SitesBLAST

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)
38% identity, 94% coverage: 7:210/218 of query aligns to 20:224/226 of P00885

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K145 (= K131) active site, Schiff-base intermediate with substrate

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

1euaA Schiff base intermediate in kdpg aldolase from escherichia coli (see paper)
39% identity, 84% coverage: 25:207/218 of query aligns to 27:209/213 of 1euaA

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active site: E45 (= E43), R49 (= R47), K133 (= K131)
binding pyruvic acid: E45 (= E43), T73 (= T71), I92 (≠ V90), K133 (= K131)

P0A955 KHG/KDPG aldolase; EC 4.1.3.16; EC 4.1.2.14 from Escherichia coli (strain K12) (see 3 papers)
39% identity, 84% coverage: 25:207/218 of query aligns to 27:209/213 of P0A955

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E45 (= E43) mutation to N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.
R49 (= R47) binding substrate
T73 (= T71) binding substrate
K133 (= K131) 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 (= T159) 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 (= G161) binding substrate
N168 (= N166) mutation to S: Shows activity significantly greater than wild-type.
S184 (≠ T182) binding substrate

1wauA Structure of kdpg aldolase e45n mutant (see paper)
39% identity, 84% coverage: 25:207/218 of query aligns to 27:209/213 of 1wauA

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active site: N45 (≠ E43), R49 (= R47), K133 (= K131)
binding sulfate ion: G162 (= G160), G163 (= G161), S184 (≠ T182)

2c0aB Mechanism of the class i kdpg aldolase (see paper)
39% identity, 84% coverage: 25:207/218 of query aligns to 28:210/214 of 2c0aB

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active site: N46 (≠ E43), R50 (= R47), K134 (= K131)
binding phosphate ion: E132 (≠ A129)

Sites not aligning to the query:

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

3vcrA Crystal structure of a putative kdpg (2-keto-3-deoxy-6- phosphogluconate) aldolase from oleispira antarctica (see paper)
37% identity, 96% coverage: 2:210/218 of query aligns to 3:215/216 of 3vcrA

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active site: E42 (= E43), R46 (= R47), K136 (= K131)
binding pyruvic acid: R46 (= R47), T70 (= T71), V89 (= V90), S90 (= S91), P91 (= P92)

6oviA Crystal structure of kdpg aldolase from legionella pneumophila with pyruvate captured at low ph as a covalent carbinolamine intermediate
40% identity, 84% coverage: 15:198/218 of query aligns to 14:197/210 of 6oviA

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L

R
|
R

T

T

Q

P

A

V

A

A

A

I

Q

K

A

A

I

L

A

E

N

L

I

L

R

I

A

N

A

T

Y

F

P

P

E

D

I

E

T

L

L

I

C

G

A

A

G

G

T
|
T

V

V

L

I

T

T

P

P

E

G

Q

Q

A

F

D

H

A

D

A

V

I

V

A

A

G

G

A

A

D

R

F

F

V

A

V

I

S

S

P
|
P

G

G

F

Q

N

T

P

R

T

E

T

L

V

L

K

I

Y

A

C

G

L

Q

D

K

N

S

D

E

I

I

K

P

I

L

I

I

P

P

G

G

V

V

N

A

N

S

P

V

S

S

Q

E

V

L

E

M

Q

E

A

G

L

L

E

G

M

M

G

G

V

Y

Q

N

A

H

M

F

K
|
K

F

F

F
|
F

P

P

A

A

E

A

A

A

S

A

G

G

I

I

S

P

M

M

L

L

K

K

S

A

L

I

T

S

G

G

P

V

Y

F

G

P

N

Q

I

V

Q

K

L

F

M

C

P

P

T

T

G

G

V

I

K

N

P

S

T

K

N

N

L

Y

M

E

D

E

Y

Y

L

L

A

C

I

L

S

P

Q

N

V

V

F

A

A

C

C

V

G

G

T

S

W

W

I

I

A

V

P

P

T

E

A

E

A

A

I

I

A

K

A

N

N

H

D

N

W

W

Q

S

S

L

I

I

binding 2,2-bis(oxidanyl)propanoic acid: E42 (= E43), R46 (= R47), T70 (= T71), P91 (= P92), K130 (= K131), F132 (= F133)

5xsfA Crystal structure of the 2-keto-3-deoxy-6-phosphogluconate aldolase of zymomonas mobilis zm4 with 3-phosphoglycerate
39% identity, 81% coverage: 10:186/218 of query aligns to 9:184/209 of 5xsfA

query
sites
5xsfA

L

M

R

R

D

L

L

A

R

P

V

V

M

M

P

P

V

V

I

L

Q
x
V

I

I

E
|
E

N
x
D

A

I

N

A

D
|
D

A

A

V

K

P

P

L

I

A

A

K

E

V

A

L

L

V

V

E

A

N

G

G

G

L

L

P

N

A

V

A

L

E

E

I

V

T

T

F

L

R

R

T

T

Q

P

A

C

A

A

A

L

Q

E

A

A

I

I

A

-

N

K

I

I

R

M

A

K

A

E

Y

V

P

P

E

G

I

A

T

V

L

V

C

G

A

A

G

G

T

T

V

V

L

L

T

N

P

A

E

K

Q

M

A

L

D

D

A

Q

A

A

I

Q

A

E

A

A

G

G

A

C

D

E

F

F

V

F

V

V

S

S

P

P

G

G

F

L

N

T

P

A

T

D

T

L

V

G

K

K

Y

H

C

A

L

V

D

A

N

Q

D

K

I

A

K

A

I

L

P

P

G

G

V

V

N

A

N

N

P

A

S

A

Q

D

V

V

E

M

Q

L

A

G

L

L

E

D

M

L

G

G

V

L

Q

D

A

R

M

F

K

K

F

F

P

P

A

A

E

E

A

N

S

I

G

G

I

L

S

P

M

A

L

L

K

K

S

S

L

M

T

A

G

S

P

V

Y

F

G

R

N

Q

I

V

Q

R

L

F

M

C

P

P

T

T

G

G

V

I

K

T

P

P

T

T

N

S

L

A

M

P

D

K

Y

Y

L

L

A

E

I

N

S

P

Q

S

V

I

F

L

A

C

C

V

G

G

T

S

W

W

I

V

A

V

P

P

binding 3-hydroxypyruvic acid: V19 (≠ Q20), E21 (= E22), D22 (≠ N23), D25 (= D26)

1wa3D Mechanism of the class i kdpg aldolase (see paper)
28% identity, 75% coverage: 8:171/218 of query aligns to 4:167/203 of 1wa3D

query
sites
1wa3D

D

E

A

L

L

F

R

K

D

K

L

H

R

K

V

I

M

V

P

A

V

V

I

L

Q

R

I

A

E

N

N

S

A

V

N

E

D

E

A

A

V

K

P

E

L

K

A

A

K

L

V

A

L

V

V

F

E

E

N

G

G

G

L

V

P

H

A

L

A

I

E
|
E

I

I

T

T

F

F

R
x
T

T

V

Q

P

A

D

A

A

A

D

Q

T

A

V

I

I

A

K

N

E

I

L

R

S

A

F

A

L

Y

K

P

E

E

K

-

G

I

A

T

I

L

I

C

G

A

A

G

G

T
|
T

V

V

L

T

T

S

P

V

E

E

Q

Q

A

C

D

R

A

K

A

A

I

V

A

E

A

S

G

G

A

A

D

E

F

F

V

I

V

V

S
|
S

P
|
P

G

H

F

L

N

D

P

E

T

E

T

I

V

S

K

Q

Y

F

C

C

L

K

D

E

N

K

D

G

I

V

K

F

I

Y

I

M

P

P

G

G

V

V

N

M

N

T

P

P

S

T

Q

E

V

L

E

V

Q

K

A

A

L

M

E

K

M

L

G

G

V

H

Q

T

A

I

M

L

K
|
K

F

L

F
|
F

P

P

A

G

E

E

A

V

S

V

G

G

G

P

I

-

S

Q

M

F

L

V

K

K

S

A

L

M

T

K

G

G

P

P

Y

F

G

P

N

N

I

V

Q

K

L

F

M

V

P

P

T

T

G

G

G
|
G

V

V

K

N

P

L

T

D

N

N

L

V

M

C

D

E

Y

W

L

F

active site: E39 (= E43), T43 (≠ R47), K128 (= K131)
binding pyruvic acid: T68 (= T71), S88 (= S91), P89 (= P92), K128 (= K131), F130 (= F133)
binding sulfate ion: G157 (= G161)

Sites not aligning to the query:

binding sulfate ion: 177, 178

2v82A Kdpgal complexed to kdpgal (see paper)
31% identity, 72% coverage: 16:171/218 of query aligns to 6:165/205 of 2v82A

query
sites
2v82A

M

L

P

P

V

L

I

I

Q

A

I

I

E

L

N
x
R

A

G

-

I

-

T

-

P

N

D

D

E

A

A

V

L

P

A

L

H

A

V

K

G

V

A

L

V

V

I

E

D

N

A

G

G

L

F

P

D

A

A

A

V

E
|
E

I

I

T

P

F

L

R
x
N

T

S

Q

P

A

Q

A

W

A

E

Q

Q

A

S

I

I

A

P

N

A

I

I

R

V

A

D

A

A

Y

Y

P

G

E

D

I

K

T

A

L

L

C

I

-

G

A

A

G

G

T
|
T

V

V

L

L

T

K

P

P

E

E

Q

Q

A

V

D

D

A

A

A

L

I

A

A

R

A

M

G

G

A

C

D

Q

F

L

V

I

V
|
V

S
x
T

P

P

G

N

F

I

N

H

P

S

T

E

T

V

V

I

K

R

Y

R

C

A

L

V

D

G

N

Y

D

G

I

M

K

T

I

V

I

C

P

P

G

G

V

C

N

A

N

T

P

A

S

T

Q

E

V

A

E

F

Q

T

A

A

L

L

E

E

M

A

G

G

V

A

Q

Q

A

A

M

L

K
|
K

F

I

F
|
F

P

P

A

S

E

S

A

A

S

F

G

G

-

P

-

Q

G

Y

I

I

S

K

M

A

L

L

K

K

S

A

L

V

T

L

G

P

P

-

Y

-

G

S

N

D

I

I

Q

A

L

V

M

F

P

A

T
x
V

G

G

V

V

K

T

P

P

T

E

N

N

L

L

M

A

D

Q

Y

W

L

I

active site: E36 (= E43), N40 (≠ R47), K125 (= K131)
binding 2-keto-deoxy-galactose: R13 (≠ N23), T65 (= T71), V84 (= V90), T85 (≠ S91), K125 (= K131), F127 (= F133), V153 (≠ T159)

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)
31% identity, 72% coverage: 16:171/218 of query aligns to 7:166/205 of Q6BF16

query
sites
Q6BF16

M

L

P

P

V

L

I

I

Q

A

I

I

E

L

N
x
R

A

G

-

I

-

T

-

P

N

D

D

E

A

A

V

L

P

A

L

H

A

V

K

G

V

A

L

V

V

I

E

D

N

A

G

G

L

F

P

D

A

A

A

V

E
|
E

I

I

T

P

F

L

R

N

T

S

Q

P

A

Q

A

W

A

E

Q

Q

A

S

I

I

A

P

N

A

I

I

R

V

A

D

A

A

Y

Y

P

G

E

D

I

K

T

A

L

L

C

I

-

G

A

A

G

G

T
|
T

V

V

L

L

T

K

P

P

E

E

Q

Q

A

V

D

D

A

A

A

L

I

A

A

R

A

M

G

G

A

C

D

Q

F

L

V

I

V

V

S

T

P

P

G

N

F

I

N

H

P

S

T

E

T

V

V

I

K

R

Y

R

C

A

L

V

D

G

N

Y

D

G

I

M

K

T

I

V

I

C

P

P

G

G

V

C

N

A

N

T

P

A

S

T

Q

E

V

A

E

F

Q

T

A

A

L

L

E

E

M

A

G

G

V

A

Q

Q

A

A

M

L

K
|
K

F

I

F

F

P

P

A

S

E

S

A

A

S

F

G

G

-

P

-

Q

G

Y

I

I

S

K

M

A

L

L

K

K

S

A

L

V

T

L

G

P

P

-

Y

-

G

S

N

D

I

I

Q

A

L

V

M

F

P

A

T
x
V

G

G

V

V

K

T

P

P

T

E

N

N

L

L

M

A

D

Q

Y

W

L

I

R14 (≠ N23) binding substrate
E37 (= E43) mutation to N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.
T66 (= T71) binding substrate
K126 (= K131) active site, Schiff-base intermediate with substrate; binding covalent
V154 (≠ T159) 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_068333494.1 NCBI__GCF_001650345.1:WP_068333494.1
MKTNTWIDALRDLRVMPVIQIENANDAVPLAKVLVENGLPAAEITFRTQAAAQAIANIRA
AYPEITLCAGTVLTPEQADAAIAAGADFVVSPGFNPTTVKYCLDNDIKIIPGVNNPSQVE
QALEMGVQAMKFFPAEASGGISMLKSLTGPYGNIQLMPTGGVKPTNLMDYLAISQVFACG
GTWIAPTAAIAANDWQSIATNVRETCKLLDQSPNQSQS

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