SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 8502070 FitnessBrowser__Miya:8502070 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)

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)
49% identity, 94% coverage: 36:648/651 of query aligns to 24:640/651 of P9WQD1

query
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P9WQD1

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K617 (= K625) modified: N6-acetyllysine; mutation to R: Complete loss of 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)
45% identity, 98% coverage: 14:648/651 of query aligns to 2:631/648 of Q89WV5

query
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Q89WV5

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G263 (= G277) mutation to I: Loss of activity.
G266 (= G280) mutation to I: Great decrease in activity.
K269 (= K283) mutation to G: Great decrease in activity.
E414 (= E428) 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)
44% identity, 95% coverage: 28:648/651 of query aligns to 13:627/640 of 5jrhA

query
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5jrhA

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E

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L

L

E

D

W

W

F

I

R

T

R

P

W

Y

D

Q

A

K

V

V

H

K

D

N

G

T

S

S

N

F

A

A

P

P

F

G

H

N

-

V

-

S

-

I

R

K

W

W

F

Y

T

E

G

D

A

G

R

T

C

L

N

N

I

L

V

A

H

A

N

N

A

C

L

L

D

D

R

R

H

H

I

L

E

Q

T

E

G

-

T

N

K

G

N

D

R

R

L

T

A

A

L

I

I

I

W
|
W

E

E

G

G

E

D

-

D

S

T

G

S

D

Q

T

S

R
x
K

S

H

F

I

T

S

Y

Y

Y

R

Q

E

L

L

Y

H

R

R

E

D

V

V

N

C

R

R

L

F

A

A

N

N

A

T

L

L

R

L

G

D

L

L

G

G

V

I

G

K

K

K

G

G

D

D

R

V

V

V

I

A

I

I

Y

Y

M

M

P

P

P

M

L
x
V

P

P

E
|
E

T

A

V

A

F

V

A

A

M

M

L

L

A

A

A

C

A

A

K

R

I

I

G

G

A

A

V

V

H

H

S

S

T

V

V

I

F
|
F

G
|
G

F

F

S

S

A

P

R

E

S

A

L

V

R

A

D
x
G

R
|
R

M

I

E

I

D

D

A

S

R

S

P

S

A

R

V

L

I

V

V

I

T

T

V

A

D

D

G

E

F

G

Y

V

R
|
R

N

A

G

G

R

R

V

S

I
|
I

P

P

L

L

K

K

P

K

I

N

A

V

D

D

E

D

A

A

V

L

A

K

T

N

L

-

P

-

P

P

D

N

L

V

A

T

A

S

G

-

V

V

R

E

H

H

M

V

V

I

V

V

V
x
L

H

K

R
|
R

A

T

H

G

V

S

E

D

T

I

P

D

M

W

T

Q

E

E

G

G

R

R

D

D

I

L

W

W

Y

W

H

R

D

D

A

L

V

I

R

E

G

K

Q

A

H

S

H

P

E

E

A

H

L

Q

T

P

E

E

I

A

M

M

D

N

S

A

T

E

D

D

P

P

L

L

F

F

L

I

L

L

Y
|
Y

T
|
T

S

S

G

G

T

S

T

T

G

G

K
|
K

P
|
P

K

K

G

G

H

V

V

L

H

H

A

T

H

T

G

G

Y

Y

M

L

V

V

G

Y

V

A

H

A

R

T

T

T

M

F

R

K

W

Y

V

V

F

F

D

D

V

Y

K

H

P

P

T

G

D

D

I

I

F

Y

W

W

C

C

T

T

A

A

E
x
D

P

V

G

G

W

W

I

V

T

T

G

G

H

H

S

S

Y

Y

V

L

Y

Y

G

G

P

P

L

L

M

A

A

C

G

G

T

A

T

T

V

L

L

M

Y

F

E

E

G

G

H

V

P

P

L

N

Y

W

P

P

E

T

P

P

G

A

R

R

V

M

W

C

S

Q

M

V

V

V

E

D

R

K

L

H

G

Q

I

V

T

N

I

I

L

L

Y

Y

T

T

A

A

P

P

T

T

L

A

V

I

R

R

M

A

L

L

M

M

R

A

H

E

G

G

A

D

Q

K

H

A

V

I

A

E

R

G

H

T

D

D

L

R

T

S

L

L

R

R

L

I

L

L

G

G

T

S

V

V

G
|
G

E
|
E

P
|
P

I

I

S

N

P

P

E

E

A

A

W

W

L

E

W

W

F

Y

H

W

R

K

H

K

V

I

G

G

R

K

G

E

R

K

C

C

P

P

V

V

L

V

D
|
D

T
|
T

W
|
W

Q
|
Q

T
|
T

E
|
E

T

T

G

G

M

G

I

F

M

M

L

I

S

T

P

P

L

L

P

P

V

G

S

A

L

I

-

E

L

L

K

K

P

A

G

G

S

S

V

A

T

T

R

R

P

P

L

F

P

F

G

G

I

V

E

Q

A

P

D

A

V

L

V

V

D

D

E

N

H

E

G

G

K

H

P

P

V

Q

G

E

P

G

G

A

H

T

G

E

G

G

L

N

L

L

V

V

L

I

Q

T

R

D

P

S

W

W

P

P

A

G

M

Q

S

A

C

R

G

T

V

L

Y

F

N

G

D

D

D

H

E

E

S

R

Y

F

R

E

R

Q

L

T

Y

Y

W

F

E

S

R

T

F

F

P

K

G

N

W

M

Y

Y

C

F

T

S

G

G

D
|
D

V

G

A

A

R

R

D

D

E

E

D

D

G

G

Y

Y

F

Y

W

W

I
|
I

Q

T

G

G

R
|
R

A

V

D

D

V

V

L

L

L
x
N

I

V

A
x
S

G

G

H
|
H

R
|
R

I

L

G

G

T

T

A

A

E

E

M

I

E

E

A

S

A

A

L

L

A
x
V

S

A

H
|
H

R

P

S

K

V
x
I

A

A

E

E

C

A

A

A

V

V

I

V

G

G

V

I

P

P

D

H

A

A

L

I

R

K

G

G

E

Q

V

A

A

I

K

Y

A

A

F

Y

V

V

V

T

L

L

V

N

D

H

D

G

H

E

P

E

P

P

L

-

G

-

T

-

M

-

V

-

N

-

A

S

D

P

E

E

L

L

A

Y

A

A

E

E

L

V

V

R

E

N

H

W

V

V

R
|
R

R

K

E

E

L

I

G

G

P
|
P

V

L

A

A

V

T

I

P

R

D

E

V

V

L

S

H

F

W

R

T

E

D

G

S

L

L

P

P

R

K

N

T

R

R

S

S

G

G

K
|
K

I

I

M

M

R

R

V

I

L

L

R

R

S

K

E

I

E

A

L

A

G

G

R

-

D

D

T

L

G

G

D

D

L

T

S

S

T

T

L

L

E

A

D

D

active site: T260 (= T275), T412 (= T427), E413 (= E428), N517 (≠ L531), R522 (= R536), K605 (= K625)
binding (r,r)-2,3-butanediol: W93 (= W106), K102 (≠ R114), V138 (≠ L150), E140 (= E152), G169 (≠ D181), R170 (= R182), L216 (≠ V231), R218 (= R233), Y259 (= Y274), K266 (= K281), P267 (= P282)
binding adenosine-3',5'-cyclic-monophosphate: G383 (= G398), E384 (= E399), P385 (= P400), D407 (= D422), T408 (= T423), W409 (= W424), W410 (= W425), Q411 (= Q426), T412 (= T427), D496 (= D510), I508 (= I522), R511 (= R525), N517 (≠ L531), R522 (= R536)
binding coenzyme a: F159 (= F171), G160 (= G172), G161 (= G173), R187 (= R199), I192 (= I204), D302 (≠ E317), S519 (≠ A533), H521 (= H535), R580 (= R600), P585 (= P605)
binding magnesium ion: V533 (≠ A547), H535 (= H549), I538 (≠ V552)

2p20A Acetyl-coa synthetase, r584a mutation (see paper)
44% identity, 95% coverage: 28:648/651 of query aligns to 13:628/641 of 2p20A

query
sites
2p20A

A

C

V

L

V

I

N

N

P

P

Q

E

D

Q

V

Y

A

E

R

T

A

K

R

Y

A

K

R

Q

A

S

A

I

A

N

D

D

P

P

D

D

G

T

Y

F

W

W

E

G

E

E

A

Q

A

G

E

K

E

I

L

L

E

D

W

W

F

I

R

T

R

P

W

Y

D

Q

A

K

V

V

H

K

D

N

G

T

S

S

N

F

A

A

P

P

F

G

H

N

-

V

-

S

-

I

R

K

W

W

F

Y

T

E

G

D

A

G

R

T

C

L

N

N

I

L

V

A

H

A

N

N

A

C

L

L

D

D

R

R

H

H

I

L

E

Q

T

E

G

-

T

N

K

G

N

D

R

R

L

T

A

A

L

I

I

I

W

W

E

E

G

G

E

D

-

D

S

T

G

S

D

Q

T

S

R

K

S

H

F

I

T

S

Y

Y

Y

R

Q

E

L

L

Y

H

R

R

E

D

V

V

N

C

R

R

L

F

A

A

N

N

A

T

L

L

R

L

G

D

L

L

G

G

V

I

G

K

K

K

G

G

D

D

R

V

V

V

I

A

I

I

Y

Y

M

M

P

P

P

M

L

V

P

P

E

E

T

A

V

A

F

V

A

A

M

M

L

L

A

A

A

C

A

A

K

R

I

I

G

G

A

A

V

V

H

H

S

S

T

V

V

I

F

F

G

G

F

F

S

S

A

P

R

E

S

A

L

V

R

A

D

G

R

R

M

I

E

I

D

D

A

S

R

S

P

S

A

R

V

L

I

V

V

I

T

T

V

A

D

D

G

E

F

G

Y

V

R

R

N

A

G

G

R

R

V

S

I

I

P

P

L

L

K

K

P

K

I

N

A

V

D

D

E

D

A

A

V

L

A

K

T

N

L

-

P

-

P

P

D

N

L

V

A

T

A

S

G

-

V

V

R

E

H

H

M

V

V

I

V

V

V

L

H

K

R

R

A

T

H

G

V

S

E

D

T

I

P

D

M

W

T

Q

E

E

G

G

R

R

D

D

I

L

W

W

Y

W

H

R

D

D

A

L

V

I

R

E

G

K

Q

A

H

S

H

P

E

E

A

H

L

Q

T

P

E

E

I

A

M

M

D

N

S

A

T

E

D

D

P

P

L

L

F

F

L

I

L

L

Y

Y

T
|
T

S

S

G

G

T

S

T

T

G

G

K

K

P

P

K

K

G

G

H

V

V

L

H

H

A

T

H

T

G

G

Y

Y

M

L

V

V

G

Y

V

A

H

A

R

T

T

T

M

F

R

K

W

Y

V

V

F

F

D

D

V

Y

K

H

P

P

T

G

D

D

I

I

F

Y

W

W

C

C

T

T

A

A

E

D

P

V

G

G

W

W

I
x
V

T
|
T

G

G

H

H

S

S

Y

Y

V

L

Y

Y

G

G

P

P

L

L

M

A

A

C

G

G

T

A

T

T

V

L

L

M

Y

F

E

E

G

G

H

V

P

P

L

N

Y

W

P

P

E

T

P

P

G

A

R

R

V

M

W

C

S

Q

M

V

V

V

E

D

R

K

L

H

G

Q

I

V

T

N

I

I

L

L

Y

Y

T

T

A

A

P

P

T

T

L

A

V

I

R

R

M

A

L

L

M

M

R

A

H

E

G

G

A

D

Q

K

H

A

V

I

A

E

R

G

H

T

D

D

L

R

T

S

L

L

R

R

L

I

L

L

G

G

T

S

V

V

G
|
G

E
|
E

P
|
P

I

I

S

N

P

P

E

E

A

A

W

W

L

E

W

W

F

Y

H

W

R

K

H

K

V

I

G

G

R

K

G

E

R

K

C

C

P

P

V

V

L

V

D
|
D

T
|
T

W
|
W

Q
|
Q

T
|
T

E
|
E

T

T

G

G

M

G

I

F

M

M

L

I

S

T

P

P

L

L

P

P

V

G

S

A

L

I

-

E

L

L

K

K

P

A

G

G

S

S

V

A

T

T

R

R

P

P

L

F

P

F

G

G

I

V

E

Q

A

P

D

A

V

L

V

V

D

D

E

N

H

E

G

G

K

H

P

P

V

Q

G

E

P

G

G

A

H

T

G

E

G

G

L

N

L

L

V

V

L

I

Q

T

R

D

P

S

W

W

P

P

A

G

M

Q

S

A

C

R

G

T

V

L

Y

F

N

G

D

D

D

H

E

E

S

R

Y

F

R

E

R

Q

L

T

Y

Y

W

F

E

S

R

T

F

F

P

K

G

N

W

M

Y

Y

C

F

T

S

G

G

D
|
D

V

G

A

A

R

R

D

D

E

E

D

D

G

G

Y

Y

F

Y

W

W

I
|
I

Q

T

G

G

R
|
R

A

V

D

D

V

V

L

L

L
x
N

I

V

A

S

G

G

H

H

R
|
R

I

L

G

G

T

T

A

A

E

E

M

I

E

E

A

S

A

A

L

L

A

V

S

A

H

H

R

P

S

K

V

I

A

A

E

E

C

A

A

A

V

V

I

V

G

G

V

I

P

P

D

H

A

A

L

I

R

K

G

G

E

Q

V

A

A

I

K

Y

A

A

F

Y

V

V

V

T

L

L

V

N

D

H

D

G

H

E

P

E

P

P

L

-

G

-

T

-

M

-

V

-

N

-

A

S

D

P

E

E

L

L

A

Y

A

A

E

E

L

V

V

R

E

N

H

W

V

V

R

A

R

K

E

E

L

I

G

G

P

P

V

L

A

A

V

T

I

P

R

D

E

V

V

L

S

H

F

W

R

T

E

D

G

S

L

L

P

P

R

K

N

T

R

R

S

S

G

G

K
|
K

I

I

M

M

R

R

V

I

L

L

R

R

S

K

E

I

E

A

L

A

G

G

R

D

D

T

T

S

G

N

D

D

L

T

S

S

T

T

L

L

E

A

D

D

active site: T260 (= T275), T412 (= T427), E413 (= E428), N517 (≠ L531), R522 (= R536), K605 (= K625)
binding adenosine-5'-monophosphate-propyl ester: V306 (≠ I321), T307 (= T322), G383 (= G398), E384 (= E399), P385 (= P400), D407 (= D422), T408 (= T423), W409 (= W424), W410 (= W425), Q411 (= Q426), T412 (= T427), D496 (= D510), I508 (= I522), R511 (= R525), N517 (≠ L531), R522 (= R536)

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)
44% identity, 95% coverage: 28:648/651 of query aligns to 17:634/652 of P27550

query
sites
P27550

A

C

V

L

V

I

N

N

P

P

Q

Q

D

Q

V

Y

A

E

R

A

A

M

R

Y

A

Q

R

Q

A

S

A

I

A

N

D

V

P

P

D

D

G

T

Y

F

W

W

E

G

E

E

A

Q

A

G

E

K

E

I

L

L

E

D

W

W

F

I

R

K

R

P

W

Y

D

Q

A

K

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V

H

K

D

N

G

T

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S

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F

A

A

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P

F

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H

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-

V

-

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-

I

R

K

W

W

F

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D

A

G

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N

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A

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N

A

C

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L

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D

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H

H

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-

T

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K

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D

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A

A

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I

I

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W

E

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-

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A

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Y

Y

Y

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L

L

Y

H

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D

V

V

N

C

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R

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F

A

A

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N

A

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L

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E

L

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I

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A

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A

A

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A

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A

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A

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L

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A

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D

A

A

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N

L

-

P

-

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P

D

N

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A

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-

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Y

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F

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D

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I

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Y

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A

A

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W

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Y

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Y

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P

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A

A

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A

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E

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P

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Y

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P

P

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A

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M

W

A

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M

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V

V

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D

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K

L

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G

Q

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N

I

I

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L

Y

Y

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A

A

P

P

T

T

L

A

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I

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A

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L

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M

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A

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A

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D

L

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L

L

R

R

L

I

L

L

G

G

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V

G

G

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E

P

P

I

I

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N

P

P

E

E

A

A

W

W

L

E

W

W

F

Y

H

W

R

K

H

K

V

I

G

G

R

N

G

E

R

K

C

C

P

P

V

V

L

V

D

D

T

T

W

W

Q

Q

T

T

E

E

T

T

G

G

M

G

I

F

M

M

L

I

S

T

P

P

L

L

P

P

-

G

V

A

S

T

L

E

L

L

K

K

P

A

G

G

S

S

V

A

T

T

R

R

P

P

L

F

P

F

G

G

I

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E

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A

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D

A

V

L

V

V

D

D

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N

H

E

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G

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N

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P

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L

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G

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A

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L

L

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V

L

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S

W

W

P

P

A

G

M

Q

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A

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G

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V

L

Y

F

N

G

D

D

D

H

E

E

S

R

Y

F

R

E

R

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L

T

Y

Y

W

F

E

S

R

T

F

F

P

K

G

N

W

M

Y

Y

C

F

T

S

G

G

D

D

V

G

A

A

R

R

D

D

E

E

D

D

G

G

Y

Y

F

Y

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W

I

I

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T

G

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R

R

A

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D

D

V

V

L

L

L

N

I

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A

S

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G

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H

R

R

I

L

G

G

T

T

A

A

E

E

M

I

E

E

A

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A

A

L

L

A

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S

A

H

H

R

P

S

K

V

I

A

A

E

E

C

A

A

A

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G

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I

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P

D

H

A

N

L

I

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G

G

E

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V

A

A

I

K

Y

A

A

F

Y

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V

V

T

L

L

V

N

D

H

D

G

H

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P

E

P

P

L

-

G

-

T

-

M

-

V

-

N

-

A

S

D

P

E

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L

L

A

Y

A

A

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L

V

V

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N

H

W

V

V

R

R

R

K

E

E

L

I

G

G

P

P

V

L

A

A

V

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I

P

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D

E

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V

L

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H

F

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G

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L

L

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P

R

K

N

T

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R

S

S

G

G

K
|
K

I

I

M

M

R

R

V

I

L

L

R

R

S

K

E

I

E

A

L

A

G

G

-

D

-

T

R

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D

N

T

L

G

G

D

D

L

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S

S

T

T

L

L

E

A

D

D

K609 (= K625) 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)
44% identity, 95% coverage: 28:648/651 of query aligns to 17:634/652 of Q8ZKF6

query
sites
Q8ZKF6

A

C

V

L

V

I

N

N

P

P

Q

E

D

Q

V

Y

A

E

R

T

A

K

R

Y

A

K

R

Q

A

S

A

I

A

N

D

D

P

P

D

D

G

T

Y

F

W

W

E

G

E

E

A

Q

A

G

E

K

E

I

L

L

E

D

W

W

F

I

R

T

R

P

W

Y

D

Q

A

K

V

V

H

K

D

N

G

T

S

S

N

F

A

A

P

P

F

G

H

N

-

V

-

S

-

I

R

K

W

W

F

Y

T

E

G

D

A

G

R

T

C

L

N

N

I

L

V

A

H

A

N

N

A

C

L

L

D

D

R

R

H

H

I

L

E

Q

T

E

G

-

T

N

K

G

N

D

R

R

L

T

A

A

L

I

I

I

W

W

E

E

G

G

E

D

-

D

S

T

G

S

D

Q

T

S

R

K

S

H

F

I

T

S

Y

Y

Y

R

Q

E

L

L

Y

H

R

R

E

D

V

V

N

C

R

R

L

F

A

A

N

N

A

T

L

L

R

L

G

D

L

L

G

G

V

I

G

K

K

K

G

G

D

D

R

V

V

V

I

A

I

I

Y

Y

M

M

P

P

P

M

L

V

P

P

E

E

T

A

V

A

F

V

A

A

M

M

L

L

A

A

A

C

A

A

K

R

I

I

G

G

A

A

V

V

H

H

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S

T

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V

I

F

F

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G

F

F

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S

A

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A

L

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A

D

G

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I

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T

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A

D

D

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E

F

G

Y

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A

G

G

R
|
R

V

S

I

I

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P

L

L

K

K

P

K

I

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A

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D

D

E

D

A

A

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A

K

T

N

L

-

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P

D

N

L

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A

T

A

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G

-

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E

H

H

M

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I

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V

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H

K

R

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A

T

H

G

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S

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T

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P

D

M

W

T

Q

E

E

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G

R

R

D

D

I

L

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Y

W

H

R

D

D

A

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I

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G

K

Q

A

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H

P

E

E

A

H

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E

E

I

A

M

M

D

N

S

A

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E

D

D

P

P

L

L

F

F

L

I

L

L

Y

Y

T

T

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S

G

G

T

S

T

T

G

G

K

K

P

P

K

K

G

G

H

V

V

L

H

H

A

T

H

T

G

G

Y

Y

M

L

V

V

G

Y

V

A

H

A

R

T

T

T

M

F

R

K

W

Y

V

V

F

F

D

D

V

Y

K

H

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P

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G

D

D

I

I

F

Y

W

W

C

C

T

T

A

A

E

D

P

V

G

G

W

W

I

V

T
|
T

G

G

H

H

S

S

Y

Y

V

L

Y

Y

G

G

P

P

L

L

M

A

A

C

G

G

T

A

T

T

V

L

L

M

Y

F

E

E

G

G

H

V

P

P

L
x
N

Y

W

P

P

E

T

P

P

G

A

R

R

V

M

W

C

S

Q

M

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V

V

E

D

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K

L

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G

Q

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N

I

I

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Y

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T

T

A
|
A

P

P

T

T

L

A

V

I

R

R

M

A

L

L

M

M

R

A

H

E

G

G

A

D

Q

K

H

A

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I

A

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R

G

H

T

D

D

L

R

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S

L

L

R

R

L

I

L

L

G

G

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S

V

V

G

G

E

E

P

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I

S

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P

P

E

E

A

A

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W

L

E

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F

Y

H

W

R

K

H

K

V

I

G

G

R

K

G

E

R

K

C

C

P

P

V

V

L

V

D

D

T

T

W

W

Q

Q

T

T

E

E

T

T

G

G

M

G

I

F

M

M

L

I

S

T

P

P

L

L

P

P

V

G

S

A

L

I

-

E

L

L

K

K

P

A

G

G

S

S

V

A

T

T

R

R

P

P

L

F

P

F

G

G

I

V

E

Q

A

P

D

A

V

L

V

V

D

D

E

N

H

E

G

G

K

H

P

P

V

Q

G

E

P

G

G

A

H

T

G

E

G

G

L

N

L

L

V

V

L

I

Q

T

R

D

P

S

W

W

P

P

A

G

M

Q

S

A

C

R

G

T

V

L

Y

F

N

G

D

D

D

H

E

E

S

R

Y

F

R

E

R

Q

L

T

Y

Y

W

F

E

S

R

T

F

F

P

K

G

N

W

M

Y

Y

C

F

T

S

G

G

D

D

V

G

A

A

R

R

D

D

E

E

D

D

G

G

Y

Y

F

Y

W

W

I

I

Q

T

G

G

R

R

A

V

D
|
D

D

D

V

V

L

L

L

N

I

V

A
x
S

G
|
G

H

H

R
|
R

I

L

G

G

T

T

A

A

E

E

M

I

E

E

A

S

A

A

L

L

A

V

S

A

H

H

R

P

S

K

V

I

A

A

E

E

C

A

A

A

V

V

I

V

G

G

V

I

P

P

D

H

A

A

L

I

R

K

G

G

E

Q

V

A

A

I

K

Y

A

A

F

Y

V

V

V

T

L

L

V

N

D

H

D

G

H

E

P

E

P

P

L

-

G

-

T

-

M

-

V

-

N

-

A

S

D

P

E

E

L

L

A

Y

A

A

E

E

L

V

V

R

E

N

H

W

V

V

R
|
R

R

K

E

E

L

I

G

G

P

P

V

L

A

A

V

T

I

P

R

D

E

V

V

L

S

H

F

W

R

T

E

D

G

S

L

L

P

P

R

K

N

T

R

R

S

S

G

G

K
|
K

I

I

M

M

R

R

V

I

L

L

R

R

S

K

E

I

E

A

L

A

G

G

-

D

-

T

R

S

D

N

T

L

G

G

D

D

L

T

S

S

T

T

L

L

E

A

D

D

R194 (= R202) 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 (= T322) binding
N335 (≠ L346) binding
A357 (= A368) 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 (= D527) 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 (≠ A533) binding
G524 (= G534) 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 (= R536) 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 (= R600) 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.

2p2fA Acetyl-coa synthetase, wild-type with acetate, amp, and coa bound (see paper)
44% identity, 95% coverage: 28:648/651 of query aligns to 12:624/637 of 2p2fA

query
sites
2p2fA

A

C

V

L

V

I

N

N

P

P

Q

E

D

Q

V

Y

A

E

R

T

A

K

R

Y

A

K

R

Q

A

S

A

I

A

N

D

D

P

P

D

D

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|
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|
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L

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D

D

active site: T259 (= T275), T411 (= T427), E412 (= E428), N516 (≠ L531), R521 (= R536), K604 (= K625)
binding adenosine monophosphate: G382 (= G398), E383 (= E399), P384 (= P400), D406 (= D422), T407 (= T423), W408 (= W424), W409 (= W425), Q410 (= Q426), T411 (= T427), D495 (= D510), I507 (= I522), R510 (= R525), N516 (≠ L531), R521 (= R536)
binding coenzyme a: F158 (= F171), G159 (= G172), G160 (= G173), R186 (= R199), I191 (= I204), A300 (= A316), W304 (= W320), T306 (= T322), V328 (≠ H344), P329 (= P345), A352 (= A368), T354 (= T370), A355 (≠ L371), S518 (≠ A533), G519 (= G534), R579 (= R600), P584 (= P605)

1pg3A Acetyl coa synthetase, acetylated on lys609 (see paper)
44% identity, 95% coverage: 28:647/651 of query aligns to 13:626/634 of 1pg3A

query
sites
1pg3A

A

C

V

L

V

I

N

N

P

P

Q

E

D

Q

V

Y

A

E

R

T

A

K

R

Y

A

K

R

Q

A

S

A

I

A

N

D

D

P

P

D

D

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Y

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W

W

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G

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A

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K

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L

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W

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P

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Y

D

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A

K

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V

H

K

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N

G

T

S

S

N

F

A

A

P

P

F

G

H

N

-

V

-

S

-

I

R

K

W

W

F

Y

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E

G

D

A

G

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L

N

N

I

L

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A

H

A

N

N

A

C

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L

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D

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H

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K

G

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A

A

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I

I

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W

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G

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D

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D

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F

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Y

Y

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L

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V

V

N

C

R

R

L

F

A

A

N

N

A

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L

L

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L

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D

L

L

G

G

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G

K

K

K

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M

L

L

A

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A

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I

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G

A

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V

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H