SitesBLAST

E45 (= E45) mutation to N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.
R49 (= R49) binding
T73 (= T73) binding
K133 (= K133) 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 (= T161) binding ; 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 (= G163) binding
N168 (≠ R168) mutation to S: Shows activity significantly greater than wild-type.
S184 (= S184) binding

6oviA Crystal structure of kdpg aldolase from legionella pneumophila with pyruvate captured at low ph as a covalent carbinolamine intermediate
46% identity, 93% coverage: 16:213/214 of query aligns to 13:210/210 of 6oviA

query
sites
6oviA

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E

binding 2,2-bis(oxidanyl)propanoic acid: E42 (= E45), R46 (= R49), T70 (= T73), P91 (= P94), K130 (= K133), F132 (= F135)

2c0aB Mechanism of the class i kdpg aldolase (see paper)
53% identity, 85% coverage: 26:207/214 of query aligns to 27:208/214 of 2c0aB

query
sites
2c0aB

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A

active site: N46 (≠ E45), R50 (= R49), K134 (= K133)
binding phosphate ion: E132 (≠ F131)

Sites not aligning to the query:

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

1wauA Structure of kdpg aldolase e45n mutant (see paper)
53% identity, 85% coverage: 26:207/214 of query aligns to 26:207/213 of 1wauA

query
sites
1wauA

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active site: N45 (≠ E45), R49 (= R49), K133 (= K133)
binding sulfate ion: G162 (= G162), G163 (= G163), S184 (= S184)

5xsfA Crystal structure of the 2-keto-3-deoxy-6-phosphogluconate aldolase of zymomonas mobilis zm4 with 3-phosphoglycerate
51% identity, 93% coverage: 16:214/214 of query aligns to 13:207/209 of 5xsfA

query
sites
5xsfA

P

P

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A

binding 3-hydroxypyruvic acid: V19 (≠ E22), E21 (≠ S24), D22 (≠ S25), D25 (≠ E28)

3vcrA Crystal structure of a putative kdpg (2-keto-3-deoxy-6- phosphogluconate) aldolase from oleispira antarctica (see paper)
50% identity, 91% coverage: 16:210/214 of query aligns to 13:213/216 of 3vcrA

query
sites
3vcrA

P

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E

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K

A

A

-

K

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A

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K

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L

active site: E42 (= E45), R46 (= R49), K136 (= K133)
binding pyruvic acid: R46 (= R49), T70 (= T73), V89 (= V92), S90 (= S93), P91 (= P94)

1mxsA Crystal structure of 2-keto-3-deoxy-6-phosphogluconate (kdpg) aldolase from pseudomonas putida. (see paper)
44% identity, 91% coverage: 17:210/214 of query aligns to 19:212/216 of 1mxsA

query
sites
1mxsA

V

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x
T

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P

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K

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Y

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A

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P

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N

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C

C

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V

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K

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D

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K

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L

active site: E47 (= E45), R51 (= R49), K135 (= K133)
binding sulfate ion: E47 (= E45), R51 (= R49), T75 (= T73), V94 (= V92), T95 (≠ S93), P96 (= P94), K135 (= K133)

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)
44% identity, 91% coverage: 17:210/214 of query aligns to 29:222/226 of P00885

query
sites
P00885

V

I

I

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P

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L

I

A

G

A

G

G

L

I

P

R

V

T

L

L

E

E

I

V

T

T

L

L

R

R

T

S

P

Q

V

H

A

G

L

L

D

K

A

A

I

I

K

Q

A

V

V

L

A

R

A

E

A

Q

F

R

P

P

Q

E

A

L

C

C

V

V

G

G

A

A

G

G

T

T

V

V

L

L

T

D

A

R

A

S

D

M

L

F

K

A

A

A

V

V

S

E

D

A

A

A

G

G

A

A

Q

Q

F

F

A

V

V

V

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P

P

G

G

L

I

T

T

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E

A

D

L

I

A

L

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E

A

A

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Q

V

G

D

A

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G

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V

I

A

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L

L

P

P

G

G

V

I

A

S

T

T

A

P

S

S

E

E

A

I

M

M

A

M

A

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M

Y

E

A

A

L

G

G

F

Y

K

R

F

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L

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K
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K

F

L

F

F

P

P

A

A

E

E

A

I

S

S

G

G

V

V

P

A

M

A

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K

K

S

A

L

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Y

G

G

G

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P

F

F

A

G

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D

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R

R

F

F

C

C

P

P

T

T

G

G

I

V

D

N

L

P

A

A

R

N

A

V

P

R

T

N

Y

Y

L

M

A

A

L

L

P

P

N

N

V

V

V

M

C

C

V

V

G

G

G

T

S

G

W

W

V

M

V

L

P

D

K

S

D

S

A

W

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A

K

K

N

G

G

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D

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W

A

A

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R

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A

E

E

A

A

A

I

A

A

L

L

K145 (= K133) active site, Schiff-base intermediate with substrate

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

1wa3D Mechanism of the class i kdpg aldolase (see paper)
36% identity, 70% coverage: 17:166/214 of query aligns to 11:160/203 of 1wa3D

query
sites
1wa3D

V

I

I

V

P

A

V

V

L

L

E

R

F

A

S

N

S

S

V

V

D

E

E

E

A

A

L

K

H

E

V

K

S

A

E

L

A

A

L

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F

G

E

G

G

L

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H

V

L

L

I

E
|
E

I

I

T

T

L

F

R
x
T

T

V

P

P

V

D

A

A

L

D

D

T

A

V

I

I

K

K

A

E

V

L

A

S

A

F

A

L

F

K

P

E

Q

K

-

G

A

A

C

I

V

I

G

G

A

A

G

G

T
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T

V

V

L

T

T

S

A

V

A

E

D

Q

L

C

K

R

A

K

V

A

S

V

D

E

A

S

G

G

A

A

Q

E

F

F

A

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V

V

S
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S

P
|
P

G

H

L

L

T

D

P

E

A

E

L

I

A

S

V

Q

A

F

A

C

Q

K

G

E

A

K

G

G

V

V

A

F

L

Y

L

M

P

P

G

G

V

V

A

M

T

T

A

P

S

T

E

E

A

L

M

V

A

K

A

A

M

M

E

K

A

L

G

G

F

H

K

T

F

I

L

L

K
|
K

F

L

F
|
F

P

P

A

G

E

E

A

V

S

V

G

G

G

P

V

-

P

Q

M

F

L

V

K

K

S

A

L

M

Y

K

G

G

P

P

F

F

A

P

Q

N

L

V

R

K

F

F

C

V

P

P

T

T

G

G

G
|
G

I

V

D

N

L

L

active site: E39 (= E45), T43 (≠ R49), K128 (= K133)
binding pyruvic acid: T68 (= T73), S88 (= S93), P89 (= P94), K128 (= K133), F130 (= F135)
binding sulfate ion: G157 (= G163)

Sites not aligning to the query:

binding sulfate ion: 177, 178

2v82A Kdpgal complexed to kdpgal (see paper)
38% identity, 60% coverage: 14:141/214 of query aligns to 5:133/205 of 2v82A

query
sites
2v82A

N

K

V

L

P

P

V

L

I

I

P

A

V

I

L

L

E
x
R

F

G

S

I

S

T

V

P

D

D

E

E

A

A

L

L

H

A

V

H

S

V

E

G

A

A

L

V

I

I

G

D

G

A

G

G

L

F

P

D

V

A

L

V

E
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E

I

I

T

P

L

L

R
x
N

T

S

P

P

V

Q

A

W

L

E

D

Q

A

S

I

I

K

P

A

A

V

I

A

V

A

D

A

A

F

Y

-

G

P

D

Q

K

A

A

C

L

V

I

G

G

A

A

G

G

T
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T

V

V

L

L

T

K

A

P

A

E

D

Q

L

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K

D

A

A

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L

S

A

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R

A

M

G

G

A

C

Q

Q

F

L

A

I

V
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V

S
x
T

P

P

G

N

L

I

T

H

P

S

A

E

L

V

A

I

V

R

A

R

A

A

Q

V

G

G

A

Y

G

G

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M

A

T

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V

L

C

P

P

G

G

V

C

A

A

T

T

A

A

S

T

E

E

A

A

M

F

A

T

A

A

M

L

E

E

A

A

G

G

F

A

K

Q

F

A

L

L

K
|
K

F

I

F
|
F

P

P

A

S

E

S

A

A

S

F

G

G

active site: E36 (= E45), N40 (≠ R49), K125 (= K133)
binding 2-keto-deoxy-galactose: R13 (≠ E22), T65 (= T73), V84 (= V92), T85 (≠ S93), K125 (= K133), F127 (= F135)

Sites not aligning to the query:

binding 2-keto-deoxy-galactose: 153, 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)
38% identity, 60% coverage: 14:141/214 of query aligns to 6:134/205 of Q6BF16

query
sites
Q6BF16

N

K

V

L

P

P

V

L

I

I

P

A

V

I

L

L

E
x
R

F

G

S

I

S

T

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P

D

D

E

E

A

A

L

L

H

A

V

H

S

V

E

G

A

A

L

V

I

I

G

D

G

A

G

G

L

F

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D

V

A

L

V

E
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E

I

I

T

P

L

L

R

N

T

S

P

P

V

Q

A

W

L

E

D

Q

A

S

I

I

K

P

A

A

V

I

A

V

A

D

A

A

F

Y

-

G

P

D

Q

K

A

A

C

L

V

I

G

G

A

A

G

G

T
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T

V

V

L

L

T

K

A

P

A

E

D

Q

L

V

K

D

A

A

V

L

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A

D

R

A

M

G

G

A

C

Q

Q

F

L

A

I

V

V

S

T

P

P

G

N

L

I

T

H

P

S

A

E

L

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A

I

V

R

A

R

A

A

Q

V

G

G

A

Y

G

G

V

M

A

T

L

V

L

C

P

P

G

G

V

C

A

A

T

T

A

A

S

T

E

E

A

A

M

F

A

T

A

A

M

L

E

E

A

A

G

G

F

A

K

Q

F

A

L

L

K
|
K

F

I

F

F

P

P

A

S

E

S

A

A

S

F

G

G

R14 (≠ E22) binding
E37 (= E45) mutation to N: 50-fold decrease in catalytic efficiency and 6-fold decrease of binding affinity.
T66 (= T73) binding
K126 (= K133) active site, Schiff-base intermediate with substrate; binding covalent

Sites not aligning to the query:

154 V→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

>RR42_RS28865 FitnessBrowser__Cup4G11:RR42_RS28865
MQSQSPSLIERLVNVPVIPVLEFSSVDEALHVSEALIGGGLPVLEITLRTPVALDAIKAV
AAAFPQACVGAGTVLTAADLKAVSDAGAQFAVSPGLTPALAVAAQGAGVALLPGVATASE
AMAAMEAGFKFLKFFPAEASGGVPMLKSLYGPFAQLRFCPTGGIDLARAPTYLALPNVVC
VGGSWVVPKDAVAKGDWARVRTLAQEAAALRKSA

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