SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_022671372.1 NCBI__GCF_000420385.1:WP_022671372.1 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)

P45359 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; CaTHL; EC 2.3.1.9 from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W) (see paper)
47% identity, 100% coverage: 1:389/389 of query aligns to 1:392/392 of P45359

query
sites
P45359

M

M

D

K

G

E

V

V

F

V

V

I

V

A

E

S

P

A

L

V

R

R

S

T

P

A

F

I

G

G

G

S

F

Y

G

G

G

K

T

S

L

L

S

K

S

D

L

V

S

P

A

A

S

V

E

D

I

L

A

G

S

A

F

T

V

A

V

I

K

K

E

E

I

A

L

V

S

K

R

K

T

A

G

G

I

I

-

K

-

P

E

E

D

D

V

V

D

N

G

E

L

V

I

I

M

L

G

G

N

N

V

V

L

L

S

Q

A

A

G

G

V

L

G

G

Q

Q

S

N

P

P

A

A

R

R

Q

Q

V

A

I

S

I

F

K

K

S

A

G

G

L

L

P

P

Y
x
V

S

E

V

I

N

P

A

A

L

M

T

T

V

I

N

N

K

K

V

V

C
|
C

G

G

S

S

G

G

L

L

K

R

S

T

L

V

M
x
S

L

L

A

A

Q

Q

S

I

I

I

K

K

L

A

K

G

D

D

S

A

S

D

L

V

I

I

A

A

G

G

M

M

E

E

S

N

M

M

S

S

N

R

A

A

P

P

Y

Y

Y

L

L

A

S

N

K

N

A

A

R

R

F

W

G

G

Y

Y

R

R

M

M

G

G

D

N

G

A

R

K

A

F

I

V

D

D

G

E

M

M

I

I

F

T

D

D

G

G

L

L

W

W

D

D

V

A

Y

F

N
|
N

N

D

V

Y

H

H

M

M

G

G

Y

I

L

T

A

A

E

E

M

N

V

I

A

A

K

E

A

R

K

W

K

N

I

I

T

S

R

R

K

E

I

E

Q

Q

D

D

D

E

Y

F

A

A

V

L

L

A

S

S

Y

Q

K

K

R

K

A

A

Q

E

H

E

S

A

A

I

E

K

N

S

G

G

V

Q

F

F

K

K

E

D

E

E

I

I

V

V

P

P

I

V

E

V

I

I

S

K

S

G

R

R

K

K

G

G

V

E

N

T

V

V

D

D

R

T

D

D

E

E

E

H

P

P

-

R

F

F

R

G

V

S

D

T

F

I

E

E

K

G

I

L

P

A

K

K

L

L

K

K

P

P

A

A

F

F

V

K

E

K

D

D

G

G

T

T

I

V

T

T

A

A

A

G

N

N

A

A

S

S

T

G

I

L

S

N

D

D

G

C

A

A

A

V

F

L

I

V

V

I

A

M

D

S

Y

A

D

E

A

K

I

A

K

K

R

E

F

L

G

G

L

V

E

K

P

P

I

L

A

A

K

K

V

I

V

V

A

S

Y

Y

S
x
G

E
x
S

F

A

S

G

L

V

D

D

P

P

K
x
A

L

I

F

M

P

G

L

Y

A

G

P

P

I

F

G

Y

A

A

I

T

E

K

K

A

L

A

L

I

K

E

K

K

T

A

G

G

L

W

D

T

V

V

N

D

D

E

I

L

D

D

L

L

F

I

E

E

I

S

N

N

E

E

A

A

F

F

S

A

C

A

V

Q

V

S

L

L

A

A

A

V

L

A

E

K

E

D

L

L

K

K

L

F

D

D

I

M

D

N

R

K

V

V

N

N

V

V

N

N

G

G

A

A

V

I

S

A

L

L

G

G

H

H

P

P

L

I

G

G

A

A

S

S

G

G

A

A

R

R

L

I

V

L

V

V

S

T

L

L

T

V

R

H

E

A

M

M

R

Q

R

K

R

R

N

D

A

A

K

K

Y

K

G

G

I

L

A

A

A

T

L

L

C
|
C

I

I

G

G

E

Q

A

G

V

T

A
|
A

T

I

L

L

F

L

E

E

R

K

V

C

V77 (≠ Y75) mutation to Q: 3-fold increase in thiolase activity, prevents disulfide bond formation under oxidized condition and results in the loss of regulatory mechanism based on redox-switch modulation; when associated with Y-153 and K-286.
C88 (= C86) modified: Disulfide link with 378, In inhibited form
S96 (≠ M94) binding acetate
N153 (= N151) mutation to Y: 3-fold increase in thiolase activity, prevents disulfide bond formation under oxidized condition and results in the loss of regulatory mechanism based on redox-switch modulation; when associated with Q-77 and K-286.
GS 279:280 (≠ SE 276:277) binding acetate
A286 (≠ K283) mutation to K: 3-fold increase in thiolase activity, prevents disulfide bond formation under oxidized condition and results in the loss of regulatory mechanism based on redox-switch modulation; when associated with Q-77 and Y-153.
C378 (= C375) modified: Disulfide link with 88, In inhibited form
A386 (= A383) binding acetate

4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
47% identity, 100% coverage: 1:389/389 of query aligns to 1:392/392 of 4xl4A

query
sites
4xl4A

M

M

D

K

G

E

V

V

F

V

V

I

V

A

E

S

P

A

L

V

R

R

S

T

P

A

F

I

G

G

G

S

F

Y

G

G

G

K

T

S

L

L

S

K

S

D

L

V

S

P

A

A

S

V

E

D

I

L

A

G

S

A

F

T

V

A

V

I

K

K

E

E

I

A

L

V

S

K

R

K

T

A

G

G

I

I

-

K

-

P

E

E

D

D

V

V

D

N

G

E

L

V

I

I

M

L

G

G

N

N

V

V

L

L

S

Q

A

A

G

G

V

L

G

G

Q

Q

S

N

P

P

A

A

R

R

Q

Q

V

A

I

S

I

F

K

K

S

A

G

G

L

L

P

P

Y

V

S

E

V

I

N

P

A

A

L

M

T

T

V

I

N

N

K

K

V

V

C
|
C

G

G

S

S

G

G

L

L

K

R

S

T

L

V

M

S

L

L

A

A

Q

Q

S

I

I

I

K

K

L

A

K

G

D

D

S

A

S

D

L

V

I

I

A

A

G

G

M

M

E

E

S

N

M

M

S

S

N

R

A

A

P

P

Y

Y

Y

L

L

A

S

N

K

N

A

A

R

R

F

W

G

G

Y

Y

R

R

M

M

G

G

D

N

G

A

R

K

A

F

I

V

D

D

G

E

M

M

I

I

F

T

D

D

G

G

L
|
L

W

W

D

D

V

A

Y

F

N

N

N

D

V

Y

H
|
H

M

M

G

G

Y

I

L

T

A

A

E

E

M

N

V

I

A

A

K

E

A

R

K

W

K

N

I

I

T

S

R

R

K

E

I

E

Q

Q

D

D

D

E

Y

F

A

A

V

L

L

A

S

S

Y

Q

K

K

R

K

A

A

Q

E

H

E

S

A

A

I

E

K

N

S

G

G

V

Q

F

F

K

K

E

D

E

E

I

I

V

V

P

P

I

V

E

V

I

I

S

K

S

G

R

R

K

K

G

G

V

E

N

T

V

V

D

D

R

T

D

D

E

E

E

H

P

P

-
x
R

F

F

R

G

V

S

D

T

F

I

E

E

K

G

I

L

P

A

K

K

L
|
L

K

K

P

P

A

A

F

F

V

K

E

K

D

D

G

G

T

T

I

V

T

T

A
|
A

A

G

N

N

A

A

S
|
S

T

G

I

L

S

N

D

D

G

C

A

A

A

V

F

L

I

V

V

I

A

M

D

S

Y

A

D

E

A

K

I

A

K

K

R

E

F

L

G

G

L

V

E

K

P

P

I

L

A

A

K

K

V

I

V

V

A

S

Y

Y

S

G

E

S

F

A

S

G

L

V

D

D

P

P

K

A

L

I

F

M

P

G

L

Y

A

G

P

P

I

F

G

Y

A

A

I

T

E

K

K

A

L

A

L

I

K

E

K

K

T

A

G

G

L

W

D

T

V

V

N

D

D

E

I

L

D

D

L

L

F

I

E

E

I

S

N

N

E

E

A

A

F
|
F

S

A

C

A

V

Q

V

S

L

L

A

A

A

V

L

A

E

K

E

D

L

L

K

K

L

F

D

D

I

M

D

N

R

K

V

V

N

N

V

V

N

N

G

G

A

A

V

I

S

A

L

L

G

G

H
|
H

P

P

L

I

G

G

A

A

S

S

G

G

A

A

R

R

L

I

V

L

V

V

S

T

L

L

T

V

R

H

E

A

M

M

R

Q

R

K

R

R

N

D

A

A

K

K

Y

K

G

G

I

L

A

A

A

T

L

L

C
x
S

I

I

G
|
G

G

G

E

Q

A

G

V

T

A

A

T

I

L

L

F

L

E

E

R

K

V

C

active site: C88 (= C86), H348 (= H345), S378 (≠ C375), G380 (= G377)
binding coenzyme a: L148 (= L146), H156 (= H154), R220 (vs. gap), L231 (= L228), A243 (= A240), S247 (= S244), F319 (= F316), H348 (= H345)

P14611 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) (see paper)
48% identity, 100% coverage: 1:388/389 of query aligns to 1:392/393 of P14611

query
sites
P14611

M

M

D

T

G

D

V

V

F

V

V

I

V

V

E

S

P

A

L

A

R

R

S

T

P

A

F

V

G

G

G

K

F

F

G

G

T

S

L

L

S

A

S

K

L

I

S

P

A

A

S

P

E

E

I

L

A

G

S

A

F

V

V

V

V

I

K

K

E

A

I

A

L

L

S

E

R

R

T

A

G

G

I

V

-

K

-

P

E

E

D

Q

V

V

D

S

G

E

L

V

I

I

M

M

G

G

N

Q

V

V

L

L

S

T

A

A

G

G

V

S

G

G

Q

Q

S

N

P

P

A

A

R

R

Q

Q

V

A

I

A

I

I

K

K

S

A

G

G

L

L

P

P

Y

A

S

M

V

V

N

P

A

A

L

M

T

T

V

I

N

N

K

K

V

V

C
|
C

G

G

S

S

G

G

L

L

K

K

S

A

L

V

M

M

L

L

A

A

Q

N

S

A

I

I

K

M

L

A

K

G

D

D

S

A

S

E

L

I

I

V

A

A

G

G

M

Q

E

E

S

N

M

M

S

S

N

A

A

A

P

P

Y

H

Y

V

L

L

S

P

K

G

A

S

R

R

F

D

G

G

Y

F

R

R

M

M

G

G

D

D

G

A

R

K

A

L

I

V

D

D

G

T

M

M

I

I

F

V

D

D

G

G

L

L

W

W

D

D

V

V

Y

Y

N

N

N

Q

V

Y

H
|
H

M

M

G

G

Y

I

L

T

A

A

E

E

M

N

V

V

A

A

K

K

A

E

K

Y

K

G

I

I

T

T

R

R

K

E

I

A

Q

Q

D

D

D

E

Y

F

A

A

V

V

L

G

S

S

Y

Q

K

N

R

K

A

A

Q

E

H

A

S

A

A

Q

E

K

N

A

G

G

V

K

F

F

K

D

E

E

I

I

V

V

P

P

I

V

E

L

I

I

S

P

S

Q

R

R

K

K

G

G

V

D

N

P

V

V

V

A

D

F

R

K

D

T

E

D

E

E

P
x
F

F

V

R
|
R

-

Q

-

G

V

A

D

T

F

L

E

D

K

S

I

M

P

S

K

G

L

L

K

K

P

P

A

A

F

F

V

D

E

K

D

A

G

G

T

T

I

V

T

T

A

A

N

N

A

A

S
|
S

T

G

I

L

S

N

D

D

G

G

A

A

F

V

I

V

V

V

A

M

D

S

Y

A

D

A

A

K

I

A

K

K

R

E

F

L

G

G

L

L

E

T

P

P

I

L

A

A

K

T

V

I

V

K

A

S

Y

Y

S

A

E

N

F

A

S

G

L

V

D

D

P

P

K

K

L

V

F

M

P

G

L

M

A

G

P

P

I

V

G

P

A

A

I

S

E

K

K

R

L

A

L

L

K

S

K

R

T

A

G

E

L

W

D

T

V

P

N

Q

D

D

I

L

D

D

L

L

F

M

E

E

I

I

N

N

E

E

A

A

F

F

S

A

C

A

V

Q

V

A

L

L

A

A

A

V

L

H

E

Q

L

M

K

G

L

W

D

D

I

T

D

S

R

K

V

V

N

N

V

V

N

N

G

G

A

A

V

I

S

A

L

I

G

G

H
|
H

P

P

L

I

G

G

A

A

S

S

G

G

A

C

R

R

L

I

V

L

V

V

S

T

L

L

T

L

R

H

E

E

M

M

R

K

R

R

N

D

A

A

K

K

Y

K

G

G

I

L

A

A

A

S

L

L

C
|
C

I

I

G

G

E

M

A

G

V

V

A

A

T

L

L

A

F

V

E

E

R

R

C88 (= C86) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
H156 (= H154) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
F219 (≠ P217) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
R221 (= R219) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
S248 (= S244) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
H349 (= H345) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
C379 (= C375) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.

8gqnA X-ray structure of thiolase with coa
48% identity, 99% coverage: 4:387/389 of query aligns to 3:388/390 of 8gqnA

query
sites
8gqnA

V

I

F

V

V

I

V

V

E

A

P

G

L

A

R

R

S

T

P

P

F

M

G

G

F

F

G

Q

G

G

T

S

L

L

S

A

S

G

L

V

S

S

A

A

S

V

E

D

I

L

A

G

S

A

F

V

V

A

V

I

K

R

E

E

I

A

L

V

S

Q

R

R

T

A

G

G

I

I

-

A

E

E

D

D

V

V

D

Q

G

E

L

V

I

I

M

M

G

G

N

C

V

V

L

L

S

P

A

A

G

G

V

L

G

K

Q

Q

S

G

P

P

A

A

R

R

Q

Q

V

A

I

A

I

L

K

A

S

A

G

G

L

L

P

P

Y

A

S

A

V

T

N

G

A

C

L

T

T

T

V

I

N

N

K

K

V

L

C

C

G

G

S

S

G

G

L

M

K

K

S

A

L

V

M

M

L

L

A

A

A

H

Q

D

S

L

I

L

K

K

L

A

K

G

D

T

S

N

S

Q

L

V

I

M

I

V

A

A

G

G

M

M

E

E

S

S

M

M

S

S

N

N

A

A

P

P

Y

Y

Y

V

L

L

S

E

K

K

A

A

R

R

F

S

G

G

Y

L

R

R

M

M

G

G

D

H

G

G

R

E

A

I

I

K

D

D

G

H

M

M

I

F

F

L

D

D

G

G

L
|
L

W

E

D

D

V

A

Y

R

N

T

N

G

V

R

H

L

M

M

G

G

Y

S

L

F

A

A

E

Q

M

E

V

T

A

A

K

D

A

K

K

Y

K

G

I

V

T

T

R

R

K

E

I

E

Q

M

D

D

D

A

Y

Y

A

A

V

I

L

E

S

S

Y

L

K

K

R

R

A

A

Q

Q

H

A

S

A

A

I

E

A

N

D

G

G

V

S

F

L

K

A

E

A

E

E

I

I

V

V

P

P

I

V

E

T

I

V

S

T

S

S

R

R

K

K

G

G

V

E

N

S

V

V

D

K

R

D

D

D

E

E

E
x
Q

P

P

F

L

R

T

V

A

D

N

F

L

E

E

K

K

I
|
I

P

P

K

S

L
|
L

K

R

P

P

A

A

F

F

V

R

E

K

D

D

G

G

T

T

I

I

T

T

A
|
A

N

N

A

A

S
|
S

T

S

I
|
I

S

S

D

D

G

G

A

A

A

S

A

A

F

L

I

V

V

L

A

M

D

T

Y

A

D

E

A

E

I

A

K

Q

R

R

F

R

G

G

L

L

E

K

P

P

I

L

A

A

K

R

V

I

V

V

A

G

Y

H

S

A

E

T

F

Q

S

S

L

Q

D

D

P

P

K

S

L

E

F

F

P

T

L

L

A

A

P

P

I

I

G

G

A

A

I

M

E

T

K

N

L

L

L

F

K

A

K

R

T

T

G

G

L

W

D

S

V

K

N

D

D

D

I

V

D

D

L

L

F

F

E

E

I

I

N

N

E

E

A

A

F

F

S

A

C

M

V

V

V

T

L

M

A

L

A

A

L

M

E

R

E

E

L

H

K

G

L

L

D

D

I

H

D

A

R

K

V

V

N

N

V

V

N

Y

G

G

A

A

V

C

S

A

L

Q

G

G

H

H

P

P

L

V

G

G

A

S

S

T

G

G

A

S

R

R

L

I

V

I

V

L

S

T

L

L

T

I

R

N

E

A

M

L

R

R

R

Q

R

K

N

G

A

G

K

K

Y

R

G

G

I

V

A

A

A

S

L

L

C

C

I

I

G

G

E

E

A

A

V

T

A

A

T

V

L

A

F

L

E

E

binding coenzyme a: L147 (= L146), Q217 (≠ E216), I226 (= I225), L229 (= L228), A241 (= A240), A242 (= A241), S245 (= S244), I247 (= I246)

4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
48% identity, 100% coverage: 1:388/389 of query aligns to 1:392/393 of 4o9cC

query
sites
4o9cC

M

M

D

T

G

D

V

V

F

V

V

I

V

V

E

S

P

A

L

A

R

R

S

T

P

A

F

V

G

G

G

K

F

F

G

G

T

S

L

L

S

A

S

K

L

I

S

P

A

A

S

P

E

E

I

L

A

G

S

A

F

V

V

V

V

I

K

K

E

A

I

A

L

L

S

E

R

R

T

A

G

G

I

V

-

K

-

P

E

E

D

Q

V

V

D

S

G

E

L

V

I

I

M

M

G

G

N

Q

V

V

L

L

S

T

A

A

G

G

V

S

G

G

Q

Q

S

N

P

P

A

A

R

R

Q

Q

V

A

I

A

I

I

K

K

S

A

G

G

L

L

P

P

Y

A

S

M

V

V

N

P

A

A

L

M

T

T

V

I

N

N

K

K

V

V

C
x
S

G

G

S

S

G

G

L

L

K

K

S

A

L

V

M

M

L

L

A

A

Q

N

S

A

I

I

K

M

L

A

K

G

D

D

S

A

S

E

L

I

I

V

A

A

G

G

M

Q

E

E

S

N

M

M

S

S

N

A

A

A

P

P

Y

H

Y

V

L

L

S

P

K

G

A

S

R

R

F

D

G

G

Y

F

R

R

M

M

G

G

D

D

G

A

R

K

A

L

I

V

D

D

G

T

M

M

I

I

F

V

D

D

G

G

L
|
L

W

W

D

D

V

V

Y

Y

N

N

N

Q

V

Y

H

H

M

M

G

G

Y

I

L

T

A

A

E

E

M

N

V

V

A

A

K

K

A

E

K

Y

K

G

I

I

T

T

R

R

K

E

I

A

Q

Q

D

D

D

E

Y

F

A

A

V

V

L

G

S

S

Y

Q

K

N

R

K

A

A

Q

E

H

A

S

A

A

Q

E

K

N

A

G

G

V

K

F

F

K

D

E

E

I

I

V

V

P

P

I

V

E

L

I

I

S

P

S

Q

R

R

K

K

G

G

V

D

N

P

V

V

V

A

D

F

R

K

D

T

E

D

E

E

P

F

F

V

R
|
R

-

Q

-

G

V

A

D

T

F

L

E

D

K

S

I

M

P

S

K

G

L

L

K

K

P

P

A

A

F
|
F

V

D

E

K

D

A

G

G

T

T

I

V

T

T

A
|
A

A

A

N

N

A

A

S
|
S

T

G

I
x
L

S

N

D

D

G

G

A

A

F

V

I

V

V

V

A

M

D

S

Y

A

D

A

A

K

I

A

K

K

R

E

F

L

G

G

L

L

E

T

P

P

I

L

A

A

K

T

V

I

V

K

A

S

Y

Y

S

A

E

N

F

A

S

G

L

V

D

D

P

P

K

K

L

V

F

M

P

G

L

M

A

G

P

P

I

V

G

P

A

A

I

S

E

K

K

R

L

A

L

L

K

S

K

R

T

A

G

E

L

W

D

T

V

P

N

Q

D

D

I

L

D

D

L

L

F

M

E

E

I

I

N

N

E

E

A
|
A

F
|
F

S

A

C

A

V

Q

V

A

L

L

A

A

A

V

L

H

E

Q

L

M

K

G

L

W

D

D

I

T

D

S

R

K

V

V

N

N

V

V

N

N

G

G

A

A

V

I

S

A

L

I

G

G

H
|
H

P

P

L

I

G

G

A

A

S

S

G

G

A

C

R

R

L

I

V

L

V

V

S

T

L

L

T

L

R

H

E

E

M

M

R

K

R

R

N

D

A

A

K

K

Y

K

G

G

I

L

A

A

A

S

L

L

C
|
C

I

I

G
|
G

G

G

E

M

A

G

V

V

A

A

T

L

L

A

F

V

E

E

R

R

active site: S88 (≠ C86), H349 (= H345), C379 (= C375), G381 (= G377)
binding coenzyme a: S88 (≠ C86), L148 (= L146), R221 (= R219), F236 (= F232), A244 (= A240), S248 (= S244), L250 (≠ I246), A319 (= A315), F320 (= F316), H349 (= H345)

6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
46% identity, 100% coverage: 1:389/389 of query aligns to 1:392/393 of 6bn2A

query
sites
6bn2A

M

M

D

K

G

E

V

V

F

F

V

I

V

V

E

S

P

A

L

V

R

R

S

T

P

P

F

M

G

G

G

S

F

F

G

M

G

G

T

S

L

L

S

S

S

G

L

V

S

P

A

A

S

T

E

Q

I

L

A

G

S

A

F

V

V

A

V

I

K

K

E

G

I

A

L

L

S

D

R

K

T

I

G

N

I

L

E

N

-

P

-

A

D

E

V

I

D

Q

G

D

L

V

I

Y

M

M

G

G

N

N

V

V

L

L

S

Q

A

A

G

G

V

E

G

G

Q

Q

S

A

P

P

A

A

R

K

Q

Q

V

A

I

A

I

L

K

G

S

A

G

G

L

L

P

P

Y

N

S

T

V

T

N

P

A

T

L

T

T

A

V

V

N

N

K

K

V

V

C
|
C

G

A

S

S

G

G

L

M

K

K

S

A

L

V

M

M

L

M

A

A

Q

Q

S

A

I

V

K

K

L

A

K

G

D

D

S

V

S

E

L

A

I

I

I

V

A

A

G

G

M

M

E

E

S

N

M

M

S

S

N

Q

A

V

P

P

Y

H

Y

Y

L

I

S

D

K

-

A

G

R

R

F

N

G

G

Y

V

R

K

M

L

G

G

D

D

G

I

R

K

A

L

I

Q

D

D

G

G

M

L

I

L

F

K

D

D

G

G

L

L

W

T

D

D

V

V

Y

Y

N

S

N

K

V

Q

H

H

M

M

G

G

Y

N

L

C

A

A

E

E

M

L

V

C

A

A

K

K

A

E

K

Y

K

N

I

I

T

T

R

R

K

E

I

E

Q

Q

D

D

D

A

Y

F

A

A

V

I

L

Q

S

S

Y
|
Y

K

E

R

R

A

S

Q

A

H

K

S

A

A

W

E

S

N

E

G

G

V

K

F

F

K

K

E

E

I

V

V

V

P

P

I

V

E

S

I

I

S

P

S

Q

R

R

K

K

G

G

V

E

N

P

V

I

-

F

D

A

R

E

D

D

E

E

P

Y

F

K

R

N

V

V

D

K

F

F

E

D

K

R

I

I

P

P

K

T

L

L

K

P

P

T

A

V

F

F

V

Q

-

K

E

E

D

N

G

G

T

T

I

V

T

T

A
|
A

N

N

A
|
A

S

S

T

T

I

L

S

N

D

D

G

G

A

A

A

S

A

A

F

L

I

V

V

L

A

M

D

S

Y

K

D

E

A

K

I

M

K

E

R

S

F

L

G

G

L

L

E

K

P

P

I

L

A

A

K

K

V

I

V

V

A

S

Y

Y

S

A

E

D

F

A

S

A

L

Q

D

A

P

P

K

E

L

W

F

F

P

T

L

T

A

A

P

P

I

A

G

K

A

A

I

L

E

P

K

I

L

A

L

L

K

A

K

K

T

A

G

N

L

L

D

T

V

I

N

N

D

D

I

I

D

D

L

F

F

F

E

E

I

F

N

N

E

E

A

A

F

F

S

S

C

V

V

V

V

G

L

L

A

A

A

N

L

N

E

K

E

I

L

L

K

G

L

L

D

D

I

A

D

A

R

K

V

V

N

N

V

V

N

N

G

G

A

A

V
|
V

S

A

L

L

G

G

H
|
H

P

P

L

L

G

G

A

S

S

S

G

G

A

S

R

R

L

I

V

I

V

V

S

T

L

L

T

I

R

N

E

V

M

L

R

K

R

Q

R

N

N

N

A

A

K

K

Y

Y

G

G

I

A

A

A

L

I

C
|
C

I

N

G
|
G

G

G

E

G

A

A

V

S

A

A

T

I

L

V

F

I

E

E

R

N

V

I

active site: C88 (= C86), H348 (= H345), C378 (= C375), G380 (= G377)
binding calcium ion: Y182 (= Y181), A243 (= A240), A244 (= A241), A246 (= A243), V344 (= V341)

2f2sA Human mitochondrial acetoacetyl-coa thiolase
46% identity, 99% coverage: 4:389/389 of query aligns to 11:389/389 of 2f2sA

query
sites
2f2sA

V

V

F

V

V

I

V

V

E

S

P

A

L

T

R

R

S

T

P

P

F

I

G

G

G

S

F

F

G

L

G

G

T

S

L

L

S

S

S

L

L

L

S

P

A

A

S

T

E

K

I

L

A

G

S

S

F

I

V

A

V

I

K

Q

E

G

I

A

L

I

S

E

R

K

T

A

G

G

I

I

-

P

-

K

E

E

D

E

V

V

D

K

G

E

L

A

I

Y

M

M

G

G

N

N

V

V

L

L

S

Q

A

G

G

G

V

E

G

G

Q

Q

S

A

P

P

A

T

R

R

Q

Q

V

A

I

V

I

L

K

G

S

A

G

G

L

L

P

P

Y

I

S

S

V

T

N

P

A

C

L

T

T

T

V

I

N

N

K

K

V

V

C
|
C

G

A

S

S

G

G

L

M

K

K

S

A

L

I

M

M

L

M

A

A

A

S

Q

Q

S

S

I

L

K

M

L

C

K

G

D

H

S

Q

S

D

L

V

I

M

I

V

A

A

G

G

M

M

E

E

S

S

M

M

S

S

N

N

A

V

P

P

Y

Y

Y

V

L

M

S

N

K

R

A

G

R

S

F

T

G

P

Y

Y

R

-

M

-

G

G

D

G

G

V

R

K

A

L

I

E

D

D

G

L

M

I

I

V

F

K

D

D

G

G

L
|
L

W

T

D

D

V

V

Y

Y

N

N

N

K

V

I

H
|
H

M
|
M

G

G

Y

S

L

C

A

A

E

E

M

N

V

T

A

A

K

K

A

K

K

L

K

N

I

I

T

A

R

R

K

N

I

E

Q

Q

D

D

D

A

Y

Y

A

A

V

I

L

N

S

S

Y
|
Y

K

T

R

R

A

S

Q

K

H

A

S

A

A

W

E

E

N

A

G

G

V

K

F

F

K

G

E

N

E

E

I

V

V

I

P

P

I

V

E

T

I

V

S

T

S

-

R

-

K

-

G

-

V

-

N

-

V

V

D

K

R

E

D

D

E

E

P

Y

F

K

R
|
R

V
|
V

D
|
D

F

F

E

S

K
|
K

I

V

P

P

K

K

L
|
L

K

K

P

T

A

V

F
|
F

V

Q

-

K

E

E

D

N

G

G

T

T

I

V

T

T

A
|
A

A

A

N

N

A

A

S
|
S

T

T

I

L

S

N

D

D

G

G

A

A

F

L

I

V

V

L

A

M

D

T

Y

A

D

D

A

A

I

A

K

K

R

R

F

L

G

N

L

V

E

T

P

P

I

L

A

A

K

R

V

I

V

V

A

A

Y

F

S

A

E

D

F

A

S

A

L

V

D

E

P

P

K

I

L

D

F

F

P

P

L

I

A

A

P

P

I

V

G

Y

A

A

I

A

E

S

K

M

L

V

L

L

K

K

K

D

T

V

G

G

L

L

D

K

V

K

N

E

D

D

I

I

D

A

L

M

F

W

E

E

I

V

N

N

E

E

A
|
A

F
|
F

S

S

C

L

V

V

L

L

A

A

A

N

L

I

E

K

E

M

L

L

K

E

L

I

D

D

I

P

D

Q

R

K

V

V

N

N

V

I

N

N

G

G

A

A

V

V

S

S

L

L

G

G

H
|
H

P

P

L

I

G

G

A

M

S

S

G

G

A

A

R

R

L

I

V

V

V

G

S

H

L

L

T

T

R

H

E

A

M

L

R

K

R

Q

R

-

N

-

A

G

K

E

Y

Y

G

G

I

L

A

A

A

S

L

I

C
|
C

I

N

G
|
G

G

G

E

G

A

A

V

S

A

A

T

M

L

L

F

I

E

Q

R

K

V

L

active site: C95 (= C86), H347 (= H345), C375 (= C375), G377 (= G377)
binding coenzyme a: C95 (= C86), L153 (= L146), H161 (= H154), M162 (= M155), Y188 (= Y181), R220 (= R219), V221 (= V220), D222 (= D221), K225 (= K224), L229 (= L228), F233 (= F232), A242 (= A240), S246 (= S244), A317 (= A315), F318 (= F316), H347 (= H345)

P24752 Acetyl-CoA acetyltransferase, mitochondrial; Acetoacetyl-CoA thiolase; T2; EC 2.3.1.9 from Homo sapiens (Human) (see 6 papers)
45% identity, 99% coverage: 4:389/389 of query aligns to 42:427/427 of P24752

query
sites
P24752

V

V

F

V

V

I

V

V

E

S

P

A

L

T

R

R

S

T

P

P

F

I

G

G

G

S

F

F

G

L

G

G

T

S

L

L

S

S

S

L

L

L

S

P

A

A

S

T

E

K

I

L

A

G

S

S

F

I

V

A

V

I

K

Q

E

G

I

A

L

I

S

E

R

K

T

A

G

G

I

I

-

P

-

K

E

E

D

E

V

V

D

K

G

E

L

A

I

Y

M

M

G

G

N
|
N

V

V

L

L

S

Q

A

G

G

G

V

E

G

G

Q

Q

S

A

P

P

A

T

R

R

Q

Q

V

A

I

V

I

L

K

G

S

A

G

G

L

L

P

P

Y

I

S

S

V

T

N

P

A

C

L

T

T

T

V

I

N

N

K

K

V

V

C

C

G

A

S

S

G

G

L

M

K

K

S

A

L

I

M

M

L

M

A

A

A

S

Q

Q

S

S

I

L

K

M

L

C

K

G

D

H

S

Q

S

D

L

V

I

M

I

V

A

A

G

G

M

M

E

E

S

S

M

M

S

S

N
|
N

A

V

P

P

Y

Y

Y

V

L

M

S

N

K

R

A

G

R

S

F

T

G

P

Y

Y

R

-

M

-

G

G

D

G

G

V

R

K

A

L

I

E

D

D

G

L

M

I

I

V

F

K

D

D

G
|
G

L

L

W

T

D

D

V

V

Y

Y

N

N

N

K

V

I

H

H

M

M

G

G

Y

S

L

C

A

A

E

E

M

N

V

T

A

A

K

K

A

K

K

L

K

N

I

I

T

A

R

R

K

N

I

E

Q

Q

D

D

D

A

Y

Y

A

A

V

I

L

N

S

S

Y
|
Y

K

T

R

R

A

S

Q

K

H

A

S

A

A

W

E

E

N

A

G

G

V

K

F

F

K

G

E

N

E

E

I

V

V

I

P

P

I

V

E

T

I

V

S

T

S

V

R

K

K

G

G

Q

V

P

N

D

V

V

-

V

D

K

R

E

D

D

E

E

P

Y

F

K

R
|
R

V
|
V

D
|
D

F

F

E

S

K
|
K

I

V

P

P

K

K

L

L

K

K

P

T

A

V

F

F

V

Q

-

K

E

E

D

N

G

G

T

T

I

V

T

T

A
|
A

N

N

A
|
A

S
|
S

T

T

I

L

S

N

D

D

G

G

A

A

F

L

I

V

V

L

A

M

D
x
T

Y

A

D

D

A

A

I
x
A

K

K

R

R

F

L

G

N

L

V

E

T

P

P

I

L

A

A

K

R

V
x
I

V

V

A

A

Y

F

S

A

E

D

F

A

S

A

L

V

D

E

P

P

K

I

L

D

F

F

P

P

L

I

A

A

P

P

I

V

G

Y

A

A

I
x
A

E

S

K

M

L

V

L

L

K

K

K

D

T

V

G

G

L

L

D

K

V

K

N

E

D

D

I

I

D

A

L

M

F

W

E

E

I

V

N

N

E

E

A

A

F

F

S

S

C

L

V

V

L

L

A

A

A

N

L

I

E

K

E

M

L

L

K

E

L

I

D

D

I

P

D

Q

R

K

V

V

N

N

V

I

N

N

G

G

A
|
A

V
|
V

S

S

L

L

G

G

H

H

P

P

L

I

G

G

A

M

S

S

G

G

A

A

R

R

L

I

V

V

V

G

S

H

L

L

T

T

R

H

E

A

M

L

R

K

R

Q

R

-

N

-

A

G

K

E

Y

Y

G

G

I

L

A

A

A

S

L

I

C

C

I

N

G

G

E

G

A

A

V

S

A

A

T

M

L

L

F

I

E

Q

R

K

V

L

N93 (= N53) to S: in 3KTD; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074145
N158 (= N118) to D: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs148639841
G183 (= G145) to R: in 3KTD; no activity; dbSNP:rs120074141
Y219 (= Y181) binding CoA; binding K(+)
RVD 258:260 (= RVD 219:221) binding CoA
K263 (= K224) binding CoA
A280 (= A240) binding K(+)
A281 (= A241) binding K(+)
A283 (= A243) binding K(+)
S284 (= S244) binding CoA
T297 (≠ D257) to M: in 3KTD; decreased protein abundance; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs886041122
A301 (≠ I261) to P: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs1420321267
I312 (≠ V272) to T: in 3KTD; decreased protein stability; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074146
A333 (≠ I293) to P: in 3KTD; loss of protein solubility; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs120074147
A380 (= A340) to T: in 3KTD; decreased protein stability; dbSNP:rs120074140
V381 (= V341) binding K(+)

Sites not aligning to the query:

5 A → P: in dbSNP:rs3741056

2ib8D Crystallographic and kinetic studies of human mitochondrial acetoacetyl-coa thiolase (t2): the importance of potassium and chloride for its structure and function (see paper)
45% identity, 99% coverage: 4:389/389 of query aligns to 8:393/393 of 2ib8D

query
sites
2ib8D

V

V

F

V

V

I

V

V

E

S

P

A

L

T

R

R

S

T

P

P

F

I

G

G

G

S

F

F

G

L

G

G

T

S

L

L

S

S

S

L

L

L

S

P

A

A

S

T

E

K

I

L

A

G

S

S

F

I

V

A

V

I

K

Q

E

G

I

A

L

I

S

E

R

K

T

A

G

G

I

I

-

P

-

K

E

E

D

E

V

V

D

K

G

E

L

A

I

Y

M

M

G

G

N

N

V

V

L

L

S

Q

A

G

G

G

V

E

G

G

Q

Q

S

A

P

P

A

T

R

R

Q

Q

V

A

I

V

I

L

K

G

S

A

G

G

L

L

P

P

Y

I

S

S

V

T

N

P

A

C

L

T

T

T

V

I

N

N

K

K

V

V

C
|
C

G

A

S

S

G

G

L

M

K

K

S

A

L

I

M

M

L

M

A

A

A

S

Q

Q

S

S

I

L

K

M

L

C

K

G

D

H

S

Q

S

D

L

V

I

M

I

V

A

A

G

G

M

M

E

E

S

S

M

M

S

S

N

N

A

V

P

P

Y

Y

Y

V

L

M

S

N

K

R

A

G

R

S

F

T

G

P

Y

Y

R

-

M

-

G

G

D

G

G

V

R

K

A

L

I

E

D

D

G

L

M

I

I

V

F

K

D

D

G

G

L

L

W

T

D

D

V

V

Y

Y

N

N

N

K

V

I

H

H

M

M

G

G

Y

S

L

C

A

A

E

E

M

N

V

T

A

A

K

K

A

K

K

L

K

N

I

I

T

A

R

R

K

N

I

E

Q

Q

D

D

D

A

Y

Y

A

A

V

I

L

N

S

S

Y
|
Y

K

T

R

R

A

S

Q

K

H

A

S

A

A

W

E

E

N

A

G

G

V

K

F

F

K

G

E

N

E

E

I

V

V

I

P

P

I

V

E

T

I

V

S

T

S

V

R

K

K

G

G

Q

V

P

N

D

V

V

-

V

D

K

R

E

D

D

E

E

P

Y

F

K

R

R

V

V

D

D

F

F

E

S

K

K

I

V

P

P

K

K

L

L

K

K

P

T

A

V

F

F

V

Q

-

K

E

E

D

N

G

G

T

T

I

V

T

T

A
|
A

N

N

A
|
A

S
|
S

T

T

I

L

S

N

D

D

G

G

A

A

F

L

I

V

V

L

A

M

D

T

Y

A

D

D

A

A

I

A

K

K

R

R

F

L

G

N

L

V

E

T

P

P

I

L

A

A

K

R

V

I

V

V

A

A

Y

F

S

A

E

D

F

A

S

A

L

V

D

E

P

P

K

I

L

D

F

F

P

P

L

I

A

A

P

P

I

V

G

Y

A

A

I

A

E

S

K

M

L

V

L

L

K

K

K

D

T

V

G

G

L

L

D

K

V

K

N

E

D

D

I

I

D

A

L

M

F

W

E

E

I

V

N

N

E

E

A

A

F

F

S

S

C

L

V

V

L

L

A

A

A

N

L

I

E

K

E

M

L

L

K

E

L

I

D

D

I

P

D

Q

R

K

V

V

N

N

V

I

N

N

G

G

A

A

V
|
V

S

S

L

L

G

G

H
|
H

P

P

L

I

G

G

A

M

S

S

G

G

A

A

R

R

L

I

V

V

V

G

S

H

L

L

T

T

R

H

E

A

M

L

R

K

R

Q

R

-

N

-

A

G

K

E

Y

Y

G

G

I

L

A

A

A

S

L

I

C
|
C

I

N

G
|
G

G

G

E

G

A

A

V

S

A

A

T

M

L

L

F

I

E

Q

R

K

V

L

active site: C92 (= C86), H351 (= H345), C379 (= C375), G381 (= G377)
binding potassium ion: Y185 (= Y181), A246 (= A240), A247 (= A241), A249 (= A243), S250 (= S244), V347 (= V341)

Q9BWD1 Acetyl-CoA acetyltransferase, cytosolic; Acetyl-CoA transferase-like protein; Cytosolic acetoacetyl-CoA thiolase; EC 2.3.1.9 from Homo sapiens (Human) (see 2 papers)
44% identity, 99% coverage: 2:388/389 of query aligns to 6:396/397 of Q9BWD1

query
sites
Q9BWD1

D

D

G

P

V

V

F

V

V

I

V

V

E

S

P

A

L

A

R

R

S

T

P

I

F

I

G

G

G

S

F

F

G

N

G

G

T

A

L

L

S

A

L

V

S

P

A

V

S

Q

E

D

I

L

A

G

S

S

F

T

V

V

V

I

K

K

E

E

I

V

L

L

S

K

R

R

T

A

G

T

I

V

-

A

-

P

E

E

D

D

V

V

D

S

G

E

L

V

I

I

M

F

G

G

N

H

V

V

L

L

S

A

A

A

G

G

V

C

G

G

Q

Q

S

N

P

P

A

V

R

R

Q

Q

V

A

I

S

I

V

K

G

S

A

G

G

L

I

P

P

Y

Y

S

S

V

V

N

P

A

A

L

W

T

S

V

C

N

Q

K

M

V

I

C

C

G

G

S

S

G

G

L

L

K

K

S

A

L

V

M

C

L

L

A

A

A

V

Q

Q

S

S

I

I

K

G

L

I

K

G

D

D

S

S

L

I

I

V

A

A

G

G

M

M

E

E

S

N

M

M

S

S

N

K

A

A

P

P

Y

H

Y

-

L

L

S

A

K

Y

A

L

R

R

F

T

G

G

Y

V

R

K

M

I

G

G

D

E

G

M

R

P

A

L

I

T

D

D

G

S

M

I

I

L

F

C

D

D

G

G

L

L

W

T

D

D

V

A

Y

F

N

H

N

N

V

C

H

H

M

M

G

G

Y

I

L

T

A

A

E

E

M

N

V

V

A

A

K

K

A

K

K

W

K

Q

I

V

T

S

R

R

K

E

I

D

Q

Q

D

D

D

K

Y

V

A

A

V

V

L

L

S

S

Y

Q

K

N

R

R

A

T

Q

E

H

N

S

A

A

Q

E

K

N

A

G

G

V

H

F

F

K

D

E

K

E

E

I

I

V

V

P

P

I

V

E

L

I

V

S

S

S

T

R

R

K
|
K

G

G

V

L

N

I

V

E

V

V

D

K

R

T

D

D

E

E

E

F

P

P

F
x
R

R

H

-

G

V
x
S

D

N

F

I

E

E

K

A

I

M

P

S

K

K

L

L

K

K

P

P

A

Y

F

F

V

L

E

T

D

D

G

G

T

T

-

G

-

T

I

V

T

T

A

P

A

A

N

N

A

A

S
|
S

T

G

I

I

S

N

D

D

G

G

A

A

F

V

I

V

V

L

A

M

D

K

Y

K

D

S

A

E

I

A

K

D

R

K

F

R

G

G

L

L

E

T

P

P

I

L

A

A

K

R

V

I

V

V

A

S

Y

W

S

S

E

Q

F

V

S

G

L

V

D

E

P

P

K

S

L

I

F

M

P

G

L

I

A

G

P

P

I

I

G

P

A

A

I

I

E

K

K

Q

L

A

L

V

K

T

K

K

T

A

G

G

L

W

D

S

V

L

N

E

D

D

I

V

D

D

L

I

F

F

E

E

I

I

N

N

E

E

A

A

F

F

S

A

C

A

V

V

V

S

L

A

A

A

A

I

L

V

E

K

E

E

L

L

K

G

L

L

D

N

I

P

D

E

R

K

V

V

N

N

V

I

N

E

G

G

A

A

V

I

S

A

L

L

G

G

H

H

P

P

L

L

G

G

A

A

S

S

G

G

A

C

R

R

L

I

V

L

V

V

S

T

L

L

T

L

R

H

E

T

M

L

R

E

R

R

R

M

N

G

A

R

K

S

Y

R

G

G

I

V

A

A

L

L

C

C

I

I

G

G

E

M

A

G

V

I

A

A

T

M

L

C

F

V

E

Q

R

R

K211 (= K206) to R: in dbSNP:rs25683
R223 (≠ F218) binding CoA
S226 (≠ V220) binding CoA
S252 (= S244) binding CoA

1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
44% identity, 99% coverage: 2:388/389 of query aligns to 3:393/394 of 1wl4A

query
sites
1wl4A

D

D

G

P

V

V

F

V

V

I

V

V

E

S

P

A

L

A

R

R

S

T

P

I

F

I

G

G

G

S

F

F

G

N

G

G

T

A

L

L

S

A

L

V

S

P

A

V

S

Q

E

D

I

L

A

G

S

S

F

T

V

V

V

I

K

K

E

E

I

V

L

L

S

K

R

R

T

A

G

T

I

V

-

A

-

P

E

E

D

D

V

V

D

S

G

E

L

V

I

I

M

F

G

G

N

H

V

V

L

L

S

A

A

A

G

G

V

C

G

G

Q

Q

S

N

P

P

A

V

R

R

Q

Q

V

A

I

S

I

V

K

G

S

A

G

G

L

I

P

P

Y

Y

S

S

V

V

N

P

A

A

L

W

T

S

V

C

N

Q

K

M

V

I

C
|
C

G

G

S

S

G

G

L

L

K

K

S

A

L

V

M

C

L

L

A

A

A

V

Q

Q

S

S

I

I

K

G

L

I

K

G

D

D

S

S

L

I

I

V

A

A

G

G

M

M

E

E

S

N

M

M

S

S

N

K

A

A

P

P

Y

H

Y

-

L

L

S

A

K

Y

A

L

R

R

F

T

G

G

Y

V

R

K

M

I

G

G

D

E

G

M

R

P

A

L

I

T

D

D

G

S

M

I

I

L

F

C

D

D

G

G

L
|
L

W

T

D

D

V

A

Y

F

N

H

N

N

V

C

H

H

M
|
M

G

G

Y

I

L

T

A

A

E

E

M

N

V

V

A

A

K

K

A

K

K

W

K

Q

I

V

T

S

R

R

K

E

I

D

Q

Q

D

D

D

K

Y

V

A

A

V

V

L

L

S

S

Y

Q

K

N

R

R

A

T

Q

E

H

N

S

A

A

Q

E

K

N

A

G

G

V

H

F

F

K

D

E

K

E

E

I

I

V

V

P

P

I

V

E

L

I

V

S

S

S

T

R

R

K

K

G

G

V

L

N

I

V

E

V

V

D

K

R

T

D

D

E

E

E

F

P

P

F
x
R

R

H

-

G

V

S

D

N

F

I

E

E

K

A

I

M

P

S

K

K

L

L

K

K

P

P

A
x
Y

F

F

V

L

E

T

D

D

G

G

T

T

-

G

-

T

I

V

T

T

A
x
P

A
|
A

N

N

A

A

S
|
S

T

G

I

I

S

N

D

D

G

G

A

A

F

V

I

V

V

L

A

M

D

K

Y

K

D

S

A

E

I

A

K

D

R

K

F

R

G

G

L

L

E

T

P

P

I

L

A

A

K

R

V

I

V

V

A

S

Y

W

S

S

E

Q

F

V

S

G

L

V

D

E

P

P

K

S

L

I

F

M

P

G

L

I

A

G

P

P

I

I

G

P

A

A

I

I

E

K

K

Q

L

A

L

V

K

T

K

K

T

A

G

G

L

W

D

S

V

L

N

E

D

D

I

V

D

D

L

I

F

F

E

E

I

I

N

N

E

E

A
|
A

F
|
F

S

A

C

A

V

V

V

S

L

A

A

A

A

I

L

V

E

K

E

E

L

L

K

G

L

L

D

N

I

P

D

E

R

K

V

V

N

N

V

I

N

E

G

G

A

A

V

I

S

A

L

L

G

G

H
|
H

P

P

L

L

G

G

A

A

S

S

G

G

A

C

R

R

L

I

V

L

V

V

S

T

L

L

T

L

R

H

E

T

M

L

R

E

R

R

R

M

N

G

A

R

K

S

Y

R

G

G

I

V

A

A

L

L

C
|
C

I

I

G
|
G

G

G

E

M

A

G

V

I

A

A

T

M

L

C

F

V

E

Q

R

R

active site: C89 (= C86), H350 (= H345), C380 (= C375), G382 (= G377)
binding coenzyme a: L148 (= L146), M157 (= M155), R220 (≠ F218), Y234 (≠ A231), P245 (≠ A240), A246 (= A241), S249 (= S244), A320 (= A315), F321 (= F316), H350 (= H345)

7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
45% identity, 99% coverage: 4:387/389 of query aligns to 3:390/394 of 7cw5B

query
sites
7cw5B

V

T

F

V

V

I

V

L

E

S

P

A

L

A

R

R

S

T

P

P

F

V

G

G

G

K

F

F

G

G

T

S

L

L

S

K

S

D

L

V

S

K

A

A

S

T

E

E

I

L

A

G

S

G

F

I

V

A

V

I

K

K

E

A

I

A

L

L

S

E

R

R

T

A

G

N

I

V

-

A

E

S

D

D

V

V

D

E

G

E

L

V

I

I

M

F

G

G

N

T

V

V

L

I

S

Q

A

G

G

G

V

Q

G

G

Q

Q

S

I

P

P

A

S

R

R

Q

Q

V

A

I

A

I

R

K

A

S

A

G

G

L

I

P

P

Y

W

S

E

V

V

N

Q

A

T

L

E

T

T

V

V

N

N

K

K

V

V

C
|
C

G

A

S

S

G

G

L

L

K

R

S

A

L

V

M

T

L

L

A

A

A

D

Q

Q

S

I

I

I

K

R

L

T

K

G

D

D

S

Q

S

S

L

L

I

I

I

V

A

A

G

G

M

M

E

E

S

S

M

M

S

S

N

N

A

S

P

P

Y

Y

Y

I

L

L

S

R

K

G

A

A

R

R

F

W

G

G

Y

Y

R

R

M

M

G

G

D

N

G

N

R

E

A

V

I

I

D

D

G

L

M

N

I

V

F

A

D

D

G

G

L
|
L

W

T

D

C

V

A

Y

F

N

S

N

G

V

T

H
|
H

M
|
M

G

G

Y

V

L

Y

A

G

E

G

M

E

V

V

A

A

K

K

A

E

K

D

K

G

I

I

T

S

R

R

K

E

I

A

Q

Q

D

D

D

E

Y

W

A

A

V

Y

L

R

S

S

Y

H

K

Q

R

R

A

A

Q

V

H

S

S

A

A

H

E

K

N

E

G

G

V

R

F

F

K

E

E

E

I

I

V

V

P

P

I

V

E

T

I

I

S

P

S

Q

R

R

K

K

G

G

V

D

N

P

-

I

V

V

D

A

R

K

D

D

E

E

E

A

P

P

F
x
R

R

E

-

D

V
x
T

D

T

F

I

E

E

K

K

I

L

P

A

K

K

L

L

K

K

P

P

A

V

F

F

V

D

E

K

D

T

G

A

T

T

I

V

T

T

A
|
A

A

G

N

N

A

A

S
x
P

T

G

I
x
L

S

N

D

D

G

G

A

G

A

A

F

L

I

V

V

L

A

M

D

S

Y

E

D

D

A

R

I

A

K

K

R

Q

F

E

G

G

L

R

E

K

P

P

I

L

A

A

K

T

V

I

V

L

A

A

Y

H

S

T

E

A

F

I

S

A

L

V

D

E

P

S

K

K

L

D

F

F

P

P

L

R

A

T

P

P

I

G

G

Y

A

A

I

I

E

N

K

A

L

L

K

E

K

K

T

T

G

G

L

K

D

T

V

I

N

E

D

D

I

I

D

D

L

L

F

F

E

E

I

I

N

N

E

E

A

A

F

F

S

A

C

A

V

V

V

A

L

I

A

A

A

S

L

T

E

E

E

I

L

A

K

G

L

I

D

D

I

P

D

E

R

K

V

L

N

N

V

V

N

N

G

G

A

A

V

V

S

A

L

M

G

G

H
|
H

P

P

L

I

G

G

A

A

S

S

G

G

A

A

R

R

L

I

V

I

V

V

S

T

L

L

T

I

R

H

E

A

M

L

R

K

R

Q

R

R

N

G

A

G

K

G

Y

I

G

G

I

I

A

A

A

S

L

I

C
|
C

I

S

G
|
G

G

G

E

Q

A

G

V

D

A

A

T

V

L

M

F

I

E

E

active site: C87 (= C86), H348 (= H345), C378 (= C375), G380 (= G377)
binding coenzyme a: L147 (= L146), H155 (= H154), M156 (= M155), R220 (≠ F218), T223 (≠ V220), A243 (= A240), P247 (≠ S244), L249 (≠ I246), H348 (= H345)

5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
47% identity, 100% coverage: 1:388/389 of query aligns to 3:394/394 of 5f38D

query
sites
5f38D

M

M

D

K

G

N

V

C

F

V

V

I

V

V

E

S

P

A

L

V

R

R

S

T

P

A

F

I

G

G

G

S

F

F

G

N

G

G

T

S

L

L

S

A

S

S

L

T

S

S

A

A

S

I

E

D

I

L

A

G

S

A

F

T

V

V

V

I

K

K

E

A

I

A

L

I

S

E

R

R

T

A

G

K

I

I

-

D

-

S

E

Q

D

H

V

V

D

D

G

E

L

V

I

I

M

M

G

G

N

N

V

V

L

L

S

Q

A

A

G

G

V

L

G

G

Q

Q

S

N

P

P

A

A

R

R

Q

Q

V

A

I

L

K

K

S

S

G

G

L

L

P

A

Y

E

S

T

V

V

N

C

A

G

L

F

T

T

V

V

N

N

K

K

V

V

C
|
C

G

G

S

S

G

G

L

L

K

K

S

S

L

V

M

A

L

L

A

A

Q

Q

S

A

I

I

K

Q

L

A

K

G

D

Q

S

A

S

Q

L

S

I

I

I

V

A

A

G

G

M

M

E

E

S

N

M

M

S

S

N

L

A

A

P

P

Y

Y

Y

L

L

L

-

D

S

A

K

K

A

A

R

R

F

S

G

G

Y

Y

R

R

M

L

G

G

D

D

G

G

R

Q

A

V

I

Y

D

D

G

V

M

I

I

L

F

R

D

D

G

G

L
|
L

W

M

D

C

V

A

Y

T

N

H

N

G

V

Y

H

H

M

M

G

G

Y

I

L

T

A

A

E

E

M

N

V

V

A

A

K

K

A

E

K

Y

K

G

I

I

T

T

R

R

K

E

I

M

Q

Q

D

D

D

E

Y

L

A

A

V

L

L

H

S

S

Y

Q

K

R

R

K

A

A

Q

A

H

A

S

A

A

I

E

E

N

S

G

G

V

A

F

F

K

T

E

A

E

E

I

I

V

V

P

P

I

V

E

N

I

V

S

V

S

T

R

R

K

K

G

K

V

T

N

F

V

V

V

F

D

S

R

Q

D

D

E

E

E

F

P

P

-

K

F

A

R

N

V

S

D

T

F

A

E

E

K

A

I

L

P

G

K

A

L

L

K

R

P

P

A

A

F

F

V

D

E

K

D

A

G

G

T

T

I

V

T

T

A
|
A

A

G

N

N

A

A

S
|
S

T

G

I
|
I

S

N

D

D

G

G

A

A

F

L

I

V

V

I

A

M

D

E

Y

E

D

S

A

A

I

A

K

L

R

A

F

A

G

G

L

L

E

T

P

P

I

L

A

A

K

R

V

I

V

K

A

S

Y

Y

S

A

E

S

F

G

S

G

L

V

D

P

P

P

K

A

L

L

F

M

P

G

L

M

A

G

P

P

I

V

G

P

A

A

I

T

E

Q

K

K

L

A

L

L

K

Q

K

L

T

A

G

G

L

L

D

Q

V

L

N

A

D

D

I

I

D

D

L

L

F

I

E

E

I

A

N

N

E

E

A
|
A

F
|
F

S

A

C

A

V

Q

V

F

L

L

A

A

A

V

L

G

E

K

E

N

L

L

K

G

L

F

D

D

I

S

D

E

R

K

V

V

N

N

V

V

N

N

G

G

A

A

V

I

S
x
A

L

L

G

G

H
|
H

P

P

L

I

G

G

A

A

S

S

G

G

A

A

R

R

L

I

V

L

V

V

S

T

L

L

T

L

R

H

E

A

M

M

R

Q

R

A

R

R

N

D

A

K

K

T

Y

L

G

G

I

L

A
|
A

A

T

L
|
L

C

C

I

I

G

G

E

Q

A

G

V

I

A

A

T

M

L

V

F

I

E

E

R

R

active site: C90 (= C86), A348 (≠ S342), A378 (= A372), L380 (= L374)
binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C86), L151 (= L146), A246 (= A240), S250 (= S244), I252 (= I246), A321 (= A315), F322 (= F316), H351 (= H345)

Q22100 Acetyl-CoA acetyltransferase homolog, mitochondrial; 3-ketoacyl-CoA thiolase; EC 2.3.1.- from Caenorhabditis elegans (see 2 papers)
44% identity, 99% coverage: 5:389/389 of query aligns to 25:407/407 of Q22100

query
sites
Q22100

F

F

V

I

V

V

E

G

P

A

L

A

R

R

S

T

P

P

F

I

G

G

G

S

F

F

G

R

G

S

T

S

L

L

S

S

L

V

S

T

A

A

S

P

E

E

I

L

A

A

S

S

F

V

V

A

V

I

K

K

E

A

I

A

L

L

S

E

R

R

T

G

G

A

I

V

E

K

-

P

-

S

D

S

V

I

D

Q

G

E

L

V

I

F

M

L

G

G

N

Q

V

V

L

C

S

Q

A

A

G

N

V

A

G

G

Q

Q

S

A

P

P

A

A

R

R

Q

Q

V

A

I

A

I

L

K

G

S

A

G

G

L

L

P

D

Y

L

S

S

V

V

N

A

A

V

L

T

T

T

V

V

N

N

K

K

V

V

C

C

G

S

S

S

G

G

L

L

K

K

S

A

L

I

M

I

L

L

A

A

A
|
A

Q

Q

S

Q

I

I

K

Q

L

T

K

G

D

H

S

Q

S

D

L

F

I

A

I

I

A

G

G

G

M

M

E

E

S

S

M

M

S

S

N

Q

A

V

P

P

Y

F

Y

Y

L

V

S

Q

K

R

A

G

R

E

F

I

G

P

Y

Y

R

-

M

-

G

G

D

G

G

F

R

Q

A

V

I

I

D

D

G

G

M

I

I

V

F

K

D

D

G

G

L

L

W

T

D

D

V

A

Y

Y

N

D

N

K

V

V

H

H

M

M

G

G

Y

N

L

C

A

G

E

E

M

K

V

T

A

S

K

K

A

E

K

M

K

G

I

I

T

T

R

R

K

K

I

D

Q

Q

D

D

D

E

Y

Y

A

A

V

I

L

N

S

S

Y

Y

K

K

R

K

A

S

Q

A

H

K

S

A

A

W

E

E

N

N

G

G

V

N

F

I

K

G

E

P

E

E

I

V

V

V

P

P

I

V

E

N

I

V

S

K

S

S

R

K

K

K

G

G

V

V

N

T

V

I

V

V

D

D

R

K

D

D

E

E

P

F

F

T

R

K

V

V

D

N

F

F

E

D

K

K

I

F

P

T

K

S

L

L

K

R

P

T

A

V

F

F

V

Q

E

K

D

D

G

G

T

T

I

I

T

T

A

A

N

N

A

A

S

S

T

T

I

L

S

N

D

D

G

G

A

A

F

V

I

I

V

V

A

A

D

S

Y

Q

D

E

A

A

I

V

K

S

R

E

F

Q

G

S

L

L

E

K

P

P

I

L

A

A

K

R

V

I

V

L

A

A

Y

Y

S

G

E

D

F

A

S

A

L

T

D

H

P

P

K

L

L

D

F

F

P

A

L

V

A

A

P

P

I

T

G

L

A

M

I

F

E

P

K

K

L

I

L

L

K

E

K

R

T

A

G

G

L

V

D

K

V

Q

N

S

D

D

I

V

D

A

L

Q

F

W

E

E

I

V

N

N

E

E

A

A

F

F

S

S

C

C

V

V

V

P

L

L

A

A

A

F

L

I

E

K

L

L

K

G

L

V

D

D

I

P

D

S

R

L

V

V

N

N

V

P

N

H

G

G

A

A

V

V

S

S

L

I

G

G

H

H

P

P

L

I

G

G

A

M

S

S

G

G

A

A

R

R

L

L

V

I

V

T

S

H

L

L

T

V

R

H

E

T

M

L

R

-

R

K

N

S

A

G

K

Q

Y

I

G

G

I

V

A

A

L

I

C

C

I

N

G

G

E

G

A

S

V

S

A

G

T

M

L

V

F

I

E

Q

R

K

V

L

A119 (= A97) mutation to P: In mg368; increased uptake of the lipophilic dye Nile Red and the synthetic fatty acid analog C1-BODIPY-C12.

5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
46% identity, 100% coverage: 1:389/389 of query aligns to 1:391/391 of 5f38B

query
sites
5f38B

M

M

D

K

G

N

V

C

F

V

V

I

V

V

E

S

P

A

L

V

R

R

S

T

P

A

F

I

G

G

G

S

F

F

G

N

G

G

T

S

L

L

S

A

S

S

L

T

S

S

A

A

S

I

E

D

I

L

A

G

S

A

F

T

V

V

V

I

K

K

E

A

I

A

L

I

S

E

R

R

T

A

G

K

I

I

-

D

-

S

E

Q

D

H

V

V

D

D

G

E

L

V

I

I

M

M

G

G

N

N

V

V

L

L

S

Q

A

A

G

G

V

L

G

G

Q

Q

S

N

P

P

A

A

R

R

Q

Q

V

A

I

L

K

K

S

S

G

G

L

L

P

A

Y

E

S

T

V

V

N

C

A

G

L

F

T

T

V

V

N

N

K

K

V

V

C
|
C

G

G

S

S

G

G

L

L

K

K

S

S

L

V

M

A

L

L

A

A

Q

Q

S

A

I

I

K

Q

L

A

K

G

D

Q

S

A

S

Q

L

S

I

I

I

V

A

A

G

G

M

M

E

E

S

N

M

M

S

S

N

L

A

A

P

P

Y

Y

Y

L

L

L

-

D

S

A

K

K

A

A

R

R

F

S

G

G

Y

Y

R

R

M

L

G

G

D

D

G

G

R

Q

A

V

I

Y

D

D

G

V

M

I

I

L

F

R

D

D

G

G

L
|
L

W

M

D

C

V

A

Y

T

N

H

N

G

V

Y

H

H

M

M

G

G

Y

I

L

T

A

A

E

E

M

N

V

V

A

A

K

K

A

E

K

Y

K

G

I

I

T

T

R

R

K

E

I

M

Q

Q

D

D

D

E

Y

L

A

A

V

L

L

H

S

S

Y

Q

K

R

R

K

A

A

Q

A

H

A

S

A

A

I

E

E

N

S

G

G

V

A

F

F

K

T

E

A

E

E

I

I

V

V

P

P

I

V

E

N

I

V

S

V

S

T

R

K

K

-

G

-

V

T

N

F

V

V

V

F

D

S

R

Q

D

D

E

E

E

F

P

P

-
x
K

F

A

R

N

V

S

D

T

F

A

E

E

K

A

I

L

P

G

K

A

L

L

K

R

P

P

A

A

F
|
F

V

D

E

K

D

A

G

G

T

T

I

V

T

T

A
|
A

A

G

N

N

A

A

S
|
S

T

G

I

I

S

N

D

D

G

G

A

A

F

L

I

V

V

I

A

M

D

E

Y

E

D

S

A

A

I

A

K

L

R

A

F

A

G

G

L

L

E

T

P

P

I

L

A

A

K

R

V

I

V

K

A

S

Y

Y

S

A

E

S

F

G

S

G

L

V

D

P

P

P

K

A

L

L

F

M

P

G

L

M

A

G

P

P

I

V

G

P

A

A

I

T

E

Q

K

K

L

A

L

L

K

Q

K

L

T

A

G

G

L

L

D

Q

V

L

N

A

D

D

I

I

D

D

L

L

F

I

E

E

I

A

N

N

E

E

A
|
A

F
|
F

S

A

C

A

V

Q

V

F

L

L

A

A

A

V

L

G

E

K

E

N

L

L

K

G

L

F

D

D

I

S

D

E

R

K

V

V

N

N

V

V

N

N

G

G

A

A

V

I

S

A

L

L

G

G

H
|
H

P

P

L

I

G

G

A

A

S

S

G

G

A

A

R

R

L

I

V

L

V

V

S

T

L

L

T

L

R

H

E

A

M

M

R

Q

R

A

R

R

N

D

A

K

K

T

Y

L

G

G

I

L

A

A

A

T

L

L

C
|
C

I

I

G
|
G

G

G

E

Q

A

G

V

I

A

A

T

M

L

V

F

I

E

E

R

R

V

L

active site: C88 (= C86), H347 (= H345), C377 (= C375), G379 (= G377)
binding coenzyme a: C88 (= C86), L149 (= L146), K219 (vs. gap), F234 (= F232), A242 (= A240), S246 (= S244), A317 (= A315), F318 (= F316), H347 (= H345)

P41338 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Ergosterol biosynthesis protein 10; EC 2.3.1.9 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
45% identity, 99% coverage: 4:389/389 of query aligns to 5:398/398 of P41338

query
sites
P41338

V

V

F

Y

V

I

V

V

E

S

P

T

L

A

R

R

S

T

P

P

F

I

G

G

G

S

F

F

G

Q

G

G

T

S

L

L

S

S

L

K

S

T

A

A

S

V

E

E

I

L

A

G

S

A

F

V

V

A

V

L

K

K

E

G

I

A

L

L

S

A

R

K

T

V

-

P

-

E

-

L

-

D

G

A

I

S

E

K

D

D

V

F

D

D

G

E

L

I

I

I

M

F

G

G

N

N

V

V

L

L

S

S

A

A

G

N

V

L

G

G

Q

Q

S

A

P

P

A

A

R

R

Q

Q

V

V

I

A

I

L

K

A

S

A

G

G

L

L

P

S

Y

N

S

H

V

I

N

V

A

A

L

S

T

T

V

V

N

N

K

K

V

V

C

C

G

A

S

S

G

A

L

M

K

K

S

A

L

I

M

I

L

L

A

G

A

A

Q

Q

S

S

I

I

K

K

L

C

K

G

D

N

S

A

S

D

L

V

I

V

A

A

G

G

M

C

E

E

S

S

M

M

S

T

N

N

A

A

P

P

Y

Y

L

M

S

P

K

A

A

A

R

R

F

A

G

G

Y

A

R

K

M

F

G

G

D

Q

G

T

R

V

A

L

I

V

D

D

G

G

M

V

I

E

F

R

D

D

G

G

L

L

W

N

D

D

V

A

Y

Y

N

D

N

G

V

L

H

A

M

M

G

G

Y

V

L

H

A

A

E

E

M

K

V

C

A

A

K

R

A

D

K

W

K

D

I

I

T

T

R

R

K

E

I

Q

Q

Q

D

D

D

N

Y

F

A

A

V

I

L

E

S

S

Y

Y

K

Q

R

K

A

S

Q

Q

H

K

S

S

A

Q

E

K

N

E

G

G

V

K

F

F

K

D

E

N

E

E

I

I

V

V

P

P

I

V

E

T

I

I

S

K

S

G

R

F

K

R

G

G

V

K

-

P

-

D

N

T

V

Q

V

V

D

T

R

K

D

D

E

E

P

P

F

A

R

R

V

L

D

H

F

V

E

E

K

K

I

L

P

R

K

S

L

A

K

R

P

T

A

V

F

F

V

Q

-

K

E

E

D

N

G

G

T

T

I

V

T

T

A

A

N

N

A

A

S

S

T

P

I

I

S

N

D

D

G

G

A

A

F

V

I

I

V

L

A

V

D

S

Y

E

D

K

A

V

I

L

K

K

R

E

F

K

G

N

L

L

E

K

P

P

I

L

A

A

K

I

V

I

V

K

A

G

Y

W

S

G

E

E

F

A

S

A

L

H

D

Q

P

P

K

A

L

D

F

F

P

T

L

W

A

A

P

P

I

S

G

L

A

A

I

V

E

P

K

K

L

A

L

L

K

K

K

H

T

A

G

G

L

I

-

E

D

D

V

I

N

N

D

S

I

V

D

D

L

Y

F

F

E

E

I

F

N

N

E

E

A

A

F

F

S

S

C

V

V

V

V

G

L

L

A

V

A

N

L

T

E

K

E

I

L

L

K

K

L

L

D

D

I

P

D

S

R

K

V

V

N

N

V

V

N

Y

G

G

A

A

V

V

S

A

L

L

G

G

H

H

P

P

L

L

G

G

A

C

S

S

G

G

A

A

R

R

L

V

V

V

S

T

L

L

T

L

R

S

E

I

M

L

R

Q

R

E

N

G

A

G

K

K

Y

I

G

G

I

V

A

A

L

I

C

C

I

N

G

G

E

G

A

A

V

S

A

S

T

I

L

V

F

I

E

E

R

K

V

I

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylserine

2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
43% identity, 99% coverage: 4:387/389 of query aligns to 2:387/389 of 2vu2A

query
sites
2vu2A

V

I

F

V

V

I

V

A

E

S

P

A

L

A

R

R

S

T

P

A

F

V

G

G

G

S

F

F

G

N

G

G

T

A

L

F

S

A

S

N

L

T

S

P

A

A

S

H

E

E

I

L

A

G

S

A

F

T

V

V

V

I

K

S

E

A

I

V

L

L

S

E

R

R

T

A

G

G

I

V

E

A

-

A

-

G

D

E

V

V

D

N

G

E

L

V

I

I

M

L

G

G

N

Q

V

V

L

L

S

P

A

A

G

G

V

E

G

G

Q

Q

S

N

P

P

A

A

R

R

Q

Q

V

A

I

A

I

M

K

K

S

A

G

G

L

V

P

P

Y

Q

S

E

V

A

N

T

A

A

L

W

T

G

V

M

N

N

K

Q

V

L

C
|
C

G

G

S

S

G

G

L

L

K

R

S

A

L

V

M

A

L

L

A

G

A

M

Q

Q

S

Q

I

I

K

A

L

T

K

G

D

D

S

A

S

S

L

I

I

I

I

V

A

A

G

G

M

M

E

E

S

S

M

M

S

S

N

M

A

A

P

P

Y

H

Y

-

L

C

S

A

K

H

A

L

R

R

F

G

G

G

Y

V

R

K

M

M

G

G

D

D

G

F

R

K

A

M

I

I

D

D

G

T

M

M

I

I

F

K

D

D

G

G

L

L

W

T

D

D

V

A

Y

F

N

Y

N

G

V

Y

H
|
H

M
|
M

G

G

Y

T

L

T

A

A

E

E

M

N

V

V

A

A

K

K

A

Q

K

W

K

Q

I

L

T

S

R

R

K

D

I

E

Q

Q

D

D

D

A

Y

F

A

A

V

V

L

A

S

S

Y

Q

K

N

R

K

A

A

Q

E

H

A

S

A

A

Q

E

K

N

D

G

G

V

R

F

F

K

K

E

D

E

E

I

I

V

V

P

P

I

F

E

I

I

V

S

K

S

G

R

R

K

K

G

G

V

D

N

I

V

T

V

V

D

D

R

A

D

D

E

E

E

Y

-

I

P

R

F

H

R

G

V

A

D

T

F

L

E

D

K

S

I

M

P

A

K

K

L

L

K

R

P

P

A

A

F
|
F

V

D

E

K

D

E

G

G

T

T

I

V

T

T

A

A

A

G

N

N

A

A

S
|
S

T
x
G

I

L

S

N

D

D

G

G

A

A

F

A

I

L

V

L

A

M

D

S

Y

E

D

A

A

E

I

A

K

S

R

R

F

R

G

G

L

I

E

Q

P

P

I

L

A

G

K

R

V

I

V

V

A

S

Y

W

S

A

E

T

F

V

S

G

L

V

D

D

P

P

K

K

L

V

F

M

P

G

L

T

A

G

P

P

I

I

G

P

A

A

I

S

E

R

K

K

L

A

L

L

K

E

K

R

T

A

G

G

L

W

D

K

V

I

N

G

D

D

I

L

D

D

L

L

F

V

E

E

I

A

N

N

E

E

A

A

F
|
F

S

A

C

A

V

Q

V

A

L

C

A

A

A

V

L

N

E

K

E

D

L

L

K

G

L

W

D

D

I

P

D

S

R

I

V

V

N

N

V

V

N

N

G

G

A

A

V

I

S

A

L

I

G

G

H
|
H

P

P

L

I

G

G

A

A

S

S

G

G

A

A

R

R

L

I

V

L

V

N

S

T

L

L

T

L

R

F

E

E

M

M

R

K

R

R

N

G

A

A

K

R

Y

K

G

G

I

L

A

A

A

T

L

L

C
|
C

I

I

G
|
G

G

G

E

M

A

G

V

V

A

A

T

M

L

C

F

I

E

E

active site: C86 (= C86), H345 (= H345), C375 (= C375), G377 (= G377)
binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (= H154), M154 (= M155), F232 (= F232), S244 (= S244), G245 (≠ T245), F316 (= F316), H345 (= H345)

1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
43% identity, 99% coverage: 4:387/389 of query aligns to 2:387/389 of 1dm3A

query
sites
1dm3A

V

I

F

V

V

I

V

A

E

S

P

A

L

A

R

R

S

T

P

A

F

V

G

G

G

S

F

F

G

N

G

G

T

A

L

F

S

A

S

N

L

T

S

P

A

A

S

H

E

E

I

L

A

G

S

A

F

T

V

V

V

I

K

S

E

A

I

V

L

L

S

E

R

R

T

A

G

G

I

V

E

A

-

A

-

G

D

E

V

V

D

N

G

E

L

V

I

I

M

L

G

G

N

Q

V

V

L

L

S

P

A

A

G

G

V

E

G

G

Q

Q

S

N

P

P

A

A

R

R

Q

Q

V

A

I

A

I

M

K

K

S

A

G

G

L

V

P

P

Y

Q

S

E

V

A

N

T

A

A

L

W

T

G

V

M

N

N

K

Q

V

L

C
|
C

G

G

S

S

G

G

L

L

K

R

S

A

L

V

M

A

L

L

A

G

A

M

Q

Q

S

Q

I

I

K

A

L

T

K

G

D

D

S

A

S

S

L

I

I

I

I

V

A

A

G

G

M

M

E

E

S

S

M

M

S

S

N

M

A

A

P

P

Y

H

Y

-

L

C

S

A

K

H

A

L

R

R

F

G

G

G

Y

V

R

K

M

M

G

G

D

D

G

F

R

K

A

M

I

I

D

D

G

T

M

M

I

I

F

K

D

D

G

G

L
|
L

W

T

D

D

V

A

Y

F

N

Y

N

G

V

Y

H
|
H

M
|
M

G

G

Y

T

L

T

A

A

E

E

M

N

V

V

A

A

K

K

A

Q

K

W

K

Q

I

L

T

S

R

R

K

D

I

E

Q

Q

D

D

D

A

Y

F

A

A

V

V

L

A

S

S

Y

Q

K

N

R

K

A

A

Q

E

H

A

S

A

A

Q

E

K

N

D

G

G

V

R

F

F

K

K

E

D

E

E

I

I

V

V

P

P

I

F

E

I

I

V

S

K

S

G

R

R

K

K

G

G

V

D

N

I

V

T

V

V

D

D

R

A

D

D

E

E

E

Y

-

I

P
x
R

F

H

R

G

V

A

D

T

F

L

E

D

K
x
S

I
x
M

P

A

K

K

L

L

K

R

P

P

A

A

F

F

V

D

E

K

D

E

G

G

T

T

I

V

T

T

A
|
A

A

G

N

N

A

A

S
|
S

T

G

I

L

S

N

D

D

G

G

A

A

F

A

I

L

V

L

A

M

D

S

Y

E

D

A

A

E

I

A

K

S

R

R

F

R

G

G

L

I

E

Q

P

P

I

L

A

G

K

R

V

I

V

V

A

S

Y

W

S

A

E

T

F

V

S

G

L

V

D

D

P

P

K

K

L

V

F
x
M

P

G

L

T

A

G

P

P

I

I

G

P

A

A

I

S

E

R

K

K

L

A

L

L

K

E

K

R

T

A

G

G

L

W

D

K

V

I

N

G

D

D

I

L

D

D

L

L

F

V

E

E

I

A

N

N

E

E

A
|
A

F
|
F

S

A

C

A

V

Q

V

A

L

C

A

A

A

V

L

N

E

K

E

D

L

L

K

G

L

W

D

D

I

P

D

S

R

I

V

V

N

N

V

V

N

N

G

G

A

A

V

I

S

A

L

I

G

G

H
|
H

P

P

L

I

G

G

A

A

S

S

G

G

A

A

R

R

L

I

V

L

V

N

S

T

L

L

T

L

R

F

E

E

M

M

R

K

R

R

N

G

A

A

K

R

Y

K

G

G

I

L

A

A

A

T

L

L

C
|
C

I

I

G
|
G

G

G

E

M

A

G

V

V

A

A

T

M

L

C

F

I

E

E

active site: C86 (= C86), H345 (= H345), C375 (= C375), G377 (= G377)
binding acetyl coenzyme *a: C86 (= C86), L145 (= L146), H153 (= H154), M154 (= M155), R217 (≠ P217), S224 (≠ K224), M225 (≠ I225), A240 (= A240), S244 (= S244), M285 (≠ F285), A315 (= A315), F316 (= F316), H345 (= H345), C375 (= C375)

1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
43% identity, 99% coverage: 4:387/389 of query aligns to 2:387/389 of 1dlvA

query
sites
1dlvA

V

I

F

V

V

I

V

A

E

S

P

A

L

A

R

R

S

T

P

A

F

V

G

G

G

S

F

F

G

N

G

G

T

A

L

F

S

A

S

N

L

T

S

P

A

A

S

H

E

E

I

L

A

G

S

A

F

T

V

V

V

I

K

S

E

A

I

V

L

L

S

E

R

R

T

A

G

G

I

V

E

A

-

A

-

G

D

E

V

V

D

N

G

E

L

V

I

I

M

L

G

G

N

Q

V

V

L

L

S

P

A

A

G

G

V

E

G

G

Q

Q

S

N

P

P

A

A

R

R

Q

Q

V

A

I

A

I

M

K

K

S

A

G

G

L

V

P

P

Y

Q

S

E

V

A

N

T

A

A

L

W

T

G

V

M

N

N

K

Q

V

L

C
|
C

G

G

S

S

G

G

L

L

K

R

S

A

L

V

M

A

L

L

A

G

A

M

Q

Q

S

Q

I

I

K

A

L

T

K

G

D

D

S

A

S

S

L

I

I

I

I

V

A

A

G

G

M

M

E

E

S

S

M

M

S

S

N

M

A

A

P

P

Y

H

Y

-

L

C

S

A

K

H

A

L

R

R

F

G

G

G

Y

V

R

K

M

M

G

G

D

D

G

F

R

K

A

M

I

I

D

D

G

T

M

M

I

I

F

K

D

D

G

G

L
|
L

W

T

D

D

V

A

Y

F

N

Y

N

G

V

Y

H
|
H

M
|
M

G

G

Y

T

L

T

A

A

E

E

M

N

V

V

A

A

K

K

A

Q

K

W

K

Q

I

L

T

S

R

R

K

D

I

E

Q

Q

D

D

D

A

Y

F

A

A

V

V

L

A

S

S

Y

Q

K

N

R

K

A

A

Q

E

H

A

S

A

A

Q

E

K

N

D

G

G

V

R

F

F

K

K

E

D

E

E

I

I

V

V

P

P

I

F

E

I

I

V

S

K

S

G

R

R

K

K

G

G

V

D

N

I

V

T

V

V

D

D

R

A

D

D

E

E

E

Y

-

I

P
x
R

F

H

R

G

V

A

D

T

F

L

E

D

K

S

I

M

P

A

K

K

L
|
L

K

R

P

P

A

A

F

F

V

D

E

K

D

E

G

G

T

T

I

V

T

T

A
|
A

A

G

N

N

A

A

S
|
S

T

G

I

L

S

N

D

D

G

G

A

A

F

A

I

L

V

L

A

M

D

S

Y

E

D

A

A

E

I

A

K

S

R

R

F

R

G

G

L

I

E

Q

P

P

I

L

A

G

K

R

V

I

V

V

A

S

Y

W

S

A

E

T

F

V

S

G

L

V

D

D

P

P

K

K

L

V

F

M

P

G

L

T

A

G

P

P

I

I

G

P

A

A

I

S

E

R

K

K

L

A

L

L

K

E

K

R

T

A

G

G

L

W

D

K

V

I

N

G

D

D

I

L

D

D

L

L

F

V

E

E

I

A

N

N

E

E

A

A

F

F

S

A

C

A

V

Q

V

A

L

C

A

A

A

V

L

N

E

K

E

D

L

L

K

G

L

W

D

D

I

P

D

S

R

I

V

V

N

N

V

V

N

N

G

G

A

A

V

I

S

A

L

I

G

G

H
|
H

P

P

L

I

G

G

A

A

S

S

G

G

A

A

R

R

L

I

V

L

V

N

S

T

L

L

T

L

R

F

E

E

M

M

R

K

R

R

N

G

A

A

K

R

Y

K

G

G

I

L

A

A

A

T

L

L

C
|
C

I

I

G
|
G

G

G

E

M

A

G

V

V

A

A

T

M

L

C

F

I

E

E

active site: C86 (= C86), H345 (= H345), C375 (= C375), G377 (= G377)
binding coenzyme a: C86 (= C86), L145 (= L146), H153 (= H154), M154 (= M155), R217 (≠ P217), L228 (= L228), A240 (= A240), S244 (= S244), H345 (= H345)

1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
43% identity, 99% coverage: 4:387/389 of query aligns to 5:390/392 of 1ou6A

query
sites
1ou6A

V

I

F

V

V

I

V

A

E

S

P

A

L

A

R

R

S

T

P

A

F

V

G

G

G

S

F

F

G

N

G

G

T

A

L

F

S

A

S

N

L

T

S

P

A

A

S

H

E

E

I

L

A

G

S

A

F

T

V

V

V

I

K

S

E

A

I

V

L

L

S

E

R

R

T

A

G

G

I

V

E

A

-

A

-

G

D

E

V

V

D

N

G

E

L

V

I

I

M

L

G

G

N

Q

V

V

L

L

S

P

A

A

G

G

V

E

G

G

Q

Q

S

N

P

P

A

A

R

R

Q

Q

V

A

I

A

I

M

K

K

S

A

G

G

L

V

P

P

Y

Q

S

E

V

A

N

T

A

A

L

W

T

G

V

M

N

N

K

Q

V

L

C
|
C

G

G

S

S

G

G

L

L

K

R

S

A

L

V

M

A

L

L

A

G

A

M

Q

Q

S

Q

I

I

K

A

L

T

K

G

D

D

S

A

S

S

L

I

I

I

I

V

A

A

G

G

M

M

E

E

S

S

M

M

S

S

N

M

A

A

P

P

Y

H

Y

-

L

C

S

A

K

H

A

L

R

R

F

G

G

G

Y

V

R

K

M

M

G

G

D

D

G

F

R

K

A

M

I

I

D

D

G

T

M

M

I

I

F

K

D

D

G

G

L
|
L

W

T

D

D

V

A

Y

F

N

Y

N

G

V

Y

H
|
H

M
|
M

G

G

Y

T

L

T

A

A

E

E

M

N

V

V

A

A

K

K

A

Q

K

W

K

Q

I

L

T

S

R

R

K

D

I

E

Q

Q

D

D

D

A

Y

F

A

A

V

V

L

A

S

S

Y

Q

K

N

R

K

A

A

Q

E

H

A

S

A

A

Q

E

K

N

D

G

G

V

R

F

F

K

K

E

D

E

E

I

I

V

V

P

P

I

F

E

I

I

V

S

K

S

G

R

R

K

K

G

G

V

D

N

I

V

T

V

V

D

D

R

A

D

D

E

E

E

Y

-

I

P

R

F

H

R

G

V

A

D

T

F

L

E

D

K

S

I

M

P

A

K

K

L

L

K

R

P

P

A

A

F
|
F

V

D

E

K

D

E

G

G

T

T

I

V

T

T

A
|
A

A

G

N

N

A

A

S
|
S

T

G

I

L

S

N

D

D

G

G

A

A

F

A

I

L

V

L

A

M

D

S

Y

E

D

A

A

E

I

A

K

S

R

R

F

R

G

G

L

I

E

Q

P

P

I

L

A

G

K

R

V

I

V

V

A

S

Y

W

S

A

E

T

F

V

S

G

L

V

D

D

P

P

K

K

L

V

F

M

P

G

L

T

A

G

P

P

I

I

G

P

A

A

I

S

E

R

K

K

L

A

L

L

K

E

K

R

T

A

G

G

L

W

D

K

V

I

N

G

D

D

I

L

D

D

L

L

F

V

E

E

I

A

N

N

E

E

A
|
A

F
|
F

S

A

C

A

V

Q

V

A

L

C

A

A

A

V

L

N

E

K

E

D

L

L

K

G

L

W

D

D

I

P

D

S

R

I

V

V

N

N

V

V

N

N

G

G

A

A

V

I

S

A

L

I

G

G

H
|
H

P

P

L

I

G

G

A

A

S

S

G

G

A

A

R

R

L

I

V

L

V

N

S

T

L

L

T

L

R

F

E

E

M

M

R

K

R

R

N

G

A

A

K

R

Y

K

G

G

I

L

A

A

A

T

L

L

C
|
C

I

I

G
|
G

G

G

E

M

A

G

V

V

A

A

T

M

L

C

F

I

E

E

active site: C89 (= C86), H348 (= H345), C378 (= C375), G380 (= G377)
binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L146), H156 (= H154), M157 (= M155), F235 (= F232), A243 (= A240), S247 (= S244), A318 (= A315), F319 (= F316), H348 (= H345)

Query Sequence

>WP_022671372.1 NCBI__GCF_000420385.1:WP_022671372.1
MDGVFVVEPLRSPFGGFGGTLSSLSASEIASFVVKEILSRTGIEDVDGLIMGNVLSAGVG
QSPARQVIIKSGLPYSVNALTVNKVCGSGLKSLMLAAQSIKLKDSSLIIAGGMESMSNAP
YYLSKARFGYRMGDGRAIDGMIFDGLWDVYNNVHMGYLAEMVAKAKKITRKIQDDYAVLS
YKRAQHSAENGVFKEEIVPIEISSRKGVNVVDRDEEPFRVDFEKIPKLKPAFVEDGTITA
ANASTISDGAAAFIVADYDAIKRFGLEPIAKVVAYSEFSLDPKLFPLAPIGAIEKLLKKT
GLDVNDIDLFEINEAFSCVVLAALEELKLDIDRVNVNGGAVSLGHPLGASGARLVVSLTR
EMRRRNAKYGIAALCIGGGEAVATLFERV

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory