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)
44% identity, 99% coverage: 1:459/464 of query aligns to 1:458/468 of P24058

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P24058

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W11 (≠ S11) 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 (= S29) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
D33 (= D33) mutation to N: 99% decrease in catalytic efficiency.
D89 (= D89) mutation to N: Loss of activity.
N116 (= N116) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
D117 (= D117) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
T161 (= T161) 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 (= H162) mutation to E: Loss of activity.
R238 (= R238) mutation to Q: Loss of activity.
T281 (= T281) mutation to V: 80% decrease in catalytic efficiency.
S283 (= S283) 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 (= N291) binding in chain B; mutation to L: Loss of activity.
D293 (= D293) mutation to N: 99% decrease in catalytic efficiency.
E296 (= E296) mutation to D: Loss of activity.
Y323 (= Y323) binding in chain A
K325 (= K325) mutation to N: 99% decrease in catalytic efficiency.
Q328 (= Q328) binding in chain A
D330 (= D330) mutation to N: Loss of activity.
K331 (= K331) binding in chain A; mutation to Q: Loss of activity.

1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
44% identity, 95% coverage: 18:459/464 of query aligns to 1:441/450 of 1k7wD

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active site: E71 (= E88), T144 (= T161), H145 (= H162), A266 (≠ S283), S267 (= S284), K272 (= K289), E279 (= E296)
binding argininosuccinate: R98 (= R115), N99 (= N116), V102 (= V119), T144 (= T161), H145 (= H162), Y306 (= Y323), Q311 (= Q328), K314 (= K331)

P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
44% identity, 98% coverage: 9:462/464 of query aligns to 7:459/464 of P04424

query
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P04424

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V

I

R
|
R

G

S

K

K

S

A

G

G

R

R

V

V

Y

F

G

G

H
x
R

L

C

V

A

S

G

L

L

T

M

L

T

M

L

K

K

S

G

Q

L

P

P

L

S

A

T

Y

Y

N

N

K

K

D

D

N

L

Q
|
Q

E

E

D

D

K

K

E

E

P

A

L

V

F

F

D

E

T
x
V

I

S

D

D

T

T

V

M

R

S

G

A

C

V

L

L

R

Q

A

V

F

A

G

T

D

G

M

V

M

I

P

S

A

T

L

L

E

Q

V

I

K

H

R

Q

D

E

N

N

T
x
M

Y

G

R

Q

A

A

A

L

R

S

N

P

G

D

F

M

A

-

T

L

A

A

T

T

D

D

L

L

A

A

D

Y

Y

Y

L

L

V

V

R

R

K

K

G

G

L
x
M

A

P

F

F

R
|
R

D

Q

A

A

H
|
H

E

E

A

A

V

S

G

G

L

K

A

A

V

V

A

F

H

M

G
x
A

V

E

K

T

T

K

Q

G

Q

V

D

A

L

L

A

N

D

Q

M

L

S

S

L

L

A

Q

T

E

L

L

Q

Q

G

T

F

I

C

S

D

P

V

L

I

F

D

S

Q

G

D

D

V

V

F

I

E

C

V

V

L

W

T

D

L

Y

E

G

G

H

S

S

V

V

N

E

A

Q

R

Y

N

G

H

A

L

L

G

G

T

T

A

A

P

R

A

S

Q

S

V

V

R

D

H

W

Q

Q

V

I

A

R

Q

Q

A

V

K
x
R

T

A

R

L

L

L

R12 (= R14) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
D31 (= D33) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
K51 (= K53) mutation to N: 2-fold reduction in activity.
K69 (≠ H71) modified: N6-acetyllysine
E73 (= E75) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
D87 (= D89) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
H89 (= H91) mutation to Q: 10-fold reduction in activity.
R94 (≠ S96) to C: in ARGINSA; severe; dbSNP:rs374304304
R95 (= R97) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
R113 (= R115) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
D120 (= D122) to E: in ARGINSA; severe
V178 (≠ E180) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
T181 (≠ V183) to S: in a breast cancer sample; somatic mutation
R182 (= R184) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
R186 (= R188) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
G200 (= G202) to V: in a breast cancer sample; somatic mutation
R236 (= R238) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
D237 (= D239) to N: in ARGINSA; severe; dbSNP:rs552951774
Q286 (= Q288) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
K288 (= K290) 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 (= R299) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
R306 (≠ H308) to W: in ARGINSA; severe; dbSNP:rs868834862
Q326 (= Q328) to L: in ARGINSA; severe
V335 (≠ T337) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
M360 (≠ T362) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
M382 (≠ L385) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
R385 (= R388) to L: in ARGINSA; severe
H388 (= H391) to Q: in ARGINSA; severe
A398 (≠ G401) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
R456 (≠ K459) to W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688

1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
43% identity, 95% coverage: 20:459/464 of query aligns to 1:439/447 of 1hy0A

query
sites
1hy0A

D

D

A

P

F

I

V

M

E

Q

E

M

F

L

T

S

A

T

S

S

I

I

Q

S

F

T

D

E

Q

Q

R

R

M

L

Y

S

K

E

Q

V

D

D

I

I

Q

Q

G

A

S

S

I

I

A

A

H

Y

A

A

R

K

M

A

L

L

Y

E

K

K

I

A

G

G

V

I

L

L

N

T

A

K

K

T

E

E

E

L

D

E

A

K

I

I

I

L

K

S

G

G

L

L

E

E

H

K

I

I

L

S

S

E

E

E

I

L

E

S

N

K

E

G

Q

V

M

I

H

V

W

V

S

T

I

Q

K

S

Q

D

E
|
E

D

D

I

I

H

Q

M

T

N

A

I

N

E

E

S

R

R

R

L

L

T

K

Q

E

M

L

I

I

G

G

V

D

T

I

G

A

K

G

K

K

L

L

H

H

T

T

G

G

R

R

S

S

R

R

N

N

D

E

Q

Q

V

V

A

V

T

T

D

D

I

L

R

K

L

L

Y

F

V

M

R

K

D

N

Q

S

I

L

D

S

L

I

I

I

Q

S

Q

T

D

H

L

L

H

L

R

Q

L

L

Q

I

Q

K

G

T

L

L

V

V

E

E

L

R

A

A

E

A

R

I

E

E

A

I

D

D

T

V

I

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

V

I

T

R

F

W

G

S

H

Q

H

F

M

L

L

L

A

S

W

H

Y

A

E

V

M

A

L

L

V

T

R

R

D

D

E

S

E

E

R

R

L

L

L

G

D

E

C

V

R

K

K

K

R

R

V

I

N

N

S

V

L

L

P

P

L

L

G

G

S

S

A

G

A

A

L

L

A

A

G

G

T

N

T

P

Y

L

P

D

I

I

D

D

R

R

E

E

Y

M

T

L

A

R

Q

S

L

E

L

L

G

E

F

F

E

A

R

S

I

I

C

S

Q

L

N

N

S

S

L

M

D

D

G

A

V

I

S

S

D

E

R

R

D

D

F

F

A

V

I

V

E

E

F

F

T

L

S

S

W

V

A

A

A

T

I

L

F

L

M

L

M

I

H

H

L

L

T

S

R

K

F

M

S

A

E

E

E

D

L

L

I

I

L

I

W

Y

S

S

S

T

A

S

Q

E

F

F

Q

G

F

F

I

L

D

T

L

L

P

S

D

D

R

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

V

S

P

L

E
|
E

L

L

V

I

R

R

G

S

K

K

S

S

G

G

R

R

V

V

Y

F

G

G

H

R

L

L

V

A

S

S

L

I

L

L

T

M

L

V

M

L

K

K

S

G

Q

L

P

P

L

S

A

T

Y

Y

N

N

K

K

D

D

N

L

Q

Q

E

E

D

D

K

K

E

E

P

A

L

V

F

I

D

D

T

V

I

V

D

D

T

T

V

L

R

T

G

A

C

V

L

L

R

Q

A

V

F

A

G

T

D

G

M

V

M

I

P

S

A

T

L

L

E

Q

V

I

K

S

R

K

D

E

N

N

T

M

Y

E

R

K

A

A

A

L

R

T

N

P

G

E

F

M

A

-

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

L

M

A

P

F

F

R

R

D

Q

A

A

H

H

E

T

A

A

V

S

G

G

L

K

A

A

V

V

A

H

H

L

G

A

V

E

K

T

T

K

Q

G

Q

I

D

A

L

I

A

N

D

N

M

L

S

T

L

L

A

E

T

D

L

L

Q

K

G

S

F

I

C

S

D

P

V

L

I

F

D

S

Q

S

D

D

V

V

F

S

E

Q

V

V

L

F

T

N

L

F

E

V

G

N

S

S

V

V

N

E

A

Q

R

Y

N

T

H

A

L

L

G

G

T

T

A

A

P

K

A

S

Q

S

V

V

R

T

H

T

Q

Q

V

I

A

E

Q

Q

A

L

K

R

active site: E69 (= E88), T142 (= T161), H143 (= H162), S264 (= S283), S265 (= S284), K270 (= K289), E277 (= E296)
binding sulfate ion: S264 (= S283), M267 (= M286), N272 (= N291)

P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
41% identity, 98% coverage: 8:463/464 of query aligns to 6:460/466 of P02521

query
sites
P02521

E

D

K

K

L

L

S

L

S

G

G

G

R

R

F

F

T

V

E

G

A

S

T

T

D

D

A

P

F

I

V

M

E

E

E

I

F

L

T

S

A

S

S

S

I

I

Q

S

F

T

D

E

Q

Q

R

R

M

L

Y

T

K

E

Q

V

D

D

I

I

Q

Q

G

A

S

S

I

M

A

A

H

Y

A

A

R

K

M

A

L

L

Y

E

K

K

I

A

G

S

V

I

L

L

N

T

A

K

K

T

E

E

E

L

D

E

A

K

I

I

I

L

K

S

G

G

L

L

E

E

H

K

I

I

L

S

S

E

E

E

I

S

E

S

N

K

E

G

Q

V

M

L

H

V

W

M

S

T

I

Q

K

S

Q

D

E

E

D

D

I

I

H

Q

M

T

N

A

I

I

E

E

S

R

R

R

L

L

T

K

Q

E

M

L

I

I

G

G

V

D

T

I

G

A

K

G

K

K

L

L

H

Q

T

T

G

G

R

R

S

S

R

R

N

N

D

E

Q

Q

V

V

A

V

T

T

D

D

I

L

R

K

L

L

Y

L

V

L

R

K

D

S

Q

S

I

I

D

S

L

V

I

I

Q

S

Q

T

D

H

L

L

H

L

R

Q

L

L

Q

I

Q

K

G

T

L

L

V

V

E

E

L

R

A

A

E

A

R

I

E

E

A

I

D

D

T

I

I

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

V

I

T

R

F

W

G

S

H

Q

H

F

M

L

L

L

A

S

W

H

Y

A

E

V

M

A

L

L

V

T

R

R

D

D

E

S

E

E

R

R

L

L

L

G

D

E

C

V

R

K

K

K

R

R

V

I

N

T

S

V

L

L

P

P

L

L

G

G

S

S

A

G

A

A

L

L

A

A

G

G

T

N

T

P

Y

L

P

E

I

I

D

D

R

R

E

E

Y

L

T

L

A

R

Q

S

L

E

L

L

G

D

F

M

E

T

R

S

I

I

C

T

Q

L

N

N

S

S

L

I

D

D

G

A

V

I

S

S

D

E

R

R

D

D

F

F

A

V

I

V

E

E

F

L

T

I

S

S

W

V

A

A

A

T

I

L

F

L

M

M

M

I

H

H

L

L

T

S

R

K

F

L

S

A

E

E

E

D

L

L

I

I

L

I

W

F

S

S

S

T

A

T

Q

E

F

F

Q

G

F

F

I

V

D

T

L

L

P

S

D

D

R

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

V

S

P

L

E

E

L

L

V

I

R

R

G

S

K

K

S

A

G

G

R

R

V

V

Y

F

G

G

H

R

L

L

V

A

S

A

L

I

L

L

T

M

L

V

M

L

K

K

S

G

Q

I

P

P

L

S

A

T

Y

F

N

S

K

K

D

D

N

L

Q

Q

E

E

D

D

K

K

E

E

P

A

L

V

F

L

D

D

T

V

I

V

D

D

T

T

V

L

R

T

G

A

C

V

L

L

R

Q

A

V

F

A

G

T

D

G

M

V

M

I

P

S

A

T

L

L

E

Q

V

V

K

N

R

K

D

E

N

N

T

M

Y

E

R

K

A

A

A

L

R

T

N

P

G

E

F

L

A

-

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

L

M

A

P

F

I

R

R

D

Q

A

A

H

Q

E

T

A

A

V

S

G

G

L

K

A

A

V

V

A

-

H

H

G

L

V

A

K

E

T

T

Q

K

Q

G

-

I

D

T

L

I

A

N

D

N

M

L

S

T

L

L

A

E

T

D

L

L

Q

K

G

S

F

I

C

S

D

P

V

L

I

F

D

A

Q

S

D

D

V

V

F

S

E

Q

V

V

L

F

T

S

L

V

E

V

G

N

S

S

V

V

N

E

A

Q

R

Y

N

T

H

A

L

V

G

G

T

T

A

A

P

K

A

S

Q

S

V

V

R

T

H

A

Q

Q

V

I

A

E

Q

Q

A

L

K

R

T

E

R

L

L

L

N

K

Sites not aligning to the query:

2 modified: Blocked amino end (Ala)

6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
40% identity, 94% coverage: 26:462/464 of query aligns to 8:448/454 of 6ienB

query
sites
6ienB

F

L

T

S

A

K

S

S

I

T

Q

H

F

F

D

D

Q

W

R

V

M

L

Y

A

K

P

Q

Y

D

D

I

L

Q

T

G

A

S

S

I

R

A

A

H

H

A

T

R

M

M

V

L

L

Y

F

K

R

I

A

G

G

V

L

L

L

N

T

A

E

K

E

E

Q

E

R

D

D

A

G

I

L

K

A

G

G

L

L

E

D

H

S

I

L

L

A

S

Q

E

D

I

V

E

A

N

D

E

G

Q

S

M

F

H

G

W

P

S

L

I

V

K

T

Q

D

E

E

D

D

I

V

H

H

M

A

N

A

I

L

E

E

S

R

R

G

L

L

T

I

Q

D

M

R

I

V

G

G

V

P

-

D

T

L

G

G

K

G

K

R

L

L

H

R

T

A

G

G

R

R

S
|
S

R
|
R

N
|
N

D

D

Q

Q

V

V

A

A

T

A

D

L

I

F

R

R

L

M

Y

W

V

L

R

R

D

D

Q

A

I

V

D

R

L

R

I

V

Q

A

Q

T

D

G

L

V

H

L

R

D

L

V

Q

V

Q

G

G

A

L

L

V

A

E

E

L

Q

A

A

E

A

R

A

E

H

A

P

D

S

T

A

I

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

V

I

T

L

F

L

G

A

H

H

M

L

L

L

A

A

W

H

Y

A

E

H

M

P

L

L

V

L

R

R

D

D

E

L

E

D

R

R

L

I

L

V

D

D

C

F

R

D

K

K

R

R

V

A

N

A

S

V

L

S

P

P

L

Y

G

G

S

S

A

G

A

A

L

L

A

A

G

G

T

S

Y

L

P

G

I

L

D

D

R

P

E

D

Y

A

T

I

A

A

Q

A

L

D

L

L

G

G

F

F

E

S

R

A

I

A

C

A

Q

D

N

N

S

S

L

V

D

D

G

A

V

T

S

A

D

A

R

R

D

D

F

F

A

A

I

A

E

E

F

A

T

A

S

F

W

V

A

F

A

A

I

M

F

I

M

A

M

V

H

D

L

L

T

S

R

R

F

L

S

A

E

E

E

D

L

I

I

I

L

V

W

W

S

S

A

T

Q

E

F

F

Q

G

F

Y

I

V

D

T

L

L

P

H

D

D

R

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

V

I

P

A

E

E

L

L

V

A

R

R

G

G

K

K

S

S

G

G

R

R

V

L

Y

I

G

G

H

N

L

L

V

A

S

G

L

L

T

A

L

T

M

L

K

K

S

A

Q

Q

P

P

L

L

A

A

Y
|
Y

N

N

K

R

D

D

N

L

Q
|
Q

E

E

D

D

K
|
K

E

E

P

P

L

V

F

F

D

D

T

S

I

V

D

A

T

Q

V

L

R

E

G

L

C

L

L

L

R

P

A

A

F

M

G

A

D

G

M

L

M

V

P

A

A

S

L

L

E

T

V

F

K

N

R

V

D

Q

N

R

T

M

Y

A

R

E

A

L

A

A

R

P

N

A

G

G

F

Y

A

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

L

V

A

P

F

F

R

R

D

S

A

A

H

H

E

E

A

A

V

A

G

G

L

A

A

A

V

V

A

R

H

A

G

A

V

E

K

Q

T

R

Q

G

Q

V

D

G

L

L

A

Q

D

E

M

L

S

T

L

D

A

D

T

E

L

L

Q

A

G

A

F

I

C

S

D

P

V

E

I

L

D

T

Q

P

D

Q

V

V

F

R

E

E

V

V

L

L

T

T

L

I

E

E

G

G

S

S

V

V

N

S

A

A

R

R

N

D

H

C

L

R

G

G

T

T

A

A

P

P

A

G

Q

R

V

V

R

A

H

E

Q

Q

-

L

-

N

-

A

V

I

A

G

Q

E

A

A

K

A

T

E

R

R

L

L

binding argininosuccinate: S97 (= S114), R98 (= R115), N99 (= N116), T144 (= T161), H145 (= H162), S266 (= S283), S267 (= S284), M269 (= M286), K272 (= K289), Y306 (= Y323), Q311 (= Q328), K314 (= K331)

6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
39% identity, 94% coverage: 26:462/464 of query aligns to 8:446/452 of 6ienA

query
sites
6ienA

F

L

T

S

A

K

S

S

I

T

Q

H

F

F

D

D

Q

W

R

V

M

L

Y

A

K

P

Q

Y

D

D

I

L

Q

T

G

A

S

S

I

R

A

A

H

H

A

T

R

M

M

V

L

L

Y

F

K

R

I

A

G

G

V

L

L

L

N

T

A

E

K

E

E

Q

E

R

D

D

A

G

I

L

K

A

G

G

L

L

E

D

H

S

I

L

L

A

S

Q

E

D

I

V

E

A

N

D

E

G

Q

S

M

F

H

G

W

P

S

L

I

V

K

T

Q

D

E

E

D

D

I

V

H

H

M

A

N

A

I

L

E

E

S

R

R

G

L

L

T

I

Q

D

M

R

I

V

G

G

V

P

-

D

T

L

G

G

K

G

K

R

L

L

H

R

T

A

G

G

R

R

S

S

R
|
R

N
|
N

D

D

Q

Q

V
|
V

A

A

T

A

D

L

I

F

R

R

L

M

Y

W

V

L

R

R

D

D

Q

A

I

V

D

R

L

R

I

V

Q

A

Q

T

D

G

L

V

H

L

R

D

L

V

Q

V

Q

G

G

A

L

L

V

A

E

E

L

Q

A

A

E

A

R

A

E

H

A

P

D

S

T

A

I

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

V

I

T

L

F

L

G

A

H

H

M

L

L

L

A

A

W

H

Y

A

E

H

M

P

L

L

V

L

R

R

D

D

E

L

E

D

R

R

L

I

L

V

D

D

C

F

R

D

K

K

R

R

V

A

N

A

S

V

L

S

P

P

L

Y

G

G

S

S

A

G

A

A

L

L

A

A

G

G

T

S

Y

L

P

G

I

L

D

D

R

P

E

D

Y

A

T

I

A

A

Q

A

L

D

L

L

G

G

F

F

E

S

R

A

I

A

C

A

Q

D

N

N

S

S

L

V

D

D

G

A

V

T

S

A

D

A

R

R

D

D

F

F

A

A

I

A

E

E

F

A

T

A

S

F

W

V

A

F

A

A

I

M

F

I

M

A

M

V

H

D

L

L

T

S

R

R

F

L

S

A

E

E

E

D

L

I

I

I

L

V

W

W

S

S

A

T

Q

E

F

F

Q

G

F

Y

I

V

D

T

L

L

P

H

D

D

R

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

V

I

P

A

E

E

L

L

V

A

R

R

G

G

K

K

S

S

G

G

R

R

V

L

Y

I

G

G

H

N

L

L

V

A

S

G

L

L

T

A

L

T

M

L

K

K

S

A

Q

Q

P

P

L

L

A

A

Y
|
Y

N

N

K

R

D

D

N

L

Q
|
Q

E

E

D

D

K
|
K

E

E

P

P

L

V

F

F

D

D

T

S

I

V

D

A

T

Q

V

L

R

E

G

L

C

L

L

L

R

P

A

A

F

M

G

A

D

G

M

L

M

V

P

A

A

S

L

L

E

T

V

F

K

N

R

V

D

Q

N

R

T

M

Y

A

R

E

A

L

A

A

R

P

N

A

G

G

F

Y

A

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

L

V

A

P

F

F

R

R

D

S

A

A

H

H

E

E

A

A

V

A

G

G

L

A

A

A

V

V

A

R

H

A

G

A

V

E

K

Q

T

R

Q

G

Q

V

D

G

L

L

A

Q

D

E

M

L

S

T

L

D

A

D

T

E

L

L

Q

A

G

A

F

I

C

S

D

P

V

E

I

L

D

T

Q

P

D

Q

V

V

F

R

E

E

V

V

L

L

T

T

L

I

E

E

G

G

S

S

V

V

N

S

A

A

R

R

N

D

H

C

L

R

G

G

T

T

A

A

P

P

A

G

Q

R

V

V

R

A

H

E

Q

Q

-

L

-

N

-

A

V

I

A

G

Q

E

A

A

K

A

T

E

R

R

L

L

binding argininosuccinate: R98 (= R115), N99 (= N116), V102 (= V119), T144 (= T161), H145 (= H162), Y304 (= Y323), Q309 (= Q328), K312 (= K331)
binding fumaric acid: S266 (= S283), S267 (= S284), K270 (= K289), N272 (= N291)

6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
38% identity, 94% coverage: 26:462/464 of query aligns to 8:412/418 of 6ienC

query
sites
6ienC

F

L

T

S

A

K

S

S

I

T

Q

H

F

F

D

D

Q

W

R

V

M

L

Y

A

K

P

Q

Y

D

D

I

L

Q

T

G

A

S

S

I

R

A

A

H

H

A

T

R

M

M

V

L

L

Y

F

K

R

I

A

G

G

V

L

L

L

N

T

A

E

K

E

E

Q

E

R

D

D

A

G

I

L

K

A

G

G

L

L

E

D

H

S

I

L

L

A

S

Q

E

D

I

V

E

A

N

D

E

G

Q

S

M

F

H

G

W

P

S

L

I

V

K

T

Q

D

E

E

D

D

I

V

H

H

M

A

N

A

I

L

E

E

S

R

R

G

L

L

T

I

Q

D

M

R

I

V

G

G

V

P

-

D

T

L

G

G

K

G

K

R

L

L

H

R

T

A

G

G

R

R

S
|
S

R
|
R

N
|
N

D

D

Q

Q

V
|
V

A

A

T

A

D

L

I

F

R

R

L

M

Y

W

V

L

R

R

D

D

Q

A

I

V

D

R

L

R

I

V

Q

A

Q

T

D

G

L

V

H

L

R

D

L

V

Q

V

Q

G

G

A

L

L

V

A

E

E

L

Q

A

A

E

A

R

A

E

H

A

P

D

S

T

A

I

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

V

I

T

L

F

L

G

A

H

H

M

L

L

L

A

A

W

H

Y

A

E

H

M

P

L

L

V

L

R

R

D

D

E

L

E

D

R

R

L

I

L

V

D

D

C

F

R

D

K

K

R

R

V

A

N

A

S

V

L

S

P

P

L

Y

G

G

S

S

A

G

A

A

L

L

A

A

G

G

T

S

Y

L

P

G

I

L

D

D

R

P

E

D

Y

A

T

I

A

A

Q

A

L

D

L

L

G

G

F

F

E

S

R

A

I

A

C

A

Q

D

N

N

S

S

L

V

D

D

G

A

V

T

S

A

D

A

R

R

D

D

F

F

A

A

I

A

E

E

F

A

T

A

S

F

W

V

A

F

A

A

I

M

F

I

M

A

M

V

H

D

L

L

T

S

R

R

F

L

S

A

E

E

E

D

L

I

I

I

L

V

W

W

S

S

A

T

Q

E

F

F

Q

G

F

Y

I

V

D

T

L

L

P

H

D

D

R

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

V

I

P

A

E

E

L

L

V

A

R

R

G

G

K

K

S

S

G

G

R

R

V

L

Y

I

G

G

H

N

L

L

V

A

S

G

L

L

T

A

L

T

M

L

K

K

S

A

Q

Q

P

P

L

L

A

A

Y
|
Y

N

N

K

R

D

D

N

L

Q
|
Q

E

E

D

D

K
|
K

E

E

P

P

L

V

F

F

D

D

T

S

I

V

D

A

T

Q

V

L

R

E

G

L

C

L

L

L

R

P

A

A

F

M

G

A

D

G

M

L

M

V

P

A

A

S

L

L

E

T

V

F

K

N

R

V

D

Q

N

R

T

M

Y

A

R

E

A

L

A

A

R

P

N

A

G

G

F

Y

A

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

L

V

A

P

F

F

R

R

D

S

A

A

H

H

E

R

A

-

V

-

G

-

L

-

A

-

V

-

A

-

H

-

G

-

V

-

K

-

T

-

Q

-

D

-

L

-

A

-

D

-

M

-

S

-

L

-

A

-

T

-

L

-

Q

-

G

-

F

-

C

-

D

-

V

-

I

-

D

-

Q

-

D

-

V

-

F

-

E

E

V

V

L

L

T

T

L

I

E

E

G

G

S

S

V

V

N

S

A

A

R

R

N

D

H

C

L

R

G

G

T

T

A

A

P

P

A

G

Q

R

V

V

R

A

H

E

Q

Q

-

L

-

N

-

A

V

I

A

G

Q

E

A

A

K

A

T

E

R

R

L

L

binding arginine: R98 (= R115), N99 (= N116), V102 (= V119), Y306 (= Y323), Q311 (= Q328), K314 (= K331)
binding argininosuccinate: T144 (= T161), H145 (= H162), S266 (= S283), S267 (= S284), M269 (= M286), K272 (= K289)
binding fumaric acid: S97 (= S114), R98 (= R115), N99 (= N116)

6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
31% identity, 97% coverage: 14:463/464 of query aligns to 6:462/496 of 6g3iA

query
sites
6g3iA

R

R

F

I

T

G

E

R

A

A

T

T

D

G

A

A

F

K

V

A

E

P

E

E

F

F

-

Q

-

E

-

L

-
x
Y

-

D

-

F

-

D

T

A

A

A

S

A

I

L

Q

T

F

L

D

T

Q

S

R

A

M

V

Y

F

K

P

Q

Y

D

D

I

S

Q

Q

G

I

S

H

I

R

A

A

H

H

A

V

R

V

M

M

L

L

Y

T

K

E

I

Q

G

G

V

I

L

L

N

T

A

V

K

E

E

E

E

S

D

A

A

T

I

I

I

L

K

S

G

G

L

L

E

A

H

Q

I

V

L

-

S

-

E

-

I

-

E

-

N

-

E

D

Q

E

M

L

H

A

W

A

S

T

I

D

K

G

Q

S

E

L

D

R

I

T

H

Y

M

L

N

P

I

Y

E

E

S

A

R

A

L

L

T

K

Q

R

M

T

I

I

G

G

V

S

T

V

G

A

K

G

K

K

L

M

H

H

T

I

G

G

R

R

S

S

R

R

N

N

D

D

Q

L

V

A

A

N

T

A

D

G

I

K

R

R

L

M

Y

F

V

L

R

R

D

D

Q

Q

I

L

D

L

L

R

I

T

Q

I

Q

E

D

A

L

V

H

I

R

G

L

Y

Q

R

Q

E

G

A

L

V

V

V

E

H

L

K

A

A

E

A

R

D

E

H

A

L

D

D

T

T

I

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

V

I

T

T

F

L

G

G

H

H

H

Y

M

L

L

M

A

A

W

I

Y

S

E

E

M

N

L

L

V

A

R

K

D

N

E

L

E

D

R

R

L

Y

L

R

D

E

C

L

R

Y

K

A

R

R

V

I

N

N

S

L

L

C

P

P

L

L

G

G

S

A

A

A

L

T

A

A

G

G

T

T

T

G

Y

W

P

P

I

L

D

N

R

R

E

D

Y

R

T

T

A

S

Q

A

L

L

G

G

F

F

E

D

R

G

I

L

C

V

Q

V

N

N

S

S

L

I

D

E

G

G

V

V

S

A

D

G

R

W

D

D

F

H

A

V

I

A

E

E

F

H

T

A

S

F

W

V

A

N

A

A

I

V

F

F

M

L

M

S

H

G

L

L

T

S

R

R

F

L

S

A

E

S

E

E

L

I

I

Q

L

L

W

W

S

S

S

T

A

D

Q

E

F

Y

Q

Q

F

V

I

A

D

E

L

L

P

D

D

A

R

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

V

S

P

L

E

E

L
x
R

V

S

R

R

G

K

K

A

S

A

G

F

R

A

V

A

Y

M

G

G

H

P

L

L

V

V

S

G

L

I

L

L

T

T

L

S

M

L

K

N

S

A

Q

I

P

E

L

Y

A

Q

Y

Y

N

S

K

A

D

A

N

R

Q

V

E

E

D

-

K

L

E

E

P

P

L

-

F

-

D

R

T

S

I

I

D

D

T

A

V

L

R

I

G

A

C

A

L

T

R

H

A

A

F

M

G

T

D

G

M

V

P

R

A

T

L

L

E

H

V

P

K

N

R

K

D

E

N

R

T

M

Y

R

R

Q

A

Y

A

A

R

A

N

E

G

N

F

Y

A

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

L

I

A

D

F

Y

R

R

D

E

A

A

H

H

E

E

A

I

V

V

G

A

-

H

-

V

-

I

L

T

A

A

V

I

A

E

H

K

G

G

V

I

K

K

T

A

Q

N

Q

K

-

I

-

G

-

L

D

D

L

L

A

V

-

Q

D

E

M

A

S

A

L

V

A

A

T

Q

L

T

Q

G

G

A

F

G

C

I

D

N

V

V

I

S

D

A

Q

D

D

D

V

I

F

K

E

D

V

A

L

L

T

D

L

P

E

W

G

Q

S

N

V

V

N

L

A

R

R

R

N

E

H

G

L

K

G

G

G

M

T

P

A

A

P

P

A

M

Q

S

V

V

R

K

H

A

Q

S

V

I

A

D

Q

D

A

A

K

M

T

A

R

E

L

L

N

H

binding (2~{S})-2-(2-azanylethylamino)butanedioic acid: S276 (= S283), S277 (= S284), M279 (= M286), K282 (= K289), N284 (= N291), D286 (= D293)
binding fumaric acid: Y22 (vs. gap), R290 (≠ L297)

6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
31% identity, 97% coverage: 14:463/464 of query aligns to 6:462/497 of 6g3hA

query
sites
6g3hA

R

R

F

I

T

G

E

R

A

A

T

T

D

G

A

A

F

K

V

A

E

P

E

E

F

F

-

Q

-

E

-

L

-
x
Y

-

D

-

F

-

D

T

A

A

A

S

A

I

L

Q

T

F

L

D

T

Q

S

R

A

M

V

Y

F

K

P

Q

Y

D

D

I

S

Q

Q

G

I

S

H

I

R

A

A

H

H

A

V

R

V

M

M

L

L

Y

T

K

E

I

Q

G

G

V

I

L

L

N

T

A

V

K

E

E

E

E

S

D

A

A

T

I

I

I

L

K

S

G

G

L

L

E

A

H

Q

I

V

L

-

S

-

E

-

I

-

E

-

N

-

E

D

Q

E

M

L

H

A

W

A

S

T

I

D

K

G

Q

S

E

L

D

R

I

T

H

Y

M

L

N

P

I

Y

E

E

S

A

R

A

L

L

T

K

Q

R

M

T

I

I

G

G

V

S

T

V

G

A

K

G

K

K

L

M

H

H

T

I

G

G

R

R

S

S

R

R

N

N

D

D

Q

L

V

A

A

N

T

A

D

G

I

K

R

R

L

M

Y

F

V

L

R

R

D

D

Q

Q

I

L

D

L

L

R

I

T

Q

I

Q

E

D

A

L

V

H

I

R

G

L

Y

Q

R

Q

E

G

A

L

V

V

V

E

H

L

K

A

A

E

A

R

D

E

H

A

L

D

D

T

T

I

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

V

I

T

T

F

L

G

G

H

H

H

Y

M

L

L

M

A

A

W

I

Y

S

E

E

M

N

L

L

V

A

R

K

D

N

E

L

E

D

R

R

L

Y

L

R

D

E

C

L

R

Y

K

A

R

R

V

I

N

N

S

L

L

C

P

P

L

L

G

G

S

A

A

A

L

T

A

A

G

G

T

T

T

G

Y

W

P

P

I

L

D

N

R

R

E

D

Y

R

T

T

A

S

Q

A

L

L

G

G

F

F

E

D

R

G

I

L

C

V

Q

V

N

N

S

S

L

I

D

E

G

G

V

V

S

A

D

G

R

W

D

D

F

H

A

V

I

A

E

E

F

H

T

A

S

F

W

V

A

N

A

A

I

V

F

F

M

L

M

S

H

G

L

L

T

S

R

R

F

L

S

A

E

S

E

E

L

I

I

Q

L

L

W

W

S

S

S

T

A

D

Q

E

F

Y

Q

Q

F

V

I

A

D

E

L

L

P

D

D

A

R

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

V

S

P

L

E

E

L
x
R

V

S

R

R

G

K

K

A

S

A

G

F

R

A

V

A

Y

M

G

G

H

P

L

L

V

V

S

G

L

I

L

L

T

T

L

S

M

L

K

N

S

A

Q

I

P

E

L

Y

A

Q

Y

Y

N

S

K

A

D

A

N

R

Q

V

E

E

D

-

K

L

E

E

P

P

L

-

F

-

D

R

T

S

I

I

D

D

T

A

V

L

R

I

G

A

C

A

L

T

R

H

A

A

F

M

G

T

D

G

M

V

P

R

A

T

L

L

E

H

V

P

K

N

R

K

D

E

N

R

T

M

Y

R

R

Q

A

Y

A

A

R

A

N

E

G

N

F

Y

A

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

L

I

A

D

F

Y

R

R

D

E

A

A

H

H

E

E

A

I

V

V

G

A

-

H

-

V

-

I

L

T

A

A

V

I

A

E

H

K

G

G

V

I

K

K

T

A

Q

N

Q

K

-

I

-

G

-

L

D

D

L

L

A

V

-

Q

D

E

M

A

S

A

L

V

A

A

T

Q

L

T

Q

G

G

A

F

G

C

I

D

N

V

V

I

S

D

A

Q

D

D

D

V

I

F

K

E

D

V

A

L

L

T

D

L

P

E

W

G

Q

S

N

V

V

N

L

A

R

R

R

N

E

H

G

L

K

G

G

G

M

T

P

A

A

P

P

A

M

Q

S

V

V

R

K

H

A

Q

S

V

I

A

D

Q

D

A

A

K

M

T

A

R

E

L

L

N

H

binding (2~{S})-2-[2-[[(2~{S})-1,4-bis(oxidanyl)-1,4-bis(oxidanylidene)butan-2-yl]amino]ethylamino]butanedioic acid: Y22 (vs. gap), S276 (= S283), S277 (= S284), M279 (= M286), K282 (= K289), N284 (= N291), D286 (= D293), R290 (≠ L297)

6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
31% identity, 97% coverage: 14:463/464 of query aligns to 6:462/497 of 6g3gA

query
sites
6g3gA

R

R

F

I

T

G

E

R

A

A

T

T

D

G

A

A

F

K

V

A

E

P

E

E

F

F

-

Q

-

E

-

L

-

Y

-

D

-

F

-

D

T

A

A

A

S

A

I

L

Q

T

F

L

D

T

Q

S

R

A

M

V

Y

F

K

P

Q

Y

D

D

I

S

Q

Q

G

I

S

H

I

R

A

A

H

H

A

V

R

V

M

M

L

L

Y

T

K

E

I

Q

G

G

V

I

L

L

N

T

A

V

K

E

E

E

E

S

D

A

A

T

I

I

I

L

K

S

G

G

L

L

E

A

H

Q

I

V

L

-

S

-

E

-

I

-

E

-

N

-

E

D

Q

E

M

L

H

A

W

A

S

T

I

D

K

G

Q

S

E

L

D

R

I

T

H

Y

M

L

N

P

I

Y

E

E

S

A

R

A

L

L

T

K

Q

R

M

T

I

I

G

G

V

S

T

V

G

A

K

G

K

K

L

M

H

H

T

I

G

G

R

R

S

S

R

R

N

N

D

D

Q

L

V

A

A

N

T

A

D

G

I

K

R

R

L

M

Y

F

V

L

R

R

D

D

Q

Q

I

L

D

L

L

R

I

T

Q

I

Q

E

D

A

L

V

H

I

R

G

L

Y

Q

R

Q

E

G

A

L

V

V

V

E

H

L

K

A

A

E

A

R

D

E

H

A

L

D

D

T

T

I

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

V

I

T

T

F

L

G

G

H

H

H

Y

M

L

L

M

A

A

W

I

Y

S

E

E

M

N

L

L

V

A

R

K

D

N

E

L

E

D

R

R

L

Y

L

R

D

E

C

L

R

Y

K

A

R

R

V

I

N

N

S

L

L

C

P

P

L

L

G

G

S

A

A

A

L

T

A

A

G

G

T

T

T

G

Y

W

P

P

I

L

D

N

R

R

E

D

Y

R

T

T

A

S

Q

A

L

L

G

G

F

F

E

D

R

G

I

L

C

V

Q

V

N

N

S

S

L

I

D

E

G

G

V

V

S

A

D

G

R

W

D

D

F

H

A

V

I

A

E

E

F

H

T

A

S

F

W

V

A

N

A

A

I

V

F

F

M

L

M

S

H

G

L

L

T

S

R

R

F

L

S

A

E

S

E

E

L

I

I

Q

L

L

W

W

S

S

S

T

A

D

Q

E

F

Y

Q

Q

F

V

I

A

D

E

L

L

P

D

D

A

R

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

V

S

P

L

E

E

L

R

V

S

R

R

G

K

K

A

S

A

G

F

R

A

V

A

Y

M

G

G

H

P

L

L

V

V

S

G

L

I

L

L

T

T

L

S

M

L

K

N

S

A

Q

I

P

E

L

Y

A

Q

Y

Y

N

S

K

A

D

A

N

R

Q

V

E

E

D

-

K

L

E

E

P

P

L

-

F

-

D

R

T

S

I

I

D

D

T

A

V

L

R

I

G

A

C

A

L

T

R

H

A

A

F

M

G

T

D

G

M

V

P

R

A

T

L

L

E

H

V

P

K

N

R

K

D

E

N

R

T

M

Y

R

R

Q

A

Y

A

A

R

A

N

E

G

N

F

Y

A

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

L

I

A

D

F

Y

R

R

D

E

A

A

H

H

E

E

A

I

V

V

G

A

-

H

-

V

-

I

L

T

A

A

V

I

A

E

H

K

G

G

V

I

K

K

T

A

Q

N

Q

K

-

I

-

G

-

L

D

D

L

L

A

V

-

Q

D

E

M

A

S

A

L

V

A

A

T

Q

L

T

Q

G

G

A

F

G

C

I

D

N

V

V

I

S

D

A

Q

D

D

D

V

I

F

K

E

D

V

A

L

L

T

D

L

P

E

W

G

Q

S

N

V

V

N

L

A

R

R

R

N

E

H

G

L

K

G

G

G

M

T

P

A

A

P

P

A

M

Q

S

V

V

R

K

H

A

Q

S

V

I

A

D

Q

D

A

A

K

M

T

A

R

E

L

L

N

H

binding succinic acid: S276 (= S283), S277 (= S284), M279 (= M286), K282 (= K289), N284 (= N291)

6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
31% identity, 97% coverage: 14:463/464 of query aligns to 6:462/497 of 6g3fA

query
sites
6g3fA

R

R

F

I

T

G

E

R

A

A

T

T

D

G

A

A

F

K

V

A

E

P

E

E

F

F

-

Q

-

E

-

L

-

Y

-

D

-

F

-

D

T

A

A

A

S

A

I

L

Q

T

F

L

D

T

Q

S

R

A

M

V

Y

F

K

P

Q

Y

D

D

I

S

Q

Q

G

I

S

H

I

R

A

A

H

H

A

V

R

V

M

M

L

L

Y

T

K

E

I

Q

G

G

V

I

L

L

N

T

A

V

K

E

E

E

E

S

D

A

A

T

I

I

I

L

K

S

G

G

L

L

E

A

H

Q

I

V

L

-

S

-

E

-

I

-

E

-

N

-

E

D

Q

E

M

L

H

A

W

A

S

T

I

D

K

G

Q

S

E

L

D

R

I

T

H

Y

M

L

N

P

I

Y

E

E

S

A

R

A

L

L

T

K

Q

R

M

T

I

I

G

G

V

S

T

V

G

A

K

G

K

K

L

M

H

H

T

I

G

G

R

R

S

S

R

R

N

N

D

D

Q

L

V

A

A

N

T

A

D

G

I

K

R

R

L

M

Y

F

V

L

R

R

D

D

Q

Q

I

L

D

L

L

R

I

T

Q

I

Q

E

D

A

L

V

H

I

R

G

L

Y

Q

R

Q

E

G

A

L

V

V

V

E

H

L

K

A

A

E

A

R

D

E

H

A

L

D

D

T

T

I

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

V

I

T

T

F

L

G

G

H

H

H

Y

M

L

L

M

A

A

W

I

Y

S

E

E

M

N

L

L

V

A

R

K

D

N

E

L

E

D

R

R

L

Y

L

R

D

E

C

L

R

Y

K

A

R

R

V

I

N

N

S

L

L

C

P

P

L

L

G

G

S

A

A

A

L

T

A

A

G

G

T

T

T

G

Y

W

P

P

I

L

D

N

R

R

E

D

Y

R

T

T

A

S

Q

A

L

L

G

G

F

F

E

D

R

G

I

L

C

V

Q

V

N

N

S

S

L

I

D

E

G

G

V

V

S

A

D

G

R

W

D

D

F

H

A

V

I

A

E

E

F

H

T

A

S

F

W

V

A

N

A

A

I

V

F

F

M

L

M

S

H

G

L

L

T

S

R

R

F

L

S

A

E

S

E

E

L

I

I

Q

L

L

W

W

S

S

S

T

A

D

Q

E

F

Y

Q

Q

F

V

I

A

D

E

L

L

P

D

D

A

R

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

V

S

P

L

E

E

L

R

V

S

R

R

G

K

K

A

S

A

G

F

R

A

V

A

Y

M

G

G

H

P

L

L

V

V

S

G

L

I

L

L

T

T

L

S

M

L

K

N

S

A

Q

I

P

E

L

Y

A

Q

Y

Y

N

S

K

A

D

A

N

R

Q

V

E

E

D

-

K

L

E

E

P

P

L

-

F

-

D

R

T

S

I

I

D

D

T

A

V

L

R

I

G

A

C

A

L

T

R

H

A

A

F

M

G

T

D

G

M

V

P

R

A

T

L

L

E

H

V

P

K

N

R

K

D

E

N

R

T

M

Y

R

R

Q

A

Y

A

A

R

A

N

E

G

N

F

Y

A

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

L

I

A

D

F

Y

R

R

D

E

A

A

H

H

E

E

A

I

V

V

G

A

-

H

-

V

-

I

L

T

A

A

V

I

A

E

H

K

G

G

V

I

K

K

T

A

Q

N

Q

K

-

I

-

G

-

L

D

D

L

L

A

V

-

Q

D

E

M

A

S

A

L

V

A

A

T

Q

L

T

Q

G

G

A

F

G

C

I

D

N

V

V

I

S

D

A

Q

D

D

D

V

I

F

K

E

D

V

A

L

L

T

D

L

P

E

W

G

Q

S

N

V

V

N

L

A

R

R

R

N

E

H

G

L

K

G

G

G

M

T

P

A

A

P

P

A

M

Q

S

V

V

R

K

H

A

Q

S

V

I

A

D

Q

D

A

A

K

M

T

A

R

E

L

L

N

H

binding fumaric acid: S276 (= S283), S277 (= S284), M279 (= M286), K282 (= K289), N284 (= N291)

3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
27% identity, 58% coverage: 41:308/464 of query aligns to 49:340/463 of 3r6vG

query
sites
3r6vG

I

V

Q

K

G

K

S

S

I

A

A

A

H

L

A

A

R

N

M

M

L

-

Y

-

K

E

I

V

G

G

V

L

L

L

N

D

A

K

K

E

E

V

E

G

D

Q

A

Y

I

I

I

V

K

K

G

A

L

A

E

D

H

E

I

V

L

I

S

E

E

G

I

K

E

W

N

N

E

D

Q

Q

M

F

H

I

W

V

S

D

I

P

K

I

Q

Q

-

G

-

A

-

G

E

T

D

S

I

I

H

N

M

M

N

N

-

A

-

N

-

E

-

V

I

I

E

A

S

N

R

R

L

A

T

L

Q

E

M

L

I

M

G

G

-

E

-

K

-

G

-

N

-

Y

-

S

-

K

-

I

V

S

T

P

G

N

K

S

K

H

L

V

H

N

T

M

G

S

R

Q

S

S

R

T

N

N

D

D

Q

A

V

F

A

P

T

T

D

A

I

T

R

H

L

I

Y

A

V

V

R

L

D

S

Q

L

I

L

D

N

L

Q

I

L

Q

I

Q

E

D

T

L

T

H

K

R

Y

L

M

Q

Q

G

E

L

F

V

M

E

K

L

K

A

A

E

D

R

E

E

F

A

A

D

G

T

V

I

I

M

K

P

M

G

G

F

R

T

T

H
|
H

L

L

Q

Q

T

D

A

A

Q

V

P

P

V

I

T

L

F

L

G

G

H

Q

H

E

M

F

L

E

A

A

W

Y

Y

A

E

R

M

V

L

I

V

A

R

R

D

D

E

I

E

E

R

R

L

I

L

A

D

N

C

T

R

R

K

N

R

N

V

L

N

Y

S

D

L

I

P

N

L

M

G

G

S

A

A

T

A

A

L

V

A

-

G

G

T

T

T

G

Y

L

P

N

I

A

D

D

R

P

E

E

Y

Y

-

I

-

S

-

I

-

V

T

T

A

E

Q

H

L

L

L

A

G

K

F

F

E

S

-

G

-

H

-

P

-

L

R

R

I

S

C

A

Q

Q

N

H

S

L

L

V

D

D

G

A

V

T

S

Q

D

N

R

T

D

D

F

C

A

Y

I

T

E

E

F

V

T

S

S

S

W

A

A

L

A

K

I

V

F

C

M

M

M

I

H

N

L

M

T

S

R

K

F

I

S

A

E

N

E

D

L

L

I

R

L

L

W

M

S

A

S

S

-

G

-

P

-

R

A

A

Q

G

F

L

Q

S

F

E

I

I

D

V

L

L

P

P

D

A

R

R

F

-

C

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

V

M

P

P

E
|
E

L

V

V

M

R

N

G

Q

K

V

S

A

G

F

R

Q

V

V

Y

F

G

G

H

N

active site: H185 (= H162), S315 (= S283), K321 (= K289), E328 (= E296)
binding aspartic acid: G314 (= G282), S315 (= S283), S316 (= S284)

Q9LCC6 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Bacillus sp. (see 3 papers)
27% identity, 58% coverage: 41:308/464 of query aligns to 52:343/468 of Q9LCC6

query
sites
Q9LCC6

I

V

Q

K

G

K

S

S

I

A

A

A

H

L

A

A

R

N

M

M

L

-

Y

-

K

E

I

V

G

G

V

L

L

L

N

D

A

K

K

E

E

V

E

G

D

Q

A

Y

I

I

I

V

K

K

G

A

L

A

E

D

H

E

I

V

L

I

S

E

E

G

I

K

E

W

N

N

E

D

Q

Q

M

F

H

I

W

V

S

D

I

P

K

I

Q

Q

-

G

-

A

-

G

E
x
T

D

S

I

I

H

N

M

M

N

N

-

A

-

N

-

E

-

V

I

I

E

A

S

N

R

R

L

A

T

L

Q

E

M

L

I

M

G

G

-

E

-

K

-

G

-

N

-

Y

-

S

-

K

-

I

V

S

T

P

G

N

K

S

K
x
H

L

V

H

N

T

M

G

S

R

Q

S
|
S

R
x
T

N
|
N

D

D

Q

A

V

F

A

P

T

T

D

A

I

T

R

H

L

I

Y

A

V

V

R

L

D

S

Q

L

I

L

D

N

L

Q

I

L

Q

I

Q

E

D

T

L

T

H

K

R

Y

L

M

Q

Q

G

E

L

F

V

M

E

K

L

K

A

A

E

D

R

E

E

F

A

A

D

G

T

V

I

I

M
x
K

P

M

G

G

F

R

T
|
T

H
|
H

L

L

Q

Q

T

D

A

A

Q

V

P

P

V

I

T

L

F

L

G

G

H

Q

H

E

M

F

L

E

A

A

W

Y

Y

A

E

R

M

V

L

I

V

A

R

R

D

D

E

I

E

E

R

R

L

I

L

A

D

N

C

T

R

R

K

N

R

N

V

L

N

Y

S

D

L

I

P

N

L

M

G

G

S

A

A

T

A

A

L

V

A

-

G

G

T

T

T

G

Y

L

P

N

I

A

D

D

R

P

E

E

Y

Y

-

I

-

S

-

I

-

V

T

T

A

E

Q

H

L

L

L

A

G

K

F

F

E

S

-

G

-

H

-

P

-

L

R

R

I

S

C

A

Q

Q

N

H

S

L

L

V

D

D

G

A

V

T

S

Q

D

N

R

T

D

D

F

C

A

Y

I

T

E

E

F

V

T

S

S

S

W

A

A

L

A

K

I

V

F

C

M

M

M

I

H

N

L

M

T

S

R

K

F

I

S

A

E

N

E

D

L

L

I

R

L

L

W

M

S

A

S

S

-

G

-

P

-

R

A

A

Q

G

F

L

Q

S

F

E

I

I

D

V

L

L

P

P

D

A

R

R

F

-

C

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

V

M

P

P

E

E

L

V

V

M

R

N

G

Q

K

V

S

A

G

F

R

Q

V

V

Y

F

G

G

H

N

T101 (≠ E88) binding L-aspartate; mutation to A: 7100-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to S: 80-fold decrease in catalytic efficiency.
H134 (≠ K108) mutation to A: Retains full activity. Shows a slightly stronger affinity for L-aspartate. Does not affect tertiary structure.
S140 (= S114) binding L-aspartate; mutation to A: 27-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation S->K,R: Loss of activity.
T141 (≠ R115) binding L-aspartate; mutation to A: 15-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to K: 40000-fold decrease in catalytic efficiency.; mutation T->V,R: Loss of activity.
N142 (= N116) binding L-aspartate; mutation to A: Loss of activity. Does not result in any major conformational changes.; mutation to Q: 3000-fold decrease in catalytic efficiency.
K183 (≠ M157) mutation to A: Loss of activity. Does not affect tertiary structure.
T187 (= T161) 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 (= H162) 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 (= S283) mutation to A: Loss of activity.
S319 (= S284) binding L-aspartate; mutation to A: Almost no change in catalytic efficiency.
I320 (= I285) mutation to A: 50-fold decrease in catalytic efficiency.
M321 (= M286) mutation to A: 338-fold decrease in catalytic efficiency.
P322 (= P287) mutation to A: Almost no change in catalytic efficiency.
K324 (= K289) 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 (= N291) 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.

3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
27% identity, 58% coverage: 41:308/464 of query aligns to 48:339/462 of 3r6qA

query
sites
3r6qA

I

V

Q

K

G

K

S

S

I

A

A

A

H

L

A

A

R

N

M

M

L

-

Y

-

K

E

I

V

G

G

V

L

L

L

N

D

A

K

K

E

E

V

E

G

D

Q

A

Y

I

I

I

V

K

K

G

A

L

A

E

D

H

E

I

V

L

I

S

E

E

G

I

K

E

W

N

N

E

D

Q

Q

M

F

H

I

W

V

S

D

I

P

K

I

Q

Q

-

G

-

A

-

G

E

T

D

S

I

I

H

N

M

M

N

N

-

A

-

N

-

E

-

V

I

I

E

A

S

N

R

R

L

A

T

L

Q

E

M

L

I

M

G

G

-

E

-

K

-

G

-

N

-

Y

-

S

-

K

-

I

V

S

T

P

G

N

K

S

K

H

L

V

H

N

T

M

G

S

R

Q

S

S

R

T

N

N

D

D

Q

A

V

F

A

P

T

T

D

A

I

T

R

H

L

I

Y

A

V

V

R

L

D

S

Q

L

I

L

D

N

L

Q

I

L

Q

I

Q

E

D

T

L

T

H

K

R

Y

L

M

Q

Q

G

E

L

F

V

M

E

K

L

K

A

A

E

D

R

E

E

F

A

A

D

G

T

V

I

I

M

K

P

M

G

G

F

R

T

T

H
|
H

L

L

Q

Q

T

D

A

A

Q

V

P

P

V

I

T

L

F

L

G

G

H

Q

H

E

M

F

L

E

A

A

W

Y

Y

A

E

R

M

V

L

I

V

A

R

R

D

D

E

I

E

E

R

R

L

I

L

A

D

N

C

T

R

R

K

N

R

N

V

L

N

Y

S

D

L

I

P

N

L

M

G

G

S

A

A

T

A

A

L

V

A

-

G

G

T

T

T

G

Y

L

P

N

I

A

D

D

R

P

E

E

Y

Y

-

I

-

S

-

I

-

V

T

T

A

E

Q

H

L

L

L

A

G

K

F

F

E

S

-

G

-

H

-

P

-

L

R

R

I

S

C

A

Q

Q

N

H

S

L

L

V

D

D

G

A

V

T

S

Q

D

N

R

T

D

D

F

C

A

Y

I

T

E

E

F

V

T

S

S

S

W

A

A

L

A

K

I

V

F

C

M

M

M

I

H

N

L

M

T

S

R

K

F

I

S

A

E

N

E

D

L

L

I

R

L

L

W

M

S

A

S

S

-

G

-

P

-

R

A

A

Q

G

F

L

Q

S

F

E

I

I

D

V

L

L

P

P

D

A

R

R

F

-

C

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

V

M

P

P

E
|
E

L

V

V

M

R

N

G

Q

K

V

S

A

G

F

R

Q

V

V

Y

F

G

G

H

N

active site: H184 (= H162), S314 (= S283), K320 (= K289), E327 (= E296)

Sites not aligning to the query:

binding calcium ion: 389, 391

2x75A Staphylococcus aureus adenylosuccinate lyase (see paper)
25% identity, 74% coverage: 85:426/464 of query aligns to 61:395/427 of 2x75A

query
sites
2x75A

I

I

K

E

Q

Q

E

E

D

T

I

R

H
|
H

-

D

-

V

M

V

N

A

I

F

E

T

S

R

R

Q

L

V

T

S

Q

E

M

T

I

L

G

G

V

E

T

E

G

R

K

K

K

W

L

V

H

H

T

Y

G

G

R

L

S

T

R

S

N

T

D

D

Q

V

V

V

A

D

T

T

D

A

I

L

R

S

L

F

Y

V

V

I

R

K

D

Q

Q

A

I

N

D

D

L

I

I

I

Q

E

Q

K

D

D

L

L

H

E

R

R

L

F

Q

I

Q

D

G

V

L

L

V

A

E

E

L

K

A

A

E

K

R

N

E

Y

A

K

D

Y

T

T

I

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

V

T

T

T

F

F

G

G

H

V

H

K

M

M

L

A

A

L

W

W

Y

Y

E

T

M

E

L

M

V

Q

R

R

D

N

E

L

E

Q

R

R

L

F

L

K

D

Q

C

V

R

R

K

E

R

E

V

I

N

E

S

V

L

G

P

K

L

M

G

S

S

G

A

A

A

V

L

G

A

T

G

F

T

A

T

N

Y

I

P

P

I

P

D

E

R

I

E

E

-

S

Y

Y

T

V

A

C

Q

K

L

H

L

L

G

G

F

I

-

G

-

T

E

A

R

P

I

V

C

S

Q

T

N

Q

S

T

L

L

D

-

G

-

V

-

S

-

D

Q

R

R

D

D

F

R

A

H

I

A

E

Y

F

Y

T

I

S

A

W

T

A

L

A

A

I

L

F

I

M

A

M

T

H

S

L

L

T

E

R

K

F

F

S

A

E

V

E

E

L

I

I

R

L

N

W

L

S

Q

S

K

A

T

Q

E

F

T

Q

R

F

-

I

-

D

E

L

V

P

E

D

E

R

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

V

G

P

S

E
|
E

L
x
N

V

I

R

T

G

G

K

I

S

S

G

R

R

V

V

I

Y

R

G

G

H

Y

L

I

V

T

S

-

L

-

T

T

L

A

M

Y

K

E

S

N

Q

V

P

P

L

L

A

W

Y

H

N

E

K

R

D

D

-

I

-

S

-

H

N

S

Q

S

E

A

D

E

K

R

E

I

P

M

L

L

F

P

D

D

T

V

I

T

D

I

T

A

V

L

R

D

G

Y

C

A

L

L

R

N

A

R

F

F

G

T

D

N

M

I

M

V

P

D

A

R

L

L

E

T

V

V

K

F

R

E

D

D

N

N

T

-

Y

-

R

-

A

-

A

M

R

R

N

N

-

N

-

I

-

D

-

K

-

T

-

F

G

G

F

L

A

I

T

F

A

S

T

Q

D

R

L

V

A

L

D

L

Y

A

L

L

V

I

R

N

K

K

G

G

L

M

A

V

F

R

R

E

D

E

A

A

H

Y

E

D

A

K

V

V

G

-

L

-

A

-

V

-

A

-

H

-

G

-

V

-

K

-

T

-

Q

-

Q

Q

D

P

L

K

A

A

D

M

M

I

S

S

L

W

A

E

T

T

L

K

Q

T

G

P

F

F

C

R

D

E

V

L

I

I

D

E

Q

Q

D

D

active site: H67 (= H91), T139 (= T161), H140 (= H162), S261 (= S283), S262 (= S284), K267 (= K289), E274 (= E296)
binding adenosine monophosphate: N275 (≠ L297)

Sites not aligning to the query:

binding adenosine monophosphate: 3, 4

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, 64% coverage: 98:394/464 of query aligns to 77:375/431 of P12047

query
sites
P12047

L

V

T

S

Q

E

M

S

I

L

G

G

V

E

T

E

G

R

K

K

K

W

L

V

H
|
H

T

Y

G

G

R

L

S

T

R

S

N

T

D

D

Q

V

V

V

A

D

T

T

D

A

I

L

R

S

L

Y

Y

L

V

L

R

K

D

Q

Q

A

I

N

D

D

L

I

I

L

Q

L

Q

K

D

D

L

L

H

E

R

R

L

F

Q

V

Q

D

G

I

L

I

V

K

E

E

L

K

A

A

E

K

R

E

E

H

A

K

D

Y

T

T

I

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

V

T

T

T

F

F

G

G

H

L

H

K

M

L

L

A

A

L

W

W

Y

H

E

E

M

E

L

M

V

K

R

R

D

N

E

L

E

E

R

R

L

F

L

K

D

Q

C

A

R

K

K

A

R

-

V

-

N

-

S

G

L

I

P

E

L

V

G

G

S

K

A

I

A

S

L

G

A

A

G

V

T

G

T

T

Y

Y

-

A

-

N

-

I

-

D

P

P

I

F

D

V

R

E

E

Q

Y

Y

T

V

A

C

Q

E

L

K

L

L

G

G

F

L

E

K

R

A

-

A

-

P

I

I

C

S

Q

T

N
x
Q

S

T

L

L

D

-

G

-

V

-

S

-

D

Q

R

R

D

D

F

R

A

H

I

A

E

D

F

Y

T

M

S

A

W

T

A

L

A

A

I

L

F

I

M

A

M

T

H

S

L

I

T

E

R

K

F

F

S

A

E

V

E

E

L

I

I

R

-

G

L

L

W

Q

S

K

S

S

A

E

Q

T

F

R

Q

E

F

V

I

E

D

E

L

F

P

F

D

A

R

K

F

G

C

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

V

G

P

S

E

E

L

N

V

M

R

T

G

G

K

M

S

A

G

R

R

V

V

I

Y

R

G

G

H

Y

L

-

V

-

S

-

L

M

T

T

L

A

M

Y

K

E

S

N

Q

V

P

P

L

L

A

W

Y

H

N

E

K
x
R

D

D

-

I

-

S

-

H

N

S

Q

S

E

A

D

E

K

R

E

I

P

I

L

L

F

P

D

D

T

A

I

T

D

I

T

A

V

L

R

N

G

Y

C

M

L

L

R

N

A

R

F

F

G

S

D

N

M

I

M

V

P

K

A

N

L

L

E

T

V

V

K

F

R

P

D

E

N

N

T

M

Y

K

R

R

A

N

A

M

R

D

N

R

-

T

-

L

G

G

F

L

A

I

T

Y

A

S

T

Q

D

R

L

V

A

L

D

L

Y

A

L

L

V

I

R

D

K

T

G

G

L

L

A

T

F

R

R

E

D

E

A

A

H

Y

E

D

A

T

V

V

H89 (= H110) mutation to Q: Abolishes enzyme activity.
H141 (= H162) mutation to Q: Abolishes enzyme activity.
Q212 (≠ N230) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
N270 (= N291) mutation N->D,L: Abolishes enzyme activity.
R301 (≠ K325) mutation R->K,Q: Abolishes enzyme activity.

3oceA Crystal structure of fumarate lyase:delta crystallin from brucella melitensis bound to cobalt
27% identity, 52% coverage: 109:351/464 of query aligns to 134:382/461 of 3oceA

query
sites
3oceA

L

V

H

N

T

M

G

S

R

Q

S

S

R

T

N

N

D

D

Q

V

V

Y

A

P

T

T

D

A

I

V

R

R

L

L

Y

A

V

L

R

L

D

L

Q

S

I

Q

D

N

L

Q

I

V

Q

Q

Q

T

D

A

L

L

H

H

R

R

L

L

Q

I

Q

A

G

A

L

F

V

E

E

A

L

K

A

G

E

R

R

E

E

F

A

A

D

T

T

V

I

I

M

K

P

I

G

G

F

R

T

T

H
x
Q

L

L

Q

Q

T

D

A

A

Q

V

P

P

V

I

T

T

F

L

G

G

H

Q

H

E

M

F

L

E

A

A

W

F

Y

A

E

A

M

T

L

L

V

R

R

E

D

D

E

T

E

A

R

R

L

L

L

E

D

E

C

V

R

A

K

A

R

L

V

F

N

R

S

E

L

V

P

N

L

L

G

G

S

G

A

T

A

A

L

I

A

-

G

G

T

T

T

R

Y

I

P

N

I

A

D

S

R

H

E

A

Y

Y

T

A

-

E

-

Q

-

A

-

I

-

V

-

E

-

L

A

S

Q

Q

L

I

L

S

G

G

F

I

E

E

-

L

R

K

I

A

C

T

Q

G

N

N

S

L

L

V

D
x
E

G

A

V

S

S

W

D
|
D

R

T

D

G

F

A

A

F

I

V

E

T

F

F

T

S

S

G

W

I

A

L

A

R

I

R

F

I

M

A

M

V

H

K

L

L

T

S

R

K

F

I

S

A

E

N

E

D

L

L

I

R

L

L

W

L

S

S

A

G

Q

P

-

R

-

S

-

G

F

L

Q

G

F

E

I

I

D

R

L

L

P

P

D

-

R

A

F

V

C

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

V

I

P

P

E
|
E

L

S

V

V

R

N

G

Q

K

V

S

C

G

Y

R

Q

V

V

Y

I

G

G

H

N

L

D

V

L

S

T

L

V

L

T

T

M

L

A

M

A

K

E

S

S

Q

G

P

Q

L

L

A

Q

Y

L

N

N

K

A

D

-

N

-

Q

-

E

-

D

-

K

F

E

E

P

P

L

L

-

I

-

V

F

Y

D

N

T

I

I

L

D

S

T

S

V

M

R

R

G

L

C

L

L

G

R

R

A

A

F

M

G

T

D

N

M

L

active site: Q187 (≠ H162), S317 (= S283), K323 (= K289), E330 (= E296)
binding cobalt (ii) ion: E265 (≠ D233), D269 (= D237)

Query Sequence

>WP_013836160.1 NCBI__GCF_000214825.1:WP_013836160.1
MSQNINQEKLSSGRFTEATDAFVEEFTASIQFDQRMYKQDIQGSIAHARMLYKIGVLNAK
EEDAIIKGLEHILSEIENEQMHWSIKQEDIHMNIESRLTQMIGVTGKKLHTGRSRNDQVA
TDIRLYVRDQIDLIQQDLHRLQQGLVELAEREADTIMPGFTHLQTAQPVTFGHHMLAWYE
MLVRDEERLLDCRKRVNSLPLGSAALAGTTYPIDREYTAQLLGFERICQNSLDGVSDRDF
AIEFTSWAAIFMMHLTRFSEELILWSSAQFQFIDLPDRFCTGSSIMPQKKNPDVPELVRG
KSGRVYGHLVSLLTLMKSQPLAYNKDNQEDKEPLFDTIDTVRGCLRAFGDMMPALEVKRD
NTYRAARNGFATATDLADYLVRKGLAFRDAHEAVGLAVAHGVKTQQDLADMSLATLQGFC
DVIDQDVFEVLTLEGSVNARNHLGGTAPAQVRHQVAQAKTRLNF

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