V

V

A

I

Y

T

A

A

I

I

E

E

K

K

G

G

V

I

D

K

L

A

S

N

E

K

L

I

S

G

M

L

D

D

-

L

-

V

-

Q

-

E

-

A

-

V

-

A

E

Q

F

T

A

G

R

A

F

G

T

I

D

N

V

V

I

S

T

A

D

D

I

I

Y

K

Q

D

Y

A

I

L

T

D

V

P

R

W

A

Q

S

N

V

V

N

L

S

R

R

R

V

E

A

G

Y

K

G

G

G

M

T

P

A

A

E

P

S

M

S

S

V

V

K

K

E

A

Q

S

I

I

K

D

S

D

A

A

K

M

K

A

F

E

L

L

N

H

E

K

binding (2~{S})-2-(2-azanylethylamino)butanedioic acid: S276 (= S278), S277 (= S279), M279 (= M281), K282 (= K284), N284 (= N286), D286 (= D288)
binding fumaric acid: R290 (≠ L292)

Sites not aligning to the query:

binding fumaric acid: 22

6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
30% identity, 95% coverage: 23:459/461 of query aligns to 27:463/497 of 6g3hA

query
sites
6g3hA

A

A

S

A

V

L

H

T

F

L

D

T

N

S

R

A

F

V

Y

F

K

P

Y

Y

D

D

I

S

K

Q

G

I

S

H

I

R

A

A

H

H

A

V

K

V

M

M

L

L

A

T

K

E

Q

Q

E

G

I

I

I

L

S

T

T

V

E

E

D

E

R

S

D

A

S

T

I

I

I

L

K

S

G

G

L

L

N

A

Q

Q

V

V

L

D

Q

E

E

L

I

A

E

A

T

T

-

D

G

G

K

S

L

L

E

R

W

-

K

-

T

-

E

-

D

-

E

-

D

-

I

T

H

Y

M

L

A

P

V

Y

E

E

K

A

R

A

L

L

T

K

E

R

L

T

V

I

G

G

D

S

A

V

G

A

K

G

R

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

F

K

R

R

M

M

Y

F

L

L

K

R

A

D

E

Q

I

L

E

R

I

T

Q

I

A

E

L

A

I

V

A

I

E

G

L

Y

L

R

N

E

T

A

L

V

M

V

K

H

K

K

A

A

E

A

A

D

E

H

H

L

E

D

V

T

M

V

M

M

P

V

G

V

F

Y

T

T

H

Q

L

R

Q

K

T

E

A

A

Q

Q

P

P

I

I

L

T

F

L

A

G

H

H

W

Y

A

L

M

M

A

A

Y

I

F

S

Q

E

M

N

I

L

K

A

R

K

D

N

F

L

S

D

R

R

F

Y

A

R

D

E

C

L

L

Y

E

A

R

R

M

I

D

N

F

L

C

C

P

P

L

L

G

G

A

A

G

A

A

A

L

T

A

A

G

G

T

T

T

G

F

W

N

P

I

L

D

N

R

R

H

D

F

R

T

T

A

S

A

A

E

L

L

L

G

G

F

F

K

D

A

G

P

L

T

V

E

V

N

N

S

S

L

I

D

E

S

G

V

V

S

A

D

G

R

W

D

D

F

H

A

V

L

A

E

E

F

H

L

A

A

F

A

V

C

N

S

A

I

V

C

F

Q

L

M

S

H

G

L

L

S

S

R

R

F

L

S

A

E

S

E

E

L

I

I

Q

I

L

Y

W

S

S

A

T

S

D

E

E

F

Y

S

Q

F

V

I

A

E

E

L

L

S

D

D

A

D

S

F

F

C

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

M

S

P

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

S

P

L

L

I

V

S

G

L

I

L

L

T

T

T

S

M

L

K

N

G

A

L

I

P

E

L

Y

A

Q

Y

Y

N

S

K

A

D

A

M

R

Q

V

E

E

D

-

K

L

E

E

P

P

V

-

F

-

D

R

A

S

V

I

D

D

T

A

I

L

K

I

A

A

S

A

L

T

K

H

I

A

F

M

S

T

P

G

M

V

V

V

E

R

K

T

M

L

T

H

L

P

R

N

K

K

D

E

K

R

M

M

E

R

K

Q

S

Y

A

A

G

A

N

E

G

N

Y

Y

S

S

T

T

A

M

T

T

D

D

L

L

A

T

D

D

Y

M

L

L

V

V

R

R

K

R

-

V

G

G

V

I

P

D

F

Y

R

R

Q

E

S

A

H

H

H

E

I

I

V

V

G

A

S

H

A

V

V

V

A

I

Y

T

A

A

I

I

E

E

K

K

G

G

V

I

D

K

L

A

S

N

E

K

L

I

S

G

M

L

D

D

-

L

-

V

-

Q

-

E

-

A

-

V

-

A

E

Q

F

T

A

G

R

A

F

G

T

I

D

N

V

V

I

S

T

A

D

D

I

I

Y

K

Q

D

Y

A

I

L

T

D

V

P

R

W

A

Q

S

N

V

V

N

L

S

R

R

R

V

E

A

G

Y

K

G

G

G

M

T

P

A

A

E

P

S

M

S

S

V

V

K

K

E

A

Q

S

I

I

K

D

S

D

A

A

K

M

K

A

F

E

L

L

N

H

E

K

binding (2~{S})-2-[2-[[(2~{S})-1,4-bis(oxidanyl)-1,4-bis(oxidanylidene)butan-2-yl]amino]ethylamino]butanedioic acid: S276 (= S278), S277 (= S279), M279 (= M281), K282 (= K284), N284 (= N286), D286 (= D288), R290 (≠ L292)

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: 23:459/461 of query aligns to 27:463/497 of 6g3gA

query
sites
6g3gA

A

A

S

A

V

L

H

T

F

L

D

T

N

S

R

A

F

V

Y

F

K

P

Y

Y

D

D

I

S

K

Q

G

I

S

H

I

R

A

A

H

H

A

V

K

V

M

M

L

L

A

T

K

E

Q

Q

E

G

I

I

I

L

S

T

T

V

E

E

D

E

R

S

D

A

S

T

I

I

I

L

K

S

G

G

L

L

N

A

Q

Q

V

V

L

D

Q

E

E

L

I

A

E

A

T

T

-

D

G

G

K

S

L

L

E

R

W

-

K

-

T

-

E

-

D

-

E

-

D

-

I

T

H

Y

M

L

A

P

V

Y

E

E

K

A

R

A

L

L

T

K

E

R

L

T

V

I

G

G

D

S

A

V

G

A

K

G

R

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

F

K

R

R

M

M

Y

F

L

L

K

R

A

D

E

Q

I

L

E

R

I

T

Q

I

A

E

L

A

I

V

A

I

E

G

L

Y

L

R

N

E

T

A

L

V

M

V

K

H

K

K

A

A

E

A

A

D

E

H

H

L

E

D

V

T

M

V

M

M

P

V

G

V

F

Y

T

T

H

Q

L

R

Q

K

T

E

A

A

Q

Q

P

P

I

I

L

T

F

L

A

G

H

H

W

Y

A

L

M

M

A

A

Y

I

F

S

Q

E

M

N

I

L

K

A

R

K

D

N

F

L

S

D

R

R

F

Y

A

R

D

E

C

L

L

Y

E

A

R

R

M

I

D

N

F

L

C

C

P

P

L

L

G

G

A

A

G

A

A

A

L

T

A

A

G

G

T

T

T

G

F

W

N

P

I

L

D

N

R

R

H

D

F

R

T

T

A

S

A

A

E

L

L

L

G

G

F

F

K

D

A

G

P

L

T

V

E

V

N

N

S

S

L

I

D

E

S

G

V

V

S

A

D

G

R

W

D

D

F

H

A

V

L

A

E

E

F

H

L

A

A

F

A

V

C

N

S

A

I

V

C

F

Q

L

M

S

H

G

L

L

S

S

R

R

F

L

S

A

E

S

E

E

L

I

I

Q

I

L

Y

W

S

S

A

T

S

D

E

E

F

Y

S

Q

F

V

I

A

E

E

L

L

S

D

D

A

D

S

F

F

C

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

M

S

P

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

S

P

L

L

I

V

S

G

L

I

L

L

T

T

T

S

M

L

K

N

G

A

L

I

P

E

L

Y

A

Q

Y

Y

N

S

K

A

D

A

M

R

Q

V

E

E

D

-

K

L

E

E

P

P

V

-

F

-

D

R

A

S

V

I

D

D

T

A

I

L

K

I

A

A

S

A

L

T

K

H

I

A

F

M

S

T

P

G

M

V

V

V

E

R

K

T

M

L

T

H

L

P

R

N

K

K

D

E

K

R

M

M

E

R

K

Q

S

Y

A

A

G

A

N

E

G

N

Y

Y

S

S

T

T

A

M

T

T

D

D

L

L

A

T

D

D

Y

M

L

L

V

V

R

R

K

R

-

V

G

G

V

I

P

D

F

Y

R

R

Q

E

S

A

H

H

H

E

I

I

V

V

G

A

S

H

A

V

V

V

A

I

Y

T

A

A

I

I

E

E

K

K

G

G

V

I

D

K

L

A

S

N

E

K

L

I

S

G

M

L

D

D

-

L

-

V

-

Q

-

E

-

A

-

V

-

A

E

Q

F

T

A

G

R

A

F

G

T

I

D

N

V

V

I

S

T

A

D

D

I

I

Y

K

Q

D

Y

A

I

L

T

D

V

P

R

W

A

Q

S

N

V

V

N

L

S

R

R

R

V

E

A

G

Y

K

G

G

G

M

T

P

A

A

E

P

S

M

S

S

V

V

K

K

E

A

Q

S

I

I

K

D

S

D

A

A

K

M

K

A

F

E

L

L

N

H

E

K

binding succinic acid: S276 (= S278), S277 (= S279), M279 (= M281), K282 (= K284), N284 (= N286)

6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
30% identity, 95% coverage: 23:459/461 of query aligns to 27:463/497 of 6g3fA

query
sites
6g3fA

A

A

S

A

V

L

H

T

F

L

D

T

N

S

R

A

F

V

Y

F

K

P

Y

Y

D

D

I

S

K

Q

G

I

S

H

I

R

A

A

H

H

A

V

K

V

M

M

L

L

A

T

K

E

Q

Q

E

G

I

I

I

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T

T

V

E

E

D

E

R

S

D

A

S

T

I

I

I

L

K

S

G

G

L

L

N

A

Q

Q

V

V

L

D

Q

E

E

L

I

A

E

A

T

T

-

D

G

G

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S

L

L

E

R

W

-

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-

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-

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-

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-

E

-

D

-

I

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H

Y

M

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A

P

V

Y

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A

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A

L

L

T

K

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I

G

G

D

S

A

V

G

A

K

G

R

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

F

K

R

R

M

M

Y

F

L

L

K

R

A

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Q

I

L

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R

I

T

Q

I

A

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A

I

E

G

L

Y

L

R

N

E

T

A

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V

K

H

K

K

A

A

E

A

A

D

E

H

H

L

E

D

V

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M

V

M

M

P

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G

V

F

Y

T

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H

Q

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R

Q

K

T

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A

A

Q

Q

P

P

I

I

L

T

F

L

A

G

H

H

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Y

A

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M

A

A

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E

M

N

I

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A

R

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D

N

F

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D

R

R

F

Y

A

R

D

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C

L

L

Y

E

A

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R

M

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N

F

L

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C

P

P

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L

G

G

A

A

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A

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A

A

G

G

T

T

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G

F

W

N

P

I

L

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N

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R

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D

F

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T

A

S

A

A

E

L

L

L

G

G

F

F

K

D

A

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P

L

T

V

E

V

N

N

S

S

L

I

D

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S

G

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V

S

A

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W

D

D

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H

A

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F

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I

A

E

E

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D

A

D

S

F

F

C

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

M

S

P

L

E

E

L

R

I

S

R

R

G

K

K

A

T

A

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A

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A

Y

M

G

G

S

P

L

L

I

V

S

G

L

I

L

L

T

T

T

S

M

L

K

N

G

A

L

I

P

E

L

Y

A

Q

Y

Y

N

S

K

A

D

A

M

R

Q

V

E

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D

-

K

L

E

E

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P

V

-

F

-

D

R

A

S

V

I

D

D

T

A

I

L

K

I

A

A

S

A

L

T

K

H

I

A

F

M

S

T

P

G

M

V

V

V

E

R

K

T

M

L

T

H

L

P

R

N

K

K

D

E

K

R

M

M

E

R

K

Q

S

Y

A

A

G

A

N

E

G

N

Y

Y

S

S

T

T

A

M

T

T

D

D

L

L

A

T

D

D

Y

M

L

L

V

V

R

R

K

R

-

V

G

G

V

I

P

D

F

Y

R

R

Q

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S

A

H

H

H

E

I

I

V

V

G

A

S

H

A

V

V

V

A

I

Y

T

A

A

I

I

E

E

K

K

G

G

V

I

D

K

L

A

S

N

E

K

L

I

S

G

M

L

D

D

-

L

-

V

-

Q

-

E

-

A

-

V

-

A

E

Q

F

T

A

G

R

A

F

G

T

I

D

N

V

V

I

S

T

A

D

D

I

I

Y

K

Q

D

Y

A

I

L

T

D

V

P

R

W

A

Q

S

N

V

V

N

L

S

R

R

R

V

E

A

G

Y

K

G

G

G

M

T

P

A

A

E

P

S

M

S

S

V

V

K

K

E

A

Q

S

I

I

K

D

S

D

A

A

K

M

K

A

F

E

L

L

N

H

E

K

binding fumaric acid: S276 (= S278), S277 (= S279), M279 (= M281), K282 (= K284), N284 (= N286)

Q9LCC6 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Bacillus sp. (see 3 papers)
27% identity, 53% coverage: 127:372/461 of query aligns to 151:425/468 of Q9LCC6

query
sites
Q9LCC6

I

I

E

A

I

V

Q

L

A

S

L

L

I

L

A

N

E

Q

L

L

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I

N

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T

-

T

-

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-

Y

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-

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K

A

A

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D

A

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E

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A

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I

M
x
K

P

M

G

G

F

R

T
|
T

H
|
H

L

L

Q

Q

T

D

A

A

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P

P

I

I

L

L

F

L

A

G

H

Q

W

E

A

F

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E

A

A

Y

Y

F

A

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M

V

I

I

K

A

R

R

D

D

F

I

S

E

R

R

F

I

A

A

D

N

C

T

L

R

E

N

R

N

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L

D

Y

F

D

C

I

P

N

L

M

G

G

A

A

G

T

A

A

L

V

A

-

G

G

T

T

T

G

F

L

N

N

I

A

D

D

R

P

H

E

F

Y

T

I

A

S

A

I

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V

L

T

G

E

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L

A

A

-

K

-

F

-

S

-

G

-

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-

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-

L

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T

A

E

Q

N

H

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L

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D

S

A

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S

Q

D

N

R

T

D

D

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C

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Y

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E

F

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A

S

A

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C

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M

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L

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S
|
S

I
|
I

M
|
M

P
|
P

Q

G

K
|
K

K

V

N
|
N

P

P

D

V

M

M

P

P

E

E

L

V

I

M

R

N

G

Q

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A

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V

Y

F

G

G

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N

L

D

I

L

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T

L

I

L

T

T

S

T

A

M

S

K

E

G

A

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G

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Q

L

F

A

E

Y

L

N

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D

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M

-

Q

-

E

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M

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E

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P

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V

-

L

-

F

F

F

D

N

A

L

V

I

D

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T

S

I

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S

A

I

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M

L

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N

I

V

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S

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F

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T

E

E

K

N

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C

T

L

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K

-

G

-

I

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K

-

A

-

N

-

E

L

R

R

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K

K

D

E

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M

V

E

E

K

K

S

S

A

I

G

G

-

I

-

T

-

A

-

I

-

N

-

P

-

H

N

V

G

G

Y

Y

S

E

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A

A

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D

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L

L

A

A

K183 (≠ M152) mutation to A: Loss of activity. Does not affect tertiary structure.
T187 (= T156) 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 (= H157) 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 (= S278) mutation to A: Loss of activity.
S319 (= S279) binding L-aspartate; mutation to A: Almost no change in catalytic efficiency.
I320 (= I280) mutation to A: 50-fold decrease in catalytic efficiency.
M321 (= M281) mutation to A: 338-fold decrease in catalytic efficiency.
P322 (= P282) mutation to A: Almost no change in catalytic efficiency.
K324 (= K284) 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 (= N286) 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)
27% identity, 53% coverage: 127:372/461 of query aligns to 148:422/463 of 3r6vG

query
sites
3r6vG

I

I

E

A

I

V

Q

L

A

S

L

L

I

L

A

N

E

Q

L

L

L

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T

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|
H

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L

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A

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D

F

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E

R

R

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A

A

D

N

C

T

L

R

E

N

R

N

M

L

D

Y

F

D

C

I

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N

L

M

G

G

A

A

G

T

A

A

L

V

A

-

G

G

T

T

T

G

F

L

N

N

I

A

D

D

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P

H

E

F

Y

T

I

A

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A

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A

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K

-

F

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S

-

G

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H

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L

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R

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S

T

A

E

Q

N

H

S

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L

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D

D

S

A

V

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S

Q

D

N

R

T

D

D

F

C

A

Y

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T

E

E

F

V

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S

A

S

A

A

C

L

S

K

I

V

C

C

Q

M

M

I

H

N

L

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R

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F

I

S

A

E

N

E

D

L

L

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R

I

L

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A

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S

A

G

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R

F

A

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F

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E

E

L

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L

D

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D

A

F

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C

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T

P

G
|
G

S
|
S

I

I

M

M

P

P

Q

G

K
|
K

K

V

N

N

P

P

D

V

M

M

P

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

S

N

L

D

I

L

S

T

L

I

L

T

T

S

T

A

M

S

K

E

G

A

L

G

P

Q

L

F

A

E

Y

L

N

N

K

V

D

-

M

-

Q

-

E

-

D

-

K

M

E

E

P

P

V

V

-

L

-

F

F

F

D

N

A

L

V

I

D

Q

T

S

I

I

K

S

A

I

S

M

L

T

K

N

I

V

F

F

S

K

P

S

M

F

V

T

E

E

K

N

M

C

T

L

-

K

-

G

-

I

-

K

-

A

-

N

-

E

L

R

R

M

K

K

D

E

K

Y

M

V

E

E

K

K

S

S

A

I

G

G

-

I

-

T

-

A

-

I

-

N

-

P

-

H

N

V

G

G

Y

Y

S

E

T

T

A

A

T

A

D

K

L

L

A

A

active site: H185 (= H157), S315 (= S278), K321 (= K284), E328 (= E291)
binding aspartic acid: G314 (= G277), S315 (= S278), S316 (= S279)

3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
27% identity, 53% coverage: 127:372/461 of query aligns to 147:421/462 of 3r6qA

query
sites
3r6qA

I

I

E

A

I

V

Q

L

A

S

L

L

I

L

A

N

E

Q

L

L

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T

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-

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M

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K

A

A

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A

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H
|
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P

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L

A

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A

R

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D

F

I

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E

R

R

F

I

A

A

D

N

C

T

L

R

E

N

R

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M

L

D

Y

F

D

C

I

P

N

L

M

G

G

A

A

G

T

A

A

L

V

A

-

G

G

T

T

T

G

F

L

N

N

I

A

D

D

R

P

H

E

F

Y

T

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A

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A

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L

A

A

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K

-

F

-

S

-

G

-

H

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-

L

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P

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T

A

E

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N

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A

V

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S

Q

D

N

R

T

D

D

F

C

A

Y

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T

E

E

F

V

L

S

A

S

A

A

C

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M

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F

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A

E

N

E

D

L

L

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L

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A

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P

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R

F

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E

L

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L

D

P

D

A

F

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C

Q

T

P

G

G

S
|
S

S

S

I

I

M

M

P

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Q

G

K
|
K

K

V

N

N

P

P

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M

M

P

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E
|
E

L

V

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M

R

N

G

Q

K

V

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A

G

F

R

Q

V

V

Y

F

G

G

S

N

L

D

I

L

S

T

L

I

L

T

T

S

T

A

M

S

K

E

G

A

L

G

P

Q

L

F

A

E

Y

L

N

N

K

V

D

-

M

-

Q

-

E

-

D

-

K

M

E

E

P

P

V

V

-

L

-

F

F

F

D

N

A

L

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I

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Q

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I

I

K

S

A

I

S

M

L

T

K

N

I

V

F

F

S

K

P

S

M

F

V

T

E

E

K

N

M

C

T

L

-

K

-

G

-

I

-

K

-
x
A

-

N

-
x
E

-

E

L

R

R

M

K

K

D

E

K

Y

M

V

E

E

K

K

S

S

A

I

G

G

-

I

-

T

-

A

-

I

-

N

-

P

-

H

N

V

G

G

Y

Y

S

E

T

T

A

A

T

A

D

K

L

L

A

A

active site: H184 (= H157), S314 (= S278), K320 (= K284), E327 (= E291)
binding calcium ion: A389 (vs. gap), E391 (vs. gap)

P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
24% identity, 86% coverage: 9:406/461 of query aligns to 4:392/431 of P12047

query
sites
P12047

R

R

F

Y

S

S

L

R

P

P

T

-

D

-

K

-

F

-

V

-

E

-

E

E

F

M

N

S

A

A

S

I

V

W

H

T

F

D

D

E

N

N

R

R

F

F

Y

Q

K

A

Y

W

D

-

I

L

K

E

G

V

S

E

I

I

A

L

H

A

A

C

K

E

M

A

L

W

A

A

K

E

Q

L

E

G

I

V

I

I

S

P

T

K

E

E

D

D

-

V

-

K

-

V

-

M

R

R

D

E

S

N

I

A

I

S

K

F

G

D

L

I

N

N

Q

R

V

I

L

L

Q

-

E

E

I

I

E

E

T

-

G

-

K

-

L

-

E

-

W

-

K

K

T

D

E

T

D

R

E

H

D

D

I

V

H

-

M

V

A

A

V

F

E

T

K

R

R

A

L

V

T

S

E

E

L

S

V

L

G

G

D

E

A

E

G

R

K

K

R

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

F

L

R

S

M

Y

Y

L

L

L

K

K

A

Q

E

A

I

N

I

D

E

I

I

L

Q

L

A

K

L

D

I

L

A

E

E

R

L

F

L

V

N

D

T

I

L

I

M

K

K

E

K

K

A

A

E

K

A

E

E

H

H

K

E

Y

V

T

M

V

M

M

P

M

G

G

F

R

T

T

H
|
H

L

G

Q

V

T

H

A

A

Q

E

P

P

I

T

L

T

F

F

A

G

H

L

W

K

A

L

M

A

A

L

Y

W

F

H

Q

E

M

E

I

M

K

K

R

R

D

N

F

L

S

E

R

R

F

F

A

K

D

Q

C

A

L

K

E

A

R

G

M

I

D

E

F

V

C

G

P

K

L

I

G

-

A

S

G

G

A

A

L

V

A

-

G

G

T

T

T

Y

F

A

N

N

I

I

D

D

-

P

-

F

-

V

R

E

H

Q

F

Y

T

V

A

C

A

E

E

K

L

L

G

G

F

L

K

K

A

A

P

A

T

P

E

I

N

S

S

T

L

-

D

-

S
x
Q

V

T

S

L

D

Q

R

R

D

D

F

R

A

H

L

A

E

D

F

Y

L

M

A

A

A

T

C

L

S

A

I

L

C

I

Q

A

M

T

H

S

L

I

S

E

R

K

F

F

S

A

E

V

E

E

L

I

I

R

I

G

Y

L

S

Q

A

K

S

S

E

E

F

T

S

R

F

-

I

-

E

E

L

V

S

E

D

E

D

F

F

F

C

A

-

K

-

G

-

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

M

G

P

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

S

-

L

-

I

-

S

Y

L

M

T

T

T

A

M

Y

K

E

G

N

L

V

P

P

L

L

A

W

Y

H

N

E

K
x
R

D

D

M

I

Q

S

E

H

-

S

-

A

D

E

K

R

E

I

P

I

V

L

F

P

D

D

A

A

V

T

D

I

T

A

I

L

K

N

A

Y

S

M

L

L

K

N

I

R

F

F

S

S

P

N

M

I

V

V

E

K

K

N

M

L

T

T

L

V

-

F

-

P

-

E

-

N

R

M

K

K

D

R

K

N

M

M

E

D

K

R

S

T

A

L

G

G

N

L

G

I

Y

Y

S

S

T

Q

A

R

T

V

D

L

L

L

A

A

D

-

Y

-

L

L

V

I

R

D

K

T

G

G

V

L

P

T

F

R

R

E

Q

E

S

A

H

Y

H

D

I

T

V

V

G

Q

S

P

A

K

V

A

A

M

Y

E

A

A

I

W

E

E

K

K

G

Q

V

V

D

P

L

F

S

R

E

E

L

L

H89 (= H105) mutation to Q: Abolishes enzyme activity.
H141 (= H157) mutation to Q: Abolishes enzyme activity.
Q212 (≠ S229) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
N270 (= N286) mutation N->D,L: Abolishes enzyme activity.
R301 (≠ K320) mutation R->K,Q: Abolishes enzyme activity.

2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
23% identity, 69% coverage: 87:406/461 of query aligns to 70:391/427 of 2x75A

query
sites
2x75A

M

V

A

A

V

F

E

T

K

R

R

Q

L

V

T

S

E

E

L

T

V

L

G

G

D

E

A

E

G

R

K

K

R

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

F

L

R

S

M

F

Y

V

L

I

K

K

A

Q

E

A

I

N

I

D

E

I

I

I

Q

E

A

K

L

D

I

L

A

E

E

R

L

F

L

I

N

D

T

V

L

L

M

A

K

E

K

K

A

A

E

K

A

N

E

Y

H

K

E

Y

V

T

M

L

M

M

P

M

G

G

F

R

T
|
T

H
|
H

L

G

Q

V

T

H

A

A

Q

E

P

P

I

T

L

T

F

F

A

G

H

V

W

K

A

M

M

A

A

L

Y

W

F

Y

Q

T

M

E

I

M

K

Q

R

R

D

N

F

L

S

Q

R

R

F

F

A

K

D

Q

C

V

L

R

E

E

R

E

M

I

D

E

F

V

C

G

P

K

L

M

G

-

A

S

G

G

A

A

L

V

A

-

G

G

T

T

T

F

F

A

N

N

I

I

D

P

-

P

-

E

-

I

R

E

H

S

F

Y

T

V

A

C

A

K

E

H

L

L

G

G

F

I

-

G

K

T

A

A

P

P

T

V

E

S

N

T

S

-

L

-

D

-

S

Q

V

T

S

L

D

Q

R

R

D

D

F

R

A

H

L

A

E

Y

F

Y

L

I

A

A

A

T

C

L

S

A

I

L

C

I

Q

A

M

T

H

S

L

L

S

E

R

K

F

F

S

A

E

V

E

E

L

I

I

R

I

N

Y

L

S

Q

A

K

S

T

E

E

F

T

S

R

F

-

I

-

E

E

L

V

S

E

D

E

D

A

F

F

C

A

-

K

-

G

-

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

M

G

P

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

S

Y

L

I

I

T

S

-

L

-

T

T

T

A

M

Y

K

E

G

N

L

V

P

P

L

L

A

W

Y

H

N

E

K

R

D

D

M

I

Q

S

E

H

-

S

-

A

D

E

K

R

E

I

P

M

V

L

F

P

D

D

A

V

V

T

D

I

T

A

I

L

K

D

A

Y

S

A

L

L

K

N

I

R

F

F

S

T

P

N

M

I

V

V

E

D

K

R

M

L

T

T

L

V

R

F

K

E

D

D

K

N

M

M

-

R

-

N

-

I

E

D

K

K

S

T

A

F

G

G

N

L

G

I

Y

F

S

S

T

Q

A

R

T

V

D

L

L

L

A

A

D

-

Y

-

L

L

V

I

R

N

K

K

G

G

V

M

P

V

F

R

R

E

Q

E

S

A

H

Y

H

D

I

K

V

V

G

Q

S

P

A

K

V

A

A

M

Y

I

A

S

I

W

E

E

K

T

G

K

V

T

D

P

L

F

S

R

E

E

L

L

active site: T139 (= T156), H140 (= H157), S261 (= S278), S262 (= S279), K267 (= K284), E274 (= E291)
binding adenosine monophosphate: N275 (≠ L292)

Sites not aligning to the query:

active site: 67
binding adenosine monophosphate: 3, 4

P9WN93 Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
26% identity, 39% coverage: 123:303/461 of query aligns to 153:343/474 of P9WN93

query
sites
P9WN93

K

E

A

A

E

A

I

V

I

A

E

H

I

L

Q

I

A

P

L

A

I

L

A

Q

E

Q

L

L

L

H

N

D

T

A

L

L

M

A

K

A

K

K

A

A

E

L

A

D

E

W

H

H

E

T

V

V

M

V

M

K

P

S

G

G

F

R

T
|
T

H

H

L

L

Q

M

T

D

A

A

Q

V

P

P

I

V

L

T

F

L

A

G

H

Q

W

E

A

F

M

S

A

G

Y

Y

F

A

Q

R

M

Q

I

I

K

E

R

A

D

G

F

I

S

E

R

R

F

V

A

R

D

A

C

C

L

L

E

P

R

R

M

L

D

G

F

E

C

L

P

A

L

I

G

G

A

-

G

G

A

T

L

A

A

V

G

G

T

T

T

G

F

L

N

N

I

A

D

P

R

D

H

D

F

F

T

G

-

V

-

R

-

V

-

A

-

V

-

L

A

V

A

A

E

Q

L

T

G

G

F

L

K

S

A

E

-

L

-

R

P

T

T

A

E

A

N

N

S

S

L

F

D

E

S

A

V

Q

S

A

D

A

R

R

D

D

F

G

A

L

L

V

E

E

F

A

L

S

A

G

A

A

C

L

S

R

I

T

C

I

Q

A

M

V

H

S

L

L

S

T

R

K

F

I

S

A

E

N

E

D

L

I

I

R

I

W

Y

M

S

G

A

S

S

G

E

P

F

L

S

T

F

G

-

L

-

A

-

E

I

I

E

Q

L

L

S

P

D

-

D

D

F

L

C

Q

T

P

G

G

S
|
S

I

I

M

M

P

P

Q

G

K
|
K

K
x
V

N
|
N

P

P

D

V

M

L

P

P

E

E

L

A

I

V

R

T

G

Q

K

V

T

A

G

A

R

Q

V

V

Y

I

G

G

S

N

T186 (= T156) binding substrate
S318 (= S278) active site; mutation S->A,C: Absence of fumarase activity.
S319 (= S279) binding substrate
KVN 324:326 (≠ KKN 284:286) binding substrate

Sites not aligning to the query:

104:106 binding substrate
138:140 binding substrate

Query Sequence

>WP_013012123.1 NCBI__GCF_000025725.1:WP_013012123.1
MSEKMWGGRFSLPTDKFVEEFNASVHFDNRFYKYDIKGSIAHAKMLAKQEIISTEDRDSI
IKGLNQVLQEIETGKLEWKTEDEDIHMAVEKRLTELVGDAGKRLHTARSRNDQVAVDFRM
YLKAEIIEIQALIAELLNTLMKKAEAEHEVMMPGFTHLQTAQPILFAHWAMAYFQMIKRD
FSRFADCLERMDFCPLGAGALAGTTFNIDRHFTAAELGFKAPTENSLDSVSDRDFALEFL
AACSICQMHLSRFSEELIIYSASEFSFIELSDDFCTGSSIMPQKKNPDMPELIRGKTGRV
YGSLISLLTTMKGLPLAYNKDMQEDKEPVFDAVDTIKASLKIFSPMVEKMTLRKDKMEKS
AGNGYSTATDLADYLVRKGVPFRQSHHIVGSAVAYAIEKGVDLSELSMDEFARFTDVITD
DIYQYITVRASVNSRVAYGGTAESSVKEQIKSAKKFLNEIY

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