SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_045680742.1 NCBI__GCF_000960975.1:WP_045680742.1 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)
49% identity, 96% coverage: 6:252/257 of query aligns to 4:258/259 of P0A6L0

query
sites
P0A6L0

L

L

Q

K

E

A

A

S

A

L

V

R

S

A

L

L

S

K

L

L

L

M

D

D

L

L

T

T

N

T

L

L

S

N

D

D

C

D

T

T

E

D

K

E

D

K

I

V

E

I

I

A

L

L

L

C

E

H

R

Q

A

A

H

K

T

T

P

P

Y

V

G

G

T

N

P

T

A

A

I

I

C
|
C

I

I

W

Y

P

P

R

R

F

F

V

I

S

P

L

I

A

A

R

R

Q

K

M

T

L

L

G

K

Q

E

D

Q

H

G

L

T

-

P

-

E

I

I

K

R

I

I

A

A

T

T

V

V

V

T

N

N

F

F

P

P

S

H

G

G

D

N

L

D

S

D

I

I

S

D

A

I

V

A

E

L

E

A

E

E

T

T

E

R

Q

A

A

A

I

I

R

A

D

Y

G

G

A

A

D

D

E

E

I

V

D
|
D

L

V

V

V

I

F

P

P

Y

Y

K

R

K

A

L

L

K

M

A

A

G

G

N

N

E

E

W

Q

A

V

V

G

S

F

E

D

M

L

I

V

R

K

A

A

V

C

R

K

F

E

H

A

C

C

R

A

E

A

P

A

-

N

V

V

R

L

L

L

K
|
K

V

V

I

I

L

I

E

E

T

T

G

G

E

E

L

L

G

K

D

D

A

E

G

A

L

L

I

I

R

R

K

K

A

A

S

S

E

E

L

I

A

S

I

I

A

K

E

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

S

A

V

V

N

N

A

A

T

T

L

P

E

E

A

S

A

A

D

R

I

I

M

M

L

M

G

E

V

V

I

I

R

R

Q

D

-

M

-

G

A

V

D

E

R

K

T

T

V

V

G

G

F

F

K
|
K

P

P

A

A

G

G

I

V

S

R

S

T

V

A

R

E

D

D

A

A

Q

Q

L

K

Y

Y

L

L

S

A

L

I

A

A

E

D

T

E

V

L

M

F

G

G

E

A

G

D

W

W

V

A

M

D

P

A

T

R

T

H

F

Y

R

R

F

F

G

G

-

A

-

S

A

L

S

L

S

A

L

S

L

L

N

L

D

K

I

A

L

L

G

G

V

H

L

G

D

D

G

G

K

K

A

S

S

A

S

S

C47 (= C49) 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.

6z9iB Escherichia coli d-2-deoxyribose-5-phosphate aldolase - n21k mutant complex with reaction products (see paper)
50% identity, 89% coverage: 6:233/257 of query aligns to 2:234/248 of 6z9iB

query
sites
6z9iB

L

L

Q

K

E

A

A

S

A

L

V

R

S

A

L

L

S

K

L

L

L

M

D

D

L

L

T

T

N

T

L

L

S

K

D

D

C

D

T

T

E

D

K

E

D

K

I

V

E

I

I

A

L

L

L

C

E

H

R

Q

A

A

H

K

T

T

P

P

Y

V

G

G

T

N

P

T

A

A

I

I

C

C

I

I

W

Y

P

P

R

R

F

F

V

I

S

P

L

I

A

A

R

R

Q

K

M

T

L

L

G

K

Q

E

D

Q

H

G

L

T

-

P

-

E

I

I

K

R

I

I

A

A

T

T

V

V

V

T

N

N

F

F

P

P

S

H

G

G

D

N

L

D

S

D

I

I

S

D

A

I

V

A

E

L

E

A

E

E

T

T

E

R

Q

A

A

A

I

I

R

A

D

Y

G

G

A

A

D

D

E

E

I

V

D

D

L

V

V

V

I

F

P

P

Y

Y

K

R

K

A

L

L

K

M

A

A

G

G

N

N

E

E

W

Q

A

V

V

G

S

F

E

D

M

L

I

V

R

K

A

A

V

C

R

K

F

E

H

A

C

C

R

A

E

A

P

A

-

N

V

V

R

L

L

L

K

K

V

V

I

I

L

I

E

E

T

T

G

G

E

E

L

L

G

K

D

D

A

E

G

A

L

L

I

I

R

R

K

K

A

A

S

S

E

E

L

I

A

S

I

I

A

K

E

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

S

A

V

V

N

N

A

A

T

T

L

P

E

E

A

S

A

A

D

R

I

I

M

M

L

M

G

E

V

V

I

I

R

R

Q

D

-

M

-

G

A

V

D

E

R

K

T

T

V

V

G

G

F

F

K

K

P

P

A

A

G
|
G

I

V

S
x
R

S

T

V

A

R

E

D

D

A

A

Q

Q

L

K

Y

Y

L

L

S

A

L

I

A

A

E

D

T

E

V

L

M

F

G

G

E

A

G

D

W

W

V

A

M

D

P

A

T

R

T

H

F

Y

R

R

F

F

G
|
G

binding glyceraldehyde-3-phosphate: T168 (= T169), G202 (= G201), G203 (= G202), R205 (≠ S204), 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)
50% identity, 89% coverage: 6:233/257 of query aligns to 2:234/248 of 5el1A

query
sites
5el1A

L

L

Q

K

E

A

A

S

A

L

V

R

S

A

L

L

S

K

L

L

L

M

D

D

L

L

T
|
T

N

T

L

L

S

N

D

D

C

D

T

T

E

D

K

E

D

K

I

V

E

I

I

A

L

L

L

C

E

H

R

Q

A

A

H

K

T

T

P

P

Y

V

G

G

T

N

P

T

A

A

I

I

C
|
C

I

I

W

Y

P

P

R

R

F

F

V

I

S

P

L

I

A

A

R

R

Q

E

M

T

L

L

G

K

Q

E

D

Q

H

G

L

T

-

P

-

E

I

I

K

R

I

I

A

A

T

T

V

V

V

T

N

N

F

F

P

P

S

H

G

G

D

N

L

D

S

D

I

I

S

D

A

I

V

A

E

L

E

A

E

E

T

T

E

R

Q

A

A

A

I

I

R

A

D

W

G

G

A

A

D

D

E

E

I

V

D
|
D

L

V

V

V

I

F

P

P

Y

Y

K

R

K

A

L

L

K

M

A

A

G

G

N

N

E

E

W

Q

A

V

V

G

S

F

E

D

M

L

I

V

R

K

A

A

V

C

R

K

F

E

H

A

C

C

R

A

E

A

P

A

-

N

V

V

R

L

L

L

K

K

V

V

I

I

L

I

E

E

T

T

G

G

E

E

L

L

G

K

D

D

A

E

G

A

L

L

I

I

R

R

K

K

A

A

S

S

E

E

L

I

A

S

I

I

A

K

E

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

S

A

V

V

N

N

A

A

T

T

L

P

E

E

A

S

A

A

D

R

I

I

M

M

L

M

G

E

V

V

I

I

R

R

Q

D

-

M

-

G

A

V

D

E

R

K

T

T

V

V

G

G

F

F

K
|
K

P

P

A

A

G

G

I

V

S

R

S

T

V

A

R

E

D

D

A

A

Q

Q

L

K

Y

Y

L

L

S

A

L

I

A

A

E

D

T

E

V

L

M

F

G

G

E

A

G

D

W

W

V

A

M

D

P

A

T

R

T

H

F

Y

R

R

F

F

G

G

active site: D100 (= D102), K165 (= K166), K199 (= K198)
binding 1-butanol: T16 (= T20), C45 (= C49), 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)
50% identity, 89% coverage: 6:233/257 of query aligns to 2:234/248 of 5ekyA

query
sites
5ekyA

L

L

Q

K

E

A

A

S

A

L

V

R

S

A

L

L

S

K

L

L

L

M

D

D

L

L

T

T

N

T

L

L

S

N

D

D

C

D

T

T

E

D

K

E

D

K

I

V

E

I

I

A

L

L

L

C

E

H

R

Q

A

A

H

K

T

T

P

P

Y

V

G

G

T

N

P

T

A

A

I

I

C

C

I

I

W

Y

P

P

R

R

F

F

V

I

S

P

L

I

A

A

R

R

Q

E

M

T

L

L

G

K

Q

E

D

Q

H

G

L

T

-

P

-

E

I

I

K

R

I

I

A

A

T

T

V

V

V

T

N

N

F

F

P

P

S

H

G

G

D

N

L

D

S

D

I

I

S

D

A

I

V

A

E

L

E

A

E

E

T

T

E

R

Q

A

A

A

I

I

R

A

D

W

G

G

A

A

D

D

E

E

I

V

D
|
D

L

V

V

V

I

F

P

P

Y

Y

K

R

K

A

L

L

K

M

A

A

G

G

N

N

E

E

W

Q

A

V

V

G

S

F

E

D

M

L

I

V

R

K

A

A

V

C

R

K

F

E

H

A

C

C

R

A

E

A

P

A

-

N

V

V

R

L

L

L

K

K

V

V

I

I

L

I

E

E

T

T

G

G

E

E

L

L

G

K

D

D

A

E

G

A

L

L

I

I

R

R

K

K

A

A

S

S

E

E

L

I

A

S

I

I

A

K

E

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

S

A

V

V

N

N

A

A

T

T

L

P

E

E

A

S

A

A

D

R

I

I

M

M

L

M

G

E

V

V

I

I

R

R

Q

D

-

M

-

G

A

V

D

E

R

K

T

T

V

V

G

G

F

F

K
|
K

P

P

A
|
A

G

G

I

V

S

R

S

T

V

A

R

E

D

D

A

A

Q

Q

L

K

Y

Y

L

L

S

A

L

I

A

A

E

D

T

E

V

L

M

F

G

G

E

A

G

D

W

W

V

A

M

D

P

A

T

R

T

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

1jcjA Observation of covalent intermediates in an enzyme mechanism at atomic resolution (see paper)
50% identity, 89% coverage: 6:233/257 of query aligns to 5:237/252 of 1jcjA

query
sites
1jcjA

L

L

Q

K

E

A

A

S

A

L

V

R

S

A

L

L

S

K

L

L

L

M

D

D

L

L

T

T

N

T

L

L

S

N

D

D

C

D

T

T

E

D

K

E

D

K

I

V

E

I

I

A

L

L

L

C

E

H

R

Q

A

A

H

K

T

T

P

P

Y

V

G

G

T

N

P

T

A

A

I

I

C

C

I

I

W

Y

P

P

R

R

F

F

V

I

S

P

L

I

A

A

R

R

Q

K

M

T

L

L

G

K

Q

E

D

Q

H

G

L

T

-

P

-

E

I

I

K

R

I

I

A

A

T

T

V

V

V

T

N

N

F

F

P

P

S

H

G

G

D

N

L

D

S

D

I

I

S

D

A

I

V

A

E

L

E

A

E

E

T

T

E

R

Q

A

A

A

I

I

R

A

D

Y

G

G

A

A

D

D

E

E

I

V

D
|
D

L

V

V

V

I

F

P

P

Y

Y

K

R

K

A

L

L

K

M

A

A

G

G

N

N

E

E

W

Q

A

V

V

G

S

F

E

D

M

L

I

V

R

K

A

A

V

C

R

K

F

E

H

A

C

C

R

A

E

A

P

A

-

N

V

V

R

L

L

L

K

K

V

V

I

I

L

I

E

E

T

T

G

G

E

E

L

L

G

K

D

D

A

E

G

A

L

L

I

I

R

R

K

K

A

A

S

S

E

E

L

I

A

S

I

I

A

K

E

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

S

A

V

V

N

N

A

A

T

T

L

P

E

E

A

S

A

A

D

R

I

I

M

M

L

M

G

E

V

V

I

I

R

R

Q

D

-

M

-

G

A

V

D

E

R

K

T

T

V

V

G

G

F

F

K
x
L

P

P

A

A

G
|
G

G

G

I

V

S

R

S

T

V

A

R

E

D

D

A

A

Q

Q

L

K

Y

Y

L

L

S

A

L

I

A

A

E

D

T

E

V

L

M

F

G

G

E

A

G

D

W

W

V

A

M

D

P

A

T

R

T

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

7p76A Re-engineered 2-deoxy-d-ribose-5-phosphate aldolase catalysing asymmetric michael addition reactions, schiff base complex with cinnamaldehyde (see paper)
47% identity, 93% coverage: 6:245/257 of query aligns to 1:245/247 of 7p76A

query
sites
7p76A

L

L

Q

K

E

A

A

S

A

L

V

R

S

A

L

L

S

K

L

L

L

M

D

D

L

L

T

S

N

T

L

L

S

N

D

G

D

D

C

Y

T

T

E

D

K

E

D

K

I

V

E

I

I

A

L

L

L

C

E

H

R

Q

A

A

H

K

T

T

P

P

Y

V

G

G

T

N

P

T

A

A

I

I

C
x
S

I
|
I

W
x
Y

P

P

R

R

F

S

V

I

S

P

L

I

A

A

R

R

Q

K

M

T

L

L

G

K

Q

E

D

Q

H

G

L

T

-

P

-

E

I

I

K

R

I

I

A

A

T

T

V
|
V

V

T

N

N

F
|
F

P

P

S

H

G

G

D

N

L

D

S

D

I

I

S

E

A

I

V

A

E

L

E

A

E

E

T

T

E

R

Q

A

A

A

I

I

R

A

D

Y

G

G

A

A

D

D

E

E

I

V

D

D

L

V

V

V

I

F

P

P

Y

Y

K

R

K

A

L

L

K

M

A

A

G

G

N

N

E

E

W

Q

A

V

V

G

S

F

E

D

M

L

I

V

R

K

A

A

V

C

R

K

F

E

H

A

C

C

R

A

E

A

P

A

-

N

V

V

R

L

L

L

K

K

V

V

I

I

L

I

E

E

T

S

G

G

E

E

L

L

G

K

D

D

A

E

G

A

L

L

I

I

R

R

K

K

A

A

S

S

E

E

L

I

A

S

I

I

A

K

E

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

S

A

V

V

N

N

A

A

T

T

L

P

E

E

A

S

A

A

D

R

I

I

M

M

L

M

G

E

V

V

I

I

R

R

Q

D

-

M

-

G

A

V

D

E

R

K

T

S

V

V

G

G

F

F

K

K

P

V

A

T

G

G

I

A

S

R

S

T

V

A

R

E

D

D

A

A

Q

Q

L

K

Y

Y

L

L

S

A

L

I

A

A

E

D

T

E

V

L

M

F

G

G

E

A

G

D

W

W

V

A

M

D

P

A

T

R

T

H

F

Y

R

R

F

F

G

G

A

A

S

S

S

G

L

L

N

A

D

S

I

L

L

L

G

K

V

A

L

L

binding (2E)-3-phenylprop-2-enal: S44 (≠ C49), I45 (= I50), Y46 (≠ W51), V70 (= V73), F73 (= F76), K164 (= K166)

8forA Crystal structure of kemp eliminase ke70-core with bound transition state analogue
44% identity, 89% coverage: 6:233/257 of query aligns to 1:234/249 of 8forA

query
sites
8forA

L

L

Q

K

E

A

A

S

A

L

V

R

S

A

L

L

S

K

L

L

L

M

D

H

L

L

-

A

T

T

N

S

L

A

S

N

D

D

C

D

T

T

E

D

K

E

D

K

I

V

E

I

I

A

L

L

L

C

E

H

R

Q

A

A

H

K

T

T

P

P

Y

V

G

G

T

T

P

T

A

D

A

A

I

I

C
x
F

I

I

W

Y

P

P

R

R

F

F

V

I

S

P

L

I

A

A

R

R

Q

K

M

T

L

L

G

K

Q

E

D

Q

H

G

L

T

-

P

-

E

I

I

K

R

I

I

A

C

T

T

V

S

V

T

N

N

F

F

P

P

S

H

G

G

D

N

L

D

S

D

I

I

S

D

A

I

V

A

E

L

E

A

E

E

T

T

E

R

Q

A

A

A

I

I

R

A

D

Y

G

G

A

A

D

D

E

S

I

V

D
x
A

L

V

V

V

I

F

P

P

Y

Y

K

R

K

A

L

L

K

M

A

A

G

G

N

N

E

E

W

Q

A

V

V

G

S

F

E

D

M

L

I

V

R

K

A

A

V

C

R

K

F

E

H

A

C

C

R

A

E

A

P

A

-

N

V

V

R

L

L

L

K

A

V

V

I

I

L

I

E

E

T

T

G

G

E

E

L

L

G

K

D

D

A

E

G

A

L

L

I

I

R

R

K

K

A

A

S

S

E

E

L

I

A

S

I

I

A

K

E

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

S

A

V

V

N

G

A

A

T

T

L

P

E

E

A

S

A

A

D

R

I

I

M

M

L

M

G

E

V

V

I

I

R

R

Q

D

-

M

-

G

A

V

D

E

R

K

T

T

V

V

G

G

F

F

K

I

P

P

A
x
V

G

G

I

V

S

R

S

T

V

A

R

E

D

D

A

A

Q

Q

L

K

Y

Y

L

L

S

A

L

I

A

A

E

D

T

E

V

L

M

F

G

G

E

A

G

D

W

W

V

A

M

D

P

A

T

R

T

H

F

Y

R

A

F

F

G
|
G

binding 6-nitrobenzotriazole: F45 (≠ C49), A100 (≠ D102), V201 (≠ A200), G234 (= G233)

3q2dA Optimization of the in silico designed kemp eliminase ke70 by computational design and directed evolution (see paper)
44% identity, 87% coverage: 11:233/257 of query aligns to 5:232/246 of 3q2dA

query
sites
3q2dA

A

A

V

S

S

S

L

L

S

R

L

A

L

L

D

K

L

L

T

M

N
x
H

L

L

S

A

D

T

D

S

C

D

T

T

E

D

K

E

D

N

I

V

E

I

I

A

L

L

L

C

E

H

R

Q

A

A

H

K

T

T

P

P

Y

V

G

G

T

N

P

T

A

D

A

A

I

I

C
x
F

I

I

W

Y

P

P

R

R

F

F

V

I

S

P

L

I

A

A

R

R

Q

K

M

T

L

L

G

K

Q

E

D

Q

H

G

L

T

-

P

-

E

I

I

K

R

I

I

A
x
C

T

T

V

S

V

T

N

N

F

F

P

P

S

H

G

G

D

N

L

D

S

D

I

I

S

D

A

I

V

A

E

L

E

A

E

E

T

T

E

R

Q

A

A

A

I

I

R

A

D

Y

G

G

A

A

D

D

E
x
S

I

V

D
x
A

L

V

V

V

I

F

P

P

Y

Y

K

R

K

A

L

L

K

M

A

A

G

G

N

N

E

E

W

Q

A

V

V

G

S

F

E

D

M

L

I

V

R

K

A

A

V

C

R

K

F

E

H

A

C

C

R

A

E

A

P

A

-

N

V

V

R

L

L

L

K
x
A

V

V

I

I

L

I

E

E

T

T

G

G

E

E

L

L

G

K

D

D

A

E

G

A

L

L

I

I

R

R

K

K

A

A

S

S

E

E

L

I

A

S

I

I

A

K

E

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

S

A

V

V

N

G

A

A

T

T

L

P

E

E

A

S

A

A

D

R

I

I

M

M

L

M

G

E

V

V

I

I

R

R

Q

D

-

M

-

G

A

V

D

E

R

K

T

T

V

V

G

G

F

F

K
x
I

P

P

A

V

G

G

I

V

S

R

S

T

V

A

R

E

D

D

A

A

Q

Q

L

K

Y

Y

L

L

S

A

L

I

A

A

E

D

T

E

V

L

M

F

G

G

E

A

G

D

W

W

V

A

M

D

P

A

T

R

T

H

F

Y

R

A

F

F

G

G

binding 5-nitro-1H-benzotriazole: H15 (≠ N21), F43 (≠ C49), 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)
39% identity, 89% coverage: 13:241/257 of query aligns to 50:297/318 of Q9Y315

query
sites
Q9Y315

S

A

L

V

S

T

L

F

L

I

D

D

L

L

T

T

N

T

L

L

S

S

D

G

D

D

C

D

T

T

E

S

K

S

D

N

I

I

E

Q

I

R

L

L

L

C

E

Y

R

K

A

A

H

K

T

Y

P

P

Y

I

G

R

-

E

-

D

-

L

-

K

-

A

-

L

-

N

-

M

-

H

-

D

-

K

-

G

-

I

T

T

P

T

A

A

I

V

C

C

I

V

W

Y

P

P

-

A

R

R

F

V

V

C

S

D

L

A

A

V

R

K

Q

A

M

L

L

K

G

A

Q

A

D

G

H

C

L

N

I

I

K

P

I

V

A

A

T

S

V

V

V

A

-

A

N

G

F

F

P

P

S

A

G

G

D

Q

L

T

S

H

I

L

S

K

A

T

V

R

E

L

E

E

T

I

E

R

Q

L

A

A

I

V

R

E

D

D

G

G

A

A

D

T

E

E

I

I

D

D

L

V

V

V

I

I

P

N

Y

R

K

S

K

L

L

V

K

L

A

T

G

G

N

Q

E

W

W

E

A

A

V

L

S

Y

E

D

M

E

I

I

R

R

A

Q

V

F

R

R

F

K

H

A

C

C

R

G

E

E

P

-

V

A

R

H

L

L

K

K

V

T

I

I

L

L

E

A

T

T

G

G

E

E

L

L

G

G

D

T

A

L

G

T

L

N

I

V

R

Y

K

K

A

A

S

S

E

M

L

I

A

A

I

M

A

M

E

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

S

T

V

V

N

N

A

A

T

T

L

F

E

P

A

V

A

A

D

I

I

V

M

M

L

L

G

R

V

A

I

I

R

R

-

D

-

F

-

W

Q

K

A

T

D

G

R

N

T

K

V

I

G

G

F

F

K
|
K

P

P

A

A

G

G

I

I

S

R

S

S

V

A

R

K

D

D

A

S

Q

L

L

A

Y

W

L

L

S

S

L

L

A

V

E

K

T

E

V

E

M

L

G

G

E

D

G

E

W

W

V

L

M

K

P

P

T

E

T

L

F

F

R

R

F

I

G

G

A

A

S

S

S

T

L

L

N

S

D

D

I

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)
39% identity, 61% coverage: 48:203/257 of query aligns to 35:184/211 of 1ub3A

query
sites
1ub3A

I

L

C

C

I

I

W

P

P

P

R

S

F

Y

V

V

S

A

L

W

A

V

R

R

Q

A

M

R

L

Y

G

P

Q

H

D

A

H

P

L

F

I

-

K

R

I

L

A

V

T

T

V

V

N

G

F

F

P

P

S

L

G

G

D

Y

L

Q

S

E

I

K

S

E

A

V

V

K

E

A

E

L

E

E

T

A

E

A

Q

L

A

A

I

C

R

A

D

R

G

G

A

A

D

D

E

E

I

V

D
|
D

L

M

V

V

I

L

P

H

Y

L

K

G

K

R

L

A

K

K

A

A

G

G

N

D

E

L

W

D

A

Y

V

L

S

E

E

A

M

E

I

V

R

R

A

A

V

V

R

R

F

E

H

A

C

V

R

P

E

Q

P

A

V

V

R

-

L

L

K

K

V

V

I

I

L

L

E

E

T

T

G

G

E

Y

L

F

G

S

D

P

A

E

G

E

L

I

I

A

R

R

K

L

A

A

S

-

E

E

L

A

A

A

I

I

A

R

E

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

S

P

V

R

N

G

A

A

T

S

L

L

E

E

A

-

D

D

I

V

M

A

L

L

G

-

V

L

I

V

R

R

Q

V

A

A

D

Q

R

G

T

R

V

A

G

Q

F

V

K
|
K

P

A

A

A

G
|
G

G

G

I

I

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

Sites not aligning to the query:

binding 1-hydroxy-pentane-3,4-diol-5-phosphate: 185, 202, 203, 204

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)
34% identity, 80% coverage: 17:221/257 of query aligns to 13:209/226 of Q4ZMV1

query
sites
Q4ZMV1

L

I

D

D

L

H

T
|
T

N

L

L

L

S

A

D

A

D

D

C

A

T

S

E

R

K

E

D

Q

I

I

E

A

I

T

L

L

L

C

E

A

-

E

-

A

R

R

A

E

H

H

T

G

P

F

Y

Y

G

-

T

-

P

-

A

-

A

S

I

V

C

C

I

V

W

N

P

S

R

S

F

Q

V

V

S

P

L

F

A

A

-

A

R

R

Q

Q

M

L

L

A

G

G

Q

S

D

-

H

-

L

A

I

V

K

K

I

V

A

C

T

A

V
|
V

V

V

N

G

F
|
F

P

P

S

L

G

G

D

A

L

G

S

L

I

S

S

A

A

S

V

K

E

A

E

S

E

E

T

A

E

A

Q

L

A

T

I

I

R

A

D

A

G

G

A

A

D

Q

E

E

I

I

D

D

L

M

V

V

I

L

P

N

Y

I

K

G

K

W

L

L

K

K

A

D

G

G

N

L

E

F

W

D

A

E

V

V

S

R

E

D

M

D

I

I

R

A

A

A

V

V

R

L

F

Q

H

A

C

C

R

G

E

K

P

-

V

V

R

P

L

L

K

K

V

V

I

I

L

L

E

E

T

T

G

C

E

L

L

L

G

D

D

E

A

A

G

Q

L

K

I

V

R

R

K

-

A

A

S

C

E

E

L

I

A

C

I

R

A

E

E

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

S

R

V

S

N

G

A

A

T

T

L

L

E

E

A

D

A

V

D

A

I

L

M

M

L

R

G

R

V

V

I

V

R

-

Q

-

A

-

D

G

R

P

T

D

V

I

G

G

F

V

K

K

P

A

A
x
S

G
|
G

G

G

I

V

S

R

S

D

V

V

R

A

D

T

A

A

Q

R

L

A

Y

M

L

I

S

E

L

A

A

G

E

A

T

T

V

R

M

L

G

G

T16 (= T20) 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, 88% coverage: 14:240/257 of query aligns to 17:248/273 of 3qyqA

query
sites
3qyqA

L

L

S

N

L

F

D

E

L

V

T

A

N

A

L

L

S

T

D

D

D
x
G

C
x
E

T

T

E

N

K

E

D
x
S

I

V

E

A

I

A

L
x
V

L

C

E

K

R

I

A

A

H

A

T

K

P

D

Y

-

G

-

T

-

P

P

A

A

-

I

-

V

A

G

I

V

C

S

I

V

W

R

P

P

R

A

F

F

V

V

S

R

L

F

A

I

R

R

Q

Q

M

E

L

L

G

V

Q

K

D

S

H

A

L

P

-

E

-

V

-

A

-

G

I

I

K

K

I

V

A

C

T

A

V

A

V

V

N

N

F

F

P

P

S
x
E

G

G

D

T

L

G

S

T

I

P

S

D

A

T

V

V

E

S

E

L

E

E

T

A

E

V

Q

G

A

A

I

L

R

K

D

D

G

G

A

A

D

D

E

E

I

I

D
x
E

L

C

V

L

I

I

P

D

Y

W

K

R

L

M

K

N

-

E

-

N

-

V

A

A

G

D

N

G

E

E

W

S

A

R

V

I

S

R

E

L

M

L

I

V

R

S

A

E

V

V

R

K

F

-

H

K

C

V

R

V

E

G

P

P

V

K

R

T

L

L

K

K

V

V

I

V

L

L

E

S

T

G

G

G

E
|
E

L

L

G

Q

D

G

A

G

G

D

L

I

I

I

R

S

K

R

A

A

S

A

E

V

L

A

A

A

I

L

A

E

E

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

S

A

V

T

N

H

A

A

T

T

L

M

E

F

A

T

A

V

D

H

I

L

M

I

L

S

G

I

V

A

I

L

R

R

Q

E

A

-

D

-

R

Y

T

M

V

V

G

R

F

E

K

N

P

E

A

R

G

I

G

R

I

V

S

E

S

G

V

V

R

R

D

C

A

I

Q

G

L

I

Y
x
K

L

I

S

E

L

V

A

G

E

D

T

V

V

H

M

M

G

A

E

E

-

T

-

A

G

D

W

F

V

L

M

M

P

Q

T

M

T

I

F

F

R

E

F

N

G

G

A

P

S

R

S

S

L

I

L

V

N

R

D

D

active site: E108 (≠ D102), Q174 (≠ K166), K218 (≠ Y212)
binding beta-D-fructofuranose: E29 (≠ C26), S33 (≠ D30), V37 (≠ L34)
binding alpha-D-glucopyranose: G28 (≠ D25), S33 (≠ D30), E84 (≠ S78), E151 (= E143)

Sites not aligning to the query:

binding beta-D-fructofuranose: 256

3ngjD Crystal structure of a putative deoxyribose-phosphate aldolase from entamoeba histolytica
31% identity, 75% coverage: 17:209/257 of query aligns to 14:198/222 of 3ngjD

query
sites
3ngjD

L

I

D

D

L

H

T

T

N

L

L

L

S

K

D

A

D

D

C

A

T

T

E

E

K

E

D

Q

I

I

E

R

I

K

L

L

L

C

-

S

E

E

R

A

A

A

H

E

T

Y

P

K

Y

F

G

-

T

-

P

-

A

A

A

S

I

V

C
|
C

I

V

W

N

P

P

R

T

F

W

V

V

S

P

L

L

A

C

R

A

Q

E

M

L

L

L

G

-

Q

K

D

G

H

T

L

G

I

V

K

K

I

V

A
x
C

T

T

V

V

V

I

N

G

F

F

P

P

S

L

G

G

D

A

L

T

S

P

I

S

S

E

A

V

V

K

E

A

E

Y

E

E

T

T

E

K

Q

V

A

A

I

V

R

E

D

Q

G

G

A

A

D

E

E

E

I

V

D
|
D

L

M

V

V

I

I

P

N

Y

I

K

G

K

M

L

V

K

K

A

A

G

K

N

K

E

Y

W

D

A

D

V

V

S

E

E

K

M

D

I

V

R

K

A

A

V

V

R

-

F

V

H

D

C

A

R

S

E

G

P

K

V

A

R

L

L

T

K

K

V

V

I

I

L

I

E

E

T

C

G

C

E

Y

L

L

G

T

D

N

A

E

G

E

L

K

I

V

R

-

K

E

A

V

S

C

E

K

L

R

A

C

I

V

A

A

E

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

S

T

V

H

N

G

A

A

T

T

L

P

E

E

A

D

A

V

D

K

I

L

M

M

L

K

G

D

V

T

I

V

R

-

Q

-

A

G

D

D

R

K

T

A

V

L

G

-

F

V

K
|
K

P

A

A

A

G

G

I

I

S

R

S

T

V

F

R
x
D

D

D

A

A

active site: D96 (= D102), K158 (= K166), K187 (= K198)
binding zinc ion: C44 (= C49), C65 (≠ A71), D96 (= D102), D196 (≠ R207)

Sites not aligning to the query:

binding zinc ion: 222

Query Sequence

>WP_045680742.1 NCBI__GCF_000960975.1:WP_045680742.1
MKHHSLQEAAAVSLSLLDLTNLSDDCTEKDIEILLERAHTPYGTPAAICIWPRFVSLARQ
MLGQDHLIKIATVVNFPSGDLSISAVEEETEQAIRDGADEIDLVIPYKKLKAGNEWAVSE
MIRAVRFHCREPVRLKVILETGELGDAGLIRKASELAIAEGADFIKTSTGKVSVNATLEA
ADIMLGVIRQADRTVGFKPAGGISSVRDAQLYLSLAETVMGEGWVMPTTFRFGASSLLND
ILGVLDGKASSSGGSGY

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