SitesBLAST

N28 (= N30) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
K42 (= K44) mutation to M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
D76 (= D77) mutation to N: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
H95 (= H96) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
H97 (= H98) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+). Inhibited by glycolaldehyde phosphate.
T116 (= T117) mutation T->E,Y: Loss of the epimerase activity due to an increased steric bulk introduced by the mutation which causes a conformational change that is incompatible with catalysis.
D120 (= D121) mutation to N: Loss of the epimerase activity.
E142 (= E143) mutation to Q: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
H171 (= H172) binding
H218 (= H219) mutation to N: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
Y229 (= Y230) mutation to F: Loss of the epimerase activity.

1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
51% identity, 94% coverage: 5:224/233 of query aligns to 3:223/223 of 1jdiA

query
sites
1jdiA

Q

E

D

D

I

L

K

K

E

R

Q

Q

A

V

Y

L

Q

E

A

A

N

N

M

L

Q

A

L

L

P

P

K

K

L

H

G

N

L

L

V

V

L

T

F

L

T

T

F

W

G

G

N

N

V

V

S

S

A

A

A

V

D

D

R

R

S

E

K

R

G

G

V

V

F

F

A

V

I

I

K

K

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P

S

S

G

G

V

V

P

D

Y

Y

E

S

D

I

L

M

S

T

P

A

E

D

K

D

M

M

V

V

I

V

V

V

D

S

F

I

-

E

N

T

G

G

N

E

T

V

V

V

E

E

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G

T

A

L

K

R

K

P

P

S

S

D
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D

T

T

K

P

T

T

H

H

A

R

V

L

L

L

Y

Y

Q

Q

H

A

W

F

A

P

E

S

I

I

G

G

I

I

V

V

H
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H

T

T

H
|
H

S

S

T

R

Y

H

G

A

T

T

A

I

W

W

A

A

Q

Q

A

A

Q

G

R

Q

A

S

I

I

P

P

I

A

F

T

G

G

T
|
T

T

T

H

H

A

A

D
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D

H

Y

L

F

T

Y

V

G

D

T

I

I

P

P

C

C

A

T

P

R

P

K

M

M

A

T

D

D

E

A

M

E

I

I

K

N

G

G

N

E

Y

Y

E

E

Y

W

E

E

T

T

G

G

F

N

Q

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I

I

M

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N

E

H

T

F

F

E

E

S

K

L

Q

G

G

L

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S

D

Y

A

Q

A

E

Q

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M

E

P

M

G

I

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L

L

V

V

G

H

N

S

H
|
H

A

G

P

P

F

F

T

A

W

W

G

G

K

K

T

N

A

A

E

E

K

D

A

A

V

V

Y

H

N

N

S

A

A

I

V

V

L

L

E

E

T

E

V

V

A

A

Q

Y

M

M

A

G

L

I

L

F

T

C

E

R

Q

Q

I

L

N

A

P

P

Q

Q

A

L

P

P

K

D

L

M

K

Q

D

Q

S

T

L

L

I

L

E

N

K

K

H

H

Y

Y

E

L

R

R

K

K

H

H

active site: D76 (= D77), H95 (= H96), H97 (= H98), T116 (= T117), D120 (= D121), H171 (= H172)
binding zinc ion: H95 (= H96), H97 (= H98), H171 (= H172)

2fuaA L-fuculose 1-phosphate aldolase crystal form t with cobalt (see paper)
30% identity, 90% coverage: 7:216/233 of query aligns to 6:199/210 of 2fuaA

query
sites
2fuaA

I

L

K

A

E

R

Q

Q

A

I

Y

I

Q

D

A

T

N

C

M

L

Q

E

L

M

P

T

K

R

L

L

G

G

L

L

V

N

L

Q

F

G

T

T

F

A

G

G

N

N

V

V

S

S

A

V

A

-

D

-

R

R

S

Y

K

Q

G

D

V

G

F

M

A

L

I

I

K

T

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P

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T

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G

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Y

E

E

D

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L

S

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P

E

E

S

K

H

M

I

V

V

I

F

V

I

D

D

F

G

N

N

G

G

N

K

T

H

V

E

E

E

G

G

T

K

L

L

R

-

P

P

S

S

D
x
E

T

W

K

R

T

F

H

H

A

M

V

A

L

A

Y

Y

Q

Q

H

S

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R

A

P

E

D

I

A

G

N

G

A

I

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V

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H
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H

T

N

H
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H

S

A

T

V

Y

H

G

C

T

T

A

A

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V

A

S

Q

I

A

L

Q

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R

R

A

S

I

I

P

P

I

A

F

I

G

H

T
x
Y

T

M

H

I

A

A

D
x
A

H

A

L

G

T

G

V

N

D

S

I

I

P

P

C

C

A

A

P

P

P

-

M

-

A

-

D

-

E

-

M

-

I

-

K

-

G

-

N

-

Y

-

E

-

Y

Y

E

A

T

T

G

-

F

F

Q

G

I

T

M

R

N

E

H

L

F

S

E

E

S

H

L

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G

A

L

L

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A

Y

L

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K

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N

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R

E

K

M

A

I

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L

L

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N

H

H
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H

A

G

P

L

F

I

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A

W

C

G

E

K

V

T

N

A

L

E

E

K

K

A

A

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Y

W

N

L

S

A

A

H

V

E

L

V

E

E

T

V

V

L

A

A

Q

Q

M

L

A

Y

L

L

L

T

T

T

E

L

Q

A

I

I

N

T

P

D

Q

P

A

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P

P

K

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L

L

K

S

D

D

S

E

L

E

I

I

active site: E73 (≠ D77), H92 (= H96), H94 (= H98), Y113 (≠ T117), A117 (≠ D121), H155 (= H172)
binding cobalt (ii) ion: E73 (≠ D77), H92 (= H96), H94 (= H98), H155 (= H172)

Sites not aligning to the query:

active site: 209

P0AB87 L-fuculose phosphate aldolase; D-ribulose-phosphate aldolase; L-fuculose-1-phosphate aldolase; EC 4.1.2.17 from Escherichia coli (strain K12) (see 4 papers)
30% identity, 90% coverage: 7:216/233 of query aligns to 6:199/215 of P0AB87

query
sites
P0AB87

I

L

K

A

E

R

Q

Q

A

I

Y

I

Q

D

A

T

N

C

M

L

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E

L

M

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T

K

R

L

L

G

G

L

L

V

N

L

Q

F

G

T
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T

F
x
A

G
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G

N
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N

V

V

S

S

A

V

A

-

D

-

R

R

S

Y

K

Q

G

D

V

G

F

M

A

L

I

I

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x
T

G
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G

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Y

E

E

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K

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L

S

T

P

E

E

S

K

H

M

I

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V

I

F

V

I

D

D

F

G

N

N

G

G

N

K

T

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E

E

G

G

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L

R

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S

D
x
E

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F

H

H

A

M

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A

L

A

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Y

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Q

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A

P

E

D

I

A

G

N

G

A

I

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H
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H

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H
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H

S

A

T

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Y

H

G

C

T

T

A

A

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V

A

S

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I

A

L

Q

N

R

R

A

S

I

I

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P

I

A

F

I

G

H

T
x
Y

T

M

H

I

A

A

D

A

H

A

L

G

T

G

V

N

D

S

I

I

P

P

C

C

A

A

P

P

P

-

M

-

A

-

D

-

E

-

M

-

I

-

K

-

G

-

N

-

Y

-

E

-

Y

Y

E

A

T

T

G

-

F
|
F

Q

G

I

T

M

R

N

E

H

L

F

S

E

E

S

H

L

V

G

A

L

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A

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L

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K

E

N

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E

K

M

A

I

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L

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L

G

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N

H

H
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H

A

G

P

L

F

I

T

A

W

C

G

E

K

V

T

N

A

L

E

E

K

K

A

A

V

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Y

W

N

L

S

A

A

H

V

E

L

V

E

E

T

V

V

L

A

A

Q

Q

M

L

A

Y

L

L

L

T

T

T

E

L

Q

A

I

I

N

T

P

D

Q

P

A

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P

P

K

V

L

L

K

S

D

D

S

E

L

E

I

I

T26 (= T27) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
A27 (≠ F28) mutation Missing: Strong decrease of the aldolase activity.
GN 28:29 (= GN 29:30) binding
N29 (= N30) mutation to L: Loss of aldolase activity; when associated with A-71.; mutation to Q: Strong decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
TG 43:44 (≠ SG 46:47) binding
S71 (= S75) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
SS 71:72 (= SS 75:76) binding
E73 (≠ D77) active site, Proton donor/acceptor; binding ; mutation to Q: Loss of aldolase activity; when associated with F-113 and F-209.; mutation to S: Loss of aldolase activity.
H92 (= H96) binding
H94 (= H98) binding
Y113 (≠ T117) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to F: Slowly inactivated. Has a preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-209.
F131 (= F148) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to A: Has a slight preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with W-206.
H155 (= H172) binding

Sites not aligning to the query:

206 F→W: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P). Loss of aldolase activity; when associated with A-131.
207:215 mutation Missing: Loss of aldolase activity. Has a slight preference for the D-aldehyde.
209 Plays a key role in the stabilization of the transition state and positioning the aldehyde component; Y→F: Slowly inactivated and unable to discriminate between the enantiomers. Shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-113.
211:215 mutation Missing: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).

4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
30% identity, 93% coverage: 7:222/233 of query aligns to 6:205/206 of 4fuaA

query
sites
4fuaA

I

L

K

A

E

R

Q

Q

A

I

Y

I

Q

D

A

T

N

C

M

L

Q

E

L

M

P

T

K

R

L

L

G

G

L

L

V

N

L

Q

F

G

T

T

F

A

G
|
G

N
|
N

V

V

S

S

A

V

A

-

D

-

R

R

S

Y

K

Q

G

D

V

G

F

M

A

L

I

I

K

T

P

P

S
x
T

G

G

V

I

P

P

Y

Y

E

E

D

K

L

L

S

T

P

E

E

S

K

H

M

I

V

V

I

F

V

I

D

D

F

G

N

N

G

G

N

K

T

H

V

E

E

E

G

G

T

K

L

L

R

-

P

P

S
|
S

D
x
E

T

W

K

R

T

F

H

H

A

M

V

A

L

A

Y

Y

Q

Q

H

S

W

R

A

P

E

D

I

A

G

N

G

A

I

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V

V

H
|
H

T

N

H
|
H

S

A

T

V

Y

H

G

C

T

T

A

A

W

V

A

S

Q

I

A

L

Q

N

R

R

A

S

I

I

P

P

I

A

F

I

G

H

T
x
Y

T

M

H

I

A

A

D
x
A

H

A

L

G

T

G

V

N

D

S

I

I

P

P

C

C

A

A

P

P

P

-

M

-

A

-

D

-

E

-

M

-

I

-

K

-

G

-

N

-

Y

-

E

-

Y

Y

E

A

T

T

G

-

F

F

Q

G

I

T

M

R

N

E

H

L

F

S

E

E

S

H

L

V

G

A

L

L

S

A

Y

L

Q

K

E

N

V

R

E

K

M

A

I

T

L

L

V

L

G

Q

N

H

H
|
H

A

G

P

L

F

I

T

A

W

C

G

E

K

V

T

N

A

L

E

E

K

K

A

A

V

L

Y

W

N

L

S

A

A

H

V

E

L

V

E

E

T

V

V

L

A

A

Q

Q

M

L

A

Y

L

L

L

T

T

T

E

L

Q

A

I

I

N

T

P

D

Q

P

A

V

P

P

K

V

L

L

K

S

D

D

S

E

L

E

I

I

E

A

K

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H

V

Y

L

E

E

R

K

active site: E73 (≠ D77), H92 (= H96), H94 (= H98), Y113 (≠ T117), A117 (≠ D121), H155 (= H172)
binding phosphoglycolohydroxamic acid: G28 (= G29), N29 (= N30), T43 (≠ S46), S71 (= S75), S72 (= S76), E73 (≠ D77), H92 (= H96), H94 (= H98), H155 (= H172)
binding zinc ion: H92 (= H96), H94 (= H98), H155 (= H172)

1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
30% identity, 90% coverage: 7:216/233 of query aligns to 6:199/209 of 1dzuP

query
sites
1dzuP

I

L

K

A

E

R

Q

Q

A

I

Y

I

Q

D

A

T

N

C

M

L

Q

E

L

M

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T

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R

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L

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G

L

L

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N

L

Q

F

G

T

A

F

A

G

G

N

N

V

V

S

S

A

V

A

-

D

-

R

R

S

Y

K

Q

G

D

V

G

F

M

A

L

I

I

K

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P

P

S

T

G

G

V

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P

Y

Y

E

E

D

K

L

L

S

T

P

E

E

S

K

H

M

I

V

V

I

F

V

I

D

D

F

G

N

N

G

G

N

K

T

H

V

E

E

E

G

G

T

K

L

L

R

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P

P

S

S

D
x
E

T

W

K

R

T

F

H

H

A

M

V

A

L

A

Y

Y

Q

Q

H

S

W

R

A

P

E

D

I

A

G

N

G

A

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V

V

H
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H

T

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H
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H

S

A

T

V

Y

H

G

C

T

T

A

A

W

V

A

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Q

I

A

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Q

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R

A

S

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P

I

A

F

I

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H

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Y

T

M

H

I

A

A

D

A

H

A

L

G

T

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V

N

D

S

I

I

P

P

C

C

A

A

P

P

P

-

M

-

A

-

D

-

E

-

M

-

I

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K

-

G

-

N

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Y

-

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-

Y

Y

E

A

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T

G

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F

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Q

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H

L

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S

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E

S

H

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A

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A

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M

A

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L

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N

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H
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H

A

G

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F

I

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A

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C

G

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K

V

T

N

A

L

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E

K

K

A

A

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A

A

H

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E

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A

A

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Q

M

L

A

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L

L

L

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I

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D

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I

I

binding zinc ion: E73 (≠ D77), H92 (= H96), H94 (= H98), H155 (= H172)

4c25A L-fuculose 1-phosphate aldolase (see paper)
36% identity, 46% coverage: 6:113/233 of query aligns to 8:115/212 of 4c25A

query
sites
4c25A

D

D

I

V

K

K

E

Q

Q

E

A

L

Y

I

Q

K

A

Y

N

G

M

K

Q

K

L

L

P

V

K

E

L

T

G

D

L

L

V

T

L

K

F

G

T

T

F
x
G

G

G

N

N

V

L

S

S

A

V

A

F

D

D

R

R

S

E

K

K

G

Q

V

L

F

M

A

A

I

I

K

T

P

P

S

S

G

G

V

I

P

D

Y

F

E

F

D

E

L

I

S

K

P

E

E

S

K

D

M

I

V

V

I

V

V

M

D

D

F

I

N

N

G

G

N

N

T

V

V

V

E

E

G

G

T

E

L

R

R

L

P

P

S

S

D
x
E

T

W

K

Y

T

M

H

H

A

L

V

I

L

Q

Y

Y

Q

Q

H

T

W

R

A

D

E

D

I

I

G

D

G

A

I

I

V

I

H
|
H

T

A

H
|
H

S

T

T

T

Y

Y

G

A

T

T

A

V

W

L

A

A

Q

C

A

L

Q

R

R

E

A

P

I

L

P

P

active site: E79 (≠ D77), H98 (= H96), H100 (= H98)
binding zinc ion: G30 (≠ F28), H98 (= H96), H100 (= H98)

Sites not aligning to the query:

active site: 119, 160
binding zinc ion: 160

7x78A L-fuculose 1-phosphate aldolase (see paper)
30% identity, 90% coverage: 7:216/233 of query aligns to 6:196/203 of 7x78A

query
sites
7x78A

I

L

K

A

E
x
R

Q

Q

A

I

Y

I

Q

D

A

T

N

C

M

L

Q

E

L

M

P

T

K

R

L

L

G

G

L

L

V

-

L

-

F

-

T

N

F

A

G

G

N
|
N

V

V

S

S

A

V

A

-

D

-

R

R

S

Y

K

Q

G

G

V

G

F

M

A

L

I

I

K

T

P

P

S
x
T

G

G

V

I

P

P

Y

Y

E

E

D

K

L

L

S

T

P

E

E

D

K

K

M

I

V

V

I

F

V

I

D

D

F

A

N

D

G

G

N

Q

T
x
H

V

E

E
x
Q

G

G

T

K

L

L

R

-

P

P

S
|
S

D
x
E

T

W

K

R

T

F

H

H

A

Q

V

A

L

A

Y

Y

Q

Q

H

T

W

R

A

P

E

D

I

A

G

Q

G

A

I

V

V

V

H
|
H

T

N

H
|
H

S

A

T

V

Y

H

G

C

T

T

A

A

W

V

A

S

Q

I

A

L

Q

N

R

R

A

P

I

I

P

P

I

A

F

I

G

H

T

Y

T

M

H

I

A

A

D

A

H

A

L

G

T

G

V

N

D

S

I

I

P

P

C

C

A

A

P

P

P

-

M

-

A

-

D

-

E

-

M

-

I

-

K

-

G

-

N

-

Y

-

E

-

Y

Y

E

A

T

T

G

-

F

F

Q

G

I

T

M

R

N

E

H

L

F

S

E

E

S

H

L

V

G

A

L

V

S

A

Y

L

Q

K

E

H

V

R

E

K

M

A

I

T

L

L

V

L

G

Q

N

H

H
|
H

A

G

P

L

F

I

T

A

W

C

G

E

K

A

T

S

A

L

E

E

K

K

A

A

V

L

Y

W

N

L

S

A

A

H

V

E

L

V

E

E

T

V

V

L

A

A

Q

Q

M

L

A

Y

L

L

L

S

T

T

E

L

Q

A

I

I

N

T

P

D

Q

P

A

V

P

P

K

V

L

L

K

D

D

D

S

E

L

A

I

I

binding magnesium ion: E70 (≠ D77), H89 (= H96), H91 (= H98), H152 (= H172)
binding sulfate ion: R8 (≠ E9), N26 (= N30), T40 (≠ S46), H61 (≠ T67), Q63 (≠ E69), S68 (= S75), S69 (= S76)

Sites not aligning to the query:

binding sulfate ion: 5

6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
32% identity, 55% coverage: 5:131/233 of query aligns to 4:129/207 of 6btgA

query
sites
6btgA

Q

Q

D

K

I

E

K

R

E

E

Q

E

A

I

Y

V

Q

A

A

Y

N

G

M

K

Q

K

L

M

P

I

K

S

L

S

G

G

L

L

V

T

L

K

F

G

T

T

F

G

G

G

N

N

V

I

S

S

A

I

A

F

D

N

R

R

S

E

K

Q

G

G

V

L

F

V

A

A

I

I

K

S

P

P

S

S

G

G

V

L

P

E

Y

Y

E

Y

D

E

L

T

S

K

P

P

E

E

K

D

M

V

V

V

I

I

V

L

D

N

F

L

N

D

G

G

N

E

T

V

V

I

E

E

G

G

T

E

L

R

R

K

P

P

S

S

D
x
E

T

L

K

D

T

M

H

H

A

L

V

I

L

Y

Y

Y

Q

R

H

K

W

R

A

E

E

D

I

I

G

N

G

A

I

L

V

V

H
|
H

T

T

H
|
H

S

S

T

P

Y

Y

G

A

T

K

A

T

W

I

A

A

Q

S

A

L

Q

G

R

W

A

E

I

L

P

P

I

A

F

V

G

S

T
x
Y

T

L

H

I

A

A

D

-

H

F

L

A

T

G

V

P

D

N

I

V

P

R

C

C

A

A

P

P

active site: E76 (≠ D77), H95 (= H96), H97 (= H98), Y116 (≠ T117)
binding manganese (ii) ion: E76 (≠ D77), H95 (= H96), H97 (= H98)

Sites not aligning to the query:

active site: 157
binding manganese (ii) ion: 157

P0DTQ0 5-deoxy-D-ribulose 1-phosphate aldolase; 5-deoxyribose disposal aldolase; EC 4.1.2.- from Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73) (see paper)
35% identity, 47% coverage: 22:131/233 of query aligns to 21:129/213 of P0DTQ0

query
sites
P0DTQ0

G

G

L

L

V

T

L

K

F

G

T

T

F

G

G

G

N

N

V

I

S

S

A

I

A

F

D

N

R

R

S

E

K

Q

G

G

V

L

F

V

A

A

I

I

K

S

P

P

S

S

G

G

V

L

P

E

Y

Y

E

Y

D

E

L

T

S

K

P

P

E

E

K

D

M

V

V

V

I

I

V

L

D

N

F

L

N

D

G

G

N

E

T

V

V

I

E

E

G

G

T

E

L

R

R

K

P

P

S

S

D
x
E

T

L

K

D

T

M

H

H

A

L

V

I

L

Y

Y

Y

Q

R

H

K

W

R

A

E

E

D

I

I

G

N

G

A

I

L

V

V

H
|
H

T

T

H
|
H

S

S

T

P

Y

Y

G

A

T

K

A

T

W

I

A

A

Q

S

A

L

Q

G

R

W

A

E

I

L

P

P

I

A

F

V

G

S

T

Y

T

L

H

I

A

A

D

-

H

F

L

A

T

G

V

P

D

N

I

V

P

R

C

C

A

A

P

P

E76 (≠ D77) binding
H95 (= H96) binding
H97 (= H98) binding

Sites not aligning to the query:

157 binding

Q58813 L-fuculose phosphate aldolase; L-fuculose-1-phosphate aldolase; EC 4.1.2.17 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
24% identity, 83% coverage: 8:200/233 of query aligns to 3:175/181 of Q58813

query
sites
Q58813

K

K

E

K

Q

Q

A

F

Y

I

Q

K

A

I

N

C

M

R

Q

K

L

L

P

Y

K

D

L

R

G

K

L

Y

V

V

L

V

F

G

T

S

F

G

G

G

N
|
N

V

V

S

S

A

V

A

K

D

E

R

G

S

D

K

K

G

-

V

-

F

I

A

Y

I

L

K

T

P

P

S

T

G

G

V

S

P

I

Y

L

E

G

D

F

L

L

S

K

P

E

E

D

K

D

M

I

V

A

I

E

V

M

D

D

F

L

N

D

G

G

N

N

T

V

V

I

E

K

G

G

T

-

L

-

R

K

P

P

S

T

S

S

D

E

T

K

K

N

T

L

H

H

A

L

V

M

L

I

Y

Y

Q

R

H

K

W

R

A

N

E

D

I

I

G

N

G

A

I

I

V

I

H

H

T

T

H

H

S

S

T

L

Y

I

G

S

T

T

A

F

W

L

A

S

Q

T

A

I

Q

N

R

K

A

E

I

I

P

E

I

L

F

L

G

-

T

-

H

-

A

-

D

-

H

-

L

-

T

-

V

-

D

-

I

T

P

P

C

E

A

G

P

K

P

I

M

F

A

L

D

K

E

K

M

I

I

G

K

Y

G

V

N

D

Y

Y

E

-

Y

Y

E

E

T

A

G

G

F

-

Q

-

I

-

M

-

N

-

H

-

F

-

E

-

S

S

L

L

G

K

L

L

-

A

-

E

-

T

S

A

Y

K

Q

R

E

D

V

E

E

D

M

V

I

I

L

I

V

L

G

K

N

N

H

H

A

G

P

V

F

V

T

C

W

L

G

G

K

K

T

D

A

L

E

I

K

D

A

A

V

Y

Y

I

N

K

S

V

A

E

V

V

L

L

E

E

T

E

V

Q

A

A

Q

K

M

L

A

T

L

L

N25 (= N30) mutation to L: It shows a 3-fold increase of the affinty for dihydroxyacetone phosphate (DHAP) and a 3-fold decrease of the affinity for DL-glyceraldehyde compared to the wild-type.; mutation to T: It shows a 5-fold decrease of the affinty for dihydroxyacetone phosphate (DHAP), but has the same affinity for DL-glyceraldehyde compared to the wild-type.

6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
25% identity, 83% coverage: 5:197/233 of query aligns to 5:186/207 of 6voqA

query
sites
6voqA

Q

Q

D

Q

I

L

K

R

E

E

Q

E

A

M

Y

V

Q

Q

A

I

N

G

M

A

Q

S

L

L

P

F

K

S

L

R

G

G

L

Y

V

A

L

T

F

G

T

S

F

A

G

G

N

N

V

L

S

S

A

L

D

L

R

P

S

D

K

G

G

N

V

L

F

L

A

A

I

-

K

T

P

P

S

T

G

G

V

A

P

C

Y

L

E

G

D

E

L

L

S

Q

P

A

E

Q

K

R

M

L

V

S

I

V

V

V

D

T

F

L

N

Q

G

G

N

E

T

W

V

I

E

S

G

G

T

D

L

-

R

K

P

P

S

S

S

K

D
x
E

T

V

K

T

T

F

H

H

A

R

V

A

L

V

Y

Y

Q

L

H

H

W

N

A

P

E

A

I

C

G

K

G

A

I

I

V

V

H
|
H

T

L

H
|
H

S

S

T

H

Y

Y

G

L

T

T

A

A

W

L

A

S

Q

C

A

L

Q

Q

-

G

-

L

-

D

-

P

-

H

R

N

A

C

I

I

P

R

I

P

F

F

G

-

T

T

T

P

H
x
Y

A

V

D

V

H

M

L

R

T

V

V

G

D

D

I

V

P

P

C

V

A

V

P

P

P

-

M

-

A

-

D

-

E

-

M

-

I

-

K

-

G

-

N

-

Y

Y

E

Y

Y

R

E

P

T

G

G

D

F

D

Q

R

I

I

M

A

N

Q

H

A

F

L

E

A

S

G

L

L

G

A

L

P

S

R

Y

Y

Q

N

E

A

V

-

E

-

M

-

I

F

L

L

V

L

G

A

N

N

H
|
H

A

G

P

P

F

V

T

V

W

T

G

G

K

S

T

S

A

L

E

R

K

E

A

A

V

T

Y

N

N

N

S

T

A

E

V

E

L

L

E

E

T

E

V

T

A

A

Q

R

M

L

active site: E75 (≠ D77), H94 (= H96), H96 (= H98), Y121 (≠ H119), H161 (= H172)
binding zinc ion: E75 (≠ D77), H94 (= H96), H96 (= H98), H161 (= H172)

4xxfA L-fuculose 1-phosphate aldolase from glaciozyma antarctica pi12 (see paper)
22% identity, 73% coverage: 41:209/233 of query aligns to 57:209/249 of 4xxfA

query
sites
4xxfA

F

F

A

W

I

V

K

N

P

P

S

F

G

G

V

L

P

A

Y

F

E

R

D

L

L

M

S

T

P

V

E

S

K

D

M

L

V

I

I

L

V

V

D

N

F

Q

N

E

G

G

N

T

T

V

V

I

E

G

G

G

-

G

-

K

-

E

-

G

-

R

T

R

L

I

R

V

P

N

S

L

S

A

D
x
G

T

F

K

M

T

I

H

H

A

S

V

A

L

I

Y

H

Q

K

H

A

W

R

A

P

E

E

I

V

G

Q

G

A

I

I

V

C

H
|
H

T

S

H
|
H

S

S

T

T

Y

Y

G

G

T

K

A

A

W

F

A

S

Q

S

A

L

Q

G

R

K

A

P

I

L

P

A

I

I

F

-

G

-

T

-

H

-

A

-

D

-

H

-

L

-

T

T

V

T

D
x
Q

I

D

P

S

C

C

A

A

P

-

P

F

M

Y

A

G

D

D

E

V

M

A

I

L

K

L

G

G

N

D

Y

-

E

-

Y

-

E

E

T

S

G

G

F

-

Q

-

I

-

M

-

N

-

H

-

F

-

E

-

S

T

L

I

G

A

L

V

S

A

Y

L

Q

Q

E

Q

V

K

E

K

M

A

I

I

L

I

V

L

G

Q

N

N

H
|
H

A

G

P

L

F

L

T

T

W

V

G

G

K

T

T

T

A

I

E

D

K

S

A

A

V

V

Y

A

N

W

S

F

A

I

V

M

L

L

E

E

T

K

V

Q

A

C

Q

Q

M

V

A

Q

L

L

T

A

E

D

Q

A

I

A

N

G

P

Q

Q

T

A

I

P

P

active site: G98 (≠ D77), H117 (= H96), H119 (= H98), Q138 (≠ D126), H172 (= H172)
binding zinc ion: H117 (= H96), H119 (= H98), H172 (= H172)

Query Sequence

>CA265_RS08620 FitnessBrowser__Pedo557:CA265_RS08620
MSNYQDIKEQAYQANMQLPKLGLVLFTFGNVSAADRSKGVFAIKPSGVPYEDLSPEKMVI
VDFNGNTVEGTLRPSSDTKTHAVLYQHWAEIGGIVHTHSTYGTAWAQAQRAIPIFGTTHA
DHLTVDIPCAPPMADEMIKGNYEYETGFQIMNHFESLGLSYQEVEMILVGNHAPFTWGKT
AEKAVYNSAVLETVAQMALLTEQINPQAPKLKDSLIEKHYERKHGDGAYYGQK

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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