SitesBLAST

P0A955 KHG/KDPG aldolase; (4S)-4-hydroxy-2-oxoglutarate aldolase; 2-dehydro-3-deoxy-phosphogluconate aldolase; 2-keto-3-deoxy-6-phosphogluconate aldolase; KDPG aldolase; 2-keto-4-hydroxyglutarate aldolase; KHG aldolase; Ketohydroxyglutarate aldolase; Entner-Douderoff aldolase; Oxaloacetate decarboxylase; Phospho-2-dehydro-3-deoxygluconate aldolase; Phospho-2-keto-3-deoxygluconate aldolase; EC 4.1.3.42; EC 4.1.2.14; EC 4.1.1.112 from Escherichia coli (strain K12) (see 5 papers)
29% identity, 84% coverage: 28:214/223 of query aligns to 27:208/213 of P0A955

query
sites
P0A955

E

E

V

H

A

A

K

V

K

P

V

M

V

A

K

K

A

A

C

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Y

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D

A

G

G

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V

R

R

A

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F

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E
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E

F

V

T

T

N

L

R
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R

G

T

D

E

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C

A

A

Q

-

E

-

V

-

F

-

A

V

E

D

I

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V

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K

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Y

A

A

I

A

A

K

K

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M

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x
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K

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T

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x
N

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N

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S

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W

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L

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P

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A

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D

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A

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L

V

E45 (= E46) mutation to N: Aldolase activity is significantly impaired.
R49 (= R50) binding pyruvate
T73 (≠ S78) binding pyruvate
K133 (= K138) active site, Schiff-base intermediate with substrate; binding covalent; mutation to Q: Absence of aldolase activity. Has reduced catalytic efficiency relative to wild-type protein but demonstrates a considerably altered substrate profile with an enhanced activity against pyridine carboxaldehyde, benzaldehyde and alpha-ketobutyrate; when associated with K-161.
T161 (= T165) mutation to A: 13-fold decrease in catalytic efficiency with KDPG as substrate and 250-fold increase in catalytic efficiency with KDPGal as substrate.; mutation to K: Has reduced catalytic efficiency relative to wild-type protein but demonstrates a considerably altered substrate profile with an enhanced activity against pyridine carboxaldehyde, benzaldehyde and alpha-ketobutyrate; when associated with Q-133.; mutation to V: Shows little stereoselectivity, accepting KDPG and KDPGal as substrate with roughly equal efficacy. The change in specificity is accompanied by a very significant loss of activity against KDPG and a 5-fold increase in catalytic efficiency with KDPGal as substrate.
N168 (≠ K172) mutation to S: Shows activity significantly greater than wild-type.
S184 (= S190) mutation to A: 1.35-fold decrease in catalytic efficiency with KDPG as substrate. Has only a modest effect on the catalytic efficiency with KDG or KHO as substrate.; mutation to D: 300-fold decrease in catalytic efficiency with KDPG as substrate. Increases the efficiency for retro-aldol cleavage of both KDG and KHO. Enhances the selectivity for reaction with KHO compared to KDPG by 780-fold.; mutation to L: 4-fold decrease in catalytic efficiency with KDPG as substrate. Increases the efficiency for retro-aldol cleavage of both KDG and KHO. 40-fold increase in catalytic efficiency for the synthesis of KHPB, a precursor of nikkomycin, making this mutant a useful biocatalyst for the preparation of fine chemicals.

1wauA Structure of kdpg aldolase e45n mutant (see paper)
29% identity, 84% coverage: 28:214/223 of query aligns to 27:208/213 of 1wauA

query
sites
1wauA

E

E

V

H

A

A

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V

K

P

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A

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K

A

A

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D

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G

G

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E
x
N

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R

G

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D

E

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C

A

A

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-

E

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V

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A

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K

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V

active site: N45 (≠ E46), R49 (= R50), K133 (= K138)
binding sulfate ion: G162 (= G166), G163 (= G167), S184 (= S190)

2c0aB Mechanism of the class i kdpg aldolase (see paper)
29% identity, 84% coverage: 28:214/223 of query aligns to 28:209/214 of 2c0aB

query
sites
2c0aB

E

E

V

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A

A

K

V

K

P

V

M

V

A

K

K

A

A

C

L

Y

V

D

A

G

G

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V

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R

A

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L

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x
N

F

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T

T

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R

G

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D

-

F

-

A

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Q

T

E

E

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K

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x
E

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K

V

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F

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P

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D

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A

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V

active site: N46 (≠ E46), R50 (= R50), K134 (= K138)
binding phosphate ion: E132 (≠ L136)

Sites not aligning to the query:

binding phosphate ion: 1, 5, 8, 9, 10

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 aldolase; EC 4.1.2.21 from Escherichia coli (strain K12) (see paper)
32% identity, 72% coverage: 34:193/223 of query aligns to 25:180/205 of Q6BF16

query
sites
Q6BF16

V

V

K

G

A

A

C

V

Y

I

D

D

G

A

G

G

V

F

R

D

A

A

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E
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E

F

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P

T

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N

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A

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G

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K

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M

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x
V

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N

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L

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Y

E37 (= E46) mutation to N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.
K126 (= K138) active site, Schiff-base intermediate with substrate
V154 (≠ T165) 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.

2v82A Kdpgal complexed to kdpgal (see paper)
32% identity, 72% coverage: 34:193/223 of query aligns to 24:179/205 of 2v82A

query
sites
2v82A

V

V

K

G

A

A

C

V

Y

I

D

D

G

A

G

G

V

F

R

D

A

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E
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E

F

I

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N
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N

R

S

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Q

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W

A

E

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Q

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S

V

I

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P

A

A

E

I

I

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V

D

K

A

Y

Y

A

G

A

D

K

K

E

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C

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P

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E

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M

-

A

-

I

I

G

G

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A

G

G

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x
T

I

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V

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D

K

P

P

A

E

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Q

A

V

A

D

M

A

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L

L

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G

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V

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x
T

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N

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E

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K

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R

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V

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Y

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T

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K

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F

P

P

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D

S

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A

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K

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A

T
x
V

G

G

V

V

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T

P

P

S

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K

-

E

E

N

N

L

L

T

A

A

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D

A

A

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G

S
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S

K

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L

L

F

Y

active site: E36 (= E46), N40 (= N49), K125 (= K138)
binding 2-keto-deoxy-galactose: T65 (≠ S78), V84 (= V97), T85 (≠ G98), K125 (= K138), F127 (= F140), V153 (≠ T165), G175 (= G189), S176 (= S190)

Sites not aligning to the query:

binding 2-keto-deoxy-galactose: 13, 205

3vcrA Crystal structure of a putative kdpg (2-keto-3-deoxy-6- phosphogluconate) aldolase from oleispira antarctica (see paper)
28% identity, 87% coverage: 18:212/223 of query aligns to 14:209/216 of 3vcrA

query
sites
3vcrA

M

L

V

I

P

P

V

V

F

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Y

V

H

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K

D

D

D

A

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K

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E

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R

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E

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A

A

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L

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A

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A

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K

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A

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A

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K

K

E

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P

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M

A

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G

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x
T

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V

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D

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A

A

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D

A

F

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K

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A

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D

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G

G

A

A

N

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F

F

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V
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V

G
x
S

P
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P

L

G

F

L

N

T

P

P

E

E

I

L

-

I

-

E

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K

-

A

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K

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Q

A

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K

K

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A

A

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A

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G

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C

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K
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K

V

C

F

F

P

P

G

A

D

S

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A

V

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Y

G

G

G

T

A

N

K

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L

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K

G

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A

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M

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K

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M

C

V

P

T

T

G

G

V

I

E

-

P

-

S

S

K

K

E

D

N

N

L

Y

T

K

A

E

W

Y

I

L

K

G

-

L

A

P

G

N

V

V

F

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C

C

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A

G

G

M

-

G

G

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S

K

W

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D

K

K

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V

L

A

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A

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E

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D

D

W

W

A

N

Y

E

V

V

T

T

A

R

K

R

C

A

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S

E

E

active site: E42 (= E46), R46 (= R50), K136 (= K138)
binding pyruvic acid: R46 (= R50), T70 (≠ S78), V89 (= V97), S90 (≠ G98), P91 (= P99)

6oviA Crystal structure of kdpg aldolase from legionella pneumophila with pyruvate captured at low ph as a covalent carbinolamine intermediate
26% identity, 88% coverage: 15:210/223 of query aligns to 11:201/210 of 6oviA

query
sites
6oviA

S

A

T

S

G

P

M

V

V

I

P

P

V

V

F

I

Y

V

H

I

K

K

D

E

A

L

E

E

V

D

A

A

K

L

K

P

V

L

V

A

K

E

A

A

C

L

Y

F

D

A

G

G

V

I

R

H

A

V

F

L

E
|
E

F

V

T

T

N

L

R
|
R

G

T

D

P

F

V

A

A

Q

I

E

K

V

A

F

L

A

E

E

L

I

L

V

I

K

N

Y

-

A

-

K

-

E

T

C

F

P

P

E

D

M

E

A

L

I

I

G

G

I

A

G

G

S
x
T

I

V

V

I

D

T

P

P

A

G

T

Q

A

F

A

H

M

D

Y

V

L

V

Q

A

L

A

G

G

A

A

N

R

F

F

V

A

V

I

G

S

P
|
P

L

G

F

Q

N

T

P

R

E

E

I

L

A

L

K

I

I

A

C

G

N

Q

R

K

R

S

L

E

V

I

A

P

Y

L

T

I

P

P

G

G

C

V

G

A

S

S

V

V

S

S

E

E

V

L

G

M

F

E

A

G

Q

L

E

G

V

M

G

G

C

Y

D

N

L

H

C

F

K
|
K

V

F

F
|
F

P

P

G

A

D

A

V

A

Y

A

-

G

G

G

T

I

N

P

F

M

V

L

K

K

G

A

L

I

M

S

A

G

P

V

M

F

P

P

W

Q

S

V

K

K

L

F

M

C

V

P

T

T

G

G

V

I

E

N

P

-

S

S

K

K

E

N

N

Y

L

E

T

E

A

Y

W

L

I

C

K

L

A

P

G

N

V

V

F

A

C

C

V

V

G

G

M

-

G

G

S

S

K

W

L

I

F

V

P

P

K

E

D

E

K

A

V

I

A

K

A

N

E

H

D

N

W

W

A

S

Y

L

V

I

T

T

A

E

K

L

C

C

binding 2,2-bis(oxidanyl)propanoic acid: E42 (= E46), R46 (= R50), T70 (≠ S78), P91 (= P99), K130 (= K138), F132 (= F140)

1mxsA Crystal structure of 2-keto-3-deoxy-6-phosphogluconate (kdpg) aldolase from pseudomonas putida. (see paper)
25% identity, 97% coverage: 1:217/223 of query aligns to 1:213/216 of 1mxsA

query
sites
1mxsA

M

L

A

S

K

M

F

A

D

D

K

K

I

A

A

A

V

R

L

I

N

D

K

A

I

I

G

C

S

E

T

K

G

A

-

R

M

I

V

L

P

P

V

V

F

I

Y

T

H

I

K

A

D

R

A

E

E

E

V

D

A

I

K

L

K

P

V

L

V

A

K

D

A

A

C

L

Y

A

D

A

G

G

V

I

R

R

A

T

F

L

E
|
E

F

V

T

T

N

L

R
|
R

G

S

D

Q

F

H

A

G

Q

L

E

K

V

A

F

-

A

-

E

-

I

-

V

I

K

Q

Y

V

A

L

A

R

K

E

E

Q

C

R

P

P

E

E

M

L

A

C

I

V

G

G

I

A

G

G

S
x
T

I

V

V

L

D

D

P

R

A

S

T

M

A

F

A

A

M

A

Y

V

L

E

Q

A

L

A

G

G

A

A

N

Q

F

F

V

V

V
|
V

G
x
T

P
|
P

L

G

F

I

N

T

P

E

E

D

I

I

A

L

K

E

I

A

C

G

N

V

R

D

R

S

L

E

V

I

A

P

Y

L

T

L

P

P

G

G

C

I

G

S

S

T

V

P

S

S

E

E

V

I

G

M

F

M

A

G

Q

Y

E

A

V

L

G

G

C

Y

D

R

L

R

C

F

K
|
K

V

L

F

F

P

P

G

A

D

E

V

I

Y

S

-

G

G

G

T

V

N

A

F

A

V

I

K

K

G

A

L

F

M

G

A

G

P

P

M

F

P

G

W

D

S

I

K

R

L

F

M

C

V

P

T

T

G

G

V

V

E

N

P

P

S

A

K

N

-

V

E

R

N

N

L

Y

T

M

A

A

W

L

I

-

K

-

A

P

G

N

V

V

F

M

C

C

V

V

G

G

M

T

G

-

S

T

K

W

L

M

F

L

P

D

K

S

D

S

K

W

V

I

A

K

A

N

E

G

D

D

W

W

A

A

Y

R

V

I

T

E

A

A

K

C

C

S

E

A

E

E

A

A

L

I

S

A

Y

L

I

L

active site: E47 (= E46), R51 (= R50), K135 (= K138)
binding sulfate ion: E47 (= E46), R51 (= R50), T75 (≠ S78), V94 (= V97), T95 (≠ G98), P96 (= P99), K135 (= K138)

5xsfA Crystal structure of the 2-keto-3-deoxy-6-phosphogluconate aldolase of zymomonas mobilis zm4 with 3-phosphoglycerate
26% identity, 89% coverage: 18:216/223 of query aligns to 14:203/209 of 5xsfA

query
sites
5xsfA

M

V

V

M

P

P

V

V

F

L

Y
x
V

H

I

K
x
E

D
|
D

A

I

E

A

V
x
D

A

A

K

K

K

P

V

I

V

A

K

E

A

A

C

L

Y

V

D

A

G

G

V

L

R

N

A

V

F

L

E

E

F

V

T

T

N

L

R

R

G

T

D

P

F

C

A

A

Q

L

E

E

V

A

F

I

A

K

E

I

I

M

V

-

K

-

Y

-

A

-

K

K

E

E

C

V

P

P

E

G

M

A

A

V

I

V

G

G

I

A

G

G

S

T

I

V

V

L

D

N

P

A

A

K

T

M

A

L

A

D

M

Q

Y

A

L

Q

Q

E

L

A

G

G

A

C

N

E

F

F

V

F

V

V

G

S

P

P

L

G

F

L

N

T

P

A

E

D

I

L

A

G

K

K

I

H

C

A

N

V

R

A

R

Q

L

K

V

A

A

A

Y

L

T

L

P

P

G

G

C

V

G

A

S

N

V

A

S

A

E

D

V

V

G

M

F

L

A

G

Q

L

E

D

V

L

G

G

C

L

D

D

L

R

C

F

K

K

V

F

F

F

P

P

G

A

-

E

D

N

V

I

Y

G

G

G

T

L

N

P

F

A

V

L

K

K

G

S

L

M

M

A

A

S

P

V

M

F

P

R

W

Q

S

V

K

R

L

F

M

C

V

P

T

T

G

G

V

I

E

T

P

P

S

T

K

S

-

A

-

P

-

K

-

Y

-

L

E

E

N

N

L

P

T

S

A

-

W

-

I

-

K

-

A

-

G

-

V

I

F

L

C

C

V

V

G

G

M

-

G

G

S

S

K

W

L

V

F

V

P

P

K

A

D

G

K

K

V

-

A

-

E

P

D

D

W

V

A

A

Y

K

V

I

T

T

A

A

K

L

C

A

E

K

E

E

A

A

L

S

S

A

Y

F

binding 3-hydroxypyruvic acid: V19 (≠ Y23), E21 (≠ K25), D22 (= D26), D25 (≠ V29)

Query Sequence

>350017 FitnessBrowser__Btheta:350017
MAKFDKIAVLNKIGSTGMVPVFYHKDAEVAKKVVKACYDGGVRAFEFTNRGDFAQEVFAE
IVKYAAKECPEMAIGIGSIVDPATAAMYLQLGANFVVGPLFNPEIAKICNRRLVAYTPGC
GSVSEVGFAQEVGCDLCKVFPGDVYGTNFVKGLMAPMPWSKLMVTGGVEPSKENLTAWIK
AGVFCVGMGSKLFPKDKVAAEDWAYVTAKCEEALSYIAEARKK

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