SitesBLAST

E45 (= E45) mutation to N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.
R49 (= R49) binding substrate
T73 (= T73) binding substrate
K133 (= K133) binding covalent; mutation to Q: Absence of aldolase activity. Shows a markedly altered substrate specificity relative to the wild-type, with an enhanced activity against pyridine carboxaldehyde, benzaldehyde, and alpha-ketobutyrate; when associated with k-161.
T161 (= T161) binding substrate; mutation to K: Shows activity significantly greater than wild-type. Shows a markedly altered substrate specificity relative to the wild-type, with an enhanced activity against pyridine carboxaldehyde, benzaldehyde, and alpha-ketobutyrate; when associated with Q-133.; mutation to V: Little stereoselectivity, accepting KDPG and KDPGal as substrate with roughly equal efficacy. It strongly diminishes the activity against KDPG and slightly increases activity against KDPGal.
G163 (= G163) binding substrate
N168 (= N168) mutation to S: Shows activity significantly greater than wild-type.
S184 (= S184) binding substrate

1wauA Structure of kdpg aldolase e45n mutant (see paper)
100% identity, 100% coverage: 1:213/213 of query aligns to 1:213/213 of 1wauA

query
sites
1wauA

M

M

K

K

N

N

W

W

K

K

T

T

S

S

A

A

E

E

S

S

I

I

L

L

T

T

G

G

P

P

V

V

P

P

V

V

I

I

V

V

K

K

L

L

E

E

H

H

A

A

V

V

P

P

M

M

A

A

K

K

A

A

L

L

V

V

A

A

G

G

V

V

R

R

V

V

L

L

E
x
N

V

V

T

T

L

L

R
|
R

T

T

E

E

C

C

A

A

V

V

D

D

A

A

I

I

R

R

A

A

I

I

A

A

K

K

E

E

V

V

P

P

E

E

A

A

I

I

V

V

G

G

A

A

G

G

T

T

V

V

L

L

N

N

P

P

Q

Q

L

L

A

A

E

E

V

V

T

T

E

E

A

A

G

G

A

A

Q

Q

F

F

A

A

I

I

S

S

P

P

G

G

L

L

T

T

E

E

P

P

L

L

K

K

A

A

T

T

E

E

G

G

T

T

I

I

P

P

L

L

I

I

P

P

G

G

I

I

S

S

T

T

V

V

S

S

E

E

L

L

M

M

L

L

G

G

M

M

D

D

Y

Y

G

G

L

L

K

K

E

E

F

F

K
|
K

F

F

P

P

A

A

E

E

A

A

N

N

G

G

V

V

K

K

A

A

L

L

Q

Q

A

A

I

I

A

A

G

G

P

P

F

F

S

S

Q

Q

V

V

R

R

F

F

C

C

P

P

T

T

G
|
G

I

I

S

S

P

P

A

A

N

N

Y

Y

R

R

D

D

Y

Y

L

L

A

A

L

L

K

K

S

S

V

V

L

L

C

C

I

I

G

G

S
|
S

W

W

L

L

V

V

P

P

A

A

D

D

A

A

L

L

E

E

A

A

G

G

D

D

Y

Y

D

D

R

R

I

I

T

T

K

K

L

L

A

A

R

R

E

E

A

A

V

V

E

E

G

G

A

A

K

K

L

L

active site: N45 (≠ E45), R49 (= R49), K133 (= K133)
binding sulfate ion: G162 (= G162), G163 (= G163), S184 (= S184)

2c0aB Mechanism of the class i kdpg aldolase (see paper)
100% identity, 100% coverage: 1:213/213 of query aligns to 2:214/214 of 2c0aB

query
sites
2c0aB

M

M

K

K

N

N

W
|
W

K

K

T

T

S
|
S

A
|
A

E
|
E

S

S

I

I

L

L

T

T

G

G

P

P

V

V

P

P

V

V

I

I

V

V

K

K

L

L

E

E

H

H

A

A

V

V

P

P

M

M

A

A

K

K

A

A

L

L

V

V

A

A

G

G

V

V

R

R

V

V

L

L

E
x
N

V

V

T

T

L

L

R
|
R

T

T

E

E

C

C

A

A

V

V

D

D

A

A

I

I

R

R

A

A

I

I

A

A

K

K

E

E

V

V

P

P

E

E

A

A

I

I

V

V

G

G

A

A

G

G

T

T

V

V

L

L

N

N

P

P

Q

Q

L

L

A

A

E

E

V

V

T

T

E

E

A

A

G

G

A

A

Q

Q

F

F

A

A

I

I

S

S

P

P

G

G

L

L

T

T

E

E

P

P

L

L

K

K

A

A

T

T

E

E

G

G

T

T

I

I

P

P

L

L

I

I

P

P

G

G

I

I

S

S

T

T

V

V

S

S

E

E

L

L

M

M

L

L

G

G

M

M

D

D

Y

Y

G

G

L

L

K

K

E
|
E

F

F

K
|
K

F

F

P

P

A

A

E

E

A

A

N

N

G

G

V

V

K

K

A

A

L

L

Q

Q

A

A

I

I

A

A

G

G

P

P

F

F

S

S

Q

Q

V

V

R

R

F

F

C

C

P

P

T

T

G

G

I

I

S

S

P

P

A

A

N

N

Y

Y

R

R

D

D

Y

Y

L

L

A

A

L

L

K

K

S

S

V

V

L

L

C

C

I

I

G

G

S

S

W

W

L

L

V

V

P

P

A

A

D

D

A

A

L

L

E

E

A

A

G

G

D

D

Y

Y

D

D

R

R

I

I

T

T

K

K

L

L

A

A

R

R

E

E

A

A

V

V

E

E

G

G

A

A

K

K

L

L

active site: N46 (≠ E45), R50 (= R49), K134 (= K133)
binding phosphate ion: W5 (= W4), S8 (= S7), A9 (= A8), E10 (= E9), E132 (= E131)

Sites not aligning to the query:

binding phosphate ion: 1

6oviA Crystal structure of kdpg aldolase from legionella pneumophila with pyruvate captured at low ph as a covalent carbinolamine intermediate
53% identity, 94% coverage: 4:203/213 of query aligns to 1:200/210 of 6oviA

query
sites
6oviA

W

W

K

K

T

T

S

Q

A

P

E

G

S

A

I

V

L

F

T

A

G

S

P

P

V

V

V

I

P

P

V

V

I

I

V

V

V

I

K

K

K

E

L

L

E

E

H

D

A

A

V

L

P

P

M

L

A

A

K

E

A

A

L

L

V

F

A

A

G

G

V

I

R

H

V

V

L

L

E
|
E

V

V

T

T

L

L

R
|
R

T

T

E

P

C

V

A

A

V

I

D

K

A

A

I

L

R

E

A

L

I

L

A

I

K

N

E

T

V

F

P

P

E

D

A

E

I

L

V

I

G

G

A

A

G

G

T
|
T

V

V

L

I

N

T

P

P

Q

G

Q

Q

L

F

A

H

E

D

V

V

T

V

E

A

A

A

G

G

A

A

Q

R

F

F

A

A

I

I

S

S

P
|
P

G

G

L

Q

T

T

E

R

P

E

L

L

K

I

A

A

A

G

T

Q

E

K

G

S

T

E

I

I

P

P

L

L

I

I

P

P

G

G

I

V

S

A

T

S

V

V

S

S

E

E

L

L

M

M

L

E

G

G

M

L

D

G

Y

M

G

G

L

Y

K

N

E

H

F

F

K
|
K

F

F

F
|
F

P

P

A

A

E

A

A

A

N

A

G

G

V

I

K

P

A

M

L

L

Q

K

A

A

I

I

A

S

G

G

P

V

F

F

S

P

Q

Q

V

V

R

K

F

F

C

C

P

P

T

T

G

G

I

I

S

N

P

S

A

K

N

N

Y

Y

R

E

D

E

Y

Y

L

L

A

C

L

L

K

P

S

N

V

V

L

A

C

C

I

V

G

G

S

S

W

W

L

I

V

V

P

P

A

E

D

E

A

A

L

I

E

K

A

N

G

H

D

N

Y

W

D

S

R

L

I

I

T

T

K

E

L

L

binding 2,2-bis(oxidanyl)propanoic acid: E42 (= E45), R46 (= R49), T70 (= T73), P91 (= P94), K130 (= K133), F132 (= F135)

1mxsA Crystal structure of 2-keto-3-deoxy-6-phosphogluconate (kdpg) aldolase from pseudomonas putida. (see paper)
46% identity, 98% coverage: 1:208/213 of query aligns to 3:210/216 of 1mxsA

query
sites
1mxsA

M

M

K

A

N

D

W

K

K

A

T

A

S

R

A

I

E

D

S

A

I

I

L

C

T

E

T

K

G

A

P

R

V

I

V

L

P

P

V

V

I

I

V

T

V

I

K

A

K

R

L

E

E

E

H

D

A

I

V

L

P

P

M

L

A

A

K

D

A

A

L

L

V

A

A

A

G

G

V

I

R

R

V

T

L

L

E
|
E

V

V

T

T

L

L

R
|
R

T

S

E

Q

C

H

A

G

V

L

D

K

A

A

I

I

R

Q

A

V

I

L

A

R

K

E

E

Q

V

R

P

P

E

E

A

L

I

C

V

V

G

G

A

A

G

G

T
|
T

V

V

L

L

N

D

P

R

Q

S

Q

M

L

F

A

A

E

A

V

V

T

E

E

A

A

A

G

G

A

A

Q

Q

F

F

A

V

I
x
V

S
x
T

P
|
P

G

G

L

I

T

T

E

E

P

D

L

I

L

L

K

E

A

A

A

G

T

V

E

D

G

S

T

E

I

I

P

P

L

L

I

L

P

P

G

G

I

I

S

S

T

T

V

P

S

S

E

E

L

I

M

M

L

M

G

G

M

Y

D

A

Y

L

G

G

L

Y

K

R

E

R

F

F

K
|
K

F

L

F

F

P

P

A

A

E

E

A

I

N

S

G

G

V

V

K

A

A

A

L

I

Q

K

A

A

I

F

A

G

G

G

P

P

F

F

S

G

Q

D

V

I

R

R

F

F

C

C

P

P

T

T

G

G

I

V

S

N

P

P

A

A

N

N

Y

V

R

R

D

N

Y

Y

L

M

A

A

L

L

K

P

S

N

V

V

L

M

C

C

I

V

G

G

G

T

S

T

W

W

L

M

V

L

P

D

A

S

D

S

A

W

L

I

E

K

A

N

G

G

D

D

Y

W

D

A

R

R

I

I

T

E

K

A

L

C

A

S

R

A

E

E

A

A

V

I

active site: E47 (= E45), R51 (= R49), K135 (= K133)
binding sulfate ion: E47 (= E45), R51 (= R49), T75 (= T73), V94 (≠ I92), T95 (≠ S93), P96 (= P94), K135 (= K133)

P00885 2-dehydro-3-deoxy-phosphogluconate aldolase; KDPG-aldolase; Phospho-2-dehydro-3-deoxygluconate aldolase; Phospho-2-keto-3-deoxygluconate aldolase; EC 4.1.2.14 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see paper)
46% identity, 98% coverage: 1:208/213 of query aligns to 13:220/226 of P00885

query
sites
P00885

M

M

K

A

N

D

W

K

K

A

T

A

S

R

A

I

E

D

S

A

I

I

L

C

T

E

T

K

G

A

P

R

V

I

V

L

P

P

V

V

I

I

V

T

V

I

K

A

K

R

L

E

E

E

H

D

A

I

V

L

P

P

M

L

A

A

K

D

A

A

L

L

V

A

A

A

G

G

V

I

R

R

V

T

L

L

E

E

V

V

T

T

L

L

R

R

T

S

E

Q

C

H

A

G

V

L

D

K

A

A

I

I

R

Q

A

V

I

L

A

R

K

E

E

Q

V

R

P

P

E

E

A

L

I

C

V

V

G

G

A

A

G

G

T

T

V

V

L

L

N

D

P

R

Q

S

Q

M

L

F

A

A

E

A

V

V

T

E

E

A

A

A

G

G

A

A

Q

Q

F

F

A

V

I

V

S

T

P

P

G

G

L

I

T

T

E

E

P

D

L

I

L

L

K

E

A

A

A

G

T

V

E

D

G

S

T

E

I

I

P

P

L

L

I

L

P

P

G

G

I

I

S

S

T

T

V

P

S

S

E

E

L

I

M

M

L

M

G

G

M

Y

D

A

Y

L

G

G

L

Y

K

R

E

R

F

F

K
|
K

F

L

F

F

P

P

A

A

E

E

A

I

N

S

G

G

V

V

K

A

A

A

L

I

Q

K

A

A

I

F

A

G

G

G

P

P

F

F

S

G

Q

D

V

I

R

R

F

F

C

C

P

P

T

T

G

G

I

V

S

N

P

P

A

A

N

N

Y

V

R

R

D

N

Y

Y

L

M

A

A

L

L

K

P

S

N

V

V

L

M

C

C

I

V

G

G

G

T

S

G

W

W

L

M

V

L

P

D

A

S

D

S

A

W

L

I

E

K

A

N

G

G

D

D

Y

W

D

A

R

R

I

I

T

E

K

A

L

C

A

S

R

A

E

E

A

A

V

I

K145 (= K133) active site, Schiff-base intermediate with substrate

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

5xsfA Crystal structure of the 2-keto-3-deoxy-6-phosphogluconate aldolase of zymomonas mobilis zm4 with 3-phosphoglycerate
53% identity, 93% coverage: 9:207/213 of query aligns to 6:200/209 of 5xsfA

query
sites
5xsfA

E

D

S

S

I

V

L

M

T

R

T

L

G

A

P

P

V

V

V

M

P

P

V

V

I

L

V
|
V

V

I

K
x
E

K
x
D

L

I

E

A

H
x
D

A

A

V

K

P

P

M

I

A

A

K

E

A

A

L

L

V

V

A

A

G

G

V

L

R

N

V

V

L

L

E

E

V

V

T

T

L

L

R

R

T

T

E

P

C

C

A

A

V

L

D

E

A

A

I

I

R

K

A

-

I

I

A

M

K

K

E

E

V

V

P

P

E

G

A

A

I

V

V

V

G

G

A

A

G

G

T

T

V

V

L

L

N

N

P

A

Q

K

Q

M

L

L

A

D

E

Q

V

A

T

Q

E

E

A

A

G

G

A

C

Q

E

F

F

A

F

I

V

S

S

P

P

G

G

L

L

T

T

E

A

P

D

L

L

L

G

K

K

A

H

A

A

T

V

E

A

G

Q

T

K

I

A

P

A

L

L

I

L

P

P

G

G

I

V

S

A

T

N

V

A

S

A

E

D

L

V

M

M

L

L

G

G

M

L

D

D

Y

L

G

G

L

L

K

D

E

R

F

F

K

K

F

F

P

P

A

A

E

E

A

N

N

I

G

G

V

L

K

P

A

A

L

L

Q

K

A

S

I

M

A

A

G

S

P

V

F

F

S

R

Q

Q

V

V

R

R

F

F

C

C

P

P

T

T

G

G

I

I

S

T

P

P

A

T

N

S

Y

A

R

P

D

K

Y

Y

L

L

A

E

L

N

K

P

S

S

V

I

L

L

C

C

I

V

G

G

S

S

W

W

L

V

V

V

P

P

A

A

D

G

A

-

L

-

E

-

A

K

G

P

D

D

Y

V

D

A

R

K

I

I

T

T

K

A

L

L

A

A

R

K

E

E

A

A

binding 3-hydroxypyruvic acid: V19 (= V22), E21 (≠ K24), D22 (≠ K25), D25 (≠ H28)

3vcrA Crystal structure of a putative kdpg (2-keto-3-deoxy-6- phosphogluconate) aldolase from oleispira antarctica (see paper)
51% identity, 92% coverage: 13:209/213 of query aligns to 10:212/216 of 3vcrA

query
sites
3vcrA

T

N

T

T

G

K

P

P

V

L

V

I

P

P

V

V

I

I

V

V

V

I

K

D

L

L

E

V

H

H

A

A

V

I

P

P

M

M

A

A

K

K

A

A

L

L

V

V

A

A

G

G

V

V

R

H

V

L

L

L

E
|
E

V

V

T

T

L

L

R
|
R

T

T

E

E

C

A

A

G

V

L

D

A

A

A

I

I

R

S

A

A

I

I

A

K

K

K

E

A

V

V

P

P

E

E

A

A

I

I

V

V

G

G

A

A

G

G

T
|
T

V

V

L

C

N

T

P

A

Q

D

L

F

A

Q

E

K

V

A

T

I

E

D

A

A

G

G

A

A

Q

Q

F

F

A

I

I
x
V

S
|
S

P
|
P

G

G

L

L

T

T

E

P

P

E

L

L

L

I

K

E

A

K

A

A

T

K

E

Q

G

V

T

K

I

L

P

D

-

G

-

Q

-

W

-

Q

-

G

-

V

L

F

I

L

P

P

G

G

I

V

S

A

T

T

V

A

S

S

E

E

L

V

M

M

L

I

G

A

M

A

D

Q

Y

A

G

G

L

I

K

T

E

Q

F

L

K
|
K

F

C

F

F

P

P

A

A

E

S

A

A

N

I

G

G

V

A

K

K

A

L

L

L

Q

K

A

A

I

W

A

S

G

G

P

P

F

F

S

P

Q

D

V

I

R

Q

F

F

C

C

P

P

T

T

G

G

I

I

S

S

P

K

A

D

N

N

Y

Y

R

K

D

E

Y

Y

L

L

A

G

L

L

K

P

S

N

V

V

L

I

C

C

I

A

G

G

S

S

W

W

L

L

V

T

P

E

A

S

D

K

A

L

L

L

E

I

A

E

G

G

D

D

Y

W

D

N

R

E

I

V

T

T

K

R

L

R

A

A

R

S

E

E

A

I

V

V

E

K

active site: E42 (= E45), R46 (= R49), K136 (= K133)
binding pyruvic acid: R46 (= R49), T70 (= T73), V89 (≠ I92), S90 (= S93), P91 (= P94)

1wa3D Mechanism of the class i kdpg aldolase (see paper)
33% identity, 94% coverage: 9:209/213 of query aligns to 3:197/203 of 1wa3D

query
sites
1wa3D

E

E

S

E

I

L

L

F

T

K

G

H

P

K

V

I

V

V

P

A

V

V

I

L

V

R

V

A

K

N

K

S

L

V

E

E

H

E

A

A

V

K

P

E

M

K

A

A

K

L

A

A

L

V

V

F

A

E

G

G

V

V

R

H

V

L

L

I

E
|
E

V

I

T

T

L

F

R
x
T

T

V

E

P

C

D

A

A

V

D

D

T

A

V

I

I

R

K

A

E

I

L

A

S

-

F

-

L

K

K

E

E

V

-

P

K

E

G

A

A

I

I

V

I

G

G

A

A

G

G

T
|
T

V

V

L

T

N

S

P

V

Q

E

Q

Q

L

C

A

R

E

K

V

A

T

V

E

E

A

S

G

G

A

A

Q

E

F

F

A

I

I

V

S
|
S

P
|
P

G

H

L

L

T

D

E

E

P

E

L

I

L

S

K

Q

A

F

A

C

T

K

E

E

G

K

T

G

I

V

P

F

L

Y

I

M

P

P

G

G

I

V

S

M

T

T

V

P

S

T

E

E

L

L

M

V

L

K

G

A

M

M

D

K

Y

L

G

G

L

H

K

T

E

I

F

L

K
|
K

F

L

F
|
F

P

P

A

G

E

E

A

V

N

V

G

G

G

P

V

-

K

Q

A

F

L

V

Q

K

A

A

I

M

A

K

G

G

P

P

F

F

S

P

Q

N

V

V

R

K

F

F

C

V

P

P

T

T

G

G

G
|
G

I

V

S

N

P

L

A

D

N

N

Y

V

R

C

D

E

Y

W

L

F

A

K

L

-

K

A

S

G

V

V

L

L

C

A

I

V

G

G

-

V

G
|
G

S
|
S

W

A

L

L

V

V

P

-

A

-

D

-

A

-

L

-

E

-

A

K

G

G

D

T

Y

P

D

D

R

E

I

V

T

R

K

E

L

K

A

A

R

K

E

A

A

F

V

V

E

E

active site: E39 (= E45), T43 (≠ R49), K128 (= K133)
binding pyruvic acid: T68 (= T73), S88 (= S93), P89 (= P94), K128 (= K133), F130 (= F135)
binding sulfate ion: G157 (= G163), G177 (= G183), S178 (= S184)

2v82A Kdpgal complexed to kdpgal (see paper)
25% identity, 74% coverage: 16:173/213 of query aligns to 7:165/205 of 2v82A

query
sites
2v82A

P

P

V

L

V

I

P

A

V

I

I

L

V
x
R

V

G

K

I

K

T

L

P

E

D

H

E

A

A

V

L

P

A

M

H

A

V

K

G

A

A

L

V

V

I

A

D

G

A

G

G

V

F

R

D

V

A

L

V

E
|
E

V

I

T

P

L

L

R
x
N

T

S

E

P

C

Q

A

W

V

E

D

Q

A

S

I

I

R

P

A

A

I

I

A

V

K

D

E

A

V

Y

-

G

P

D

E

K

A

A

I

L

V

I

G

G

A

A

G

G

T
|
T

V

V

L

L

N

K

P

P

Q

E

Q

Q

L

V

A

D

E

A

V

L

T

A

E

R

A

M

G

G

A

C

Q

Q

F

L

A

I

I
x
V

S
x
T

P

P

G

N

L

I

T

H

E

S

P

E

L

V

L

I

K

R

A

R

A

A

T

V

E

G

G

Y

T

G

I

M

P

T

L

V

I

C

P

P

G

G

I

C

S

A

T

T

V

A

S

T

E

E

L

A

M

F

L

T

G

A

M

L

D

E

Y

A

G

G

L

A

K

Q

E

A

F

L

K
|
K

F

I

F
|
F

P

P

A

S

E

S

A

A

N

F

G

G

-

P

-

Q

G

Y

V

I

K

K

A

A

L

L

Q

K

A

A

I

V

A

L

G

P

P

-

F

-

S

S

Q

D

V

I

R

A

F

V

C

F

P

A

T
x
V

G

G

I

V

S

T

P

P

A

E

N

N

Y

L

R

A

D

Q

Y

W

L

I

active site: E36 (= E45), N40 (≠ R49), K125 (= K133)
binding 2-keto-deoxy-galactose: R13 (≠ V22), T65 (= T73), V84 (≠ I92), T85 (≠ S93), K125 (= K133), F127 (= F135), V153 (≠ T161)

Sites not aligning to the query:

binding 2-keto-deoxy-galactose: 175, 176, 205

Q6BF16 2-dehydro-3-deoxy-6-phosphogalactonate aldolase; 2-oxo-3-deoxygalactonate 6-phosphate aldolase; 6-phospho-2-dehydro-3-deoxygalactonate aldolase; 6-phospho-2-keto-3-deoxygalactonate aldolase; KDPGal; EC 4.1.2.21 from Escherichia coli (strain K12) (see paper)
25% identity, 74% coverage: 16:173/213 of query aligns to 8:166/205 of Q6BF16

query
sites
Q6BF16

P

P

V

L

V

I

P

A

V

I

I

L

V
x
R

V

G

K

I

K

T

L

P

E

D

H

E

A

A

V

L

P

A

M

H

A

V

K

G

A

A

L

V

V

I

A

D

G

A

G

G

V

F

R

D

V

A

L

V

E
|
E

V

I

T

P

L

L

R

N

T

S

E

P

C

Q

A

W

V

E

D

Q

A

S

I

I

R

P

A

A

I

I

A

V

K

D

E

A

V

Y

-

G

P

D

E

K

A

A

I

L

V

I

G

G

A

A

G

G

T
|
T

V

V

L

L

N

K

P

P

Q

E

Q

Q

L

V

A

D

E

A

V

L

T

A

E

R

A

M

G

G

A

C

Q

Q

F

L

A

I

I

V

S

T

P

P

G

N

L

I

T

H

E

S

P

E

L

V

L

I

K

R

A

R

A

A

T

V

E

G

G

Y

T

G

I

M

P

T

L

V

I

C

P

P

G

G

I

C

S

A

T

T

V

A

S

T

E

E

L

A

M

F

L

T

G

A

M

L

D

E

Y

A

G

G

L

A

K

Q

E

A

F

L

K
|
K

F

I

F

F

P

P

A

S

E

S

A

A

N

F

G

G

-

P

-

Q

G

Y

V

I

K

K

A

A

L

L

Q

K

A

A

I

V

A

L

G

P

P

-

F

-

S

S

Q

D

V

I

R

A

F

V

C

F

P

A

T
x
V

G

G

I

V

S

T

P

P

A

E

N

N

Y

L

R

A

D

Q

Y

W

L

I

R14 (≠ V22) binding substrate
E37 (= E45) mutation to N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.
T66 (= T73) binding substrate
K126 (= K133) active site, Schiff-base intermediate with substrate; binding covalent
V154 (≠ T161) mutation to T: Little stereoselectivity, accepting KDPG and KDPGal as substrate with roughly equal efficacy. Reduced the preference for KDPGal. It diminishes the activity against KDPGal and increases activity against KDPG.

Query Sequence

>15968 FitnessBrowser__Keio:15968
MKNWKTSAESILTTGPVVPVIVVKKLEHAVPMAKALVAGGVRVLEVTLRTECAVDAIRAI
AKEVPEAIVGAGTVLNPQQLAEVTEAGAQFAISPGLTEPLLKAATEGTIPLIPGISTVSE
LMLGMDYGLKEFKFFPAEANGGVKALQAIAGPFSQVRFCPTGGISPANYRDYLALKSVLC
IGGSWLVPADALEAGDYDRITKLAREAVEGAKL

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