SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing CCNA_00996 FitnessBrowser__Caulo:CCNA_00996 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)

Q9P4U9 Enoyl-CoA hydratase AKT3-1; AF-toxin biosynthesis protein 3-1; EC 4.2.1.17 from Alternaria alternata (Alternaria rot fungus) (Torula alternata) (see paper)
44% identity, 89% coverage: 15:277/294 of query aligns to 23:272/296 of Q9P4U9

query
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Q9P4U9

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Sites not aligning to the query:

294:296 Peroxisomal targeting signal type 1

5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
35% identity, 92% coverage: 6:276/294 of query aligns to 3:259/259 of 5zaiC

query
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5zaiC

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active site: A65 (= A68), F70 (= F77), S82 (≠ E89), R86 (= R102), G110 (≠ V125), E113 (≠ T128), P132 (≠ V147), E133 (≠ F148), I138 (= I153), P140 (= P155), G141 (≠ E156), A226 (= A248), F236 (vs. gap)
binding coenzyme a: D23 (= D26), K24 (≠ R27), L25 (≠ M28), A27 (= A30), A63 (= A66), G64 (= G67), A65 (= A68), D66 (= D69), I67 (≠ L70), L108 (≠ V123), G109 (= G124), P132 (≠ V147), E133 (≠ F148), R166 (≠ V181), F248 (= F265), K251 (= K268)

6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 91% coverage: 9:276/294 of query aligns to 5:257/257 of 6slbAAA

query
sites
6slbAAA

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active site: Q64 (≠ A68), F69 (= F77), L80 (≠ R97), N84 (≠ G101), A108 (≠ V125), S111 (≠ T128), A130 (≠ V147), F131 (= F148), L136 (≠ I153), P138 (= P155), D139 (≠ E156), A224 (≠ K243), G234 (= G253)
binding (~{E})-6-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethylsulfanyl]-6-oxidanylidene-hex-3-enoic acid: L24 (≠ M28), A26 (= A30), R58 (= R62), A62 (= A66), G63 (= G67), Q64 (≠ A68), D65 (= D69), L66 (= L70), Y76 (≠ A84), H79 (≠ Y96), Y83 (≠ G100), V104 (≠ A121), A106 (≠ V123), G107 (= G124), A108 (≠ V125), A130 (≠ V147), F131 (= F148), I134 (≠ R151), D139 (≠ E156)

6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 91% coverage: 9:276/294 of query aligns to 2:245/245 of 6slaAAA

query
sites
6slaAAA

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active site: Q61 (≠ A68), L68 (= L85), N72 (≠ G101), A96 (≠ V125), S99 (≠ T128), A118 (≠ V147), F119 (= F148), L124 (≠ I153), P126 (= P155), N127 (≠ E156), A212 (≠ K243), G222 (= G253)
binding ~{S}-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethyl] 2-(2,5-dihydrooxepin-7-yl)ethanethioate: K20 (≠ R27), L21 (≠ M28), A23 (= A30), R55 (= R62), A59 (= A66), G60 (= G67), Q61 (≠ A68), D62 (= D69), L63 (= L70), L68 (= L85), Y71 (≠ E88), V92 (≠ A121), A94 (≠ V123), G95 (= G124), A96 (≠ V125), A118 (≠ V147), F119 (= F148), I122 (≠ R151), L124 (≠ I153), N127 (≠ E156), F234 (= F265), K237 (= K268)

3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
31% identity, 93% coverage: 5:276/294 of query aligns to 1:256/256 of 3h81A

query
sites
3h81A

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D

Q

R

A

M

L

N

N

A

A

F

L

T

N

A

S

R

Q

M

V

M

M

K

N

D

E

L

V

I

T

E

S

V

A

F

A

D

T

V

E

T

L

D

D

A

D

D

D

D

P

A

D

V

I

K

G

V

A

V

I

I

I

T

T

G

G

A

S

G

A

R

K

A

A

F

F

C

A

A

A

G

G

A
|
A

D

D

L

I

G

K

G

-

A

E

T
x
M

F

A

D

D

R

L

T

T

S

F

P

A

Q

D

A

A

L

F

E

-

R

-

E

-

G

-

K

-

V
x
T

G

A

D

D

I

F

Y
x
F

R

A

D

T

G

W

G

G

G

K

R

L

V

A

T

A

L

V

R

R

M

-

Y

-

D

-

S

-

L

-

K

T

P

P

I

T

I

I

G

A

A

A

I

V

N

A

G

G

A

Y

A

A

V

L

G

G

V
x
G

G

G

V

C

T
x
E

M

L

Q

A

L

M

P

M

M

C

D

D

I

V

R

L

L

I

A

A

S

A

T

D

E

T

A

A

K

K

F

F

G

G

F

Q

V
x
P

F
x
E

A

I

R

K

R

L

G

G

I
x
V

N

L

P
|
P

E
x
G

A

M

A

G

S

G

S

S

W

Q

F

R

L

L

P

T

R

R

L

A

V

I

G

G

L

K

Q

A

T

K

A

A

L

M

E

D

W

L

C

I

Y

L

T

T

G

G

R

R

V

T

F

M

P

D

A

A

S

A

E

E

A

A

L

E

E
x
R

K
x
S

G

G

L

L

V

V

R

S

S

R

L

V

H

V

A

P

P

A

D

D

E

D

L

L

P

T

A

E

A

A

R

R

A

A

L

T

A

A

R

T

E

T

I

I

A

S

D

Q

N

M

T

S

A

A

P

S

V

-

S

A

V

A

A

R

L

M

T

A

R

K

Q

E

L

A

L

V

W

N

R

R

M

-

A

A

G

F

A

E

D

S

H

S

P

L

M

S

E

E

A

G

H

L

K
x
L

A

Y

D

E

S

R

R

R

A

L

I

F

Q

H

S

S

R

A

G
x
F

S

A

S

T

G

E

D

D

A
x
Q

K

S

E

E

G

G

V

M

T

A

S

A

F

F

L

I

E

E

K

K

R

R

A

A

P

P

V

Q

Y

F

P

T

N

H

K

R

active site: A64 (= A68), M69 (≠ T76), T79 (≠ V92), F83 (≠ Y96), G107 (≠ V125), E110 (≠ T128), P129 (≠ V147), E130 (≠ F148), V135 (≠ I153), P137 (= P155), G138 (≠ E156), L223 (≠ K243), F233 (≠ G253)
binding calcium ion: R171 (≠ E189), S172 (≠ K190), F233 (≠ G253), Q238 (≠ A258)

3q0jA Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
31% identity, 91% coverage: 5:273/294 of query aligns to 2:254/255 of 3q0jA

query
sites
3q0jA

T

T

F

Y

E

E

T

T

L

I

L

L

Y

V

D

E

V

R

E

D

D

Q

G

R

I

V

A

G

T

I

I

I

T

T

L

L

N

N

R

R

P

P

D

Q

R

A

M

L

N

N

A

A

F

L

T

N

A

S

R

Q

M

V

M

M

K

N

D

E

L

V

I

T

E

S

V

A

F

A

D

T

V

E

T

L

D

D

A

D

D

D

D

P

A

D

V

I

K

G

V

A

V

I

I

I

T

T

G

G

A

S

G

A

R

K

A

A

F

F

C

A

A

A

G

G

A
|
A

D

D

L

I

G

K

G

-

A

E

T
x
M

F

A

D

D

R

L

T

T

S

F

P

A

Q

D

A

A

L

F

E

-

R

-

E

-

G

-

K

-

V
x
T

G

A

D

D

I

F

Y
x
F

R

A

D

T

G

W

G

G

G

K

R

L

V

A

T

A

L

V

R

R

M

-

Y

-

D

-

S

-

L

-

K

T

P

P

I

T

I

I

G

A

A

A

I

V

N

A

G

G

A

Y

A

A

V

L

G

G

V
x
G

G

G

V

C

T
x
E

M

L

Q

A

L

M

P

M

M

C

D

D

I

V

R

L

L

I

A

A

S

A

T

D

E

T

A

A

K

K

F

F

G

G

F

Q

V
x
P

F
x
E

A

I

R

K

R

L

G

G

I
x
V

N

L

P
|
P

E
x
G

A

M

A

G

S

G

S

S

W

Q

F

R

L

L

P

T

R

R

L

A

V

I

G

G

L

K

Q

A

T

K

A

A

L

M

E

D

W

L

C

I

Y

L

T

T

G

G

R

R

V

T

F

M

P

D

A

A

S

A

E

E

A

A

L

E

E

R

K

S

G

G

L

L

V

V

R

S

S

R

L

V

H

V

A

P

P

A

D

D

E

D

L

L

P

T

A

E

A

A

R

R

A

A

L

T

A

A

R

T

E

T

I

I

A

S

D

Q

N

M

T

S

A

A

P

S

V

-

S

A

V

A

A

R

L

M

T

A

R

K

Q

E

L

A

L

V

W

N

R

R

M

-

A

A

G

F

A

E

D

S

H

S

P

L

M

S

E

E

A

G

H

L

K
x
L

A

Y

D

E

S

R

R

R

A

L

I

F

Q

H

S

S

R

A

G
x
F

S

A

S

T

G

E

D

D

A

Q

K

S

E

E

G

G

V

M

T

A

S

A

F
|
F

L

I

E

E

K
|
K

R

R

A

A

P

P

V

Q

Y

F

active site: A65 (= A68), M70 (≠ T76), T80 (≠ V92), F84 (≠ Y96), G108 (≠ V125), E111 (≠ T128), P130 (≠ V147), E131 (≠ F148), V136 (≠ I153), P138 (= P155), G139 (≠ E156), L224 (≠ K243), F234 (≠ G253)
binding acetoacetyl-coenzyme a: F246 (= F265), K249 (= K268)

3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 91% coverage: 5:273/294 of query aligns to 2:254/255 of 3q0gC

query
sites
3q0gC

T

T

F

Y

E

E

T

T

L

I

L

L

Y

V

D

E

V

R

E

D

D

Q

G

R

I

V

A

G

T

I

I

I

T

T

L

L

N

N

R

R

P

P

D

Q

R
x
A

M
x
L

N

N

A
|
A

F

L

T

N

A

S

R

Q

M

V

M

M

K

N

D

E

L

V

I

T

E

S

V

A

F

A

D

T

V

E

T

L

D

D

A

D

D

D

D

P

A

D

V

I

K

G

V

A

V

I

I

I

T

T

G

G

A

S

G

A

R

K

A

A

F

F

C

A

A
|
A

G

G

A
|
A

D
|
D

L
x
I

G
x
K

G

-

A

E

T
x
M

F

A

D

D

R

L

T

T

S

F

P

A

Q

D

A

A

L

F

E

-

R

-

E

-

G

-

K

-

V
x
T

G

A

D

D

I

F

Y
x
F

R

A

D

T

G

W

G

G

G

K

R

L

V

A

T

A

L

V

R

R

M

-

Y

-

D

-

S

-

L

-

K

T

P

P

I

T

I

I

G

A

A

A

I

V

N

A

G

G

A
x
Y

A

A

V

L

G

G

V
x
G

G

G

V

C

T
x
E

M

L

Q

A

L

M

P

M

M

C

D

D

I

V

R

L

L

I

A

A

S

A

T

D

E

T

A

A

K

K

F

F

G

G

F

Q

V
x
P

F
x
E

A

I

R

K

R
x
L

G

G

I
x
V

N

L

P
|
P

E
x
G

A

M

A

G

S

G

S

S

W

Q

F

R

L

L

P

T

R

R

L

A

V

I

G

G

L

K

Q

A

T

K

A

A

L

M

E

D

W

L

C

I

Y

L

T

T

G

G

R

R

V

T

F

M

P

D

A

A

S

A

E

E

A

A

L

E

E

R

K

S

G

G

L

L

V

V

R

S

S

R

L

V

H

V

A

P

P

A

D

D

E

D

L

L

P

T

A

E

A

A

R

R

A

A

L

T

A

A

R

T

E

T

I

I

A

S

D

Q

N

M

T

S

A

A

P

S

V

-

S

A

V

A

A

R

L

M

T

A

R

K

Q

E

L

A

L

V

W

N

R

R

M

-

A

A

G

F

A

E

D

S

H

S

P

L

M

S

E

E

A

G

H

L

K
x
L

A

Y

D

E

S

R

R

R

A

L

I

F

Q

H

S

S

R

A

G
x
F

S

A

S

T

G

E

D

D

A

Q

K

S

E

E

G

G

V

M

T

A

S

A

F

F

L

I

E

E

K

K

R

R

A

A

P

P

V

Q

Y

F

active site: A65 (= A68), M70 (≠ T76), T80 (≠ V92), F84 (≠ Y96), G108 (≠ V125), E111 (≠ T128), P130 (≠ V147), E131 (≠ F148), V136 (≠ I153), P138 (= P155), G139 (≠ E156), L224 (≠ K243), F234 (≠ G253)
binding coenzyme a: A24 (≠ R27), L25 (≠ M28), A27 (= A30), A63 (= A66), A65 (= A68), D66 (= D69), I67 (≠ L70), K68 (≠ G71), Y104 (≠ A121), P130 (≠ V147), E131 (≠ F148), L134 (≠ R151)

3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
30% identity, 91% coverage: 5:273/294 of query aligns to 1:249/250 of 3q0gD

query
sites
3q0gD

T

T

F

Y

E

E

T

T

L

I

L

L

Y

V

D

E

V

R

E

D

D

Q

G

R

I

V

A

G

T

I

I

I

T

T

L

L

N

N

R

R

P

P

D

Q

R

A

M

L

N

N

A

A

F

L

T

N

A

S

R

Q

M

V

M

M

K

N

D

E

L

V

I

T

E

S

V

A

F

A

D

T

V

E

T

L

D

D

A

D

D

D

D

P

A

D

V

I

K

G

V

A

V

I

I

I

T

T

G

G

A

S

G

A

R

K

A

A

F

F

C

A

A

A

G

G

A
|
A

D

D

L

I

G

K

G

E

G
x
M

G

F

A

A

T

-

F

-

D

-

R

-

T

-

S

-

P

-

Q

-

A

-

L

-

E

-

R

-

E

-

E

D

G

A

K

F

V
x
T

G

A

D

D

I

F

Y
x
F

R

A

D

T

G

W

G

G

G

K

R

L

V

A

T

A

L

V

R

R

M

-

Y

-

D

-

S

-

L

-

K

T

P

P

I

T

I

I

G

A

A

A

I

V

N

A

G

G

A

Y

A

A

V

L

G

G

V
x
G

G

G

V

C

T
x
E

M

L

Q

A

L

M

P

M

M

C

D

D

I

V

R

L

L

I

A

A

S

A

T

D

E

T

A

A

K

K

F

F

G

G

F

Q

V
x
P

F
x
E

A

I

R

K

R

L

G

G

I
x
V

N

L

P
|
P

E
x
G

A

M

A

G

S

G

S

S

W

Q

F

R

L

L

P

T

R

R

L

A

V

I

G

G

L

K

Q

A

T

K

A

A

L

M

E

D

W

L

C

I

Y

L

T

T

G

G

R

R

V

T

F

M

P

D

A

A

S

A

E

E

A

A

L

E

E

R

K

S

G

G

L

L

V

V

R

S

S

R

L

V

H

V

A

P

P

A

D

D

E

D

L

L

P

T

A

E

A

A

R

R

A

A

L

T

A

A

R

T

E

T

I

I

A

S

D

Q

N

M

T

S

A

A

P

S

V

-

S

A

V

A

A

R

L

M

T

A

R

K

Q

E

L

A

L

V

W

N

R

R

M

-

A

A

G

F

A

E

D

S

H

S

P

L

M

S

E

E

A

G

H

L

K
x
L

A

Y

D

E

S

R

R

R

A

L

I
x
F

Q

H

S

S

R

A

G
x
F

S

A

S

T

G

E

D

D

A

Q

K

S

E

E

G

G

V

M

T

A

S

A

F
|
F

L

I

E

E

K
|
K

R

R

A

A

P

P

V

Q

Y

F

active site: A64 (= A68), M69 (≠ G73), T75 (≠ V92), F79 (≠ Y96), G103 (≠ V125), E106 (≠ T128), P125 (≠ V147), E126 (≠ F148), V131 (≠ I153), P133 (= P155), G134 (≠ E156), L219 (≠ K243), F229 (≠ G253)
binding Butyryl Coenzyme A: F225 (≠ I249), F241 (= F265), K244 (= K268)

O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
32% identity, 87% coverage: 20:276/294 of query aligns to 21:266/266 of O53561

query
sites
O53561

I

V

T

T

L

M

N

N

R

R

P

P

D

A

R

A

M

R

N

N

A

A

F

L

T

S

A

T

R

E

M

M

K

R

D

I

L

M

I

V

E

Q

V

A

F

W

D

D

V

R

T

V

D

D

A

N

D

D

D

P

A

D

V

I

K

R

V

C

I

I

I

L

T

T

G

G

A

A

G

G

R

G

A

Y

F

F

C

C

A

A

G

G

A

M

D

D

L

L

G

K

G

A

G

-

A

-

T

-

F

-

D

-

R

-

T

-

S

-

P

-

Q

-

A

-

L

-

E

-

R

-

E

T

E

Q

G

K

K

P

V

P

G

G

D

D

I

S

Y

F

R

K

D

D

G

G

G

S

-

Y

-

G

-

P

G

S

R

R

V

I

-

D

-

A

T

L

L

L

R

K

M

G

Y

R

D

R

S

L

L

T

K

K

P

P

I

L

I

I

G

A

A

A

I

V

N

E

G

G

A

P

A

A

V

I

G

A

V

G

G

G

V

T

T

E

M

I

Q

L

L

Q

P

G

M

T

D

D

I

I

R

R

L

V

A

A

S

G

T

E

E

S

A

A

K
|
K

F
|
F

G
|
G

F
x
I

V
x
S

F
x
E

A
|
A

R
x
K

R

W

G

S

I

L

N

Y

P

P

E

M

A

G

S

S

S

A

W

V

F

R

L

L

P

V

R

R

L

Q

V

I

G

P

L

Y

Q

T

T

L

A

A

L

C

E

D

W

L

C

L

Y

L

T

T

G

G

R

R

V

H

F

I

P

T

A

A

S

A

E

E

A

A

L

K

E

E

K

M

G

G

L

L

V

I

R

G

S

H

L

V

H

V

A

P

P

D

D

G

E

Q

L

A

L

L

P

T

A

K

A

A

R

L

A

E

L

L

A

A

R

D

E

A

I

I

A

S

D

A

N

N

T

G

A

P

P

L

V

A

S

V

V

Q

A

A

L

I

T

L

R

R

Q

S

L

I

L

-

W

-

R

R

M

E

A

T

G

E

A

C

D

M

H

P

P

E

M

N

E

E

A

A

H

F

K

K

A

I

D

D

S

T

R

Q

A

I

I

G

Q

I

S

K

R

V

G

F

S

L

S

S

G

D

D

D

A

A

K

K

E

E

G

G

V

P

T

R

S

A

F

F

L

A

E

E

K

K

R

R

A

A

P

P

V

N

Y

F

P

Q

N

N

K

R

K135 (= K143) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
135:142 (vs. 143:150, 50% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
K142 (≠ R150) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.

A5JTM5 4-chlorobenzoyl coenzyme A dehalogenase; 4-CBA-CoA dehalogenase; 4-CBCoA dehalogenase; 4-chlorobenzoyl-CoA dehalogenase; EC 3.8.1.7 from Pseudomonas sp. (strain CBS-3) (see 7 papers)
33% identity, 71% coverage: 6:214/294 of query aligns to 2:203/269 of A5JTM5

query
sites
A5JTM5

F

Y

E

E

T

A

L

I

L

G

Y

H

D

R

V

V

E

E

D

D

G

G

I

V

A

A

T

E

I

I

T

T

L

I

N

K

R

L

P

P

D

R

R

H

M
x
R

N

N

A

A

F

L

T

S

A

V

R

K

M

A

M

M

K

Q

D
x
E

L

V

I

T

E

D

V

A

F

L

D

N

V

R

T

A

D
x
E

A

E

D
|
D

A

S

V

V

K

G

V

A

V

V

I

M

I

I

T

T

G

G

A

A

G

E

R

D

A

A

F

F

C

C

A

A

G
|
G

A
x
F

D
x
Y

L

L

G

-

A

-

T

-

F

-

D

-

R
|
R

T
x
E

S

I

P

P

Q

-

A

-

L

L

E

D

R

K

E

G

E

V

G

A

K

G

V

V

G

R

D

D

I
x
H

Y
x
F

R

R

D

I

G

G

G

A

-

L

-

W

-
x
W

G
x
H

R

Q

V

M

T

I

L
x
H

R

K

M

I

Y

I

D

R

S

V

L

K

K

R

P

P

I

V

I

L

G

A

A

A

I

I

N

N

G

G

A

V

A

A

V
x
A

G
|
G

V
x
G

G
|
G

V

L

T

G

M

I

Q

S

L

L

P

A

M

S

D
|
D

I

M

R

A

L

I

A

C

S

A

T
x
D

E

S

A

A

K

K

F

F

G

V

F

C

V

A

F
x
W

A

H

R

T

R

I

G

G

I

I

N

G

P

N

E
x
D

A

T

A

A

S

T

S

S

W

Y

F

S

L

L

P

A

R

R

L

I

V

V

G

G

L

M

Q

R

T

R

A

A

L

M

E
|
E

W

L

C

M

Y

L

T

T

G

N

R

R

V

T

F

L

P

Y

A

P

S

E

E
|
E

A

A

L

K

E

D

K
x
W

G

G

L

L

V

V

R

S

S

R

L

V

H

Y

A

P

P

K

D

D

E

D

L

F

L

R

P

E

A

V

A

A

R

W

A

K

L

V

A

A

R

R

E

E

I

L

A

A

R24 (≠ M28) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
E34 (≠ D38) mutation to T: Forms inclusion bodies.
E43 (≠ D47) mutation to A: No effect on catalytic activity.
D45 (= D49) mutation to A: No effect on catalytic activity.
D46 (= D50) mutation to A: No effect on catalytic activity.
G63 (= G67) mutation G->A,I,P: Yields insoluble protein.
F64 (≠ A68) mutation to A: 30-fold reduction in catalytic activity, substrate benzoyl group binding is unaffected.; mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to P: Severely reduces catalytic activity. Arylated intermediate does not accumulate.
Y65 (≠ D69) mutation to D: Catalytic activity is almost as efficient as wild type.
R67 (= R79) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
E68 (≠ T80) mutation to T: No effect on catalytic activity.
H81 (≠ I95) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
F82 (≠ Y96) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
W89 (vs. gap) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
H90 (≠ G101) active site, Proton acceptor; mutation to Q: Complete loss of catalytic activity (PubMed:8718880, PubMed:9063883). Significantly reduced activity (PubMed:11695894). Substrate binding is not significantly affected. Reduced arylated intermediate formation.
H94 (≠ L105) mutation to Q: No effect on catalytic activity.
A112 (≠ V123) mutation to G: Yields insoluble protein.; mutation to S: Protein precipitates upon purification.; mutation to V: Catalytic activity is almost as efficient as wild type.
G113 (= G124) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding. Arylated intermediate does not accumulate.; mutation G->N,S: Strongly reduced catalytic activity. Arylated intermediate does not accumulate.; mutation to V: Protein precipitates upon purification.
G114 (≠ V125) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
G115 (= G126) mutation G->L,N,S,V: Yields insoluble protein.
D123 (= D134) mutation to T: No effect on catalytic activity.
D129 (≠ T140) mutation to T: No effect on catalytic activity.
W137 (≠ F148) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
D145 (≠ E156) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
E163 (= E174) mutation to T: No effect on catalytic activity.
E175 (= E186) mutation to D: No effect on catalytic activity.
W179 (≠ K190) mutation to F: No effect on catalytic activity.

Sites not aligning to the query:

208 H→Q: No effect on catalytic activity.
216 mutation R->E,K,L: Yields insoluble protein.
232 mutation E->A,N,Q,R: Yields insoluble protein.; E→D: Reduced catalytic activity, increased substrate binding.
257 R→K: Retains catalytic activity and substrate CoA binding.; R→L: Significantly reduces catalytic activity and substrate CoA binding.

Q4WF54 Mevalonyl-coenzyme A hydratase sidH; Siderophore biosynthesis protein H; EC 4.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
35% identity, 89% coverage: 17:277/294 of query aligns to 21:270/270 of Q4WF54

query
sites
Q4WF54

I

I

A

L

T

L

I

L

T

T

L

L

N

N

R

R

P

P

D

E

R

K

M

R

N

N

A

C

F

I

T

S

A

L

R

A

M

T

M

S

K

A

D

E

L

I

I

Q

E

R

V

L

F

W

D

T

V

W

T

F

D

D

A

T

D

Q

D

P

A

A

V

L

K

Y

V

V

V

A

I

I

T

T

G

G

A

T

G

G

R

E

A

S

F

F

C

C

A

A

G

G

A

A

D

D

L

L

-

K

-

E

-

W

-

N

-

D

-

L

G

N

G

A

G

R

G

G

A

I

T

T

F

N

D

E

R

M

T

T

S

A

P

P

Q

-

A

-

L

-

E

-

R

-

E

-

G

G

K

L

V

A

G

G

D

L

I

P

Y

R

R

R

D

R

G

G

G

S

G

-

R

-

V

-

T

-

L

-

R

-

M

-

Y

-

D

-

S

-

L

-

K

K

P

P

I

I

G

A

A

A

I

V

N

N

G

G

A

Y

A

C

V

L

G

G

V

G

G

G

V

F

T

E

M

M

Q

V

L

A

P

N

M

C

D

D

I

I

R

V

L

V

A

A

S

S

T

E

E

N

A

A

K

T

F

F

G

G

F

L

V

P

F

E

A

V

R

Q

R

R

G

G

I

I

N

A

P

A

E

V

A

A

A

G

S

S

S

L

W

P

F

R

L

L

P

V

R

R

L

V

V

L

G

G

L

K

Q

Q

T

R

A

A

L

A

E

E

W

I

C

A

Y

L

T

S

G

G

R

L

V

S

F

F

P

S

A

A

S

S

E

Q

A

L

L

E

E

R

K

W

G

G

L

L

V

V

R

N

S

R

L

V

H

V

A

E

P

H

D

D

E

Q

L

L

P

A

A

T

A

A

R

V

A

E

L

I

A

A

R

T

E

A

I

I

A

S

D

R

N

N

T

S

A

-

P

P

V

D

S

S

V

V

A

R

L

V

T

T

R

M

Q

E

L

G

L

L

-

H

-

Y

-

G

W

W

R

E

M

M

A

A

G

S

A

V

D

E

H

-

P

-

M

-

E

E

A

A

H

S

K

S

A

A

D

L

S

V

R

D

A

Q

I

W

Q

Y

S

A

R

K

G

L

S

M

S

A

G

G

D

E

A

N

-

F

K

H

E

E

G

G

V

V

T

R

S

A

F

F

L

V

E

E

K

K

R

R

A

K

P

P

V

Q

Y

W

-

R

P

P

N
x
S

K
|
K

V
x
L

SKL 268:270 (≠ NKV 275:277) PTS1-type peroxisomal targeting signal

1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
33% identity, 71% coverage: 6:214/294 of query aligns to 2:203/269 of 1jxzB

query
sites
1jxzB

F

Y

E

E

T

A

L

I

L

G

Y

H

D

R

V

V

E

E

D

D

G

G

I

V

A

A

T

E

I

I

T

T

L

I

N

K

R

L

P

P

D
x
R

R
x
H

M
x
R

N

N

A
|
A

F

L

T

S

A

V

R

K

M

A

M

M

K

Q

D

E

L

V

I

T

E

D

V

A

F

L

D

N

V

R

T

A

D

E

A

E

D

D

A

S

V

V

K
x
G

V

A

V

V

I

M

I

I

T

T

G

G

A

A

G

E

R

D

A

A

F

F

C
|
C

A
|
A

G
|
G

A
x
F

D
x
Y

L
|
L

G

-

A

-

T

-

F

-

D

-

R
|
R

T

E

S
x
I

P

P

Q

-

A

-

L

L

E

D

R

K

E

G

E

V

G

A

K

G

V

V

G

R

D

D

I

H

Y

F

R

R

D

I

G

A

G
x
A

-

L

-

W

-
x
W

G
x
Q

R

Q

V

M

T

I

L

H

R

K

M

I

Y

I

D

R

S

V

L

K

K

R

P

P

I

V

I

L

G

A

A

A

I

I

N

N

G

G

A

V

A

A

V

A

G
|
G

V
x
G

G

G

V

L

T
x
G

M

I

Q

S

L

L

P

A

M

S

D

D

I

M

R

A

L

I

A

C

S

A

T

D

E

S

A

A

K

K

F

F

G

V

F

C

V
x
A

F
x
W

A

H

R

T

R
x
I

G

G

I
|
I

N

G

P
x
N

E
x
D

A
x
T

A

A

S

T

S

S

W

Y

F

S

L

L

P

A

R

R

L

I

V

V

G

G

L

M

Q

R

T

R

A

A

L

M

E

E

W

L

C

M

Y

L

T

T

G

N

R

R

V

T

F

L

P

Y

A

P

S

E

E

E

A

A

L

K

E

D

K

W

G

G

L

L

V

V

R

S

S

R

L

V

H

Y

A

P

P

K

D

D

E

E

L

F

L

R

P

E

A

V

A

A

R

W

A

K

L

V

A

A

R

R

E

E

I
x
L

A
|
A

active site: C61 (= C65), F64 (≠ A68), I69 (≠ S81), A86 (≠ G100), Q90 (≠ G101), G113 (= G124), G114 (≠ V125), G117 (≠ T128), A136 (≠ V147), W137 (≠ F148), I142 (= I153), N144 (≠ P155), D145 (≠ E156)
binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D26), H23 (≠ R27), R24 (≠ M28), A26 (= A30), A62 (= A66), G63 (= G67), F64 (≠ A68), Y65 (≠ D69), L66 (= L70), R67 (= R79), A86 (≠ G100), W89 (vs. gap), G113 (= G124), G114 (≠ V125), A136 (≠ V147), W137 (≠ F148), I140 (≠ R151), I142 (= I153), D145 (≠ E156), T146 (≠ A157)
binding calcium ion: G49 (≠ K53), L202 (≠ I213), A203 (= A214)

Sites not aligning to the query:

active site: 230
binding 4-hydroxybenzoyl coenzyme a: 236, 252, 257
binding calcium ion: 205, 207, 210

1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
33% identity, 71% coverage: 6:214/294 of query aligns to 2:203/269 of 1nzyB

query
sites
1nzyB

F

Y

E

E

T

A

L

I

L

G

Y

H

D

R

V

V

E

E

D

D

G

G

I

V

A

A

T

E

I

I

T

T

L

I

N

K

R

L

P

P

D
x
R

R
x
H

M
x
R

N

N

A
|
A

F

L

T

S

A

V

R

K

M

A

M

M

K

Q

D

E

L

V

I

T

E

D

V

A

F

L

D

N

V

R

T

A

D

E

A

E

D

D

A

S

V

V

K
x
G

V

A

V

V

I

M

I

I

T

T

G

G

A

A

G
x
E

R
x
D

A

A

F

F

C
|
C

A
|
A

G
|
G

A
x
F

D
x
Y

L
|
L

G

-

A

-

T

-

F

-

D

-

R
|
R

T

E

S
x
I

P

P

Q

-

A

-

L

L

E

D

R

K

E

G

E

V

G

A

K

G

V

V

G

R

D

D

I

H

Y

F

R

R

D

I

G

A

G
x
A

-

L

-

W

-
x
W

G
x
H

R

Q

V

M

T

I

L

H

R

K

M

I

Y

I

D

R

S

V

L

K

K

R

P

P

I

V

I

L

G

A

A

A

I

I

N
|
N

G

G

A

V

A

A

V
x
A

G
|
G

V
x
G

G

G

V

L

T
x
G

M

I

Q

S

L

L

P

A

M

S

D

D

I

M

R

A

L

I

A

C

S

A

T

D

E

S

A

A

K

K

F

F

G

V

F

C

V
x
A

F
x
W

A

H

R

T

R
x
I

G

G

I
|
I

N

G

P
x
N

E
x
D

A
x
T

A

A

S

T

S

S

W

Y

F

S

L

L

P

A

R

R

L

I

V

V

G

G

L

M

Q

R

T

R

A

A

L

M

E

E

W

L

C

M

Y

L

T

T

G

D

R

R

V

T

F

L

P

Y

A

P

S

E

E

E

A

A

L

K

E

D

K

W

G

G

L

L

V

V

R

S

S

R

L

V

H

Y

A

P

P
x
K

D

D

E

E

L
x
F

L
x
R

P

E

A

V

A

A

R

W

A

K

L

V

A

A

R

R

E

E

I
x
L

A
|
A

active site: C61 (= C65), F64 (≠ A68), I69 (≠ S81), A86 (≠ G100), H90 (≠ G101), G114 (≠ V125), G117 (≠ T128), A136 (≠ V147), W137 (≠ F148), I142 (= I153), N144 (≠ P155), D145 (≠ E156)
binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D26), H23 (≠ R27), R24 (≠ M28), A26 (= A30), A62 (= A66), G63 (= G67), F64 (≠ A68), Y65 (≠ D69), L66 (= L70), R67 (= R79), W89 (vs. gap), A112 (≠ V123), G113 (= G124), G114 (≠ V125), A136 (≠ V147), W137 (≠ F148), I140 (≠ R151), I142 (= I153), D145 (≠ E156), T146 (≠ A157)
binding calcium ion: G49 (≠ K53), L202 (≠ I213), A203 (= A214)
binding phosphate ion: E57 (≠ G61), D58 (≠ R62), N108 (= N119), K188 (≠ P199), F191 (≠ L202), R192 (≠ L203)

Sites not aligning to the query:

active site: 230
binding 4-hydroxybenzoyl coenzyme a: 252, 257
binding calcium ion: 205, 207, 210

5jbxC Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
33% identity, 87% coverage: 21:276/294 of query aligns to 19:261/261 of 5jbxC

query
sites
5jbxC

T

T

L

I

N

D

R

G

P

E

D

S

R

R

M

R

N

N

A

A

F

I

T

S

A

R

R

A

M

M

M

L

K

K

D

E

L

L

I

G

E

E

V

L

F

V

D

T

V

R

T

V

D

S

A

S

D

S

D

R

A

D

V

V

K

R

V

A

V

V

I

V

I

I

T

T

G

G

A

A

G

G

-

D

R

K

A

A

F

F

C

C

A

A

G

G

A
|
A

D

D

L

L

G

-

A

-

T

-

F

-

D

-

R

-

T

K

S

E

P
x
R

Q

A

A

T

L

M

E

A

R

E

E

D

E

E

G

V

K

R

V

A

G

-

D

-

I

-

Y

F

R
x
L

D

D

G

G

G

L

G
x
R

R

R

V

T

T

F

L

R

R

A

M

I

Y

E

D

K

S

S

L

D

K

C

P

V

I

F

I

I

G

A

A

A

I

I

N

N

G

G

A

A

V

L

G

G

V
x
G

G

G

V

T

T
x
E

M

L

Q

A

L

L

P

A

M

C

D

D

I

L

R

R

L

V

A

A

S

A

T

P

E

A

A

A

K

E

F

L

G

G

F

L

V
x
T

F
x
E

A

V

R

K

R

L

G

G

I
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I

N

I

P
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P

E
x
G

A

G

S

G

S

T

W

Q

F

R

L

L

P

A

R

R

L

L

V

V

G

G

L

P

Q

G

T

R

A

A

L

K

E

D

W

L

C

I

Y

L

T

T

G

A

R

R

V

R

F

I

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N

A

A

S

A

E

E

A

A

L

F

E

S

K

V

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G

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L

V

A

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N

S

R

L

L

H

A

A

P

P

E

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G

E

H

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L

P

A

A

V

A

A

R

Y

A

G

L

L

A

A

R

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E

S

I

V

A

V

D

E

N

N

T

-

A

A

P

P

V

I

S

A

V

V

A

A

L

T

T

A

R

K

Q

H

L

A

L

I

W

D

R

E

M

G

A

T

G

G

A

L

D

E

H

L

P

D

M

-

E

D

A

A

H

L

K
x
A

A

L

D

E

S

L

R

R

A

K

I

Y

Q

E

S

E

R

I

G
x
L

S

K

S

T

G

E

D

D

A

R

K

L

E

E

G

G

V

L

T

R

S

A

F
|
F

L

A

E

E

K
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K

R

R

A

A

P

P

V

V

Y

Y

P

K

N

G

K

R

active site: A67 (= A68), R72 (≠ P82), L84 (≠ R97), R88 (≠ G101), G112 (≠ V125), E115 (≠ T128), T134 (≠ V147), E135 (≠ F148), I140 (= I153), P142 (= P155), G143 (≠ E156), A228 (≠ K243), L238 (≠ G253)
binding coenzyme a: F250 (= F265), K253 (= K268)

Q8GYN9 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal; DHNS; Enoyl-CoA hydratase/isomerase D; ECHID; Naphthoate synthase; EC 4.1.3.36 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
28% identity, 91% coverage: 6:273/294 of query aligns to 74:330/337 of Q8GYN9

query
sites
Q8GYN9

F

F

E

V

T

D

L

I

Y

Y

D

E

-

K

-

A

V

L

E

D

D

E

G

G

I

I

A

A

T

K

I

I

T

T

L

I

N

N

R

R

P

P

D

E

R

R

M

R

N

N

A

A

F

F

T

R

A

P

R

Q

M

T

M

V

K

K

D

E

L

L

I

M

E

R

V

A

F

F

D

N

V

D

T

A

D

R

A

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D

D

D

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A

S

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V

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G

V

V

V

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I

I

I

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T

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G

A

K

G

G

-

T

R

K

A

A

F

F

C

C

A

S

G

G

A

G

D

D

L

-

G

-

A

-

T

-

F

-

D

-

R

-

T

-

S

-

P

-

Q

Q

A

A

L

L

E

R

R

T

E

Q

E

D

G

G

K

Y

V

A

-

D

-

P

G

N

D

D

I

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Y

G

R

R

D

L

G

N

G

V

G

L

R

D

V

L

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Q

L

V

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Q

M

I

Y

R

D

R

S

L

L

P

K

K

P

P

I

V

I

I

G

A

A

M

I

V

N

A

G

G

A

Y

A

A

V

V

G

G

V

G

G

G

V

H

T

I

M

L

Q

H

L

M

P

V

M

C

D

D

I

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R

T

L

I

A

A

S

A

T

D

E

N

A

A

K

I

F

F

G

G

F

Q

V

T

F

G

A

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K

R

V

G

G

I

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N

F

P

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E

A

A

G

A

Y

S

G

S

S

W

S

F

I

L

M

P

S

R

R

L

L

V

V

G

G

L

P

Q

K

T

K

A

A

L

R

E

E

W

M

C

W

Y

F

T

M

G

T

R

R

V

F

F

Y

P

T

A

A

S

S

E

E

A

A

L

E

E

K

K

M

G

G

L

L

V

I

R

N

S

T

L

V

H

V

A

P

P

L

D

E

E

D

L

L

L

E

P

K

A

E

A

T

R

V

A

K

L

W

A

C

R

R

E

E

I

I

A

L

D

R

N

N

T

S

A

-

P

P

V

T

S

A

V

I

A

R

L

V

T

L

R

K

Q

A

L

A

L

L

W

N

R

A

M

V

A

D

G

D

A

G

D

H

H

A

P

G

M

L

E

Q

A

G

H

L

K

G

A

G

D

D

S

A

R

T

A

L

I

L

Q

F

S

Y

R

-

G

-

S

G

S

T

G

E

D

E

A

A

K

T

E

E

G

G

V

R

T

T

S

A

F

Y

L

M

E

H

K

R

R

R

A

P

P

P

V

D

Y

F

Sites not aligning to the query:

20 H→V: Loss of peroxisomal targeting.

Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
29% identity, 90% coverage: 6:271/294 of query aligns to 12:264/273 of Q5HH38

query
sites
Q5HH38

F

Y

E

D

T

E

L

I

L

K

Y

Y

D

E

V

F

E

Y

D

E

G

G

I

I

A

A

T

K

I

V

T

T

L

I

N

N

R

R

P

P

D

E

R

V

M
x
R

N

N

A

A

F

F

T

T

A

P

R

K

M

T

M

V

K

A

D

E

L

M

I

I

E

D

V

A

F

F

D

S

V

R

T

A

D

R

A

D

D

D

D

Q

A

N

V

V

K

S

V

V

V

I

I

V

I

L

T

T

G

G

A

E

G

G

R

D

-

L

A

A

F

F

C

C

A
x
S

G
|
G

A
x
G

D
|
D

L
x
Q

-

K

-

R

G

G

G

H

G

G

A

Y

T

V

F

G

D

E

R

D

T

Q

S

I

P

P

Q

R

A

L

L

-

E

-

R

-

E

-

G

-

K

N

V

V

G

L

D

D

I

L

Y

Q

R

R

D

-

G

-

R

-

V

-

T

L

L

I

R

R

M

I

Y

I

D

P

S

-

L

-

K

K

P

P

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I

I

G

A

A

M

I

V

N

K

G

G

A

Y

A

A

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G

G

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G

G

G

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N

L

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C

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I

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L

I

A

A

S

A

T

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E

N

A

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I

F

F

G

G

F

Q

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F

G

A

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K

R

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G

G

I
x
S

N

F

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E

A

A

G

A

Y

S

G

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W

G

F

Y

L

L

P

A

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R

L

I

V

V

G

G

L

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Q

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K

A

A

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E

E

W

I

C

W

Y

Y

T

L

G

C

R

R

V

Q

F

Y

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N

A

A

S

Q

E

E

A

A

L

L

E

D

K

M

G

G

L

L

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N

S

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L

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H

V

A

P

P

L

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E

E

K

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L

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P

D

A

E

A

T

R

V

A

Q

L

W

A

C

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K

E

E

I

I

A

M

D

K

N

H

T

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A

-

P

P

V

T

S

A

V

L

A

R

L

F

T

L

R

K

Q

A

L

A

L

M

W

-

R

-

M

N

A

A

G

D