SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing H281DRAFT_04953 H281DRAFT_04953 acetyl-coenzyme A synthetase 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)

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)
51% identity, 95% coverage: 32:658/660 of query aligns to 24:643/652 of P27550

query
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P27550

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K609 (= K625) modified: N6-acetyllysine; by autocatalysis

2p20A Acetyl-coa synthetase, r584a mutation (see paper)
50% identity, 95% coverage: 30:658/660 of query aligns to 18:637/641 of 2p20A

query
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2p20A

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active site: T260 (= T270), T412 (= T426), E413 (= E427), N517 (= N534), R522 (= R539), K605 (= K625)
binding adenosine-5'-monophosphate-propyl ester: V306 (≠ I316), T307 (= T317), G383 (= G397), E384 (= E398), P385 (= P399), D407 (= D421), T408 (= T422), W409 (= W423), W410 (= W424), Q411 (= Q425), T412 (= T426), D496 (= D512), I508 (= I525), R511 (= R528), N517 (= N534), R522 (= R539)

P9WQD1 Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
52% identity, 99% coverage: 5:656/660 of query aligns to 3:647/651 of P9WQD1

query
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P9WQD1

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K
|
K

I

I

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M

R

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L

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I

K617 (= K625) modified: N6-acetyllysine; mutation to R: Complete loss of acetyl-coenzyme A synthetase activity.

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)
50% identity, 95% coverage: 30:658/660 of query aligns to 22:643/652 of Q8ZKF6

query
sites
Q8ZKF6

D

E

A

Q

Y

Y

H

E

A

T

L

K

T

Y

A

K

E

Q

A

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x
R

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K

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L

L

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K

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A

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A

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G

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L

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G

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E

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K

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E

R194 (≠ K200) 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 (= T317) binding
N335 (≠ T341) binding
A357 (= A363) 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 (= D530) 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 (= S536) binding
G524 (= G537) 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 (= R539) 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 (≠ G600) binding ; 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 (= K625) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.

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)
52% identity, 95% coverage: 32:656/660 of query aligns to 23:638/648 of Q89WV5

query
sites
Q89WV5

Y

Y

H

K

A

E

L

M

T

Y

A

A

E

R

A

S

E

I

R

S

D

D

Y

P

E

N

G

G

F

F

W

W

G

A

R

E

L

Q

A

A

R

K

E

R

T

-

L

I

S

D

W

W

N

M

K

K

P

A

F

P

T

T

K

K

V

I

L

E

D

N

E

V

S

S

K

F

A

A

P

P

-

G

-

N

-

V

F

S

Y

I

T

K

W

W

F

F

E

E

D

D

G

G

Q

V

L

L

N

N

A

V

S

A

Y

H

N

N

S

C

I

I

D

D

R

R

H

H

V

L

E

H

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R

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A

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A

A

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F

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E

E

A

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G

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V

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T

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-

R

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E

L

L

L

H

Q

D

R

E

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C

R

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F

M

A

A

N

N

A

I

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K

R

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T

R

R

G

N

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K

G

G

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D

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R

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V

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G

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F

F

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A

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A

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L

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G

A

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-

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A

A

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T

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G

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G

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K

G

G

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K

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C

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A

A

D

D

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G

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W

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T

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G

H

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S

S

Y

Y

I

I

T

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Y

Y

G

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L

N

G

G

G

A

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T

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T

V

L

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M

F

F

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E

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G

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P

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T

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Y

Y

P

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D

A

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W

W

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D

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F

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-

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-

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R

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G

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G

E

E

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N

P

P

E

E

A

A

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V

G

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C

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P

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A

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D

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A

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D

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P

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A

R

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E

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Y

Y

F

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P

S

E

T

E

Y

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K

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G

G

K

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-

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-

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F

A

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G

G

D

D

G

G

A

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V

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R

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D

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A

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-

G

G

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Y

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Y

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I

I

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T

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G

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R

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D

D

V

V

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I

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V

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S

G

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G

G

T

T

M

A

E

E

I

V

E

E

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S

A

A

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L

V

V

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A

N

H

P

E

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K

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E

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P

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D

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A

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T

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A

G

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Y

A

A

F

Y

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V

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T

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L

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M

R

A

A

G

R

V

P

Q

E

P

G

T

E

E

E

D

A

-

V

-

K

-

L

L

A

R

N

K

E

E

L

L

R

V

N

T

W

W

V

V

G

R

K

K

E

E

I

I

G

G

P

P

I

I

A

A

K

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P

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K

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D

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I

R

Q

F

F

G

A

E

P

N

G

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L

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P

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K

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T

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S

G

G

K

K

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M

R

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L

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S

K

L

I

A

A

K

E

G

D

E

E

E

P

I

G

T

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Q

L

-

G

D

D

V

T

S

S

T

T

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A

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Q

D

L

L

G263 (= G272) mutation to I: Loss of activity.
G266 (= G275) mutation to I: Great decrease in activity.
K269 (= K278) mutation to G: Great decrease in activity.
E414 (= E427) mutation to Q: Great decrease in activity.

5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
50% identity, 95% coverage: 30:658/660 of query aligns to 18:636/640 of 5jrhA

query
sites
5jrhA

D

E

A

Q

Y

Y

H

E

A

T

L

K

T

Y

A

K

E

Q

A

S

E

I

R

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D

D

Y

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E

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G

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L

Q

A

G

R

K

E

-

T

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L

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D

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W

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T

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P

F

Y

T

Q

K

K

V

V

L

K

D

N

E

T

S

S

K

F

A

A

P

P

-

G

-

N

-

V

F

S

Y

I

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K

W

W

F

Y

E

E

D

D

G

G

Q

T

L

L

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N

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A

Y

A

N

N

S

C

I

L

D

D

R

R

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Q

A

E

G

-

N

N

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G

E

D

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R

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T

A

A

I

I

F
x
W

E

E

A

G

D

D

G

T

T

S

V

Q

T

S

-
x
K

N

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Y

Q

R

D

E

L

L

L

H

Q

R

R

D

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C

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R

F

F

A

A

N

N

A

T

L

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K

L

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G

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K

G

G

D

D

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V

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Y

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M

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P

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S
x
V

I

P

E
|
E

G

A

I

A

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V

A

A

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M

Q

L

A

A

C

C

A

A

R

R

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I

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G

A

A

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S

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V

V

I

F
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F

G
|
G

F

F

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S

A

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A

E
x
G

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R

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R

G

A

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x
I

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N

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R

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A

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A

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T
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T

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S

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G

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G

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K

P
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P

K

K

G

G

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T

T

G

G

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Y

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A

A

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D

I

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G

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D

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A

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-

A

-

A

A

E

E

A

G

D

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A

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K

A

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I

I

L

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G

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E
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E

P
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P

I

I

N

N

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P

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E

A

A

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T
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E
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E

T

T

G

G

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G

A

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G

G

A

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R

R

D

D

K

E

D

D

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-

G

G

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I
|
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M

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G

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R
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R

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D

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|
N

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S
|
S

G

G

H
|
H

R
|
R

L

L

G

G

T

T

M

A

E

E

I

I

E

E

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S

A

A

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S

A

N
x
H

P

P

I

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V
x
I

A

A

E

E

A

A

V

V

G

G

R

I

P

P

D

H

A

A

T

I

T

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G

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A

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C

Y

A

A

F

Y

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V

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T

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L

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N

R

H

A

G

R

E

P

-

E

-

G

-

E

E

E

P

A

S

V

P

K

E

L

L

A

Y

N

A

E

E

L

V

R

R

N

N

W

W

V

V

G
x
R

K

K

E

E

I

I

G

G

P
|
P

I

L

A

A

K

T

P

P

K

D

D

V

I

L

R

H

F

W

G

T

E

D

N

S

L

L

P

P

K

K

T

T

R

R

S

S

G

G

K
|
K

I

I

M

M

R

R

L

I

L

L

R

R

S

K

L

I

A

A

K

A

G

G

E

D

E

-

I

-

T

L

Q

G

D

D

V

T

S

S

T

T

L

L

E

A

N

D

P

P

A

G

I

V

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V

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E

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K

L

L

G

L

E

E

active site: T260 (= T270), T412 (= T426), E413 (= E427), N517 (= N534), R522 (= R539), K605 (= K625)
binding (r,r)-2,3-butanediol: W93 (≠ F104), K102 (vs. gap), V138 (≠ S148), E140 (= E150), G169 (≠ E179), R170 (= R180), L216 (≠ Y226), R218 (= R228), Y259 (= Y269), K266 (= K276), P267 (= P277)
binding adenosine-3',5'-cyclic-monophosphate: G383 (= G397), E384 (= E398), P385 (= P399), D407 (= D421), T408 (= T422), W409 (= W423), W410 (= W424), Q411 (= Q425), T412 (= T426), D496 (= D512), I508 (= I525), R511 (= R528), N517 (= N534), R522 (= R539)
binding coenzyme a: F159 (= F169), G160 (= G170), G161 (= G171), R187 (= R197), I192 (≠ L202), D302 (= D312), S519 (= S536), H521 (= H538), R580 (≠ G600), P585 (= P605)
binding magnesium ion: V533 (= V550), H535 (≠ N552), I538 (≠ V555)

2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
50% identity, 95% coverage: 30:658/660 of query aligns to 17:633/637 of 2p2fA

query
sites
2p2fA

D

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A

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Y

H

E

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x
R

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K

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E

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|
P

I

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A

A

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T

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K

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M

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L

L

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R

S

K

L

I

A

A

K

A

G

G

E

D

E

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I

-

T

-

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-

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E

active site: T259 (= T270), T411 (= T426), E412 (= E427), N516 (= N534), R521 (= R539), K604 (= K625)
binding adenosine monophosphate: G382 (= G397), E383 (= E398), P384 (= P399), D406 (= D421), T407 (= T422), W408 (= W423), W409 (= W424), Q410 (= Q425), T411 (= T426), D495 (= D512), I507 (= I525), R510 (= R528), N516 (= N534), R521 (= R539)
binding coenzyme a: F158 (= F169), G159 (= G170), G160 (= G171), R186 (= R197), I191 (≠ L202), A300 (= A311), W304 (= W315), T306 (= T317), V328 (= V339), P329 (= P340), A352 (= A363), T354 (= T365), A355 (= A366), S518 (= S536), G519 (= G537), R579 (≠ G600), P584 (= P605)

1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
50% identity, 95% coverage: 30:658/660 of query aligns to 18:630/634 of 1pg3A

query
sites
1pg3A

D

E

A

Q

Y

Y

H

E

A

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A

K

E

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A

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I

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N

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D

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D

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F

W

W

G

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A

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W

N

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Y

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K

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V

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K

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N

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S

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A

A

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-

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-

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-

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Y

I

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W

F

Y

E

E

D

D

G

G

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T

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L

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N

A

L

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A

Y

A

N

N

S

C

I

L

D

D

R

R

H

H

V

L

E

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A

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N

N

G

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A

A

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I

F

W

E

E

A

G

D

D

G

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N

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Y

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D

E