SitesBLAST

Q9ZU52 Fructose-bisphosphate aldolase 3, chloroplastic; AtFBA3; Protein PIGMENT DEFECTIVE 345; EC 4.1.2.13 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 87% coverage: 17:274/298 of query aligns to 62:342/391 of Q9ZU52

query
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Q9ZU52

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Sites not aligning to the query:

387 modified: N6,N6,N6-trimethyllysine

Q944G9 Fructose-bisphosphate aldolase 2, chloroplastic; AtFBA2; EC 4.1.2.13 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 87% coverage: 17:274/298 of query aligns to 69:349/398 of Q944G9

query
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Q944G9

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Sites not aligning to the query:

394 modified: N6,N6,N6-trimethyllysine; K→A: Loss of methylation, but no effect on enzyme activity.

2qdhA Fructose-1,6-bisphosphate aldolase from leishmania mexicana in complex with mannitol-1,6-bisphosphate, a competitive inhibitor (see paper)
31% identity, 44% coverage: 52:182/298 of query aligns to 64:202/366 of 2qdhA

query
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2qdhA

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active site: K156 (= K140), E197 (= E177), E199 (= E179)
binding d-mannitol-1,6-diphosphate: K156 (= K140), R158 (= R142), E197 (= E177)

Sites not aligning to the query:

active site: 43, 239, 310
binding d-mannitol-1,6-diphosphate: 43, 45, 48, 239, 281, 282, 312, 313

2qdgA Fructose-1,6-bisphosphate schiff base intermediate in fbp aldolase from leishmania mexicana (see paper)
31% identity, 44% coverage: 52:182/298 of query aligns to 64:202/366 of 2qdgA

query
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2qdgA

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active site: K156 (= K140), E197 (= E177), E199 (= E179)
binding 1,6-fructose diphosphate (linear form): K156 (= K140), R158 (= R142)
binding phosphate ion: K116 (= K103), D118 (= D105), R158 (= R142), E197 (= E177), E199 (= E179)

Sites not aligning to the query:

active site: 43, 239, 310
binding 1,6-fructose diphosphate (linear form): 41, 43, 44, 45, 48, 239, 281, 282, 310, 311, 312, 313
binding phosphate ion: 313

5tlzA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor naphthalene 2,6-bisphosphate (see paper)
28% identity, 55% coverage: 17:180/298 of query aligns to 26:187/346 of 5tlzA

query
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5tlzA

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active site: D30 (= D21), K143 (= K140), E184 (= E177), E186 (= E179)
binding naphthalene-2,6-diyl bis[dihydrogen (phosphate)]: D30 (= D21), S32 (= S23), S35 (= S26), K104 (= K103)

Sites not aligning to the query:

active site: 226, 297, 346
binding naphthalene-2,6-diyl bis[dihydrogen (phosphate)]: 268, 269, 299, 300

5tlhA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor 2-naphthol 6-bisphosphonate (see paper)
28% identity, 55% coverage: 17:180/298 of query aligns to 29:190/350 of 5tlhA

query
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5tlhA

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M

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D33 (= D21), K146 (= K140), E187 (= E177), E189 (= E179)
binding methylenediphosphonic acid: S38 (= S26), K107 (= K103), K146 (= K140), R148 (= R142)
binding [(6-hydroxynaphthalen-2-yl)methylene]bis(phosphonic acid): E34 (≠ Q22), R42 (≠ A30), S45 (≠ Q33)

Sites not aligning to the query:

active site: 229, 300, 350
binding [(6-hydroxynaphthalen-2-yl)methylene]bis(phosphonic acid): 303

2ot0A Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with a c-terminal peptide of wiskott-aldrich syndrome protein (see paper)
28% identity, 55% coverage: 17:180/298 of query aligns to 29:190/356 of 2ot0A

query
sites
2ot0A

I

I

A

L

A

A

L

A

D
|
D

Q
x
E

S

S

G

T

G

G

S
|
S

T

I

P

A

G

K

A
x
R

L

L

R

Q

Q

S

Y

I

G

G

I

T

P

E

D

N

D

T

A

E

Y

E

N

N

G

-

D

-

A

-

E

R

M

R

F

F

K

-

L

-

I

-

H

-

E

-

M

Y

R

R

V

Q

R

L

I

L

T

T

A

A

P

D

A

D

F

R

T

V

G

N

E

P

K

C

V

I

I

G

A

G

A

V

I

I

L

L

F

F

E

H

A

E

T

T

M

L

D

Y

G

Q

Q

K

A

A

Q

D

-

D

G

G

K

R

P

P

V

F

P

P

S

Q

F

V

L

I

W

-

K

K

D

S

R

K

G

G

V

G

V

V

P

V

F

G

L

I

K

K

V

V

D

D

K

K

G

G

L

V

E

V

-

P

-

L

A

A

E

G

S

T

D

N

G

G

V

E

R

T

L

T

M

T

K

Q

P

G

I

L

P

D

G

G

L

L

D

S

A

E

L

R

L

C

A

A

R

Q

A

Y

G

K

K

K

L

D

G

G

I

A

F

D

G

F

T

A

K
|
K

M

W

R
|
R

S

C

V

V

I

L

E

K

-

I

-

G

Q

E

N

H

S

T

P

P

A

S

G

A

I

L

A

A

A

I

V

M

V

E

K

N

Q

A

Q

N

F

V

-

L

-

A

E

R

Y

Y

G

A

A

S

Q

I

I

C

D

Q

A

Q

G

N

G

G

L

I

M

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D33 (= D21), K146 (= K140), E187 (= E177), E189 (= E179)
binding : E34 (≠ Q22), S38 (= S26), R42 (≠ A30), K146 (= K140), R148 (= R142)

Sites not aligning to the query:

active site: 229, 300, 356
binding : 303, 306

5tlwA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor 1-phosphate-benzene 4-bisphosphonate (see paper)
28% identity, 55% coverage: 17:180/298 of query aligns to 29:190/349 of 5tlwA

query
sites
5tlwA

I

I

A

L

A

A

L

A

D
|
D

Q

E

S
|
S

G

T

G

G

S
|
S

T

I

P

A

G

K

A

R

L

L

R

Q

Q

S

Y

I

G

G

I

T

P

E

D

N

D

T

A

E

Y

E

N

N

G

-

D

-

A

-

E

R

M

R

F

F

K

-

L

-

I

-

H

-

E

-

M

Y

R

R

V

Q

R

L

I

L

T

T

A

A

P

D

A

D

F

R

T

V

G

N

E

P

K

C

V

I

I

G

A

G

A

V

I

I

L

L

F

F

E

H

A

E

T

T

M

L

D

Y

G

Q

Q

K

A

A

Q

D

-

D

G

G

K

R

P

P

V

F

P

P

S

Q

F

V

L

I

W

-

K

K

D

S

R

K

G

G

V

G

V

V

P

V

F

G

L

I

K
|
K

V

V

D

D

K

K

G

G

L

V

E

V

-

P

-

L

A

A

E

G

S

T

D

N

G

G

V

E

R

T

L

T

M

T

K

Q

P

G

I

L

P

D

G

G

L

L

D

S

A

E

L

R

L

C

A

A

R

Q

A

Y

G

K

K

K

L

D

G

G

I

A

F

D

G

F

T

A

K
|
K

M

W

R
|
R

S

C

V

V

I

L

E

K

-

I

-

G

Q

E

N

H

S

T

P

P

A

S

G

A

I

L

A

A

A

I

V

M

V

E

K

N

Q

A

Q

N

F

V

-

L

-

A

E

R

Y

Y

G

A

A

S

Q

I

I

C

D

Q

A

Q

G

N

G

G

L

I

M

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D33 (= D21), K146 (= K140), E187 (= E177), E189 (= E179)
binding {[4-(phosphonooxy)phenyl]methylene}bis(phosphonic acid): S35 (= S23), S38 (= S26), K107 (= K103), K146 (= K140), R148 (= R142)

Sites not aligning to the query:

active site: 229, 300, 349
binding {[4-(phosphonooxy)phenyl]methylene}bis(phosphonic acid): 303

5tleA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor 2-phosphate-naphthalene 6-bisphosphonate (see paper)
28% identity, 55% coverage: 17:180/298 of query aligns to 29:190/349 of 5tleA

query
sites
5tleA

I

I

A

L

A

A

L

A

D
|
D

Q

E

S
|
S

G

T

G

G

S
|
S

T

I

P

A

G

K

A

R

L

L

R

Q

Q

S

Y

I

G

G

I

T

P

E

D

N

D

T

A

E

Y

E

N

N

G

-

D

-

A

-

E

R

M

R

F

F

K

-

L

-

I

-

H

-

E

-

M

Y

R

R

V

Q

R

L

I

L

T

T

A

A

P

D

A

D

F

R

T

V

G

N

E

P

K

C

V

I

I

G

A

G

A

V

I

I

L

L

F

F

E

H

A

E

T

T

M

L

D

Y

G

Q

Q

K

A

A

Q

D

-

D

G

G

K

R

P

P

V

F

P

P

S

Q

F

V

L

I

W

-

K

K

D

S

R

K

G

G

V

G

V

V

P

V

F

G

L

I

K
|
K

V

V

D

D

K

K

G

G

L

V

E

V

-

P

-

L

A

A

E

G

S

T

D

N

G

G

V

E

R

T

L

T

M

T

K

Q

P

G

I

L

P

D

G

G

L

L

D

S

A

E

L

R

L

C

A

A

R

Q

A

Y

G

K

K

K

L

D

G

G

I

A

F

D

G

F

T

A

K
|
K

M

W

R

R

S

C

V

V

I

L

E

K

-

I

-

G

Q

E

N

H

S

T

P

P

A

S

G

A

I

L

A

A

A

I

V

M

V

E

K

N

Q

A

Q

N

F

V

-

L

-

A

E

R

Y

Y

G

A

A

S

Q

I

I

C

D

Q

A

Q

G

N

G

G

L

I

M

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D33 (= D21), K146 (= K140), E187 (= E177), E189 (= E179)
binding {[6-(phosphonooxy)naphthalen-2-yl]methylene}bis(phosphonic acid): D33 (= D21), S35 (= S23), S38 (= S26), K107 (= K103)

Sites not aligning to the query:

active site: 229, 300, 349
binding {[6-(phosphonooxy)naphthalen-2-yl]methylene}bis(phosphonic acid): 229, 270, 272, 302, 303

3tu9A Crystal structure of rabbit muscle aldolase bound with 5-o-methyl mannitol 1,6-phosphate (see paper)
28% identity, 55% coverage: 17:180/298 of query aligns to 29:190/349 of 3tu9A

query
sites
3tu9A

I

I

A

L

A
|
A

L

A

D
|
D

Q
x
E

S
|
S

G

T

G

G

S
|
S

T

I

P

A

G

K

A

R

L

L

R

Q

Q

S

Y

I

G

G

I

T

P

E

D

N

D

T

A

E

Y

E

N

N

G

-

D

-

A

-

E

R

M

R

F

F

K

-

L

-

I

-

H

-

E

-

M

Y

R

R

V

Q

R

L

I

L

T

T

A

A

P

D

A

D

F

R

T

V

G

N

E

P

K

C

V

I

I

G

A

G

A

V

I

I

L

L

F

F

E

H

A

E

T

T

M

L

D

Y

G

Q

Q

K

A

A

Q

D

-

D

G

G

K

R

P

P

V

F

P

P

S

Q

F

V

L

I

W

-

K

K

D

S

R

K

G

G

V

G

V

V

P

V

F

G

L

I

K
|
K

V

V

D

D

K

K

G

G

L

V

E

V

-

P

-

L

A

A

E

G

S

T

D

N

G

G

V

E

R

T

L

T

M

T

K

Q

P

G

I

L

P

D

G

G

L

L

D

S

A

E

L

R

L

C

A

A

R

Q

A

Y

G

K

K

K

L

D

G

G

I

A

F

D

G

F

T

A

K
|
K

M

W

R

R

S

C

V

V

I

L

E

K

-

I

-

G

Q

E

N

H

S

T

P

P

A

S

G

A

I

L

A

A

A

I

V

M

V

E

K

N

Q

A

Q

N

F

V

-

L

-

A

E

R

Y

Y

G

A

A

S

Q

I

I

C

D

Q

A

Q

G

N

G

G

L

I

M

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D33 (= D21), K146 (= K140), E187 (= E177), E189 (= E179)
binding 2-O-methyl-1,6-di-O-phosphono-D-mannitol: A31 (= A19), D33 (= D21), E34 (≠ Q22), S35 (= S23), S38 (= S26), K107 (= K103), K146 (= K140), E187 (= E177)

Sites not aligning to the query:

active site: 229, 300, 349
binding 2-O-methyl-1,6-di-O-phosphono-D-mannitol: 229, 271, 272, 301, 302, 303

2ot1A Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with naphthol as-e phosphate, a competitive inhibitor (see paper)
28% identity, 55% coverage: 17:180/298 of query aligns to 29:190/349 of 2ot1A

query
sites
2ot1A

I

I

A

L

A

A

L

A

D
|
D

Q

E

S

S

G

T

G

G

S

S

T

I

P

A

G

K

A
x
R

L

L

R

Q

Q

S

Y

I

G

G

I

T

P

E

D

N

D

T

A

E

Y

E

N

N

G

-

D

-

A

-

E

R

M

R

F

F

K

-

L

-

I

-

H

-

E

-

M

Y

R

R

V

Q

R

L

I

L

T

T

A

A

P

D

A

D

F

R

T

V

G

N

E

P

K

C

V

I

I

G

A

G

A

V

I

I

L

L

F

F

E

H

A

E

T

T

M

L

D

Y

G

Q

Q

K

A

A

Q

D

-

D

G

G

K

R

P

P

V

F

P

P

S

Q

F

V

L

I

W

-

K

K

D

S

R

K

G

G

V

G

V

V

P

V

F

G

L

I

K

K

V

V

D

D

K

K

G

G

L

V

E

V

-

P

-

L

A

A

E

G

S

T

D

N

G

G

V

E

R

T

L

T

M

T

K

Q

P

G

I

L

P

D

G

G

L

L

D

S

A

E

L

R

L

C

A

A

R

Q

A

Y

G

K

K

K

L

D

G

G

I

A

F

D

G

F

T

A

K
|
K

M

W

R

R

S

C

V

V

I

L

E

K

-

I

-

G

Q

E

N

H

S

T

P

P

A

S

G

A

I

L

A

A

A

I

V

M

V

E

K

N

Q

A

Q

N

F

V

-

L

-

A

E

R

Y

Y

G

A

A

S

Q

I

I

C

D

Q

A

Q

G

N

G

G

L

I

M

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D33 (= D21), K146 (= K140), E187 (= E177), E189 (= E179)
binding n-(4-chlorophenyl)-3-(phosphonooxy)naphthalene-2-carboxamide: R42 (≠ A30)

Sites not aligning to the query:

active site: 229, 300, 349
binding n-(4-chlorophenyl)-3-(phosphonooxy)naphthalene-2-carboxamide: 303, 306

1zalA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with partially disordered tagatose-1,6-bisphosphate, a weak competitive inhibitor (see paper)
28% identity, 55% coverage: 17:180/298 of query aligns to 29:190/363 of 1zalA

query
sites
1zalA

I

I

A

L

A

A

L

A

D
|
D

Q

E

S
|
S

G

T

G

G

S

S

T

I

P

A

G

K

A

R

L

L

R

Q

Q

S

Y

I

G

G

I

T

P

E

D

N

D

T

A

E

Y

E

N

N

G

-

D

-

A

-

E

R

M

R

F

F

K

-

L

-

I

-

H

-

E

-

M

Y

R

R

V

Q

R

L

I

L

T

T

A

A

P

D

A

D

F

R

T

V

G

N

E

P

K

C

V

I

I

G

A

G

A

V

I

I

L

L

F

F

E

H

A

E

T

T

M

L

D

Y

G

Q

Q

K

A

A

Q

D

-

D

G

G

K

R

P

P

V

F

P

P

S

Q

F

V

L

I

W

-

K

K

D

S

R

K

G

G

V

G

V

V

P

V

F

G

L

I

K
|
K

V

V

D

D

K

K

G

G

L

V

E

V

-

P

-

L

A

A

E

G

S

T

D

N

G

G

V

E

R

T

L

T

M

T

K

Q

P

G

I

L

P

D

G

G

L

L

D

S

A

E

L

R

L

C

A

A

R

Q

A

Y

G

K

K

K

L

D

G

G

I

A

F

D

G

F

T

A

K
|
K

M

W

R

R

S

C

V

V

I

L

E

K

-

I

-

G

Q

E

N

H

S

T

P

P

A

S

G

A

I

L

A

A

A

I

V

M

V

E

K

N

Q

A

Q

N

F

V

-

L

-

A

E

R

Y

Y

G

A

A

S

Q

I

I

C

D

Q

A

Q

G

N

G

G

L

I

M

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D33 (= D21), K146 (= K140), E187 (= E177), E189 (= E179)
binding phosphate ion: S35 (= S23), K107 (= K103)

Sites not aligning to the query:

active site: 229, 300, 363
binding phosphate ion: 271, 302

1zajA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with mannitol-1,6-bisphosphate, a competitive inhibitor (see paper)
28% identity, 55% coverage: 17:180/298 of query aligns to 29:190/363 of 1zajA

query
sites
1zajA

I

I

A

L

A

A

L

A

D
|
D

Q

E

S
|
S

G

T

G

G

S
|
S

T

I

P

A

G

K

A

R

L

L

R

Q

Q

S

Y

I

G

G

I

T

P

E

D

N

D

T

A

E

Y

E

N

N

G

-

D

-

A

-

E

R

M

R

F

F

K

-

L

-

I

-

H

-

E

-

M

Y

R

R

V

Q

R

L

I

L

T

T

A

A

P

D

A

D

F

R

T

V

G

N

E

P

K

C

V

I

I

G

A

G

A

V

I

I

L

L

F

F

E

H

A

E

T

T

M

L

D

Y

G

Q

Q

K

A

A

Q

D

-

D

G

G

K

R

P

P

V

F

P

P

S

Q

F

V

L

I

W

-

K

K

D

S

R

K

G

G

V

G

V

V

P

V

F

G

L

I

K
|
K

V

V

D

D

K

K

G

G

L

V

E

V

-

P

-

L

A

A

E

G

S

T

D

N

G

G

V

E

R

T

L

T

M

T

K

Q

P

G

I

L

P

D

G

G

L

L

D

S

A

E

L

R

L

C

A

A

R

Q

A

Y

G

K

K

K

L

D

G

G

I

A

F

D

G

F

T

A

K
|
K

M

W

R

R

S

C

V

V

I

L

E

K

-

I

-

G

Q

E

N

H

S

T

P

P

A

S

G

A

I

L

A

A

A

I

V

M

V

E

K

N

Q

A

Q

N

F

V

-

L

-

A

E

R

Y

Y

G

A

A

S

Q

I

I

C

D

Q

A

Q

G

N

G

G

L

I

M

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D33 (= D21), K146 (= K140), E187 (= E177), E189 (= E179)
binding d-mannitol-1,6-diphosphate: D33 (= D21), S35 (= S23), S38 (= S26), K107 (= K103), K146 (= K140), E187 (= E177)

Sites not aligning to the query:

active site: 229, 300, 363
binding d-mannitol-1,6-diphosphate: 229, 271, 272, 301, 302, 303

P00883 Fructose-bisphosphate aldolase A; Muscle-type aldolase; EC 4.1.2.13 from Oryctolagus cuniculus (Rabbit) (see 5 papers)
28% identity, 55% coverage: 17:180/298 of query aligns to 30:191/364 of P00883

query
sites
P00883

I

I

A

L

A

A

L

A

D

D

Q
x
E

S

S

G

T

G

G

S

S

T

I

P

A

G

K

A
x
R

L

L

R

Q

Q

S

Y

I

G

G

I

T

P

E

D

N

D

T

A

E

Y

E

N

N

G

-

D

-

A

-

E

R

M

R

F

F

K

-

L

-

I

-

H

-

E

-

M

Y

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Q

R

L

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L

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T

A

A

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D

A

D

F

R

T

V

G

N

E

P

K

C

V

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I

G

A

G

A

V

I

I

L

L

F

F

E

H

A

E

T

T

M

L

D

Y

G

Q

Q

K

A

A

Q

D

-

D

G

G

K

R

P

P

V

F

P

P

S

Q

F

V

L

I

W

-

K

K

D

S

R

K

G

G

V

G

V

V

P

V

F

G

L

I

K

K

V

V

D

D

K

K

G

G

L

V

E

V

-

P

-

L

A

A

E

G

S

T

D

N

G

G

V

E

R

T

L

T

M

T

K

Q

P

G

I

L

P

D

G

G

L

L

D

S

A

E

L

R

L

C

A

A

R

Q

A

Y

G

K

K

K

L

D

G

G

I

A

F

D

G

F

T

A

K
|
K

M

W

R

R

S

C

V

V

I

L

E

K

-

I

-

G

Q

E

N

H

S

T

P

P

A

S

G

A

I

L

A

A

A

I

V

M

V

E

K

N

Q

A

Q

N

F

V

-

L

-

A

E

R

Y

Y

G

A

A

S

Q

I

I

C

D

Q

A

Q

G

N

G

G

L

I

M

V

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P

I

I

L

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E
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E

P

P

E
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E

V

I

E35 (≠ Q22) mutation to A: Reduces activity 14-fold.
R43 (≠ A30) binding beta-D-fructose 1,6-bisphosphate; mutation to A: Reduces activity 14-fold.
K147 (= K140) mutation to A: Loss of activity.
E188 (= E177) active site, Proton acceptor; mutation to A: Reduces activity over 100-fold.; mutation to Q: Reduces activity over 1000-fold.
E190 (= E179) mutation to Q: Reduces activity 20-fold.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
230 active site, Schiff-base intermediate with dihydroxyacetone-P; K→M: Loss of activity.
272:274 binding beta-D-fructose 1,6-bisphosphate
301 binding beta-D-fructose 1,6-bisphosphate
304 binding beta-D-fructose 1,6-bisphosphate; R→A: Reduces activity 400-fold.
361 modified: Deamidated asparagine; in form beta

4aldA Human muscle fructose 1,6-bisphosphate aldolase complexed with fructose 1,6-bisphosphate (see paper)
28% identity, 55% coverage: 17:180/298 of query aligns to 29:190/363 of 4aldA

query
sites
4aldA

I

I

A

L

A

A

L

A

D
|
D

Q
x
E

S
|
S

G

T

G

G

S
|
S

T

I

P

A

G

K

A

R

L

L

R

Q

Q

S

Y

I

G

G

I

T

P

E

D

N

D

T

A

E

Y

E

N

N

G

-

D

-

A

-

E

R

M

R

F

F

K

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L

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I

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H

-

E

-

M

Y

R

R

V

Q

R

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L

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T

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A

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D

A

D

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R

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V

G

N

E

P

K

C

V

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I

G

A

G

A

V

I

I

L

L

F

F

E

H

A

E

T

T

M

L

D

Y

G

Q

Q

K

A

A

Q

D

-

D

G

G

K

R

P

P

V

F

P

P

S

Q

F

V

L

I

W

-

K

K

D

S

R

K

G

G

V

G

V

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P

V

F

G

L

I

K
|
K

V

V

D

D

K

K

G

G

L

V

E

V

-

P

-

L

A

A

E

G

S

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D

N

G

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G

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A

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A

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G

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K

K

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D

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G

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A

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A

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K

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R
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R

S

C

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V

I

L

E

K

-

I

-

G

Q

E

N

H

S

T

P

P

A

S

G

A

I

L

A

A

A

I

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M

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E

K

N

Q

A

Q

N

F

V

-

L

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A

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R

Y

Y

G

A

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I

C

D

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A

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G

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E
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E

P

P

E
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E

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I

active site: D33 (= D21), K146 (= K140), E187 (= E177), E189 (= E179)
binding 1,6-fructose diphosphate (linear form): E34 (≠ Q22), S35 (= S23), S38 (= S26), K107 (= K103), K146 (= K140), R148 (= R142), E187 (= E177)

Sites not aligning to the query:

active site: 229, 300, 363
binding 1,6-fructose diphosphate (linear form): 270, 271, 272, 303

P04075 Fructose-bisphosphate aldolase A; Lung cancer antigen NY-LU-1; Muscle-type aldolase; EC 4.1.2.13 from Homo sapiens (Human) (see 11 papers)
28% identity, 55% coverage: 17:180/298 of query aligns to 30:191/364 of P04075

query
sites
P04075

I

I

A

L

A

A

L

A

D

D

Q

E

S

S

G

T

G

G

S

S

T

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P

A

G

K

A

R

L

L

R

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Q

S

Y

I

G

G

I

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D

N

D

T

A

E

Y

E

N

N

G

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D

-

A

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F

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L

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I

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H

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D

A

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G

A

G

A

V

I

I

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L

F

F

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A

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T

M

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D

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G

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Q

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A

A

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D

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D

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P

S

Q

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K
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K

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S

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K

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G

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G

V

V

P

V

F

G

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I

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K

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D

K
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K

G

G

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V

E

V

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P

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L

A

A

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D

N

G

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x
D

G

G

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L

D

S

A

E

L

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L

C

A

A

R

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A

Y

G

K

K

K

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D

G

G

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A

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A

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K

M

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R

R

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C

V

V

I

L

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K

-

I

-

G

Q

E

N

H

S

T

P

P

A

S

G

A

I

L

A

A

A

I

V

M

V

E

K

N

Q

A

Q

N

F

V

-

L

-

A

E

R

Y

Y

G

A

A

S

Q

I

I

C

D

Q

A

Q

G

N

G

G

L

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M

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P

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I

L

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E

E

P

P

E

E

V

I

K99 (= K94) modified: N6-(2-hydroxyisobutyryl)lysine
K111 (= K106) modified: N6-malonyllysine; alternate
D129 (≠ P122) to G: in GSD12; thermolabile; dbSNP:rs121909533
K147 (= K140) modified: N6-(2-hydroxyisobutyryl)lysine

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
207 E → K: in GSD12; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity; dbSNP:rs121909534
312 modified: N6-malonyllysine
347 G → S: in GSD12; likely benign; does not affect thermal stability; 4-fold decrease in catalytic efficiency due to reduced enzyme activity; dbSNP:rs138824667

Q8I8I2 Fructose-bisphosphate aldolase 1; TgALD; TgALD1; TgAldolase; EC 4.1.2.13 from Toxoplasma gondii (see 2 papers)
34% identity, 39% coverage: 66:180/298 of query aligns to 70:192/363 of Q8I8I2

query
sites
Q8I8I2

G

G

E

Q

K

Y

V

I

I

S

A

G

A

A

I

I

L

L

F

F

E

E

A

E

T

T

M

L

D

Y

G

Q

Q

K

A

S

-

P

Q

S

G

G

K

V

P

P

V

M

P

V

S

D

F

L

L

L

W

-

K

K

D

A

R

E

G

G

V

I

P

P

F

G

L

I

K
|
K

V

V

D

D

K

K

G

G

L

L

E

E

A

T

-

L

-

P

-

L

E

T

S

D

D

D

G

E

V

K

R

A

L

T

M

M

K

-

P

-

I

-

P

-

G

G

L

L

D

D

A

G

L

L

L

S

A

E

R

R

A

C

G

K

K

K

L

Y

-

Y

-

E

-

A

G

G

I

A

F

R

G

F

T

A

K
|
K

M

W

R
|
R

S

A

V

V

I

L

E

S

Q

I

N

D

S

P

P

A

A

K

G

G

-

K

-

P

-

T

-

N

-

L

-

S

I

I

A

T

A

E

V

V

V

A

K

H

Q

G

Q

L

F

A

E

R

Y

Y

G

A

A

A

Q

I

I

C

D

Q

A

A

G

N

G

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L

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M

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E
|
E

P

P

E

E

V

I

K107 (= K103) binding D-glyceraldehyde 3-phosphate; mutation to A: Abolishes enzymatic activity. Reduces MIC2 binding.
K146 (= K140) binding dihydroxyacetone phosphate; mutation to A: Abolishes enzymatic activity. Reduces MIC2 binding.
R148 (= R142) mutation to A: Abolishes enzymatic activity. Reduces ACT1 binding. Reduces MIC2 binding.
E189 (= E177) binding D-glyceraldehyde 3-phosphate

Sites not aligning to the query:

34 binding dihydroxyacetone phosphate; D→A: Abolishes enzymatic activity. Reduces ACT1 binding. Slightly reduces MIC2 binding.
35 E→A: Reduces enzymatic activity. Enhances MIC2 binding.
36 binding D-glyceraldehyde 3-phosphate
39 binding D-glyceraldehyde 3-phosphate
42 K→A: Does not affect enzymatic activity. Reduces ACT1 binding. Reduces MIC2 binding. Abolishes enzymatic activity and reduces MIC2 binding; when associated with A-43.; K→E: Does not affect enzymatic activity. Reduces MIC2 binding. Reduces enzymatic activity, ACT1 binding and MIC2 binding; when associated with G-43.
43 R→A: Does not affect enzymatic activity. Reduces ACT1 binding. Reduces MIC2 binding. Abolishes enzymatic activity and reduces MIC2 binding; when associated with A-42.; R→D: Abolishes enzymatic activity. Reduces MIC2 binding.
231 active site, Schiff-base intermediate with dihydroxyacetone phosphate; binding dihydroxyacetone phosphate; K→A: Abolishes enzymatic activity. Reduces MIC2 binding.
273 binding dihydroxyacetone phosphate
274 binding dihydroxyacetone phosphate
303 binding dihydroxyacetone phosphate
304 binding dihydroxyacetone phosphate; R→A: Abolishes enzymatic activity. Reduces MIC2 binding.
307 Q→F: Abolishes enzymatic activity. Reduces MIC2 binding.; Q→G: Does not affect enzymatic activity. Does not affect MIC2 binding.

5tklA Crystal structure of fbp aldolase from toxoplasma gondii, condensation intermediate (see paper)
34% identity, 39% coverage: 66:180/298 of query aligns to 70:192/350 of 5tklA

query
sites
5tklA

G

G

E

Q

K

Y

V

I

I

S

A

G

A

A

I

I

L

L

F

F

E

E

A

E

T

T

M

L

D

Y

G

Q

Q

K

A

S

-

P

Q

S

G

G

K

V

P

P

V

M

P

V

S

D

F

L

L

L

W

-

K

K

D

A

R

E

G

G

V

I

P

P

F

G

L

I

K
|
K

V

V

D

D

K

K

G

G

L

L

E

E

A

T

-

L

-

P

-

L

E

T

S

D

D

D

G

E

V

K

R

A

L

T

M

M

K

-

P

-

I

-

P

-

G

G

L

L

D

D

A

G

L

L

L

S

A

E

R

R

A

C

G

K

K

K

L

Y

-

Y

-

E

-

A

G

G

I

A

F

R

G

F

T

A

K
|
K

M

W

R
|
R

S

A

V

V

I

L

E

S

Q

I

N

D

S

P

P

A

A

K

G

G

-

K

-

P

-

T

-

N

-

L

-

S

I

I

A

T

A

E

V

V

V

A

K

H

Q

G

Q

L

F

A

E

R

Y

Y

G

A

A

A

Q

I

I

C

D

Q

A

A

G

N

G

R

L

L

M

V

P

P

I

I

L

V

E
|
E

P

P

E
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E

V

I

active site: K146 (= K140), E189 (= E177), E191 (= E179)
binding glyceraldehyde-3-phosphate: K107 (= K103), K146 (= K140), R148 (= R142), E189 (= E177)
binding 1,6-di-O-phosphono-D-fructose: K107 (= K103), K146 (= K140), R148 (= R142), E189 (= E177)

Sites not aligning to the query:

active site: 34, 231, 301, 350
binding glyceraldehyde-3-phosphate: 36, 39, 231
binding 1,6-di-O-phosphono-D-fructose: 32, 34, 36, 39, 231, 273, 274, 303, 304

Query Sequence

>WP_012402890.1 NCBI__GCF_000020045.1:WP_012402890.1
MANEKMLAQISEKAGFIAALDQSGGSTPGALRQYGIPDDAYNGDAEMFKLIHEMRVRIIT
APAFTGEKVIAAILFEATMDGQAQGKPVPSFLWKDRGVVPFLKVDKGLEAESDGVRLMKP
IPGLDALLARAGKLGIFGTKMRSVIEQNSPAGIAAVVKQQFEYGAQIDAGGLMPILEPEV
SIKTPDKAGAEKTLRDEILKGLDALPAGKQVMLKLTIPDVADFYKPLIDHPRVLRVVALS
GGYTRTEACKLLAKNHGMIASFSRALINDLKKSMSDSEFNAKLSEAIDEIYDASALKV

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