SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_048507311.1 NCBI__GCF_001045465.1:WP_048507311.1 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 20 (the maximum) hits to proteins with known functional sites (download)

Q89WV5 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110) (see paper)
54% identity, 99% coverage: 8:634/636 of query aligns to 19:642/648 of Q89WV5

query
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Q89WV5

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G263 (= G252) mutation to I: Loss of activity.
G266 (= G255) mutation to I: Great decrease in activity.
K269 (= K258) mutation to G: Great decrease in activity.
E414 (= E403) mutation to Q: Great decrease in activity.

P27550 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Escherichia coli (strain K12) (see paper)
53% identity, 98% coverage: 10:634/636 of query aligns to 21:645/652 of P27550

query
sites
P27550

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K609 (= K598) modified: N6-acetyllysine; by autocatalysis

Q8ZKF6 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
53% identity, 98% coverage: 11:634/636 of query aligns to 23:645/652 of Q8ZKF6

query
sites
Q8ZKF6

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F

-

V

-

W

W

Y

I

Q

T

R

P

W

Y

S

Q

K

K

V

V

-

K

-

N

V

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Y

F

D

A

M

P

N

G

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N

A

V

K

S

I

I

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W

W

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K

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D

A

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L

L

N

N

I

L

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A

K

A

N

N

C

C

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L

D

D

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H

H

L

L

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L

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V

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C

K

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A

A

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N

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L

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L

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M

L

G

G

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K

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V

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M

M

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A

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A

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M

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L

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C

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x
R

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L

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K

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L

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K

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K

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A

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|
T

G

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Y

Y

I

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L

L

Y

Y

G

G

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P

L

L

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A

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C

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G

A

A

T

T

V

L

I

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F

E

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G

G

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x
N

Y

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P

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A

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A
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A

P

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A

A

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A

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L

A

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A

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D

L

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L

L

K

R

V

I

I

L

G

G

S

S

V

V

G

G

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E

P

P

I

I

N

N

E

P

E

E

A

A

W

W

H

E

W

W

F

Y

N

W

D

K

H

K

V

I

G

G

K

K

K

E

K

K

C

C

P

P

V

V

D

D

T

T

W

W

Q

Q

T

T

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T

G

G

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F

M

M

I

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P

L

L

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A

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I

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K

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A

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P

L

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P

F

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G

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L

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D

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N

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L

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Y

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F

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G

N

K

M

Y

Y

F

F

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G

G

D

D

G

G

A

A

L

R

R

R

D

D

E

E

V

D

G

G

Y

Y

R

W

I

I

T

T

G

G

R

R

V

V

D
|
D

D

D

V

V

I

L

I

N

V

V

S
|
S

G
|
G

H

H

N
x
R

L

L

G

G

T

T

A

A

P

E

I

I

E

E

D

S

S

A

I

L

N

V

E

A

H

H

P

P

A

K

V

I

A

A

E

E

S

A

A

A

I

V

V

V

G

G

Y

I

P

P

H

H

D

A

I

I

K

K

G

G

N

Q

A

A

L

I

Y

Y

G

A

F

Y

V

V

I

T

L

L

K

N

E

H

T

-

G

G

E

E

G

E

R

P

D

S

K

P

E

E

N

-

L

L

K

Y

K

A

E

E

I

V

N

R

Q

N

L

W

I

V

S
x
R

D

K

Q

E

I

I

G

G

P

P

I

L

A

A

K

T

L

P

D

D

K

V

I

L

Q

H

F

W

V

T

S

D

G

S

L

L

P

P

K

K

T

T

R

R

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S

G

G

K
|
K

I

I

M

M

R

R

I

I

L

L

R

R

K

K

I

I

A

A

E

A

G

G

D

D

F

T

S

S

N

N

F

L

G

G

D

D

I

T

S

S

T

T

L

L

L

A

N

D

P

P

E

G

I

V

V

V

E

E

E

K

I

L

K

L

N

E

E

E

R

K

R194 (≠ K182) mutation to A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 3-fold reduction for CoA.; mutation to E: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 2-fold reduction for CoA.
T311 (= T297) binding CoA
N335 (≠ T321) binding CoA
A357 (= A343) mutation to V: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 3-fold reduction for CoA.
D517 (= D504) mutation to G: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 10-fold reduction for CoA.; mutation to P: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold reduction in the affinity for ATP and 4.5-fold reduction for CoA.
S523 (= S510) binding CoA
G524 (= G511) mutation to L: No acetyl-coenzyme A synthetase activity.; mutation to S: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. Almost the same affinity as the wild-type for ATP, but 9-fold reduction in the affinity for CoA.
R526 (≠ N513) mutation to A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 4-fold reduction for CoA.
R584 (≠ S573) binding CoA; mutation to A: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 2-fold increase in the affinity for ATP and 7-fold reduction for CoA.; mutation to E: Results in a 2-fold reduction in the catalytic efficiency for both ATP and CoA. 3-fold increase in the affinity for ATP and 8-fold reduction for CoA.
K609 (= K598) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.

2p20A Acetyl-coa synthetase, r584a mutation (see paper)
53% identity, 98% coverage: 11:634/636 of query aligns to 19:639/641 of 2p20A

query
sites
2p20A

H

Q

Y

Y

F

E

E

T

E

K

Y

Y

K

K

K

Q

S

S

I

I

K

N

N

D

P

P

K

D

K

T

F

F

W

W

D

G

-

E

-

Q

-

G

K

K

I

I

A

L

D

D

Q

-

N

-

F

-

V

-

W

W

Y

I

Q

T

R

P

W

Y

S

Q

K

K

V

V

-

K

-

N

V

T

K

S

Y

F

D

A

M

P

N

G

E

N

A

V

K

S

I

I

T

K

W

W

F

Y

K

E

N

D

A

G

K

T

L

L

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N

I

L

T

A

K

A

N

N

C

C

I

L

D

D

R

R

H

H

L

L

A

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V

E

R

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G

G

E

D

K

R

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T

A

A

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I

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W

E

E

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D

D

D

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-

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T

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E

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A

S

Q

K

H

H

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S

Y

Y

N

R

D

E

L

L

Y

H

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R

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V

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C

K

R

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F

A

A

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N

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T

L

L

R

L

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D

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L

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E

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G

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E

E

L

A

A

A

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A

M

M

L

L

A

A

C

C

A

A

K

R

L

I

G

G

A

A

V

V

H

H

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S

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V

I

I

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F

A

G

G

G

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F

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S

A

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E

A

A

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V

A

A

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I

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A

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A

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D

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Y

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G

A

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L

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L

L

K

K

S

K

I

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V

V

D

D

E

D

A

A

L

L

E

K

K

N

-

P

-

N

T

V

P

T

S

S

V

V

E

E

S

H

V

V

L

I

V

V

V

L

K

K

R

R

T

T

H

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E

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I

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K

Q

E

E

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G

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R

D

D

Y

L

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W

M

W

A

R

D

D

L

L

Y

I

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E

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K

A

A

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S

A

P

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E

F

H

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Q

T

P

V

E

I

A

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M

D

N

A

A

E

E

D

D

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P

L

L

F

F

I

I

L

L

Y

Y

T
|
T

S

S

G

G

S

S

T

T

G

G

K

K

P

P

K

K

G

G

M

V

L

L

H

H

T

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C

T

A

G

G

G

Y

Y

M

L

V

V

Y

Y

T

A

A

A

Y

T

T

T

F

F

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K

N

Y

V

V

F

F

N

D

Y

Y

K

H

E

P

N

G

D

D

I

I

Y

Y

W

W

C

C

T

T

A

A

D

D

I

V

G

G

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W

I

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T

G

G

H

H

S

S

Y

Y

I

L

L

L

Y

Y

G

G

P

P

L

L

L

A

N

C

G

G

A

A

T

T

V

L

I

M

F

F

E

E

G

G

V

V

P

P

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N

Y

W

P

P

E

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P

P

D

A

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F

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W

C

E

Q

V

V

I

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E

D

K

K

H

H

K

Q

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N

Q

I

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Y

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A

A

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P

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T

A

A

I

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A

L

L

A

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A

E

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E

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A

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I

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E

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D

L

R

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S

L

L

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R

V

I

I

L

G

G

S

S

V

V

G
|
G

E
|
E

P
|
P

I

I

N

N

E

P

E

E

A

A

W

W

H

E

W

W

F

Y

N

W

D

K

H

K

V

I

G

G

K

K

K

E

K

K

C

C

P

P

V

V

D

D

T
|
T

W
|
W

Q
|
Q

T
|
T

E
|
E

T

T

G

G

I

F

M

M

I

I

S

T

P

P

L

L

P

P

F

G

V

A

T

I

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E

T

L

K

K

P

A

T

G

Y

S

A

A

T

T

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R

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P

L

F

P

F

G

G

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V

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Q

P

P

V

A

L

L

M

V

D

D

D

N

K

E

R

G

N

H

E

P

I

Q

T

E

G

G

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-

Q

A

V

T

T

E

G

G

N

N

L

L

C

V

I

I

R

T

F

D

P

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P

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A

A

R

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T

I

L

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F

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G

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D

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H

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E

R

R

Y

F

K

E

E

Q

T

T

Y

Y

F

F

S

S

A

T

F

F

P

K

G

N

K

M

Y

Y

F

F

T

S

G

G

D
|
D

G

G

A

A

L

R

R

R

D

D

E

E

V

D

G

G

Y

Y

R

W

I
|
I

T

T

G

G

R
|
R

V

V

D

D

V

V

I

L

I
x
N

V

V

S

S

G

G

H

H

N
x
R

L

L

G

G

T

T

A

A

P

E

I

I

E

E

D

S

S

A

I

L

N

V

E

A

H

H

P

P

A

K

V

I

A

A

E

E

S

A

A

A

I

V

V

V

G

G

Y

I

P

P

H

H

D

A

I

I

K

K

G

G

N

Q

A

A

L

I

Y

Y

G

A

F

Y

V

V

I

T

L

L

K

N

E

H

T

-

G

G

E

E

G

E

R

P

D

S

K

P

E

E

N

-

L

L

K

Y

K

A

E

E

I

V

N

R

Q

N

L

W

I

V

S

A

D

K

Q

E

I

I

G

G

P

P

I

L

A

A

K

T

L

P

D

D

K

V

I

L

Q

H

F

W

V

T

S

D

G

S

L

L

P

P

K

K

T

T

R

R

S

S

G

G

K
|
K

I

I

M

M

R

R

I

I

L

L

R

R

K

K

I

I

A

A

E

A

G

G

D

D

F

T

S

S

N

N

F

-

G

-

D

D

I

T

S

S

T

T

L

L

L

A

N

D

P

P

E

G

I

V

V

V

E

E

E

K

I

L

K

L

N

E

E

E

R

K

active site: T260 (= T250), T412 (= T402), E413 (= E403), N517 (≠ I508), R522 (≠ N513), K605 (= K598)
binding adenosine-5'-monophosphate-propyl ester: G383 (= G373), E384 (= E374), P385 (= P375), T408 (= T398), W409 (= W399), W410 (= W400), Q411 (= Q401), T412 (= T402), D496 (= D487), I508 (= I499), R511 (= R502), R522 (≠ N513)

5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
53% identity, 98% coverage: 11:634/636 of query aligns to 19:638/640 of 5jrhA

query
sites
5jrhA

H

Q

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Y

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G

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I

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-

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-

L

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x
R

D

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G

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|
P

I

L

A

A

K

T

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D

D

K

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H

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D

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S

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L

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P

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K

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T

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K

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I

M

M

R

R

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I

L

L

R

R

K

K

I

I

A

A

E

A

G

G

D

D

F

-

S

-

N

-

F

L

G

G

D

D

I

T

S

S

T

T

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L

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N

D

P

P

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K

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E

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K

active site: T260 (= T250), T412 (= T402), E413 (= E403), N517 (≠ I508), R522 (≠ N513), K605 (= K598)
binding (r,r)-2,3-butanediol: W93 (= W84), E140 (= E132), G169 (≠ S161), K266 (= K256), P267 (= P257)
binding adenosine-3',5'-cyclic-monophosphate: G383 (= G373), E384 (= E374), P385 (= P375), T408 (= T398), W409 (= W399), W410 (= W400), Q411 (= Q401), T412 (= T402), D496 (= D487), I508 (= I499), N517 (≠ I508), R522 (≠ N513)
binding coenzyme a: F159 (= F151), G160 (≠ A152), G161 (= G153), R187 (= R179), S519 (= S510), R580 (≠ S573), P585 (= P578)
binding magnesium ion: V533 (≠ N524), H535 (= H526), I538 (≠ V529)

2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
53% identity, 98% coverage: 11:634/636 of query aligns to 18:635/637 of 2p2fA

query
sites
2p2fA

H

Q

Y

Y

F

E

E

T

E

K

Y

Y

K

K

K

Q

S

S

I

I

K

N

N

D

P

P

K

D

K

T

F

F

W

W

D

G

-

E

-

Q

-

G

K

K

I

I

A

L

D

D

Q

-

N

-

F

-

V

-

W

W

Y

I

Q

T

R

P

W

Y

S

Q

K

K

V

V

-

K

-

N

V

T

K

S

Y

F

D

A

M

P

N

G

E

N

A

V

K

S

I

I

T

K

W

W

F

Y

K

E

N

D

A

G

K

T

L

L

N

N

I

L

T

A

K

A

N

N

C

C

I

L

D

D

R

R

H

H

L

L

A

Q

V

E

R

N

G

G

E

D

K

R

T

T

A

A

I

I

W

W

E

E

P

G

N

D

D

D

P

-

K

T

E

S

E

Q

A

S

Q

K

H

H

I

I

S

S

Y

Y

N

R

D

E

L

L

Y

H

T

R

R

D

V

V

N

C

K

R

T

F

A

A

N

N

V

T

L

L

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E

D

M

L

G

G

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I

E

K

K

K

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G

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A

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M

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A

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L

A

A

C

C

A

A

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G

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A

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H

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S

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F

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G

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E

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K

A

A

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A

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M

D

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A

A

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E

D

D

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F

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I

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T

S

S

G

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T

T

G

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K

K

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K

G

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G

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G

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Y

M

L

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V

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A

A

A

Y

T

T

T

F

F

K

K

N

Y

V

V

F

F

N

D

Y

Y

K

H

E

P

N

G

D

D

I

I

Y

Y

W

W

C

C

T

T

A

A

D

D

I

V

G

G

W
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W

I

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T
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T

G

G

H

H

S

S

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Y

I

L

L

L

Y

Y

G

G

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P

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L

L

A

N

C

G

G

A

A

T

T

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M

F

F

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E

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W

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P

D

A

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M

W

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E

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A

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A
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A

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A

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A

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I

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E

A

A

W

W

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W

W

F

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D

K

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G

G

K

K

K

E

K

K

C

C

P

P

V

V

D

D

T
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T

W
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W

Q
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Q

T
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T

E
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E

T

T

G

G

I

F

M

M

I

I

S

T

P

P

L

L

P

P

F

G

V

A

T

I

P

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T

L

K

K

P

A

T

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A

A

T

T

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R

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P

L

F

P

F

G

G

I

V

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Q

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P

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A

L

L

M

V

D

D

D

N

K

E

R

G

N

H

E

P

I

Q

T

E

G

G

N

-

Q

A

V

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T

E

G

G

N

N

L

L

C

V

I

I

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T

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D

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S

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A

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F

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H

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F

K

E

E

Q

T

T

Y

Y

F

F

S

S

A

T

F

F

P

K

G

N

K

M

Y

Y

F

F

T

S

G

G

D
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D

G

G

A

A

L

R

R

R

D

D

E

E

V

D

G

G

Y

Y

R

W

I
|
I

T

T

G

G

R
|
R

V

V

D

D

V

V

I

L

I
x
N

V

V

S
|
S

G

G

H

H

N
x
R

L

L

G

G

T

T

A

A

P

E

I

I

E

E

D

S

S

A

I

L

N

V

E

A

H

H

P

P

A

K

V

I

A

A

E

E

S

A

A

A

I

V

V

V

G

G

Y

I

P

P

H

H

D

A

I

I

K

K

G

G

N

Q

A

A

L

I

Y

Y

G

A

F

Y

V

V

I

T

L

L

K

N

E

H

T

-

G

G

E

E

G

E

R

P

D

S

K

P

E

E

N

-

L

L

K

Y

K

A

E

E

I

V

N

R

Q

N

L

W

I

V

S
x
R

D

K

Q

E

I

I

G

G

P
|
P

I

L

A

A

K

T

L

P

D

D

K

V

I

L

Q

H

F

W

V

T

S

D

G

S

L

L

P

P

K

K

T

T

R

R

S

S

G

G

K
|
K

I

I

M

M

R

R

I

I

L

L

R

R

K

K

I

I

A

A

E

A

G

G

D

D

F

T

S

S

N

-

F

-

G

-

D

-

I

-

S

S

T

T

L

L

L

A

N

D

P

P

E

G

I

V

V

V

E

E

E

K

I

L

K

L

N

E

E

E

R

K

active site: T259 (= T250), T411 (= T402), E412 (= E403), N516 (≠ I508), R521 (≠ N513), K604 (= K598)
binding adenosine monophosphate: G382 (= G373), E383 (= E374), P384 (= P375), T407 (= T398), W408 (= W399), W409 (= W400), Q410 (= Q401), T411 (= T402), D495 (= D487), I507 (= I499), R510 (= R502), N516 (≠ I508), R521 (≠ N513)
binding coenzyme a: F158 (= F151), R186 (= R179), W304 (= W295), T306 (= T297), P329 (= P320), A352 (= A343), A355 (= A346), S518 (= S510), R579 (≠ S573), P584 (= P578)

1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
53% identity, 96% coverage: 11:622/636 of query aligns to 19:629/634 of 1pg3A

query
sites
1pg3A

H

Q

Y

Y

F

E

E

T

E

K

Y

Y

K

K

K

Q

S

S

I

I

K

N

N

D

P

P

K

D

K

T

F

F

W

W

D

G

-

E

-

Q

-

G

K

K

I

I

A

L

D

D

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-

N

-

F

-

V

-

W

W

Y

I

Q

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R

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W

Y

S

Q

K

K

V

V

-

K

-

N

V

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K

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A

M

P

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G

E

N

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I

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K

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W

F

Y

K

E

N

D

A

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N

I

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K

A

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N

C

C

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D

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G

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D

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-

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S

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Y

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A

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G

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x
G

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x
R

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K

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-

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N

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T

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A

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T

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A

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D

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A

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D

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G

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T

T

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R

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D

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I
x
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S

G

G

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H

N
x
R

L

L

G

G

T

T

A

A

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E

I

I

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S

S

A

I

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x
V

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A

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H

P

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A

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x
I

A

A

E

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A

A

A

I

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V

V

G

G

Y

I

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P

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H

D

A

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I

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K

G

G

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A

A

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Y

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A

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L

K

N

E

H

T

-

G

G

E

E

G

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D

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P

E

E

N

-

L

L

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A

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I

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S
x
R

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K

Q

E

I

I

G

G

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|
P

I

L

A

A

K

T

L

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D

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H

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W

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T

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D

G

S

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L

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P

K

K

T

T

R

R

S

S

G

G

K
|
K

I

I

M

M

R

R

I

I

L

L

R

R

K

K

I

I

A

A

E

A

G

G

D

D

F

L

S

A

N

D

F

P

G

G

D

V

I

V

S

E

T

K

L

L

active site: T260 (= T250), T412 (= T402), E413 (= E403), N517 (≠ I508), R522 (≠ N513), K605 (= K598)
binding coenzyme a: F159 (= F151), G160 (≠ A152), R187 (= R179), R190 (≠ K182), A301 (= A291), T307 (= T297), P330 (= P320), A356 (= A346), S519 (= S510), R580 (≠ S573), P585 (= P578)
binding magnesium ion: V533 (≠ N524), H535 (= H526), I538 (≠ V529)
binding adenosine-5'-monophosphate-propyl ester: G383 (= G373), E384 (= E374), P385 (= P375), T408 (= T398), W409 (= W399), W410 (= W400), Q411 (= Q401), T412 (= T402), D496 (= D487), R511 (= R502), R522 (≠ N513)

Q9NUB1 Acetyl-coenzyme A synthetase 2-like, mitochondrial; Acetate--CoA ligase 2; Acetyl-CoA synthetase 2; AceCS2; Acyl-CoA synthetase short-chain family member 1; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Homo sapiens (Human) (see 3 papers)
50% identity, 96% coverage: 18:630/636 of query aligns to 64:674/689 of Q9NUB1

query
sites
Q9NUB1

K

Q

S

A

I

A

K

R

N

E

P

P

K

A

F

F

W

W

D

G

K

P

I

L

A

A

D

R

Q

D

N

T

F

L

V

V

W

W

Y

D

Q

T

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W

Y

S

H

K

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V

W

K

D

Y

C

D

D

M

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A

G

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K

I

I

T

G

W

W

F

F

K

L

N

G

A

G

K

Q

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L

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N

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S

K

V

N

N

C

C

I

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D

R

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H

L

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A

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V

K

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P

E

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A

A

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W

E

E

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N

D

D

E

P

P

K

G

E

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E

E

A

V

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R

H

-

I

I

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T

Y

Y

N

R

D

E

L

L

Y

L

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E

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T

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C

K

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A

A

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N

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L

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G

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A

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P

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L

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I

A

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A

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L

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C