SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing GFF3382 FitnessBrowser__Phaeo:GFF3382 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 / LMG 5710 / VKM B-1787) (see paper)
46% identity, 100% coverage: 1:390/391 of query aligns to 1:391/392 of P45359

query
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P45359

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V77 (≠ N78) 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 (= C89) modified: Disulfide link with 378, In inhibited form
S96 (≠ V97) binding
N153 (≠ G153) 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 (≠ AH 278:279) binding
A286 (≠ E285) 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 (= C377) modified: Disulfide link with 88, In inhibited form
A386 (= A385) binding

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)
50% identity, 100% coverage: 1:390/391 of query aligns to 1:392/393 of P14611

query
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P14611

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C88 (= C89) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
H156 (= H156) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
F219 (≠ H218) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
R221 (≠ K220) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
S248 (= S246) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
H349 (= H347) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
C379 (= C377) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.

4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
45% identity, 100% coverage: 1:390/391 of query aligns to 1:391/392 of 4xl4A

query
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4xl4A

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active site: C88 (= C89), H348 (= H347), S378 (≠ C377), G380 (= G379)
binding coenzyme a: L148 (= L148), H156 (= H156), M157 (= M157), R220 (≠ K220), L228 (= L227), L231 (= L230), F235 (= F234), A243 (= A242), G244 (= G243), S247 (= S246), G248 (= G247), L249 (≠ I248), A318 (= A317), F319 (= F318), H348 (= H347)

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)
47% identity, 99% coverage: 4:389/391 of query aligns to 7:394/397 of P42765

query
sites
P42765

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C92 (= C89) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
R224 (≠ K220) binding
T227 (≠ S222) binding
S251 (= S246) binding
C382 (= C377) 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)
49% identity, 100% coverage: 1:390/391 of query aligns to 1:392/393 of 4o9cC

query
sites
4o9cC

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active site: S88 (≠ C89), H349 (= H347), C379 (= C377), G381 (= G379)
binding coenzyme a: S88 (≠ C89), L148 (= L148), H156 (= H156), R221 (≠ K220), S228 (≠ T226), L232 (= L230), F236 (= F234), A244 (= A242), A247 (= A245), S248 (= S246), G249 (= G247), L250 (≠ I248), A319 (= A317), F320 (= F318), H349 (= H347), I351 (≠ V349), C379 (= C377)

4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
47% identity, 99% coverage: 4:389/391 of query aligns to 10:393/395 of 4c2jD

query
sites
4c2jD

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active site: C95 (= C89), H351 (= H347), C381 (= C377), G383 (= G379)
binding coenzyme a: C95 (= C89), W152 (≠ L145), L155 (= L148), M164 (= M157), R223 (≠ K220), T226 (≠ S222), Q230 (≠ T226), L231 (= L227), L234 (= L230), A246 (= A242), G247 (= G243), S250 (= S246), V252 (≠ I248), A321 (= A317), F322 (= F318), H351 (= H347), L353 (≠ V349)

5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
48% identity, 100% coverage: 1:390/391 of query aligns to 3:394/394 of 5f38D

query
sites
5f38D

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G

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N

V

V

I

L

N

Q

T

A

-

G

-

L

-

G

-

Q

E

N

P

P

R

-

D

-

M

-

Y

-

L

-

S

A

R

R

V

Q

A

A

A

L

M

L

Q

K

A

S

G

G

I

L

P

A

N

E

G

T

T

V

P

C

A

G

M

F

N

T

V

V

N

N

R

K

L

V

C
|
C

G

G

S

S

G

G

A

L

Q

K

A

S

I

V

V

A

S

L

G

A

I

A

Q

Q

S

A

L

I

M

Q

L

A

G

G

D

Q

A

A

E

Q

F

S

A

I

L

V

T

A

G

G

A

M

E

E

N

N

M

M

S

S

R

L

S

A

P

P

F

Y

I

L

V

L

P

D

S

A

-

K

A

A

R

R

W

S

G

G

Q

Y

K

R

M

L

G

G

D

D

A

G

R

Q

A

V

L

Y

D

D

M

V

M

I

L

L

-

R

G

D

A

G

L
|
L

N

M

C

C

P

A

F

T

G

H

T

G

G

Y

H
|
H

M
|
M

G

G

V

I

T

T

A

A

E

E

N

N

V

V

A

A

D

K

E

E

H

Y

D

G

I

I

T

T

R

R

A

E

Q

M

M

Q

D

D

E

E

F

L

A

A

L

L

A

H

S

S

Q

Q

T

R

R

K

A

A

I

I

E

E

A

S

G

G

Y

A

F

F

A

T

S

A

Q

E

I

I

T

V

P

P

V

V

E

N

V

V

K

V

V

T

K

R

R

K

D

K

M

T

V

F

P

V

F

F

D

S

V

Q

D

D

E

E

H

F

P

P

K

K

A

A

-

N

S

S

T

T

L

A

E

E

T

A

L

L

G

G

G

A

L

L

K

R

A

P

V

A

F
|
F

K

D

K

K

D

A

G

G

R

T

V

V

T

T

A
|
A

G

G

N

N

A

A

S
|
S

G
|
G

I
|
I

N

N

D

D

G

G

A

A

I

L

V

V

M

I

A

M

T

E

A

E

D

S

A

A

R

L

Q

A

A

A

G

G

L

L

K

T

P

P

K

L

A

A

R

R

I

I

L

K

G

S

Y

Y

A

A

H

S

A

G

G

G

V

V

R

P

P

P

E

A

V

L

M
|
M

G

G

I

M

G

G

P

P

V

V

P

P

A

A

V

T

Q

Q

N

K

L

A

L

L

K

Q

K

L

T

A

G

G

L

L

S

Q

A

L

S

A

D

D

F

I

D

D

V

L

V

I

E

E

S

A

N

N

E

E

A
|
A

F
|
F

A

A

Q

Q

A

F

L

L

A

A

V

V

N

G

K

K

E

N

L

L

G

G

L

F

D

D

P

S

A

E

K

K

V

V

N

N

P

V

N

N

G

G

A

A

I

I

A
|
A

L

L

G

G

H
|
H

P

P

V

I

G

G

A

A

T

S

G

G

A

A

I

R

I

I

T

L

L

V

K

T

T

L

L

L

Y

H

E

A

L

M

E

Q

R

A

I

R

G

D

G

K

S

T

K

L

G

G

L

L

I
x
A

T

T

M
x
L

C

C

I

I

G

G

Q

Q

G

G

I

I

A

A

L

M

A

V

I

I

E

E

R

R

active site: C90 (= C89), A348 (= A344), A378 (≠ I374), L380 (≠ M376)
binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C89), L151 (= L148), H159 (= H156), M160 (= M157), F238 (= F234), A246 (= A242), S250 (= S246), G251 (= G247), I252 (= I248), M291 (= M287), A321 (= A317), F322 (= F318), H351 (= H347)

5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
49% identity, 100% coverage: 1:391/391 of query aligns to 1:391/391 of 5f38B

query
sites
5f38B

M

M

T

K

D

N

I

C

V

V

I

I

L

V

D

S

G

A

A

V

R

R

T

T

A

A

I

I

G

G

T

S

F

F

G

N

G

G

S

S

L

L

A

A

G

S

T

T

T

S

P

A

I

I

D

D

L

L

A

G

T

A

V

T

A

V

S

I

K

K

A

A

M

I

E

E

R

R

S

A

G

K

V

I

A

D

P

S

E

Q

Q

H

I

V

G

D

N

E

V

V

V

I

F

M

G

G

H

N

V

V

I

L

N

Q

T

A

-

G

-

L

-

G

-

Q

E

N

P

P

R

-

D

-

M

-

Y

-

L

-

S

A

R

R

V

Q

A

A

A

L

M

L

Q

K

A

S

G

G

I

L

P

A

N

E

G

T

T

V

P

C

A

G

M

F

N

T

V

V

N

N

R

K

L

V

C
|
C

G

G

S

S

G

G

A

L

Q

K

A

S

I

V

V

A

S

L

G

A

I

A

Q

Q

S

A

L

I

M

Q

L

A

G

G

D

Q

A

A

E

Q

F

S

A

I

L

V

T

A

G

G

A

M

E

E

N

N

M

M

S

S

R

L

S

A

P

P

F

Y

I

L

V

L

P

D

S

A

-

K

A

A

R

R

W

S

G

G

Q

Y

K

R

M

L

G

G

D

D

A

G

R

Q

A

V

L

Y

D

D

M

V

M

I

L

L

-

R

G

D

A

G

L
|
L

N

M

C

C

P

A

F

T

G

H

T

G

G

Y

H
|
H

M
|
M

G

G

V

I

T

T

A

A

E

E

N

N

V

V

A

A

D

K

E

E

H

Y

D

G

I

I

T

T

R

R

A

E

Q

M

M

Q

D

D

E

E

F

L

A

A

L

L

A

H

S

S

Q

Q

T

R

R

K

A

A

I

I

E

E

A

S

G

G

Y

A

F

F

A

T

S

A

Q

E

I

I

T

V

P

P

V

V

E

N

V

V

K

V

V

T

K

K

R

T

D

F

M

V

V

-

P

-

F

F

D

S

V

Q

D

D

E

E

H

F

P

P

K
|
K

A

A

-

N

S
|
S

T

T

L

A

E

E

T

A

L
|
L

G

G

G

A

L
|
L

K

R

A

P

V

A

F
|
F

K

D

K

K

D

A

G

G

R

T

V

V

T

T

A
|
A

G
|
G

N

N

A

A

S
|
S

G
|
G

I
|
I

N

N

D

D

G

G

A

A

I

L

V

V

M

I

A

M

T

E

A

E

D

S

A

A

R

L

Q

A

A

A

G

G

L

L

K

T

P

P

K

L

A

A

R

R

I

I

L

K

G

S

Y

Y

A

A

H

S

A

G

G

G

V

V

R

P

P

P

E

A

V

L

M
|
M

G

G

I

M

G

G

P

P

V

V

P

P

A

A

V

T

Q

Q

N

K

L

A

L

L

K

Q

K

L

T

A

G

G

L

L

S

Q

A

L

S

A

D

D

F

I

D

D

V

L

V

I

E

E

S

A

N

N

E

E

A
|
A

F
|
F

A

A

Q

Q

A

F

L

L

A

A

V

V

N

G

K

K

E

N

L

L

G

G

L

F

D

D

P

S

A

E

K

K

V

V

N

N

P

V

N

N

G

G

A

A

I

I

A

A

L

L

G

G

H
|
H

P

P

V

I

G

G

A

A

T

S

G

G

A

A

I

R

I

I

T

L

L

V

K

T

T

L

L

L

Y

H

E

A

L

M

E

Q

R

A

I

R

G

D

G

K

S

T

K

L

G

G

L

L

I

A

T

T

M

L

C
|
C

I

I

G
|
G

G

G

Q

Q

G

G

I

I

A

A

L

M

A

V

I

I

E

E

R

R

L

L

active site: C88 (= C89), H347 (= H347), C377 (= C377), G379 (= G379)
binding coenzyme a: C88 (= C89), L149 (= L148), H157 (= H156), M158 (= M157), K219 (= K220), S222 (= S222), L227 (= L227), L230 (= L230), F234 (= F234), A242 (= A242), G243 (= G243), S246 (= S246), G247 (= G247), I248 (= I248), M287 (= M287), A317 (= A317), F318 (= F318), H347 (= H347)

1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
46% identity, 99% coverage: 4:391/391 of query aligns to 5:392/392 of 1ou6A

query
sites
1ou6A

I

I

V

V

I

I

L

A

D

S

G

A

A

A

R

R

T

T

A

A

I

V

G

G

T

S

F

F

G

N

G

G

S

A

L

F

A

A

G

N

T

T

T

P

P

A

I

H

D

E

L

L

A

G

T

A

V

T

A

V

S

I

K

S

A

A

A

V

M

L

E

E

R

R

S

A

G

G

V

V

A

A

P

A

E

G

Q

E

I

V

G

N

N

E

V

V

V

I

F

L

G

G

H

Q

V

V

I

L

N

P

T

A

E

-

P

G

R

E

D

G

M

Q

Y

N

L

P

S

A

R

R

V

Q

A

A

M

M

Q

K

A

A

G

G

I

V

P

P

N

Q

G

E

T

A

P

T

A

A

M

W

N

G

V

M

N

N

R

Q

L

L

C
|
C

G

G

S

S

G

G

A

L

Q

R

A

A

I

V

V

A

S

L

G

G

I

M

Q

Q

S

Q

L

I

M

A

L

T

G

G

D

D

A

A

E

S

F

I

A

I

L

V

T

A

G

G

A

M

E

E

N

S

M

M

S

S

R

M

S

A

P

P

F

H

I

C

V

A

P

-

S

H

A

L

R

R

W

G

G

G

Q

V

K

K

M

M

G

G

D

D

A

F

R

K

A

M

L

I

D

D

M

T

M

M

L
x
I

-

K

G

D

A

G

L
|
L

N

T

C

D

P

A

F

F

G

Y

T

G

G

Y

H
|
H

M
|
M

G

G

V

T

T

T

A

A

E

E

N

N

V

V

A

A

D

K

E

Q

H

W

D

Q

I

L

T

S

R

R

A

D

Q

E

M

Q

D

D

E

A

F

F

A

A

L

V

A

A

S

S

Q

Q

T

N

R

K

A

A

A

E

A

A

I

Q

E

K

A

D

G

G

Y

R

F

F

A

K

S

D

Q

E

I

I

T

V

P

P

V

F

E

I

V

V

K

K

V

G

K

R

R

K

D

G

M

D

V

I

P

T

F

V

D

D

V

A

D

D

E

E

H

Y

P

I

K

R

-

H

A

G

S

A

T

T

L

L

E

D

T

S

L

M

G

A

G

K

L

L

K

R

A

P

V
x
A

F
|
F

K

D

K

K

D

E

G

G

R

T

V

V

T

T

A
|
A

G

G

N

N

A

A

S
|
S

G
|
G

I
x
L

N

N

D

D

G

G

A

A

-

A

I

L

V

L

M

M

A

S

T

E

A

A

D

E

A

A

A

S

R

R

Q

R

A

-

G

G

L

I

K

Q

P

P

K

L

A

G

R

R

I

I

L

V

G

S

Y

W

A

A

H

T

A

V

G

G

V

V

R

D

P

P

E

K

V

V

M

M

G

G

I

T

G

G

P

P

V

I

P

P

A

A

V

S

Q

R

N

K

L

A

L

L

K

E

K

R

T

A

G

G

L

W

S

K

A

I

S

G

D

D

F

L

D

D

V

L

V

V

E

E

S

A

N

N

E

E

A
|
A

F
|
F

A

A

Q

Q

A

A

L

C

A

A

V

V

N

N

K

K

E

D

L

L

G

G

L

W

D

D

P

P

A

S

K

I

V

V

N

N

P

V

N

N

G

G

A

A

I

I

A

A

L

I

G

G

H
|
H

P

P

V

I

G

G

A

A

T

S

G

G

A

A

I

R

I

I

T

L

L

N

K

T

T

L

L

L

Y

F

E

E

L

M

E

K

R

R

I

R

G

G

G

A

S

R

K

K

G

G

L

L

I

A

T

T

M

L

C
|
C

I

I

G
|
G

G

G

Q

M

G

G

I

V

A

A

L

M

A

C

I

I

E

E

R

S

L

L

active site: C89 (= C89), H348 (= H347), C378 (= C377), G380 (= G379)
binding pantothenyl-aminoethanol-acetate pivalic acid: I144 (≠ L145), L148 (= L148), H156 (= H156), M157 (= M157), A234 (≠ V233), F235 (= F234), A243 (= A242), S247 (= S246), G248 (= G247), L249 (≠ I248), A318 (= A317), F319 (= F318), H348 (= H347)

2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
46% identity, 99% coverage: 4:391/391 of query aligns to 4:391/391 of 2vu1A

query
sites
2vu1A

I

I

V

V

I

I

L

A

D

S

G

A

A

A

R

R

T

T

A

A

I

V

G

G

T

S

F

F

G

N

G

G

S

A

L

F

A

A

G

N

T

T

T

P

P

A

I

H

D

E

L

L

A

G

T

A

V

T

A

V

S

I

K

S

A

A

A

V

M

L

E

E

R

R

S

A

G

G

V

V

A

A

P

A

E

G

Q

E

I

V

G

N

N

E

V

V

V

I

F

L

G

G

H

Q

V

V

I

L

N

P

T

A

E

-

P

G

R

E

D

G

M

Q

Y

N

L

P

S

A

R

R

V

Q

A

A

M

M

Q

K

A

A

G

G

I

V

P

P

N

Q

G

E

T

A

P

T

A

A

M

W

N

G

V

M

N

N

R

Q

L

L

C
|
C

G

G

S

S

G

G

A

L

Q

R

A

A

I

V

V

A

S

L

G

G

I

M

Q

Q

S

Q

L

I

M

A

L

T

G

G

D

D

A

A

E

S

F

I

A

I

L

V

T

A

G

G

A

M

E

E

N

S

M

M

S

S

R

M

S

A

P

P

F

H

I

C

V

A

P

-

S

H

A

L

R

R

W

G

G

G

Q

V

K

K

M

M

G

G

D

D

A

F

R

K

A

M

L

I

D

D

M

T

M

M

L

I

-

K

G

D

A

G

L
|
L

N

T

C

D

P

A

F

F

G

Y

T

G

G

Y

H
|
H

M

M

G

G

V

T

T

T

A

A

E

E

N

N

V

V

A

A

D

K

E

Q

H

W

D

Q

I

L

T

S

R

R

A

D

Q

E

M

Q

D

D

E

A

F

F

A

A

L

V

A

A

S

S

Q

Q

T

N

R

K

A

A

A

E

A

A

I

Q

E

K

A

D

G

G

Y

R

F

F

A

K

S

D

Q

E

I

I

T

V

P

P

V

F

E

I

V

V

K

K

V

G

K

R

R

K

D

G

M

D

V

I

P

T

F

V

D

D

V

A

D

D

E

E

H

Y

P

I

K

R

-

H

A

G

S

A

T

T

L

L

E

D

T

S

L

M

G

A

G

K

L

L

K

R

A

P

V

A

F
|
F

K

D

K

K

D

E

G

G

R

T

V

V

T

T

A
|
A

G

G

N

N

A

A

S
|
S

G
|
G

I
x
L

N

N

D

D

G

G

A

A

-

A

I

L

V

L

M

M

A

S

T

E

A

A

D

E

A

A

A

S

R

R

Q

R

A

-

G

G

L

I

K

Q

P

P

K

L

A

G

R

R

I

I

L

V

G

S

Y

W

A

A

H

T

A

V

G

G

V

V

R

D

P

P

E

K

V

V

M

M

G

G

I

T

G

G

P

P

V

I

P

P

A

A

V

S

Q

R

N

K

L

A

L

L

K

E

K

R

T

A

G

G

L

W

S

K

A

I

S

G

D

D

F

L

D

D

V

L

V

V

E

E

S

A

N

N

E

E

A
|
A

F
|
F

A

A

Q

Q

A

A

L

C

A

A

V

V

N

N

K

K

E

D

L

L

G

G

L

W

D

D

P

P

A

S

K

I

V

V

N

N

P

V

N

N

G

G

A

A

I

I

A

A

L

I

G

G

H
|
H

P

P

V

I

G

G

A

A

T

S

G

G

A

A

I

R

I

I

T

L

L

N

K

T

T

L

L

L

Y

F

E

E

L

M

E

K

R

R

I

R

G

G

G

A

S

R

K

K

G

G

L

L

I

A

T

T

M

L

C
|
C

I

I

G
|
G

G

G

Q

M

G

G

I

V

A

A

L

M

A

C

I

I

E

E

R

S

L

L

active site: C88 (= C89), H347 (= H347), C377 (= C377), G379 (= G379)
binding pantothenyl-aminoethanol-11-pivalic acid: L147 (= L148), H155 (= H156), F234 (= F234), A242 (= A242), S246 (= S246), G247 (= G247), L248 (≠ I248), A317 (= A317), F318 (= F318), H347 (= H347)

2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
46% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 2vu2A

query
sites
2vu2A

I

I

V

V

I

I

L

A

D

S

G

A

A

A

R

R

T

T

A

A

I

V

G

G

T

S

F

F

G

N

G

G

S

A

L

F

A

A

G

N

T

T

T

P

P

A

I

H

D

E

L

L

A

G

T

A

V

T

A

V

S

I

K

S

A

A

A

V

M

L

E

E

R

R

S

A

G

G

V

V

A

A

P

A

E

G

Q

E

I

V

G

N

N

E

V

V

V

I

F

L

G

G

H

Q

V

V

I

L

N

P

T

A

E

-

P

G

R

E

D

G

M

Q

Y

N

L

P

S

A

R

R

V

Q

A

A

M

M

Q

K

A

A

G

G

I

V

P

P

N

Q

G

E

T

A

P

T

A

A

M

W

N

G

V

M

N

N

R

Q

L

L

C
|
C

G

G

S

S

G

G

A

L

Q

R

A

A

I

V

V

A

S

L

G

G

I

M

Q

Q

S

Q

L

I

M

A

L

T

G

G

D

D

A

A

E

S

F

I

A

I

L

V

T

A

G

G

A

M

E

E

N

S

M

M

S

S

R

M

S

A

P

P

F

H

I

C

V

A

P

-

S

H

A

L

R

R

W

G

G

G

Q

V

K

K

M

M

G

G

D

D

A

F

R

K

A

M

L

I

D

D

M

T

M

M

L

I

-

K

G

D

A

G

L
|
L

N

T

C

D

P

A

F

F

G

Y

T

G

G

Y

H
|
H

M
|
M

G

G

V

T

T

T

A

A

E

E

N

N

V

V

A

A

D

K

E

Q

H

W

D

Q

I

L

T

S

R

R

A

D

Q

E

M

Q

D

D

E

A

F

F

A

A

L

V

A

A

S

S

Q

Q

T

N

R

K

A

A

A

E

A

A

I

Q

E

K

A

D

G

G

Y

R

F

F

A

K

S

D

Q

E

I

I

T

V

P

P

V

F

E

I

V

V

K

K

V

G

K

R

R

K

D

G

M

D

V

I

P

T

F

V

D

D

V

A

D

D

E

E

H

Y

P

I

K

R

-

H

A

G

S

A

T

T

L

L

E

D

T

S

L

M

G

A

G

K

L

L

K

R

A

P

V

A

F
|
F

K

D

K

K

D

E

G

G

R

T

V

V

T

T

A
|
A

G

G

N

N

A

A

S
|
S

G
|
G

I
x
L

N

N

D

D

G

G

A

A

-

A

I

L

V

L

M

M

A

S

T

E

A

A

D

E

A

A

A

S

R

R

Q

R

A

-

G

G

L

I

K

Q

P

P

K

L

A

G

R

R

I

I

L

V

G

S

Y

W

A

A

H

T

A

V

G

G

V

V

R

D

P

P

E

K

V

V

M

M

G

G

I

T

G

G

P

P

V

I

P

P

A

A

V

S

Q

R

N

K

L

A

L

L

K

E

K

R

T

A

G

G

L

W

S

K

A

I

S

G

D

D

F

L

D

D

V

L

V

V

E

E

S

A

N

N

E

E

A
|
A

F
|
F

A

A

Q

Q

A

A

L

C

A

A

V

V

N

N

K

K

E

D

L

L

G

G

L

W

D

D

P

P

A

S

K

I

V

V

N

N

P

V

N

N

G

G

A

A

I

I

A

A

L

I

G

G

H
|
H

P

P

V

I

G

G

A

A

T

S

G

G

A

A

I

R

I

I

T

L

L

N

K

T

T

L

L

L

Y

F

E

E

L

M

E

K

R

R

I

R

G

G

G

A

S

R

K

K

G

G

L

L

I

A

T

T

M

L

C
|
C

I

I

G
|
G

G

G

Q

M

G

G

I

V

A

A

L

M

A

C

I

I

E

E

R

S

L

L

active site: C86 (= C89), H345 (= H347), C375 (= C377), G377 (= G379)
binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: C86 (= C89), L145 (= L148), H153 (= H156), M154 (= M157), F232 (= F234), A240 (= A242), S244 (= S246), G245 (= G247), L246 (≠ I248), A315 (= A317), F316 (= F318), H345 (= H347)

1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
46% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 1dm3A

query
sites
1dm3A

I

I

V

V

I

I

L

A

D

S

G

A

A

A

R

R

T

T

A

A

I

V

G

G

T

S

F

F

G

N

G

G

S

A

L

F

A

A

G

N

T

T

T

P

P

A

I

H

D

E

L

L

A

G

T

A

V

T

A

V

S

I

K

S

A

A

A

V

M

L

E

E

R

R

S

A

G

G

V

V

A

A

P

A

E

G

Q

E

I

V

G

N

N

E

V

V

V

I

F

L

G

G

H

Q

V

V

I

L

N

P

T

A

E

-

P

G

R

E

D

G

M

Q

Y

N

L

P

S

A

R

R

V

Q

A

A

M

M

Q

K

A

A

G

G

I

V

P

P

N

Q

G

E

T

A

P

T

A

A

M

W

N

G

V

M

N

N

R

Q

L

L

C
|
C

G

G

S

S

G

G

A

L

Q

R

A

A

I

V

V

A

S

L

G

G

I

M

Q

Q

S

Q

L

I

M

A

L

T

G

G

D

D

A

A

E

S

F

I

A

I

L

V