SitesBLAST

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)
33% identity, 68% coverage: 73:222/222 of query aligns to 61:202/205 of Q6BF16

query
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Q6BF16

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T66 (≠ S78) binding substrate
K126 (= K138) active site, Schiff-base intermediate with substrate; binding covalent
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.

Sites not aligning to the query:

14 binding substrate
37 E→N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.

1euaA Schiff base intermediate in kdpg aldolase from escherichia coli (see paper)
28% identity, 85% coverage: 27:214/222 of query aligns to 26:208/213 of 1euaA

query
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1euaA

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active site: E45 (= E46), R49 (= R50), K133 (= K138)
binding pyruvic acid: E45 (= E46), T73 (≠ S78), I92 (≠ V97), K133 (= K138)

P0A955 KHG/KDPG aldolase; EC 4.1.3.16; EC 4.1.2.14 from Escherichia coli (strain K12) (see 3 papers)
28% identity, 85% coverage: 27:214/222 of query aligns to 26:208/213 of P0A955

query
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P0A955

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E45 (= E46) mutation to N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.
R49 (= R50) binding substrate
T73 (≠ S78) binding substrate
K133 (= K138) 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 (= T165) 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 (= G167) binding substrate
N168 (= N174) mutation to S: Shows activity significantly greater than wild-type.
S184 (= S190) binding substrate

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)
32% identity, 81% coverage: 40:219/222 of query aligns to 51:225/226 of P00885

query
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P00885

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K145 (= K138) active site, Schiff-base intermediate with substrate

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

1wauA Structure of kdpg aldolase e45n mutant (see paper)
28% identity, 85% coverage: 27:214/222 of query aligns to 26:208/213 of 1wauA

query
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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)
28% identity, 85% coverage: 27:214/222 of query aligns to 27:209/214 of 2c0aB

query
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active site: N46 (≠ E46), R50 (= R50), K134 (= K138)
binding phosphate ion: E132 (≠ I136)

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)
31% identity, 81% coverage: 40:219/222 of query aligns to 41:215/216 of 1mxsA

query
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1mxsA

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F

F

I

V

V
|
V

T
|
T

P
|
P

V

G

L

I

R

T

E

E

D

D

I

I

A

L

I

E

A

A

C

G

N

V

R

D

R

S

K

E

V

I

L

P

W

L

S

L

P

P

G

G

C

I

G

S

T

T

L

P

T

S

E

E

I

I

T

M

R

M

A

G

E

Y

E

A

L

L

G

G

C

Y

E

R

I

R

V

F

K
|
K

L

L

F

F

P

P

G

A

D

E

I

I

Y

S

-

G

G

G

P

V

Q

A

F

A

V

I

K

K

G

A

I

F

K

G

G

G

P

P

Q

F

Q

G

W

D

T

I

S

R

I

F

M

C

P

P

T

T

G

G

V

V

S

N

P

P

T

A

E

-

N

N

L

V

K

R

A

N

W

Y

F

M

D

A

-

L

A

P

G

N

V

V

T

M

C

C

V

V

G

G

M

T

G

-

S

T

K

W

L

M

I

L

S

D

K

S

E

S

I

W

I

I

A

K

N

N

K

G

D

D

Y

W

A

A

K

R

L

I

E

E

K

A

D

C

V

S

K

A

A

E

A

A

L

I

A

A

I

L

V

L

K

D

S

A

active site: E47 (= E46), R51 (= R50), K135 (= K138)
binding sulfate ion: E47 (= E46), R51 (= R50), T75 (≠ S78), V94 (= V97), T95 (= T98), P96 (= P99), K135 (= K138)

5xsfA Crystal structure of the 2-keto-3-deoxy-6-phosphogluconate aldolase of zymomonas mobilis zm4 with 3-phosphoglycerate
27% identity, 81% coverage: 8:187/222 of query aligns to 4:178/209 of 5xsfA

query
sites
5xsfA

E

D

V

I

A

D

Q

S

A

V

M

M

K

R

D

L

T

A

G

P

M

V

I

M

P

P

L

V

F

L

F
x
V

H

I

N
x
E

D
|
D

I

I

E

A

L
x
D

S

A

K

K

K

P

V

I

L

A

K

E

A

A

C

L

Y

V

D

A

G

G

A

L

R

N

L

V

M

L

E

E

F

V

T

T

A

L

R

R

G

T

D

P

F

C

A

A

H

L

E

E

V

A

F

I

G

-

E

-

L

-

T

-

K

-

Y

K

A

I

I

M

K

K

E

E

L

V

P

P

G

G

M

A

I

V

M

V

G

G

V

A

G

G

S

T

V

V

T

L

D

N

A

A

G

K

Q

M

A

L

S

D

L

Q

Y

A

M

Q

T

E

L

A

G

G

A

C

N

E

F

F

I

F

V

V

T

S

P

P

V

G

L

L

R

T

E

A

D

D

I

L

A

G

I

K

A

H

C

A

N

V

R

A

R

Q

K

K

V

A

L

A

W

L

S

L

P

P

G

G

C

V

G

A

T

N

L

A

T

A

E

D

I

V

T

M

R

L

A

G

E

L

E

D

L

L

G

G

C

L

E

D

I

R

V

F

K

K

L

F

F

F

P

P

G

A

-

E

D

N

I

I

Y

G

G

G

P

L

Q

P

F

A

V

L

K

K

G

S

I

M

K

A

G

S

P

V

Q

F

Q

R

W

Q

T

V

S

R

I

F

M

C

P

P

T

T

G

G

V

I

S

T

P

P

T

T

E

S

E

A

N

P

L

-

K

K

A

Y

W

L

F

E

D

N

A

P

G

S

V

I

T

L

C

C

V

V

G

G

binding 3-hydroxypyruvic acid: V19 (≠ F23), E21 (≠ N25), D22 (= D26), D25 (≠ L29)

3vcrA Crystal structure of a putative kdpg (2-keto-3-deoxy-6- phosphogluconate) aldolase from oleispira antarctica (see paper)
27% identity, 86% coverage: 18:208/222 of query aligns to 14:205/216 of 3vcrA

query
sites
3vcrA

M

L

I

I

P

P

L

V

F

I

F

V

H

I

N

D

D

D

I

L

E

V

L

H

S

A

K

I

K

P

V

M

L

A

K

K

A

A

C

L

Y

V

D

A

G

G

A

V

R

H

L

L

M

L

E
|
E

F

V

T

T

A

L

R
|
R

G

T

D

E

F

A

A

G

H

L

E

A

V

A

F

I

G

S

E

A

L

I

T

K

K

K

Y

-

A

-

I

-

K

-

E

A

L

V

P

P

G

E

M

A

I

I

M

V

G

G

V

A

G

G

S
x
T

V

V

T

C

D

T

A

A

G

D

Q

D

A

F

S

Q

L

K

Y

A

M

I

T

D

L

A

G

G

A

A

N

Q

F

F

I

I

V
|
V

T
x
S

P
|
P

V

G

L

L

R

T

E

P

D

E

I

L

A

I

I

E

A

K

C

A

N

K

R

Q

R

V

K

K

V

L

-

D

-

G

-

Q

-

W

-

Q

-

G

L

V

W

F

S

L

P

P

G

G

C

V

G

A

T

T

L

A

T

S

E

E

I

V

T

M

R

I

A

A

E

A

E

Q

L

A

G

G

C

I

E

T

I

Q

V

L

K
|
K

L

C

F

F

P

P

G

A

D

S

-

A

I

I

Y

G

G

G

P

A

Q

K

F

L

V

L

K

K

G

A

I

W

K

S

G

G

P

P

Q

F

Q

P

W

D

T

I

S

Q

I

F

M

C

P

P

T

T

G

G

V

I

S

S

P

-

T

-

E

K

E

D

N

N

L

Y

K

K

A

E

W

Y

F

L

D

G

-

L

A

P

G

N

V

V

T

I

C

C

V

A

G

G

M

-

G

G

S

S

K

W

L

L

I

T

S

E

K

S

E

K

I

L

A

I

N

E

K

G

D

D

Y

W

A

N

K

E

L

V

E

T

K

R

active site: E42 (= E46), R46 (= R50), K136 (= K138)
binding pyruvic acid: R46 (= R50), T70 (≠ S78), V89 (= V97), S90 (≠ T98), P91 (= P99)

6oviA Crystal structure of kdpg aldolase from legionella pneumophila with pyruvate captured at low ph as a covalent carbinolamine intermediate
25% identity, 84% coverage: 18:204/222 of query aligns to 14:195/210 of 6oviA

query
sites
6oviA

M

V

I

I

P

P

L

V

F

I

F

V

H

I

N

K

D

E

I

L

E

E

L

D

S

A

K

L

K

P

V

L

L

A

K

E

A

A

C

L

Y

F

D

A

G

G

A

I

R

H

L

V

M

L

E
|
E

F

V

T

T

A

L

R
|
R

G

T

D

P

F

V

A

A

H

I

E

K

V

A

F

L

G

-

E

-

L

-

T

-

K

E

Y

L

A

L

I

I

K

N

E

T

L

F

P

P

G

D

M

E

I

L

M

I

G

G

V

A

G

G

S
x
T

V

V

T

I

D

T

A

P

G

G

Q

Q

A

F

S

H

L

D

Y

V

M

V

T

A

L

A

G

G

A

A

N

R

F

F

I

A

V

I

T

S

P
|
P

V

G

L

Q

R

T

E

R

D

E

I

L

A

L

I

I

A

A

C

G

N

Q

R

K

R

S

K

E

V

I

L

P

W

L

S

I

P

P

G

G

C

V

G

A

T

S

L

V

T

S

E

E

I

L

T

M

R

E

A

G

E

L

E

G

L

M

G

G

C

Y

E

N

I

H

V

F

K
|
K

L

F

F
|
F

P

P

G

A

D

A

I

A

Y

A

G

G

P

G

-

I

Q

P

F

M

V

L

K

K

G

A

I

I

K

S

G

G

P

V

Q

F

Q

P

W

Q

T

V

S

K

I

F

M

C

P

P

T

T

G

G

V

I

S

N

P

-

T

-

E

S

E

K

N

N

L

Y

K

E

A

E

W

Y

F

L

D

C

-

L

A

P

G

N

V

V

T

A

C

C

V

V

G

G

M

-

G

G

S

S

K

W

L

I

I

V

S

P

K

E

E

E

I

A

I

I

A

K

N

N

K

H

D

N

Y

W

A

S

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

Query Sequence

>WP_019388255.1 NCBI__GCF_000283015.1:WP_019388255.1
MAQFSRLEVAQAMKDTGMIPLFFHNDIELSKKVLKACYDGGARLMEFTARGDFAHEVFGE
LTKYAIKELPGMIMGVGSVTDAGQASLYMTLGANFIVTPVLREDIAIACNRRKVLWSPGC
GTLTEITRAEELGCEIVKLFPGDIYGPQFVKGIKGPQQWTSIMPTGGVSPTEENLKAWFD
AGVTCVGMGSKLISKEIIANKDYAKLEKDVKAALAIVKSVRK

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