SitesBLAST

D34 (= D24) binding dihydroxyacetone phosphate; mutation to A: Abolishes enzymatic activity. Reduces ACT1 binding. Slightly reduces MIC2 binding.
E35 (= E25) mutation to A: Reduces enzymatic activity. Enhances MIC2 binding.
S36 (= S26) binding D-glyceraldehyde 3-phosphate
T39 (= T29) binding D-glyceraldehyde 3-phosphate
K42 (= K32) mutation to A: Does not affect enzymatic activity. Reduces ACT1 binding. Reduces MIC2 binding. Abolishes enzymatic activity and reduces MIC2 binding; when associated with A-43.; mutation to E: Does not affect enzymatic activity. Reduces MIC2 binding. Reduces enzymatic activity, ACT1 binding and MIC2 binding; when associated with G-43.
R43 (= R33) mutation to A: Does not affect enzymatic activity. Reduces ACT1 binding. Reduces MIC2 binding. Abolishes enzymatic activity and reduces MIC2 binding; when associated with A-42.; mutation to D: Abolishes enzymatic activity. Reduces MIC2 binding.
K107 (= K97) binding D-glyceraldehyde 3-phosphate; mutation to A: Abolishes enzymatic activity. Reduces MIC2 binding.
K146 (= K136) binding dihydroxyacetone phosphate; mutation to A: Abolishes enzymatic activity. Reduces MIC2 binding.
R148 (= R138) mutation to A: Abolishes enzymatic activity. Reduces ACT1 binding. Reduces MIC2 binding.
E189 (= E178) binding D-glyceraldehyde 3-phosphate
K231 (= K220) active site, Schiff-base intermediate with dihydroxyacetone phosphate; binding dihydroxyacetone phosphate; mutation to A: Abolishes enzymatic activity. Reduces MIC2 binding.
S273 (= S262) binding dihydroxyacetone phosphate
G274 (= G263) binding dihydroxyacetone phosphate
G303 (= G292) binding dihydroxyacetone phosphate
R304 (= R293) binding dihydroxyacetone phosphate; mutation to A: Abolishes enzymatic activity. Reduces MIC2 binding.
Q307 (= Q296) mutation to F: Abolishes enzymatic activity. Reduces MIC2 binding.; mutation to G: Does not affect enzymatic activity. Does not affect MIC2 binding.

5tklA Crystal structure of fbp aldolase from toxoplasma gondii, condensation intermediate (see paper)
56% identity, 96% coverage: 10:332/338 of query aligns to 20:343/350 of 5tklA

query
sites
5tklA

A

A

N

R

A

K

I

I

V

A

T

A

R

P

E

G

K

K

G

G

V

I

L

L

A
|
A

A

A

D
|
D

E

E

S
|
S

A

T

P

G

T
|
T

I

I

R

K

K

K

R

R

F

F

D

D

S

S

V

I

G

G

V

V

E

E

S

N

T

T

E

E

E

A

N

N

R

R

R

A

R

F

Y

Y

R

R

E

D

I

L

L

L

F

F

T

S

T

T

A

K

G

G

I

L

E

G

R

Q

H

Y

I

I

G

S

G

G

V

A

I

I

L

L

F

F

D

E

E

E

T

T

L

L

R

Y

Q

Q

S

K

T

S

R

P

D

S

G

G

T

V

P

P

F

M

A

V

R

D

L

L

S

K

D

A

R

E

G

G

I

I

P

P

G

G

I

I

K
|
K

V

V

D

D

K

K

G

G

A

L

R

E

E

T

L

L

A

P

L

L

Y

T

P

D

G

D

E

E

K

K

I

A

A

T

E

M

G

G

L

L

D

D

G

G

L

L

R

S

E

E

R

R

L

C

V

K

E

K

Y

Y

R

Y

Q

E

L

A

G

G

A

A

E

R

F

F

A

A

K
|
K

W

W

R
|
R

A

A

V

V

I

L

E

S

I

I

D

D

-

P

G

A

H

K

D

G

M

K

P

P

S

T

P

N

F

L

G

S

I

I

R

T

A

E

N

V

A

A

H

H

A

G

L

L

A

A

R

R

Y

Y

A

A

L

I

C

C

Q

Q

E

A

L

N

D

R

I

L

V

V

P

P

I

I

V

V

E
|
E

P

P

E
|
E

V

I

L

L

M

T

D

D

G

G

A

S

H

H

G

D

I

I

D

T

R

V

C

C

E

A

E

E

V

V

T

T

S

E

G

R

V

V

L

L

Q

A

A

A

V

V

F

F

S

K

E

A

L

L

D

N

A

D

H

H

R

H

V

V

L

L

F

L

E

E

G

G

M

A

L

L

K
|
K

P

P

N

N

M

M

V

V

I

T

A

H

G

G

K

S

R

D

C

C

D

P

R

K

C

P

S

A

S

S

V

H

E

E

Q

E

V

I

A

A

E

F

A

Y

T

T

I

V

R

R

C

S

M

L

T

K

R

R

Y

T

V

V

P

P

A

P

A

A

V

L

P

P

G

G

I

V

V

M

F

F

L

L

S
|
S

G
|
G

G

G

Q

Q

S

S

A

E

E

E

D

D

A

A

T

S

D

L

H

N

L

L

N

N

A

E

M

M

N

N

R

K

M

M

G

G

P

P

H

H

P

P

W

F

Q

Q

V

L

S

S

F

F

S
|
S

Y

Y

G
|
G

R
|
R

A

A

L

L

Q

Q

A

A

P

S

V

C

L

L

A

K

A

A

W

W

K

K

G

G

D

V

E

P

S

E

N

N

L

K

E

A

S

K

A

A

R

Q

H

Q

A

V

L

L

A

M

K

E

R

R

C

A

L

R

L

A

N

N

G

G

L

E

A

A

R

Q

Q

L

G

G

K

K

Y

Y

active site: D34 (= D24), K146 (= K136), E189 (= E178), E191 (= E180), K231 (= K220), S301 (= S290)
binding glyceraldehyde-3-phosphate: S36 (= S26), T39 (= T29), K107 (= K97), K146 (= K136), R148 (= R138), E189 (= E178), K231 (= K220)
binding 1,6-di-O-phosphono-D-fructose: A32 (= A22), D34 (= D24), S36 (= S26), T39 (= T29), K107 (= K97), K146 (= K136), R148 (= R138), E189 (= E178), K231 (= K220), S273 (= S262), G274 (= G263), G303 (= G292), R304 (= R293)

Sites not aligning to the query:

active site: 350

4tr9A Ternary co-crystal structure of fructose-bisphosphate aldolase from plasmodium falciparum in complex with trap and a small molecule inhibitor (see paper)
51% identity, 97% coverage: 4:332/338 of query aligns to 15:344/347 of 4tr9A

query
sites
4tr9A

D

E

R

E

L

L

R

A

S

T

V

T

A

A

N

Q

A

K

I

L

V

V

T

Q

R

A

E

G

K

K

G

G

V

I

L

L

A

A

D
|
D

E
|
E

S

S

A

T

P

Q

T

T

I

I

R

K

K

K

R
|
R

F

F

D

D

S

N

V

I

G

K

V

L

E

E

S

N

T

T

E

I

E

E

N

N

R

R

R

A

R

S

Y

Y

R

R

E

D

I

L

L

L

F

F

T

G

T

T

A

K

G

G

I

L

E

G

R

K

H

F

I

I

G

S

G

G

V

A

I

I

L

L

F

F

D

E

E

E

T

T

L

L

R

F

Q

Q

S

K

T

N

R

E

D

A

G

G

T

V

P

P

F

M

A

V

R

N

L

L

S

H

D

N

R

E

G

N

I

I

P

P

G

G

I

I

K

K

V

V

D

D

K

K

G

G

A

L

R

V

E

N

L

I

A

P

L

C

Y

T

P

D

G

E

E

E

K

K

I

S

A

T

E

Q

G

G

L

L

D

D

G

G

L

L

R

A

E

E

R

R

L

C

V

K

E

E

Y

Y

R

Y

Q

K

L

A

G

G

A

A

E

R

F

F

A

A

K
|
K

W

W

R
|
R

A

T

V

V

I

L

E

V

I

I

D

D

-

T

G

A

H

K

D

G

M

K

P

P

S

T

P

D

F

L

G

S

I

I

R

H

A

E

N

T

A

A

H

W

A

G

L

L

A

A

R

R

Y

Y

A

A

A

S

L

I

C

C

Q

Q

E

Q

L

N

D

R

I

L

V

V

P

P

I

I

V

V

E
|
E

P

P

E
|
E

V

I

L

L

M

A

D

D

G

G

A

P

H

H

G

S

I

I

D

E

R

V

C

C

E

A

E

V

V

V

T

T

S

Q

G

K

V

V

L

L

Q

S

A

C

V

V

F

F

S

K

E

A

L

L

D

Q

A

E

H

N

R

G

V

V

L

L

F

L

E

E

G

G

M

A

L

L

K
|
K

P

P

N

N

M

M

V

V

I

T

A

A

G

G

K

Y

R

E

C

C

D

T

R

A

C

K

S

T

V

T

E

Q

Q

D

V

V

A

G

E
x
F

A

L

T

T

I
x
V

R
|
R

C

T

M

L

T
x
R

R

R

Y

T

V

V

P

P

A

P

A

A

V

L

P

P

G

G

I

V

V

V

F

F

L

L

S
|
S

G
|
G

G

G

Q

Q

S

S

A

E

E

E

D

E

A

A

T

S

D

V

H

N

L

L

N

N

A

S

M

I

N

N

R

A

M
x
L

G
|
G

P
|
P

H

H

P

P

W

W

Q

A

V

L

S

T

F

F

S
|
S

Y

Y

G
|
G

R
|
R

A

A

L

L

Q

Q

A

A

P

S

V

V

L

L

A

N

A

T

W

W

K

Q

G

G

D

K

E

K

S

E

N

N

L

V

E

A

S

K

A

A

R

R

H

E

A

V

L

L

A

L

K

Q

R

R

C

A

L

E

L

A

N

N

G

S

L

L

A

A

R

T

Q

Y

G

G

K

K

Y

Y

active site: D35 (= D24), K147 (= K136), E190 (= E178), E192 (= E180), K232 (= K220), S302 (= S290)
binding N'-[(E)-(2,4-dichlorophenyl)methylidene]-3,4-dihydroxybenzohydrazide: D35 (= D24), K147 (= K136), R149 (= R138)
binding : E36 (= E25), R44 (= R33), E192 (= E180), F253 (≠ E241), V256 (≠ I244), R257 (= R245), R260 (≠ T248), S274 (= S262), G275 (= G263), L292 (≠ M280), G293 (= G281), P294 (= P282), G304 (= G292), R305 (= R293)

2ephD Crystal structure of fructose-bisphosphate aldolase from plasmodium falciparum in complex with trap-tail determined at 2.7 angstrom resolution (see paper)
51% identity, 97% coverage: 4:332/338 of query aligns to 17:346/351 of 2ephD

query
sites
2ephD

D

E

R

E

L

L

R

A

S

T

V

T

A

A

N

Q

A

K

I

L

V

V

T

Q

R

A

E

G

K

K

G

G

V

I

L

L

A

A

D
|
D

E
|
E

S

S

A

T

P

Q

T

T

I

I

R

K

K

K

R
|
R

F

F

D

D

S

N

V

I

G

K

V

L

E

E

S

N

T

T

E

I

E

E

N

N

R

R

R

A

R

S

Y

Y

R

R

E

D

I

L

L

L

F

F

T

G

T

T

A

K

G

G

I

L

E

G

R

K

H

F

I

I

G

S

G

G

V

A

I

I

L

L

F

F

D

E

E

E

T

T

L

L

R

F

Q

Q

S

K

T

N

R

E

D

A

G

G

T

V

P

P

F

M

A

V

R

N

L

L

S

H

D

N

R

E

G

N

I

I

P

P

G

G

I

I

K

K

V

V

D

D

K

K

G

G

A

L

R

V

E

N

L

I

A

P

L

C

Y

T

P

D

G

E

E

E

K

K

I

S

A

T

E

Q

G

G

L

L

D

D

G

G

L

L

R

A

E

E

R

R

L

C

V

K

E

E

Y

Y

R

Y

Q

K

L

A

G

G

A

A

E

R

F

F

A

A

K
|
K

W

W

R
|
R

A

T

V

V

I

L

E

V

I

I

D

D

-

T

G

A

H

K

D

G

M

K

P

P

S

T

P

D

F

L

G

S

I

I

R

H

A

E

N

T

A

A

H

W

A

G

L

L

A

A

R

R

Y

Y

A

A

A

S

L

I

C

C

Q

Q

E

Q

L

N

D

R

I

L

V

V

P

P

I

I

V

V

E
|
E

P

P

E
|
E

V

I

L

L

M

A

D

D

G

G

A

P

H

H

G

S

I

I

D

E

R

V

C

C

E

A

E

V

V

V

T

T

S

Q

G

K

V

V

L

L

Q

S

A

C

V

V

F

F

S

K

E

A

L

L

D

Q

A

E

H

N

R

G

V

V

L

L

F

L

E

E

G

G

M

A

L

L

K
|
K

P

P

N

N

M

M

V

V

I

T

A

A

G

G

K

Y

R

E

C

C

D

T

R

A

C

K

S

T

V

T

E

Q

Q

D

V

V

A

G

E

F

A

L

T

T

I

V

R

R

C

T

M

L

T

R

R

R

Y

T

V

V

P

P

A

P

A

A

V

L

P

P

G

G

I

V

V

V

F

F

L

L

S

S

G

G

Q

Q

S

S

A

E

E

E

D

E

A

A

T

S

D

V

H

N

L

L

N

N

A

S

M

I

N

N

R

A

M

L

G

G

P

P

H

H

P

P

W

W

Q

A

V

L

S

T

F

F

S
|
S

Y

Y

G

G

R
|
R

A

A

L

L

Q
|
Q

A
|
A

P

S

V

V

L

L

A

N

A

T

W

W

K

Q

G

G

D

K

E

K

S

E

N

N

L

V

E

A

S

K

A

A

R

R

H

E

A

V

L

L

A

L

K

Q

R

R

C

A

L

E

L

A

N

N

G

S

L

L

A

A

R

T

Q

Y

G

G

K

K

Y

Y

active site: D37 (= D24), K149 (= K136), E192 (= E178), E194 (= E180), K234 (= K220), S304 (= S290)
binding : E38 (= E25), R46 (= R33), K149 (= K136), R151 (= R138), R307 (= R293), Q310 (= Q296), A311 (= A297)

6rngB Dipeptide gly-pro binds to a glycolytic enzyme fructose bisphosphate aldolase
53% identity, 97% coverage: 4:332/338 of query aligns to 5:332/334 of 6rngB

query
sites
6rngB

D

D

R

E

L

L

R

I

S

A

V

N

A

A

N

A

A

Y

I

I

V

G

T

T

R

P

E

G

K

K

G

G

V

I

L

L

A

A

D
|
D

E

E

S

S

A

T

P

G

T

T

I

I

R

G

K

K

R

R

F

L

D

A

S

S

V

I

G

N

V

V

E

E

S

N

T

V

E

E

E

S

N

N

R

R

R

A

Y

L

R

R

E

E

I

L

L

L

F

F

T

T

A

P

G

G

I

A

E

L

R

P

H

C

I

L

G

S

G

G

V

V

I

I

L

L

F

F

D

E

E

E

T

T

L

L

R

Y

Q

Q

S

K

T

S

R

S

D

D

G

G

T

T

P

P

F

F

A

V

R

D

L

M

L

L

S

K

D

S

R

A

G

G

I

V

I

L

P

P

G

G

I

I

K

K

V

V

D

D

K

K

G

G

A

T

R

V

E

E

L

L

A

A

L

G

Y

T

P

N

G

G

E

E

K

T

I

T

A

T

E

Q

G

G

L

L

D

D

G

G

L

L

R

G

E

D

R

R

L

C

V

K

E

K

Y

Y

R

Y

Q

E

L

A

G

G

A

A

E

R

F

F

A

A

K
|
K

W

W

R

R

A

A

V

V

I

L

E

K

I

I

D

-

G

G

H

V

D

N

M

E

P

P

S

S

P

Q

F

L

G

A

I

I

R

H

A

E

N

N

A

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active site: D25 (= D24), K137 (= K136), E178 (= E178), E180 (= E180), K220 (= K220), S290 (= S290)
binding glycine: G262 (= G263), R293 (= R293)
binding proline: G262 (= G263), R293 (= R293)

Q9SJQ9 Fructose-bisphosphate aldolase 6, cytosolic; AtFBA6; Cytosolic aldolase 2; cAld2; EC 4.1.2.13 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
53% identity, 97% coverage: 4:332/338 of query aligns to 10:337/358 of Q9SJQ9

query
sites
Q9SJQ9

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C68 (≠ H62) modified: S-glutathionyl cysteine; transient
C173 (= C168) modified: S-glutathionyl cysteine; transient; alternate; modified: S-nitrosocysteine; transient; alternate

P05062 Fructose-bisphosphate aldolase B; Liver-type aldolase; EC 4.1.2.13 from Homo sapiens (Human) (see 14 papers)
52% identity, 97% coverage: 6:332/338 of query aligns to 16:343/364 of P05062

query
sites
P05062

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Y

R43 (= R33) mutation to A: Loss of enzymatic activity. Retains the ability to interact with G6PD.
R46 (≠ S36) to W: in HFI; reduced enzymatic activity; dbSNP:rs41281039; mutation to A: Decreases enzymatic activity. Retains the ability to interact with G6PD.
I74 (= I63) to T: in HFI; affects proper folding; dbSNP:rs781023784
K108 (= K97) mutation to A: Decreases enzymatic activity. Retains the ability to interact with G6PD.
C135 (≠ L124) to R: in HFI; America; partial activity
K147 (= K136) mutation to A: Loss of enzymatic activity. Impairs the interaction with G6PD.
W148 (= W137) to R: in one subject with fructose intolerance; rare variant; America; dbSNP:rs118204430
R149 (= R138) mutation to A: Loss of enzymatic activity. Impairs the interaction with G6PD.
A150 (= A139) to P: in HFI; frequent mutation; dbSNP:rs1800546
A175 (= A165) to D: in HFI; frequent mutation; dbSNP:rs76917243
V222 (= V212) to F: in HFI; affects proper folding; dbSNP:rs1554702442
L229 (= L219) to P: in HFI; affects proper folding; dbSNP:rs1554702433
K230 (= K220) mutation to A: Loss of enzymatic activity. Impairs the interaction with G6PD.
L257 (≠ M247) to P: in HFI; Italy; dbSNP:rs764701775
R304 (= R293) to Q: in HFI; 100-fold decrease in catalytic efficiency for substrates F1,6BP and F1P; dbSNP:rs145078268; to W: in HFI; Turkey; 4800-fold decrease in catalytic efficiency for F1,6BP and inactive with F1P; dbSNP:rs555935217; mutation to A: Decreases enzymatic activity. Impairs the interaction with G6PD.
N335 (= N324) to K: in HFI; frequent mutation; dbSNP:rs78340951
A338 (= A327) to V: in HFI; Turkey and South Europe; dbSNP:rs77718928
Y343 (= Y332) to H: in HFI; almost no effect on enzymatic activity at 30 degrees Celsius, but reduced activity at higher temperatures; dbSNP:rs369586696

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

P14223 Fructose-bisphosphate aldolase; PfAldo; 41 kDa antigen; EC 4.1.2.13 from Plasmodium falciparum (see paper)
50% identity, 96% coverage: 4:327/338 of query aligns to 20:344/369 of P14223

query
sites
P14223

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D40 (= D24) mutation to G: Reduces binding to TRAP.
E41 (= E25) mutation to G: Abolishes binding to TRAP.
R49 (= R33) mutation R->D,G: Abolishes binding to TRAP.
K152 (= K136) mutation to D: Severe reduction in the binding to TRAP.
R154 (= R138) mutation to G: Abolishes binding to TRAP.
R310 (= R293) mutation to S: Severe reduction in the binding to TRAP.
Q313 (= Q296) mutation to S: Severe reduction in the binding to TRAP.
A314 (= A297) mutation to G: Reduces binding to TRAP.
L317 (= L300) mutation to D: Abolishes binding to TRAP.

Q91Y97 Fructose-bisphosphate aldolase B; Aldolase 2; Liver-type aldolase; EC 4.1.2.13 from Mus musculus (Mouse)
52% identity, 97% coverage: 6:332/338 of query aligns to 16:343/364 of Q91Y97

query
sites
Q91Y97

L

L

R

S

S

E

V

I

A

A

N

Q

A

R

I

I

V

V

T

A

R

N

E

G

K

K

G

G

V

I

L

L

A

A

D

D

E

E

S

S

A

V

P

G

T

T

I

M

R

G

K

N

R

R

F

L

D

Q

S

R

V

I

G

K

V

V

E

E

S

N

T

T

E

E

N

N

R

R

R

Q

Y

F

R

R

E

E

I

L

L

L

F

F

T

S

T

V

-

D

A

N

G

S

I

I

E

S

R

Q

H

S

I

I

G

G

V

V

I

I

L

L

F

F

D

H

E

E

T

T

L

L

R

Y

Q

Q

S

K

T

D

R

S

D

Q

G

G

T

N

P

L

F

F

A

R

R

N

L

V

L

L

S

K

D

E

R

K

G

G

I

I

I

V

P

V

G

G

I

I

K

K

V

L

D

D

K

Q

G

G

A

G

R

A

E

P

L

L

A

A

L

G

Y

T

P

N

G

K

E

E

K

T

I

T

A

I

E

Q

G

G

L

L

D

D

G

G

L

L

R

S

E

E

R

R

L

C

V

A

E

Q

Y

Y

R

K

Q

K

L

D

G

G

A

V

E

D

F

F

A

G

K

K

W

W

R

R

A

A

V

V

I

L

E

R

I

I

D

-

G

A

H

D

D

Q

M

C

P

P

S

S

P

S

F

L

G

A

I

I

R

Q

A

E

N

N

A

A

H

N

A

A

L

L

A

A

R

R

Y

Y

A

A

A

S

L

I

C

C

Q

Q

E

Q

L

N

D

G

I

L

V

V

P

P

I

I

V

V

E

E

P

P

E

E

V

V

L

L

M

P

D

D

G

G

A

D

H

H

G

D

I

L

D

E

R

H

C

C

E

Q

E

Y

V

V

T

S

S

E

G

K

V

V

L

L

Q

A

A

A

V

V

F

Y

S

K

E

A

L

L

D

N

A

D

H

H

R

H

V

V

L

Y

F

L

E

E

G

G

M

T

L

L

K

K

P

P

N

N

M

M

V

V

I

T

A

A

G

G

K

H

R

A

C

C

D

T

R

K

C

K

S

Y

S

T

V

P

E

E

Q

Q

V

V

A

A

E

M

A

A

T

T

I

V

R

T

C

A

M

L

T

H

R

R

Y

T

V

V

P

P

A

A

V

V

P

P

G

G

I

I

V

C

F

F

L

L

S

S

G

G

Q

M

S

S

A

E

E

E

D

D

A

A

T

T

D

L

H

N

L

L

N

N

A

A

M

I

N

N

R

R

M

C

G

P

-

L

P

P

H

R

P

P

W

W

Q

K

V

L

S

S

F

F

S

S

Y

Y

G

G

R

R

A

A

L

L

Q

Q

A

A

P

S

V

A

L

L

A

A

W

W

K

G

G

G

D

K

E

A

S

A

N

N

L

K

E

K

S

A

A

T

R

Q

H

E

A

A

L

F

A

M

K

K

R

R

C

A

L

M

L

A

N

N

G

C

L

Q

A

A

R

A

Q

Q

G

G

K

Q

Y

Y

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylalanine

P07764 Fructose-bisphosphate aldolase; Aldolase-1; EC 4.1.2.13 from Drosophila melanogaster (Fruit fly) (see 2 papers)
52% identity, 97% coverage: 4:332/338 of query aligns to 14:342/361 of P07764

query
sites
P07764

D

D

R

E

L

L

R

R

S

E

V

I

A

A

N

Q

A

K

I

I

V

V

T

A

R

P

E

G

K

K

G

G

V

I

L

L

A

A

D

D

E

E

S

S

A

G

P

P

T

T

I

M

R

G

K

K

R

R

F

L

D

Q

S

D

V

I

G

G

V

V

E

E

S

N

T

T

E

E

E

D

N

N

R

R

R

A

Y

Y

R

R

E

Q

I

L

L

L

F

F

T

S

T

T

-

D

A

P

G

K

I

L

E

A

R

E

H

N

I

I

G

S

G

G

V

V

I

I

L

L

F

F

D

H

E

E

T

T

L

L

R

Y

Q

Q

S

K

T

A

R

D

D

D

G

G

T

T

P

P

F

F

A

A

R

E

L

I

L

L

S

K

D

K

R

K

G

G

I

I

P

L

G

G

I

I

K

K

V

V

D

D

K

K

G

G

A

V

R

V

E

P

L

L

A

F

L

G

Y

S

P

E

G

D

E

E

K

V

I

T

A

T

E

Q

G

G

L

L

D

D

G

D

L

L

R

A

E

A

R

R

L

C

V

A

E

Q

Y

Y

R

K

Q

K

L

D

G

G

A

C

E

D

F

F

A

A

K

K

W

W

R

R

A

C

V

V

I

L

E

K

I

I

D

-

G

G

H

K

D

N

M

T

P

P

S

S

P

Y

F

Q

G

S

I

I

R

L

A

E

N

N

A

A

H

N

A

V

L

L

A

A

R

R

Y

Y

A

A

A

S

L

I

C

C

Q

Q

E

S

L

Q

D

R

I

I

V

V

P

P

I

I

V

V

E

E

P

P

E

E

V

V

L

L

M

P

D

D

G

G

A

D

H

H

G

D

I

L

D

D

R

R

C

A

E

Q

E

K

V

V

T

T

S

E

G

T

V

V

L

L

Q

A

A

A

V

V

F

Y

S

K

E

A

L

L

D

S

A

D

H

H

R

H

V

V

L

Y

F

L

E

E

G

G

M

T

L

L

K

K

P

P

N

N

M

M

V

V

I

T

A

A

G

G

K

Q

R

S

C

A

D

K

R

K

C

-

S

N

S

T

V

P

E

E

Q

E

V

I

A

A

E

L

A

A

T

T

I

V

R

Q

C

A

M

L

T

R

R

R

Y

T

V

V

P

P

A

A

V

V

P

T

G

G

I

V

V

T

F

F

L

L

S

S

G

G

Q

Q

S

S

A

E

E

E

D

E

A

A

T

T

D

V

H

N

L

L

N

S

A

A

M

I

N

N

R

N

M

V

G

-

P

P

-

L

-

I

H

R

P

P

W

W

Q

A

V

L

S

T

F

F

S

S

Y

Y

G

G

R

R

A

A

L

L

Q

Q

A

A

P

S

V

V

L

L

A

R

A

A

W

W

K

A

G

G

D

K

E

K

S

E

N

N

L

I

E

A

S

A

A

G

R

Q

H

N

A

E

L

L

A

L

K

K

R

R

C

A

L

K

L

A

N

N

G

G

L

D

A

A

R

A

Q

Q

G

G

K

K

Y

Y

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylthreonine

4aldA Human muscle fructose 1,6-bisphosphate aldolase complexed with fructose 1,6-bisphosphate (see paper)
52% identity, 97% coverage: 6:332/338 of query aligns to 15:342/363 of 4aldA

query
sites
4aldA

L

L

R

S

S

D

V

I

A

A

N

H

A

R

I

I

V

V

T

A

R

P

E

G

K

K

G

G

V

I

L

L

A

A

D
|
D

E
|
E

S
|
S

A

T

P

G

T
x
S

I

I

R

A

K

K

R

R

F

L

D

Q

S

S

V

I

G

G

V

T

E

E

S

N

T

T

E

E

N

N

R

R

R

F

Y

Y

R

R

E

Q

I

L

L

L

F

L

T

T

T

A

A

D

G

D

-

R

I

V

E

N

R

P

H

C

I

I

G

G

V

V

I

I

L

L

F

F

D

H

E

E

T

T

L

L

R

Y

Q

Q

S

K

T

A

R

D

D

D

G

G

T

R

P

P

F

F

A

P

R

Q

L

V

L

I

S

K

D

S

R

K

G

G

I

G

I

V

P

V

G

G

I

I

K
|
K

V

V

D

D

K

K

G

G

A

V

R

V

E

P

L

L

A

A

L

G

Y

T

P

N

G

G

E

E

K

T

I

T

A

T

E

Q

G

G

L

L

D

D

G

G

L

L

R

S

E

E

R

R

L

C

V

A

E

Q

Y

Y

R

K

Q

K

L

D

G

G

A

A

E

D

F

F

A

A

K
|
K

W

W

R
|
R

A

C

V

V

I

L

E

K

I

I

D

-

G

G

H

E

D

H

M

T

P

P

S

S

P

A

F

L

G

A

I

I

R

M

A

E

N

N

A

A

H

N

A

V

L

L

A

A

R

R

Y

Y

A

A

A

S

L

I

C

C

Q

Q

E

Q

L

N

D

G

I

I

V

V

P

P

I

I

V

V

E
|
E

P

P

E
|
E

V

I

L

L

M

P

D

D

G

G

A

D

H

H

G

D

I

L

D

K

R

R

C

C

E

Q

E

Y

V

V

T

T

S

E

G

K

V

V

L

L

Q

A

A

A

V

V

F

Y

S

K

E

A

L

L

D

S

A

D

H

H

R

H

V

I

L

Y

F

L

E

E

G

G

M

T

L

L

K
|
K

P

P

N

N

M

M

V

V

I

T

A

P

G

G

K

H

R

A

C

C

D

T

R

Q

C

K

S

F

S

S

V

H

E

E

Q

E

V

I

A

A

E

M

A

A

T

T

I

V

R

T

C

A

M

L

T

R

R

R

Y

T

V

V

P

P

A

P

A

A

V

V

P

T

G

G

I

I

V

T

F

F

L
|
L

S
|
S

G
|
G

G

G

Q

Q

S

S

A

E

E

E

D

E

A

A

T

S

D

I

H

N

L

L

N

N

A

A

M

I

N

N

R

K

M

C

G

-

P

P

-

L

H

K

P

P

W

W

Q

A

V

L

S

T

F

F

S
|
S

Y

Y

G

G

R
|
R

A

A

L

L

Q

Q

A

A

P

S

V

A

L

L

A

K

A

A

W

W

K

G

G

G

D

K

E

K

S

E

N

N

L

L

E

K

S

A

A

A

R

Q

H

E

A

E

L

Y

A

V

K

K

R

R

C

A

L

L

L

A

N

N

G

S

L

L

A

A

R

C

Q

Q

G

G

K

K

Y

Y

active site: D33 (= D24), K146 (= K136), E187 (= E178), E189 (= E180), K229 (= K220), S300 (= S290)
binding 1,6-fructose diphosphate (linear form): E34 (= E25), S35 (= S26), S38 (≠ T29), K107 (= K97), K146 (= K136), R148 (= R138), E187 (= E178), L270 (= L261), S271 (= S262), G272 (= G263), R303 (= R293)

Sites not aligning to the query:

active site: 363

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)
52% identity, 97% coverage: 6:332/338 of query aligns to 16:343/364 of P04075

query
sites
P04075

L

L

R

S

S

D

V

I

A

A

N

H

A

R

I

I

V

V

T

A

R

P

E

G

K

K

G

G

V

I

L

L

A

A

D

D

E

E

S

S

A

T

P

G

T

S

I

I

R

A

K

K

R

R

F

L

D

Q

S

S

V

I

G

G

V

T

E

E

S

N

T

T

E

E

N

N

R

R

R

F

Y

Y

R

R

E

Q

I

L

L

L

F

L

T

T

T

A

A

D

G

D

-

R

I

V

E

N

R

P

H

C

I

I

G

G

V

V

I

I

L

L

F

F

D

H

E

E

T

T

L

L

R

Y

Q

Q

S

K

T

A

R

D

D

D

G

G

T

R

P

P

F

F

A

P

R

Q

L

V

L

I

S
x
K

D

S

R

K

G

G

I

G

I

V

P

V

G

G

I

I

K

K

V

V

D

D

K
|
K

G

G

A

V

R

V

E

P

L

L

A

A

L

G

Y

T

P

N

G

G

E

E

K

T

I

T

A

T

E

Q

G

G

L

L

D
|
D

G

G

L

L

R

S

E

E

R

R

L

C

V

A

E

Q

Y

Y

R

K

Q

K

L

D

G

G

A

A

E

D

F

F

A

A

K
|
K

W

W

R

R

A

C

V

V

I

L

E

K

I

I

D

-

G

G

H

E

D

H

M

T

P

P

S

S

P

A

F

L

G

A

I

I

R

M

A

E

N

N

A

A

H

N

A

V

L

L

A

A

R

R

Y

Y

A

A

A

S

L

I

C

C

Q

Q

E

Q

L

N

D

G

I

I

V

V

P

P

I

I

V

V

E

E

P

P

E

E

V

I

L

L

M

P

D

D

G

G

A

D

H

H

G

D

I

L

D

K

R

R

C

C

E

Q

E

Y

V

V

T

T

S
x
E

G

K

V

V

L

L

Q

A

A

A

V

V

F

Y

S

K

E

A

L

L

D

S

A

D

H

H

R

H

V

I

L

Y

F

L

E

E

G

G

M

T

L

L

K

K

P

P

N

N

M

M

V

V

I

T

A

P

G

G

K

H

R

A

C

C

D

T

R

Q

C

K

S

F

S

S

V

H

E

E

Q

E

V

I

A

A

E

M

A

A

T

T

I

V

R

T

C

A

M

L

T

R

R

R

Y

T

V

V

P

P

A

P

A

A

V

V

P

T

G

G

I

I

V

T

F

F

L

L

S

S

G

G

Q

Q

S

S

A

E

E

E

D

E

A

A

T

S

D

I

H

N

L

L

N

N

A

A

M

I

N

N

R

K

M

C

G

-

P

P

-

L

H

K

P

P

W

W

Q

A

V

L

S

T

F

F

S

S

Y

Y

G

G

R

R

A

A

L

L

Q

Q

A

A

P

S

V

A

L

L

A
x
K

A

A

W

W

K

G

G

G

D

K

E

K

S

E

N

N

L

L

E

K

S

A

A

A

R

Q

H

E

A

E

L

Y

A

V

K

K

R

R

C

A

L

L

L

A

N

N

G

S

L

L

A

A

R

C

Q

Q

G

G

K

K

Y

Y

K99 (≠ S88) modified: N6-(2-hydroxyisobutyryl)lysine
K111 (= K100) modified: N6-malonyllysine; alternate
D129 (= D118) to G: in GSD12; thermolabile; dbSNP:rs121909533
K147 (= K136) modified: N6-(2-hydroxyisobutyryl)lysine
E207 (≠ S197) to K: in GSD12; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity; dbSNP:rs121909534
K312 (≠ A301) modified: N6-malonyllysine

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
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

P00883 Fructose-bisphosphate aldolase A; Muscle-type aldolase; EC 4.1.2.13 from Oryctolagus cuniculus (Rabbit) (see 5 papers)
52% identity, 97% coverage: 6:332/338 of query aligns to 16:343/364 of P00883

query
sites
P00883

L

L

R

S

S

D

V

I

A

A

N

H

A

R

I

I

V

V

T

A

R

P

E

G

K

K

G

G

V

I

L

L

A

A

D

D

E
|
E

S

S

A

T

P

G

T

S

I

I

R

A

K

K

R
|
R

F

L

D

Q

S

S

V

I

G

G

V

T

E

E

S

N

T

T

E

E

N

N

R

R

R

F

Y

Y

R

R

E

Q

I

L

L

L

F

L

T

T

T

A

A

D

G

D

-

R

I

V

E

N

R

P

H

C

I

I

G

G

V

V

I

I

L

L

F

F

D

H

E

E

T

T

L

L

R

Y

Q

Q

S

K

T

A

R

D

D

D

G

G

T

R

P

P

F

F

A

P

R

Q

L

V

L

I

S

K

D

S

R

K

G

G

I

G

I

V

P

V

G

G

I

I

K

K

V

V

D

D

K

K

G

G

A

V

R

V

E

P

L

L

A

A

L

G

Y

T

P

N

G

G

E

E

K

T

I

T

A

T

E

Q

G

G

L

L

D

D

G

G

L

L

R

S

E

E

R

R

L

C

V

A

E

Q

Y

Y

R

K

Q

K

L

D

G

G

A

A

E

D

F

F

A

A

K
|
K

W

W

R

R

A

C

V

V

I

L

E

K

I

I

D

-

G

G

H

E

D

H

M

T

P

P

S

S

P

A

F

L

G

A

I

I

R

M

A

E

N

N

A

A

H

N

A

V

L

L

A

A

R

R

Y

Y

A

A

A

S

L

I

C

C

Q

Q

E

Q

L

N

D

G

I

I

V

V

P

P

I

I

V

V

E
|
E

P

P

E
|
E

V

I

L

L

M

P

D

D

G

G

A

D

H

H

G

D

I

L

D

K

R

R

C

C

E

Q

E

Y

V

V

T

T

S

E

G

K

V

V

L

L

Q

A

A

A

V

V

F

Y

S

K

E

A

L

L

D

S

A

D

H

H

R

H

V

I

L

Y

F

L

E

E

G

G

M

T

L

L

K
|
K

P

P

N

N

M

M

V

V

I

T

A

P

G

G

K

H

R

A

C

C

D

T

R

Q

C

K

S

Y

S

S

V

H

E

E

Q

E

V

I

A

A

E

M

A

A

T

T

I

V

R

T

C

A

M

L

T

R

R

R

Y

T

V

V

P

P

A

P

A

A

V

V

P

T

G

G

I

V

V

T

F

F

L

L

S
|
S

G
|
G

Q

Q

S

S

A

E

E

E

D

E

A

A

T

S

D

I

H

N

L

L

N

N

A

A

M

I

N

N

R

K

M

C

G

-

P

P

-

L

H

K

P

P

W

W

Q

A

V

L

S

T

F

F

S
|
S

Y

Y

G

G

R
|
R

A

A

L

L

Q

Q

A

A

P

S

V

A

L

L

A

K

A

A

W

W

K

G

G

G

D

K

E

K

S

E

N

N

L

L

E

K

S

A

A

A

R

Q

H

E

A

E

L

Y

A

V

K

K

R

R

C

A

L

L

L

A

N

N

G

S

L

L

A

A

R

C

Q

Q

G

G

K

K

Y

Y

E35 (= E25) mutation to A: Reduces activity 14-fold.
R43 (= R33) binding beta-D-fructose 1,6-bisphosphate; mutation to A: Reduces activity 14-fold.
K147 (= K136) mutation to A: Loss of activity.
E188 (= E178) active site, Proton acceptor; mutation to A: Reduces activity over 100-fold.; mutation to Q: Reduces activity over 1000-fold.
E190 (= E180) mutation to Q: Reduces activity 20-fold.
K230 (= K220) active site, Schiff-base intermediate with dihydroxyacetone-P; mutation to M: Loss of activity.
SGG 272:274 (= SGG 262:264) binding beta-D-fructose 1,6-bisphosphate
S301 (= S290) binding beta-D-fructose 1,6-bisphosphate
R304 (= R293) binding beta-D-fructose 1,6-bisphosphate; mutation to A: Reduces activity 400-fold.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
361 modified: Deamidated asparagine; in form beta

1zalA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with partially disordered tagatose-1,6-bisphosphate, a weak competitive inhibitor (see paper)
52% identity, 97% coverage: 6:332/338 of query aligns to 15:342/363 of 1zalA

query
sites
1zalA

L

L

R

S

S

D

V

I

A

A

N

H

A

R

I

I

V

V

T

A

R

P

E

G

K

K

G

G

V

I

L

L

A

A

D
|
D

E

E

S
|
S

A

T

P

G

T

S

I

I

R

A

K

K

R

R

F

L

D

Q

S

S

V

I

G

G

V

T

E

E

S

N

T

T

E

E

N

N

R

R

R

F

Y

Y

R

R

E

Q

I

L

L

L

F

L

T

T

T

A

A

D

G

D

-

R

I

V

E

N

R

P

H

C

I

I

G

G

V

V

I

I

L

L

F

F

D

H

E

E

T

T

L

L

R

Y

Q

Q

S

K

T

A

R

D

D

D

G

G

T

R

P

P

F

F

A

P

R

Q

L

V

L

I

S

K

D

S

R

K

G

G

I

G

I

V

P

V

G

G

I

I

K
|
K

V

V

D

D

K

K

G

G

A

V

R

V

E

P

L

L

A

A

L

G

Y

T

P

N

G

G

E

E

K

T

I

T

A

T

E

Q

G

G

L

L

D

D

G

G

L

L

R

S

E

E

R

R

L

C

V

A

E

Q

Y

Y

R

K

Q

K

L

D

G

G

A

A

E

D

F

F

A

A

K
|
K

W

W

R

R

A

C

V

V

I

L

E

K

I

I

D

-

G

G

H

E

D

H

M

T

P

P

S

S

P

A

F

L

G

A

I

I

R

M

A

E

N

N

A

A

H

N

A

V

L

L

A

A

R

R

Y

Y

A

A

A

S

L

I

C

C

Q

Q

E

Q

L

N

D

G

I

I

V

V

P

P

I

I

V

V

E
|
E

P

P

E
|
E

V

I

L

L

M

P

D

D

G

G

A

D

H

H

G

D

I

L

D

K

R

R

C

C

E

Q

E

Y

V

V

T

T

S

E

G

K

V

V

L

L

Q

A

A

A

V

V

F

Y

S

K

E

A

L

L

D

S

A

D

H

H

R

H

V

I

L

Y

F

L

E

E

G

G

M

T

L

L

K
|
K

P

P

N

N

M

M

V

V

I

T

A

P

G

G

K

H

R

A

C

C

D

T

R

Q

C

K

S

Y

S

S

V

H

E

E

Q

E

V

I

A

A

E

M

A

A

T

T

I

V

R

T

C

A

M

L

T

R

R

R

Y

T

V

V

P

P

A

P

A

A

V

V

P

T

G

G

I

V

V

T

F

F

L

L

S
|
S

G

G

Q

Q

S

S

A

E

E

E

D

E

A

A

T

S

D

I

H

N

L

L

N

N

A

A

M

I

N

N

R

K

M

C

G

-

P

P

-

L

H

K

P

P

W

W

Q

A

V

L

S

T

F

F

S
|
S

Y

Y

G
|
G

R

R

A

A

L

L

Q

Q

A

A

P

S

V

A

L

L

A

K

A

A

W

W

K

G

G

G

D

K

E

K

S

E

N

N

L

L

E

K

S

A

A

A

R

Q

H

E

A

E

L

Y

A

V

K

K

R

R

C

A

L

L

L

A

N

N

G

S

L

L

A

A

R

C

Q

Q

G

G

K

K

Y

Y

active site: D33 (= D24), K146 (= K136), E187 (= E178), E189 (= E180), K229 (= K220), S300 (= S290)
binding phosphate ion: S35 (= S26), K107 (= K97), S271 (= S262), G302 (= G292)

Sites not aligning to the query:

active site: 363

1zajA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with mannitol-1,6-bisphosphate, a competitive inhibitor (see paper)
52% identity, 97% coverage: 6:332/338 of query aligns to 15:342/363 of 1zajA

query
sites
1zajA

L

L

R

S

S

D

V

I

A

A

N

H

A

R

I

I

V

V

T

A

R

P

E

G

K

K

G

G

V

I

L

L

A

A

D
|
D

E

E

S
|
S

A

T

P

G

T
x
S

I

I

R

A

K

K

R

R

F

L

D

Q

S

S

V

I

G

G

V

T

E

E

S

N

T

T

E

E

N

N

R

R

R

F

Y

Y

R

R

E

Q

I

L

L

L

F

L

T

T

T

A

A

D

G

D

-

R

I

V

E

N

R

P

H

C

I

I

G

G

V

V

I

I

L

L

F

F

D

H

E

E

T

T

L

L

R

Y

Q

Q

S

K

T

A

R

D

D

D

G

G

T

R

P

P

F

F

A

P

R

Q

L

V

L

I

S

K

D

S

R

K

G

G

I

G

I

V

P

V

G

G

I

I

K
|
K

V

V

D

D

K

K

G

G

A

V

R

V

E

P

L

L

A

A

L

G

Y

T

P

N

G

G

E

E

K

T

I

T

A

T

E

Q

G

G

L

L

D

D

G

G

L

L

R

S

E

E

R

R

L

C

V

A

E

Q

Y

Y

R

K

Q

K

L

D

G

G

A

A

E

D

F

F

A

A

K
|
K

W

W

R

R

A

C

V

V

I

L

E

K

I

I

D

-

G

G

H

E

D

H

M

T

P

P

S

S

P

A

F

L

G

A

I

I

R

M

A

E

N

N

A

A

H

N

A

V

L

L

A

A

R

R

Y

Y

A

A

A

S

L

I

C

C

Q

Q

E

Q

L

N

D

G

I

I

V

V

P

P

I

I

V

V

E
|
E

P

P

E
|
E

V

I

L

L

M

P

D

D

G

G

A

D

H

H

G

D

I

L

D

K

R

R

C

C

E

Q

E

Y

V

V

T

T

S

E

G

K

V

V

L

L

Q

A

A

A

V

V

F

Y

S

K

E

A

L

L

D

S

A

D

H

H

R

H

V

I

L

Y

F

L

E

E

G

G

M

T

L

L

K
|
K

P

P

N

N

M

M

V

V

I

T

A

P

G

G

K

H

R

A

C

C

D

T

R

Q

C

K

S

Y

S

S

V

H

E

E

Q

E

V

I

A

A

E

M

A

A

T

T

I

V

R

T

C

A

M

L

T

R

R

R

Y

T

V

V

P

P

A

P

A

A

V

V

P

T

G

G

I

V

V

T

F

F

L

L

S
|
S

G
|
G

G

G

Q

Q

S

S

A

E

E

E

D

E

A

A

T

S

D

I

H

N

L

L

N

N

A

A

M

I

N

N

R

K

M

C

G

-

P

P

-

L

H

K

P

P

W

W

Q

A

V

L

S

T

F

F

S
|
S

Y
|
Y

G
|
G

R
|
R

A

A

L

L

Q

Q

A

A

P

S

V

A

L

L

A

K

A

A

W

W

K

G

G

G

D

K

E

K

S

E

N

N

L

L

E

K

S

A

A

A

R

Q

H

E

A

E

L

Y

A

V

K

K

R

R

C

A

L

L

L

A

N

N

G

S

L

L

A

A

R

C

Q

Q

G

G

K

K

Y

Y

active site: D33 (= D24), K146 (= K136), E187 (= E178), E189 (= E180), K229 (= K220), S300 (= S290)
binding d-mannitol-1,6-diphosphate: D33 (= D24), S35 (= S26), S38 (≠ T29), K107 (= K97), K146 (= K136), E187 (= E178), K229 (= K220), S271 (= S262), G272 (= G263), Y301 (= Y291), G302 (= G292), R303 (= R293)

Sites not aligning to the query:

active site: 363

5tlzA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor naphthalene 2,6-bisphosphate (see paper)
52% identity, 97% coverage: 6:332/338 of query aligns to 12:339/346 of 5tlzA

query
sites
5tlzA

L

L

R

S

S

D

V

I

A

A

N

H

A

R

I

I

V

V

T

A

R

P

E

G

K

K

G

G

V

I

L

L

A

A

D
|
D

E

E

S
|
S

A

T

P

G

T
x
S

I

I

R

A

K

K

R

R

F

L

D

Q

S

S

V

I

G

G

V

T

E

E

S

N

T

T

E

E

N

N

R

R

R

F

Y

Y

R

R

E

Q

I

L

L

L

F

L

T

T

T

A

A

D

G

D

-

R

I

V

E

N

R

P

H

C

I

I

G

G

V

V

I

I

L

L

F

F

D

H

E

E

T

T

L

L

R

Y

Q

Q

S

K

T

A

R

D

D

D

G

G

T

R

P

P

F

F

A

P

R

Q

L

V

L

I

S

K

D

S

R

K

G

G

I

G

I

V

P

V

G

G

I

I

K
|
K

V

V

D

D

K

K

G

G

A

V

R

V

E

P

L

L

A

A

L

G

Y

T

P

N

G

G

E

E

K

T

I

T

A

T

E

Q

G

G

L

L

D

D

G

G

L

L

R

S

E

E

R

R

L

C

V

A

E

Q

Y

Y

R

K

Q

K

L

D

G

G

A

A

E

D

F

F

A

A

K
|
K

W

W

R

R

A

C

V

V

I

L

E

K

I

I

D

-

G

G

H

E

D

H

M

T

P

P

S

S

P

A

F

L

G

A

I

I

R

M

A

E

N

N

A

A

H

N

A

V

L

L

A

A

R

R

Y

Y

A

A

A

S

L

I

C

C

Q

Q

E

Q

L

N

D

G

I

I

V

V

P

P

I

I

V

V

E
|
E

P

P

E
|
E

V

I

L

L

M

P

D

D

G

G

A

D

H

H

G

D

I

L

D

K

R

R

C

C

E

Q

E

Y

V

V

T

T

S

E

G

K

V

V

L

L

Q

A

A

A

V

V

F

Y

S

K

E

A

L

L

D

S

A

D

H

H

R

H

V

I

L

Y

F

L

E

E

G

G

M

T

L

L

K
|
K

P

P

N

N

M

M

V

V

I

T

A

P

G

G

K

H

R

A

C

C

D

T

R

Q

C

K

S

Y

S

S

V

H

E

E

Q

E

V

I

A

A

E

M

A

A

T

T

I

V

R

T

C

A

M

L

T

R

R

R

Y

T

V

V

P

P

A

P

A

A

V

V

P

T

G

G

I

V

V

T

F

F

L

L

S
|
S

G
|
G

G

G

Q

Q

S

S

A

E

E

E

D

E

A

A

T

S

D

I

H

N

L

L

N

N

A

A

M

I

N

N

R

K

M

C

G

-

P

P

-

L

H

K

P

P

W

W

Q

A

V

L

S

T

F

F

S
|
S

Y

Y

G
|
G

R
|
R

A

A

L

L

Q

Q

A

A

P

S

V

A

L

L

A

K

A

A

W

W

K

G

G

G

D

K

E

K

S

E

N

N

L

L

E

K

S

A

A

A

R

Q

H

E

A

E

L

Y

A

V

K

K

R

R

C

A

L

L

L

A

N

N

G

S

L

L

A

A

R

C

Q

Q

G

G

K

K

Y

Y

active site: D30 (= D24), K143 (= K136), E184 (= E178), E186 (= E180), K226 (= K220), S297 (= S290)
binding naphthalene-2,6-diyl bis[dihydrogen (phosphate)]: D30 (= D24), S32 (= S26), S35 (≠ T29), K104 (= K97), S268 (= S262), G269 (= G263), G299 (= G292), R300 (= R293)

Sites not aligning to the query:

active site: 346

5tlwA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor 1-phosphate-benzene 4-bisphosphonate (see paper)
52% identity, 97% coverage: 6:332/338 of query aligns to 15:342/349 of 5tlwA

query
sites
5tlwA

L

L

R

S

S

D

V

I

A

A

N

H

A

R

I

I

V

V

T

A

R

P

E

G

K

K

G

G

V

I

L

L

A

A

D
|
D

E

E

S
|
S

A

T

P

G

T
x
S

I

I

R

A

K

K

R

R

F

L

D

Q

S

S

V

I

G

G

V

T

E

E

S

N

T

T

E

E

N

N

R

R

R

F

Y

Y

R

R

E

Q

I

L

L

L

F

L

T

T

T

A

A

D

G

D

-

R

I

V

E

N

R

P

H

C

I

I

G

G

V

V

I

I

L

L

F

F

D

H

E

E

T

T

L

L

R

Y

Q

Q

S

K

T

A

R

D

D

D

G

G

T

R

P

P

F

F

A

P

R

Q

L

V

L

I

S

K

D

S

R

K

G

G

I

G

I

V

P

V

G

G

I

I

K
|
K

V

V

D

D

K

K

G

G

A

V

R

V

E

P

L

L

A

A

L

G

Y

T

P

N

G

G

E

E

K

T

I

T

A

T

E

Q

G

G

L

L

D

D

G

G

L

L

R

S

E

E

R

R

L

C

V

A

E

Q

Y

Y

R

K

Q

K

L

D

G

G

A

A

E

D

F

F

A

A

K
|
K

W

W

R
|
R

A

C

V

V

I

L

E

K

I

I

D

-

G

G

H

E

D

H

M

T

P

P

S

S

P

A

F

L

G

A

I

I

R

M

A

E

N

N

A

A

H

N

A

V

L

L

A

A

R

R

Y

Y

A

A

A

S

L

I

C

C

Q

Q

E

Q

L

N

D

G

I

I

V

V

P

P

I

I

V

V

E
|
E

P

P

E
|
E

V

I

L

L

M

P

D

D

G

G

A

D

H

H

G

D

I

L

D

K

R

R

C

C

E

Q

E

Y

V

V

T

T

S

E

G

K

V

V

L

L

Q

A

A

A

V

V

F

Y

S

K

E

A

L

L

D

S

A

D

H

H

R

H

V

I

L

Y

F

L

E

E

G

G

M

T

L

L

K
|
K

P

P

N

N

M

M

V

V

I

T

A

P

G

G

K

H

R

A

C

C

D

T

R

Q

C

K

S

Y

S

S

V

H

E

E

Q

E

V

I

A

A

E

M

A

A

T

T

I

V

R

T

C

A

M

L

T

R

R

R

Y

T

V

V

P

P

A

P

A

A

V

V

P

T

G

G

I

V

V

T

F

F

L

L

S

S

G

G

Q

Q

S

S

A

E

E

E

D

E

A

A

T

S

D

I

H

N

L

L

N

N

A

A

M

I

N

N

R

K

M

C

G

-

P

P

-

L

H

K

P

P

W

W

Q

A

V

L

S

T

F

F

S
|
S

Y

Y

G

G

R
|
R

A

A

L

L

Q

Q

A

A

P

S

V

A

L

L

A

K

A

A

W

W

K

G

G

G

D

K

E

K

S

E

N

N

L

L

E

K

S

A

A

A

R

Q

H

E

A

E

L

Y

A

V

K

K

R

R

C

A

L

L

L

A

N

N

G

S

L

L

A

A

R

C

Q

Q

G

G

K

K

Y

Y

active site: D33 (= D24), K146 (= K136), E187 (= E178), E189 (= E180), K229 (= K220), S300 (= S290)
binding {[4-(phosphonooxy)phenyl]methylene}bis(phosphonic acid): S35 (= S26), S38 (≠ T29), K107 (= K97), K146 (= K136), R148 (= R138), R303 (= R293)

Sites not aligning to the query:

active site: 349

5tleA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor 2-phosphate-naphthalene 6-bisphosphonate (see paper)
52% identity, 97% coverage: 6:332/338 of query aligns to 15:342/349 of 5tleA

query
sites
5tleA

L

L

R

S

S

D

V

I

A

A

N

H

A

R

I

I

V

V

T

A

R

P

E

G

K

K

G

G

V

I

L

L

A

A

D
|
D

E

E

S
|
S

A

T

P

G

T
x
S

I

I

R

A

K

K

R

R

F

L

D

Q

S

S

V

I

G

G

V

T

E

E

S

N

T

T

E

E

N

N

R

R

R

F

Y

Y

R

R

E

Q

I

L

L

L

F

L

T

T

T

A

A

D

G

D

-

R

I

V

E

N

R

P

H

C

I

I

G

G

V

V

I

I

L

L

F

F

D

H

E

E

T

T

L

L

R

Y

Q

Q

S

K

T

A

R

D

D

D

G

G

T

R

P

P

F

F

A

P

R

Q

L

V

L

I

S

K

D

S

R

K

G

G

I

G

I

V

P

V

G

G

I

I

K
|
K

V

V

D

D

K

K

G

G

A

V

R

V

E

P

L

L

A

A

L

G

Y

T

P

N

G

G

E

E

K

T

I

T

A

T

E

Q

G

G

L

L

D

D

G

G

L

L

R

S

E

E

R

R

L

C

V

A

E

Q

Y

Y

R

K

Q

K

L

D

G

G

A

A

E

D

F

F

A

A

K
|
K

W

W

R

R

A

C

V

V

I

L

E

K

I

I

D

-

G

G

H

E

D

H

M

T

P

P

S

S

P

A

F

L

G

A

I

I

R

M

A

E

N

N

A

A

H

N

A

V

L

L

A

A

R

R

Y

Y

A

A

A

S

L

I

C

C

Q

Q

E

Q

L

N

D

G

I

I

V

V

P

P

I

I

V

V

E
|
E

P

P

E
|
E

V

I

L

L

M

P

D

D

G

G

A

D

H

H

G

D

I

L

D

K

R

R

C

C

E

Q

E

Y

V

V

T

T

S

E

G

K

V

V

L

L

Q

A

A

A

V

V

F

Y

S

K

E

A

L

L

D

S

A

D

H

H

R

H

V

I

L

Y

F

L

E

E

G

G

M

T

L

L

K
|
K

P

P

N

N

M

M

V

V

I

T

A

P

G

G

K

H

R

A

C

C

D

T

R

Q

C

K

S

Y

S

S

V

H

E

E

Q

E

V

I

A

A

E

M

A

A

T

T

I

V

R

T

C

A

M

L

T

R

R

R

Y

T

V

V

P

P

A

P

A

A

V

V

P

T

G

G

I

V

V

T

F

F

L
|
L

S

S

G
|
G

G

G

Q

Q

S

S

A

E

E

E

D

E

A

A

T

S

D

I

H

N

L

L

N

N

A

A

M

I

N

N

R

K

M

C

G

-

P

P

-

L

H

K

P

P

W

W

Q

A

V

L

S

T

F

F

S
|
S

Y

Y

G
|
G

R
|
R

A

A

L

L

Q

Q

A

A

P

S

V

A

L

L

A

K

A

A

W

W

K

G

G

G

D

K

E

K

S

E

N

N

L

L

E

K

S

A

A

A

R

Q

H

E

A

E

L

Y

A

V

K

K

R

R

C

A

L

L

L

A

N

N

G

S

L

L

A

A

R

C

Q

Q

G

G

K

K

Y

Y

active site: D33 (= D24), K146 (= K136), E187 (= E178), E189 (= E180), K229 (= K220), S300 (= S290)
binding {[6-(phosphonooxy)naphthalen-2-yl]methylene}bis(phosphonic acid): D33 (= D24), S35 (= S26), S38 (≠ T29), K107 (= K97), K229 (= K220), L270 (= L261), G272 (= G263), G302 (= G292), R303 (= R293)

Sites not aligning to the query:

active site: 349

3tu9A Crystal structure of rabbit muscle aldolase bound with 5-o-methyl mannitol 1,6-phosphate (see paper)
52% identity, 97% coverage: 6:332/338 of query aligns to 15:342/349 of 3tu9A

query
sites
3tu9A

L

L

R

S

S

D

V

I

A

A

N

H

A

R

I

I

V

V

T

A

R

P

E

G

K

K

G

G

V

I

L

L

A
|
A

A

A

D
|
D

E
|
E

S
|
S

A

T

P

G

T
x
S

I

I

R

A

K

K

R

R

F

L

D

Q

S

S

V

I

G

G

V

T

E

E

S

N

T

T

E

E

N

N

R

R

R

F

Y

Y

R

R

E

Q

I

L

L

L

F

L

T

T

T

A

A

D

G

D

-

R

I

V

E

N

R

P

H

C

I

I

G

G

V

V

I

I

L

L

F

F

D

H

E

E

T

T

L

L

R

Y

Q

Q

S

K

T

A

R

D

D

D

G

G

T

R

P

P

F

F

A

P

R

Q

L

V

L

I

S

K

D

S

R

K

G

G

I

G

I

V

P

V

G

G

I

I

K
|
K

V

V

D

D

K

K

G

G

A

V

R

V

E

P

L

L

A

A

L

G

Y

T

P

N

G

G

E

E

K

T

I

T

A

T

E

Q

G

G

L

L

D

D

G

G

L

L

R

S

E

E

R

R

L

C

V

A

E

Q

Y

Y

R

K

Q

K

L

D

G

G

A

A

E

D

F

F

A

A

K
|
K

W

W

R

R

A

C

V

V

I

L

E

K

I

I

D

-

G

G

H

E

D

H

M

T

P

P

S

S

P

A

F

L

G

A

I

I

R

M

A

E

N

N

A

A

H

N

A

V

L

L

A

A

R

R

Y

Y

A

A

A

S

L

I

C

C

Q

Q

E

Q

L

N

D

G

I

I

V

V

P

P

I

I

V

V

E
|
E

P

P

E
|
E

V

I

L

L

M

P

D

D

G

G

A

D

H

H

G

D

I

L

D

K

R

R

C

C

E

Q

E

Y

V

V

T

T

S

E

G

K

V

V

L

L

Q

A

A

A

V

V

F

Y

S

K

E

A

L

L

D

S

A

D

H

H

R

H

V

I

L

Y

F

L

E

E

G

G

M

T

L

L

K
|
K

P

P

N

N

M

M

V

V

I

T

A

P

G

G

K

H

R

A

C

C

D

T

R

Q

C

K

S

Y

S

S

V

H

E

E

Q

E

V

I

A

A

E

M

A

A

T

T

I

V

R

T

C

A

M

L

T

R

R

R

Y

T

V

V

P

P

A

P

A

A

V

V

P

T

G

G

I

V

V

T

F

F

L

L

S
|
S

G
|
G

G

G

Q

Q

S

S

A

E

E

E

D

E

A

A

T

S

D

I

H

N

L

L

N

N

A

A

M

I

N

N

R

K

M

C

G

-

P

P

-

L

H

K

P

P

W

W

Q

A

V

L

S

T

F

F

S
|
S

Y
|
Y

G
|
G

R
|
R

A

A

L

L

Q

Q

A

A

P

S

V

A

L

L

A

K

A

A

W

W

K

G

G

G

D

K

E

K

S

E

N

N

L

L

E

K

S

A

A

A

R

Q

H

E

A

E

L

Y

A

V

K

K

R

R

C

A

L

L

L

A

N

N

G

S

L

L

A

A

R

C

Q

Q

G

G

K

K

Y

Y

active site: D33 (= D24), K146 (= K136), E187 (= E178), E189 (= E180), K229 (= K220), S300 (= S290)
binding 2-O-methyl-1,6-di-O-phosphono-D-mannitol: A31 (= A22), D33 (= D24), E34 (= E25), S35 (= S26), S38 (≠ T29), K107 (= K97), K146 (= K136), E187 (= E178), K229 (= K220), S271 (= S262), G272 (= G263), Y301 (= Y291), G302 (= G292), R303 (= R293)

Sites not aligning to the query:

active site: 349

Query Sequence

>WP_012466828.1 NCBI__GCF_000020465.1:WP_012466828.1
MDNDRLRSVANAIVTREKGVLAADESAPTIRKRFDSVGVESTEENRRRYREILFTTAGIE
RHIGGVILFDETLRQSTRDGTPFARLLSDRGIIPGIKVDKGARELALYPGEKIAEGLDGL
RERLVEYRQLGAEFAKWRAVIEIDGHDMPSPFGIRANAHALARYAALCQELDIVPIVEPE
VLMDGAHGIDRCEEVTSGVLQAVFSELDAHRVLFEGMLLKPNMVIAGKRCDRCSSVEQVA
EATIRCMTRYVPAAVPGIVFLSGGQSAEDATDHLNAMNRMGPHPWQVSFSYGRALQAPVL
AAWKGDESNLESARHALAKRCLLNGLARQGKYARYMEA

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