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)
53% identity, 98% coverage: 2:200/203 of query aligns to 7:209/213 of P0A955

query
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P0A955

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E45 (= E40) mutation to N: Aldolase activity is significantly impaired.
R49 (= R44) binding pyruvate
T73 (= T67) binding pyruvate
K133 (= K127) 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 (= T155) 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 (= N162) mutation to S: Shows activity significantly greater than wild-type.
S184 (= S178) 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.

2c0aB Mechanism of the class i kdpg aldolase (see paper)
52% identity, 98% coverage: 2:200/203 of query aligns to 8:210/214 of 2c0aB

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2c0aB

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active site: N46 (≠ E40), R50 (= R44), K134 (= K127)
binding phosphate ion: S8 (≠ T2), A9 (≠ V3), E10 (= E4), E132 (≠ H125)

Sites not aligning to the query:

binding phosphate ion: 1, 5

1wauA Structure of kdpg aldolase e45n mutant (see paper)
52% identity, 98% coverage: 2:200/203 of query aligns to 7:209/213 of 1wauA

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1wauA

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active site: N45 (≠ E40), R49 (= R44), K133 (= K127)
binding sulfate ion: G162 (= G156), G163 (= G157), S184 (= S178)

6oviA Crystal structure of kdpg aldolase from legionella pneumophila with pyruvate captured at low ph as a covalent carbinolamine intermediate
48% identity, 87% coverage: 6:182/203 of query aligns to 8:185/210 of 6oviA

query
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6oviA

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binding 2,2-bis(oxidanyl)propanoic acid: E42 (= E40), R46 (= R44), T70 (= T67), P91 (= P88), K130 (= K127), F132 (= F129)

3vcrA Crystal structure of a putative kdpg (2-keto-3-deoxy-6- phosphogluconate) aldolase from oleispira antarctica (see paper)
47% identity, 94% coverage: 11:201/203 of query aligns to 13:213/216 of 3vcrA

query
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3vcrA

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active site: E42 (= E40), R46 (= R44), K136 (= K127)
binding pyruvic acid: R46 (= R44), T70 (= T67), V89 (= V86), S90 (= S87), P91 (= P88)

1mxsA Crystal structure of 2-keto-3-deoxy-6-phosphogluconate (kdpg) aldolase from pseudomonas putida. (see paper)
39% identity, 88% coverage: 3:181/203 of query aligns to 10:189/216 of 1mxsA

query
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1mxsA

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V

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L

M

C

C

V

V

G

G

G

T

S

T

W

W

I

M

V

L

active site: E47 (= E40), R51 (= R44), K135 (= K127)
binding sulfate ion: E47 (= E40), R51 (= R44), T75 (= T67), V94 (= V86), T95 (≠ S87), P96 (= P88), K135 (= K127)

1wa3D Mechanism of the class i kdpg aldolase (see paper)
32% identity, 96% coverage: 3:197/203 of query aligns to 2:194/203 of 1wa3D

query
sites
1wa3D

V

M

E

E

Q

E

V

L

M

F

T

K

L

K

A

H

P

K

V

I

I

V

P

A

V

V

L

L

V

R

V

A

H

N

D

S

V

V

K

E

H

E

A

A

R

K

P

E

I

K

A

A

E

L

A

A

L

V

V

F

E

E

G

G

L

V

P

H

A

L

L

I

E
|
E

V

I

T

T

L

F

R
x
T

T

V

P

P

V

D

A

A

L

D

D

T

V

V

I

I

R

K

E

E

M

L

A

S

-

F

-

L

K

K

V

E

E

K

G

G

A

A

V

I

G

G

A

A

G

G

T
|
T

V

V

L

T

N

S

P

V

D

E

D

Q

V

C

K

R

A

K

S

A

V

V

D

E

A

S

G

G

A

A

R

E

F

F

L

I

V

V

S
|
S

P
|
P

G

H

L

L

T

D

D

E

R

E

L

I

A

S

N

Q

A

F

A

C

I

K

G

E

C

K

G

G

L

V

P

F

F

Y

L

M

P

P

G

G

T

V

A

M

N

T

A

P

G

T

D

E

I

L

M

V

R

K

G

A

L

M

D

K

M

L

G

G

L

H

T

T

H

I

F

L

K
|
K

F

L

F
|
F

P

P

A

G

M

E

A

V

N

V

G

G

G

-

V

-

P

P

A

Q

L

F

-

V

K

K

A

A

L

M

A

K

A

G

P

P

L

F

A

P

A

N

A

V

R

K

F

F

C

V

P

P

T

T

G

G

G
|
G

I

V

S

N

E

L

A

D

N

N

A

V

P

C

D

E

W

W

L

F

A

K

L

A

D

-

A

G

V

V

L

L

C

A

V

V

G

G

G

V

S
x
G

W
x
S

I

A

V

L

P

V

P

K

G

G

K

T

P

P

D

D

T

-

A

-

E

E

I

V

T

R

R

E

R

K

A

A

R

K

A

A

active site: E39 (= E40), T43 (≠ R44), K128 (= K127)
binding pyruvic acid: T68 (= T67), S88 (= S87), P89 (= P88), K128 (= K127), F130 (= F129)
binding sulfate ion: G157 (= G157), G177 (≠ S178), S178 (≠ W179)

2v82A Kdpgal complexed to kdpgal (see paper)
31% identity, 80% coverage: 5:167/203 of query aligns to 1:165/205 of 2v82A

query
sites
2v82A

Q

Q

V

W

M

Q

T

T

L

K

A

L

P

P

V

L

I

I

P

A

V

I

L

L

V
x
R

V

G

H

I

D

T

V

P

K

D

H

E

A

A

R

L

P

A

I

H

A

V

E

G

A

A

L

V

V

I

E

D

G

A

G

G

L

F

P

D

A

A

L

V

E
|
E

V

I

T

P

L

L

R
x
N

T

S

P

P

V

Q

A

W

L

E

D

Q

V

S

I

I

R

P

E

A

M

I

A

V

K

D

V

A

E

Y

G

G

-

D

-

K

A

A

V

L

V

I

G

G

A

A

G

G

T
|
T

V

V

L

L

N

K

P

P

D

E

D

Q

V

V

K

D

A

A

S

L

V

A

D

R

A

M

G

G

A

C

R

Q

F

L

L

I

V
|
V

S
x
T

P

P

G

N

L

I

T

H

D

S

R

E

L

V

A

I

N

R

A

R

A

A

I

V

G

G

C

Y

G

G

L

M

P

T

F

V

L

C

P

P

G

G

T

C

A

A

N

T

A

A

G

T

D

E

I

A

M

F

R

T

G

A

L

L

D

E

M

A

G

G

L

A

T

Q

H

A

F

L

K
|
K

F

I

F
|
F

P

P

A

S

M

S

A

A

N

F

G

G

-

P

-

Q

G

Y

V

I

P

K

A

A

L

L

K

K

A

A

L

V

A

-

A

L

P

P

L

S

A

D

A

I

A

A

R

V

F

F

C

A

P

-

T
x
V

G

G

I

V

S

T

E

P

A

E

N

N

A

L

P

A

D

Q

W

W

L

I

active site: E36 (= E40), N40 (≠ R44), K125 (= K127)
binding 2-keto-deoxy-galactose: R13 (≠ V17), T65 (= T67), V84 (= V86), T85 (≠ S87), K125 (= K127), F127 (= F129), V153 (≠ T155)

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 aldolase; EC 4.1.2.21 from Escherichia coli (strain K12) (see paper)
31% identity, 80% coverage: 5:167/203 of query aligns to 2:166/205 of Q6BF16

query
sites
Q6BF16

Q

Q

V

W

M

Q

T

T

L

K

A

L

P

P

V

L

I

I

P

A

V

I

L

L

V

R

V

G

H

I

D

T

V

P

K

D

H

E

A

A

R

L

P

A

I

H

A

V

E

G

A

A

L

V

V

I

E

D

G

A

G

G

L

F

P

D

A

A

L

V

E
|
E

V

I

T

P

L

L

R

N

T

S

P

P

V

Q

A

W

L

E

D

Q

V

S

I

I

R

P

E

A

M

I

A

V

K

D

V

A

E

Y

G

G

-

D

-

K

A

A

V

L

V

I

G

G

A

A

G

G

T

T

V

V

L

L

N

K

P

P

D

E

D

Q

V

V

K

D

A

A

S

L

V

A

D

R

A

M

G

G

A

C

R

Q

F

L

L

I

V

V

S

T

P

P

G

N

L

I

T

H

D

S

R

E

L

V

A

I

N

R

A

R

A

A

I

V

G

G

C

Y

G

G

L

M

P

T

F

V

L

C

P

P

G

G

T

C

A

A

N

T

A

A

G

T

D

E

I

A

M

F

R

T

G

A

L

L

D

E

M

A

G

G

L

A

T

Q

H

A

F

L

K
|
K

F

I

F

F

P

P

A

S

M

S

A

A

N

F

G

G

-

P

-

Q

G

Y

V

I

P

K

A

A

L

L

K

K

A

A

L

V

A

-

A

L

P

P

L

S

A

D

A

I

A

A

R

V

F

F

C

A

P

-

T
x
V

G

G

I

V

S

T

E

P

A

E

N

N

A

L

P

A

D

Q

W

W

L

I

E37 (= E40) mutation to N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.
K126 (= K127) active site, Schiff-base intermediate with substrate
V154 (≠ T155) 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

>WP_011952721.1 NCBI__GCF_000016765.1:WP_011952721.1
MTVEQVMTLAPVIPVLVVHDVKHARPIAEALVEGGLPALEVTLRTPVALDVIREMAKVEG
AVVGAGTVLNPDDVKASVDAGARFLVSPGLTDRLANAAIGCGLPFLPGTANAGDIMRGLD
MGLTHFKFFPAMANGGVPALKALAAPLAAARFCPTGGISEANAPDWLALDAVLCVGGSWI
VPPGKPDTAEITRRARAAAKLGR

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