SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing PfGW456L13_2498 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2498 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)

P09110 3-ketoacyl-CoA thiolase, peroxisomal; Acetyl-CoA C-myristoyltransferase; Acetyl-CoA acyltransferase; Beta-ketothiolase; Peroxisomal 3-oxoacyl-CoA thiolase; EC 2.3.1.16; EC 2.3.1.155; EC 2.3.1.9 from Homo sapiens (Human) (see 3 papers)
41% identity, 99% coverage: 3:398/400 of query aligns to 37:420/424 of P09110

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P09110

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V387 (= V366) to A: in dbSNP:rs2229528

Sites not aligning to the query:

1:26 PTS2-type peroxisomal targeting signal
5 mutation Q->D,K,L: Does not affect localization to peroxisomes.
6 V→D: Abolished localization to peroxisomes.; V→K: Does not affect localization to peroxisomes.
7 mutation V->D,K: Abolished localization to peroxisomes.
8 mutation L->D,K: Does not affect localization to peroxisomes.
9 mutation G->D,R,L: Does not affect localization to peroxisomes.
10 H→E: In S3E mutant; Abolished localization to peroxisomes.

2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
37% identity, 100% coverage: 2:400/400 of query aligns to 5:390/390 of 2d3tC

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2d3tC

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active site: C94 (= C90), H346 (= H356), C376 (= C386), G378 (= G388)
binding acetyl coenzyme *a: C94 (= C90), M129 (vs. gap), M150 (≠ I139), H176 (≠ Q175), R214 (= R222), L222 (= L230), L225 (= L233), A238 (= A251), G239 (= G252), S242 (= S255), I244 (≠ L257), M283 (= M296), A313 (= A326), F314 (= F327), H346 (= H356), C376 (= C386)

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)
39% identity, 100% coverage: 1:398/400 of query aligns to 1:391/393 of P14611

query
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P14611

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C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
H156 (≠ P148) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
F219 (≠ C220) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
R221 (= R222) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
S248 (= S255) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
H349 (= H356) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
C379 (= C386) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.

4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
36% identity, 100% coverage: 1:398/400 of query aligns to 7:393/395 of 4c2jD

query
sites
4c2jD

M

L

K

R

E

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A

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A

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A

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P

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C

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G

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-

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D

I

I

E

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-

E

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A

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-

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-

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-

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-

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x
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F

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|
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x
L

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S

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G

A

S

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R

M

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G

A

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H

A

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H

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G

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A

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active site: C95 (= C90), H351 (= H356), C381 (= C386), G383 (= G388)
binding coenzyme a: C95 (= C90), W152 (vs. gap), L155 (vs. gap), M164 (= M149), R223 (= R222), T226 (= T225), Q230 (≠ S229), L231 (= L230), L234 (= L233), A246 (= A251), G247 (= G252), S250 (= S255), V252 (≠ L257), A321 (= A326), F322 (= F327), H351 (= H356), L353 (≠ F358)

P42765 3-ketoacyl-CoA thiolase, mitochondrial; Acetyl-CoA acetyltransferase; Acetyl-CoA acyltransferase; Acyl-CoA hydrolase, mitochondrial; Beta-ketothiolase; Mitochondrial 3-oxoacyl-CoA thiolase; T1; EC 2.3.1.16; EC 2.3.1.9; EC 3.1.2.-; EC 3.1.2.1; EC 3.1.2.2 from Homo sapiens (Human) (see paper)
36% identity, 100% coverage: 1:398/400 of query aligns to 4:394/397 of P42765

query
sites
P42765

M

L

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A

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C92 (= C90) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
R224 (= R222) binding
T227 (= T225) binding
S251 (= S255) binding
C382 (= C386) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.

4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
39% identity, 100% coverage: 1:398/400 of query aligns to 1:391/393 of 4o9cC

query
sites
4o9cC

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M

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T

E

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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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A

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G

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-

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A

A

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C
x
S

S

G

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S

G

G

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A

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A

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A

A

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A

D

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I

I

A

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A

A

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E

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S

N

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S

L

A

-

A

-

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-

H

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-

M

-

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-

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-
x
L

-

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D

D

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H

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A

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x
H

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A

A

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A

A

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D

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E

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-

A

-

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A

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K

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Y

-

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-

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R

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|
S

L

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A

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L

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x
F

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-

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-

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-

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D

K

K

G

A

G

G

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I

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T

T

A
|
A

G

A

N

N

A
|
A

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S

Q
x
G

L
|
L

S

N

D

D

G

G

A

A

S

A

A

A

S

V

V

V

L

V

M

M

S

S

A

A

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A

M

K

A

A

E

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K

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G

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P

L

L

G

A

I

T

Y

I

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G

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M

Y

A

A

V

N

A

A

G

G

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P

D

K

E

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M

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M

P

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D

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D

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M

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A
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A

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F

A

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C

A

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G

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H
|
H

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x
I

G

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S

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G

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G

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G

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A

A

A

L

L

A

F

V

E

E

active site: S88 (≠ C90), H349 (= H356), C379 (= C386), G381 (= G388)
binding coenzyme a: S88 (≠ C90), L148 (vs. gap), H156 (≠ P148), R221 (= R222), S228 (= S229), L232 (= L233), F236 (≠ W237), A244 (= A251), A247 (= A254), S248 (= S255), G249 (≠ Q256), L250 (= L257), A319 (= A326), F320 (= F327), H349 (= H356), I351 (≠ F358), C379 (= C386)

P45359 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; CaTHL; EC 2.3.1.9 from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) (see paper)
36% identity, 100% coverage: 1:398/400 of query aligns to 1:390/392 of P45359

query
sites
P45359

M

M

K

K

E

E

A

V

V

V

I

I

V

A

S

S

T

A

A

V

R

R

T

T

P

A

I

I

G

G

K

-

A

S

F

Y

R

G

G

K

A

S

F

L

N

K

D

D

T

V

E

P

A

A

P

V

Q

D

L

L

G

G

G

A

H

T

V

A

V

I

R

K

E

E

A

A

V

V

R

K

A

A

G

G

I

I

E

K

P

P

G

E

E

D

V

V

D

N

D

E

V

V

I

I

I

L

G

G

A

N

A

V

A

L

Q

Q

Q

A

G

G

T

L

Q

-

S

G

Y

Q

N

N

L

P

G

A

R

R

L

Q

C

A

A

S

I

F

A

K

G

A

G

G

L

L

P

P

A
x
V

S

E

V

I

A

P

G

A

M

M

A

T

V

I

E

N

R

K

Q

V

C
|
C

S

G

S

S

G

G

L

L

M

R

S

T

I

V

A
x
S

M

L

A

A

K

Q

G

I

I

I

M

K

C

A

D

G

E

D

I

A

D

D

I

V

A

I

V

I

A

A

G

G

L

M

E

E

S

N

I

M

S

S

-

R

-

A

-

P

L

Y

V

L

Q

A

N

N

K

N

H

A

K

R

N

W

L

G

Y

Y

R

R

N

M

Q

G

S

N

G

A

S

K

V

F

I

V

E

D

-

E

-

M

-

I

-

T

-

D

-

G

-

L

L

W

D

D

P

A

H

F

A
x
N

Y

D

I

Y

P

H

M

M

I

G

E

I

T

T

A

A

E

E

I

N

V

I

S

A

A

E

R

R

Y

W

G

N

I

I

S

S

R

R

D

E

E

E

Q

Q

D

D

E

E

Y

F

S

A

Y

L

Q

A

S

S

Q

Q

L

K

R

K

T

A

A

E

Q

E

A

A

Q

I

S

K

A

S

G

G

R

Q

F

F

D

K

R

D

E

E

L

I

A

V

P

P

L

V

T

-

S

-

R

-

K

-

A

-

L

V

F

I

D

K

K

G

A

R

T

K

G

G

E

E

T

T

S

V

Y

V

E

D

T

T

V

-

T

-

L

-

R

-

D

D

E

E

C

H

N

P

R

R

I

F

D

G

T

S

T

T

L

I

Q

E

S

G

L

L

K

A

A

K

L

L

E

K

P

P

V

A

W

F

P

-

G

-

Q

-

W

-

S

-

D

K

K

K

G

D

G

G

F

T

I

V

T

T

A

A

G

G

N

N

A

A

S

S

Q

G

L

L

S

N

D

D

G

C

A

A

S

A

A

V

S

L

V

V

L

I

M

M

S

S

A

A

K

E

M

K

A

A

E

K

K

E

R

L

G

G

L

V

E

K

P

P

L

L

G

A

I

K

Y

I

R

V

G

S

M

Y

A
x
G

V
x
S

A

A

G

G

C

V

N

D

S

P

D
x
A

E

I

M

M

G

G

I

Y

G

G

P

P

I

F

Y

Y

A

A

I

T

P

K

K

A

L

A

L

I

K

E

R

K

H

A

G

G

L

W

T

T

M

V

D

D

H

E

I

L

G

D

L

L

W

I

E

E

L

S

N

N

E

E

A

A

F

F

A

A

C

A

Q

Q

V

S

L

L

H

A

C

V

R

A

D

K

T

D

L

L

G

K

I

F

P

D

A

M

E

N

R

K

L

V

N

N

V

V

N

N

G

G

A

A

I

I

A

A

I

L

G

G

H

H

P

P

F

I

G

G

M

A

S

S

G

G

A

A

R

R

M

I

V

L

G

V

H

T

A

L

L

V

V

H

E

A

G

M

Q

Q

R

K

R

R

G

D

L

A

R

K

Y

K

V

G

V

L

V

A

S

T

M

L

C
|
C

I

I

G

G

M

Q

G

G

A

T

A
|
A

A

I

L

L

F

L

E

E

V77 (≠ A79) 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 (= C90) modified: Disulfide link with 378, In inhibited form
S96 (≠ A98) binding
N153 (≠ A145) 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 (≠ AV 287:288) binding
A286 (≠ D294) 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 (= C386) modified: Disulfide link with 88, In inhibited form
A386 (= A394) binding

2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
38% identity, 99% coverage: 5:398/400 of query aligns to 3:387/389 of 2vu2A

query
sites
2vu2A

V

V

I

I

V

A

S

S

T

A

A

A

R

R

T

T

P

A

I

V

G

G

K

-

A

S

F

F

R

N

G

G

A

A

F

F

N

A

D

N

T

T

E

P

A

A

P

H

Q

E

L

L

G

G

G

A

H

T

V

V

V

I

R

S

E

A

A

V

V

L

R

E

R

R

A

A

G

G

I

V

E

A

P

A

G

G

E

E

V

V

D

N

D

E

V

V

I

I

I

L

G

G

A

Q

A

V

A

L

Q

P

Q

A

G

G

T

-

Q

E

S

G

Y

Q

N

N

L

P

G

A

R

R

L

Q

C

A

A

A

I

M

A

K

G

A

G

G

L

V

P

P

A

Q

S

E

V

A

A

T

G

A

M

W

A

G

V

M

E

N

R

Q

Q

L

C
|
C

S

G

S

S

G

G

L

L

M

R

S

A

I

V

A

A

M

L

A

G

A

M

K

Q

G

Q

I

I

M

A

C

T

D

G

E

D

I

A

D

S

I

I

A

I

V

V

A

A

G

G

L

M

E

E

S

S

I

M

S

S

L

M

V

A

Q

P

N

H

K

C

H

A

K

H

N

L

L

R

Y

G

R

G

N

V

Q

K

S

M

G

G

S

D

V

F

I

K

E

M

L

I

D

D

P

T

-

M

-

I

-

K

-

D

-

G

-
x
L

-

T

-

D

-

A

-

F

H

Y

A

G

Y

Y

I

-

P
x
H

M
|
M

I

G

E

T

T

T

A

A

E

E

I

N

V

V

S

A

A

K

R

Q

Y

W

G

Q

I

L

S

S

R

R

D

D

E

E

Q

Q

D

D

E

A

Y

F

S

A

Y

V

Q

A

S

S

Q

Q

L

N

R

K

T

A

A

E

Q

A

A

A

Q

Q

S

K

A

D

G

G

R

R

F

F

D

K

R

D

E

E

L

I

A

V

P

P

L

F

T

I

S

V

R

K

K

G

A

R

L

K

F

G

D

D

K

-

A

-

T

-

G

-

E

-

T

-

S

-

Y

-

E

-

T

-

V

I

T

T

L

V

L

D

R

A

D

D

E

E

C

Y

N

I

R

R

I

H

D

G

T

A

T

T

L

L

Q

D

S

S

L

M

K

A

A

K

L

L

E

R

P

P

V

A

W
x
F

P

-

G

-

Q

-

W

-

S

-

D

D

K

K

G

E

G

G

F

T

I

V

T

T

A
|
A

G

G

N

N

A

A

S
|
S

Q
x
G

L
|
L

S

N

D

D

G

G

A

A

S

A

A

A

S

A

V

L

L

L

M

M

S

S

A

E

K

A

M

E

A

A

E

S

K

R

R

R

G

G

L

I

E

Q

P

P

L

L

G

G

I

R

Y

I

R

V

G

S

M

W

A

A

V

T

A

V

G

G

C

V

N

D

S

P

D

K

E

V

M

M

G

G

I

T

G

G

P

P

I

I

Y

P

A

A

I

S

P

R

K

K

L

A

L

L

K

E

R

R

H

A

G

G

L

W

T

K

M

I

D

G

H

D

I

L

G

D

L

L

W

V

E

E

L

A

N

N

E

E

A
|
A

F
|
F

A

A

C

A

Q

Q

V

A

L

C

H

A

C

V

R

N

D

K

T

D

L

L

G

G

I

W

P

D

A

P

E

S

R

I

L

V

N

N

V

V

N

N

G

G

A

A

I

I

A

A

I

I

G

G

H
|
H

P

P

F

I

G

G

M

A

S

S

G

G

A

A

R

R

M

I

V

L

G

N

H

T

A

L

L

L

V

F

E

E

G

M

Q

K

R

R

G

G

L

A

R

R

Y

K

V

G

V

L

V

A

S

T

M

L

C
|
C

I

I

G
|
G

G

G

M

M

G

G

A

V

A

A

A

M

L

C

F

I

E

E

active site: C86 (= C90), H345 (= H356), C375 (= C386), G377 (= G388)
binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: C86 (= C90), L145 (vs. gap), H153 (≠ P148), M154 (= M149), F232 (≠ W237), A240 (= A251), S244 (= S255), G245 (≠ Q256), L246 (= L257), A315 (= A326), F316 (= F327), H345 (= H356)

1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
38% identity, 99% coverage: 5:398/400 of query aligns to 3:387/389 of 1dm3A

query
sites
1dm3A

V

V

I

I

V

A

S

S

T

A

A

A

R

R

T

T

P

A

I

V

G

G

K

-

A

S

F

F

R

N

G

G

A

A

F

F

N

A

D

N

T

T

E

P

A

A

P

H

Q

E

L

L

G

G

G

A

H

T

V

V

V

I

R

S

E

A

A

V

V

L

R

E

R

R

A

A

G

G

I

V

E

A

P

A

G

G

E

E

V

V

D

N

D

E

V

V

I

I

I

L

G

G

A

Q

A

V

A

L

Q

P

Q

A

G

G

T

-

Q

E

S

G

Y

Q

N

N

L

P

G

A

R

R

L

Q

C

A

A

A

I

M

A

K

G

A

G

G

L

V

P

P

A

Q

S

E

V

A

A

T

G

A

M

W

A

G

V

M

E

N

R

Q

Q

L

C
|
C

S

G

S

S

G

G

L

L

M

R

S

A

I

V

A

A

M

L

A

G

A

M

K

Q

G

Q

I

I

M

A

C

T

D

G

E

D

I

A

D

S

I

I

A

I

V

V

A

A

G

G

L

M

E

E

S

S

I

M

S

S

L

M

V

A

Q

P

N

H

K

C

H

A

K

H

N

L

L

R

Y

G

R

G

N

V

Q

K

S

M

G

G

S

D

V

F

I

K

E

M

L

I

D

D

P

T

-

M

-

I

-

K

-

D

-

G

-
x
L

-

T

-

D

-

A

-

F

H

Y

A

G

Y

Y

I

-

P
x
H

M
|
M

I

G

E

T

T

T

A

A

E

E

I

N

V

V

S

A

A

K

R

Q

Y

W

G

Q

I

L

S

S

R

R

D

D

E

E

Q

Q

D

D

E

A

Y

F

S

A

Y

V

Q

A

S

S

Q

Q

L

N

R

K

T

A

A

E

Q

A

A

A

Q

Q

S

K

A

D

G

G

R

R

F

F

D

K

R

D

E

E

L

I

A

V

P

P

L

F

T

I

S

V

R

K

K

G

A

R

L

K

F

G

D

D

K

-

A

-

T

-

G

-

E

-

T

-

S

-

Y

-

E

-

T

-

V

I

T

T

L

V

L

D

R

A

D

D

E

E

C

Y

N

I

R
|
R

I

H

D

G

T

A

T

T

L

L

Q

D

S
|
S

L
x
M

K

A

A

K

L
|
L

E

R

P

P

V

A

W
x
F

P

-

G

-

Q

-

W

-

S

-

D

D

K

K

G

E

G

G

F

T

I

V

T

T

A
|
A

G
|
G

N

N

A
|
A

S
|
S

Q
x
G

L
|
L

S

N

D

D

G

G

A

A

S

A

A

A

S

A

V

L

L

L

M

M

S

S

A

E

K

A

M

E

A

A

E

S

K

R

R

R

G

G

L

I

E

Q

P

P

L

L

G

G

I

R

Y

I

R

V

G

S

M

W

A

A

V

T

A

V

G

G

C

V

N

D

S

P

D

K

E

V

M
|
M

G

G

I

T

G

G

P

P

I

I

Y

P

A

A

I

S

P

R

K

K

L

A

L

L

K

E

R

R

H

A

G

G

L

W

T

K

M

I

D

G

H

D

I

L

G

D

L

L

W

V

E

E

L

A

N

N

E

E

A
|
A

F
|
F

A

A

C

A

Q

Q

V

A

L

C

H

A

C

V

R

N

D

K

T

D

L

L

G

G

I

W

P

D

A

P

E

S

R

I

L

V

N

N

V

V

N

N

G

G

A

A

I

I

A

A

I

I

G

G

H
|
H

P

P

F

I

G

G

M

A

S

S

G

G

A

A

R

R

M

I

V

L

G

N

H

T

A

L

L

L

V

F

E

E

G

M

Q

K

R

R

G

G

L

A

R

R

Y

K

V

G

V

L

V

A

S

T

M

L

C
|
C

I
|
I

G
|
G

G

G

M

M

G

G

A

V

A

A

A

M

L

C

F

I

E

E

active site: C86 (= C90), H345 (= H356), C375 (= C386), G377 (= G388)
binding acetyl coenzyme *a: C86 (= C90), L145 (vs. gap), H153 (≠ P148), M154 (= M149), R217 (= R222), S224 (= S229), M225 (≠ L230), L228 (= L233), F232 (≠ W237), A240 (= A251), G241 (= G252), A243 (= A254), S244 (= S255), G245 (≠ Q256), L246 (= L257), M285 (= M296), A315 (= A326), F316 (= F327), H345 (= H356), C375 (= C386), I376 (= I387)

1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
38% identity, 99% coverage: 5:398/400 of query aligns to 3:387/389 of 1dlvA

query
sites
1dlvA

V

V

I

I

V

A

S

S

T

A

A

A

R

R

T

T

P

A

I

V

G

G

K

-

A

S

F

F

R

N

G

G

A

A

F

F

N

A

D

N

T

T

E

P

A

A

P

H

Q

E

L

L

G

G

G

A

H

T

V

V

V

I

R

S

E

A

A

V

V

L

R

E

R

R

A

A

G

G

I

V

E

A

P

A

G

G

E

E

V

V

D

N

D

E

V

V

I

I

I

L

G

G

A

Q

A

V

A

L

Q

P

Q

A

G

G

T

-

Q

E

S

G

Y

Q

N

N

L

P

G

A

R

R

L

Q

C

A

A

A

I

M

A

K

G

A

G

G

L

V

P

P

A

Q

S

E

V

A

A

T

G

A

M

W

A

G

V

M

E

N

R

Q

Q

L

C
|
C

S

G

S

S

G

G

L

L

M

R

S

A

I

V

A

A

M

L

A

G

A

M

K

Q

G

Q

I

I

M

A

C

T

D

G

E

D

I

A

D

S

I

I

A

I

V

V

A

A

G

G

L

M

E

E

S

S

I

M

S

S

L

M

V

A

Q

P

N

H

K

C

H

A

K

H

N

L

L

R

Y

G

R

G

N

V

Q

K

S

M

G

G

S

D

V

F

I

K

E

M

L

I

D

D

P

T

-

M

-

I

-

K

-

D

-

G

-
x
L

-

T

-

D

-

A

-

F

H

Y

A

G

Y

Y

I

-

P
x
H

M
|
M

I

G

E

T

T

T

A

A

E

E

I

N

V

V

S

A

A

K

R

Q

Y

W

G

Q

I

L

S

S

R

R

D

D

E

E

Q

Q

D

D

E

A

Y

F

S

A

Y

V

Q

A

S

S

Q

Q

L

N

R

K

T

A

A

E

Q

A

A

A

Q

Q

S

K

A

D

G

G

R

R

F

F

D

K

R

D

E

E

L

I

A

V

P

P

L

F

T

I

S

V

R

K

K

G

A

R

L

K

F

G

D

D

K

-

A

-

T

-

G

-

E

-

T

-

S

-

Y

-

E

-

T

-

V

I

T

T

L

V

L

D

R

A

D

D

E

E

C

Y

N

I

R
|
R

I

H

D

G

T

A

T

T

L

L

Q

D

S
|
S

L
x
M

K

A

A

K

L
|
L

E

R

P

P

V

A

W
x
F

P

-

G

-

Q

-

W

-

S

-

D

D

K

K

G

E

G

G

F

T

I

V

T

T

A
|
A

G
|
G

N

N

A

A

S
|
S

Q
x
G

L
|
L

S

N

D

D

G

G

A

A

S

A

A

A

S

A

V

L

L

L

M

M

S

S

A

E

K

A

M

E

A

A

E

S

K

R

R

R

G

G

L

I

E

Q

P

P

L

L

G

G

I

R

Y

I

R

V

G

S

M

W

A

A

V

T

A

V

G

G

C

V

N

D

S

P

D

K

E

V

M

M

G

G

I

T

G

G

P

P

I

I

Y

P

A

A

I

S

P

R

K

K

L

A

L

L

K

E

R

R

H

A

G

G

L

W

T

K

M

I

D

G

H

D

I

L

G

D

L

L

W

V

E

E

L

A

N

N

E

E

A

A

F
|
F

A

A

C

A

Q

Q

V

A

L

C

H

A

C

V

R

N

D

K

T

D

L

L

G

G

I

W

P

D

A

P

E

S

R

I

L

V

N

N

V

V

N

N

G

G

A

A

I

I

A

A

I

I

G

G

H
|
H

P

P

F

I

G

G

M

A

S

S

G

G

A

A

R

R

M

I

V

L

G

N

H

T

A

L

L

L

V

F

E

E

G

M

Q

K

R

R

G

G

L

A

R

R

Y

K

V

G

V

L

V

A

S

T

M

L

C
|
C

I

I

G
|
G

G

G

M

M

G

G

A

V

A

A

A

M

L

C

F

I

E

E

active site: C86 (= C90), H345 (= H356), C375 (= C386), G377 (= G388)
binding coenzyme a: C86 (= C90), L145 (vs. gap), H153 (≠ P148), M154 (= M149), R217 (= R222), S224 (= S229), M225 (≠ L230), L228 (= L233), F232 (≠ W237), A240 (= A251), G241 (= G252), S244 (= S255), G245 (≠ Q256), L246 (= L257), F316 (= F327), H345 (= H356)

2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
38% identity, 99% coverage: 5:398/400 of query aligns to 5:389/391 of 2vu1A

query
sites
2vu1A

V

V

I

I

V

A

S

S

T

A

A

A

R

R

T

T

P

A

I

V

G

G

K

-

A

S

F

F

R

N

G

G

A

A

F

F

N

A

D

N

T

T

E

P

A

A

P

H

Q

E

L

L

G

G

G

A

H

T

V

V

V

I

R

S

E

A

A

V

V

L

R

E

R

R

A

A

G

G

I

V

E

A

P

A

G

G

E

E

V

V

D

N

D

E

V

V

I

I

I

L

G

G

A

Q

A

V

A

L

Q

P

Q

A

G

G

T

-

Q

E

S

G

Y

Q

N

N

L

P

G

A

R

R

L

Q

C

A

A

A

I

M

A

K

G

A

G

G

L

V

P

P

A

Q

S

E

V

A

A

T

G

A

M

W

A

G

V

M

E

N

R

Q

Q

L

C
|
C

S

G

S

S

G

G

L

L

M

R

S

A

I

V

A

A

M

L

A

G

A

M

K

Q

G

Q

I

I

M

A

C

T

D

G

E

D

I

A

D

S

I

I

A

I

V

V

A

A

G

G

L

M

E

E

S

S

I

M

S

S

L

M

V

A

Q

P

N

H

K

C

H

A

K

H

N

L

L

R

Y

G

R

G

N

V

Q

K

S

M

G

G

S

D

V

F

I

K

E

M

L

I

D

D

P

T

-

M

-

I

-

K

-

D

-

G

-
x
L

-

T

-

D

-

A

-

F

H

Y

A

G

Y

Y

I

-

P
x
H

M

M

I

G

E

T

T

T

A

A

E

E

I

N

V

V

S

A

A

K

R

Q

Y

W

G

Q

I

L

S

S

R

R

D

D

E

E

Q

Q

D

D

E

A

Y

F

S

A

Y

V

Q

A

S

S

Q

Q

L

N

R

K

T

A

A

E

Q

A

A

A

Q

Q

S

K

A

D

G

G

R

R

F

F

D

K

R

D

E

E

L

I

A

V

P

P

L

F

T

I

S

V

R

K

K

G

A

R

L

K

F

G

D

D

K

-

A

-

T

-

G

-

E

-

T

-

S

-

Y

-

E

-

T

-

V

I

T

T

L

V

L

D

R

A

D

D

E

E

C

Y

N

I

R

R

I

H

D

G

T

A

T

T

L

L

Q

D

S

S

L

M

K

A

A

K

L

L

E

R

P

P

V

A

W
x
F

P

-

G

-

Q

-

W

-

S

-

D

D

K

K

G

E

G

G

F

T

I

V

T

T

A
|
A

G

G

N

N

A

A

S
|
S

Q
x
G

L
|
L

S

N

D

D

G

G

A

A

S

A

A

A

S

A

V

L

L

L

M

M

S

S

A

E

K

A

M

E

A

A

E

S

K

R

R

R

G

G

L

I

E

Q

P

P

L

L

G

G

I

R

Y

I

R

V

G

S

M

W

A

A

V

T

A

V

G

G

C

V

N

D

S

P

D

K

E

V

M

M

G

G

I

T

G

G

P

P

I

I

Y

P

A

A

I

S

P

R

K

K

L

A

L

L

K

E

R

R

H

A

G

G

L

W

T

K

M

I

D

G

H

D

I

L

G

D

L

L

W

V

E

E

L

A

N

N

E

E

A
|
A

F
|
F

A

A

C

A

Q

Q

V

A

L

C

H

A

C

V

R

N

D

K

T

D

L

L

G

G

I

W

P

D

A

P

E

S

R

I

L

V

N

N

V

V

N

N

G

G

A

A

I

I

A

A

I

I

G

G

H
|
H

P

P

F

I

G

G

M

A

S

S

G

G

A

A

R

R

M

I

V

L

G

N

H

T

A

L

L

L

V

F

E

E

G

M

Q

K

R

R

G

G

L

A

R

R

Y

K

V

G

V

L

V

A

S

T

M

L

C
|
C

I

I

G
|
G

G

G

M

M

G

G

A

V

A

A

A

M

L

C

F

I

E

E

active site: C88 (= C90), H347 (= H356), C377 (= C386), G379 (= G388)
binding pantothenyl-aminoethanol-11-pivalic acid: L147 (vs. gap), H155 (≠ P148), F234 (≠ W237), A242 (= A251), S246 (= S255), G247 (≠ Q256), L248 (= L257), A317 (= A326), F318 (= F327), H347 (= H356)

1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
38% identity, 99% coverage: 5:398/400 of query aligns to 6:390/392 of 1ou6A

query
sites
1ou6A

V

V

I

I

V

A

S

S

T

A

A

A

R

R

T

T

P

A

I

V

G

G

K

-

A

S

F

F

R

N

G

G

A

A

F

F

N

A

D

N

T

T

E

P

A

A

P

H

Q

E

L

L

G

G

G

A

H

T

V

V

V

I

R

S

E

A

A

V

V

L

R

E

R

R

A

A

G

G

I

V

E

A

P

A

G

G

E

E

V

V

D

N

D

E

V

V

I

I

I

L

G

G