SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_017221003.1 NCBI__GCF_000276805.1:WP_017221003.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 13 hits to proteins with known functional sites (download)

P0A6L0 Deoxyribose-phosphate aldolase; DERA; 2-deoxy-D-ribose 5-phosphate aldolase; Phosphodeoxyriboaldolase; Deoxyriboaldolase; EC 4.1.2.4 from Escherichia coli (strain K12) (see 2 papers)
67% identity, 91% coverage: 1:233/257 of query aligns to 1:236/259 of P0A6L0

query
sites
P0A6L0

M

M

S

T

N

D

F

L

K

K

V

A

A

S

Q

L

R

R

A

A

L

L

S

K

M

L

M

M

D

D

L

L

T

T

L

L

N

N

D

D

T

T

D

D

A

E

K

K

V

V

I

I

E

A

L

L

C

C

H

H

K

Q

A

A

K

K

S

T

A

P

A

V

G

G

N

N

T

T

A

A

V

I

C
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C

I

I

Y

Y

P

P

R

R

F

F

V

I

P

P

I

I

A

A

R

R

K

K

T

T

L

L

N

K

A

E

I

Q

G

G

A

T

E

P

T

E

V

I

K

R

I

I

A

A

T

T

V

V

T

T

N

N

F

F

P

P

H

H

G

G

N

N

D

D

V

I

A

D

I

I

A

A

V

L

A

A

E

E

T

T

K

R

A

A

V

I

A

A

Y

Y

G

G

A

A

D

D

E

E

V

V

D
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D

V

V

F

F

P

P

Y

Y

R

R

A

A

L

L

M

M

A

A

G

G

N

N

A

E

E

Q

V

V

G

G

F

F

E

D

L

L

V

V

-

K

K

A

A

C

C

K

K

E

A

A

A

C

C

A

P

A

A

A

N

N

V

V

Q

L

L

L

K
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K

V

V

I

I

V

I

E

E

T

T

G

G

E

E

L

L

K

K

T

D

E

E

A

A

L

L

I

I

R

R

Q

K

A

A

S

S

E

E

I

I

S

S

I

I

D

K

A

A

G

G

A

A

D

D

F

F

I

I

K
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K

T

T

S

S

T

T

G

G

K

K

V

V

P

A

V

V

N

N

A

A

T

T

L

P

E

E

F

S

A

A

K

R

I

I

M

M

L

M

T

E

V

V

I

I

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E

D

K

M

N

G

T

V

D

E

-

K

-

T

V

V

G

G

F

F

K
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K

P

P

A

A

G

G

V

V

K

R

N

T

A

A

E

E

Q

D

A

A

G

Q

E

K

Y

Y

L

L

A

A

L

I

A

A

E

D

S

E

I

L

L

F

G

G

K

A

D

D

W

W

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A

S

D

P

A

A

R

K

H

F

Y

R

R

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F

G

G

C47 (= C47) mutation C->A,S: 3-fold decrease in catalytic efficiency.
D102 (= D102) mutation to E: 44-fold decrease in catalytic efficiency.; mutation to L: 2000-fold decrease in catalytic efficiency.; mutation to N: 1500-fold decrease in catalytic efficiency.
K137 (= K136) mutation to L: 20-fold decrease in catalytic efficiency.
K167 (= K166) active site, Schiff-base intermediate with acetaldehyde; modified: N6-acetyllysine; mutation to L: 1000-fold decrease in catalytic efficiency.; mutation to R: 20-fold decrease in catalytic efficiency.
K201 (= K198) mutation to L: 1500-fold decrease in catalytic efficiency.; mutation to R: 1000-fold decrease in catalytic efficiency.

Sites not aligning to the query:

259 Y→F: 200-fold decrease in catalytic efficiency.

1jcjA Observation of covalent intermediates in an enzyme mechanism at atomic resolution (see paper)
67% identity, 91% coverage: 1:233/257 of query aligns to 2:237/252 of 1jcjA

query
sites
1jcjA

M

M

S

T

N

D

F

L

K

K

V

A

A

S

Q

L

R

R

A

A

L

L

S

K

M

L

M

M

D

D

L

L

T

T

L

L

N

N

D

D

T

T

D

D

A

E

K

K

V

V

I

I

E

A

L

L

C

C

H

H

K

Q

A

A

K

K

S

T

A

P

A

V

G

G

N

N

T

T

A

A

V

I

C

C

I

I

Y

Y

P

P

R

R

F

F

V

I

P

P

I

I

A

A

R

R

K

K

T

T

L

L

N

K

A

E

I

Q

G

G

A

T

E

P

T

E

V

I

K

R

I

I

A

A

T

T

V

V

T

T

N

N

F

F

P

P

H

H

G

G

N

N

D

D

V

I

A

D

I

I

A

A

V

L

A

A

E

E

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T

K

R

A

A

V

I

A

A

Y

Y

G

G

A

A

D

D

E

E

V

V

D
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D

V

V

F

F

P

P

Y

Y

R

R

A

A

L

L

M

M

A

A

G

G

N

N

A

E

E

Q

V

V

G

G

F

F

E

D

L

L

V

V

-

K

K

A

A

C

C

K

K

E

A

A

A

C

C

A

P

A

A

A

N

N

V

V

Q

L

L

L

K

K

V

V

I

I

V

I

E

E

T

T

G

G

E

E

L

L

K

K

T

D

E

E

A

A

L

L

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I

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K

A

A

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E

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S

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I

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K

A

A

G

G

A

A

D

D

F

F

I

I

K
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K

T

T

S

S

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T

G

G

K

K

V

V

P

A

V

V

N

N

A

A

T

T

L

P

E

E

F

S

A

A

K

R

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I

M

M

L

M

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E

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V

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D

K

M

N

G

T

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D

E

-

K

-

T

V

V

G

G

F

F

K
x
L

P

P

A

A

G
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G

G

G

V

V

K

R

N

T

A

A

E

E

Q

D

A

A

G

Q

E

K

Y

Y

L

L

A

A

L

I

A

A

E

D

S

E

I

L

L

F

G

G

K

A

D

D

W

W

V

A

S

D

P

A

A

R

K

H

F

Y

R

R

F

F

G
|
G

active site: D103 (= D102), K168 (= K166), L202 (≠ K198)
binding 1-hydroxy-pentane-3,4-diol-5-phosphate: K168 (= K166), T171 (= T169), G205 (= G201), G237 (= G233)

Sites not aligning to the query:

binding 1-hydroxy-pentane-3,4-diol-5-phosphate: 238, 239

6z9iB Escherichia coli d-2-deoxyribose-5-phosphate aldolase - n21k mutant complex with reaction products (see paper)
67% identity, 90% coverage: 3:233/257 of query aligns to 1:234/248 of 6z9iB

query
sites
6z9iB

N

D

F

L

K

K

V

A

A

S

Q

L

R

R

A

A

L

L

S

K

M

L

M

M

D

D

L

L

T

T

L

L

N

K

D

D

T

T

D

D

A

E

K

K

V

V

I

I

E

A

L

L

C

C

H

H

K

Q

A

A

K

K

S

T

A

P

A

V

G

G

N

N

T

T

A

A

V

I

C

C

I

I

Y

Y

P

P

R

R

F

F

V

I

P

P

I

I

A

A

R

R

K

K

T

T

L

L

N

K

A

E

I

Q

G

G

A

T

E

P

T

E

V

I

K

R

I

I

A

A

T

T

V

V

T

T

N

N

F

F

P

P

H

H

G

G

N

N

D

D

V

I

A

D

I

I

A

A

V

L

A

A

E

E

T

T

K

R

A

A

V

I

A

A

Y

Y

G

G

A

A

D

D

E

E

V

V

D

D

V

V

F

F

P

P

Y

Y

R

R

A

A

L

L

M

M

A

A

G

G

N

N

A

E

E

Q

V

V

G

G

F

F

E

D

L

L

V

V

-

K

K

A

A

C

C

K

K

E

A

A

A

C

C

A

P

A

A

A

N

N

V

V

Q

L

L

L

K

K

V

V

I

I

V

I

E

E

T

T

G

G

E

E

L

L

K

K

T

D

E

E

A

A

L

L

I

I

R

R

Q

K

A

A

S

S

E

E

I

I

S

S

I

I

D

K

A

A

G

G

A

A

D

D

F

F

I

I

K

K

T

T

S

S

T
|
T

G

G

K

K

V

V

P

A

V

V

N

N

A

A

T

T

L

P

E

E

F

S

A

A

K

R

I

I

M

M

L

M

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V

V

I

I

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R

E

D

K

M

N

G

T

V

D

E

-

K

-

T

V

V

G

G

F

F

K

K

P

P

A

A

G
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G

V

V

K
x
R

N

T

A

A

E

E

Q

D

A

A

G

Q

E

K

Y

Y

L

L

A

A

L

I

A

A

E

D

S

E

I

L

L

F

G

G

K

A

D

D

W

W

V

A

S

D

P

A

A

R

K

H

F

Y

R

R

F

F

G
|
G

binding glyceraldehyde-3-phosphate: T168 (= T169), G202 (= G201), G203 (= G202), R205 (≠ K204), G234 (= G233)

Sites not aligning to the query:

binding glyceraldehyde-3-phosphate: 235, 236

5el1A Crystal structure of deoxyribose-phosphate aldolase from escherichia coli (k58e-y96w mutant) after acetaldehyde treatment (see paper)
67% identity, 90% coverage: 3:233/257 of query aligns to 1:234/248 of 5el1A

query
sites
5el1A

N

D

F

L

K

K

V

A

A

S

Q

L

R

R

A

A

L

L

S

K

M

L

M

M

D

D

L

L

T
|
T

T

T

L

L

N

N

D

D

T

T

D

D

A

E

K

K

V

V

I

I

E

A

L

L

C

C

H

H

K

Q

A

A

K

K

S

T

A

P

A

V

G

G

N

N

T

T

A

A

V

I

C
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C

I

I

Y

Y

P

P

R

R

F

F

V

I

P

P

I

I

A

A

R

R

K

E

T

T

L

L

N

K

A

E

I

Q

G

G

A

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E

P

T

E

V

I

K

R

I

I

A

A

T

T

V

V

T

T

N

N

F

F

P

P

H

H

G

G

N

N

D

D

V

I

A

D

I

I

A

A

V

L

A

A

E

E

T

T

K

R

A

A

V

I

A

A

Y

W

G

G

A

A

D

D

E

E

V

V

D
|
D

V

V

F

F

P

P

Y

Y

R

R

A

A

L

L

M

M

A

A

G

G

N

N

A

E

E

Q

V

V

G

G

F

F

E

D

L

L

V

V

-

K

K

A

A

C

C

K

K

E

A

A

A

C

C

A

P

A

A

A

N

N

V

V

Q

L

L

L

K

K

V

V

I

I

V

I

E

E

T

T

G

G

E

E

L

L

K

K

T

D

E

E

A

A

L

L

I

I

R

R

Q

K

A

A

S

S

E

E

I

I

S

S

I

I

D

K

A

A

G

G

A

A

D

D

F

F

I

I

K
|
K

T

T

S

S

T

T

G

G

K

K

V

V

P

A

V

V

N

N

A

A

T

T

L

P

E

E

F

S

A

A

K

R

I

I

M

M

L

M

T

E

V

V

I

I

S

R

E

D

K

M

N

G

T

V

D

E

-

K

-

T

V

V

G

G

F

F

K
|
K

P

P

A

A

G

G

V

V

K

R

N

T

A

A

E

E

Q

D

A

A

G

Q

E

K

Y

Y

L

L

A

A

L

I

A

A

E

D

S

E

I

L

L

F

G

G

K

A

D

D

W

W

V

A

S

D

P

A

A

R

K

H

F

Y

R

R

F

F

G

G

active site: D100 (= D102), K165 (= K166), K199 (= K198)
binding 1-butanol: T16 (= T18), C45 (= C47), K165 (= K166), K199 (= K198)

Sites not aligning to the query:

binding 1-butanol: 248

5ekyA Crystal structure of deoxyribose-phosphate aldolase from escherichia coli (k58e-y96w mutant) (see paper)
67% identity, 90% coverage: 3:233/257 of query aligns to 1:234/248 of 5ekyA

query
sites
5ekyA

N

D

F

L

K

K

V

A

A

S

Q

L

R

R

A

A

L

L

S

K

M

L

M

M

D

D

L

L

T

T

L

L

N

N

D

D

T

T

D

D

A

E

K

K

V

V

I

I

E

A

L

L

C

C

H

H

K

Q

A

A

K

K

S

T

A

P

A

V

G

G

N

N

T

T

A

A

V

I

C

C

I

I

Y

Y

P

P

R

R

F

F

V

I

P

P

I

I

A

A

R

R

K

E

T

T

L

L

N

K

A

E

I

Q

G

G

A

T

E

P

T

E

V

I

K

R

I

I

A

A

T

T

V

V

T

T

N

N

F

F

P

P

H

H

G

G

N

N

D

D

V

I

A

D

I

I

A

A

V

L

A

A

E

E

T

T

K

R

A

A

V

I

A

A

Y

W

G

G

A

A

D

D

E

E

V

V

D
|
D

V

V

F

F

P

P

Y

Y

R

R

A

A

L

L

M

M

A

A

G

G

N

N

A

E

E

Q

V

V

G

G

F

F

E

D

L

L

V

V

-

K

K

A

A

C

C

K

K

E

A

A

A

C

C

A

P

A

A

A

N

N

V

V

Q

L

L

L

K

K

V

V

I

I

V

I

E

E

T

T

G

G

E

E

L

L

K

K

T

D

E

E

A

A

L

L

I

I

R

R

Q

K

A

A

S

S

E

E

I

I

S

S

I

I

D

K

A

A

G

G

A

A

D

D

F

F

I

I

K
|
K

T

T

S

S

T
|
T

G
|
G

K

K

V

V

P

A

V

V

N

N

A

A

T

T

L

P

E

E

F

S

A

A

K

R

I

I

M

M

L

M

T

E

V

V

I

I

S

R

E

D

K

M

N

G

T

V

D

E

-

K

-

T

V

V

G

G

F

F

K
|
K

P

P

A
|
A

G

G

V

V

K

R

N

T

A

A

E

E

Q

D

A

A

G

Q

E

K

Y

Y

L

L

A

A

L

I

A

A

E

D

S

E

I

L

L

F

G

G

K

A

D

D

W

W

V

A

S

D

P

A

A

R

K

H

F

Y

R

R

F

F

G

G

active site: D100 (= D102), K165 (= K166), K199 (= K198)
binding 1,3-butanediol: K165 (= K166), T168 (= T169), G169 (= G170), A201 (= A200)

Sites not aligning to the query:

binding 1,3-butanediol: 248

7p76A Re-engineered 2-deoxy-d-ribose-5-phosphate aldolase catalysing asymmetric michael addition reactions, schiff base complex with cinnamaldehyde (see paper)
64% identity, 94% coverage: 4:245/257 of query aligns to 1:245/247 of 7p76A

query
sites
7p76A

F

L

K

K

V

A

A

S

Q

L

R

R

A

A

L

L

S

K

M

L

M

M

D

D

L

L

T

S

T

T

L

L

N

N

D

G

D

D

D

Y

T

T

D

D

A

E

K

K

V

V

I

I

E

A

L

L

C

C

H

H

K

Q

A

A

K

K

S

T

A

P

A

V

G

G

N

N

T

T

A

A

V

I

C
x
S

I
|
I

Y
|
Y

P

P

R

R

F

S

V

I

P

P

I

I

A

A

R

R

K

K

T

T

L

L

N

K

A

E

I

Q

G

G

A

T

E

P

T

E

V

I

K

R

I

I

A

A

T

T

V
|
V

T

T

N

N

F
|
F

P

P

H

H

G

G

N

N

D

D

V

I

A

E

I

I

A

A

V

L

A

A

E

E

T

T

K

R

A

A

V

I

A

A

Y

Y

G

G

A

A

D

D

E

E

V

V

D

D

V

V

F

F

P

P

Y

Y

R

R

A

A

L

L

M

M

A

A

G

G

N

N

A

E

E

Q

V

V

G

G

F

F

E

D

L

L

V

V

-

K

K

A

A

C

C

K

K

E

A

A

A

C

C

A

P

A

A

A

N

N

V

V

Q

L

L

L

K

K

V

V

I

I

V

I

E

E

T

S

G

G

E

E

L

L

K

K

T

D

E

E

A

A

L

L

I

I

R

R

Q

K

A

A

S

S

E

E

I

I

S

S

I

I

D

K

A

A

G

G

A

A

D

D

F

F

I

I

K
|
K

T

T

S

S

T

T

G

G

K

L

V

V

P

A

V

V

N

N

A

A

T

T

L

P

E

E

F

S

A

A

K

R

I

I

M

M

L

M

T

E

V

V

I

I

S

R

E

D

K

M

N

G

T

V

D

E

-

K

-

S

V

V

G

G

F

F

K

K

P

V

A

T

G

G

V

A

K

R

N

T

A

A

E

E

Q

D

A

A

G

Q

E

K

Y

Y

L

L

A

A

L

I

A

A

E

D

S

E

I

L

L

F

G

G

K

A

D

D

W

W

V

A

S

D

P

A

A

R

K

H

F

Y

R

R

F

F

G

G

A

A

S

S

S

G

L

L

A

A

N

S

L

L

A

K

E

A

L

L

binding (2E)-3-phenylprop-2-enal: S44 (≠ C47), I45 (= I48), Y46 (= Y49), V70 (= V73), F73 (= F76), K164 (= K166)

8forA Crystal structure of kemp eliminase ke70-core with bound transition state analogue
60% identity, 89% coverage: 4:233/257 of query aligns to 1:234/249 of 8forA

query
sites
8forA

F

L

K

K

V

A

A

S

Q

L

R

R

A

A

L

L

S

K

M

L

M

M

D

H

L

L

-

A

T

T

T

S

L

A

N

N

D

D

T

T

D

D

A

E

K

K

V

V

I

I

E

A

L

L

C

C

H

H

K

Q

A

A

K

K

S

T

A

P

A

V

G

G

N

T

T

T

A

D

A

A

V

I

C
x
F

I

I

Y

Y

P

P

R

R

F

F

V

I

P

P

I

I

A

A

R

R

K

K

T

T

L

L

N

K

A

E

I

Q

G

G

A

T

E

P

T

E

V

I

K

R

I

I

A

C

T

T

V

S

T

T

N

N

F

F

P

P

H

H

G

G

N

N

D

D

V

I

A

D

I

I

A

A

V

L

A

A

E

E

T

T

K

R

A

A

V

I

A

A

Y

Y

G

G

A

A

D

D

E

S

V

V

D
x
A

V

V

F

F

P

P

Y

Y

R

R

A

A

L

L

M

M

A

A

G

G

N

N

A

E

E

Q

V

V

G

G

F

F

E

D

L

L

V

V

-

K

K

A

A

C

C

K

K

E

A

A

A

C

C

A

P

A

A

A

N

N

V

V

Q

L

L

L

K

A

V

V

I

I

V

I

E

E

T

T

G

G

E

E

L

L

K

K

T

D

E

E

A

A

L

L

I

I

R

R

Q

K

A

A

S

S

E

E

I

I

S

S

I

I

D

K

A

A

G

G

A

A

D

D

F

N

I

I

K

V

T

T

S

S

T

T

G

G

K

K

V

V

P

A

V

V

N

G

A

A

T

T

L

P

E

E

F

S

A

A

K

R

I

I

M

M

L

M

T

E

V

V

I

I

S

R

E

D

K

M

N

G

T

V

D

E

-

K

-

T

V

V

G

G

F

F

K

I

P

P

A
x
V

G

G

V

V

K

R

N

T

A

A

E

E

Q

D

A

A

G

Q

E

K

Y

Y

L

L

A

A

L

I

A

A

E

D

S

E

I

L

L

F

G

G

K

A

D

D

W

W

V

A

S

D

P

A

A

R

K

H

F

Y

R

A

F

F

G
|
G

binding 6-nitrobenzotriazole: F45 (≠ C47), A100 (≠ D102), V201 (≠ A200), G234 (= G233)

3q2dA Optimization of the in silico designed kemp eliminase ke70 by computational design and directed evolution (see paper)
59% identity, 90% coverage: 2:233/257 of query aligns to 1:232/246 of 3q2dA

query
sites
3q2dA

S

T

N

D

F

L

K

K

V

A

A

S

Q

L

R

R

A

A

L

L

S

K

M

L

M

M

D
x
H

L

L

T

A

T

T

L

-

N

-

D

-

D

S

D

D

T

T

D

D

A

E

K

N

V

V

I

I

E

A

L

L

C

C

H

H

K

Q

A

A

K

K

S

T

A

P

A

V

G

G

N

N

T

T

A

D

A

A

V

I

C
x
F

I

I

Y

Y

P

P

R

R

F

F

V

I

P

P

I

I

A

A

R

R

K

K

T

T

L

L

N

K

A

E

I

Q

G

G

A

T

E

P

T

E

V

I

K

R

I

I

A
x
C

T

T

V

S

T

T

N

N

F

F

P

P

H

H

G

G

N

N

D

D

V

I

A

D

I

I

A

A

V

L

A

A

E

E

T

T

K

R

A

A

V

I

A

A

Y

Y

G

G

A

A

D

D

E
x
S

V

V

D
x
A

V

V

F

F

P

P

Y

Y

R

R

A

A

L

L

M

M

A

A

G

G

N

N

A

E

E

Q

V

V

G

G

F

F

E

D

L

L

V

V

-

K

K

A

A

C

C

K

K

E

A

A

A

C

C

A

P

A

A

A

N

N

V

V

Q

L

L

L

K
x
A

V

V

I

I

V

I

E

E

T

T

G

G

E

E

L

L

K

K

T

D

E

E

A

A

L

L

I

I

R

R

Q

K

A

A

S

S

E

E

I

I

S

S

I

I

D

K

A

A

G

G

A

A

D

D

F

N

I

I

K

V

T

T

S

S

T

T

G

G

K

K

V

V

P

A

V

V

N

G

A

A

T

T

L

P

E

E

F

S

A

A

K

R

I

I

M

M

L

M

T

E

V

V

I

I

S

R

E

D

K

M

N

G

T

V

D

E

-

K

-

T

V

V

G

G

F

F

K
x
I

P

P

A

V

G

G

V

V

K

R

N

T

A

A

E

E

Q

D

A

A

G

Q

E

K

Y

Y

L

L

A

A

L

I

A

A

E

D

S

E

I

L

L

F

G

G

K

A

D

D

W

W

V

A

S

D

P

A

A

R

K

H

F

Y

R

A

F

F

G

G

binding 5-nitro-1H-benzotriazole: H15 (≠ D16), F43 (≠ C47), C67 (≠ A71), S96 (≠ E100), A98 (≠ D102), A133 (≠ K136), I197 (≠ K198)

Q9Y315 Deoxyribose-phosphate aldolase; DERA; 2-deoxy-D-ribose 5-phosphate aldolase; Phosphodeoxyriboaldolase; Deoxyriboaldolase; EC 4.1.2.4 from Homo sapiens (Human) (see paper)
38% identity, 90% coverage: 10:241/257 of query aligns to 49:297/318 of Q9Y315

query
sites
Q9Y315

R

K

A

A

L

V

S

T

M

F

M

I

D

D

L

L

T

T

L

L

N

S

D

G

D

D

T

T

D

S

A

S

K

N

V

I

I

Q

E

R

L

L

C

C

H

Y

K

K

A

A

K

K

-

Y

-

P

-

I

-

R

-

E

-

D

-

L

-

K

-

A

-

L

-

N

-

M

-

H

S

D

A

K

A

G

G

I

N

T

T

T

A

A

V

V

C

C

I

V

Y

Y

P

P

R

A

F

R

V

V

P

C

I

D

A

A

R

V

K

K

T

A

L

L

N

K

A

A

I

A

G

G

A

C

E

N

T

I

V

P

K

V

I

A

A

S

T

V

V

A

T

A

N

G

F

F

P

P

H

A

G

G

N

Q

D

T

D

H

V

L

A

K

I

T

A

R

V

L

A

E

E

E

T

I

K

R

A

L

A

A

V

V

A

E

Y

D

G

G

A

A

D

T

E

E

V

I

D

D

V

V

F

I

P

N

Y

R

R

S

A

L

L

V

M

L

A

T

G

G

N

Q

A

W

E

E

V

A

G

L

F

Y

E

D

L

E

V

I

K

R

A

Q

C

F

K

R

A

K

A

A

C

C

P

-

A

G

N

E

V

A

Q

H

L

L

K

K

V

T

I

I

V

L

E

A

T

T

G

G

E

E

L

L

K

G

T

T

E

L

A

T

L

N

I

V

R

Y

Q

K

A

A

S

S

E

M

I

I

S

A

I

M

D

M

A

A

G

G

A

S

D

D

F

F

I

I

K
|
K

T

T

S

S

T

T

G

G

K

K

V

E

P

T

V

V

N

N

A

A

T

T

L

F

E

P

F

V

A

A

K

I

I

V

M

M

L

L

T

R

V

A

I

I

S

R

E

D

-

F

-

W

-

K

K

T

N

G

T

N

D

K

V

I

G

G

F

F

K
|
K

P

P

A

A

G

G

V

I

K

R

N

S

A

A

E

K

Q

D

A

S

G

L

E

A

Y

W

L

L

A

S

L

L

A

V

E

K

S

E

I

E

L

L

G

G

K

D

D

E

W

W

V

L

S

K

P

P

A

E

K

L

F

F

R

R

F

I

G

G

A

A

S

S

S

T

L

L

A

S

N

D

L

I

K218 (= K166) active site, Schiff-base intermediate with acetaldehyde; mutation to A: Abolishes deoxyribose-phosphate aldolase activity.
K254 (= K198) active site, Proton donor/acceptor; mutation to A: Abolishes deoxyribose-phosphate aldolase activity.

1ub3A Crystal structure of tetrameric structure of aldolase from thermus thermophilus hb8 (see paper)
36% identity, 68% coverage: 46:221/257 of query aligns to 35:202/211 of 1ub3A

query
sites
1ub3A

V

L

C

C

I

I

Y

P

P

P

R

S

F

Y

V

V

P

A

I

W

A

V

R

R

K

A

T

R

L

Y

N

P

A

H

I

-

G

-

A

-

E

A

T

P

V

F

K

R

I

L

A

V

T

T

V

V

T

V

N

G

F

F

P

P

H

L

G

G

N

Y

D

Q

D

E

V

K

A

E

I

V

A

K

V

A

A

L

E

E

T

A

K

A

A

L

A

A

V

C

A

A

Y

R

G

G

A

A

D

D

E

E

V

V

D
|
D

V

M

V

V

F

L

P

H

Y

L

R

G

A

R

L

A

M

K

A

A

G

G

N

D

A

L

E

D

V

Y

G

L

F

E

E

A

L

E

V

V

K

R

A

A

C

V

K

R

A

E

A

A

C

V

P

P

A

Q

N

A

V

V

Q

-

L

L

K

K

V

V

I

I

V

L

E

E

T

T

G

G

E

Y

L

F

K

S

T

P

E

E

A

E

L

I

I

A

R

R

Q

L

A

A

S

-

E

E

I

A

S

A

I

I

D

R

A

G

G

G

A

A

D

D

F

F

I

L

K
|
K

T

T

S

S

T
|
T

G

G

K

F

V

G

P

P

V

R

N

G

A

A

T

S

L

L

E

E

F

D

A

V

K

A

I

L

M

L

L

V

T

R

V

V

I

A

S

Q

E

G

K

R

N

A

T

Q

D

-

V

-

G

-

F

V

K
|
K

P

A

A

A

G
|
G

G

G

V

I

K
x
R

N

D

A

R

E

E

Q

T

A

A

G

L

E

R

Y

M

L

L

A

K

L

A

A

G

E

A

S

S

I

R

L

L

G
|
G

active site: D88 (= D102), K150 (= K166), K179 (= K198)
binding 1-hydroxy-pentane-3,4-diol-5-phosphate: K150 (= K166), T153 (= T169), G182 (= G201), R185 (≠ K204), G202 (= G221)

Sites not aligning to the query:

binding 1-hydroxy-pentane-3,4-diol-5-phosphate: 203, 204

3ngjD Crystal structure of a putative deoxyribose-phosphate aldolase from entamoeba histolytica
32% identity, 81% coverage: 15:221/257 of query aligns to 14:210/222 of 3ngjD

query
sites
3ngjD

M

I

D

D

L

H

T

T

T

L

L

L

N

K

D

A

D

D

D

A

T

T

D

E

A

E

K

Q

V

I

I

R

E

K

L

L

C

C

H

S

K

E

A

A

K

-

S

-

A

A

A

E

G

Y

N

K

T

F

A

A

A

S

V

V

C
|
C

I

V

Y

N

P

P

R

T

F

W

V

V

P

P

I

L

A

C

R

A

K

E

T

L

L

L

N

K

A

G

I

T

G

G

A

-

E

-

T

-

V

V

K

K

I

V

A
x
C

T

T

V

V

T

I

N

G

F

F

P

P

H

L

G

G

N

A

D

T

D

P

V

S

A

E

I

V

A

K

V

A

A

Y

E

E

T

T

K

K

A

V

A

A

V

V

A

E

Y

Q

G

G

A

A

D

E

E

E

V

V

D
|
D

V

M

V

V

F

I

P

N

Y

I

R

G

A

M

L

V

M

K

A

A

G

K

N

K

A

Y

E

D

V

-

G

-

F

-

E

D

L

V

V

E

K

K

A

D

C

V

K

K

A

A

A

V

C

V

P

D

A

A

N

S

V

G

Q

K

-

A

-

L

L

T

K

K

V

V

I

I

V

I

E

E

T

C

G

C

E

Y

L

L

K

T

T

N

E

E

A

E

L

K

I

V

R

-

Q

E

A

V

S

C

E

K

I

R

S

C

I

V

D

A

A

A

G

G

A

A

D

E

F

Y

I

V

K
|
K

T

T

S

S

T

T

G

G

K

F

V

G

P

T

V

H

N

G

A

A

T

T

L

P

E

E

F

D

A

V

K

K

I

L

M

M

L

K

T

D

V

T

I

V

S

G

E

D

K

K

N

A

T

L

D

-

V

-

G

-

F

V

K
|
K

P

A

A

A

G

G

V

I

K

R

N

T

A

F

E
x
D

Q

D

A

A

G

M

E

K

Y

M

L

I

A

N

L

N

A

G

E

A

S

S

I

R

L

I

G

G

active site: D96 (= D102), K158 (= K166), K187 (= K198)
binding zinc ion: C44 (= C47), C65 (≠ A71), D96 (= D102), D196 (≠ E207)

Sites not aligning to the query:

binding zinc ion: 222

Q4ZMV1 Deoxyribose-phosphate aldolase; DERA; 2-deoxy-D-ribose 5-phosphate aldolase; Phosphodeoxyriboaldolase; Deoxyriboaldolase; EC 4.1.2.4 from Pseudomonas syringae pv. syringae (strain B728a) (see paper)
33% identity, 74% coverage: 15:205/257 of query aligns to 13:193/226 of Q4ZMV1

query
sites
Q4ZMV1

M

I

D

D

L

H

T
|
T

T

L

L

L

N

A

D

A

D

D

D

A

T

S

D

R

A

E

K

Q

V

I

I

A

E

T

L

L

C

C

H

A

K

E

A

A

K

R

S

E

A

H

A

-

G

-

N

G

T

F

A

Y

A

S

V

V

C

C

I

V

Y

N

P

S

R

S

F

Q

V

V

P

P

I

F

A

A

R

A

K

R

T

Q

L

L

N

-

A

-

I

-

G

A

A

G

E

S

T

A

V

V

K

K

I

V

A

C

T

A

V
|
V

T

V

N

G

F
|
F

P

P

H

L

G

G

N

A

D

G

D

L

V

S

A

A

I

S

A

K

V

A

A

S

E

E

T

A

K

A

A

L

A

T

V

I

A

A

Y

A

G

G

A

A

D

Q

E

E

V

I

D

D

V

M

V

V

F

L

P

N

Y

I

R

G

A

W

L

L

M

K

A

D

G

G

N

L

A

F

E

D

V

E

G

V

F

R

E

D

L

D

V

I

K

A

A

A

C

V

K

L

A

Q

A

A

C

C

P

-

A

G

N

K

V

V

Q

P

L

L

K

K

V

V

I

I

V

L

E

E

T

T

G

C

E

L

L

L

K

D

T

E

E

A

A

Q

L

K

I

V

R

R

Q

-

A

A

S

C

E

E

I

I

S

C

I

R

D

E

A

L

G

G

A

V

D

A

F

F

I

V

K

K

T

T

S

S

T

T

G

G

K

F

V

S

P

R

V

S

N

G

A

A

T

T

L

L

E

E

F

D

A

V

K

A

I

L

M

M

L

R

T

R

V

V

I

V

S

-

E

-

K

-

N

G

T

P

D

D

V

I

G

G

F

V

K

K

P

A

A
x
S

G
|
G

G

G

V

V

K

R

N

D

T16 (= T18) mutation to L: Decreases synthesis of CTeHP.
V66 (= V73) mutation to K: Exhibits 12% higher activity for synthesis of CTeHP.
F69 (= F76) mutation to R: Decreases synthesis of CTeHP.
S188 (≠ A200) mutation to V: Decreases synthesis of CTeHP.
G189 (= G201) mutation to R: Exhibits higher activity toward DR5P. Decreases synthesis of CTeHP.

3qyqA 1.8 angstrom resolution crystal structure of a putative deoxyribose- phosphate aldolase from toxoplasma gondii me49 (see paper)
27% identity, 95% coverage: 12:256/257 of query aligns to 17:273/273 of 3qyqA

query
sites
3qyqA

L

L

S

N

M

F

D

E

L

V

T

A

L

L

N

T

D

D

D
x
G

D
x
E

T

T

D

N

A

E

K
x
S

V

V

I

A

E

A

L
x
V

C

C

H

-

K

-

A

-

K

K

S

I

A

A

G

K

N

D

T

P

A

A

-

I

-

V

A

G

V

V

C

S

I

V

Y

R

P

P

R

A

F

F

V

V

P

R

I

F

A

I

R

R

K

Q

T

E

L

L

N

V

A

K

I

S

G

A

A

P

E

E

T

V

-

A

-

G

V

I

K

K

I

V

A

C

T

A

V

A

T

V

N

N

F

F

P

P

H
x
E

G

G

N

T

D

G

D

T

V

P

A

D

I

T

A

V

V

S

A

L

E

E

T

A

K

V

A

G

A

A

V

L

A

K

Y

D

G

G

A

A

D

D

E

E

V

I

D
x
E

V

C

V

L

F

I

P

D

Y

W

R

R

A

R

L

M

M

N

A

E

-

N

-

V

-

A

-

D

G

G

N

E

A

S

E

R

V

I

G

R

F

L

E

L

L

V

V

S

K

E

A

V

C

K

K

K

A

V

C

G

P

P

A

K

N

T

V

-

Q

-

L

L

K

K

V

V

I

V

V

L

E

S

T

G

G

G

E
|
E

L

L

K

Q

T

G

E

G

A

D

L

I

I

I

R

S

Q

R

A

A

S

A

E

V

I

A

S

A

I

L

D

E

A

G

G

G

A

A

D

D

F

F

I

L

K
x
Q

T

T

S

S

T

S

G

G

K

L

V

G

P

A

V

T

N

H

A

A

T

T

L

M

E

F

F

T

A

V

K

H

I

L

M

I

L

S

T

I

V

A

I

L

S

R

E

E

K

Y

N

M

T

V

D

R

-

E

-

N

-

E

-

R

-

I

-

R

-

V

-

E

-

G

-

V

-

R

-

C

V

I

G

G

F

I

K
|
K

-

I

P

E

A

V

G

G

G

D

V

V

K

H

N

M

A

A

E

E

Q

T

A

A

G

-

E

D

Y

F

L

L

A

M

L

Q

A

M

E

I

S

F

I

E

L

N

G

G

K

P

D

R

W

S

V

I

S

V

P

R

A

D

K

K

F

F

R

R

F

V

G

G

A

G

S

G

S

-

L

-

A
x
F

N

N

L

L

A

K

E

E

L

L

E

R

L

D

A

C

D

Y

K

E

P

S

A

W

D

D

S

S

S

V

G

G

active site: E108 (≠ D102), Q174 (≠ K166), K218 (= K198)
binding beta-D-fructofuranose: E29 (≠ D24), S33 (≠ K28), V37 (≠ L32), F256 (≠ A239)
binding alpha-D-glucopyranose: G28 (≠ D23), S33 (≠ K28), E84 (≠ H78), E151 (= E143)

Query Sequence

>WP_017221003.1 NCBI__GCF_000276805.1:WP_017221003.1
MSNFKVAAQRALSMMDLTTLNDDDTDAKVIELCHKAKSAAGNTAAVCIYPRFVPIARKTL
NAIGAETVKIATVTNFPHGNDDVAIAVAETKAAVAYGADEVDVVFPYRALMAGNAEVGFE
LVKACKAACPANVQLKVIVETGELKTEALIRQASEISIDAGADFIKTSTGKVPVNATLEF
AKIMLTVISEKNTDVGFKPAGGVKNAEQAGEYLALAESILGKDWVSPAKFRFGASSLLAN
LLAELELADKPADSSGY

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