SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 16884 FitnessBrowser__Keio:16884 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 17 hits to proteins with known functional sites (download)

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)
100% identity, 100% coverage: 1:215/215 of query aligns to 1:215/215 of P0AB87

query
sites
P0AB87

M

M

E

E

R

R

N

N

K

K

L

L

A

A

R

R

Q

Q

I

I

D

D

T

T

C

C

L

L

E

E

M

M

T

T

R

R

L

L

G

G

L

L

N

N

Q

Q

G

G

T
|
T

A
|
A

G
|
G

N
|
N

V

V

S

S

V

V

R

R

Y

Y

Q

Q

D

D

G

G

M

M

L

L

I

I

T

T

P

P

T
|
T

G
|
G

I

I

P

P

Y

Y

E

E

K

K

L

L

T

T

E

E

S

S

H

H

I

I

V

V

F

F

I

I

D

D

G

G

N

N

G

G

K

K

H

H

E

E

G

G

K

K

L

L

P

P

S
|
S

E
|
E

W

W

R

R

F

F

H

H

M

M

A

A

Y

Y

Q

Q

S

S

R

R

P

P

D

D

A

A

N

N

A

A

V

V

H
|
H

N

N

H
|
H

A

A

V

V

H

H

C

C

T

T

A

A

V

V

S

S

I

I

L

L

N

N

R

R

S

S

I

I

P

P

A

A

I

I

H

H

Y
|
Y

M

M

I

I

A

A

G

G

N

N

S

S

I

I

P

P

C

C

A

A

P

P

Y

Y

A

A

T

T

F
|
F

G

G

T

T

R

R

E

E

L

L

S

S

E

E

H

H

V

V

A

A

L

L

A

A

L

L

K

K

N

N

R

R

K

K

A

A

T

T

L

L

Q

Q

H

H

H
|
H

G

G

L

L

I

I

A

A

C

C

E

E

V

V

N

N

L

L

E

E

K

K

A

A

L

L

W

W

L

L

A

A

H

H

E

E

V

V

E

E

V

V

L

L

A

A

Q

Q

L

L

Y

Y

L

L

T

T

L

L

A

A

I

I

T

T

D

D

P

P

V

V

P

P

V

V

L

L

S

S

D

D

E

E

I

I

A

A

V

V

L

L

E

E

K

K

F
|
F

K
|
K

T
|
T

Y
|
Y

G
|
G

L
|
L

R
|
R

I
|
I

E
|
E

T26 (= T26) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
A27 (= A27) mutation Missing: Strong decrease of the aldolase activity.
GN 28:29 (= GN 28:29) binding
N29 (= N29) 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 (= TG 43:44) binding
S71 (= S71) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
SS 71:72 (= SS 71:72) binding
E73 (= E73) 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 (= H92) binding
H94 (= H94) binding
Y113 (= Y113) 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 (= F131) 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 (= H155) binding
F206 (= F206) 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.
207:215 (vs. 207:215, 100% identical) mutation Missing: Loss of aldolase activity. Has a slight preference for the D-aldehyde.
Y209 (= Y209) 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.
LRIEE 211:215 (= LRIEE 211:215) mutation Missing: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).

2fuaA L-fuculose 1-phosphate aldolase crystal form t with cobalt (see paper)
100% identity, 98% coverage: 1:210/215 of query aligns to 1:210/210 of 2fuaA

query
sites
2fuaA

M

M

E

E

R

R

N

N

K

K

L

L

A

A

R

R

Q

Q

I

I

D

D

T

T

C

C

L

L

E

E

M

M

T

T

R

R

L

L

G

G

L

L

N

N

Q

Q

G

G

T

T

A

A

G

G

N

N

V

V

S

S

V

V

R

R

Y

Y

Q

Q

D

D

G

G

M

M

L

L

I

I

T

T

P

P

T

T

G

G

I

I

P

P

Y

Y

E

E

K

K

L

L

T

T

E

E

S

S

H

H

I

I

V

V

F

F

I

I

D

D

G

G

N

N

G

G

K

K

H

H

E

E

G

G

K

K

L

L

P

P

S

S

E
|
E

W

W

R

R

F

F

H

H

M

M

A

A

Y

Y

Q

Q

S

S

R

R

P

P

D

D

A

A

N

N

A

A

V

V

H
|
H

N

N

H
|
H

A

A

V

V

H

H

C

C

T

T

A

A

V

V

S

S

I

I

L

L

N

N

R

R

S

S

I

I

P

P

A

A

I

I

H

H

Y
|
Y

M

M

I

I

A

A

A
|
A

A

A

G

G

N

N

S

S

I

I

P

P

C

C

A

A

P

P

Y

Y

A

A

T

T

F

F

G

G

T

T

R

R

E

E

L

L

S

S

E

E

H

H

V

V

A

A

L

L

A

A

L

L

K

K

N

N

R

R

K

K

A

A

T

T

L

L

Q

Q

H

H

H
|
H

G

G

L

L

I

I

A

A

C

C

E

E

V

V

N

N

L

L

E

E

K

K

A

A

L

L

W

W

L

L

A

A

H

H

E

E

V

V

E

E

V

V

L

L

A

A

Q

Q

L

L

Y

Y

L

L

T

T

L

L

A

A

I

I

T

T

D

D

P

P

V

V

P

P

V

V

L

L

S

S

D

D

E

E

I

I

A

A

V

V

L

L

E

E

K

K

F

F

K

K

T

T

Y
|
Y

G

G

active site: E73 (= E73), H92 (= H92), H94 (= H94), Y113 (= Y113), A117 (= A117), H155 (= H155), Y209 (= Y209)
binding cobalt (ii) ion: E73 (= E73), H92 (= H92), H94 (= H94), H155 (= H155)

1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
100% identity, 97% coverage: 1:209/215 of query aligns to 1:209/209 of 1dzuP

query
sites
1dzuP

M

M

E

E

R

R

N

N

K

K

L

L

A

A

R

R

Q

Q

I

I

D

D

T

T

C

C

L

L

E

E

M

M

T

T

R

R

L

L

G

G

L

L

N

N

Q

Q

G

G

T

A

A

A

G

G

N

N

V

V

S

S

V

V

R

R

Y

Y

Q

Q

D

D

G

G

M

M

L

L

I

I

T

T

P

P

T

T

G

G

I

I

P

P

Y

Y

E

E

K

K

L

L

T

T

E

E

S

S

H

H

I

I

V

V

F

F

I

I

D

D

G

G

N

N

G

G

K

K

H

H

E

E

G

G

K

K

L

L

P

P

S

S

E
|
E

W

W

R

R

F

F

H

H

M

M

A

A

Y

Y

Q

Q

S

S

R

R

P

P

D

D

A

A

N

N

A

A

V

V

H
|
H

N

N

H
|
H

A

A

V

V

H

H

C

C

T

T

A

A

V

V

S

S

I

I

L

L

N

N

R

R

S

S

I

I

P

P

A

A

I

I

H

H

Y

Y

M

M

I

I

A

A

G

G

N

N

S

S

I

I

P

P

C

C

A

A

P

P

Y

Y

A

A

T

T

F

F

G

G

T

T

R

R

E

E

L

L

S

S

E

E

H

H

V

V

A

A

L

L

A

A

L

L

K

K

N

N

R

R

K

K

A

A

T

T

L

L

Q

Q

H

H

H
|
H

G

G

L

L

I

I

A

A

C

C

E

E

V

V

N

N

L

L

E

E

K

K

A

A

L

L

W

W

L

L

A

A

H

H

E

E

V

V

E

E

V

V

L

L

A

A

Q

Q

L

L

Y

Y

L

L

T

T

L

L

A

A

I

I

T

T

D

D

P

P

V

V

P

P

V

V

L

L

S

S

D

D

E

E

I

I

A

A

V

V

L

L

E

E

K

K

F

F

K

K

T

T

Y

Y

binding zinc ion: E73 (= E73), H92 (= H92), H94 (= H94), H155 (= H155)

4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
100% identity, 96% coverage: 1:206/215 of query aligns to 1:206/206 of 4fuaA

query
sites
4fuaA

M

M

E

E

R

R

N

N

K

K

L

L

A

A

R

R

Q

Q

I

I

D

D

T

T

C

C

L

L

E

E

M

M

T

T

R

R

L

L

G

G

L

L

N

N

Q

Q

G

G

T
|
T

A
|
A

G
|
G

N
|
N

V

V

S

S

V

V

R

R

Y

Y

Q

Q

D

D

G

G

M

M

L

L

I

I

T

T

P

P

T
|
T

G
|
G

I

I

P

P

Y

Y

E

E

K

K

L

L

T

T

E

E

S

S

H

H

I

I

V

V

F

F

I

I

D

D

G

G

N

N

G

G

K

K

H

H

E

E

G

G

K

K

L

L

P

P

S
|
S

E
|
E

W

W

R

R

F

F

H

H

M

M

A

A

Y

Y

Q

Q

S

S

R

R

P

P

D

D

A

A

N

N

A

A

V

V

H
|
H

N

N

H
|
H

A

A

V

V

H

H

C

C

T

T

A

A

V

V

S

S

I

I

L

L

N

N

R

R

S

S

I

I

P

P

A

A

I

I

H

H

Y
|
Y

M

M

I

I

A

A

A
|
A

A

A

G

G

N

N

S

S

I

I

P

P

C

C

A

A

P

P

Y

Y

A

A

T

T

F

F

G

G

T

T

R

R

E

E

L

L

S

S

E

E

H

H

V

V

A

A

L

L

A

A

L

L

K

K

N

N

R

R

K

K

A

A

T

T

L

L

Q

Q

H

H

H
|
H

G

G

L

L

I

I

A

A

C

C

E

E

V

V

N

N

L

L

E

E

K

K

A

A

L

L

W

W

L

L

A

A

H

H

E

E

V

V

E

E

V

V

L

L

A

A

Q

Q

L

L

Y

Y

L

L

T

T

L

L

A

A

I

I

T

T

D

D

P

P

V

V

P

P

V

V

L

L

S

S

D

D

E

E

I

I

A

A

V

V

L

L

E

E

K

K

F

F

active site: E73 (= E73), H92 (= H92), H94 (= H94), Y113 (= Y113), A117 (= A117), H155 (= H155)
binding phosphoglycolohydroxamic acid: T26 (= T26), A27 (= A27), G28 (= G28), N29 (= N29), T43 (= T43), G44 (= G44), S71 (= S71), S72 (= S72), E73 (= E73), H92 (= H92), H94 (= H94), H155 (= H155)
binding zinc ion: H92 (= H92), H94 (= H94), H155 (= H155)

7x78A L-fuculose 1-phosphate aldolase (see paper)
89% identity, 96% coverage: 1:206/215 of query aligns to 1:203/203 of 7x78A

query
sites
7x78A

M

M

E

E

R

R

N

N

K
x
R

L

L

A

A

R
|
R

Q

Q

I

I

D

D

T

T

C

C

L

L

E

E

M

M

T

T

R

R

L

L

G

G

L

L

N

N

Q

-

G

-

T

-

A

A

G

G

N
|
N

V

V

S

S

V

V

R

R

Y

Y

Q

Q

D

G

G

G

M

M

L

L

I

I

T

T

P

P

T
|
T

G

G

I

I

P

P

Y

Y

E

E

K

K

L

L

T

T

E

E

S

D

H

K

I

I

V

V

F

F

I

I

D

D

G

A

N

D

G

G

K

Q

H
|
H

E

E

E
x
Q

G
|
G

K

K

L

L

P

P

S
|
S

E
|
E

W

W

R

R

F

F

H

H

M

Q

A

A

Y

Y

Q

Q

S

T

R

R

P

P

D

D

A

A

N

Q

A

A

V

V

H
|
H

N

N

H
|
H

A

A

V

V

H

H

C

C

T

T

A

A

V

V

S

S

I

I

L

L

N

N

R

R

S

P

I

I

P

P

A

A

I

I

H

H

Y

Y

M

M

I

I

A

A

G

G

N

N

S

S

I

I

P

P

C

C

A

A

P

P

Y

Y

A

A

T

T

F

F

G

G

T

T

R

R

E

E

L

L

S

S

E

E

H

H

V

V

A

A

L

V

A

A

L

L

K

K

N

H

R

R

K

K

A

A

T

T

L

L

Q

Q

H

H

H
|
H

G

G

L

L

I

I

A

A

C

C

E

E

V

A

N

S

L

L

E

E

K

K

A

A

L

L

W

W

L

L

A

A

H

H

E

E

V

V

E

E

V

V

L

L

A

A

Q

Q

L

L

Y

Y

L

L

T

S

T

T

L

L

A

A

I

I

T

T

D

D

P

P

V

V

P

P

V

V

L

L

S

D

D

D

E

E

E

A

I

I

A

A

V

I

V

V

L

L

E

E

K

K

F

F

binding magnesium ion: E70 (= E73), H89 (= H92), H91 (= H94), H152 (= H155)
binding sulfate ion: R5 (≠ K5), R8 (= R8), N26 (= N29), T40 (= T43), H61 (= H64), Q63 (≠ E66), G64 (= G67), S68 (= S71), S69 (= S72)

4c25A L-fuculose 1-phosphate aldolase (see paper)
41% identity, 96% coverage: 1:207/215 of query aligns to 4:211/212 of 4c25A

query
sites
4c25A

M

M

E

A

R

S

N

S

K

D

L

V

A

K

R

Q

Q

E

I

L

I

I

D

K

T

Y

C

G

L

K

E

K

M

L

T

V

R

E

L

T

G

D

L

L

N

T

Q

K

G

G

T

T

A
x
G

G

G

N

N

V

L

S

S

V

V

-

F

-

D

R

R

Y

E

Q

K

D

Q

G

L

M

M

L

A

I

I

T

T

P

P

T

S

G

G

I

I

P

D

Y

F

E

F

K

E

L

I

T

K

E

E

S

S

H

D

I

I

V

V

F

V

I

M

D

D

G

I

N

N

G

G

K

N

H

V

E

V

E

E

G

G

-

E

K

R

L

L

P

P

S

S

E
|
E

W

W

R

Y

F

M

H

H

M

L

A

I

A

Q

Y

Y

Q

Q

S

T

R

R

P

D

D

D

A

I

N

D

A

A

V

I

H
|
H

N

A

H
|
H

A

T

V

T

H

Y

C

A

T

T

A

V

V

L

S

A

I

C

L

L

N

R

R

E

S

P

I

L

P

P

A

A

I

S

H

H

Y
|
Y

M

M

I

I

A

A

A

V

A

A

G

G

G

K

N

D

S

-

I

V

P

R

C

V

A

A

P

E

Y

Y

A

A

T

T

F

Y

G

G

T

T

R

K

E

E

L

L

S

A

E

V

H

N

V

A

A

A

L

K

A

A

L

M

K

E

N

G

R

R

K

R

A

A

T

V

L

L

Q

A

H

N

H
|
H

G

G

L

I

I

L

A

A

C

G

E

A

V

Q

N

N

L

L

E

L

K

N

A

A

L

F

W

N

L

I

A

V

H

E

E

E

V

V

E

E

V

Y

L

C

A

A

Q

K

L

I

Y

Y

L

C

T

L

T

A

L

K

A

N

I

F

T

G

D

E

P

P

V

V

P

-

V

V

L

L

S

P

D

D

E

E

I

M

A

E

V

L

V

M

L

A

E

E

K

K

F

F

K

K

active site: E79 (= E73), H98 (= H92), H100 (= H94), Y119 (= Y113), H160 (= H155)
binding zinc ion: G30 (≠ A27), H98 (= H92), H100 (= H94), H160 (= H155)

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)
37% identity, 96% coverage: 4:210/215 of query aligns to 4:211/213 of P0DTQ0

query
sites
P0DTQ0

N

Q

K

K

L

E

A

R

R

E

Q

E

I

I

I

V

D

A

T

Y

C

G

L

K

E

K

M

M

T

I

R

S

L

S

G

G

L

L

N

T

Q

K

G

G

T

T

A

G

G

G

N

N

V

I

S

S

V

I

-

F

-

N

R

R

Y

E

Q

Q

D

G

G

L

M

V

L

A

I

I

T

S

P

P

T

S

G

G

I

L

P

E

Y

Y

E

Y

K

E

L

T

T

K

E

P

S

E

H

D

I

V

V

V

F

I

I

L

D

N

G

L

N

D

G

G

K

E

H

V

E

I

E

E

G

G

-

E

K

R

L

K

P

P

S

S

E
|
E

W

L

R

D

F

M

H

H

M

L

A

I

A

Y

Y

Y

Q

R

S

K

R

R

P

E

D

D

A

I

N

N

A

A

V

L

V

V

H
|
H

N

T

H
|
H

A

S

V

P

H

Y

C

A

T

K

A

T

V

I

S

A

I

S

L

L

N

G

R

W

S

E

I

L

P

P

A

A

I

V

H

S

Y

Y

M

L

I

I

A

A

A

F

A

A

G

G

G

P

N

N

S

-

I

V

P

R

C

C

A

A

P

P

Y

Y

A

E

T

T

F

F

G

G

T

T

R

K

E

Q

L

L

S

A

E

D

H

A

V

A

A

F

L

E

A

G

L

M

K

I

N

D

R

R

K

R

A

A

T

V

L

L

Q

A

H

N

H
|
H

G

G

L

L

I

I

A

A

C

G

E

A

V

N

N

N

L

I

E

K

K

M

A

A

L

F

W

T

L

V

A

A

H

E

E

E

V

I

E

E

V

F

L

C

A

A

Q

Q

L

I

Y

Y

L

Y

T

Q

T

T

L

K

A

S

I

I

T

G

D

E

P

P

V

-

P

K

V

L

L

L

S

P

D

E

E

D

E

E

I

M

A

E

V

N

V

L

L

A

E

K

K

K

F

F

K

E

T

G

Y

Y

G

G

E76 (= E73) binding
H95 (= H92) binding
H97 (= H94) binding
H157 (= H155) binding

6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
36% identity, 94% coverage: 4:206/215 of query aligns to 4:207/207 of 6btgA

query
sites
6btgA

N

Q

K

K

L

E

A

R

R

E

Q

E

I

I

I

V

D

A

T

Y

C

G

L

K

E

K

M

M

T

I

R

S

L

S

G

G

L

L

N

T

Q

K

G

G

T

T

A

G

G

G

N

N

V

I

S

S

V

I

-

F

-

N

R

R

Y

E

Q

Q

D

G

G

L

M

V

L

A

I

I

T

S

P

P

T

S

G

G

I

L

P

E

Y

Y

E

Y

K

E

L

T

T

K

E

P

S

E

H

D

I

V

V

V

F

I

I

L

D

N

G

L

N

D

G

G

K

E

H

V

E

I

E

E

G

G

-

E

K

R

L

K

P

P

S

S

E
|
E

W

L

R

D

F

M

H

H

M

L

A

I

A

Y

Y

Y

Q

R

S

K

R

R

P

E

D

D

A

I

N

N

A

A

V

L

V

V

H
|
H

N

T

H
|
H

A

S

V

P

H

Y

C

A

T

K

A

T

V

I

S

A

I

S

L

L

N

G

R

W

S

E

I

L

P

P

A

A

I

V

H

S

Y
|
Y

M

L

I

I

A

A

A

F

A

A

G

G

G

P

N

N

S

-

I

V

P

R

C

C

A

A

P

P

Y

Y

A

E

T

T

F

F

G

G

T

T

R

K

E

Q

L

L

S

A

E

D

H

A

V

A

A

F

L

E

A

G

L

M

K

I

N

D

R

R

K

R

A

A

T

V

L

L

Q

A

H

N

H
|
H

G

G

L

L

I

I

A

A

C

G

E

A

V

N

N

N

L

I

E

K

K

M

A

A

L

F

W

T

L

V

A

A

H

E

E

E

V

I

E

E

V

F

L

C

A

A

Q

Q

L

I

Y

Y

L

Y

T

Q

T

T

L

K

A

S

I

I

T

G

D

E

P

P

V

-

P

K

V

L

L

L

S

P

D

E

E

D

E

E

I

M

A

E

V

N

V

L

L

A

E

K

K

K

F

F

active site: E76 (= E73), H95 (= H92), H97 (= H94), Y116 (= Y113), H157 (= H155)
binding manganese (ii) ion: E76 (= E73), H95 (= H92), H97 (= H94), H157 (= H155)

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)
29% identity, 84% coverage: 8:187/215 of query aligns to 4:179/181 of Q58813

query
sites
Q58813

R

K

Q

Q

I

F

I

I

D

K

T

I

C

C

L

R

E

K

M

L

T

Y

R

D

L

R

G

K

L

Y

N

V

Q

V

G

G

T

S

A

G

G

G

N
|
N

V

V

S

S

V

V

R

K

Y

E

Q

G

D

D

G

K

M

I

L

Y

I

L

T

T

P

P

T

T

G

G

I

S

P

I

Y

L

E

G

K

F

L

L

T

K

E

E

S

D

H

D

I

I

V

A

F

E

I

M

D

D

G

L

N

D

G

G

K

N

H

V

E

I

E

K

G

G

K

K

L

-

P

P

S

T

S

S

E

E

W

K

R

N

F

L

H

H

M

L

A

M

A

I

Y

Y

Q

R

S

K

R

R

P

N

D

D

A

I

N

N

A

A

V

I

H

H

N

T

H

H

A

S

V

L

H

I

C

S

T

T

A

F

V

L

S

S

I

T

L

I

N

N

R

K

S

E

I

I

P

E

A

-

I

-

H

-

Y

-

M

L

I

L

A

T

A

P

A

E

G

G

G

K

-

I

-

F

-

L

N

K

S

K

I

I

P

G

C

Y

A

V

P

D

Y

Y

A

Y

T

E

F

A

G

G

T

S

R

L

E

K

L

L

S

A

E

E

H

E

V

T

A

-

L

-

A

A

L

K

K

R

N

D

R

E

K

D

A

V

T

I

L

I

L

L

Q

K

H

N

H

H

G

G

L

V

I

V

A

C

C

L

E

G

V

K

N

D

L

L

E

I

K

D

A

A

L

Y

W

I

L

K

A

V

H

E

E

V

V

L

E

E

V

E

L

Q

A

A

Q

K

L

L

Y

T

L

L

T

L

T

N

L

L

A

L

I

V

N25 (= N29) 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
29% identity, 85% coverage: 1:183/215 of query aligns to 2:189/207 of 6voqA

query
sites
6voqA

M

M

E

T

R

E

N

Q

K

Q

L

L

A

R

R

E

Q

E

I

M

I

V

D

Q

T

I

C

G

L

A

E

S

M

L

T

F

R

S

L

R

G

G

L

Y

N

A

Q

T

G

G

T

S

A

A

G

G

N

N

V

L

S

S

V

L

R

L

Y

L

Q

P

D

D

G

G

-

N

M

L

L

L

I

A

T

T

P

P

T

T

G

G

I

A

P

C

Y

L

E

G

K

E

L

L

T

Q

E

A

S

Q

H

R

I

L

V

S

F

V

I

V

D

T

G

L

N

Q

G

G

K

E

H

W

E

I

E

S

G

G

K

D

L

K

P

P

S

S

S

K

E
|
E

W

V

R

T

F

F

H

H

M

R

A

A

A

V

Y

Y

Q

L

S

H

R

N

P

P

D

A

A

C

N

K

A

A

V

I

V

V

H
|
H

N

L

H
|
H

A

S

V

H

H

Y

C

L

T

T

A

A

V

L

S

S

I

C

L

L

-

Q

-

G

-

L

-

D

-

P

-

H

N

N

R

C

S

I

I

R

P

P

A

F

I

T

H

P

Y
|
Y

M

V

I

V

A

M

A

R

A

V

G

G

G

-

N

-

S

D

I

V

P

P

C

V

A

V

P

P

Y

Y

A

Y

T

R

F

P

G

G

T

D

R

D

E

R

L

I

S

A

E

Q

H

A

V

L

A

A

L

G

A

L

L

A

K

P

N

R

R

Y

K

N

A

A

T

F

L

L

Q

A

H

N

H
|
H

G

G

L

P

I

V

A

V

C

T

E

G

V

S

N

S

L

L

E

R

K

E

A

A

L

T

W

N

L

N

A

T

H

E

E

E

V

L

E

E

V

E

L

T

A

A

Q

R

L

L

Y

I

L

F

T

T

active site: E75 (= E73), H94 (= H92), H96 (= H94), Y121 (= Y113), H161 (= H155)
binding zinc ion: E75 (= E73), H94 (= H92), H96 (= H94), H161 (= H155)

4xxfA L-fuculose 1-phosphate aldolase from glaciozyma antarctica pi12 (see paper)
23% identity, 93% coverage: 2:200/215 of query aligns to 18:223/249 of 4xxfA

query
sites
4xxfA

E

E

R

R

N

A

K

W

L

L

A

K

R

E

Q

R

I

L

I

V

D

A

T

A

C

I

L

R

E

I

M

F

T

A

R

N

L

E

G

G

L

F

N

D

Q

H

G

T

T

V

A

A

G

G

N

H

V

L

S

T

V

V

R

R

Y

D

Q

P

D

E

G

N

-

K

-

H

M

F

L

W

I

V

T

N

P

P

T

F

G

G

I

L

P

A

Y

F

E

R

K

L

L

M

T

T

E

V

S

S

H

D

I

L

V

I

F

L

I

V

D

N

-

Q

-

E

-

G

-

T

-

V

-

I

G

G

N

G

G

G

K

K

H

E

E

G

E

R

G

R

K

I

L

V

P

N

S

L

S

A

E
x
G

W

F

R

M

F

I

H

H

M

S

A

A

A

I

Y

H

Q

K

S

A

R

R

P

P

D

E

A

V

N

Q

A

A

V

I

V

C

H
|
H

N

S

H
|
H

A

S

V

T

H

Y

C

G

T

K

A

A

V

F

S

S

I

S

L

L

N

G

R

K

S

P

I

L

P

-

A

-

I

-

H

-

Y

-

M

-

I

-

A

-

A

A

G

I

G

T

N

T

S
x
Q

I

D

P

S

C

C

A

A

P

F

Y

Y

A

G

T

D

F

V

G

A

T

L

-

L

R

G

E

D

L

E

S

S

E

G

H

T

V

I

A

A

L

V

A

A

L

L

K

Q

N

Q

R

K

K

K

A

A

T

I

L

I

L

L

Q

Q

H

N

H
|
H

G

G

L

L

I

L

A

T

C

V

E

G

V

T

N

T

L

I

E

D

K

S

A

A

L

V

-

A

W

W

L

F

A

I

H

M

-

L

-

E

-

K

-

Q

-

C

E

Q

V

V

E

Q

V

L

L

L

A

A

Q

D

L

A

Y

A

L

G

T

Q

T

T

L

I

A

P

I

I

T

D

D

E

P

P

V

Q

P

A

V

A

L

F

S

T

D

F

E

K

E

E

I

L

A

G

active site: G98 (≠ E73), H117 (= H92), H119 (= H94), Q138 (≠ S122), H172 (= H155)
binding zinc ion: H117 (= H92), H119 (= H94), H172 (= H155)

P08203 L-ribulose-5-phosphate 4-epimerase AraD; Phosphoribulose isomerase; EC 5.1.3.4 from Escherichia coli (strain K12) (see 4 papers)
33% identity, 56% coverage: 6:125/215 of query aligns to 5:128/231 of P08203

query
sites
P08203

L

L

A

K

R

R

Q

Q

I

V

I

L

D

E

T

A

C

N

L

L

E

A

M

L

T

P

R

K

L

H

G

N

L

L

N

V

Q

T

G

L

T

T

A

W

G

G

N
|
N

V

V

S

S

V

A

-

V

-

D

R

R

Y

E

Q

R

D

G

G

V

M

F

L

V

I

I

T
x
K

P

P

T

S

G

G

I

V

P

D

Y

Y

E

S

K

V

L

M

T

T

E

A

S

D

H

D

I

M

V

V

F

V

I

V

D

S

-

I

G

E

N

T

G

G

K

E

H

V

E

V

E

E

G

G

-

T

K

K

L

K

P

P

S

S

E
x
D

W

T

R

P

F

T

H

H

M

R

A

L

Y

Y

Q

Q

S

A

R

F

P

P

D

S

A

I

N

G

A

G

V

I

V

V

H
|
H

N

T

H
|
H

A

S

V

R

H

H

C

A

T

T

A

I

V

W

S

A

I

Q

L

A

N

G

R

Q

S

S

I

I

P

P

A

A

I

T

H

G

Y
x
T

M

T

I

H

A

A

A
x
D

A

Y

G

F

G

Y

N

G

S

T

I

I

P

P

C

C

N28 (= N29) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
K42 (≠ T41) mutation to M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
D76 (≠ E73) 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 (= H92) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
H97 (= H94) 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 (≠ Y113) 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 (≠ A117) mutation to N: Loss of the epimerase activity.

Sites not aligning to the query:

142 E→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.
171 binding
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.

1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
33% identity, 56% coverage: 6:125/215 of query aligns to 5:128/223 of 1jdiA

query
sites
1jdiA

L

L

A

K

R

R

Q

Q

I

V

I

L

D

E

T

A

C

N

L

L

E

A

M

L

T

P

R

K

L

H

G

N

L

L

N

V

Q

T

G

L

T

T

A

W

G

G

N

N

V

V

S

S

V

A

-

V

-

D

R

R

Y

E

Q

R

D

G

G

V

M

F

L

V

I

I

T

K

P

P

T

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G

G

I

V

P

D

Y

Y

E

S

K

I

L

M

T

T

E

A

S

D

H

D

I

M

V

V

F

V

I

V

D

S

-

I

G

E

N

T

G

G

K

E

H

V

E

V

E

E

G

G

-

A

K

K

L

K

P

P

S

S

E
x
D

W

T

R

P

F

T

H

H

M

R

A

L

Y

Y

Q

Q

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A

R

F

P

P

D

S

A

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N

G

A

G

V

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H
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H

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T

H
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H

A

S

V

R

H

H

C

A

T

T

A

I

V

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S

A

I

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L

A

N

G

R

Q

S

S

I

I

P

P

A

A

I

T

H

G

Y
x
T

M

T

I

H

A

A

A
x
D

A

Y

G

F

G

Y

N

G

S

T

I

I

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P

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C

active site: D76 (≠ E73), H95 (= H92), H97 (= H94), T116 (≠ Y113), D120 (≠ A117)
binding zinc ion: H95 (= H92), H97 (= H94)

Sites not aligning to the query:

active site: 171
binding zinc ion: 171

4m6rA Structural and biochemical basis for the inhibition of cell death by apip, a methionine salvage enzyme (see paper)
27% identity, 48% coverage: 1:104/215 of query aligns to 1:109/224 of 4m6rA

query
sites
4m6rA

M

M

E

D

R

K

N

E

K

H

L

P

A

R

R

Y

Q

L

I

I

I

P

D

E

T

L

C

C

L

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E

Q

M

F

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Y

R

H

L

L

G

G

L

W

N

V

Q

T

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G

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T

A

G

G

G

N

G

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I

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S

V

L

R

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Y

H

Q

G

D

D

G

E

M

I

L

Y

I

I

T

A

P

P

T

S

G

G

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K

E

E

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I

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Q

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P

S

E

H

D

I

M

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F

F

V

I

C

D

D

G

I

N

N

G

E

K

K

H

D

E

I

E

S

G

G

K

P

L

S

P

P

S

S

S

K

E

K

W

L

R

K

-

K

-

S

-

Q

-

C

-

T

-

P

F

L

H

F

M

M

A

N

A

A

Y

Y

Q

T

S

M

R

R

P

-

D

G

A

A

N

G

A

A

V

V

V

I

H
|
H

N

T

H
|
H

A

S

V

K

H

A

C

A

T

V

A

M

V

A

S

T

I

L

L

L

binding zinc ion: H97 (= H92), H99 (= H94)

Sites not aligning to the query:

binding zinc ion: 177

Q96GX9 Methylthioribulose-1-phosphate dehydratase; MTRu-1-P dehydratase; APAF1-interacting protein; hAPIP; EC 4.2.1.109 from Homo sapiens (Human) (see 5 papers)
30% identity, 40% coverage: 10:95/215 of query aligns to 28:118/242 of Q96GX9

query
sites
Q96GX9

I

I

I

P

D

E

T

L

C

C

L

K

E

Q

M

F

T

Y

R

H

L

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G

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T

A

G

G

G

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G

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H

Q

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D

D

G

E

M

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T

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Y

K

E

E

K

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I

T

Q

E

P

S

E

H

D

I

M

V

F

F

V

I
x
C

D

D

G

I

N

N

G

E

K

K

H

D

E

I

E
x
S

G

G

K

P

L
x
S

P

P

S
|
S

S

K

E

K

W

L

R

K

-

K

-

S

-
x
Q

-
x
C

-

T

-

P

F

L

H

F

M

M

A

N

A

A

Y

Y

Q

T

S

M

R

R

P

-

D

G

A

A

N

G

A

A

V

V

V

I

H
|
H

N

T

H
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H

A

S

C76 (≠ I58) to Y: in dbSNP:rs1977420
S84 (≠ E66) mutation S->A,D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-87 and A,D-89.
S87 (≠ L69) mutation S->A,D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-84 and A,D-89.
S89 (= S71) mutation S->A,D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-84 and A,D-87.
Q96 (vs. gap) mutation to A: Mildly reduced enzyme activity.
C97 (vs. gap) mutation to A: Acts as a dominant negative mutant; unable to use 5'-methylthioadenosine as source of methionine. Does not affect the ability to bind CASP1 and to inhibit cell death induced by CASP9 overexpression.; mutation to A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.
H115 (= H92) mutation to A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.; mutation to A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A-117 and A-195. Unable to inhibit both CASP1 and CASP9 mediated cell death.
H117 (= H94) mutation to A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A-115 and A-195.

Sites not aligning to the query:

7 R → W: in dbSNP:rs2956114
23 H → R: in dbSNP:rs17850326
139 active site, Proton donor/acceptor; E→A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.
181 M → V: in dbSNP:rs17850327
195 H→A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with 87-A--A-89.

P35611 Alpha-adducin; Erythrocyte adducin subunit alpha from Homo sapiens (Human) (see 5 papers)
28% identity, 71% coverage: 35:186/215 of query aligns to 177:333/737 of P35611

query
sites
P35611

Q

Q

D

E

G

H

M

F

L

L

I

I

T

V

P

P

T

F

G

G

I

L

P

L

Y

Y

E

S

K

E

L

V

T

T

E

A

S

S

H

S

I

L

V

V

F

K

I

I

D

N

G

L

N

Q

G

G

K

D

-

I

H

V

E

D

E

R

G

G

K

S

-

T

-

N

-

L

-

G

L

V

P

N

S

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S

A

E

G

W

F

R

T

F

L

H

H

M

S

A

A

A

I

Y

Y

Q

A

S

A

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R

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P

D

D

A

V

N

K

A

C

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V

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H

N

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H

H

A

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V

P

H

A

C

G

T

A

A

A

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V

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S

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A

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M

N

K

R

C

S

G

I

L

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L

A

P

I

I

H

S

Y

P

M

E

I

A

A

L

A

S

A

L

G

G

G

E

N

-

S

-

I

-

P

-

C

V

A

A

P

Y

Y

H

A

D

T

Y

F

H

G

G

T

I

R

L

E

V

L

D

S

E

E

E

H

E

V

K

A

V

L

L

A

I

L

Q

K

K

N

N

-

L

-

G

-

P

-

K

R

S

K

K

A

V

T

L

L

I

L

L

Q

R

H

N

H

H

G

G

L

L

I

V

A

S

C

V

E

G

V

E

N

S

L

V

E

E

K

E

A

A

L

F

W

Y

L

Y

A

I

H

H

E

N

V

L

E

V

V

V

L

A

A

C

Q

E

L

I

Y

Q

L

V

T

R

T

T

L

L

A

A

Sites not aligning to the query:

59 modified: Phosphoserine; by PKA
408 modified: Phosphoserine; by PKA
436 modified: Phosphoserine; by PKA
445 modified: Phosphothreonine; by ROCK2; T→D: Abolishes phosphorylation by ROCK2; when associated with D-480.
460 G → W: in dbSNP:rs4961
480 modified: Phosphothreonine; by ROCK2; T→D: Abolishes phosphorylation by ROCK2; when associated with D-445.
481 modified: Phosphoserine; by PKA
586 S → C: in dbSNP:rs4963
716 modified: Phosphoserine; by PKC
726 modified: Phosphoserine; by PKA and PKC

Q9QYB5 Gamma-adducin; Adducin-like protein 70 from Mus musculus (Mouse) (see paper)
26% identity, 84% coverage: 30:209/215 of query aligns to 161:344/706 of Q9QYB5

query
sites
Q9QYB5

V

I

S

S

V

V

R

R

Y

I

-

S

-

K

-

E

Q

Q

D

D

G

H

M

I

L

I

I

I

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P

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R

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G

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A

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A

S

S

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V

F

K

I

V

D

N

G

I

N

I

G

G

K

E

H

V

-

V

E

D

E

Q

G

G

-

S

-

T

-

D

-

L

K

K

L

I

P

D

S

H

S

T

E

G

W

F

R

S

F

P

H

H

M

A

A

A

A

I

Y

Y

Q

S

S

T

R

R

P

P

D

D

A

V

N

K

A

C

V

V

V

I

H

H

N

I

H

H

A

T

V

L

H

A

C

T

T

A

A

A

V

V

S

S

I

S

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M

N

K

R

C

S

G

I

I

P

L

A

P

I

I

H

S

Y

Q

M

E

I

S

A

L

A

I

A

L

G

G

G

D

N

-

S

-

I

-

P

-

C

V

A

A

P

Y

Y

Y

A

D

T

Y

F

Q

G

G

T

S

-

L

R

D

E

E

L

E

S

E

E

E

H

R

V

I

A

E

L

L

A

Q

L

K

-

V

-

L

-

G

K

P

N

S

R

C

K

K

A

V

T

L

L

V

L

L

Q

R

H

N

H

H

G

G

L

M

I

V

A

A

C

L

E

G

V

E

N

T

L

L

E

E

K

E

A

A

L

F

W

H

L

Y

A

I

H

F

E

N

V

V

E

Q

V

M

L

A

A

C

Q

E

L

I

Y

Q

L

V

T

Q

T

A

L

V

A

A

I

G

T

A

D

G

P

G

V

V

P

-

V

-

L

-

S

-

D

D

E

N

E

L

I

L

A

V

V

L

V

D

L

L

E

Q

K

K

F

Y

K

K

T

A

Y

F

Sites not aligning to the query:

357 Cleavage by asparagine endopeptidase (AEP); N→A: Loss of cleavage by asparagine endopeptidase (AEP).
450 N→A: No effect on cleavage by asparagine endopeptidase (AEP).
457 N→A: No effect on cleavage by asparagine endopeptidase (AEP).

Query Sequence

>16884 FitnessBrowser__Keio:16884
MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFIDG
NGKHEEGKLPSSEWRFHMAAYQSRPDANAVVHNHAVHCTAVSILNRSIPAIHYMIAAAGG
NSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIACEVNLEKALWLAHEVEVLAQL
YLTTLAITDPVPVLSDEEIAVVLEKFKTYGLRIEE

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