SitesBLAST

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)
45% identity, 91% coverage: 5:215/232 of query aligns to 2:210/215 of P0AB87

query
sites
P0AB87

E

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L

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T26 (= T31) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
A27 (= A32) mutation Missing: Strong decrease of the aldolase activity.
GN 28:29 (= GN 33:34) binding
N29 (= N34) 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 (≠ SS 48:49) 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 (= E77) 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 (= Y117) 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 (= F135) 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 (= H159) binding
F206 (≠ M209) mutation to 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.
Y209 (= Y214) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to 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.

Sites not aligning to the query:

207:215 mutation Missing: Loss of aldolase activity. Has a slight preference for the D-aldehyde.
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)
45% identity, 88% coverage: 5:209/232 of query aligns to 2:206/206 of 4fuaA

query
sites
4fuaA

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active site: E73 (= E77), H92 (= H96), H94 (= H98), Y113 (= Y117), A117 (≠ I121), H155 (= H159)
binding phosphoglycolohydroxamic acid: G28 (= G33), N29 (= N34), T43 (≠ S48), S71 (= S75), S72 (= S76), E73 (= E77), H92 (= H96), H94 (= H98), H155 (= H159)
binding zinc ion: H92 (= H96), H94 (= H98), H155 (= H159)

1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
44% identity, 89% coverage: 5:210/232 of query aligns to 2:207/209 of 1dzuP

query
sites
1dzuP

E

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binding zinc ion: E73 (= E77), H92 (= H96), H94 (= H98), H155 (= H159)

7x78A L-fuculose 1-phosphate aldolase (see paper)
43% identity, 86% coverage: 11:209/232 of query aligns to 6:203/203 of 7x78A

query
sites
7x78A

L

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binding magnesium ion: E70 (= E77), H89 (= H96), H91 (= H98), H152 (= H159)
binding sulfate ion: R8 (= R13), N26 (= N34), T40 (≠ S48), H61 (≠ Y69), Q63 (≠ V70), S68 (= S75), S69 (= S76)

Sites not aligning to the query:

binding sulfate ion: 5

4c25A L-fuculose 1-phosphate aldolase (see paper)
39% identity, 86% coverage: 11:210/232 of query aligns to 9:211/212 of 4c25A

query
sites
4c25A

L

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x
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active site: E79 (= E77), H98 (= H96), H100 (= H98), Y119 (= Y117), H160 (= H159)
binding zinc ion: G30 (≠ A32), H98 (= H96), H100 (= H98), H160 (= H159)

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)
39% identity, 88% coverage: 12:216/232 of query aligns to 7:212/213 of P0DTQ0

query
sites
P0DTQ0

R

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R

T

E

D

D

I

I

D

N

V

A

V

L

L

V

H
|
H

C

T

H
|
H

S

S

I

P

Y

Y

A

A

T

K

T

T

L

I

A

A

C

S

H

L

H

G

K

W

T

E

I

L

P

P

S

A

F

V

H

S

Y

Y

M

L

T

I

G

A

I

F

A

A

G

G

G

-

T

P

T

N

I

V

R

R

C

C

A

A

E

P

Y

Y

A

E

T

T

F

F

G

G

T

T

Q

K

A

Q

L

L

S

A

D

D

N

A

A

A

L

F

L

E

A

G

L

M

K

I

D

D

R

R

L

R

A

A

C

V

L

L

G

A

Q

N

H
|
H

G

G

Q

L

I

I

S

A

L

G

G

A

K

N

T

N

L

I

E

K

Q

M

A

A

L

F

W

T

L

V

A

A

I

E

E

E

V

I

E

E

T

F

L

C

S

A

R

Q

I

I

Y

Y

V

Y

Q

Q

A

T

L

K

T

S

L

I

G

G

E

E

P

P

P

K

I

L

L

L

P

P

D

E

D

D

E

E

M

M

E

E

R

N

V

L

I

A

A

K

Q

K

M

F

R

E

R

-

M

-

S

G

Y

Y

G

G

Q

Q

E76 (= E77) binding
H95 (= H96) binding
H97 (= H98) binding
H157 (= H159) binding

6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
39% identity, 85% coverage: 12:209/232 of query aligns to 7:207/207 of 6btgA

query
sites
6btgA

R

R

R

E

E

E

M

I

V

V

D

A

I

Y

C

G

R

K

M

M

N

I

L

S

S

S

G

G

I

L

N

T

Q

K

G

G

T

T

A

G

G

G

N

N

L

I

S

S

V

I

-

F

-

N

R

R

T

E

D

Q

D

G

G

L

F

V

L

A

I

I

T

S

P

P

S

S

S

G

M

L

P

E

Y

Y

D

Y

T

E

M

T

Q

K

P

P

D

E

D

D

L

V

V

V

E

I

M

L

G

N

F

L

D

D

G

G

T

E

Y

V

V

I

-

E

G

G

H

E

R

R

-

K

P

P

S

S

E
|
E

W

L

R

D

F

M

H

H

R

L

D

I

I

Y

L

Y

R

R

A

K

R

R

T

E

D

D

I

I

D

N

V

A

V

L

L

V

H
|
H

C

T

H
|
H

S

S

I

P

Y

Y

A

A

T

K

T

T

L

I

A

A

C

S

H

L

H

G

K

W

T

E

I

L

P

P

S

A

F

V

H

S

Y
|
Y

M

L

T

I

G

A

I

F

A

A

G

G

G

-

T

P

T

N

I

V

R

R

C

C

A

A

E

P

Y

Y

A

E

T

T

F

F

G

G

T

T

Q

K

A

Q

L

L

S

A

D

D

N

A

A

A

L

F

L

E

A

G

L

M

K

I

D

D

R

R

L

R

A

A

C

V

L

L

G

A

Q

N

H
|
H

G

G

Q

L

I

I

S

A

L

G

G

A

K

N

T

N

L

I

E

K

Q

M

A

A

L

F

W

T

L

V

A

A

I

E

E

E

V

I

E

E

T

F

L

C

S

A

R

Q

I

I

Y

Y

V

Y

Q

Q

A

T

L

K

T

S

L

I

G

G

E

E

P

P

P

K

I

L

L

L

P

P

D

E

D

D

E

E

M

M

E

E

R

N

V

L

I

A

A

K

Q

K

M

F

active site: E76 (= E77), H95 (= H96), H97 (= H98), Y116 (= Y117), H157 (= H159)
binding manganese (ii) ion: E76 (= E77), H95 (= H96), H97 (= H98), H157 (= H159)

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)
30% identity, 72% coverage: 12:178/232 of query aligns to 3:165/181 of Q58813

query
sites
Q58813

R

K

E

Q

M

F

V

I

D

K

I

I

C

C

R

R

R

K

M

L

N

Y

L

D

S

R

G

K

I

Y

N

V

Q

V

G

G

T

S

A

G

G

G

N
|
N

L

V

S

S

V

V

R

K

T

E

D

G

D

D

G

K

F

I

L

Y

I

L

T

T

P

P

S

T

S

G

M

S

P

I

Y

L

D

G

T

F

M

L

Q

K

P

E

D

D

L

I

V

A

E

E

M

M

G

D

F

L

D

D

G

G

T

N

Y

V

V

I

G

K

H

G

R

K

P

P

S

T

S

S

E

E

W

K

R

N

F

L

H

H

R

L

D

M

I

I

L

Y

R

R

A

K

R

R

T

N

D

D

I

I

D

N

V

A

V

I

L

I

H

H

C

T

H

H

S

S

I

L

Y

I

A

S

T

T

T

F

L

L

A

S

C

T

H

I

H

N

K

K

T

E

I

I

P

E

S

L

F

L

H

T

Y

-

M

P

T

E

G

G

I

K

A

I

G

F

G

L

T

K

I

I

R

G

C

Y

A

V

E

D

Y

Y

A

Y

T

E

F

A

G

G

T

S

Q

L

A

K

L

L

S

A

D

E

N

E

A

T

L

-

A

A

L

K

K

R

D

D

R

E

L

D

A

V

C

I

L

I

L

L

G

K

Q

N

H

H

G

G

Q

V

I

V

S

C

L

L

G

G

K

K

T

D

L

L

E

I

Q

D

A

A

L

-

W

Y

L

I

A

K

I

V

E

E

V

V

N25 (= N34) 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
31% identity, 84% coverage: 11:205/232 of query aligns to 7:206/207 of 6voqA

query
sites
6voqA

L

L

R

R

R

E

E

E

M

M

V

V

D

Q

I

I

C

G

R

A

R

S

M

L

N

F

L

S

S

R

G

G

I

Y

N

A

Q

T

G

G

T

S

A

A

G

G

N

N

L

L

S

S

V

L

R

L

T

L

D

P

D

D

G

G

-

N

F

L

L

L

I

A

T

T

P

P

S

T

S

G

M

A

P

C

Y

L

D

G

T

E

M

L

Q

Q

P

A

D

Q

D

R

L

L

V

S

E

V

M

V

G

T

F

L

D

Q

G

G

T

E

Y

W

V

I

-

S

G

G

H

D

R

K

P

P

S

S

S

K

E
|
E

W

V

R

T

F

F

H

H

R

R

D

A

I

V

L

Y

R

L

A

H

R

N

T

P

D

A

I

C

D

K

V

A

V

I

L

V

H
|
H

C

L

H
|
H

S

S

I

H

Y

Y

A

L

T

T

T

A

L

L

A

S

C

C

-

L

-

Q

-

G

-

L

-

D

-

P

H

H

H

N

K

C

T

I

I

R

P

P

S

F

F

T

H

P

Y
|
Y

M

V

T

V

G

M

I

R

A

V

G

G

G

D

T

V

T

P

I

V

R

-

C

-

A

V

E

P

Y

Y

A

Y

T

R

F

P

G

G

T

D

Q

D

A

R

L

I

S

A

D

Q

N

-

A

A

L

L

L

A

A

G

L

L

K

A

D

P

R

R

L

Y

-

N

A

A

C

F

L

L

G

A

Q

N

H
|
H

G

G

Q

P

I

V

S

V

L

T

G

G

K

S

T

S

L

L

E

R

Q

E

A

A

L

T

W

N

L

N

A

T

I

E

E

E

V

L

E

E

T

E

L

T

S

A

R

R

I

L

Y

I

V

-

Q

-

A

-

L

F

T

T

L

L

G

G

E

N

P

R

P

E

I

I

-

R

-

Y

L

L

P

T

D

A

D

D

E

E

M

V

E

K

R

E

V

L

active site: E75 (= E77), H94 (= H96), H96 (= H98), Y121 (= Y117), H161 (= H159)
binding zinc ion: E75 (= E77), H94 (= H96), H96 (= H98), H161 (= H159)

4xxfA L-fuculose 1-phosphate aldolase from glaciozyma antarctica pi12 (see paper)
24% identity, 87% coverage: 1:201/232 of query aligns to 12:212/249 of 4xxfA

query
sites
4xxfA

M

F

A

A

E

T

T

V

E

E

T

A

D

E

K

R

L

A

A

W

L

L

R

K

R

E

E

R

M

L

V

V

D

A

I

A

C

I

R

R

R

I

M

F

N

A

L

N

S

E

G

G

I

F

N

D

Q

H

G

T

T

V

A

A

G

G

N

H

L

L

S

T

V

V

R

R

T

D

D

P

D

E

G

N

-

K

-

H

F

F

L

W

I

V

T

N

P

P

S

F

S

G

M

L

P

A

Y

F

D

R

T

L

M

M

Q

T

P

V

D

S

D

D

L

L

V

I

E

L

M

V

G

N

F

Q

D

E

G

G

T

T

Y

V

V

I

G

G

H

G

R

G

P

K

S

E

S

G

E

R

-

R

-

I

-

V

-

N

-

L

-

A

-
x
G

W

F

R

M

F

I

H

H

R

S

D

A

I

I

L

H

R

K

A

A

R

R

T

P

D

E

I

V

D

Q

V

A

V

I

L

C

H
|
H

C

S

H
|
H

S

S

I

T

Y

Y

A

G

T

K

T

A

L

F

A

S

C

S

H

L

H

G

K

K

T

P

I

-

P

-

S

-

F

-

H

-

Y

-

M

-

T

-

G

-

I

L

A

A

G

I

G

T

T

T

T
x
Q

I

D

R

S

C

C

A

A

E

F

Y

Y

-

G

-

D

-

V

A

A

T

L

F

L

G

G

T

D

Q

E

A

-

L

-

S

S

D

G

N

T

A

I

L

A

L

V

A

A

L

L

K

Q

D

Q

R

K

L

K

A

A

C

I

L

I

L

L

G

Q

Q

N

H
|
H

G

G

Q

L

I

L

S

T

L

V

G

G

K

T

T

T

L

I

E

D

Q

S

A

A

L

V

W

A

L

W

A

F

I

I

E

M

V

L

E

E

T

K

L

Q

S

C

R

Q

I

V

Y

Q

V

L

Q

L

A

A

L

D

T

A

L

A

G

G

E

Q

P

-

I

T

L

I

P

P

D

I

D

D

E

E

active site: G98 (vs. gap), H117 (= H96), H119 (= H98), Q138 (≠ T126), H172 (= H159)
binding zinc ion: H117 (= H96), H119 (= H98), H172 (= H159)

1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
26% identity, 81% coverage: 11:199/232 of query aligns to 5:209/223 of 1jdiA

query
sites
1jdiA

L

L

R

K

R

R

E

Q

M

V

V

L

D

E

I

A

C

N

R

L

R

A

M

L

N

P

L

K

S

H

G

N

I

L

N

V

Q

T

G

L

T

T

A

W

G

G

N

N

L

V

S

S

V

A

-

V

-

D

R

R

T

E

D

R

D

G

G

V

F

F

L

V

I

I

T

K

P

P

S

S

S

G

M

V

P

D

Y

Y

D

S

T

I

M

M

Q

T

P

A

D

D

L

M

V

V

E

V

M

V

G

S

F

I

D

E

G

T

T

G

Y

E

V

V

-

V

-

E

-

G

G

A

H

K

R

K

P

P

S

S

E
x
D

W

T

R

P

F

T

H

H

R

R

D

L

I

L

L

Y

R

Q

A

A

R

F

T

P

D

S

I

I

D

G

V

G

V

I

L

V

H
|
H

C

T

H
|
H

S

S

I

R

Y

H

A

A

T

T

T

I

L

W

A

A

C

Q

H

A

H

G

K

Q

T

S

I

I

P

P

S

-

F

-

H

-

Y

-

M

-

T

-

G

-

I

-

A

A

G

T

G

G

T
|
T

T

T

I

H

R

A

C
x
D

A

Y

E

F

Y

Y

A

G

T

T

F

I

G

P

-

C

T

T

Q

R

A

K

L

M

S

T

D

D

-

A

-

E

-

I

-

N

-

G

-

E

-

Y

-

E

-

W

-

E

-

T

-

G

N

N

A

V

L

I

L

V

A

E

L

T

K

F

D

E

R

K

L

Q

A

G

-

I

-

D

-

A

-

Q

-

M

-

P

-

G

C

V

L

L

L

V

G

H

Q

S

H
|
H

G

G

Q

P

I

F

S

A

L

W

G

G

K

K

T

N

L

A

E

E

Q

D

A

A

L

V

W

H

L

N

A

A

I

I

E

V

V

L

E

E

T

E

L

V

S

A

R

Y

I

M

Y

G

V

I

Q

F

A

C

L

R

T

Q

L

L

G

A

E

-

P

-

P

P

I

Q

L

L

P

P

D

D

active site: D76 (≠ E77), H95 (= H96), H97 (= H98), T116 (= T125), D120 (≠ C129), H171 (= H159)
binding zinc ion: H95 (= H96), H97 (= H98), H171 (= H159)

P08203 L-ribulose-5-phosphate 4-epimerase AraD; Phosphoribulose isomerase; EC 5.1.3.4 from Escherichia coli (strain K12) (see 4 papers)
26% identity, 81% coverage: 11:199/232 of query aligns to 5:209/231 of P08203

query
sites
P08203

L

L

R

K

R

R

E

Q

M

V

V

L

D

E

I

A

C

N

R

L

R

A

M

L

N

P

L

K

S

H

G

N

I

L

N

V

Q

T

G

L

T

T

A

W

G

G

N
|
N

L

V

S

S

V

A

-

V

-

D

R

R

T

E

D

R

D

G

G

V

F

F

L

V

I

I

T
x
K

P

P

S

S

S

G

M

V

P

D

Y

Y

D

S

T

V

M

M

Q

T

P

A

D

D

L

M

V

V

E

V

M

V

G

S

F

I

D

E

G

T

T

G

Y

E

V

V

-

V

-

E

-

G

G

T

H

K

R

K

P

P

S

S

E
x
D

W

T

R

P

F

T

H

H

R

R

D

L

I

L

L

Y

R

Q

A

A

R

F

T

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-

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M

-

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T

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Y

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N

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N

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D

N28 (= N34) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
K42 (≠ T46) mutation to M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
D76 (≠ E77) 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 (= T125) 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 (≠ C129) mutation to N: Loss of the epimerase activity.
E142 (vs. gap) 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 (= H159) binding

Sites not aligning to the query:

218 H→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.
229 Y→F: Loss of the epimerase activity.

Query Sequence

>SM_b20490 FitnessBrowser__Smeli:SM_b20490
MAETETDKLALRREMVDICRRMNLSGINQGTAGNLSVRTDDGFLITPSSMPYDTMQPDDL
VEMGFDGTYVGHRPSSEWRFHRDILRARTDIDVVLHCHSIYATTLACHHKTIPSFHYMTG
IAGGTTIRCAEYATFGTQALSDNALLALKDRLACLLGQHGQISLGKTLEQALWLAIEVET
LSRIYVQALTLGEPPILPDDEMERVIAQMRRMSYGQAPDPEGVNDVARPRVS

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