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)
43% identity, 94% coverage: 12:207/208 of query aligns to 28:223/226 of P00885

query
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K145 (= K129) 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)
44% identity, 89% coverage: 23:208/208 of query aligns to 27:212/213 of 1euaA

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active site: E45 (= E41), R49 (= R45), K133 (= K129)
binding pyruvic acid: E45 (= E41), T73 (= T69), I92 (≠ V88), K133 (= K129)

P0A955 KHG/KDPG aldolase; EC 4.1.3.16; EC 4.1.2.14 from Escherichia coli (strain K12) (see 3 papers)
44% identity, 89% coverage: 23:208/208 of query aligns to 27:212/213 of P0A955

query
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E45 (= E41) mutation to N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.
R49 (= R45) binding substrate
T73 (= T69) binding substrate
K133 (= K129) 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 (= T157) 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 (= G159) binding substrate
N168 (= N164) mutation to S: Shows activity significantly greater than wild-type.
S184 (= S180) binding substrate

1wauA Structure of kdpg aldolase e45n mutant (see paper)
43% identity, 89% coverage: 23:208/208 of query aligns to 27:212/213 of 1wauA

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active site: N45 (≠ E41), R49 (= R45), K133 (= K129)
binding sulfate ion: G162 (= G158), G163 (= G159), S184 (= S180)

2c0aB Mechanism of the class i kdpg aldolase (see paper)
43% identity, 89% coverage: 23:208/208 of query aligns to 28:213/214 of 2c0aB

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active site: N46 (≠ E41), R50 (= R45), K134 (= K129)
binding phosphate ion: E132 (≠ T127)

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)
38% identity, 99% coverage: 1:206/208 of query aligns to 1:213/216 of 3vcrA

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active site: E42 (= E41), R46 (= R45), K136 (= K129)
binding pyruvic acid: R46 (= R45), T70 (= T69), V89 (= V88), S90 (= S89), P91 (= P90)

6oviA Crystal structure of kdpg aldolase from legionella pneumophila with pyruvate captured at low ph as a covalent carbinolamine intermediate
43% identity, 90% coverage: 13:200/208 of query aligns to 14:201/210 of 6oviA

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V

T

T

F

L

R
|
R

S

T

D

P

A

V

A

A

V

I

E

K

A

A

I

L

R

E

L

L

R

I

Q

N

A

T

Q

F

P

P

D

D

M

E

L

L

I

I

G

G

A

A

G

G

T
|
T

V

V

L

I

T

T

R

P

E

G

Q

Q

V

F

V

H

A

D

A

V

K

V

E

A

A

A

G

G

A

A

S

R

F

F

I

A

V

I

S

S

P
|
P

G

G

F

Q

N

T

P

R

N

E

T

L

V

L

K

I

A

A

C

G

Q

Q

D

K

L

S

N

E

I

I

P

P

I

L

I

I

P

P

G

G

T

V

N

A

N

S

P

V

S

S

T

E

I

L

E

M

A

E

A

G

L

L

E

G

M

M

G

G

L

Y

T

N

T

H

V

F

K
|
K

F

F

F
|
F

P

P

A

A

E

A

A

A

S

A

G

G

V

I

K

P

M

M

I

L

K

K

A

A

L

I

L

S

G

G

P

V

F

F

N

P

Q

Q

L

V

K

K

I

F

M

C

P

P

T

T

G

G

V

I

N

N

A

S

N

K

N

N

I

Y

N

E

D

E

Y

Y

L

L

A

C

I

L

P

P

G

N

V

V

I

A

A

C

C

V

G

G

S

S

W

W

M

I

V

V

D

P

K

E

A

E

L

A

V

I

N

K

A

N

G

H

N

N

W

W

D

S

E

L

I

I

G

T

R

E

L

L

T

C

binding 2,2-bis(oxidanyl)propanoic acid: E42 (= E41), R46 (= R45), T70 (= T69), P91 (= P90), K130 (= K129), F132 (= F131)

5xsfA Crystal structure of the 2-keto-3-deoxy-6-phosphogluconate aldolase of zymomonas mobilis zm4 with 3-phosphoglycerate
36% identity, 82% coverage: 13:183/208 of query aligns to 14:183/209 of 5xsfA

query
sites
5xsfA

I

V

L

M

P

P

V

V

I

L

V
|
V

I

I

D
x
E

K
x
D

A

I

E

A

D
|
D

I

A

V

K

P

P

L

I

G

A

K

E

V

A

L

L

A

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

S

T

D

P

A

C

A

A

V

L

E

E

A

A

I

I

R

K

L

I

L

M

R

K

Q

E

A

V

Q

-

P

P

D

G

M

A

L

V

I

V

G

G

A

A

G

G

T

T

V

V

L

L

T

N

R

A

E

K

Q

M

V

L

V

D

A

Q

A

A

K

Q

E

E

A

A

G

G

A

C

S

E

F

F

I

F

V

V

S

S

P

P

G

G

F

L

N

T

P

A

N

D

T

L

V

G

K

K

A

H

C

A

Q

V

D

A

L

Q

N

K

I

A

P

A

I

L

P

P

G

G

T

V

N

A

N

N

P

A

S

A

T

D

I

V

E

M

A

L

A

G

L

L

E

D

M

L

G

G

L

L

T

D

T

R

V

F

K

K

F

F

P

P

A

A

E

E

A

N

S

I

G

G

V

L

K

P

M

A

I

L

K

K

A

S

L

M

L

A

G

S

P

V

F

F

N

R

Q

Q

L

V

K

R

I

F

M

C

P

P

T

T

G

G

V

I

N

T

A

P

N

T

N

S

I

A

N

P

D

K

Y

Y

L

L

A

E

I

N

P

P

G

S

V

I

I

L

A

C

C

V

G

G

S

S

W

W

M

V

V

V

binding 3-hydroxypyruvic acid: V19 (= V18), E21 (≠ D20), D22 (≠ K21), D25 (= D24)

1wa3D Mechanism of the class i kdpg aldolase (see paper)
33% identity, 98% coverage: 6:208/208 of query aligns to 4:200/203 of 1wa3D

query
sites
1wa3D

E

E

Q

L

I

F

A

K

D

K

L

H

K

K

I

I

L

V

P

A

V

V

I

L

V

R

I

A

D

N

K

S

A

V

E

E

D

E

I

A

V

K

P

E

L

K

G

A

K

L

V

A

L

V

A

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

-

V

-

P

-

D

S

A

D

D

A

T

A

V

V

I

E

K

A

E

I

L

R

S

L

F

L

L

R

K

Q

E

A

K

Q

-

P

-

D

G

M

A

L

I

I

I

G

G

A

A

G

G

T
|
T

V

V

L

T

T

S

R

V

E

E

Q

Q

V

C

V

R

A

K

A

A

K

V

E

E

A

S

G

G

A

A

S

E

F

F

I

I

V

V

S
|
S

P
|
P

G

H

F

L

N

D

P

E

N

E

T

I

V

S

K

Q

A

F

C

C

Q

K

D

E

L

K

N

G

I

V

P

F

I

Y

I

M

P

P

G

G

T

V

N

M

N

T

P

P

S

T

T

E

I

L

E

V

A

K

A

A

L

M

E

K

M

L

G

G

L

H

T

T

T

I

V

L

K
|
K

F

L

F
|
F

P

P

A

G

E

E

A

V

S

V

G

G

G

P

V

-

K

Q

M

F

I

V

K

K

A

A

L

M

L

K

G

G

P

P

F

F

N

P

Q

N

L

V

K

K

I

F

M

V

P

P

T

T

G

G

G
|
G

V

V

N

N

A

L

N

D

N

N

I

V

N

C

D

E

Y

W

L

F

A

K

I

-

P

A

G

G

V

V

I

L

A

A

C

V

G

G

G

-

S

-

W

-

M

-

V

V

D
x
G

K
x
S

A

A

L

L

V

V

N

K

A

-

G

G

N

T

W

P

D

D

E

E

I

V

G

R

R

E

L

K

T

A

R

K

E

A

A

F

V

V

K

E

L

K

V

I

K

R

active site: E39 (= E41), T43 (≠ R45), K128 (= K129)
binding pyruvic acid: T68 (= T69), S88 (= S89), P89 (= P90), K128 (= K129), F130 (= F131)
binding sulfate ion: G157 (= G159), G177 (≠ D184), S178 (≠ K185)

2v82A Kdpgal complexed to kdpgal (see paper)
29% identity, 94% coverage: 14:208/208 of query aligns to 6:197/205 of 2v82A

query
sites
2v82A

L

L

P

P

V

L

I

I

V

A

I

I

D

L

K
x
R

A

G

-

I

-

T

-

P

-

D

E

E

D

A

I

L

V

A

P

H

L

V

G

G

K

A

V

V

L

I

A

-

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

S

S

D

P

A

Q

A

W

V

E

E

Q

A

S

I

I

R

P

L

A

L

I

R

V

Q

D

A

A

Q

Y

P

G

D

D

-

K

M

A

L

L

I

I

G

G

A

A

G

G

T
|
T

V

V

L

L

T

K

R

P

E

E

Q

Q

V

V

V

D

A

A

A

L

K

A

E

R

A

M

G

G

A

C

S

Q

F

L

I

I

V
|
V

S
x
T

P

P

G

N

F

I

N

H

P

S

N

E

T

V

V

I

K

R

A

R

C

A

Q

V

D

G

L

Y

N

G

I

M

P

T

I

V

I

C

P

P

G

G

T

C

N

A

N

T

P

A

S

T

T

E

I

A

E

F

A

T

A

A

L

L

E

E

M

A

G

G

L

A

T

Q

T

A

V

L

K
|
K

F

I

F
|
F

P

P

A

S

E

S

A

A

S

F

G

G

-

P

-

Q

G

Y

V

I

K

K

M

A

I

L

K

K

A

A

L

V

L

L

G

P

P

-

F

-

N

S

Q

D

L

I

K

A

I

V

M

F

P

A

T
x
V

G

G

V

V

N

T

A

P

N

E

N

N

I

L

N

A

D

Q

Y

W

L

I

A

D

I

-

P

-

G

-

V

-

I

A

A

G

C

C

G

A

G

G

S

A

W

G

M

L

V

-

D
x
G

K
x
S

A

D

L

L

V

Y

N

R

A

A

G

G

N

Q

W

-

D

-

E

S

I

V

G

E

R

R

L

T

T

A

R

Q

E

Q

A

A

V

A

K

A

L

F

V

V

K

K

active site: E36 (= E41), N40 (≠ R45), K125 (= K129)
binding 2-keto-deoxy-galactose: R13 (≠ K21), T65 (= T69), V84 (= V88), T85 (≠ S89), K125 (= K129), F127 (= F131), V153 (≠ T157), G175 (≠ D184), S176 (≠ K185)

Sites not aligning to the query:

binding 2-keto-deoxy-galactose: 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)
29% identity, 94% coverage: 14:208/208 of query aligns to 7:198/205 of Q6BF16

query
sites
Q6BF16

L

L

P

P

V

L

I

I

V

A

I

I

D

L

K
x
R

A

G

-

I

-

T

-

P

-

D

E

E

D

A

I

L

V

A

P

H

L

V

G

G

K

A

V

V

L

I

A

-

E

D

N

A

G

G

L

F

P

D

A

A

A

V

E
|
E

I

I

T

P

F

L

R

N

S

S

D

P

A

Q

A

W

V

E

E

Q

A

S

I

I

R

P

L

A

L

I

R

V

Q

D

A

A

Q

Y

P

G

D

D

-

K

M

A

L

L

I

I

G

G

A

A

G

G

T
|
T

V

V

L

L

T

K

R

P

E

E

Q

Q

V

V

V

D

A

A

A

L

K

A

E

R

A

M

G

G

A

C

S

Q

F

L

I

I

V

V

S

T

P

P

G

N

F

I

N

H

P

S

N

E

T

V

V

I

K

R

A

R

C

A

Q

V

D

G

L

Y

N

G

I

M

P

T

I

V

I

C

P

P

G

G

T

C

N

A

N

T

P

A

S

T

T

E

I

A

E

F

A

T

A

A

L

L

E

E

M

A

G

G

L

A

T

Q

T

A

V

L

K
|
K

F

I

F

F

P

P

A

S

E

S

A

A

S

F

G

G

-

P

-

Q

G

Y

V

I

K

K

M

A

I

L

K

K

A

A

L

V

L

L

G

P

P

-

F

-

N

S

Q

D

L

I

K

A

I

V

M

F

P

A

T
x
V

G

G

V

V

N

T

A

P

N

E

N

N

I

L

N

A

D

Q

Y

W

L

I

A

D

I

-

P

-

G

-

V

-

I

A

A

G

C

C

G

A

G

G

S

A

W

G

M

L

V

-

D

G

K

S

A

D

L

L

V

Y

N

R

A

A

G

G

N

Q

W

-

D

-

E

S

I

V

G

E

R

R

L

T

T

A

R

Q

E

Q

A

A

V

A

K

A

L

F

V

V

K

K

R14 (≠ K21) binding substrate
E37 (= E41) mutation to N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.
T66 (= T69) binding substrate
K126 (= K129) active site, Schiff-base intermediate with substrate; binding covalent
V154 (≠ T157) 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_104487768.1 NCBI__GCF_002936955.1:WP_104487768.1
MSTLVEQIADLKILPVIVIDKAEDIVPLGKVLAENGLPAAEITFRSDAAVEAIRLLRQAQ
PDMLIGAGTVLTREQVVAAKEAGASFIVSPGFNPNTVKACQDLNIPIIPGTNNPSTIEAA
LEMGLTTVKFFPAEASGGVKMIKALLGPFNQLKIMPTGGVNANNINDYLAIPGVIACGGS
WMVDKALVNAGNWDEIGRLTREAVKLVK

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