SitesBLAST

Q9LKJ1 3-hydroxyisobutyryl-CoA hydrolase 1; CoA-thioester hydrolase CHY1; EC 3.1.2.-; EC 3.1.2.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
42% identity, 97% coverage: 1:341/353 of query aligns to 5:353/378 of Q9LKJ1

query
sites
Q9LKJ1

M

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S

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D

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G

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F

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G

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G

D

D

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-

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Y

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-

A

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E

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D

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G70 (= G67) mutation to S: Loss of activity.
E142 (= E144) mutation to A: Loss of activity.
D150 (= D152) mutation to G: Reduced activity.

4hdtA Crystal structure of a carnitinyl-coa dehydratase from mycobacterium thermoresistibile (see paper)
43% identity, 99% coverage: 4:352/353 of query aligns to 1:338/340 of 4hdtA

query
sites
4hdtA

D

N

A

E

E

D

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G

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A

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x
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active site: G64 (= G67), I69 (≠ L72), W84 (≠ F93), Y88 (= Y97), G112 (= G121), G115 (= G124), E135 (= E144), P142 (= P151), D143 (= D152), R283 (≠ V292)
binding zinc ion: H28 (≠ L31), E42 (≠ D45), E57 (= E60), E79 (≠ P88), H93 (≠ L102), H185 (≠ S194)

Sites not aligning to the query:

binding zinc ion: 340

5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
33% identity, 54% coverage: 10:198/353 of query aligns to 9:188/259 of 5zaiC

query
sites
5zaiC

E

K

R

K

R

E

G

G

A

N

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F

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T

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N

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x
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L

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G

G

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G

E

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G
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G

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active site: A65 (≠ G67), F70 (≠ L72), S82 (≠ A79), R86 (= R83), G110 (= G121), E113 (≠ G124), P132 (= P143), E133 (= E144), I138 (≠ L149), P140 (= P151), G141 (≠ D152)
binding coenzyme a: K24 (≠ A25), L25 (= L26), A63 (= A65), G64 (= G66), A65 (≠ G67), D66 (= D68), I67 (≠ V69), P132 (= P143), R166 (= R176)

Sites not aligning to the query:

active site: 226, 236
binding coenzyme a: 248, 251

2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
36% identity, 53% coverage: 7:193/353 of query aligns to 5:178/254 of 2dubA

query
sites
2dubA

I

I

L

I

F

T

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G

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A

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active site: A67 (≠ G67), M72 (≠ G82), S82 (≠ V98), G105 (= G121), E108 (≠ G124), P127 (= P143), E128 (= E144), T133 (≠ L149), P135 (= P151), G136 (≠ D152)
binding octanoyl-coenzyme a: K25 (= K24), A26 (= A25), L27 (= L26), A29 (= A28), A65 (= A65), A67 (≠ G67), D68 (= D68), I69 (≠ V69), K70 (= K80), G105 (= G121), E108 (≠ G124), P127 (= P143), E128 (= E144), G136 (≠ D152), A137 (≠ V153)

Sites not aligning to the query:

active site: 221, 231

1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
35% identity, 53% coverage: 7:193/353 of query aligns to 6:184/260 of 1dubA

query
sites
1dubA

I

I

L

I

F

T

E

E

R

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G

G

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G

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L

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I

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L

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N

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K

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A

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L

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A

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Y

F

V
x
L

L

S

N

H

-

W

R

D

L

H

I

I

K

T

R

R

L

I

S

K

K

K

P

P

Y

V

V

I

A

A

V

A

I

V

D

N

G

G

I
x
Y

S

A

M

L

G
|
G

G

G

V

C

G
x
E

L

L

S

A

V

M

H

M

G

C

S

D

H

I

R

I

I

Y

V

A

T

G

E

E

R

K

T

A

L

Q

F

F

A

G

M

Q

P
|
P

E
|
E

T

I

G

L

I
x
L

G

G

L
x
T

Y

I

P
|
P

D
x
G

V

A

G

G

T

T

Y

Q

F

R

L

L

P

T

R

R

L

A

P

V

G

G

Q

K

-

S

V

L

G

A

V

M

W

E

L

M

G

V

L

L

T

T

G

G

D

D

R

R

L

I

K

S

A

A

A

Q

D

D

L

A

L

K

A

Q

I

A

G

G

A

L

A

V

D

S

A

K

F

I

V

F

P

P

active site: A68 (≠ G67), M73 (≠ G82), S83 (= S94), L87 (≠ V98), G111 (= G121), E114 (≠ G124), P133 (= P143), E134 (= E144), T139 (≠ L149), P141 (= P151), G142 (≠ D152)
binding acetoacetyl-coenzyme a: K26 (= K24), A27 (= A25), L28 (= L26), A30 (= A28), A66 (= A65), A68 (≠ G67), D69 (= D68), I70 (≠ V69), Y107 (≠ I117), G110 (= G120), G111 (= G121), E114 (≠ G124), P133 (= P143), E134 (= E144), L137 (≠ I147), G142 (≠ D152)

Sites not aligning to the query:

active site: 227, 237
binding acetoacetyl-coenzyme a: 233, 249

1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
35% identity, 53% coverage: 7:193/353 of query aligns to 4:182/258 of 1ey3A

query
sites
1ey3A

I

I

L

I

F

T

E

E

R

K

G

G

-

K

-

N

-

S

A

S

I

V

G

G

L

L

V

I

T

Q

L

L

N

N

R

R

P

P

K
|
K

A

A

L
|
L

N

N

A
|
A

L

L

T

C

L

N

G

G

M

L

I

I

R

E

L

E

F

L

D

N

P

Q

Q

A

L

L

R

E

A

T

W

F

D

E

A

E

D

D

P

P

E

A

V

V

K

G

A

A

V

I

V

V

I

L

R

T

G

G

A

-

G

G

E

E

K

K

A

A

F

F

C

A

A
|
A

G
|
G

G
x
A

D
|
D

V
x
I

V

-

S

-

L

-

Y

-

E

-

A

-

G

-

K

-

A

-

K

K

E

E

G
x
M

R

Q

G

N

D

R

T

T

S

-

P

-

I

F

R

Q

A

D

F

C

F

Y

S
|
S

E

G

E

K

Y

F

V
x
L

L

S

N

H

-
x
W

R

D

L

H

I

I

K

T

R

R

L

I

S

K

K

K

P

P

Y

V

V

I

A

A

V

A

I

V

D

N

G

G

I

Y

S

A

M

L

G

G

G
|
G

G

G

V

C

G
x
E

L

L

S

A

V

M

H

M

G

C

S

D

H

I

R

I

I

Y

V

A

T

G

E

E

R

K

T

A

L

Q

F

F

A

G

M

Q

P
|
P

E
|
E

T

I

G

L

I
x
L

G

G

L
x
T

Y

I

P
|
P

D
x
G

V

A

G

G

T

T

Y

Q

F

R

L

L

P

T

R

R

L

A

P

V

G

G

Q

K

-

S

V

L

G

A

V

M

W

E

L

M

G

V

L

L

T

T

G

G

D

D

R

R

L

I

K

S

A

A

A

Q

D

D

L

A

L

K

A

Q

I

A

G

G

A

L

A

V

D

S

A

K

F

I

V

F

P

P

active site: A66 (≠ G67), M71 (≠ G82), S81 (= S94), L85 (≠ V98), G109 (= G121), E112 (≠ G124), P131 (= P143), E132 (= E144), T137 (≠ L149), P139 (= P151), G140 (≠ D152)
binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K24), L26 (= L26), A28 (= A28), A64 (= A65), G65 (= G66), A66 (≠ G67), D67 (= D68), I68 (≠ V69), L85 (≠ V98), W88 (vs. gap), G109 (= G121), P131 (= P143), L135 (≠ I147), G140 (≠ D152)

Sites not aligning to the query:

active site: 225, 235

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)
35% identity, 53% coverage: 7:193/353 of query aligns to 36:214/290 of P14604

query
sites
P14604

I

I

L

I

F

T

E

E

R

K

G

G

-

K

-

N

-

S

A

S

I

V

G

G

L

L

V

I

T

Q

L

L

N

N

R

R

P

P

K

K

A

A

L

L

N

N

A

A

L

L

T

C

L

N

G

G

M

L

I

I

R

E

L

E

F

L

D

N

P

Q

Q

A

L

L

R

E

A

T

W

F

D

E

A

E

D

D

P

P

E

A

V

V

K

G

A

A

V

I

V

V

I

L

R

T

G

G

A

-

G

G

E

E

K

K

A

A

F

F

C

A

A

A

G

G

G

A

D

D

V

I

V

-

S

-

L

-

Y

-

E

-

A

-

G

-

K

-

A

-

K

K

E

E

G

M

R

Q

G

N

D

R

T

T

S

-

P

-

I

F

R

Q

A

D

F

C

F

Y

S

S

E

G

E

K

Y

F

V

L

L

S

N

H

-

W

R

D

L

H

I

I

K

T

R

R

L

I

S

K

K

K

P

P

Y

V

V

I

A

A

V

A

I

V

D

N

G

G

I

Y

S

A

M

L

G

G

V

C

G
x
E

L

L

S

A

V

M

H

M

G

C

S

D

H

I

R

I

I

Y

V

A

T

G

E

E

R

K

T

A

L

Q

F

F

A

G

M

Q

P

P

E
|
E

T

I

G

L

I

L

G

G

L

T

Y

I

P

P

D

G

V

A

G

G

T

T

Y

Q

F

R

L

L

P

T

R

R

L

A

P

V

G

G

Q

K

-

S

V

L

G

A

V

M

W

E

L

M

G

V

L

L

T

T

G

G

D

D

R

R

L

I

K

S

A

A

A

Q

D

D

L

A

L

K

A

Q

I

A

G

G

A

L

A

V

D

S

A

K

F

I

V

F

P

P

E144 (≠ G124) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
E164 (= E144) 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

1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
36% identity, 53% coverage: 7:193/353 of query aligns to 6:182/258 of 1mj3A

query
sites
1mj3A

I

I

L

I

F

T

E

E

R

K

G

G

-

K

-

N

-

S

A

S

I

V

G

G

L

L

V

I

T

Q

L

L

N

N

R

R

P

P

K
|
K

A
|
A

L
|
L

N

N

A
|
A

L

L

T

C

L

N

G

G

M

L

I

I

R

E

L

E

F

L

D

N

P

Q

Q

A

L

L

R

E

A

T

W

F

D

E

A

E

D

D

P

P

E

A

V

V

K

G

A

A

V

I

V

V

I

L

R

T

G

G

A

-

G

G

E

E

K

K

A

A

F

F

C

A

A
|
A

G
|
G

G
x
A

D
|
D

V
x
I

V

-

S

-

L

-

Y

-

E

-

A

-

G

-

K

-

A

-

K

K

E

E

G
x
M

R

Q

G

N

D

R

T

T

S

-

P

-

I

-

R

-

A

-

F

-

F

F

S

Q

E

D

E

C

Y

Y

V
x
S

-

G

L
|
L

N

S

R

H

-

W

-

D

L

H

I

I

K

T

R

R

L

I

S

K

K

K

P

P

Y

V

V

I

A

A

V

A

I

V

D

N

G

G

I

Y

S

A

M

L

G

G

G
|
G

G

G

V

C

G
x
E

L

L

S

A

V

M

H

M

G

C

S

D

H

I

R

I

I

Y

V

A

T

G

E

E

R

K

T

A

L

Q

F

F

A

G

M

Q

P
|
P

E
|
E

T

I

G

L

I
x
L

G

G

L
x
T

Y

I

P
|
P

D
x
G

V

A

G

G

T

T

Y

Q

F

R

L

L

P

T

R

R

L

A

P

V

G

G

Q

K

-

S

V

L

G

A

V

M

W

E

L

M

G

V

L

L

T

T

G

G

D

D

R

R

L

I

K

S

A

A

A

Q

D

D

L

A

L

K

A

Q

I

A

G

G

A

L

A

V

D

S

A

K

F

I

V

F

P

P

active site: A68 (≠ G67), M73 (≠ G82), S83 (≠ V98), L85 (= L99), G109 (= G121), E112 (≠ G124), P131 (= P143), E132 (= E144), T137 (≠ L149), P139 (= P151), G140 (≠ D152)
binding hexanoyl-coenzyme a: K26 (= K24), A27 (= A25), L28 (= L26), A30 (= A28), A66 (= A65), G67 (= G66), A68 (≠ G67), D69 (= D68), I70 (≠ V69), G109 (= G121), P131 (= P143), E132 (= E144), L135 (≠ I147), G140 (≠ D152)

Sites not aligning to the query:

active site: 225, 235

2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
33% identity, 53% coverage: 7:193/353 of query aligns to 6:184/260 of 2hw5C

query
sites
2hw5C

I

I

L

I

F

A

E

E

R

K

R

R

G

G

-

K

-

N

A

T

I

V

G

G

L

L

V

I

T

Q

L

L

N

N

R

R

P

P

K
|
K

A
|
A

L
|
L

N

N

A
|
A

L

L

T

C

L

D

G

G

M

L

I

I

R

D

L

E

F

L

D

N

P

Q

Q

A

L

L

R

K

A

I

W

F

D

E

A

E

D

D

P

P

E

A

V

V

K

G

A

A

V

I

V

V

I

L

R

T

G

G

A

-

G

G

E

D

K
|
K

A

A

F

F

C

A

A

A

G

G

G
x
A

D

D

V
x
I

V

K

S

E

L
x
M

Y

-

E

-

A

-

G

-

K

-

A

-

K

-

E

-

G

-

R

-

G

-

D

Q

T

N

S

L

P

S

I

F

R

Q

A

D

F

C

F

Y

S
|
S

E

S

E

K

Y

F

V
x
L

L

K

N

H

-

W

R

D

L

H

I

L

K

T

R

Q

L

V

S

K

K

K

P

P

Y

V

V

I

A

A

V

A

I

V

D

N

G

G

I

Y

S

A

M
x
F

G

G

G
|
G

G

G

V

C

G
x
E

L

L

S

A

V

M

H

M

G

C

S

D

H

I

R

I

I

Y

V

A

T

G

E

E

R

K

T

A

L

Q

F

F

A

A

M

Q

P
|
P

E
|
E

T

I

G

L

I

I

G

G

L
x
T

Y

I

P
|
P

D
x
G

V

A

G

G

T

T

Y

Q

F

R

L

L

P

T

R

R

L

A

P

V

G

G

Q

K

-

S

V

L

G

A

V

M

W

E

L

M

G

V

L

L

T

T

G

G

D

D

R

R

L

I

K

S

A

A

A

Q

D

D

L

A

L

K

A

Q

I

A

G

G

A

L

A

V

D

S

A

K

F

I

V

C

P

P

active site: A68 (≠ G67), M73 (≠ L72), S83 (= S94), L87 (≠ V98), G111 (= G121), E114 (≠ G124), P133 (= P143), E134 (= E144), T139 (≠ L149), P141 (= P151), G142 (≠ D152)
binding crotonyl coenzyme a: K26 (= K24), A27 (= A25), L28 (= L26), A30 (= A28), K62 (= K61), I70 (≠ V69), F109 (≠ M119)

Sites not aligning to the query:

active site: 227, 237

6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 54% coverage: 7:197/353 of query aligns to 5:185/257 of 6slbAAA

query
sites
6slbAAA

I

I

L

L

F

K

E

E

R

R

R

Q

G

D

A

G

I

V

G

L

L

V

V

L

T

T

L

L

N

N

R

R

P

P

K

E

A

K

L

L

N

N

A

A

L

I

T

T

L

G

G

E

M

L

I

L

R

D

L

A

F

L

D

Y

P

A

Q

A

L

L

R

K

A

E

W

G

D

E

A

E

D

D

P

R

E

E

V

V

K

R

A

A

V

L

I

L

R

T

G

G

A

A

G

G

E

-

K
x
R

A

A

F

F

C

S

A
|
A

G

G

G
x
Q

D
|
D

V
x
L

V

T

S

E

L
x
F

Y

-

E

-

A

-

G

-

K

-

A

-

K

-

E

-

G

-

R

-

G

G

D

D

T

R

S

K

P

P

I

D

R
x
Y

A

E

F

A

F

H

S
x
L

E

R

Y

Y

V

-

L

-

N
|
N

R

R

L

V

I

V

K

E

R

A

L

L

S

S

-

G

-

L

-

E

K

K

P

P

Y

L

V

V

A

V

V

A

I

V

D

N

G

G

I

V

S

A

M

A

G

G

G
x
A

G

G

V

M

G
x
S

L

L

S

A

V

L

H

W

G

G

S

D

H

L

R

R

I

L

V

A

T

A

E

V

R

G

T

A

L

S

F

F

A

T

M

T

P
x
A

E
x
F

T

V

G

R

I

I

G

G

L
|
L

Y

V

P
|
P

D
|
D

V

S

G

G

G

L

T

S

Y

F

F

L

L

L

P

P

R

R

L

L

P

V

G

G

Q

L

V

A

G

K

V

A

W

Q

-

E

L

L

G

L

L

L

T

L

G

S

D

P

R

R

L

L

K

S

A

A

A

E

D

E

L

A

L

L

A

A

I

L

G

G

A

L

A

V

D

H

A

R

F

V

V

V

P

P

S

A

G

E

E

K

I

L

active site: Q64 (≠ G67), F69 (≠ L72), L80 (≠ S94), N84 (= N100), A108 (≠ G121), S111 (≠ G124), A130 (≠ P143), F131 (≠ E144), L136 (= L149), P138 (= P151), D139 (= D152)
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: R58 (≠ K61), A62 (= A65), Q64 (≠ G67), D65 (= D68), L66 (≠ V69), Y76 (≠ R90), A108 (≠ G121), F131 (≠ E144), D139 (= D152)

Sites not aligning to the query:

active site: 224, 234

O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
33% identity, 54% coverage: 8:196/353 of query aligns to 11:193/266 of O53561

query
sites
O53561

L

L

F

V

E

E

R

R

G

G

A

H

I

T

G

L

L

I

V

V

T

T

L

M

N

N

R

R

P

P

K

A

A

A

L

R

N

N

A

A

L

L

T

S

L

T

G

E

M

M

I

M

R

R

L

I

F

M

D

-

P

-

Q

-

L

V

R

Q

A

A

W

W

-

D

-

R

-

V

D

D

A

N

D

D

P

P

E

D

V

I

K

R

A

C

V

C

V

I

I

L

R

T

G

G

A

A

G

G

E

-

K

G

A

Y

F

F

C

C

A

A

G

G

G

M

D

D

V

L

V

K

S

A

L

A

Y

T

E

Q

A

K

-

P

G

G

K

D

A

S

A

F

K

K

E

D

G

G

R

S

G

Y

D

G

T

P

S

S

P

R

I

I

R

D

A

A

F

L

S

K

E

G

E

-

Y

-

V

-

L

-

N

-

R

-

L

-

I

-

K

R

R

R

L

L

S

T

K

K

P

P

Y

L

V

I

A

A

V

A

I

V

D

E

G

G

I

P

S

A

M

I

G

A

G

G

V

T

G

E

L

I

S

L

V

Q

H

G

G

T

S

D

H

I

R

R

I

V

V

A

T

G

E

E

R

S

T

A

L
x
K

F
|
F

A
x
G

M
x
I

P
x
S

E
|
E

T
x
A

G
x
K

I

W

G

S

L

L

Y

Y

P

P

D

M

V

G

G

G

G

S

T

A

Y

V

F

R

L

L

P

V

R

R

-

Q

L

I

P

P

G

Y

Q

T

V

L

G

A

V

C

W

D

L

L

G

L

L

L

T

T

G

G

D

R

R

H

L

I

K

T

A

A

D

E

L

A

L

K

A

E

I

M

G

G

A

L

A

I

D

G

A

H

F

V

V

V

P

P

S

D

G

G

E

Q

K135 (≠ L139) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
135:142 (vs. 139:146, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
K142 (≠ G146) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.

6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
31% identity, 54% coverage: 7:197/353 of query aligns to 2:173/245 of 6slaAAA

query
sites
6slaAAA

I

I

L

L

F

K

E

E

R

R

R

Q

G

D

A

G

I

V

G

L

L

V

V

L

T

T

L

L

N

N

R

R

P

P

K

E

A

K

L
|
L

N

N

A

A

L

I

T

T

L

G

G

E

M

L

I

L

R

D

L

A

F

L

D

Y

P

A

Q

A

L

L

R

K

A

E

W

G

D

E

A

E

D

D

P

R

E

E

V

V

K

R

A

A

V

L

I

L

R

T

G

G

A

A

G

G

E

-

K

R

A

A

F

F

C

S

A
|
A

G

G

G
x
Q

D
|
D

V
x
L

V

T

S

E

L

A

Y

H

E

-

A

-

G

-

K

-

A

-

K

-

E

-

G

-

R

-

G

-

D

-

T

-

S

-

P

-

I
x
L

R

R

A

R

F
x
Y

F

-

S

-

E

-

Y

-

V

-

L

-

N
|
N

R

R

L

V

I

V

K

E

R

A

L

L

S

S

-

G

-

L

-

E

K

K

P

P

Y

L

V

V

A

V

V

A

I

V

D

N

G

G

I

V

S

A

M
x
A

G
|
G

G
x
A

G

G

V

M

G
x
S

L

L

S

A

V

L

H

W

G

G

S

D

H

L

R

R

I

L

V

A

T

A

E

V

R

G

T

A

L

S

F

F

A

T

M

T

P
x
A

E
x
F

T

V

G

R

I
|
I

G

G

L
|
L

Y

V

P
|
P

D
x
N

V

S

G

G

G

L

T

S

Y

F

F

L

L

L

P

P

R

R

L

L

P

V

G

G

Q

L

V

A

G

K

V

A

W

Q

-

E

L

L

G

L

L

L

T

L

G

S

D

P

R

R

L

L

K

S

A

A

A

E

D

E

L

A

L

L

A

A

I

L

G

G

A

L

A

V

D

H

A

R

F

V

V

V

P

P

S

A

G

E

E

K

I

L

active site: Q61 (≠ G67), L68 (≠ I89), N72 (= N100), A96 (≠ G121), S99 (≠ G124), A118 (≠ P143), F119 (≠ E144), L124 (= L149), P126 (= P151), N127 (≠ D152)
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: L21 (= L26), A59 (= A65), Q61 (≠ G67), D62 (= D68), L63 (≠ V69), L68 (≠ I89), Y71 (≠ F92), A94 (≠ M119), G95 (= G120), A96 (≠ G121), F119 (≠ E144), I122 (= I147), L124 (= L149), N127 (≠ D152)

Sites not aligning to the query:

3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
30% identity, 54% coverage: 7:197/353 of query aligns to 5:184/256 of 3h81A

query
sites
3h81A

I

I

L

L

F

V

E

E

R

R

R

D

G

Q

A

R

I

V

G

G

L

I

V

I

T

T

L

L

N

N

R

R

P

P

K

Q

A

A

L

L

N

N

A

A

L

L

T

N

L

S

G

Q

M

V

I

M

R

N

L

E

F

V

D

T

P

S

Q

A

L

A

R

T

A

E

W

L

D

D

A

D

D

D

P

P

E

D

V

I

K

G

A

A

V

I

I

I

R

T

G

G

A

S

G

A

E

-

K

K

A

A

F

F

C

A

A

A

G

G

G
x
A

D

D

V

I

V

K

S

E

L
x
M

Y

-

E

-

A

-

G

-

K

-

A

-

K

-

E

-

G

-

R

-

G

A

D

D

T

L

S

T

P

F

I

A

R

D

A

A

F

F

F
x
T

S

A

E

D

E

F

Y
x
F

V

A

L

T

N

W

R

G

L

K

I

L

K

A

R

A

L

V

S

R

K

T

P

P

Y

T

V

I

A

A

V

A

I

V

D

A

G

G

I

Y

S

A

M

L

G

G

G
|
G

G

G

V

C

G
x
E

L

L

S

A

V

M

H

M

G

C

S

D

H

V

R

L

I

I

V

A

T

A

E

D

R

T

T

A

L

K

F

F

A

G

M

Q

P
|
P

E
|
E

T

I

G

K

I

L

G

G

L
x
V

Y

L

P
|
P

D
x
G

V

M

G

G

T

S

Y

Q

F

R

L

L

P

T

R

R

L

A

P

I

G

G

Q

K

V

A

G

K

V

A

W

M

-

D

L

L

G

I

L

L

T

T

G

G

D

R

R

T

L

M

K

D

A

A

D

E

L

A

L

E

A

R

I

S

G

G

A

L

A

V

D

S

A

R

F

V

V

V

P

P

S

A

G

D

E

D

I

L

active site: A64 (≠ G67), M69 (≠ L72), T79 (≠ F93), F83 (≠ Y97), G107 (= G121), E110 (≠ G124), P129 (= P143), E130 (= E144), V135 (≠ L149), P137 (= P151), G138 (≠ D152)

Sites not aligning to the query:

active site: 223, 233
binding calcium ion: 233, 238

3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
30% identity, 54% coverage: 7:197/353 of query aligns to 6:185/255 of 3q0jC

query
sites
3q0jC

I

I

L

L

F

V

E

E

R

R

R

D

G

Q

A

R

I

V

G

G

L

I

V

I

T

T

L

L

N

N

R

R

P

P

K
x
Q

A
|
A

L
|
L

N

N

A
|
A

L

L

T

N

L

S

G

Q

M

V

I

M

R

N

L

E

F

V

D

T

P

S

Q

A

L

A

R

T

A

E

W

L

D

D

A

D

D

D

P

P

E

D

V

I

K

G

A

A

V

I

I

I

R

T

G

G

A

S

G

A

E

-

K

K

A

A

F

F

C

A

A
|
A

G
|
G

G
x
A

D
|
D

V
x
I

V
x
K

S

E

L
x
M

Y

-

E

-

A

-

G

-

K

-

A

-

K

-

E

-

G

-

R

-

G

A

D

D

T

L

S

T

P

F

I

A

R

D

A

A

F

F

F
x
T

S

A

E

D

E

F

Y
x
F

V

A

L

T

N

W

R

G

L

K

I

L

K

A

R

A

L

V

S

R

K

T

P

P

Y

T

V

I

A

A

V

A

I

V

D

A

G

G

I

Y

S

A

M

L

G
|
G

G

G

V

C

G
x
E

L

L

S

A

V

M

H

M

G

C

S

D

H

V

R

L

I

I

V

A

T

A

E

D

R

T

T

A

L

K

F

F

A

G

M

Q

P
|
P

E
|
E

T

I

G

K

I

L

G

G

L
x
V

Y

L

P
|
P

D
x
G

V
x
M

G

G

T

S

Y

Q

F

R

L

L

P

T

R

R

L

A

P

I

G

G

Q

K

V

A

G

K

V

A

W

M

-

D

L

L

G

I

L

L

T

T

G

G

D

R

R

T

L

M

K

D

A

A

D

E

L

A

L

E

A

R

I

S

G

G

A

L

A

V

D

S

A

R

F

V

V

V

P

P

S

A

G

D

E

D

I

L

active site: A65 (≠ G67), M70 (≠ L72), T80 (≠ F93), F84 (≠ Y97), G108 (= G121), E111 (≠ G124), P130 (= P143), E131 (= E144), V136 (≠ L149), P138 (= P151), G139 (≠ D152)
binding acetoacetyl-coenzyme a: Q23 (≠ K24), A24 (= A25), L25 (= L26), A27 (= A28), A63 (= A65), G64 (= G66), A65 (≠ G67), D66 (= D68), I67 (≠ V69), K68 (≠ V70), M70 (≠ L72), F84 (≠ Y97), G107 (= G120), G108 (= G121), E111 (≠ G124), P130 (= P143), E131 (= E144), P138 (= P151), G139 (≠ D152), M140 (≠ V153)

Sites not aligning to the query:

active site: 224, 234

3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
30% identity, 54% coverage: 7:197/353 of query aligns to 6:185/255 of 3q0gC

query
sites
3q0gC

I

I

L

L

F

V

E

E

R

R

R

D

G

Q

A

R

I

V

G

G

L

I

V

I

T

T

L

L

N

N

R

R

P

P

K

Q

A

A

L
|
L

N

N

A

A

L

L

T

N

L

S

G

Q

M

V

I

M

R

N

L

E

F

V

D

T

P

S

Q

A

L

A

R

T

A

E

W

L

D

D

A

D

D

D

P

P

E

D

V

I

K

G

A

A

V

I

I

I

R

T

G

G

A

S

G

A

E

-

K

K

A

A

F

F

C

A

A
|
A

G

G

G
x
A

D

D

V
x
I

V
x
K

S

E

L
x
M

Y

-

E

-

A

-

G

-

K

-

A

-

K

-

E

-

G

-

R

-

G

A

D

D

T

L

S

T

P

F

I

A

R

D

A

A

F

F

F
x
T

S

A

E

D

E

F

Y
x
F

V

A

L

T

N

W

R

G

L

K

I

L

K

A

R

A

L

V

S

R

K

T

P

P

Y

T

V

I

A

A

V

A

I

V

D

A

G

G

I
x
Y

S

A

M

L

G

G

G
|
G

G

G

V

C

G
x
E

L

L

S

A

V

M

H

M

G

C

S

D

H

V

R

L

I

I

V

A

T

A

E

D

R

T

T

A

L

K

F

F

A

G

M

Q

P
|
P

E
|
E

T

I

G

K

I
x
L

G

G

L
x
V

Y

L

P
|
P

D
x
G

V

M

G

G

T

S

Y

Q

F

R

L

L

P

T

R

R

L

A

P

I

G

G

Q

K

V

A

G

K

V

A

W

M

-

D

L

L

G

I

L

L

T

T

G

G

D

R

R

T

L

M

K

D

A

A

D

E

L

A

L

E

A

R

I

S

G

G

A

L

A

V

D

S

A

R

F

V

V

V

P

P

S

A

G

D

E

D

I

L

active site: A65 (≠ G67), M70 (≠ L72), T80 (≠ F93), F84 (≠ Y97), G108 (= G121), E111 (≠ G124), P130 (= P143), E131 (= E144), V136 (≠ L149), P138 (= P151), G139 (≠ D152)
binding coenzyme a: L25 (= L26), A63 (= A65), I67 (≠ V69), K68 (≠ V70), Y104 (≠ I117), P130 (= P143), E131 (= E144), L134 (≠ I147)

Sites not aligning to the query:

active site: 224, 234

3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 54% coverage: 7:197/353 of query aligns to 5:180/250 of 3q0gD

query
sites
3q0gD

I

I

L

L

F

V

E

E

R

R

R

D

G

Q

A

R

I

V

G

G

L

I

V

I

T

T

L

L

N

N

R

R

P

P

K

Q

A

A

L

L

N

N

A

A

L

L

T

N

L

S

G

Q

M

V

I

M

R

N

L

E

F

V

D

T

P

S

Q

A

L

A

R

T

A

E

W

L

D

D

A

D

D

D

P

P

E

D

V

I

K

G

A

A

V

I

I

I

R

T

G

G

A

S

G

A

E

-

K

K

A

A

F

F

C

A

A

A

G

G

G
x
A

D

D

V

I

V

K

S

E

L
x
M

Y

F

E

A

A

-

G

-

K

-

A

-

K

-

E

-

G

-

R

-

G

-

D

-

T

-

S

-

P

-

I

-

R

D

A

A

F

F

F
x
T

S

A

E

D

E

F

Y
x
F

V

A

L

T

N

W

R

G

L

K

I

L

K

A

R

A

L

V

S

R

K

T

P

P

Y

T

V

I

A

A

V

A

I

V

D

A

G

G

I

Y

S

A

M

L

G

G

G
|
G

G

G

V

C

G
x
E

L

L

S

A

V

M

H

M

G

C

S

D

H

V

R

L

I

I

V

A

T

A

E

D

R

T

T

A

L

K

F

F

A

G

M

Q

P
|
P

E
|
E

T

I

G

K

I

L

G

G

L
x
V

Y

L

P
|
P

D
x
G

V

M

G

G

T

S

Y

Q

F

R

L

L

P

T

R

R

L

A

P

I

G

G

Q

K

V

A

G

K

V

A

W

M

-

D

L

L

G

I

L

L

T

T

G

G

D

R

R

T

L

M

K

D

A

A

D

E

L

A

L

E

A

R

I

S

G

G

A

L

A

V

D

S

A

R

F

V

V

V

P

P

S

A

G

D

E

D

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L

active site: A64 (≠ G67), M69 (≠ L72), T75 (≠ F93), F79 (≠ Y97), G103 (= G121), E106 (≠ G124), P125 (= P143), E126 (= E144), V131 (≠ L149), P133 (= P151), G134 (≠ D152)

Sites not aligning to the query:

active site: 219, 229
binding Butyryl Coenzyme A: 225, 241

5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
30% identity, 54% coverage: 6:197/353 of query aligns to 6:189/261 of 5jbxB

query
sites
5jbxB

E

E

I

F

L

K

F

V

E

D

R

A

R

R

G

G

A

P

I

I

G

E

L

I

V

W

T

T

L

I

N

D

R

G

P

E

K
x
S

A
x
R

L
x
R

N

N

A
|
A

L

I

T

S

L

R

G

A

M

M

I

L

R

K

L

E

F

L

D

G

P

E

Q

L

L

V

R

T

A

R

W

V

D

S

A

S

D

S

P

R

E

D

V

V

K

R

A

A

V

V

I

I

R

T

G

G

A

A

G

G

E

D

K

K

A

A

F

F

C

C

A
|
A

G

G

G
x
A

D
|
D

V

-

S

-

L
|
L

Y
x
K

E

E

A
x
R

G

A

K

T

A

M

A

A

K

E

E

D

G

-

R

-

G

-

D

-

T

-

S

-

P

E

I

V

R

R

A

A

F

F

F
x
L

S

D

E

G

E

L

Y
x
R

V

R

L

T

N

F

R

R

L

A

I

I

K

E

R

K

L

S

S

D

K

C

P

V

Y

F

V

I

A

A

V

A

I

I

D

N

G

G

I

A

S

A

M
x
L

G
|
G

G

G

V

T

G
x
E

L

L

S

A

V

L

H

A

G

C

S

D

H

L

R

R

I

V

V

A

T

A

E

P

R

A

T

A

L

E

F

L

A

G

M

L

P
x
T

E
|
E

T

V

G

K

I
x
L

G

G

L
x
I

Y

I

P
|
P

D
x
G

V

G

G

G

T

T

Y

Q

F

R

L

L

P

A

R

R

L

L

-

V

-

G

P

P

G

G

Q

R

V

A

G

K

V

D

W

L

L

I

G

-

L

L

T

T

G

A

D

R

R
|
R

L

I

K

N

A

A

D

E

L

A

L

F

A

S

I

V

G

G

A

L

A

A

D

N

A

R

F

L

V

A

P

P

S

E

G

G

E

H

I

L

active site: A67 (≠ G67), R72 (≠ A75), L84 (≠ F93), R88 (≠ Y97), G112 (= G121), E115 (≠ G124), T134 (≠ P143), E135 (= E144), I140 (≠ L149), P142 (= P151), G143 (≠ D152)
binding coenzyme a: S24 (≠ K24), R25 (≠ A25), R26 (≠ L26), A28 (= A28), A65 (= A65), D68 (= D68), L69 (= L72), K70 (≠ Y73), L110 (≠ M119), G111 (= G120), T134 (≠ P143), E135 (= E144), L138 (≠ I147), R168 (= R176)

Sites not aligning to the query:

active site: 228, 238

Q08426 Peroxisomal bifunctional enzyme; PBE; PBFE; L-bifunctional protein; LBP; Multifunctional enzyme 1; MFE1; EC 4.2.1.17; EC 5.3.3.8; EC 1.1.1.35 from Homo sapiens (Human) (see 5 papers)
31% identity, 59% coverage: 12:218/353 of query aligns to 8:197/723 of Q08426

query
sites
Q08426

R

H

G

N

A

A

I

L

G

A

L

L

V

I

T

R

L

L

N

R

R

N

P

P

K

-

A

P

L

V

N

N

A

A

L

I

T

S

L

T

G

T

M

L

I

L

R

R

L

D

F

I

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K

P

E

Q

G

L

L

R

Q

A

K

W

A

D
x
V

A
x
I

D

D

P

H

E

T

V

I

K

K

A

A

V

I

V

V

I

I

R

C

G

G

A

A

G

-

E

E

K

G

A

K

F

F

C

S

A

A

G

G

G

A

D

D

V

I

V

-

S

-

L

-

Y

-

E

-

A

-

G

-

K

-

A

-

K

-

E

-

G

-

R

R

G

G

D

F

T

S

S

A

P

P

I

R

R

T

A

F

F

G

F

L

S
x
T

E

L

E

G

Y

H

V

V

L

V

N

D

R

E

L

-

I

I

K

Q

R

R

L

N

S

E

K

K

P

P

Y

V

V

V

A

A

V

A

I

I

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Q

G

G

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M

S

A

M

F

G

G

V

L

G

E

L

L

S

A

V

L

H

G

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H

H

Y

R

R

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I

V

A

T

H

E

A

R

E

T

A

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F

V

A

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M

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P

E

E

T

V

G

T

I

L

G

G

L

L

Y

L

P

P

D

G

V

A

G

R

G

G

T

T

Y

Q

F

L

L

L

P

P

R

R

L

L

P

T

G

G

-

V

Q

P

V

A

G

A

V

L

W

D

L

L

G

I

L

T

T

S

G

G

D

R

R

R

L

I

K

L

A

A

A

D

D

E

L

A

L

L

A
x
K

I

L

G

G

A

I

A

L

D

D

A
x
K

F

V

V

V

P

N

S

S

G

D

E

P

I

V

D

E

G

E

L

A

I

I

G

R

D

-

L

-

A

F

A

A

G

Q

R

R

P

V

A

S

D

D

E

Q

A

P

I

L

A

E

T

S

R

R

V40 (≠ D45) to G: in dbSNP:rs1062551
I41 (≠ A46) to R: in dbSNP:rs1062552
T75 (≠ S94) to I: in dbSNP:rs1062553
K165 (≠ A184) modified: N6-acetyllysine; alternate; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584.
K171 (≠ A190) modified: N6-acetyllysine; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584.

Sites not aligning to the query:

3 E → K: in FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells; dbSNP:rs398124646
274 A → T: in dbSNP:rs2302819
325 A → G: in dbSNP:rs1062555
346 modified: N6-acetyllysine; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584.
584 modified: N6-acetyllysine; alternate; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346.
598 K → T: in dbSNP:rs1042437
606 T → P: in dbSNP:rs1042438

6eqoA Tri-functional propionyl-coa synthase of erythrobacter sp. Nap1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester (see paper)
30% identity, 50% coverage: 15:191/353 of query aligns to 867:1043/1804 of 6eqoA

query
sites
6eqoA

I

V

G

A

L

T

V

V

T

T

L

V

N

K

R

N

P

P

-

P

-

V

K

N

A

A

L

L

N

N

A

E

L

R

T

A

L

L

G

D

M

E

I

L

R

V

L

I

F

I

D

A

P

E

Q

H

L

L

R

A

A

R

W

K

D

D

A

-

D

-

P

-

E

D

V

V

K

A

A

A

V

V

I

F

R

T

G

G

A

S

G

G

E

T

K

A

A

S

F

F

C

V

A

A

G

G

G
x
A

D

D

V

I

V

R

S

Q

L

M

Y

L

E

E

A

E

G

V

K

N

A

S

A

V

K

E

E

E

G

A

R

K

G

A

D

L

T

P

S

D

P

N

I

A

R

Q

A

L

F

A

F

F

S

-

E

-

Y

-

V

-

L

-

N

-

R

R

L

T

I

I

K

E

R

E

L

M

S

D

K

K

P

P

Y

C

V

I

A

A

V

A

I

I

D

Q

G

G

I

V

S

A

M

L

G

G

G
|
G

G

G

V

M

G
x
E

L

F

S

A

V

L

H

A

G

C

S

H

H

Y

R

R

I

V

V

A

T

E

E

P

R

K

T

A

L

R

F

F

A

G

M

Q

P

P

E
|
E

T

I

G

N

I

L

G

R

L

L

Y

L

P

P

D
x
G

V

Y

G

G

T

T

Y

Q

F

R

L

L

P

P

R

R

L

L

-

L

-

A

-

D

-

G

P

G

G

G

Q

E

V

T

G

G

V

L

W

R

-

D

-

A

-

L

-

D

L

L

G

I

L

L

T

G

G

G

D

R

R

A

L

I

K

D

A

A

A

D

D

A

L

A

L

L

A

A

I

V

G

G

A

A

A

V

D

D

A

A

F

L

active site: A918 (≠ G67), G965 (= G121), E968 (≠ G124), E988 (= E144), G996 (≠ D152)

Sites not aligning to the query:

binding phosphomethylphosphonic acid adenylate ester: 456, 458, 535, 536, 537, 538, 558, 559, 560, 561, 562, 688, 714
binding nadp nicotinamide-adenine-dinucleotide phosphate: 1261, 1265, 1379, 1400, 1403, 1404, 1405, 1424, 1425, 1429, 1444, 1492, 1493, 1497, 1514, 1517, 1713, 1730, 1731, 1774

Query Sequence

>WP_012974023.1 NCBI__GCF_000010725.1:WP_012974023.1
MSDDAEILFERRGAIGLVTLNRPKALNALTLGMIRLFDPQLRAWDADPEVKAVVIRGAGE
KAFCAGGDVVSLYEAGKAAKEGRGDTSPIRAFFSEEYVLNRLIKRLSKPYVAVIDGISMG
GGVGLSVHGSHRIVTERTLFAMPETGIGLYPDVGGTYFLPRLPGQVGVWLGLTGDRLKAA
DLLAIGAADAFVPSGEIDGLIGDLAAGRPADEAIATRRGDAGEAMVRALRAVIDRCYAFD
SVEAIVKALEAEGGDWANGQLATLRRVSPTSLKVTLAALRRGAGLDFDGCMVQELRLSLA
CLAGVDFYEGIRAVLVDKDKSPKWKPANLADVGPSDVARHFTEPAGGDLLFRD

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