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)
34% identity, 95% coverage: 3:175/182 of query aligns to 12:184/205 of Q6BF16

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Q6BF16

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R14 (= R5) binding substrate
E37 (= E28) mutation to N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.
T66 (= T58) binding substrate
K126 (= K118) active site, Schiff-base intermediate with substrate; binding covalent
V154 (≠ T145) 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.

1euaA Schiff base intermediate in kdpg aldolase from escherichia coli (see paper)
38% identity, 74% coverage: 23:157/182 of query aligns to 40:173/213 of 1euaA

query
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1euaA

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active site: E45 (= E28), R49 (≠ G32), K133 (= K118)
binding pyruvic acid: E45 (= E28), T73 (= T58), I92 (≠ V77), K133 (= K118)

P0A955 KHG/KDPG aldolase; EC 4.1.3.16; EC 4.1.2.14 from Escherichia coli (strain K12) (see 3 papers)
38% identity, 74% coverage: 23:157/182 of query aligns to 40:173/213 of P0A955

query
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E45 (= E28) mutation to N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.
R49 (≠ G32) binding substrate
T73 (= T58) binding substrate
K133 (= K118) 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 (= T145) 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 (= G147) binding substrate
N168 (≠ V152) mutation to S: Shows activity significantly greater than wild-type.

Sites not aligning to the query:

184 binding substrate

3vcrA Crystal structure of a putative kdpg (2-keto-3-deoxy-6- phosphogluconate) aldolase from oleispira antarctica (see paper)
41% identity, 68% coverage: 54:176/182 of query aligns to 66:195/216 of 3vcrA

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3vcrA

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active site: K136 (= K118)
binding pyruvic acid: T70 (= T58), V89 (= V77), S90 (= S78), P91 (= P79)

Sites not aligning to the query:

active site: 42, 46
binding pyruvic acid: 46

2c0aB Mechanism of the class i kdpg aldolase (see paper)
43% identity, 57% coverage: 54:157/182 of query aligns to 70:174/214 of 2c0aB

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2c0aB

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active site: K134 (= K118)
binding phosphate ion: E132 (≠ W116)

Sites not aligning to the query:

active site: 46, 50
binding phosphate ion: 1, 5, 8, 9, 10

1wauA Structure of kdpg aldolase e45n mutant (see paper)
43% identity, 57% coverage: 54:157/182 of query aligns to 69:173/213 of 1wauA

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active site: K133 (= K118)
binding sulfate ion: G162 (= G146), G163 (= G147)

Sites not aligning to the query:

active site: 45, 49
binding sulfate ion: 184

6oviA Crystal structure of kdpg aldolase from legionella pneumophila with pyruvate captured at low ph as a covalent carbinolamine intermediate
34% identity, 86% coverage: 1:157/182 of query aligns to 17:170/210 of 6oviA

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binding 2,2-bis(oxidanyl)propanoic acid: E42 (= E28), R46 (≠ G32), T70 (= T58), P91 (= P79), K130 (= K118), F132 (= F120)

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)
34% identity, 81% coverage: 11:157/182 of query aligns to 40:185/226 of P00885

query
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P00885

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K145 (= K118) active site, Schiff-base intermediate with substrate

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

1mxsA Crystal structure of 2-keto-3-deoxy-6-phosphogluconate (kdpg) aldolase from pseudomonas putida. (see paper)
34% identity, 81% coverage: 11:157/182 of query aligns to 30:175/216 of 1mxsA

query
sites
1mxsA

D

D

T

I

V

L

A

P

T

L

A

A

E

D

A

A

A

L

W

A

E

A

L

G

G

G

V

I

V

R

L

T

V

L

E
|
E

I

V

P

T

I

L

G
x
R

Q

S

T

Q

D

H

Q

G

I

L

P

K

A

A

L

I

R

Q

A

-

T

-

V

V

S

L

A

R

A

E

Q

Q

A

R

R

P

G

E

L

L

T

C

V

V

G

G

A

A

G

G

T
|
T

V

V

T

L

T

D

P

R

A

S

H

M

V

F

S

A

A

A

A

V

V

E

E

A

A

A

G

G

A

A

A

Q

Y

F

A

V

V
|
V

S
x
T

P
|
P

G

G

L

I

S

T

E

E

E

D

V

I

A

L

S

E

E

A

C

G

R

V

R

D

V

S

G

E

I

I

P

P

Y

L

L

L

P

P

G

G

V

I

A

S

T

T

P

P

T

S

E

E

V

I

Q

M

R

M

A

G

L

Y

D

A

L

L

G

G

L

Y

E

R

W

R

V

F

K
|
K

V

L

F

F

P

P

A

A

S

E

-

I

T

S

L

G

G

G

P

V

R

A

W

A

F

I

K

K

A

A

V

F

R

G

G

G

P

P

F

F

P

G

D

D

V

I

K

R

M

F

V

C

A

P

T

T

G

G

I

V

A

N

P

P

A

A

V

N

A

V

D

R

D

N

Y

Y

L

M

active site: E47 (= E28), R51 (≠ G32), K135 (= K118)
binding sulfate ion: E47 (= E28), R51 (≠ G32), T75 (= T58), V94 (= V77), T95 (≠ S78), P96 (= P79), K135 (= K118)

5xsfA Crystal structure of the 2-keto-3-deoxy-6-phosphogluconate aldolase of zymomonas mobilis zm4 with 3-phosphoglycerate
34% identity, 87% coverage: 1:158/182 of query aligns to 17:170/209 of 5xsfA

query
sites
5xsfA

M

V

L

L

I
x
V

L

I

R
x
E

N
x
D

L

I

S

A

A
x
D

T

A

D

K

T

P

V

I

A

A

T

E

A

A

E

L

A

V

A

A

W

G

E

G

L

L

G

N

V

V

V

L

L

E

V

V

E

-

I

-

P

-

I

-

G

-

Q

-

T

T

D

L

Q

R

I

T

P

P

-

C

A

A

L

L

R

E

A

A

T

I

V

K

S

I

A

M

A

K

Q

E

A

V

R

P

G

G

L

A

T

V

V

V

G

G

A

A

G

G

T

T

V

V

T

L

T

N

P

A

A

K

H

M

V

L

S

D

A

Q

A

A

V

Q

E

E

A

A

G

G

A

C

A

E

Y

F

A

F

V

V

S

S

P

P

G

G

L

L

S

T

E

A

E

D

V

L

A

G

S

K

E

H

C

A

R

V

R

A

V

Q

G

K

I

A

P

A

Y

L

L

L

P

P

G

G

V

V

A

A

T

N

P

A

T

A

E

D

V

V

Q

M

R

L

A

G

L

L

D

D

L

L

G

G

L

L

E

D

W

R

V

F

K

K

V

F

F

F

P

P

A

A

S

E

T

N

L

I

G

G

P

G

R

L

-

P

W

A

F

L

K

K

A

S

V

M

R

A

G

S

P

V

F

F

P

R

D

Q

V

V

K

R

M

F

V

C

A

P

T

T

G

G

I

I

A

T

P

P

A

T

V

S

A

A

D

P

D

K

Y

Y

L

L

D

E

binding 3-hydroxypyruvic acid: V19 (≠ I3), E21 (≠ R5), D22 (≠ N6), D25 (≠ A9)

Query Sequence

>WP_051463092.1 NCBI__GCF_000527155.1:WP_051463092.1
MLILRNLSATDTVATAEAAWELGVVLVEIPIGQTDQIPALRATVSAAQARGLTVGAGTVT
TPAHVSAAVEAGAAYAVSPGLSEEVASECRRVGIPYLPGVATPTEVQRALDLGLEWVKVF
PASTLGPRWFKAVRGPFPDVKMVATGGIAPAVADDYLDAGARIVGMGSALNEPEQLRPLL
RR

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