SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_110804301.1 NCBI__GCF_003217355.1:WP_110804301.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

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, 89% coverage: 1:262/294 of query aligns to 48:331/391 of Q9ZU52

query
sites
Q9ZU52

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Sites not aligning to the query:

387 modified: N6,N6,N6-trimethyllysine

Q8I8I2 Fructose-bisphosphate aldolase 1; TgALD; TgALD1; TgAldolase; EC 4.1.2.13 from Toxoplasma gondii (see 2 papers)
30% identity, 68% coverage: 1:201/294 of query aligns to 12:214/363 of Q8I8I2

query
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Q8I8I2

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D34 (= D20) binding dihydroxyacetone phosphate; mutation to A: Abolishes enzymatic activity. Reduces ACT1 binding. Slightly reduces MIC2 binding.
E35 (≠ Q21) mutation to A: Reduces enzymatic activity. Enhances MIC2 binding.
S36 (= S22) binding D-glyceraldehyde 3-phosphate
T39 (≠ S25) binding D-glyceraldehyde 3-phosphate
K42 (= K28) 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 (≠ A29) 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 (= K102) binding D-glyceraldehyde 3-phosphate; mutation to A: Abolishes enzymatic activity. Reduces MIC2 binding.
K146 (= K139) binding dihydroxyacetone phosphate; mutation to A: Abolishes enzymatic activity. Reduces MIC2 binding.
R148 (= R141) mutation to A: Abolishes enzymatic activity. Reduces ACT1 binding. Reduces MIC2 binding.
E189 (= E176) binding D-glyceraldehyde 3-phosphate

Sites not aligning to the query:

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)
30% identity, 68% coverage: 1:201/294 of query aligns to 12:214/350 of 5tklA

query
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5tklA

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active site: D34 (= D20), K146 (= K139), E189 (= E176), E191 (= E178)
binding glyceraldehyde-3-phosphate: S36 (= S22), T39 (≠ S25), K107 (= K102), K146 (= K139), R148 (= R141), E189 (= E176)
binding 1,6-di-O-phosphono-D-fructose: A32 (= A17), D34 (= D20), S36 (= S22), T39 (≠ S25), K107 (= K102), K146 (= K139), R148 (= R141), E189 (= E176)

Sites not aligning to the query:

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

Q9SJU4 Fructose-bisphosphate aldolase 1, chloroplastic; AtFBA1; EC 4.1.2.13 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 89% coverage: 1:263/294 of query aligns to 56:342/399 of Q9SJU4

query
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Q9SJU4

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Sites not aligning to the query:

1:48 modified: transit peptide, Chloroplast
395 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, 89% coverage: 1:263/294 of query aligns to 55:341/398 of Q944G9

query
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Q944G9

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M

A

V

T

D

Y

V

L

L

W

V

E

E

K

Q

R

N

G

-

V

I

V

V

P

P

F

G

L

I

K

K

I

V

D

D

K

K

G

G

L

L

-

V

-

P

-

L

-

V

-

G

E

S

E

N

K

E

N

S

G

W

C

C

Q

Q

M

-

L

-

K

-

A

-

M

-

P

-

T

G

L

L

D

D

A

G

L

L

L

S

E

S

R

R

A

T

A

A

-

A

-

Y

E

Q

A

Q

G

G

I

A

F

R

G

F

T

A

K

K

E

W

R

R

S

T

V

V

I

V

S

S

A

I

A

-

D

-

P

P

M

N

G

G

I

P

A

S

S

A

V

L

V

A

A

V

Q

K

Q

E

F

A

E

A

V

W

G

G

E

L

Q

A

V

R

L

Y

G

A

A

A

-

I

-

S

-

Q

-

D

-

S

G

G

M

L

V

V

P

P

I

I

L

V

E

E

P

P

E

E

V

I

-

L

-

D

-

G

-

E

-

H

-

D

-

I

-

D

-

R

T

T

I

Y

S

D

I

V

A

A

D

E

K

K

I

V

D

W

A

A

E

E

A

V

M

F

L

F

R

-

D

-

A

-

L

Y

L

L

A

A

G

Q

L

N

E

N

T

V

V

M

S

F

S

E

P

G

V

I

M

L

L

L

K

K

L

P

S

S

L

M

P

V

T

T

-

P

-

G

-

A

-

E

-

S

-

K

-

D

-

R

-

A

-

T

-

P

-

E

-

Q

I

V

D

A

N

A

F

Y

Y

T

L

L

P

K

L

L

V

L

E

R

H

N

-

R

-

V

-

P

P

P

N

A

V

V

I

P

K

G

V

I

V

M

A

F

L

L

S

S

G

G

Y

Q

A

S

R

E

N

V

D

E

A

A

N

T

A

L

I

N

L

L

-

N

-

A

-

M

-

N

-

Q

A

A

R

P

N

N

K

P

G

W

M

H

I

V

A

S

-

F

S

S

F

Y

S

A

R

R

A

A

L

L

Sites not aligning to the query:

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

6rngB Dipeptide gly-pro binds to a glycolytic enzyme fructose bisphosphate aldolase
29% identity, 64% coverage: 12:199/294 of query aligns to 18:201/334 of 6rngB

query
sites
6rngB

G

G

E

K

G

G

F

I

I

L

A

A

L

-

D
|
D

Q

E

S

S

G

T

G

G

S

T

T

I

P

G

K

K

A

-

L

-

R

R

L

L

Y

A

G

S

I

I

T

N

-

V

E

E

D

N

A

V

Y

E

S

S

N

N

E

R

T

R

E

A

M

L

Y

R

D

E

L

L

I

L

H

F

A

T

M

T

R

P

A

G

R

A

I

L

I

P

K

C

S

L

S

S

A

-

F

-

T

-

G

-

D

-

K

-

V

-

G

G

A

V

I

I

L

L

F

F

E

E

Q

E

T

T

M

L

-

Y

D

Q

R

K

D

S

I

S

D

D

G

G

I

T

P

P

T

F

A

V

T

D

Y

M

L

L

W

-

E

K

K

S

R

A

G

G

V

V

V

L

P

P

F

G

L

I

K

K

I

V

D

D

K

K

G

G

L

T

E

V

E

E

-

L

-

A

E

G

K

T

N

N

G

G

C

E

Q

T

M

T

L

T

K

Q

A

G

M

L

P

D

T

G

L

L

D

G

A

D

L

R

L

C

E

K

R

K

A

Y

E

E

A

A

G

G

I

A

F

R

G

F

T

A

K
|
K

E

W

R

R

S

A

V

V

I

L

S

K

A

-

D

-

P

-

M

I

G

G

I

V

A

N

S

E

V

-

A

P

Q

S

Q

Q

F

L

E

A

V

I

G

H

E

E

Q

N

V

A

L

Y

G

G

-

L

-

A

-

R

-

Y

-

A

-

V

-

I

-

C

-

Q

-

E

A

N

G

G

M

L

V

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

T

L

I

V

S

D

I

G

A

S

D

H

K

D

I

I

D

Q

A

K

E

C

A

A

M

A

L

V

R

T

D

E

A

R

L

V

L

L

A

A

active site: D25 (= D20), K137 (= K139), E178 (= E176), E180 (= E178)

Sites not aligning to the query:

Q9SJQ9 Fructose-bisphosphate aldolase 6, cytosolic; AtFBA6; Cytosolic aldolase 2; cAld2; EC 4.1.2.13 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 64% coverage: 12:199/294 of query aligns to 23:206/358 of Q9SJQ9

query
sites
Q9SJQ9

G

G

E

K

G

G

F

I

I

L

A

A

L

-

D

D

Q

E

S

S

G

T

G

G

S

T

T

I

P

G

K

K

A

-

L

-

R

R

L

L

Y

A

G

S

I

I

T

N

-

V

E

E

D

N

A

V

Y

E

S

S

N

N

E

R

T

R

E

A

M

L

Y

R

D

E

L

L

I

L

H

F

A

T

M

T

R

P

A

G

R

A

I

L

I

P

K
x
C

S

L

S

S

A

-

F

-

T

-

G

-

D

-

K

-

V

-

G

G

A

V

I

I

L

L

F

F

E

E

Q

E

T

T

M

L

-

Y

D

Q

R

K

D

S

I

S

D

D

G

G

I

T

P

P

T

F

A

V

T

D

Y

M

L

L

W

-

E

K

K

S

R

A

G

G

V

V

V

L

P

P

F

G

L

I

K

K

I

V

D

D

K

K

G

G

L

T

E

V

E

E

-

L

-

A

E

G

K

T

N

N

G

G

C

E

Q

T

M

T

L

T

K

Q

A

G

M

L

P

D

T

G

L

L

D

G

A

D

L

R

L

C

E

K

R

K

A

Y

E

E

A

A

G

G

I

A

F

R

G

F

T

A

K

K

E

W

R

R

S

A

V

V

I

L

S

K

A

-

D

-

P

-

M

I

G

G

I

V

A

N

S

E

V

-

A

P

Q

S

Q

Q

F

L

E

A

V

I

G

H

E

E

Q

N

V

A

L

Y

G

G

-

L

-

A

-

R

-

Y

-

A

-

V

-

I

-
x
C

-

Q

-

E

A

N

G

G

M

L

V

V

P

P

I

I

L

V

E

E

P

P

E

E

V

I

T

L

I

V

S

D

I

G

A

S

D

H

K

D

I

I

D

Q

A

K

E

C

A

A

M

A

L

V

R

T

D

E

A

R

L

V

L

L

A

A

C68 (≠ K59) modified: S-glutathionyl cysteine; transient
C173 (vs. gap) modified: S-glutathionyl cysteine; transient; alternate; modified: S-nitrosocysteine; transient; alternate

2ephD Crystal structure of fructose-bisphosphate aldolase from plasmodium falciparum in complex with trap-tail determined at 2.7 angstrom resolution (see paper)
27% identity, 68% coverage: 1:199/294 of query aligns to 19:215/351 of 2ephD

query
sites
2ephD

M

L

A

A

K

T

T

T

M

A

M

Q

E

K

H

L

M

V

R

Q

K

A

G

G

E

K

G

G

F

I

I

L

A

A

L

-

D
|
D

Q
x
E

S

S

G

T

G

Q

S

T

T

I

P

K

K

K

A

-

L

-

R
|
R

L

F

Y

D

G

N

I

I

T

K

-

L

E

E

D

N

A

T

Y

I

S

E

N

N

E

R

T

A

E

S

M

Y

Y

R

D

D

L

L

I

L

H

F

A

G

M

T

R

K

A

G

R

-

I

-

K

-

S

-

A

-

F

-

T

L

G

G

D

K

K

F

V

I

V

S

G

G

A

A

I

I

L

L

F

F

E

E

Q

E

T

T

M

L

-

F

D

Q

R

K

D

N

I

E

D

A

G

G

I

V

P

P

T

M

A

V

T

N

Y

L

L

L

W

-

E

H

K

N

R

E

G

N

V

I

P

P

F

G

L

I

K

K

I

V

D

D

K

K

G

G

L

L

-

V

-

N

-

I

-

P

-

C

-

T

E

D

E

E

K

-

N

-

G

-

C

-

Q

-

M

-

L

-

K

K

A

S

M

T

P

Q

T

G

L

L

D

D

A

G

L

L

L

A

E

E

R

R

A

C

A

K

E

E

-

Y

-

K

A

A

G

G

I

A

F

R

G

F

T

A

K
|
K

E

W

R
|
R

S

T

V

V

I

L

-

V

-

I

-

D

-

T

S

A

A

K

A

G

D

K

P

P

M

T

G

D

I

L

-

S

-

I

-

H

-

E

-

T

A

A

S

W

V

G

V

L

A

A

Q

R

Q

Y

F

A

E

S

V

I

G

C

E

Q

Q

Q

V

-

L

-

G

-

A

N

G

R

M

L

V

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

T

L

I

A

S

D

I

G

A

P

D

H

K

S

I

I

D

E

A

V

E

C

A

A

M

V

L

V

R

T

D

Q

A

K

L

V

L

L

A

S

active site: D37 (= D20), K149 (= K139), E192 (= E176), E194 (= E178)
binding : E38 (≠ Q21), R46 (= R31), K149 (= K139), R151 (= R141)

Sites not aligning to the query:

active site: 234, 304
binding : 307, 310, 311

P14223 Fructose-bisphosphate aldolase; PfAldo; 41 kDa antigen; EC 4.1.2.13 from Plasmodium falciparum (see paper)
27% identity, 68% coverage: 1:199/294 of query aligns to 22:218/369 of P14223

query
sites
P14223

M

L

A

A

K

T

T

T

M

A

M

Q

E

K

H

L

M

V

R

Q

K

A

G

G

E

K

G

G

F

I

I

L

A

A

L

-

D
|
D

Q
x
E

S

S

G

T

G

Q

S

T

T

I

P

K

K

K

A

-

L

-

R
|
R

L

F

Y

D

G

N

I

I

T

K

-

L

E

E

D

N

A

T

Y

I

S

E

N

N

E

R

T

A

E

S

M

Y

Y

R

D

D

L

L

I

L

H

F

A

G

M

T

R

K

A

G

R

-

I

-

K

-

S

-

A

-

F

-

T

L

G

G

D

K

K

F

V

I

V

S

G

G

A

A

I

I

L

L

F

F

E

E

Q

E

T

T

M

L

-

F

D

Q

R

K

D

N

I

E

D

A

G

G

I

V

P

P

T

M

A

V

T

N

Y

L

L

L

W

-

E

H

K

N

R

E

G

N

V

I

P

P

F

G

L

I

K

K

I

V

D

D

K

K

G

G

L

L

-

V

-

N

-

I

-

P

-

C

-

T

E

D

E

E

K

-

N

-

G

-

C

-

Q

-

M

-

L

-

K

K

A

S

M

T

P

Q

T

G

L

L

D

D

A

G

L

L

L

A

E

E

R

R

A

C

A

K

E

E

-

Y

-

K

A

A

G

G

I

A

F

R

G

F

T

A

K
|
K

E

W

R
|
R

S

T

V

V

I

L

-

V

-

I

-

D

-

T

S

A

A

K

A

G

D

K

P

P

M

T

G

D

I

L

-

S

-

I

-

H

-

E

-

T

A

A

S

W

V

G

V

L

A

A

Q

R

Q

Y

F

A

E

S

V

I

G

C

E

Q

Q

Q

V

-

L

-

G

-

A

N

G

R

M

L

V

V

P

P

I

I

L

V

E

E

P

P

E

E

V

I

T

L

I

A

S

D

I

G

A

P

D

H

K

S

I

I

D

E

A

V

E

C

A

A

M

V

L

V

R

T

D

Q

A

K

L

V

L

L

A

S

D40 (= D20) mutation to G: Reduces binding to TRAP.
E41 (≠ Q21) mutation to G: Abolishes binding to TRAP.
R49 (= R31) mutation R->D,G: Abolishes binding to TRAP.
K152 (= K139) mutation to D: Severe reduction in the binding to TRAP.
R154 (= R141) mutation to G: Abolishes binding to TRAP.

Sites not aligning to the query:

310 R→S: Severe reduction in the binding to TRAP.
313 Q→S: Severe reduction in the binding to TRAP.
314 A→G: Reduces binding to TRAP.
317 L→D: Abolishes binding to TRAP.

4tr9A Ternary co-crystal structure of fructose-bisphosphate aldolase from plasmodium falciparum in complex with trap and a small molecule inhibitor (see paper)
27% identity, 68% coverage: 1:199/294 of query aligns to 17:213/347 of 4tr9A

query
sites
4tr9A

M

L

A

A

K

T

T

T

M

A

M

Q

E

K

H

L

M

V

R

Q

K

A

G

G

E

K

G

G

F

I

I

L

A

A

L

-

D
|
D

Q
x
E

S

S

G

T

G

Q

S

T

T

I

P

K

K

K

A

-

L

-

R
|
R

L

F

Y

D

G

N

I

I

T

K

-

L

E

E

D

N

A

T

Y

I

S

E

N

N

E

R

T

A

E

S

M

Y

Y

R

D

D

L

L

I

L

H

F

A

G

M

T

R

K

A

G

R

-

I

-

K

-

S

-

A

-

F

-

T

L

G

G

D

K

K

F

V

I

V

S

G

G

A

A

I

I

L

L

F

F

E

E

Q

E

T

T

M

L

-

F

D

Q

R

K

D

N

I

E

D

A

G

G

I

V

P

P

T

M

A

V

T

N

Y

L

L

L

W

-

E

H

K

N

R

E

G

N

V

I

P

P

F

G

L

I

K

K

I

V

D

D

K

K

G

G

L

L

-

V

-

N

-

I

-

P

-

C

-

T

E

D

E

E

K

-

N

-

G

-

C

-

Q

-

M

-

L

-

K

K

A

S

M

T

P

Q

T

G

L

L

D

D

A

G

L

L

L

A

E

E

R

R

A

C

A

K

E

E

-

Y

-

K

A

A

G

G

I

A

F

R

G

F

T

A

K
|
K

E

W

R
|
R

S

T

V

V

I

L

-

V

-

I

-

D

-

T

S

A

A

K

A

G

D

K

P

P

M

T

G

D

I

L

-

S

-

I

-

H

-

E

-

T

A

A

S

W

V

G

V

L

A

A

Q

R

Q

Y

F

A

E

S

V

I

G

C

E

Q

Q

Q

V

-

L

-

G

-

A

N

G

R

M

L

V

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

T

L

I

A

S

D

I

G

A

P

D

H

K

S

I

I

D

E

A

V

E

C

A

A

M

V

L

V

R

T

D

Q

A

K

L

V

L

L

A

S

active site: D35 (= D20), K147 (= K139), E190 (= E176), E192 (= E178)
binding N'-[(E)-(2,4-dichlorophenyl)methylidene]-3,4-dihydroxybenzohydrazide: D35 (= D20), K147 (= K139), R149 (= R141)
binding : E36 (≠ Q21), R44 (= R31), E192 (= E178)

Sites not aligning to the query:

active site: 232, 302
binding : 253, 256, 257, 260, 274, 275, 292, 293, 294, 304, 305

2qdhA Fructose-1,6-bisphosphate aldolase from leishmania mexicana in complex with mannitol-1,6-bisphosphate, a competitive inhibitor (see paper)
29% identity, 60% coverage: 12:188/294 of query aligns to 36:209/366 of 2qdhA

query
sites
2qdhA

G

G

E

K

G

G

F

L

I

L

A

A

L

-

D
|
D

Q

E

S
|
S

G

I

G

G

S
|
S

T

C

P

T

K

K

A

R

L

F

R

Q

L

P

Y

I

G

G

I

L

T

-

E

-

D

-

A

-

Y

-

S

S

N

N

E

T

T

E

E

E

M

H

Y

R

D

-

L

-

I

-

H

R

A

Q

M

Y

R

R

A

A

R

L

I

M

I

L

K

E

S

A

S

E

A

G

F

F

T

E

G

-

D

Q

K

Y

V

I

V

S

G

G

A

V

I

I

L

L

F

H

E

D

Q

E

T

T

M

V

D

G

R

Q

D

K

I

A

D

S

G

N

I

G

P

Q

T

T

A

F

T

P

Y

E

L

Y

W

L

E

T

K

A

R

R

G

G

V

V

P

P

F

G

L

I

K

K

I

T

D

D

K

M

G

G

L

L

E

C

E

P

E

L

K

L

N

E

G

G

C

A

Q

E

M

G

L

E

K

Q

A

M

M

T

P

E

T

G

L

L

D

D

A

G

L

Y

L

V

E

K

R

R

A

A

A

S

-

A

-

Y

E

K

A

K

G

G

I

C

F

R

G

F

T

C

K
|
K

E

W

R
|
R

S

N

V

V

I

Y

S

K

A

I

A

Q

D

N

P

-

M

-

G

G

I

T

A

V

S

S

V

E

V

S

A

A

Q

V

Q

R

F

F

E

N

V

A

G

-

E

-

Q

E

V

T

L

L

G

A

-

R

-

Y

-

A

-

I

-

L

-

S

-

Q

-

M

A

S

G

G

M

L

V

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

V

T

M

I

I

S

D

I

G

A

K

D

H

K

D

I

I

D

D

active site: D43 (= D20), K156 (= K139), E197 (= E176), E199 (= E178)
binding d-mannitol-1,6-diphosphate: D43 (= D20), S45 (= S22), S48 (= S25), K156 (= K139), R158 (= R141), E197 (= E176)

Sites not aligning to the query:

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

2qdgA Fructose-1,6-bisphosphate schiff base intermediate in fbp aldolase from leishmania mexicana (see paper)
29% identity, 60% coverage: 12:188/294 of query aligns to 36:209/366 of 2qdgA

query
sites
2qdgA

G

G

E

K

G

G

F

L

I

L

A
|
A

A

A

L

-

D
|
D

Q
x
E

S
|
S

G

I

G

G

S
|
S

T

C

P

T

K

K

A

R

L

F

R

Q

L

P

Y

I

G

G

I

L

T

-

E

-

D

-

A

-

Y

-

S

S

N

N

E

T

T

E

E

E

M

H

Y

R

D

-

L

-

I

-

H

R

A

Q

M

Y

R

R

A

A

R

L

I

M

I

L

K

E

S

A

S

E

A

G

F

F

T

E

G

-

D

Q

K

Y

V

I

V

S

G

G

A

V

I

I

L

L

F

H

E

D

Q

E

T

T

M

V

D

G

R

Q

D

K

I

A

D

S

G

N

I

G

P

Q

T

T

A

F

T

P

Y

E

L

Y

W

L

E

T

K

A

R

R

G

G

V

V

P

P

F

G

L

I

K
|
K

I

T

D
|
D

K

M

G

G

L

L

E

C

E

P

E

L

K

L

N

E

G

G

C

A

Q

E

M

G

L

E

K

Q

A

M

M

T

P

E

T

G

L

L

D

D

A

G

L

Y

L

V

E

K

R

R

A

A

A

S

-

A

-

Y

E

K

A

K

G

G

I

C

F

R

G

F

T

C

K
|
K

E

W

R
|
R

S

N

V

V

I

Y

S

K

A

I

A

Q

D

N

P

-

M

-

G

G

I

T

A

V

S

S

V

E

V

S

A

A

Q

V

Q

R

F

F

E

N

V

A

G

-

E

-

Q

E

V

T

L

L

G

A

-

R

-

Y

-

A

-

I

-

L

-

S

-

Q

-

M

A

S

G

G

M

L

V

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

V

T

M

I

I

S

D

I

G

A

K

D

H

K

D

I

I

D

D

active site: D43 (= D20), K156 (= K139), E197 (= E176), E199 (= E178)
binding 1,6-fructose diphosphate (linear form): A41 (= A17), D43 (= D20), E44 (≠ Q21), S45 (= S22), S48 (= S25), K156 (= K139), R158 (= R141)
binding phosphate ion: K116 (= K102), D118 (= D104), R158 (= R141), E197 (= E176), E199 (= E178)

Sites not aligning to the query:

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

2ot0A Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with a c-terminal peptide of wiskott-aldrich syndrome protein (see paper)
32% identity, 57% coverage: 12:179/294 of query aligns to 26:190/356 of 2ot0A

query
sites
2ot0A

G

G

E

K

G

G

F

I

I

L

A

A

L

-

D
|
D

Q
x
E

S

S

G

T

G

G

S
|
S

T

I

P

A

K

K

A
x
R

L

L

R

Q

L

S

Y

I

G

G

I

-

T

T

E

E

D

N

A

T

Y

E

S

E

N

N

E

R

T

R

E

F

M

Y

Y

R

D

Q

L

L

I

L

H

L

A

T

M

A

R

D

A

D

R

R

I

V

I

N

K

P

S

C

S

-

A

-

F

-

T

-

G

-

D

-

K

-

V

I

V

G

G

G

A

V

I

I

L

L

F

F

E

H

Q

E

T

T

M

L

-

Y

D

Q

R

K

D

A

I

D

D

D

G

G

I

R

P

P

T

F

A

P

T

Q

Y

V

L

I

W

K

E

S

K

K

R

G

G

G

V

V

P

-

F

G

L

I

K

K

I

V

D

D

K

K

G

G

L

V

E

V

E

P

E

L

K

A

N

-

G

G

C

T

Q

N

M

G

L

E

K

T

A

T

M

T

P

Q

T

G

L

L

D

D

A

G

L

L

L

S

E

E

R

R

A

C

A

A

E

Q

A

Y

G

K

I

K

F

D

G

G

-

A

-

D

-

F

T

A

K
|
K

E

W

R
|
R

S

C

V

V

I

L

-

K

-

I

-

G

-

E

-

H

-

T

-

P

S

S

A

A

A

L

D

A

P

I

M

M

G

E

I

N

A

A

S

N

V

V

V

L

A

A

Q

R

Q

Y

F

A

E

S

V

I

G

C

E

Q

Q

Q

V

-

L

-

G

-

A

N

G

G

M

I

V

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D33 (= D20), K146 (= K139), E187 (= E176), E189 (= E178)
binding : E34 (≠ Q21), S38 (= S25), R42 (≠ A29), K146 (= K139), R148 (= R141)

Sites not aligning to the query:

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

5tlzA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor naphthalene 2,6-bisphosphate (see paper)
32% identity, 57% coverage: 12:179/294 of query aligns to 23:187/346 of 5tlzA

query
sites
5tlzA

G

G

E

K

G

G

F

I

I

L

A

A

L

-

D
|
D

Q

E

S
|
S

G

T

G

G

S
|
S

T

I

P

A

K

K

A

R

L

L

R

Q

L

S

Y

I

G

G

I

-

T

T

E

E

D

N

A

T

Y

E

S

E

N

N

E

R

T

R

E

F

M

Y

Y

R

D

Q

L

L

I

L

H

L

A

T

M

A

R

D

A

D

R

R

I

V

I

N

K

P

S

C

S

-

A

-

F

-

T

-

G

-

D

-

K

-

V

I

V

G

G

G

A

V

I

I

L

L

F

F

E

H

Q

E

T

T

M

L

-

Y

D

Q

R

K

D

A

I

D

D

D

G

G

I

R

P

P

T

F

A

P

T

Q

Y

V

L

I

W

K

E

S

K

K

R

G

G

G

V

V

P

-

F

G

L

I

K
|
K

I

V

D

D

K

K

G

G

L

V

E

V

E

P

E

L

K

A

N

-

G

G

C

T

Q

N

M

G

L

E

K

T

A

T

M

T

P

Q

T

G

L

L

D

D

A

G

L

L

L

S

E

E

R

R

A

C

A

A

E

Q

A

Y

G

K

I

K

F

D

G

G

-

A

-

D

-

F

T

A

K
|
K

E

W

R

R

S

C

V

V

I

L

-

K

-

I

-

G

-

E

-

H

-

T

-

P

S

S

A

A

A

L

D

A

P

I

M

M

G

E

I

N

A

A

S

N

V

V

V

L

A

A

Q

R

Q

Y

F

A

E

S

V

I

G

C

E

Q

Q

Q

V

-

L

-

G

-

A

N

G

G

M

I

V

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D30 (= D20), K143 (= K139), E184 (= E176), E186 (= E178)
binding naphthalene-2,6-diyl bis[dihydrogen (phosphate)]: D30 (= D20), S32 (= S22), S35 (= S25), K104 (= K102)

Sites not aligning to the query:

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

5tlwA Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor 1-phosphate-benzene 4-bisphosphonate (see paper)
32% identity, 57% coverage: 12:179/294 of query aligns to 26:190/349 of 5tlwA

query
sites
5tlwA

G

G

E

K

G

G

F

I

I

L

A

A

L

-

D
|
D

Q

E

S
|
S

G

T

G

G

S
|
S

T

I

P

A

K

K

A

R

L

L

R

Q

L

S

Y

I

G

G

I

-

T

T

E

E

D

N

A

T

Y

E

S

E

N

N

E

R

T

R

E

F

M

Y

Y

R

D

Q

L

L

I

L

H

L

A

T

M

A

R

D

A

D

R

R

I

V

I

N

K

P

S

C

S

-

A

-

F

-

T

-

G

-

D

-

K

-

V

I

V

G

G

G

A

V

I

I

L

L

F

F

E

H

Q

E

T

T

M

L

-

Y

D

Q

R

K

D

A

I

D

D

D

G

G

I

R

P

P

T

F

A

P

T

Q

Y

V

L

I

W

K

E

S

K

K

R

G

G

G

V

V

P

-

F

G

L

I

K
|
K

I

V

D

D

K

K

G

G

L

V

E

V

E

P

E

L

K

A

N

-

G

G

C

T

Q

N

M

G

L

E

K

T

A

T

M

T

P

Q

T

G

L

L

D

D

A

G

L

L

L

S

E

E

R

R

A

C

A

A

E

Q

A

Y

G

K

I

K

F

D

G

G

-

A

-

D

-

F

T

A

K
|
K

E

W

R
|
R

S

C

V

V

I

L

-

K

-

I

-

G

-

E

-

H

-

T

-

P

S

S

A

A

A

L

D

A

P

I

M

M

G

E

I

N

A

A

S

N

V

V

V

L

A

A

Q

R

Q

Y

F

A

E

S

V

I

G

C

E

Q

Q

Q

V

-

L

-

G

-

A

N

G

G

M

I

V

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D33 (= D20), K146 (= K139), E187 (= E176), E189 (= E178)
binding {[4-(phosphonooxy)phenyl]methylene}bis(phosphonic acid): S35 (= S22), S38 (= S25), K107 (= K102), K146 (= K139), R148 (= R141)

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)
32% identity, 57% coverage: 12:179/294 of query aligns to 26:190/349 of 5tleA

query
sites
5tleA

G

G

E

K

G

G

F

I

I

L

A

A

L

-

D
|
D

Q

E

S
|
S

G

T

G

G

S
|
S

T

I

P

A

K

K

A

R

L

L

R

Q

L

S

Y

I

G

G

I

-

T

T

E

E

D

N

A

T

Y

E

S

E

N

N

E

R

T

R

E

F

M

Y

Y

R

D

Q

L

L

I

L

H

L

A

T

M

A

R

D

A

D

R

R

I

V

I

N

K

P

S

C

S

-

A

-

F

-

T

-

G

-

D

-

K

-

V

I

V

G

G

G

A

V

I

I

L

L

F

F

E

H

Q

E

T

T

M

L

-

Y

D

Q

R

K

D

A

I

D

D

D

G

G

I

R

P

P

T

F

A

P

T

Q

Y

V

L

I

W

K

E

S

K

K

R

G

G

G

V

V

P

-

F

G

L

I

K
|
K

I

V

D

D

K

K

G

G

L

V

E

V

E

P

E

L

K

A

N

-

G

G

C

T

Q

N

M

G

L

E

K

T

A

T

M

T

P

Q

T

G

L

L

D

D

A

G

L

L

L

S

E

E

R

R

A

C

A

A

E

Q

A

Y

G

K

I

K

F

D

G

G

-

A

-

D

-

F

T

A

K
|
K

E

W

R

R

S

C

V

V

I

L

-

K

-

I

-

G

-

E

-

H

-

T

-

P

S

S

A

A

A

L

D

A

P

I

M

M

G

E

I

N

A

A

S

N

V

V

V

L

A

A

Q

R

Q

Y

F

A

E

S

V

I

G

C

E

Q

Q

Q

V

-

L

-

G

-

A

N

G

G

M

I

V

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D33 (= D20), K146 (= K139), E187 (= E176), E189 (= E178)
binding {[6-(phosphonooxy)naphthalen-2-yl]methylene}bis(phosphonic acid): D33 (= D20), S35 (= S22), S38 (= S25), K107 (= K102)

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)
32% identity, 57% coverage: 12:179/294 of query aligns to 26:190/349 of 3tu9A

query
sites
3tu9A

G

G

E

K

G

G

F

I

I

L

A
|
A

A

A

L

-

D
|
D

Q
x
E

S
|
S

G

T

G

G

S
|
S

T

I

P

A

K

K

A

R

L

L

R

Q

L

S

Y

I

G

G

I

-

T

T

E

E

D

N

A

T

Y

E

S

E

N

N

E

R

T

R

E

F

M

Y

Y

R

D

Q

L

L

I

L

H

L

A

T

M

A

R

D

A

D

R

R

I

V

I

N

K

P

S

C

S

-

A

-

F

-

T

-

G

-

D

-

K

-

V

I

V

G

G

G

A

V

I

I

L

L

F

F

E

H

Q

E

T

T

M

L

-

Y

D

Q

R

K

D

A

I

D

D

D

G

G

I

R

P

P

T

F

A

P

T

Q

Y

V

L

I

W

K

E

S

K

K

R

G

G

G

V

V

P

-

F

G

L

I

K
|
K

I

V

D

D

K

K

G

G

L

V

E

V

E

P

E

L

K

A

N

-

G

G

C

T

Q

N

M

G

L

E

K

T

A

T

M

T

P

Q

T

G

L

L

D

D

A

G

L

L

L

S

E

E

R

R

A

C

A

A

E

Q

A

Y

G

K

I

K

F

D

G

G

-

A

-

D

-

F

T

A

K
|
K

E

W

R

R

S

C

V

V

I

L

-

K

-

I

-

G

-

E

-

H

-

T

-

P

S

S

A

A

A

L

D

A

P

I

M

M

G

E

I

N

A

A

S

N

V

V

V

L

A

A

Q

R

Q

Y

F

A

E

S

V

I

G

C

E

Q

Q

Q

V

-

L

-

G

-

A

N

G

G

M

I

V

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D33 (= D20), K146 (= K139), E187 (= E176), E189 (= E178)
binding 2-O-methyl-1,6-di-O-phosphono-D-mannitol: A31 (= A17), D33 (= D20), E34 (≠ Q21), S35 (= S22), S38 (= S25), K107 (= K102), K146 (= K139), E187 (= E176)

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)
32% identity, 57% coverage: 12:179/294 of query aligns to 26:190/349 of 2ot1A

query
sites
2ot1A

G

G

E

K

G

G

F

I

I

L

A

A

L

-

D
|
D

Q

E

S

S

G

T

G

G

S

S

T

I

P

A

K

K

A
x
R

L

L

R

Q

L

S

Y

I

G

G

I

-

T

T

E

E

D

N

A

T

Y

E

S

E

N

N

E

R

T

R

E

F

M

Y

Y

R

D

Q

L

L

I

L

H

L

A

T

M

A

R

D

A

D

R

R

I

V

I

N

K

P

S

C

S

-

A

-

F

-

T

-

G

-

D

-

K

-

V

I

V

G

G

G

A

V

I

I

L

L

F

F

E

H

Q

E

T

T

M

L

-

Y

D

Q

R

K

D

A

I

D

D

D

G

G

I

R

P

P

T

F

A

P

T

Q

Y

V

L

I

W

K

E

S

K

K

R

G

G

G

V

V

P

-

F

G

L

I

K

K

I

V

D

D

K

K

G

G

L

V

E

V

E

P

E

L

K

A

N

-

G

G

C

T

Q

N

M

G

L

E

K

T

A

T

M

T

P

Q

T

G

L

L

D

D

A

G

L

L

L

S

E

E

R

R

A

C

A

A

E

Q

A

Y

G

K

I

K

F

D

G

G

-

A

-

D

-

F

T

A

K
|
K

E

W

R

R

S

C

V

V

I

L

-

K

-

I

-

G

-

E

-

H

-

T

-

P

S

S

A

A

A

L

D

A

P

I

M

M

G

E

I

N

A

A

S

N

V

V

V

L

A

A

Q

R

Q

Y

F

A

E

S

V

I

G

C

E

Q

Q

Q

V

-

L

-

G

-

A

N

G

G

M

I

V

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D33 (= D20), K146 (= K139), E187 (= E176), E189 (= E178)
binding n-(4-chlorophenyl)-3-(phosphonooxy)naphthalene-2-carboxamide: R42 (≠ A29)

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)
32% identity, 57% coverage: 12:179/294 of query aligns to 26:190/363 of 1zalA

query
sites
1zalA

G

G

E

K

G

G

F

I

I

L

A

A

L

-

D
|
D

Q

E

S
|
S

G

T

G

G

S

S

T

I

P

A

K

K

A

R

L

L

R

Q

L

S

Y

I

G

G

I

-

T

T

E

E

D

N

A

T

Y

E

S

E

N

N

E

R

T

R

E

F

M

Y

Y

R

D

Q

L

L

I

L

H

L

A

T

M

A

R

D

A

D

R

R

I

V

I

N

K

P

S

C

S

-

A

-

F

-

T

-

G

-

D

-

K

-

V

I

V

G

G

G

A

V

I

I

L

L

F

F

E

H

Q

E

T

T

M

L

-

Y

D

Q

R

K

D

A

I

D

D

D

G

G

I

R

P

P

T

F

A

P

T

Q

Y

V

L

I

W

K

E

S

K

K

R

G

G

G

V

V

P

-

F

G

L

I

K
|
K

I

V

D

D

K

K

G

G

L

V

E

V

E

P

E

L

K

A

N

-

G

G

C

T

Q

N

M

G

L

E

K

T

A

T

M

T

P

Q

T

G

L

L

D

D

A

G

L

L

L

S

E

E

R

R

A

C

A

A

E

Q

A

Y

G

K

I

K

F

D

G

G

-

A

-

D

-

F

T

A

K
|
K

E

W

R

R

S

C

V

V

I

L

-

K

-

I

-

G

-

E

-

H

-

T

-

P

S

S

A

A

A

L

D

A

P

I

M

M

G

E

I

N

A

A

S

N

V

V

V

L

A

A

Q

R

Q

Y

F

A

E

S

V

I

G

C

E

Q

Q

Q

V

-

L

-

G

-

A

N

G

G

M

I

V

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D33 (= D20), K146 (= K139), E187 (= E176), E189 (= E178)
binding phosphate ion: S35 (= S22), K107 (= K102)

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)
32% identity, 57% coverage: 12:179/294 of query aligns to 26:190/363 of 1zajA

query
sites
1zajA

G

G

E

K

G

G

F

I

I

L

A

A

L

-

D
|
D

Q

E

S
|
S

G

T

G

G

S
|
S

T

I

P

A

K

K

A

R

L

L

R

Q

L

S

Y

I

G

G

I

-

T

T

E

E

D

N

A

T

Y

E

S

E

N

N

E

R

T

R

E

F

M

Y

Y

R

D

Q

L

L

I

L

H

L

A

T

M

A

R

D

A

D

R

R

I

V

I

N

K

P

S

C

S

-

A

-

F

-

T

-

G

-

D

-

K

-

V

I

V

G

G

G

A

V

I

I

L

L

F

F

E

H

Q

E

T

T

M

L

-

Y

D

Q

R

K

D

A

I

D

D

D

G

G

I

R

P

P

T

F

A

P

T

Q

Y

V

L

I

W

K

E

S

K

K

R

G

G

G

V

V

P

-

F

G

L

I

K
|
K

I

V

D

D

K

K

G

G

L

V

E

V

E

P

E

L

K

A

N

-

G

G

C

T

Q

N

M

G

L

E

K

T

A

T

M

T

P

Q

T

G

L

L

D

D

A

G

L

L

L

S

E

E

R

R

A

C

A

A

E

Q

A

Y

G

K

I

K

F

D

G

G

-

A

-

D

-

F

T

A

K
|
K

E

W

R

R

S

C

V

V

I

L

-

K

-

I

-

G

-

E

-

H

-

T

-

P

S

S

A

A

A

L

D

A

P

I

M

M

G

E

I

N

A

A

S

N

V

V

V

L

A

A

Q

R

Q

Y

F

A

E

S

V

I

G

C

E

Q

Q

Q

V

-

L

-

G

-

A

N

G

G

M

I

V

V

P

P

I

I

L

V

E
|
E

P

P

E
|
E

V

I

active site: D33 (= D20), K146 (= K139), E187 (= E176), E189 (= E178)
binding d-mannitol-1,6-diphosphate: D33 (= D20), S35 (= S22), S38 (= S25), K107 (= K102), K146 (= K139), E187 (= E176)

Sites not aligning to the query:

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

Query Sequence

>WP_110804301.1 NCBI__GCF_003217355.1:WP_110804301.1
MAKTMMEHMRKGEGFIAALDQSGGSTPKALRLYGITEDAYSNETEMYDLIHAMRARIIKS
SAFTGDKVVGAILFEQTMDRDIDGIPTATYLWEKRGVVPFLKIDKGLEEEKNGCQMLKAM
PTLDALLERAAEAGIFGTKERSVISAADPMGIASVVAQQFEVGEQVLGAGMVPILEPEVT
ISIADKIDAEAMLRDALLAGLETVSSPVMLKLSLPTIDNFYLPLVEHPNVIKVVALSGGY
ARNDANAILARNKGMIASFSRALTEGLTAQMTDAEFDAALGEAIDSIYRASIAG

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