SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_078429031.1 NCBI__GCF_002019605.1:WP_078429031.1 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)

Q13825 Methylglutaconyl-CoA hydratase, mitochondrial; 3-MG-CoA hydratase; AU-specific RNA-binding enoyl-CoA hydratase; AU-binding protein/enoyl-CoA hydratase; Itaconyl-CoA hydratase; EC 4.2.1.18; EC 4.2.1.56 from Homo sapiens (Human) (see 4 papers)
51% identity, 97% coverage: 10:260/260 of query aligns to 85:339/339 of Q13825

query
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Q13825

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K105 (≠ L30) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
105:119 (vs. 30:44, 20% identical) RNA-binding
K109 (≠ Y34) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
K113 (≠ E38) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
A240 (= A165) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315

Sites not aligning to the query:

1:67 modified: transit peptide, Mitochondrion

5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
43% identity, 100% coverage: 1:260/260 of query aligns to 1:259/259 of 5zaiC

query
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5zaiC

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active site: A65 (= A66), F70 (≠ R71), S82 (≠ V83), R86 (≠ Q87), G110 (= G111), E113 (= E114), P132 (≠ T133), E133 (= E134), I138 (= I139), P140 (= P141), G141 (= G142), A226 (= A227), F236 (≠ I237)
binding coenzyme a: K24 (≠ A24), L25 (≠ A25), A63 (= A64), G64 (= G65), A65 (= A66), D66 (= D67), I67 (≠ L68), P132 (≠ T133), R166 (= R167), F248 (= F249), K251 (= K252)

5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
47% identity, 93% coverage: 18:259/260 of query aligns to 19:260/261 of 5jbxB

query
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5jbxB

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active site: A67 (= A66), R72 (= R71), L84 (≠ V83), R88 (≠ Q87), G112 (= G111), E115 (= E114), T134 (= T133), E135 (= E134), I140 (= I139), P142 (= P141), G143 (= G142), A228 (= A227), L238 (≠ I237)
binding coenzyme a: S24 (≠ E23), R25 (≠ A24), R26 (≠ A25), A28 (= A27), A65 (= A64), D68 (= D67), L69 (= L68), K70 (= K69), L110 (≠ F109), G111 (= G110), T134 (= T133), E135 (= E134), L138 (= L137), R168 (= R167)

3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
40% identity, 99% coverage: 1:258/260 of query aligns to 1:255/255 of 3q0jC

query
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3q0jC

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active site: A65 (= A66), M70 (≠ R71), T80 (≠ V83), F84 (≠ Q87), G108 (= G111), E111 (= E114), P130 (≠ T133), E131 (= E134), V136 (≠ I139), P138 (= P141), G139 (= G142), L224 (≠ A227), F234 (≠ I237)
binding acetoacetyl-coenzyme a: Q23 (≠ E23), A24 (= A24), L25 (≠ A25), A27 (= A27), A63 (= A64), G64 (= G65), A65 (= A66), D66 (= D67), I67 (≠ L68), K68 (= K69), M70 (≠ R71), F84 (≠ Q87), G107 (= G110), G108 (= G111), E111 (= E114), P130 (≠ T133), E131 (= E134), P138 (= P141), G139 (= G142), M140 (≠ A143)

3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
40% identity, 99% coverage: 1:258/260 of query aligns to 1:255/255 of 3q0gC

query
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3q0gC

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x
Y

A

A

F

L

G

G

G
|
G

G

G

L

C

E
|
E

L

L

A

A

L

M

A

M

C

C

D

D

I

V

R

L

I

I

A

A

D

D

H

T

I

A

K

K

V

F

G

G

L

Q

T
x
P

E
|
E

T

I

S

K

L
|
L

A

G

I
x
V

I

L

P
|
P

G
|
G

A

M

G

G

T

S

Q

Q

R

R

L

L

P

T

R

R

L

A

I

I

G

G

K

K

G

A

K

K

A

A

K

M

E

D

L

L

I

I

Y

L

T

T

A

G

R

R

R

T

V

M

D

D

A

A

Y

A

E

E

A

A

E

E

K

R

I

S

G

G

L

L

V

V

E

S

Y

R

V

V

S

P

L

A

E

D

N

D

L

L

D

L

E

T

K

E

V

A

N

R

E

A

I

T

T

A

T

T

L

T

I

I

A

S

K

Q

N

M

G

S

P

A

V

S

A

A

L

A

Q

R

Q

M

A

A

K

K

Y

E

A

A

I

V

D

N

K

R

G

A

L

F

E

E

V

S

D

S

L

L

Q

S

T

E

G

G

L

L

A
x
L

I

Y

E

E

R

R

K

R

A

L

Y

F

E

H

V

S

T

A

I
x
F

P

A

T

T

K

E

D

D

R

Q

I

S

E

E

G

G

L

M

T

A

A

A

F

F

K

I

E

E

K

K

R

R

T

A

P

P

K

Q

Y

F

T

T

active site: A65 (= A66), M70 (≠ R71), T80 (≠ V83), F84 (≠ Q87), G108 (= G111), E111 (= E114), P130 (≠ T133), E131 (= E134), V136 (≠ I139), P138 (= P141), G139 (= G142), L224 (≠ A227), F234 (≠ I237)
binding coenzyme a: L25 (≠ A25), A63 (= A64), I67 (≠ L68), K68 (= K69), Y104 (≠ S107), P130 (≠ T133), E131 (= E134), L134 (= L137)

3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
40% identity, 98% coverage: 4:258/260 of query aligns to 3:254/256 of 3h81A

query
sites
3h81A

K

E

V

T

V

I

L

L

V

V

I

E

D

R

E

D

T

Q

G

R

V

V

A

G

H

I

I

I

T

T

L

L

D

N

R

R

P

P

E

Q

A

A

A

L

N

N

A

A

L

L

S

N

L

S

Q

Q

M

V

L

M

Y

N

E

E

L

V

H

T

E

S

A

A

I

A

Q

T

E

E

V

L

K

D

F

D

N

D

P

P

E

D

V

I

R

G

C

A

V

I

I

I

K

T

A

G

S

S

G

A

E

-

K

K

V

A

F

F

C

A

A

A

G

G

A
|
A

D

D

L

I

K

K

E

E

R
x
M

A

A

G

D

M

L

E

T

P

F

V

A

Q

D

V

A

K

-

R

-

T

F

V
x
T

S

A

L

D

I

F

Q
x
F

G

A

N

T

I

W

N

G

D

K

I

L

E

A

A

A

L

V

P

R

Q

T

P

P

V

T

I

I

C

A

A

A

L

V

N

A

G

G

S

Y

A

A

F

L

G

G

G
|
G

G

G

L

C

E
|
E

L

L

A

A

L

M

A

M

C

C

D

D

I

V

R

L

I

I

A

A

D

D

H

T

I

A

K

K

V

F

G

G

L

Q

T
x
P

E
|
E

T

I

S

K

L

L

A

G

I
x
V

I

L

P
|
P

G
|
G

A

M

G

G

T

S

Q

Q

R

R

L

L

P

T

R

R

L

A

I

I

G

G

K

K

G

A

K

K

A

A

K

M

E

D

L

L

I

I

Y

L

T

T

A

G

R

R

R

T

V

M

D

D

A

A

Y

A

E

E

A

A

E

E

K

R

I

S

G

G

L

L

V

V

E

S

Y

R

V

V

S

P

L

A

E

D

N

D

L

L

D

L

E

T

K

E

V

A

N

R

E

A

I

T

T

A

T

T

L

T

I

I

A

S

K

Q

N

M

G

S

P

A

V

S

A

A

L

A

Q

R

Q

M

A

A

K

K

Y

E

A

A

I

V

D

N

K

R

G

A

L

F

E

E

V

S

D

S

L

L

Q

S

T

E

G

G

L

L

A
x
L

I

Y

E

E

R

R

K

R

A

L

Y

F

E

H

V

S

T

A

I
x
F

P

A

T

T

K

E

D

D

R
x
Q

I

S

E

E

G

G

L

M

T

A

A

A

F

F

K

I

E

E

K

K

R

R

T

A

P

P

K

Q

Y

F

T

T

active site: A64 (= A66), M69 (≠ R71), T79 (≠ V83), F83 (≠ Q87), G107 (= G111), E110 (= E114), P129 (≠ T133), E130 (= E134), V135 (≠ I139), P137 (= P141), G138 (= G142), L223 (≠ A227), F233 (≠ I237)
binding calcium ion: F233 (≠ I237), Q238 (≠ R242)

3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
39% identity, 98% coverage: 4:258/260 of query aligns to 3:250/250 of 3q0gD

query
sites
3q0gD

K

E

V

T

V

I

L

L

V

V

I

E

D

R

E

D

T

Q

G

R

V

V

A

G

H

I

I

I

T

T

L

L

D

N

R

R

P

P

E

Q

A

A

A

L

N

N

A

A

L

L

S

N

L

S

Q

Q

M

V

L

M

Y

N

E

E

L

V

H

T

E

S

A

A

I

A

Q

T

E

E

V

L

K

D

F

D

N

D

P

P

E

D

V

I

R

G

C

A

V

I

I

I

K

T

A

G

S

S

G

A

E

-

K

K

V

A

F

F

C

A

A

A

G

G

A
|
A

D

D

L

I

K

K

E

E

R

-

A

-

G

-

M

-

E

-

P

-

V
x
M

Q

F

V

A

K

D

R

A

T

F

V
x
T

S

A

L

D

I

F

Q
x
F

G

A

N

T

I

W

N

G

D

K

I

L

E

A

A

A

L

V

P

R

Q

T

P

P

V

T

I

I

C

A

A

A

L

V

N

A

G

G

S

Y

A

A

F

L

G

G

G
|
G

G

G

L

C

E
|
E

L

L

A

A

L

M

A

M

C

C

D

D

I

V

R

L

I

I

A

A

D

D

H

T

I

A

K

K

V

F

G

G

L

Q

T
x
P

E
|
E

T

I

S

K

L

L

A

G

I
x
V

I

L

P
|
P

G
|
G

A

M

G

G

T

S

Q

Q

R

R

L

L

P

T

R

R

L

A

I

I

G

G

K

K

G

A

K

K

A

A

K

M

E

D

L

L

I

I

Y

L

T

T

A

G

R

R

R

T

V

M

D

D

A

A

Y

A

E

E

A

A

E

E

K

R

I

S

G

G

L

L

V

V

E

S

Y

R

V

V

S

P

L

A

E

D

N

D

L

L

D

L

E

T

K

E

V

A

N

R

E

A

I

T

T

A

T

T

L

T

I

I

A

S

K

Q

N

M

G

S

P

A

V

S

A

A

L

A

Q

R

Q

M

A

A

K

K

Y

E

A

A

I

V

D

N

K

R

G

A

L

F

E

E

V

S

D

S

L

L

Q

S

T

E

G

G

L

L

A
x
L

I

Y

E

E

R

R

K

R

A

L

Y
x
F

E

H

V

S

T

A

I
x
F

P

A

T

T

K

E

D

D

R

Q

I

S

E

E

G

G

L

M

T

A

A

A

F
|
F

K

I

E

E

K

K

R

R

T

A

P

P

K

Q

Y

F

T

T

active site: A64 (= A66), M69 (≠ V77), T75 (≠ V83), F79 (≠ Q87), G103 (= G111), E106 (= E114), P125 (≠ T133), E126 (= E134), V131 (≠ I139), P133 (= P141), G134 (= G142), L219 (≠ A227), F229 (≠ I237)
binding Butyryl Coenzyme A: F225 (≠ Y233), F241 (= F249)

2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
38% identity, 95% coverage: 12:257/260 of query aligns to 14:251/254 of 2dubA

query
sites
2dubA

T

S

G

S

V

V

A

G

H

L

I

I

T

Q

L

L

D

N

R

R

P

P

E
x
K

A
|
A

A
x
L

N

N

A
|
A

L

L

S

C

L

N

Q

G

M

L

L

I

Y

E

E

E

L

L

H

N

E

Q

A

A

I

L

Q

E

E

T

V

F

K

E

F

E

N

D

P

P

E

A

V

V

R

G

C

A

V

I

V

V

I

L

K

-

A

T

S

G

G

G

E

E

K

K

V

A

F

F

C

A

A
|
A

G

G

A
|
A

D
|
D

L
x
I

K
|
K

E

E

R
x
M

A

Q

G

-

M

-

E

-

P

-

V

-

Q

-

V

-

K

N

R

R

T

T

V

F

S

Q

L

D

I

C

Q

Y

G
x
S

N

H

I

W

N

D

D

H

I

I

E

T

A

R

L

I

P

K

Q

K

P

P

V

V

I

I

C

A

A

A

L

V

N

N

G

G

S

Y

A

A

F

L

G

G

G
|
G

G

G

L

C

E
|
E

L

L

A

A

L

M

A

M

C

C

D

D

I

I

R

I

I

Y

A

A

A

G

D

E

H

K

I

A

K

Q

V

F

G

G

L

Q

T
x
P

E
|
E

T

I

S

L

L

L

A

G

I
x
T

I

I

P
|
P

G
|
G

A
|
A

G

G

T

T

Q

Q

R

R

L

L

P

T

R

R

L

A

I

V

G

G

K

K

G

S

K

L

A

A

K

M

E

E

L

M

I

V

Y

L

T

T

A

G

R

D

R

R

V

I

D

S

A

A

Y

Q

E

D

A

A

E

K

K

Q

I

A

G

G

L

L

V

V

E

S

Y

K

V

I

V

F

S

P

L

V

E

E

N

T

L

L

D

V

E

E

K

E

V

A

N

I

E

Q

I

C

T

A

T

E

L

K

I

I

A

A

K

N

N

N

G

S

P

K

V

I

A

I

L

V

Q

A

Q

M

A

A

K

K

Y

E

A

S

I

V

D

N

K

A

G

A

L

F

E

E

V

M

D

T

L

L

Q

T

T

E

G

G

L

N

A
x
K

I

L

E

E

R

K

K

K

A

L

Y

F

E

Y

V

S

T

T

I
x
F

P

A

T

T

K

D

D

D

R

R

I

R

E

E

G

G

L

M

T

S

A

A

F

F

K

V

E

E

K

K

R

R

T

K

P

A

K

N

Y

F

active site: A67 (= A66), M72 (≠ R71), S82 (≠ G88), G105 (= G111), E108 (= E114), P127 (≠ T133), E128 (= E134), T133 (≠ I139), P135 (= P141), G136 (= G142), K221 (≠ A227), F231 (≠ I237)
binding octanoyl-coenzyme a: K25 (≠ E23), A26 (= A24), L27 (≠ A25), A29 (= A27), A65 (= A64), A67 (= A66), D68 (= D67), I69 (≠ L68), K70 (= K69), G105 (= G111), E108 (= E114), P127 (≠ T133), E128 (= E134), G136 (= G142), A137 (= A143)

1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
38% identity, 95% coverage: 12:257/260 of query aligns to 15:255/258 of 1mj3A

query
sites
1mj3A

T

S

G

S

V

V

A

G

H

L

I

I

T

Q

L

L

D

N

R

R

P

P

E
x
K

A
|
A

A
x
L

N

N

A
|
A

L

L

S

C

L

N

Q

G

M

L

L

I

Y

E

E

E

L

L

H

N

E

Q

A

A

I

L

Q

E

E

T

V

F

K

E

F

E

N

D

P

P

E

A

V

V

R

G

C

A

V

I

V

V

I

L

K

-

A

T

S

G

G

G

E

E

K

K

V

A

F

F

C

A

A
|
A

G
|
G

A
|
A

D
|
D

L
x
I

K

K

E

E

R

-

A

-

G

-

M
|
M

E

Q

P

N

V

R

Q

T

V

F

K

Q

R

D

T

C

V

Y

S
|
S

L

G

I
x
L

Q

S

G

-

N

H

I

W

N

D

D

H

I

I

E

T

A

R

L

I

P

K

Q

K

P

P

V

V

I

I

C

A

A

A

L

V

N

N

G

G

S

Y

A

A

F

L

G

G

G
|
G

G

G

L

C

E
|
E

L

L

A

A

L

M

A

M

C

C

D

D

I

I

R

I

I

Y

A

A

A

G

D

E

H

K

I

A

K

Q

V

F

G

G

L

Q

T
x
P

E
|
E

T

I

S

L

L
|
L

A

G

I
x
T

I

I

P
|
P

G
|
G

A

A

G

G

T

T

Q

Q

R

R

L

L

P

T

R

R

L

A

I

V

G

G

K

K

G

S

K

L

A

A

K

M

E

E

L

M

I

V

Y

L

T

T

A

G

R

D

R

R

V

I

D

S

A

A

Y

Q

E

D

A

A

E

K

K

Q

I

A

G

G

L

L

V

V

E

S

Y

K

V

I

V

F

S

P

L

V

E

E

N

T

L

L

D

V

E

E

K

E

V

A

N

I

E

Q

I

C

T

A

T

E

L

K

I

I

A

A

K

N

N

N

G

S

P

K

V

I

A

I

L

V

Q

A

Q

M

A

A

K

K

Y

E

A

S

I

V

D

N

K

A

G

A

L

F

E

E

V

M

D

T

L

L

Q

T

T

E

G

G

L

N

A
x
K

I

L

E

E

R

K

K

K

A

L

Y

F

E

Y

V

S

T

T

I
x
F

P

A

T

T

K

D

D

D

R

R

I

R

E

E

G

G

L

M

T

S

A

A

F

F

K

V

E

E

K

K

R

R

T

K

P

A

K

N

Y

F

active site: A68 (= A66), M73 (= M74), S83 (= S84), L85 (≠ I86), G109 (= G111), E112 (= E114), P131 (≠ T133), E132 (= E134), T137 (≠ I139), P139 (= P141), G140 (= G142), K225 (≠ A227), F235 (≠ I237)
binding hexanoyl-coenzyme a: K26 (≠ E23), A27 (= A24), L28 (≠ A25), A30 (= A27), A66 (= A64), G67 (= G65), A68 (= A66), D69 (= D67), I70 (≠ L68), G109 (= G111), P131 (≠ T133), E132 (= E134), L135 (= L137), G140 (= G142)

1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
38% identity, 95% coverage: 12:257/260 of query aligns to 15:257/260 of 1dubA

query
sites
1dubA

T

S

G

S

V

V

A

G

H

L

I

I

T

Q

L

L

D

N

R

R

P

P

E
x
K

A
|
A

A
x
L

N

N

A
|
A

L

L

S

C

L

N

Q

G

M

L

L

I

Y

E

E

E

L

L

H

N

E

Q

A

A

I

L

Q

E

E

T

V

F

K

E

F

E

N

D

P

P

E

A

V

V

R

G

C

A

V

I

V

V

I

L

K

-

A

T

S

G

G

G

E

E

K

K

V

A

F

F

C

A

A
|
A

G

G

A
|
A

D
|
D

L
x
I

K

K

E

E

R

-

A

-

G

-

M
|
M

E

Q

P

N

V

R

Q

T

V

F

K

Q

R

D

T

C

V

Y

S
|
S

-

G

L

K

I

F

Q
x
L

G

S

N

H

I

W

N

D

D

H

I

I

E

T

A

R

L

I

P

K

Q

K

P

P

V

V

I

I

C

A

A

A

L

V

N

N

G

G

S
x
Y

A

A

F

L

G
|
G

G

G

L

C

E
|
E

L

L

A

A

L

M

A

M

C

C

D

D

I

I

R

I

I

Y

A

A

A

G

D

E

H

K

I

A

K

Q

V

F

G

G

L

Q

T
x
P

E
|
E

T

I

S

L

L
|
L

A

G

I
x
T

I

I

P
|
P

G
|
G

A

A

G

G

T

T

Q

Q

R

R

L

L

P

T

R

R

L

A

I

V

G

G

K

K

G

S

K

L

A

A

K

M

E

E

L

M

I

V

Y

L

T

T

A

G

R

D

R

R

V

I

D

S

A

A

Y

Q

E

D

A

A

E

K

K

Q

I

A

G

G

L

L

V

V

E

S

Y

K

V

I

V

F

S

P

L

V

E

E

N

T

L

L

D

V

E

E

K

E

V

A

N

I

E

Q

I

C

T

A

T

E

L

K

I

I

A

A

K

N

N

N

G

S

P

K

V

I

A

I

L

V

Q

A

Q

M

A

A

K

K

Y

E

A

S

I

V

D

N

K

A

G

A

L

F

E

E

V

M

D

T

L

L

Q

T

T

E

G

G

L

N

A
x
K

I

L

E

E

R

K

K

K

A

L

Y
x
F

E

Y

V

S

T

T

I
x
F

P

A

T

T

K

D

D

D

R

R

I

R

E

E

G

G

L

M

T

S

A

A

F
|
F

K

V

E

E

K

K

R

R

T

K

P

A

K

N

Y

F

active site: A68 (= A66), M73 (= M74), S83 (= S84), L87 (≠ Q87), G111 (= G111), E114 (= E114), P133 (≠ T133), E134 (= E134), T139 (≠ I139), P141 (= P141), G142 (= G142), K227 (≠ A227), F237 (≠ I237)
binding acetoacetyl-coenzyme a: K26 (≠ E23), A27 (= A24), L28 (≠ A25), A30 (= A27), A66 (= A64), A68 (= A66), D69 (= D67), I70 (≠ L68), Y107 (≠ S107), G110 (= G110), G111 (= G111), E114 (= E114), P133 (≠ T133), E134 (= E134), L137 (= L137), G142 (= G142), F233 (≠ Y233), F249 (= F249)

1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
38% identity, 95% coverage: 12:257/260 of query aligns to 13:255/258 of 1ey3A

query
sites
1ey3A

T

S

G

S

V

V

A

G

H

L

I

I

T

Q

L

L

D

N

R

R

P

P

E
x
K

A

A

A
x
L

N

N

A
|
A

L

L

S

C

L

N

Q

G

M

L

L

I

Y

E

E

E

L

L

H

N

E

Q

A

A

I

L

Q

E

E

T

V

F

K

E

F

E

N

D

P

P

E

A

V

V

R

G

C

A

V

I

V

V

I

L

K

-

A

T

S

G

G

G

E

E

K

K

V

A

F

F

C

A

A
|
A

G
|
G

A
|
A

D
|
D

L
x
I

K

K

E

E

R

-

A

-

G

-

M
|
M

E

Q

P

N

V

R

Q

T

V

F

K

Q

R

D

T

C

V

Y

S
|
S

-

G

L

K

I

F

Q
x
L

G

S

N

H

I
x
W

N

D

D

H

I

I

E

T

A

R

L

I

P

K

Q

K

P

P

V

V

I

I

C

A

A

A

L

V

N

N

G

G

S

Y

A

A

F

L

G

G

G
|
G

G

G

L

C

E
|
E

L

L

A

A

L

M

A

M

C

C

D

D

I

I

R

I

I

Y

A

A

A

G

D

E

H

K

I

A

K

Q

V

F

G

G

L

Q

T
x
P

E
|
E

T

I

S

L

L
|
L

A

G

I
x
T

I

I

P
|
P

G
|
G

A

A

G

G

T

T

Q

Q

R

R

L

L

P

T

R

R

L

A

I

V

G

G

K

K

G

S

K

L

A

A

K

M

E

E

L

M

I

V

Y

L

T

T

A

G

R

D

R

R

V

I

D

S

A

A

Y

Q

E

D

A

A

E

K

K

Q

I

A

G

G

L

L

V

V

E

S

Y

K

V

I

V

F

S

P

L

V

E

E

N

T

L

L

D

V

E

E

K

E

V

A

N

I

E

Q

I

C

T

A

T

E

L

K

I

I

A

A

K

N

N

N

G

S

P

K

V

I

A

I

L

V

Q

A

Q

M

A

A

K

K

Y

E

A

S

I

V

D

N

K

A

G

A

L

F

E

E

V

M

D

T

L

L

Q

T

T

E

G

G

L

N

A
x
K

I

L

E

E

R

K

K

K

A

L

Y

F

E

Y

V

S

T

T

I
x
F

P

A

T

T

K

D

D

D

R

R

I

R

E

E

G

G

L

M

T

S

A

A

F

F

K

V

E

E

K

K

R

R

T

K

P

A

K

N

Y

F

active site: A66 (= A66), M71 (= M74), S81 (= S84), L85 (≠ Q87), G109 (= G111), E112 (= E114), P131 (≠ T133), E132 (= E134), T137 (≠ I139), P139 (= P141), G140 (= G142), K225 (≠ A227), F235 (≠ I237)
binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E23), L26 (≠ A25), A28 (= A27), A64 (= A64), G65 (= G65), A66 (= A66), D67 (= D67), I68 (≠ L68), L85 (≠ Q87), W88 (≠ I90), G109 (= G111), P131 (≠ T133), L135 (= L137), G140 (= G142)

P14604 Enoyl-CoA hydratase, mitochondrial; mECH; mECH1; Enoyl-CoA hydratase 1; ECHS1; Short-chain enoyl-CoA hydratase; SCEH; EC 4.2.1.17; EC 5.3.3.8 from Rattus norvegicus (Rat) (see 3 papers)
38% identity, 95% coverage: 12:257/260 of query aligns to 45:287/290 of P14604

query
sites
P14604

T

S

G

S

V

V

A

G

H

L

I

I

T

Q

L

L

D

N

R

R

P

P

E

K

A

A

A

L

N

N

A

A

L

L

S

C

L

N

Q

G

M

L

L

I

Y

E

E

E

L

L

H

N

E

Q

A

A

I

L

Q

E

E

T

V

F

K

E

F

E

N

D

P

P

E

A

V

V

R

G

C

A

V

I

V

V

I

L

K

-

A

T

S

G

G

G

E

E

K

K

V

A

F

F

C

A

A

A

G

G

A

A

D

D

L

I

K

K

E

E

R

-

A

-

G

-

M

M

E

Q

P

N

V

R

Q

T

V

F

K

Q

R

D

T

C

V

Y

S

S

-

G

L

K

I

F

Q

L

G

S

N

H

I

W

N

D

D

H

I

I

E

T

A

R

L

I

P

K

Q

K

P

P

V

V

I

I

C

A

A

A

L

V

N

N

G

G

S

Y

A

A

F

L

G

G

L

C

E
|
E

L

L

A

A

L

M

A

M

C

C

D

D

I

I

R

I

I

Y

A

A

A

G

D

E

H

K

I

A

K

Q

V

F

G

G

L

Q

T

P

E
|
E

T

I

S

L

L

L

A

G

I

T

I

I

P

P

G

G

A

A

G

G

T

T

Q

Q

R

R

L

L

P

T

R

R

L

A

I

V

G

G

K

K

G

S

K

L

A

A

K

M

E

E

L

M

I

V

Y

L

T

T

A

G

R

D

R

R

V

I

D

S

A

A

Y

Q

E

D

A

A

E

K

K

Q

I

A

G

G

L

L

V

V

E

S

Y

K

V

I

V

F

S

P

L

V

E

E

N

T

L

L

D

V

E

E

K

E

V

A

N

I

E

Q

I

C

T

A

T

E

L

K

I

I

A

A

K

N

N

N

G

S

P

K

V

I

A

I

L

V

Q

A

Q

M

A

A

K

K

Y

E

A

S

I

V

D

N

K

A

G

A

L

F

E

E

V

M

D

T

L

L

Q

T

T

E

G

G

L

N

A

K

I

L

E

E

R

K

K

K

A

L

Y

F

E

Y

V

S

T

T

I

F

P

A

T

T

K

D

D

D

R

R

I

R

E

E

G

G

L

M

T

S

A

A

F

F

K

V

E

E

K

K

R

R

T

K

P

A

K

N

Y

F

E144 (= E114) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
E164 (= E134) mutation to D: Reduces activity 1250-fold.; mutation to Q: Reduces activity 330000-fold.

Sites not aligning to the query:

1:29 modified: transit peptide, Mitochondrion

2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
38% identity, 94% coverage: 14:257/260 of query aligns to 17:257/260 of 2hw5C

query
sites
2hw5C

V

V

A

G

H

L

I

I

T

Q

L

L

D

N

R

R

P

P

E
x
K

A
|
A

A
x
L

N

N

A
|
A

L

L

S

C

L

D

Q

G

M

L

L

I

Y

D

E

E

L

L

H

N

E

Q

A

A

I

L

Q

K

E

I

V

F

K

E

F

E

N

D

P

P

E

A

V

V

R

G

C

A

V

I

V

V

I

L

K

-

A

T

S

G

G

G

E

D

K
|
K

V

A

F

F

C

A

A

A

G

G

A
|
A

D

D

L
x
I

K

K

E

E

R

-

A

-

G

-

M
|
M

E

Q

P

N

V

L

Q

S

V

F

K

Q

R

D

T

C

V

Y

S
|
S

L

S

-

K

I

F

Q
x
L

G

K

N

H

I

W

N

D

D

H

I

L

E

T

A

Q

L

V

P

K

Q

K

P

P

V

V

I

I

C

A

A

A

L

V

N

N

G

G

S

Y

A

A

F
|
F

G

G

G
|
G

G

G

L

C

E
|
E

L

L

A

A

L

M

A

M

C

C

D

D

I

I

R

I

I

Y

A

A

A

G

D

E

H

K

I

A

K

Q

V

F

G

A

L

Q

T
x
P

E
|
E

T

I

S

L

L

I

A

G

I
x
T

I

I

P
|
P

G
|
G

A

A

G

G

T

T

Q

Q

R

R

L

L

P

T

R

R

L

A

I

V

G

G

K

K

G

S

K

L

A

A

K

M

E

E

L

M

I

V

Y

L

T

T

A

G

R

D

R

R

V

I

D

S

A

A

Y

Q

E

D

A

A

E

K

K

Q

I

A

G

G

L

L

V

V

E

S

Y

K

V

I

V

C

S

P

L

V

E

E

N

T

L

L

D

V

E

E

K

E

V

A

N

I

E

Q

I

C

T

A

T

E

L

K

I

I

A

A

K

S

N

N

G

S

P

K

V

I

A

V

L

V

Q

A

Q

M

A

A

K

K

Y

E

A

S

I

V

D

N

K

A

G

A

L

F

E

E

V

M

D

T

L

L

Q

T

T

E

G

G

L

S

A
x
K

I

L

E

E

R

K

K

K

A

L

Y

F

E

Y

V

S

T

T

I
x
F

P

A

T

T

K

D

D

D

R

R

I

K

E

E

G

G

L

M

T

T

A

A

F

F

K

V

E

E

K

K

R

R

T

K

P

A

K

N

Y

F

active site: A68 (= A66), M73 (= M74), S83 (= S84), L87 (≠ Q87), G111 (= G111), E114 (= E114), P133 (≠ T133), E134 (= E134), T139 (≠ I139), P141 (= P141), G142 (= G142), K227 (≠ A227), F237 (≠ I237)
binding crotonyl coenzyme a: K26 (≠ E23), A27 (= A24), L28 (≠ A25), A30 (= A27), K62 (= K60), I70 (≠ L68), F109 (= F109)

Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
31% identity, 95% coverage: 13:258/260 of query aligns to 33:279/285 of Q7CQ56

query
sites
Q7CQ56

G

G

V

I

A

A

H

K

I

I

T

T

L

I

D

N

R

R

P

P

E

Q

A

V

A

R

N

N

A

A

L

F

S

R

L

P

Q

L

M

T

L

V

Y

K

E

E

L

M

H

I

E

Q

A

A

I

L

Q

A

E

D

V

A

K

R

F

Y

N

D

P

D

E

N

V

V

R

G

C

V

V

I

I

L

K

T

A

G

S

E

G

G

E

D

K

K

V

A

F

F

C

C

A

A

G

G

A

G

D

D

L

Q

K

K

E

V

R

R

A

G

G

D

M

Y

E

G

P

G

V

Y

Q

Q

V

D

K

D

R

S

T

G

V

V

S

H

L

H

I

L

Q

-

G

-

N

N

I

V

N

L

D

D

-

F

-

Q

-

R

-

Q

I

I

E

R

A

T

L

C

P

P

Q

K

P

P

V

V

I

V

C

A

A

M

L

V

N

A

G

G

S

Y

A

S

F

I

G

G

L

H

E

V

L

L

A

H

L

M

A

M

C

C

D

D

I

L

R

T

I

I

A

A

D

E

H

N

I

A

K

I

V

F

G

G

L
x
Q

T
|
T

E
x
G

T

P

S

K

L

V

A

G

I

S

I

F

P

D

G

G

A

G

G

W

G

G

T

A

Q

S

R

Y

L

M

P

A

R

R

L

I

I

V

G

G

K

Q

G

K

K

K

A

A

K

R

E

E

L

I

I

W

Y

F

T

L

A

C

R

R

R

Q

V

Y

D

D

A

A

Y

Q

E

Q

A

A

E

L

K

D

I

M

G

G

L

L

V

V

E

N

Y

T

V

V

S

P

L

L

E

A

N

D

L

L

D

E

E

K

K

E

V

T

N

V

E

R

I

W

T

C

T

R

L

E

I

M

A

L

K

Q

N

N

G

S

P

P

V

M

A

A

L

L

Q

R

Q

C

A

L

K

K

Y

A

A

A

I

L

D

N

K

A

G

-

L

-

E

D

V

C

D

D

L

G

Q

Q

T

A

G

G

L

L

A

Q

-

E

I

L

E

A

R

G

K

N

A

A

Y

T

E

M

V

L

T

F

I

Y

P

M

T

T

K

E

D

E

R

G

I

Q

E

E

G

G

L

R

T

N

A

A

F

F

K

N

E

Q

K

K

R

R

T

Q

P

P

K

D

Y

F

T

S

QTG 154:156 (≠ LTE 132:134) binding hydrogencarbonate

3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
30% identity, 95% coverage: 13:258/260 of query aligns to 29:275/281 of 3t88A

query
sites
3t88A

G

G

V

I

A

A

H

K

I

I

T

T

L

I

D

N

R

R

P

P

E
x
Q

A
x
V

A
x
R

N

N

A
|
A

L

F

S

R

L

P

Q

L

M

T

L

V

Y

K

E

E

L

M

H

I

E

Q

A

A

I

L

Q

A

E

D

V

A

K

R

F

Y

N

D

P

D

E

N

V

I

R

G

C

V

V

I

I

L

K

T

A

G

S

A

G

G

E

D

K

K

V

A

F

F

C

C

A
x
S

G
|
G

A
x
G

D
|
D

L
x
Q

K
|
K

E

V

R
|
R

A

G

G

D

M

Y

E

G

P

G

V
x
Y

Q

K

V

D

K

D

R

S

T

G

V

V

S

H

L
x
H

I

L

Q

-

G

-

N

N

I
x
V

N
x
L

D

D

-

F

-

Q

-

R

-

Q

I

I

E

R

A

T

L

C

P

P

Q

K

P

P

V

V

I

V

C

A

A

M

L

V

N

A

G

G

S
x
Y

A

S

F

I

G

G

G
|
G

G

G

L

H

E
x
V

L

L

A

H

L

M

A

M

C

C

D

D

I

L

R

T

I

I

A

A

D

D

H

N

I

A

K

I

V

F

G

G

L

Q

T
|
T

E
x
G

T

P

S

K

L
x
V

A

G

I
x
S

I
x
F

P
x
D

G
|
G

A

G

G

W

G

G

T

A

Q

S

R

Y

L

M

P

A

R

R

L

I

I

V

G

G

K

Q

G

K

K

K

A

A

K

R

E

E

L

I

I

W

Y

F

T

L

A

C

R

R

R

Q

V

Y

D

D

A

A

Y

K

E

Q

A

A

E

L

K

D

I

M

G

G

L

L

V

V

E

N

Y

T

V

V

S

P

L

L

E

A

N

D

L

L

D

E

E

K

K

E

V

T

N

V

E

R

I

W

T

C

T

R

L

E

I

M

A

L

K

Q

N

N

G

S

P

P

V

M

A

A

L

L

Q

R

Q

C

A

L

K

K

Y

A

A

A

I

L

D

N

K

A

G

-

L

-

E

D

V

C

D

D

L

G

Q

Q

T

A

G

G

L

L

A

Q

-

E

I

L

E
x
A

R

G

K

N

A

A

Y
x
T

E

M

V

L

T

F

I
x
Y

P

M

T

T

K

E

D

E

R

G

I

Q

E

E

G

G

L

R

T

N

A

A

F
|
F

K

N

E

Q

K
|
K

R

R

T

Q

P

P

K

D

Y

F

T

S

active site: G82 (≠ A66), R87 (= R71), Y93 (≠ V77), H101 (≠ L85), L105 (≠ N91), G129 (= G111), V132 (≠ E114), G152 (≠ E134), S157 (≠ I139), D159 (≠ P141), G160 (= G142), A246 (≠ E229), Y254 (≠ I237)
binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ E23), V40 (≠ A24), R41 (≠ A25), A43 (= A27), S80 (≠ A64), G81 (= G65), G82 (≠ A66), D83 (= D67), Q84 (≠ L68), K85 (= K69), Y93 (≠ V77), V104 (≠ I90), L105 (≠ N91), Y125 (≠ S107), G129 (= G111), T151 (= T133), V155 (≠ L137), F158 (≠ I140), D159 (≠ P141), T250 (≠ Y233), Y254 (≠ I237), F266 (= F249), K269 (= K252)

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)
34% identity, 96% coverage: 9:258/260 of query aligns to 83:331/337 of Q8GYN9

query
sites
Q8GYN9

I

L

D

D

E

E

T

-

G

G

V

I

A

A

H

K

I

I

T

T

L

I

D

N

R

R

P

P

E

E

A

R

N

N

A

A

L

F

S

R

L

P

Q

Q

M

T

L

V

Y

K

E

E

L

L

H

M

E

R

A

A

I

F

Q

N

E

D

V

A

K

R

F

D

N

D

P

S

E

S

V

V

R

G

C

V

V

I

I

L

K

T

A

G

S

K

G

G

E

T

K

K

V

A

F

F

C

C

A

S

G

G

A

G

D

D

-

Q

-

A

L

L

K

R

E

T

R

Q

A

D

G

G

M

Y

-

A

E

D

P

P

V

N

Q

D

V

V

K

G

R

R

T

-

V

L

S

N

L

V

I

L

Q

D

G

L

N

Q

I

V

N

Q

D

-

I

I

E

R

A

R

L

L

P

P

Q

K

P

P

V

V

I

I

C

A

A

M

L

V

N

A

G

G

S

Y

A

A

F

V

G

G

L

H

E

I

L

L

A

H

L

M

A

V

C

C

D

D

I

L

R

T

I

I

A

A

D

D

H

N

I

A

K

I

V

F

G

G

L

Q

T

T

E

G

T

P

S

K

L

V

A

G

I

S

I

F

P

D

G

A

A

G

G

Y

G

G

T

S

Q

S

R

I

L

M

P

S

R

R

L

L

I

V

G

G

K

P

G

K

K

K

A

A

K

R

E

E

L

M

I

W

Y

F

T

M

A

T

R

R

R

F

V

Y

D

T

A

A

Y

S

E

E

A

A

E

E

K

K

I

M

G

G

L

L

V

I

E

N

Y

T

V

V

S

P

L

L

E

E

N

D

L

L

D

E

E

K

K

E

V

T

N

V

E

K

I

W

T

C

T

R

L

E

I

I

A

L

K

R

N

N

G

S

P

P

V

T

A

A

-

I

-

R

-

V

L

L

Q

K

Q

A

A

A

K

L

Y

N

A

A

I

V

D

D

K

D

G

G

L

-

E

H

V

A

D

G

L

L

Q

Q

T

-

G

G

L

L

A

G

I

G

E

D

R

-

K

-

A

A

Y

T

E

L

V

L

T

F

I

Y

P

G

T

T

K

E

D

E

R

A

I

T

E

E

G

G

L

R

T

T

A

A

F

Y

K

M

E

H

K

R

R

R

T

P

P

P

K

D

Y

F

T

S

Sites not aligning to the query:

20 H→V: Loss of peroxisomal targeting.

4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
30% identity, 95% coverage: 13:258/260 of query aligns to 33:279/285 of 4i42A

query
sites
4i42A

G

G

V

I

A

A

H

K

I

I

T

T

L

I

D

N

R

R

P

P

E

Q

A
x
V

A
x
R

N

N

A

A

L

F

S

R

L

P

Q

L

M

T

L

V

Y

K

E

E

L

M

H

I

E

Q

A

A

I

L

Q

A

E

D

V

A

K

R

F

Y

N

D

P

D

E

N

V

I

R

G

C

V

V

I

I

L

K

T

A

G

S

A

G

G

E

D

K

K

V

A

F

F

C

C

A
x
S

G
|
G

A
x
G

D
|
D

L
x
Q

K
|
K

E

V

R
|
R

A

G

G

D

M

Y

E

G

P

G

V
x
Y

Q

K

V

D

K

D

R

S

T

G

V

V

S

H

L
x
H

I

L

Q

-

G

-

N

N

I
x
V

N
x
L

D

D

-

F

-

Q

-

R

-

Q

I

I

E

R

A

T

L

C

P

P

Q

K

P

P

V

V

I

V

C

A

A

M

L

V

N

A

G

G

S
x
Y

A

S

F

I

G

G

G
|
G

G

G

L

H

E
x
V

L

L

A

H

L

M

A

M

C

C

D

D

I

L

R

T

I

I

A

A

D

D

H

N

I

A

K

I

V

F

G

G

L

Q

T
|
T

E
x
G

T

P

S

K

L

V

A

G

I
x
S

I

F

P
x
D

G
|
G

A

G

G

W

G

G

T

A

Q

S

R

Y

L

M

P

A

R

R

L

I

I

V

G

G

K

Q

G

K

K

K

A

A

K

R

E

E

L

I

I

W

Y

F

T

L

A

C

R

R

R

Q

V

Y

D

D

A

A

Y

K

E

Q

A

A

E

L

K

D

I

M

G

G

L

L

V

V

E

N

Y

T

V

V

S

P

L

L

E

A

N

D

L

L

D

E

E

K

K

E

V

T

N

V

E

R

I

W

T

C

T

R

L

E

I

M

A

L

K

Q

N

N

G

S

P

P

V

M

A

A

L

L

Q

R

Q

C

A

L

K

K

Y

A

A

A

I

L

D

N

K

A

G

-

L

-

E

D

V

C

D

D

L

G

Q

Q

T

A

G

G

L

L

A

Q

-

E

I

L

E
x
A

R

G

K

N

A

A

Y
x
T

E

M

V

L

T

F

I
x
Y

P

M

T

T

K

E

D

E

R

G

I

Q

E

E

G

G

L

R

T

N

A

A

F
|
F

K

N

E

Q

K
|
K

R

R

T

Q

P

P

K

D

Y

F

T

S

active site: G86 (≠ A66), R91 (= R71), Y97 (≠ V77), H105 (≠ L85), L109 (≠ N91), G133 (= G111), V136 (≠ E114), G156 (≠ E134), S161 (≠ I139), D163 (≠ P141), G164 (= G142), A250 (≠ E229), Y258 (≠ I237)
binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ A24), R45 (≠ A25), S84 (≠ A64), G85 (= G65), G86 (≠ A66), D87 (= D67), Q88 (≠ L68), K89 (= K69), Y97 (≠ V77), V108 (≠ I90), Y129 (≠ S107), G133 (= G111), T155 (= T133), S161 (≠ I139), T254 (≠ Y233), F270 (= F249), K273 (= K252)

P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
30% identity, 95% coverage: 13:258/260 of query aligns to 33:279/285 of P0ABU0

query
sites
P0ABU0

G

G

V

I

A

A

H

K

I

I

T

T

L

I

D

N

R

R

P

P

E

Q

A

V

A
x
R

N

N

A

A

L

F

S

R

L

P

Q

L

M

T

L

V

Y

K

E

E

L

M

H

I

E

Q

A

A

I

L

Q

A

E

D

V

A

K

R

F

Y

N

D

P

D

E

N

V

I

R

G

C

V

V

I

I

L

K

T

A

G

S

A

G

G

E

D

K

K

V

A

F

F

C

C

A
x
S

G
|
G

A
x
G

D
|
D

L
x
Q

K
|
K

E

V

R
|
R

A

G

G

D

M

Y

E

G

P

G

V
x
Y

Q

K

V

D

K

D

R

S

T

G

V

V

S

H

L

H

I

L

Q

-

G

-

N

N

I

V

N

L

D

D

-

F

-

Q

-

R

-

Q

I

I

E

R

A

T

L

C

P

P

Q

K

P

P

V

V

I

V

C

A

A

M

L

V

N

A

G

G

S
x
Y

A
x
S

F
x
I

G
|
G

G

G

L

H

E

V

L

L

A

H

L

M

A

M

C

C

D

D

I

L

R

T

I

I

A

A

D

D

H

N

I

A

K

I

V

F

G

G

L
x
Q

T
|
T

E
x
G

T

P

S

K

L

V

A

G

I
x
S

I

F

P

D

G

G

A

G

G

W

G

G

T

A

Q

S

R

Y

L

M

P

A

R

R

L

I

I

V

G

G

K

Q

G

K

K

K

A

A

K

R

E

E

L

I

I
x
W

Y

F

T

L

A

C

R

R

R

Q

V

Y

D

D

A

A

Y

K

E

Q

A

A

E

L

K

D

I

M

G

G

L

L

V

V

E

N

Y

T

V

V

S

P

L

L

E

A

N

D

L

L

D

E

E

K

K

E

V

T

N

V

E

R

I

W

T

C

T

R

L

E

I

M

A

L

K

Q

N

N

G

S

P

P

V

M

A

A

L

L

Q

R

Q

C

A

L

K

K

Y

A

A

A

I

L

D

N

K

A

G

-

L

-

E

D

V

C

D

D

L

G

Q

Q

T

A

G

G

L

L

A

Q

-

E

I

L

E

A

R

G

K

N

A

A

Y

T

E

M

V

L

T

F

I
x
Y

P

M

T

T

K

E

D

E

R

G

I

Q

E

E

G

G

L
x
R

T

N

A

A

F
|
F

K

N

E

Q

K
|
K

R

R

T

Q

P

P

K

D

Y

F

T

S

R45 (≠ A25) binding in other chain
SGGDQK 84:89 (≠ AGADLK 64:69) binding in other chain
K89 (= K69) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
R91 (= R71) mutation to A: Loss of DHNA-CoA synthase activity.
Y97 (≠ V77) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
YSIGG 129:133 (≠ SAFGG 107:111) binding in other chain
Q154 (≠ L132) mutation to A: Reduces the specific DHNA-CoA synthase activity by 15-fold, whereas its affinity for hydrogencarbonate is reduced by 36-fold.
QTG 154:156 (≠ LTE 132:134) binding hydrogencarbonate
T155 (= T133) binding in other chain
G156 (≠ E134) mutation to D: Loss of DHNA-CoA synthase activity.
S161 (≠ I139) binding in other chain
W184 (≠ I162) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
Y258 (≠ I237) binding substrate
R267 (≠ L246) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
F270 (= F249) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
K273 (= K252) binding substrate; mutation to A: Impairs protein folding.

4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
29% identity, 95% coverage: 13:258/260 of query aligns to 30:262/268 of 4elxA

query
sites
4elxA

G

G

V

I

A

A

H

K

I

I

T

T

L

I

D

N

R

R

P

P

E

Q

A

V

A

R

N

N

A

A

L

F

S

R

L

P

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L

M

T

L

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Y

K

E

E

L

M

H

I

E

Q

A

A

I

L

Q

A

E

D

V

A

K

R

F

Y

N

D

P

D

E

N

V

I

R

G

C

V

V

I

I

L

K

T

A

G

S

A

G

G

E

D

K

K

V

A

F

F

C

C

A

S

G

G

A
x
G

D

D

L

Q

K

K

E

H

R
x
H

A

L

G

N

M

V

E
x
L

P

D

V

F

Q

Q

V

R

K

Q

R

-

T

-

V

-

S

-

L

-

I

-

Q

-

G

-

N

-

I

-

N

-

D

-

I

I

E

R

A

T

L

C

P

P

Q

K

P

P

V

V

I

V

C

A

A

M

L

V

N

A

G

G

S

Y

A

S

F

I

G
|
G

G

G

L

H

E
x
V

L

L

A

H

L

M

A

M

C

C

D

D

I

L

R

T

I

I

A

A

D

D

H

N

I

A

K

I

V

F

G

G

L

Q

T

T

E
x
G

T

P

S

K

L

V

A

G

I
x
S

I

F

P
x
D

G
|
G

A

G

G

W

G

G

T

A

Q

S

R

Y

L

M

P

A

R

R

L

I

I

V

G

G

K

Q

G

K

K

K

A

A

K

R

E

E

L

I

I
x
W

Y

F

T

L

A

C

R

R

R

Q

V

Y

D

D

A

A

Y

K

E

Q

A

A

E

L

K

D

I

M

G

G

L

L

V

V

E

N

Y

T

V

V

S

P

L

L

E

A

N

D

L

L

D

E

E

K

K

E

V

T

N

V

E

R

I

W

T

C

T

R

L

E

I

M

A

L

K

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N

N

G

S

P

P

V

M

A

A

L

L

Q

R

Q

C

A

L

K

K

Y

A

A

A

I

L

D

N

K

A

G

-

L

-

E

D

V

C

D

D

L

G

Q

Q

T

A

G

G

L

L

A

Q

-

E

I

L

E
x
A

R

G

K

N

A

A

Y

T

E

M

V

L

T

F

I
x
Y

P

M

T

T

K

E

D

E

R

G

I

Q

E

E

G

G

L

R

T

N

A

A

F

F

K

N

E

Q

K

K

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R

T

Q

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P

K

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Y

F

T

S

active site: G83 (≠ A66), H88 (≠ R71), L92 (≠ E75), G116 (= G111), V119 (≠ E114), G139 (≠ E134), S144 (≠ I139), D146 (≠ P141), G147 (= G142), A233 (≠ E229), Y241 (≠ I237)
binding chloride ion: G115 (= G110), G139 (≠ E134), W167 (≠ I162)

Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
33% identity, 94% coverage: 13:257/260 of query aligns to 22:266/273 of Q5HH38

query
sites
Q5HH38

G

G

V

I

A

A

H

K

I

V

T

T

L

I

D

N

R

R

P

P

E

E

A

V

A
x
R

N

N

A

A

L

F

S

T

L

P

Q

K

M

T

L

V

Y

A

E

E

L

M

H

I

E

D

A

A

I

F

Q

S

E

R

V

A

K

R

F

D

N

D

P

Q

E

N

V

V

R

S

C

V

V

I

V

V

I

L

K

T

A

G

S

E

G

G

E

D

K

L

V

A

F

F

C

C

A
x
S

G
|
G

A
x
G

D
|
D

L
x
Q

K

K

E

K

R

R

A

G

G

H

M

G

E

G

P

Y

V

V

Q

G

V

E

K

D

R

Q

T

I

V

P

S

R

L

L

I

-

Q

-

G

-

N

N

I

V

N

L

D

D

I

L

E

Q

A

R

L

L

-

I

-

R

-

I

P

P

Q

K

P

P

V

V

I

I

C

A

A

M

L

V

N

K

G

G

S

Y

A

A

F

V

G

G

L

N

E

V

L

L

A

N

L

V

A

V

C

C

D

D

I

L

R

T

I

I

A

A

D

D

H

N

I

A

K

I

V

F

G

G

L

Q

T

T

E

G

T

P

S

K

L

V

A

G

I
x
S

I

F

P

D

G

A

A

G

G

Y

G

G

T

S

Q

G

R

Y

L

L

P

A

R

R

L

I

I

V

G

G

K

H

G

K

K

K

A

A

K

R

E

E

L

I

I

W

Y

Y

T

L

A

C

R

R

R

Q

V

Y

D

N

A

A

Y

Q

E

E

A

A

E

L

K

D

I

M

G

G

L

L

V

V

E

N

Y

T

V

V

S

P

L

L

E

E

N

K

L

V

D

E

E

D

K

E

V

T

N

V

E

Q

I

W

T

C

T

K

L

E

I

I

A

M

K

K

N

H

G

S

P

P

V

T

A

A

L

L

Q

R

Q

F

A

L

K

K

Y

A

A

A

I

M

D

N

K

A

G

D

L

T

E

D

V

-

D

-

L

-

Q

-

T

-

G

G

L

L

A

A

-

G

I

L

E

Q

R

Q

K

M

A

A

Y

G

E

D

V

A

T

T

I

L

-

L

-

Y

P

T

T

T

K

D

D

E

R

A

I

K

E

E

G

G

L

R

T

D

A

A

F

F

K

K

E

E

K

K

R

R

T

D

P

P

K

D

Y

F

R34 (≠ A25) binding in other chain
SGGDQ 73:77 (≠ AGADL 64:68) binding in other chain
S149 (≠ I139) binding in other chain

Query Sequence

>WP_078429031.1 NCBI__GCF_002019605.1:WP_078429031.1
MEKKVVLVIDETGVAHITLDRPEAANALSLQMLYELHEAIQEVKFNPEVRCVVIKASGEK
VFCAGADLKERAGMEPVQVKRTVSLIQGNINDIEALPQPVICALNGSAFGGGLELALACD
IRIAADHIKVGLTETSLAIIPGAGGTQRLPRLIGKGKAKELIYTARRVDAYEAEKIGLVE
YVVSLENLDEKVNEITTLIAKNGPVALQQAKYAIDKGLEVDLQTGLAIERKAYEVTIPTK
DRIEGLTAFKEKRTPKYTGE

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