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)
55% identity, 83% coverage: 30:211/218 of query aligns to 26:207/213 of P0A955

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E45 (= E49) mutation to N: Aldolase activity is significantly impaired.
R49 (= R53) binding pyruvate
T73 (= T77) binding pyruvate
K133 (= K137) 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 (≠ T172) mutation to S: Shows activity significantly greater than wild-type.
S184 (= S188) 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)
54% identity, 83% coverage: 30:211/218 of query aligns to 26:207/213 of 1wauA

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active site: N45 (≠ E49), R49 (= R53), K133 (= K137)
binding sulfate ion: G162 (= G166), G163 (= G167), S184 (= S188)

2c0aB Mechanism of the class i kdpg aldolase (see paper)
54% identity, 83% coverage: 30:211/218 of query aligns to 27:208/214 of 2c0aB

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active site: N46 (≠ E49), R50 (= R53), K134 (= K137)
binding phosphate ion: E132 (≠ Q135)

Sites not aligning to the query:

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

1mxsA Crystal structure of 2-keto-3-deoxy-6-phosphogluconate (kdpg) aldolase from pseudomonas putida. (see paper)
47% identity, 93% coverage: 15:217/218 of query aligns to 13:215/216 of 1mxsA

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active site: E47 (= E49), R51 (= R53), K135 (= K137)
binding sulfate ion: E47 (= E49), R51 (= R53), T75 (= T77), V94 (= V96), T95 (≠ S97), P96 (= P98), K135 (= K137)

6oviA Crystal structure of kdpg aldolase from legionella pneumophila with pyruvate captured at low ph as a covalent carbinolamine intermediate
45% identity, 93% coverage: 15:216/218 of query aligns to 8:209/210 of 6oviA

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binding 2,2-bis(oxidanyl)propanoic acid: E42 (= E49), R46 (= R53), T70 (= T77), P91 (= P98), K130 (= K137), F132 (= F139)

5xsfA Crystal structure of the 2-keto-3-deoxy-6-phosphogluconate aldolase of zymomonas mobilis zm4 with 3-phosphoglycerate
46% identity, 93% coverage: 15:217/218 of query aligns to 8:206/209 of 5xsfA

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K

K

R

A

A

binding 3-hydroxypyruvic acid: V19 (≠ A26), E21 (≠ D28), D22 (= D29), D25 (≠ H32)

1wa3D Mechanism of the class i kdpg aldolase (see paper)
31% identity, 85% coverage: 11:195/218 of query aligns to 1:188/203 of 1wa3D

query
sites
1wa3D

Q

K

L

M

L

E

D

E

I

L

M

F

R

K

A

K

S

H

A

K

V

I

I

V

P

A

V

V

I

L

A

R

I

A

D

N

D

S

I

V

D

E

H

E

A

A

V

K

P

E

L

K

A

A

K

L

A

A

L

V

V

F

A

E

G

G

I

V

R

H

V

L

L

I

E
|
E

V

I

T

T

L

F

R
x
T

T

V

V

P

H

D

G

A

L

D

P

T

A

V

I

I

R

K

A

E

I

L

A

S

E

F

-

L

Q

K

V

E

P

K

G

G

A

A

I

I

V

I

G

G

V

A

G

G

T
|
T

L

V

T

T

Q

S

A

V

D

E

E

Q

F

C

V

R

A

K

A

A

R

V

D

E

A

S

G

G

A

A

V

E

F

F

G

I

V

V

S
|
S

P
|
P

G

H

L

L

T

D

P

E

A

E

L

I

I

S

A

Q

A

F

A

C

K

K

S

E

S

K

G

G

L

V

P

F

L

Y

L

M

P

P

G

G

V

V

M

M

T

T

P

P

S

T

E

E

V

L

M

V

A

K

A

A

R

M

E

K

A

L

G

G

F

H

R

T

Q

I

L

L

K
|
K

L

L

F
|
F

P

P

A

G

V

-

P

E

A

V

G

V

G

G

V

P

G

Q

M

F

L

V

N

K

A

A

I

M

A

K

G

G

P

P

L

F

G

P

D

N

V

V

T

K

F

F

C

V

P

P

T

T

G

G

G
|
G

I

V

S

N

L

L

E

D

T

N

A

V

P

C

D

E

F

W

L

F

A

K

C

A

K

G

N

V

V

L

A

A

C

V

V

G

G

V

G
|
G

S
|
S

W

A

L

L

-

V

-

K

-

G

T

T

P

P

K

D

D

E

V

V

active site: E39 (= E49), T43 (≠ R53), K128 (= K137)
binding pyruvic acid: T68 (= T77), S88 (= S97), P89 (= P98), K128 (= K137), F130 (= F139)
binding sulfate ion: G157 (= G167), G177 (= G187), S178 (= S188)

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)
27% identity, 90% coverage: 16:211/218 of query aligns to 1:195/205 of Q6BF16

query
sites
Q6BF16

M

M

R

Q

A

W

S

Q

A

T

V

K

I

L

P

P

V

L

I

I

A

A

I

I

-

L

-

R

-

G

D

I

D

T

I

P

D

D

H

E

A

A

V

L

P

A

L

H

A

V

K

G

A

A

L

V

V

I

A

D

G

A

G

G

I

F

R

D

V

A

L

V

E
|
E

V

I

T

P

L

L

R

N

T

S

V

P

H

Q

G

W

L

E

P

Q

A

S

I

I

R

P

A

A

I

I

A

V

E

D

Q

A

V

Y

-

G

P

D

G

K

A

A

I

L

V

I

G

G

V

A

G

G

T

T

L

V

T

L

Q

K

A

P

D

E

E

Q

F

V

V

D

A

A

A

L

R

A

D

R

A

M

G

G

A

C

V

Q

F

L

G

I

V

V

S

T

P

P

G

N

L

I

T

H

P

S

A

E

L

V

I

I

A

R

A

A

K

V

S

G

S

Y

G

G

L

M

P

T

L

V

L

C

P

P

G

G

V

C

M

A

T

T

P

A

S

T

E

E

V

A

M

F

A

T

A

A

R

L

E

E

A

A

G

G

F

A

R

Q

Q

A

L

L

K
|
K

L

I

F

F

P

P

A

S

V

-

P

S

A

A

G

F

G

G

V

P

G

Q

M

Y

L

I

N

K

A

A

I

L

A

K

G

A

P

V

L

L

-

P

G

S

D

D

V

I

T

A

F

V

C

F

P

A

T
x
V

G

G

I

V

S

T

L

P

E

E

T

N

A

L

P

A

D

Q

F

W

L

I

A

-

C

-

K

-

N

D

V

A

A

G

C

C

V

A

G

G

G

A

S

G

W

-

L

-

T

L

P

G

K

S

D

D

V

L

L

Y

K

R

S

A

G

G

D

Q

W

S

A

V

R

E

I

R

T

T

A

A

L

Q

A

Q

A

A

E37 (= E49) mutation to N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.
K126 (= K137) 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)
27% identity, 83% coverage: 31:211/218 of query aligns to 18:194/205 of 2v82A

query
sites
2v82A

D

D

H

E

A

A

V

L

P

A

L

H

A

V

K

G

A

A

L

V

V

I

A

D

G

A

G

G

I

F

R

D

V

A

L

V

E
|
E

V

I

T

P

L

L

R
x
N

T

S

V

P

H

Q

G

W

L

E

P

Q

A

S

I

I

R

P

A

A

I

I

A

V

E

D

Q

A

V

Y

-

G

P

D

G

K

A

A

I

L

V

I

G

G

V

A

G

G

T
|
T

L

V

T

L

Q

K

A

P

D

E

E

Q

F

V

V

D

A

A

A

L

R

A

D

R

A

M

G

G

A

C

V

Q

F

L

G

I

V
|
V

S
x
T

P

P

G

N

L

I

T

H

P

S

A

E

L

V

I

I

A

R

A

A

K

V

S

G

S

Y

G

G

L

M

P

T

L

V

L

C

P

P

G

G

V

C

M

A

T

T

P

A

S

T

E

E

V

A

M

F

A

T

A

A

R

L

E

E

A

A

G

G

F

A

R

Q

Q

A

L

L

K
|
K

L

I

F
|
F

P

P

A

S

V

-

P

S

A

A

G

F

G

G

V

P

G

Q

M

Y

L

I

N

K

A

A

I

L

A

K

G

A

P

V

L

L

-

P

G

S

D

D

V

I

T

A

F

V

C

F

P

A

T
x
V

G

G

I

V

S

T

L

P

E

E

T

N

A

L

P

A

D

Q

F

W

L

I

A

-

C

-

K

-

N

D

V

A

A

G

C

C

V

A

G

G

G

A

S

G

W

-

L

-

T

L

P
x
G

K
x
S

D

D

V

L

L

Y

K

R

S

A

G

G

D

Q

W

S

A

V

R

E

I

R

T

T

A

A

L

Q

A

Q

A

A

active site: E36 (= E49), N40 (≠ R53), K125 (= K137)
binding 2-keto-deoxy-galactose: T65 (= T77), V84 (= V96), T85 (≠ S97), K125 (= K137), F127 (= F139), V153 (≠ T165), G175 (≠ P192), S176 (≠ K193)

Sites not aligning to the query:

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

Query Sequence

>WP_061533896.1 NCBI__GCF_001584165.1:WP_061533896.1
MTSANLLYGNQLLDIMRASAVIPVIAIDDIDHAVPLAKALVAGGIRVLEVTLRTVHGLPA
IRAIAEQVPGAIVGVGTLTQADEFVAARDAGAVFGVSPGLTPALIAAAKSSGLPLLPGVM
TPSEVMAAREAGFRQLKLFPAVPAGGVGMLNAIAGPLGDVTFCPTGGISLETAPDFLACK
NVACVGGSWLTPKDVLKSGDWARITALAAAASKLRKAL

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