SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing GFF2177 FitnessBrowser__psRCH2:GFF2177 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)
37% identity, 98% coverage: 13:585/585 of query aligns to 48:632/648 of Q89WV5

query
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Q89WV5

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G263 (= G225) mutation to I: Loss of activity.
G266 (= G228) mutation to I: Great decrease in activity.
K269 (= K231) mutation to G: Great decrease in activity.
E414 (= E369) 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)
37% identity, 93% coverage: 44:585/585 of query aligns to 73:635/652 of P27550

query
sites
P27550

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K609 (= K561) modified: N6-acetyllysine; by autocatalysis

Q9QXG4 Acetyl-coenzyme A synthetase, cytoplasmic; Acetate--CoA ligase; Acetyl-CoA synthetase; ACS; AceCS; Acetyl-CoA synthetase 1; AceCS1; Acyl-CoA synthetase short-chain family member 2; Acyl-activating enzyme; Propionate--CoA ligase; EC 6.2.1.1; EC 6.2.1.17 from Mus musculus (Mouse) (see paper)
37% identity, 93% coverage: 41:585/585 of query aligns to 96:686/701 of Q9QXG4

query
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Q9QXG4

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L

L

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K661 (= K561) modified: N6-acetyllysine

2p20A Acetyl-coa synthetase, r584a mutation (see paper)
36% identity, 93% coverage: 44:585/585 of query aligns to 69:629/641 of 2p20A

query
sites
2p20A

G

G

G

T

L

L

N

N

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L

A

A

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G

G

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|
K

L

I

M

M

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L

L

K

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A

K

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A

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A

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G

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N

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active site: T260 (= T223), T412 (= T368), E413 (= E369), N517 (≠ K473), R522 (≠ L478), K605 (= K561)
binding adenosine-5'-monophosphate-propyl ester: V306 (= V268), T307 (= T269), G383 (= G342), E384 (= E343), P385 (= P344), D407 (= D363), T408 (≠ N364), W409 (= W365), W410 (= W366), Q411 (= Q367), T412 (= T368), D496 (= D452), I508 (≠ F464), R511 (= R467), N517 (≠ K473), R522 (≠ L478)

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)
36% identity, 93% coverage: 44:585/585 of query aligns to 73:635/652 of Q8ZKF6

query
sites
Q8ZKF6

G

G

G

T

L

L

N

N

L

L

A

A

H

A

E

N

A

C

V

L

D

D

R

R

H

H

A

L

A

Q

G

E

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N

R

G

A

D

G

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Y

T

C

A

A

I

L

I

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W

F

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D

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D

N

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Y

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N

C

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F

F

A

A

N

N

V

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L

L

A

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G

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D

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S

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L

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|
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N

V

I

W

L

Y

Y

T

T

A
|
A

P

P

T

T

A

A

I

I

R

R

M

A

L

L

M

M

K

A

A

E

G

G

P

D

E

K

L

A

A

I

R

E

R

G

H

T

F

D

H

R

P

S

Q

S

L

L

R

R

F

I

V

L

A

G

S

S

V

V

G

G

E

E

P

P

L

I

N

N

P

P

E

E

A

A

V

W

W

E

W

W

G

Y

K

W

E

K

V

K

L

I

G

G

-

K

-

E

-

K

L

C

P

P

I

V

H

V

D

D

N

T

W

W

Q

Q

T

T

E

E

T

T

G

G

I

F

M

M

I

I

A

T

N

P

I

L

P

P

-

G

A

A

M

I

P

E

I

L

K

K

P

A

G

G

S

S

M

A

G

T

K

R

P

P

L

F

P

F

G

G

V

V

E

Q

A

P

A

A

I

L

V

V

R

D

-

N

-

E

-

G

H

H

G

P

E

Q

D

E

G

G

N

A

L

T

T

E

F

-

L

-

G

-

D

-

E

-

I

-

G

G

E

N

L

L

A

V

L

I

K

T

Q

D

P

S

W

W

P

P

G

G

M

Q

F

A

R

R

T

T

Y

L

L

F

G

G

Q

D

E

H

E

E

R

R

Y

F

R

E

R

Q

C

T

F

Y

A

F

G

S

-

T

-

F

-

K

D

N

W

M

Y

Y

L

F

S

S

G

G

D

D

L

G

A

A

R

R

D

D

A

E

D

D

G

G

Y

Y

W

W

F

I

I

T

G

G

R

R

S

V

D
|
D

D

D

V

V

I

L

K

N

S

V

A
x
S

G
|
G

H

H

L
x
R

I

L

G

G

P

T

F

A

E

E

V

I

E

E

S

S

A

A

L

L

M

V

E

A

H

H

S

P

A

K

V

I

A

A

E

E

A

A

V

V

I

V

G

G

K

I

P

P

D

H

P

A

L

I

L

K

G

G

E

Q

T

A

V

I

K

Y

A

A

F

Y

V

V

S

T

L

L

K

N

R

H

G

G

R

E

E

E

A

P

S

S

E

P

A

E

L

L

H

Y

D

A

E

E

L

V

I

R

G

N

H

W

A

V

R
|
R

K

K

R

E

L

I

G

G

A

P

A

L

V

A

A

T

P

P

K

D

E

V

L

L

E

H

F

W

L

T

A

D

S

S

L

L

P

P

R

K

T

T

R

R

S

S

G

G

K
|
K

L

I

M

M

R

R

L

I

L

L

K

R

A

K

R

I

E

A

L

A

G

G

L

D

P

T

E

S

-

N

-

L

G

G

D

D

I

T

S

S

T

T

L

L

E

A

N

D

P

P

R194 (vs. gap) 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 (= T269) binding
N335 (≠ D293) binding
A357 (= A312) 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 (= D469) 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 (≠ A475) binding
G524 (= G476) 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 (≠ L478) 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 (= R536) 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 (= K561) modified: N6-acetyllysine; by Pat; mutation to A: No acetyl-coenzyme A synthetase activity.

5jrhA Crystal structure of salmonella enterica acetyl-coa synthetase (acs) in complex with camp and coenzyme a (see paper)
37% identity, 93% coverage: 44:585/585 of query aligns to 69:628/640 of 5jrhA

query
sites
5jrhA

G

G

G

T

L

L

N

N

L

L

A

A

H

A

E

N

A

C

V

L

D

D

R

R

H

H

A

L

A

Q

G

E

P

N

R

G

A

D

G

R

Y

T

C

A

A

I

L

I

R
x
W

F

E

L

G

E

D

R

D

N

T

G

S

S

Q

R

S

R
x
K

E

H

L

I

S

S

Y

Y

L

R

Q

E

L

L

K

H

R

R

Q

D

T

V

N

C

R

R

F

F

A

A

N

N

V

T

L

L

A

L

Q

D

L

L

G

G

V

I

A

K

R

K

G

G

E

D

R

V

L

V

F

A

V

I

L

Y

C

M

N

P

R

M

G
x
V

V

P

E
|
E

L

A

Y

A

L

V

G

A

V

M

L

L

G

A

G

C

L

A

K

R

N

I

G

G

C

A

V

V

V

H

S

S

P

V

L

I

F
|
F

A
x
G

F

F

G

S

P

P

E

E

P

A

L

V

E

A

T
x
G

R
|
R

L

I

R

I

L

D

G

S

D

S

C

S

S

R

V

L

L

V

L

I

T

T

S

A

E

D

-

E

-

G

-

V

-
x
R

-

A

-

G

-

R

-

S

M
x
I

L

P

Y

L

R

K

K

K

K

N

V

V

-

D

A

A

R

L

L

K

R

N

D

P

R

N

L

V

P

T

L

S

L

V

K

E

H

H

V

V

L

I

L

V

Y
x
L

D

K

E
x
R

S

T

G

G

G

S

H

D

T

I

S

D

I

W

D

Q

G

E

T

G

L

R

D

D

L

L

-

W

H

R

D

D

L

L

L

I

A

E

A

K

A

A

G

S

E

P

E

E

F

H

K

Q

I

P

A

E

P

A

T

M

T

N

A

A

D

E

S

D

P

P

S

L

L

F

L

I

H

L

F
x
Y

T
|
T

S

S

G

G

T

S

T

T

G

G

T
x
K

P
|
P

K

K

G

G

A

V

L

L

H

H

V

T

H

T

G

G

A

G

A

Y

L

L

T

V

H

Y

Y

A

V

A

T

T

G

T

-

F

R

K

Y

Y

A

V

L

F

D

D

L

Y

H

H

P

P

D

G

D

D

I

I

Y

Y

W

W

C

C

S

T

A

A

D
|
D

P

V

G

G

W

W

V

V

T

T

G

G

T

H

S

S

Y

Y

G

L

I

L

L

Y

A

G

P

P

L

L

L

A

L

C

G

G

V

A

T

T

S

T

V

L

V

M

D

F

C

E

G

G

E

V

F

P

D

N

-

W

-

P

-

T

A

P

E

A

R

R

W

M

Y

C

G

Q

I

V

L

V

E

D

K

K

E

H

R

Q

I

V

S

N

V

I

W

L

Y

Y

T

T

A

A

P

P

T

T

A

A

I

I

R

R

M

A

L

L

M

M

K

A

A

E

G

G

P

D

E

K

L

A

A

I

R

E

R

G

H

T

F

D

H

R

P

S

Q

S

L

L

R

R

F

I

V

L

A

G

S

S

V

V

G
|
G

E
|
E

P
|
P

L

I

N

N

P

P

E

E

A

A

V

W

W

E

W

W

G

Y

K

W

E

K

V

K

L

I

G

G

-

K

-

E

-

K

L

C

P

P

I

V

H

V

D
|
D

N
x
T

W
|
W

Q
|
Q

T
|
T

E
|
E

T

T

G

G

I

F

M

M

I

I

A

T

N

P

I

L

P

P

-

G

A

A

M

I

P

E

I

L

K

K

P

A

G

G

S

S

M

A

G

T

K

R

P

P

L

F

P

F

G

G

V

V

E

Q

A

P

A

A

I

L

V

V

R

D

-

N

-

E

-

G

H

H

G

P

E

Q

D

E

G

G

N

A

L

T

T

E

F

-

L

-

G

-

D

-

E

-

I

-

G

G

E

N

L

L

A

V

L

I

K

T

Q

D

P

S

W

W

P

P

G

G

M

Q

F

A

R

R

T

T

Y

L

L

F

G

G

Q

D

E

H

E

E

R

R

Y

F

R

E

R

Q

C

T

F

Y

A

F

G

S

-

T

-

F

-

K

D

N

W

M

Y

Y

L

F

S

S

G

G

D
|
D

L

G

A

A

R

R

D

D

A

E

D

D

G

G

Y

Y

W

W

F
x
I

I

T

G

G

R
|
R

S

V

D

D

V

V

I

L

K
x
N

S

V

A
x
S

G

G

H
|
H

L
x
R

I

L

G

G

P

T

F

A

E

E

V

I

E

E

S

S

A

A

L

L

M
x
V

E

A

H
|
H

S

P

A

K

V
x
I

A

A

E

E

A

A

V

V

I

V

G

G

K

I

P

P

D

H

P

A

L

I

L

K

G

G

E

Q

T

A

V

I

K

Y

A

A

F

Y

V

V

S

T

L

L

K

N

R

H

G

G

R

E

E

E

A

P

S

S

E

P

A

E

L

L

H

Y

D

A

E

E

L

V

I

R

G

N

H

W

A

V

R
|
R

K

K

R

E

L

I

G

G

A
x
P

A

L

V

A

A

T

P

P

K

D

E

V

L

L

E

H

F

W

L

T

A

D

S

S

L

L

P

P

R

K

T

T

R

R

S

S

G

G

K
|
K

L

I

M

M

R

R

L

I

L

L

K

R

A

K

R

I

E

A

L

A

G

G

L

-

P

D

E

L

G

G

D

D

I

T

S

S

T

T

L

L

E

A

N

D

P

P

active site: T260 (= T223), T412 (= T368), E413 (= E369), N517 (≠ K473), R522 (≠ L478), K605 (= K561)
binding (r,r)-2,3-butanediol: W93 (≠ R68), K102 (≠ R77), V138 (≠ G113), E140 (= E115), G169 (≠ T144), R170 (= R145), L216 (≠ Y181), R218 (≠ E183), Y259 (≠ F222), K266 (≠ T229), P267 (= P230)
binding adenosine-3',5'-cyclic-monophosphate: G383 (= G342), E384 (= E343), P385 (= P344), D407 (= D363), T408 (≠ N364), W409 (= W365), W410 (= W366), Q411 (= Q367), T412 (= T368), D496 (= D452), I508 (≠ F464), R511 (= R467), N517 (≠ K473), R522 (≠ L478)
binding coenzyme a: F159 (= F134), G160 (≠ A135), G161 (≠ A136), R187 (vs. gap), I192 (≠ M159), D302 (= D264), S519 (≠ A475), H521 (= H477), R580 (= R536), P585 (≠ A541)
binding magnesium ion: V533 (≠ M489), H535 (= H491), I538 (≠ V494)

2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
36% identity, 93% coverage: 44:585/585 of query aligns to 68:625/637 of 2p2fA

query
sites
2p2fA

G

G

G

T

L

L

N

N

L

L

A

A

H

A

E

N

A

C

V

L

D

D

R

R

H

H

A

L

A

Q

G

E

P

N

R

G

A

D

G

R

Y

T

C

A

A

I

L

I

R

W

F

E

L

G

E

D

R

D

N

T

G

S

S

Q

R

S

R

K

E

H

L

I

S

S

Y

Y

L

R

Q

E

L

L

K

H

R

R

Q

D

T

V

N

C

R

R

F

F

A

A

N

N

V

T

L

L

A

L

Q

D

L

L

G

G

V

I

A

K

R

K

G

G

E

D

R

V

L

V

F

A

V

I

L

Y

C

M

N

P

R

M

G

V

V

P

E

E

L

A

Y

A

L

V

G

A

V

M

L

L

G

A

G

C

L

A

K

R

N

I

G

G

C

A

V

V

V

H

S

S

P

V

L

I

F
|
F

A
x
G

F

F

G

S

P

P

E

E

P

A

L

V

E

A

T

G

R

R

L

I

R

I

L

D

G

S

D

S

C

S

S

R

V

L

L

V

L

I

T

T

S

A

E

D

-

E

-

G

-

V

-
x
R

-

A

-

G

-

R

-

S

M
x
I

L

P

Y

L

R

K

K

K

K

N

V

V

-

D

A

A

R

L

L

K

R

N

D

P

R

N

L

V

P

T

L

S

L

V

K

E

H

H

V

V

L

I

L

V

Y

L

D

K

E

R

S

T

G

G

G

S

H

D

T

I

S

D

I

W

D

Q

G

E

T

G

L

R

D

D

L

L

-

W

H

R

D

D

L

L

L

I

A

E

A

K

A

A

G

S

E

P

E

E

F

H

K

Q

I

P

A

E

P

A

T

M

T

N

A

A

D

E

S

D

P

P

S

L

L

F

L

I

H

L

F

Y

T
|
T

S

S

G

G

T

S

T

T

G

G

T

K

P

P

K

K

G

G

A

V

L

L

H

H

V

T

H

T

G

G

A

G

A

Y

L

L

T

V

H

Y

Y

A

V

A

T

T

G

T

-

F

R

K

Y

Y

A

V

L

F

D

D

L

Y

H

H

P

P

D

G

D

D

I

I

Y

Y

W

W

C

C

S

T

A
|
A

D

D

P

V

G

G

W
|
W

V

V

T
|
T

G

G

T

H

S

S

Y

Y

G

L

I

L

L

Y

A

G

P

P

L

L

L

A

L

C

G

G

V

A

T

T

S

T

V

L

V

M

D

F

C

E

G

G

E
x
V

F
x
P

D

N

-

W

-

P

-

T

A

P

E

A

R

R

W

M

Y

C

G

Q

I

V

L

V

E

D

K

K

E

H

R

Q

I

V

S

N

V

I

W

L

Y

Y

T

T

A
|
A

P

P

T
|
T

A
|
A

I

I

R

R

M

A

L

L

M

M

K

A

A

E

G

G

P

D

E

K

L

A

A

I

R

E

R

G

H

T

F

D

H

R

P

S

Q

S

L

L

R

R

F

I

V

L

A

G

S

S

V

V

G
|
G

E
|
E

P
|
P

L

I

N

N

P

P

E

E

A

A

V

W

W

E

W

W

G

Y

K

W

E

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E

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active site: T259 (= T223), T411 (= T368), E412 (= E369), N516 (≠ K473), R521 (≠ L478), K604 (= K561)
binding adenosine monophosphate: G382 (= G342), E383 (= E343), P384 (= P344), D406 (= D363), T407 (≠ N364), W408 (= W365), W409 (= W366), Q410 (= Q367), T411 (= T368), D495 (= D452), I507 (≠ F464), R510 (= R467), N516 (≠ K473), R521 (≠ L478)
binding coenzyme a: F158 (= F134), G159 (≠ A135), G160 (≠ A136), R186 (vs. gap), I191 (≠ M159), A300 (= A263), W304 (= W267), T306 (= T269), V328 (≠ E291), P329 (≠ F292), A352 (= A312), T354 (= T314), A355 (= A315), S518 (≠ A475), G519 (= G476), R579 (= R536), P584 (≠ A541)

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)
37% identity, 93% coverage: 43:585/585 of query aligns to 70:641/651 of P9WQD1

query
sites
P9WQD1

G

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L

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A

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A

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