SitesBLAST

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)
34% identity, 94% coverage: 16:258/259 of query aligns to 50:287/290 of P14604

query
sites
P14604

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E144 (≠ T115) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
E164 (≠ Y135) 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

1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
32% identity, 88% coverage: 13:240/259 of query aligns to 13:242/269 of 1jxzB

query
sites
1jxzB

V

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H

active site: C61 (= C61), F64 (≠ G64), I69 (≠ F72), A86 (= A84), Q90 (≠ N88), G113 (= G111), G114 (≠ A112), G117 (≠ T115), A136 (= A134), W137 (≠ Y135), I142 (≠ L140), N144 (≠ I142), D145 (= D143), E230 (= E228)
binding 4-hydroxybenzoyl coenzyme a: R22 (≠ K22), H23 (≠ N23), R24 (≠ L24), A62 (= A62), F64 (≠ G64), Y65 (≠ D65), L66 (= L66), R67 (≠ K67), W89 (≠ L87), G113 (= G111), A136 (= A134), W137 (≠ Y135), I142 (≠ L140), D145 (= D143), T146 (≠ G144)
binding calcium ion: G49 (≠ R49), L202 (= L200), A203 (= A201), A205 (≠ R203), T207 (≠ L205), Q210 (≠ F208)

Sites not aligning to the query:

binding 4-hydroxybenzoyl coenzyme a: 252, 257

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)
31% identity, 93% coverage: 13:252/259 of query aligns to 13:254/269 of A5JTM5

query
sites
A5JTM5

V

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R24 (≠ L24) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
E34 (= E34) mutation to T: Forms inclusion bodies.
E43 (≠ A43) mutation to A: No effect on catalytic activity.
D45 (= D45) mutation to A: No effect on catalytic activity.
D46 (≠ A46) mutation to A: No effect on catalytic activity.
G63 (= G63) mutation G->A,I,P: Yields insoluble protein.
F64 (≠ G64) 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 (≠ D65) mutation to D: Catalytic activity is almost as efficient as wild type.
R67 (≠ K67) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
E68 (≠ D71) mutation to T: No effect on catalytic activity.
H81 (vs. gap) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
F82 (= F80) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
W89 (≠ L87) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
H90 (≠ N88) 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 (≠ V92) mutation to Q: No effect on catalytic activity.
A112 (= A110) 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 (= G111) 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 (≠ A112) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
G115 (= G113) mutation G->L,N,S,V: Yields insoluble protein.
D123 (= D121) mutation to T: No effect on catalytic activity.
D129 (≠ K127) mutation to T: No effect on catalytic activity.
W137 (≠ Y135) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
D145 (= D143) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
E163 (= E161) mutation to T: No effect on catalytic activity.
E175 (≠ K173) mutation to D: No effect on catalytic activity.
W179 (= W177) mutation to F: No effect on catalytic activity.
H208 (= H206) mutation to Q: No effect on catalytic activity.
R216 (≠ L214) mutation R->E,K,L: Yields insoluble protein.
E232 (= E230) mutation E->A,N,Q,R: Yields insoluble protein.; mutation to D: Reduced catalytic activity, increased substrate binding.

Sites not aligning to the query:

257 R→K: Retains catalytic activity and substrate CoA binding.; R→L: Significantly reduces catalytic activity and substrate CoA binding.

5du6A Crystal structure of m. Tuberculosis echa6 bound to ligand gsk059a. (see paper)
33% identity, 99% coverage: 3:258/259 of query aligns to 1:239/242 of 5du6A

query
sites
5du6A

E

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L

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D

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G
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A

D

D

L

L

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D

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A
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D

D

D

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Y

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L

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L

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D

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A

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M

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L

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A

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L

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A

L

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F

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K

L

D

N

L

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F

D

N

D

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A

A

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N

E

D
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A

F

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x
P

T

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A
x
K

E

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E
x
F

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D

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A

A

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x
W

A

G

A

S

C

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A

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D

D

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E

E

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A

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E

K

K

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P

K

K

F

F

active site: A61 (≠ G64), P71 (≠ A73), I75 (≠ N88), A99 (= A112), Q102 (≠ T115), P121 (≠ A134), T122 (≠ Y135), L127 (= L140), L129 (≠ I142), D130 (= D143), P209 (≠ E224), W219 (≠ L234)
binding (5R,7R)-5-(4-ethylphenyl)-N-(4-fluorobenzyl)-7-methyl-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L74 (= L87), D82 (≠ R95), D130 (= D143), W132 (≠ G145), A207 (≠ D222), K212 (≠ A227), F215 (≠ E230)

5dufA Crystal structure of m. Tuberculosis echa6 bound to ligand gsk729a (see paper)
33% identity, 99% coverage: 3:258/259 of query aligns to 2:242/245 of 5dufA

query
sites
5dufA

E

H

L

M

V

I

E

G

I

I

V

T

D

Q

H

A

G

E

M

A

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T

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A

E

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P

K

E

N

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L

R

N

N

A

A

L

L

N

N

L

S

Q

Q

L

L

M

V

T

E

E

E

L

L

A

T

D

Q

A

A

L

I

T

R

A

K

A

A

A

G

A

-

D

D

A

G

S

S

V

A

R

R

G

A

V

I

L

V

L

L

T

T

G

G

R

Q

G

G

K

T

A

A

F

F

C

C

A

A

G

G

G
x
A

D

D

L

L

K

S

-

G

-
x
D

-

A

W

F

A

A

L

A

D

D

F

Y

A
x
P

D

D

D

-

P

-

G

-

V

-

S

-

F

-

H

-

T

-

L

-

A

-

G

-

Q

R

L
|
L

N
x
I

R

E

V

L

A
x
H

V

K

E

A

L

M

R
x
D

N

A

M

S

P

P

K

M

P

P

V

V

A

V

A

G

A

A

V

I

Q

N

G

G

A

P

A

A

A

I

G

G

A
|
A

G

G

F

L

T
x
Q

L

L

A

A

L

M

A

Q

C

C

D

D

F

L

R

R

V

V

M

V

E

A

K

P

S

D

A

A

F

F

Q

Q

Q

F

A
x
P

Y
x
T

T

S

S

K

N

Y

G

G

L
|
L

C

A

I
x
L

D
|
D

G

N

G
x
W

G

S

T

I

F

R

T

R

L

L

P

S

R

S

L

L

V

V

G

G

M

H

A

G

R

R

A

A

L

R

E

A

I

M

A

L

F

S

D

A

E

E

R

K

I

L

P

T

A

A

E

E

K

I

A

A

L

L

E

H

W

T

G

G

L

M

V

A

T

N

R

R

L

I

A

G

E

T

D

L

G

A

A

D

A

A

R

Q

D

A

E

W

A

A

L

A

D

E

M

-

L

I

N

A

R

R

L

L

A

A

E

P

R

L

S

A

L

I

H

Q

S

H

F

A

A

K

R

R

C

V

K

L

D

N

L

-

F

D

N

D

R

G

A

A

F

I

Q

E

N

E

D

A

F

W

E
x
P

T

A

Q

H

A

K

E

E

R

L

E

F

R

D

R

K

A

A

L
x
W

A

G

A

S

C

-

A

-

R

-

H

-

E

Q

D

D

G

V

R

I

E

E

G

A

L

Q

R

V

A

A

F

R

V

M

E

E

K

K

R

R

P

P

K

K

F

F

active site: A62 (≠ G64), D67 (vs. gap), P74 (≠ A73), I78 (≠ N88), A102 (= A112), Q105 (≠ T115), P124 (≠ A134), T125 (≠ Y135), L130 (= L140), L132 (≠ I142), D133 (= D143), P212 (≠ E224), W222 (≠ L234)
binding (5R,7S)-5-(4-ethylphenyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxylic acid: L77 (= L87), I78 (≠ N88), H81 (≠ A91), D85 (≠ R95), Q105 (≠ T115), D133 (= D143), W135 (≠ G145)

5ducA Crystal structure of m. Tuberculosis echa6 bound to ligand gsk951a (see paper)
33% identity, 99% coverage: 3:258/259 of query aligns to 1:241/244 of 5ducA

query
sites
5ducA

E

H

L

M

V

I

E

G

I

I

V

T

D

Q

H

A

G

E

M

A

V

V

R

L

E

T

V

I

A

E

M

L

N

Q

R

R

P

P

K

E

N

R

L

R

N

N

A

A

L

L

N

N

L

S

Q

Q

L

L

M

V

T

E

E

E

L

L

A

T

D

Q

A

A

L

I

T

R

A

K

A

A

A

G

A

-

D

D

A

G

S

S

V

A

R

R

G

A

V

I

L

V

L

L

T

T

G

G

R

Q

G

G

K

T

A

A

F

F

C

C

A

A

G

G

G
x
A

D

D

L

L

K

S

-

G

-
x
D

-

A

W

F

A

A

L

A

D

D

F

Y

A
x
P

D

D

D

-

P

-

G

-

V

-

S

-

F

-

H

-

T

-

L

-

A

-

G

-

Q

R

L
|
L

N
x
I

R

E

V

L

A
x
H

V

K

E

A

L

M

R
x
D

N

A

M

S

P

P

K

M

P

P

V

V

A

V

A

G

A

A

V

I

Q

N

G

G

A

P

A

A

A

I

G

G

A
|
A

G

G

F

L

T
x
Q

L

L

A

A

L

M

A

Q

C

C

D

D

F

L

R

R

V

V

M

V

E

A

K

P

S

D

A

A

F

F

Q

Q

Q

F

A
x
P

Y
x
T

T

S

S

K

N

Y

G

G

L
|
L

C

A

I
x
L

D
|
D

G

N

G
x
W

G

S

T

I

F

R

T

R

L

L

P

S

R

S

L

L

V

V

G

G

M

H

A

G

R

R

A

A

L

R

E

A

I

M

A

L

F

S

D

A

E

E

R

K

I

L

P

T

A

A

E

E

K

I

A

A

L

L

E

H

W

T

G

G

L

M

V

A

T

N

R

R

L

I

A

G

E

T

D

L

G

A

A

D

A

A

R

Q

D

A

E

W

A

A

L

A

D

E

M

-

L

I

N

A

R

R

L

L

A

A

E

P

R

L

S

A

L

I

H

Q

S

H

F

A

A

K

R

R

C

V

K

L

D

N

L

-

F

D

N

D

R

G

A

A

F

I

Q

E

N

E

D

A

F

W

E
x
P

T

A

Q

H

A

K

E

E

R

L

E
x
F

R

D

R

K

A

A

L
x
W

A

G

A

S

C

-

A

-

R

-

H

-

E

Q

D

D

G

V

R

I

E

E

G

A

L

Q

R

V

A

A

F

R

V

M

E

E

K

K

R

R

P

P

K

K

F

F

active site: A61 (≠ G64), D66 (vs. gap), P73 (≠ A73), I77 (≠ N88), A101 (= A112), Q104 (≠ T115), P123 (≠ A134), T124 (≠ Y135), L129 (= L140), L131 (≠ I142), D132 (= D143), P211 (≠ E224), W221 (≠ L234)
binding (5R,7S)-N-(1,3-benzodioxol-5-ylmethyl)-5-(4-ethylphenyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L76 (= L87), H80 (≠ A91), D84 (≠ R95), Q104 (≠ T115), D132 (= D143), W134 (≠ G145), F217 (≠ E230)

5du4A Crystal structure of m. Tuberculosis echa6 bound to ligand gsk366a (see paper)
33% identity, 99% coverage: 3:258/259 of query aligns to 1:241/244 of 5du4A

query
sites
5du4A

E

H

L

M

V

I

E

G

I

I

V

T

D

Q

H

A

G

E

M

A

V

V

R

L

E

T

V

I

A

E

M

L

N

Q

R

R

P

P

K

E

N

R

L

R

N

N

A

A

L

L

N

N

L

S

Q

Q

L

L

M

V

T

E

E

E

L

L

A

T

D

Q

A

A

L

I

T

R

A

K

A

A

A

G

A

-

D

D

A

G

S

S

V

A

R

R

G

A

V

I

L

V

L

L

T

T

G

G

R

Q

G

G

K

T

A

A

F

F

C

C

A

A

G

G

G
x
A

D

D

L

L

K

S

-

G

-
x
D

-

A

W

F

A

A

L

A

D

D

F

Y

A
x
P

D

D

D

-

P

-

G

-

V

-

S

-

F

-

H

-

T

-

L

-

A

-

G

-

Q

R

L
|
L

N
x
I

R

E

V

L

A
x
H

V

K

E

A

L

M

R
x
D

N

A

M

S

P

P

K

M

P

P

V

V

A

V

A

G

A

A

V

I

Q

N

G

G

A

P

A

A

A

I

G

G

A
|
A

G

G

F

L

T
x
Q

L

L

A

A

L

M

A

Q

C

C

D

D

F

L

R

R

V

V

M

V

E

A

K

P

S

D

A

A

F

F

Q

Q

Q

F

A
x
P

Y
x
T

T

S

S

K

N

Y

G

G

L
|
L

C

A

I
x
L

D
|
D

G

N

G
x
W

G

S

T

I

F

R

T

R

L

L

P

S

R

S

L

L

V

V

G

G

M

H

A

G

R

R

A

A

L

R

E

A

I

M

A

L

F

S

D

A

E

E

R

K

I

L

P

T

A

A

E

E

K

I

A

A

L

L

E

H

W

T

G

G

L

M

V

A

T

N

R

R

L

I

A

G

E

T

D

L

G

A

A

D

A

A

R

Q

D

A

E

W

A

A

L

A

D

E

M

-

L

I

N

A

R

R

L

L

A

A

E

P

R

L

S

A

L

I

H

Q

S

H

F

A

A

K

R

R

C

V

K

L

D

N

L

-

F

D

N

D

R

G

A

A

F

I

Q

E

N

E

D

A

F

W

E
x
P

T

A

Q

H

A

K

E

E

R

L

E

F

R

D

R

K

A

A

L
x
W

A

G

A

S

C

-

A

-

R

-

H

-

E

Q

D

D

G

V

R

I

E

E

G

A

L

Q

R

V

A

A

F

R

V

M

E

E

K

K

R

R

P

P

K

K

F

F

active site: A61 (≠ G64), D66 (vs. gap), P73 (≠ A73), I77 (≠ N88), A101 (= A112), Q104 (≠ T115), P123 (≠ A134), T124 (≠ Y135), L129 (= L140), L131 (≠ I142), D132 (= D143), P211 (≠ E224), W221 (≠ L234)
binding (5R,7S)-5-(4-ethylphenyl)-N-(4-methoxybenzyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L76 (= L87), I77 (≠ N88), H80 (≠ A91), D84 (≠ R95), Q104 (≠ T115), D132 (= D143), W134 (≠ G145)

5dtwA Crystal structure of m. Tuberculosis echa6 bound to c20-coa (see paper)
33% identity, 99% coverage: 3:258/259 of query aligns to 1:241/244 of 5dtwA

query
sites
5dtwA

E

H

L

M

V

I

E

G

I

I

V

T

D

Q

H

A

G

E

M

A

V

V

R

L

E

T

V

I

A

E

M

L

N

Q

R
|
R

P

P

K
x
E

N
x
R

L
x
R

N

N

A
|
A

L

L

N

N

L

S

Q

Q

L

L

M

V

T

E

E

E

L

L

A

T

D

Q

A

A

L

I

T

R

A

K

A

A

A

G

A

-

D

D

A

G

S

S

V

A

R

R

G

A

V

I

L

V

L

L

T

T

G

G

R

Q

G

G

K

T

A

A

F

F

C

C

A
|
A

G

G

G
x
A

D
|
D

L
|
L

K

S

-

G

-
x
D

-

A

W

F

A

A

L

A

D

D

F

Y

A
x
P

D

D

D

-

P

-

G

-

V

-

S

-

F

-

H

-

T

-

L

-

A

-

G

-

Q

R

L

L

N
x
I

R

E

V

L

A
x
H

V

K

E

A

L

M

R
x
D

N

A

M

S

P

P

K

M

P

P

V

V

A

V

A

G

A

A

V

I

Q

N

G

G

A

P

A

A

A

I

G
|
G

A
|
A

G

G

F

L

T
x
Q

L

L

A

A

L

M

A

Q

C

C

D

D

F

L

R

R

V

V

M

V

E

A

K

P

S

D

A

A

F

F

Q

Q

Q

F

A
x
P

Y
x
T

T

S

S

K

N
x
Y

G

G

L
|
L

C

A

I
x
L

D
|
D

G

N

G
x
W

G

S

T

I

F

R

T

R

L

L

P

S

R

S

L

L

V

V

G

G

M

H

A

G

R

R

A

A

L

R

E

A

I

M

A

L

F

S

D

A

E

E

R

K

I

L

P

T

A

A

E

E

K

I

A

A

L

L

E

H

W

T

G

G

L

M

V

A

T

N

R

R

L

I

A

G

E

T

D

L

G

A

A

D

A

A

R

Q

D

A

E

W

A

A

L

A

D

E

M

-

L

I

N

A

R

R

L

L

A

A

E

P

R

L

S

A

L

I

H

Q

S

H

F

A

A

K

R

R

C

V

K

L

D

N

L

-

F

D

N

D

R

G

A

A

F

I

Q

E

N

E

D

A

F

W

E
x
P

T

A

Q

H

A

K

E

E

R

L

E

F

R

D

R

K

A

A

L
x
W

A

G

A

S

C

-

A

-

R

-

H

-

E

Q

D

D

G

V

R

I

E

E

G

A

L

Q

R

V

A

A

F

R

V

M

E

E

K

K

R

R

P

P

K

K

F

F

active site: A61 (≠ G64), D66 (vs. gap), P73 (≠ A73), I77 (≠ N88), A101 (= A112), Q104 (≠ T115), P123 (≠ A134), T124 (≠ Y135), L129 (= L140), L131 (≠ I142), D132 (= D143), P211 (≠ E224), W221 (≠ L234)
binding Arachinoyl-CoA: R18 (= R20), E20 (≠ K22), R21 (≠ N23), R21 (≠ N23), R22 (≠ L24), A24 (= A26), A59 (= A62), A61 (≠ G64), D62 (= D65), L63 (= L66), H80 (≠ A91), D84 (≠ R95), G100 (= G111), A101 (= A112), Y127 (≠ N138), W134 (≠ G145)

2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
33% identity, 94% coverage: 16:258/259 of query aligns to 19:251/254 of 2dubA

query
sites
2dubA

V

I

A

Q

M

L

N

N

R

R

P

P

K
|
K

N
x
A

L
|
L

N

N

A
|
A

L

L

N

C

L

N

Q

G

L

L

M

I

T

E

E

E

L

L

A

N

D

Q

A

A

L

L

T

E

A

T

A

F

A

E

D

D

A

P

S

A

V

V

R

G

G

A

V

I

L

V

L

L

T

T

G

G

R

G

G

E

K

K

A

A

F

F

C

A

A
|
A

G

G

G
x
A

D
|
D

L
x
I

K
|
K

W

-

A

-

L

-

D

-

F

-

A

-

D

E

D
x
M

P

Q

G

N

V

R

S

T

F

F

H

Q

T

D

L

C

A

Y

G
x
S

Q

H

L

W

N

D

R

H

V

I

A

T

V

-

E

-

L

-

R

-

N

R

M

I

P

K

K

K

P

P

V

V

A

I

A

A

V

V

Q

N

G

G

A

Y

A

A

A

L

G

G

A
x
G

G

G

F

C

T
x
E

L

L

A

A

L

M

A

M

C

C

D

D

F

I

R

I

V

Y

M

A

E

G

K

E

S

K

A

A

F

Q

F

F

Q

G

Q

Q

A
x
P

Y
x
E

T

I

S

L

N

L

G

G

L
x
T

C

I

I
x
P

D
x
G

G
x
A

G

G

T

T

F

Q

T

R

L

L

P

T

R

R

L

A

V

V

G

G

M

K

A

S

R

L

A

A

L

M

E

E

I

M

A

V

A

L

F

T

D

G

E

D

R

R

I

I

P

S

A

A

E

Q

K

D

A

A

L

K

E

Q

W

A

G

G

L

L

V

V

T

S

R

K

L

I

A

F

E

P

D

V

G

E

A

T

A

L

R

V

D

E

E

E

A

A

L

I

D

Q

M

C

L

A

N

E

R

K

L

I

A

A

E

N

R

N

S

S

L

K

H

I

S

I

F

V

A

A

R

M

C

A

K

K

D

E

L

S

F

V

N

N

R

A

A

A

F

F

Q

E

N

M

D

T

F

L

E

T

T

E

Q

G

A

N

E
x
K

R

L

E

E

R

K

A

L

L

F

A

Y

A

S

C

T

A
x
F

R

A

H

T

E

D

D

D

G

R

R

R

E

E

G

G

L

M

R

S

A

A

F

F

V

V

E

E

K

K

R

R

P

K

P

A

K

N

F

F

active site: A67 (≠ G64), M72 (≠ D75), S82 (≠ G85), G105 (≠ A112), E108 (≠ T115), P127 (≠ A134), E128 (≠ Y135), T133 (≠ L140), P135 (≠ I142), G136 (≠ D143), K221 (≠ E228), F231 (≠ A238)
binding octanoyl-coenzyme a: K25 (= K22), A26 (≠ N23), L27 (= L24), A29 (= A26), A65 (= A62), A67 (≠ G64), D68 (= D65), I69 (≠ L66), K70 (= K67), G105 (≠ A112), E108 (≠ T115), P127 (≠ A134), E128 (≠ Y135), G136 (≠ D143), A137 (≠ G144)

Query Sequence

>WP_073038817.1 NCBI__GCF_900129305.1:WP_073038817.1
MPELVEIVDHGMVREVAMNRPKNLNALNLQLMTELADALTAAAADASVRGVLLTGRGKAF
CAGGDLKWALDFADDPGVSFHTLAGQLNRVAVELRNMPKPVAAAVQGAAAGAGFTLALAC
DFRVMEKSAFFQQAYTSNGLCIDGGGTFTLPRLVGMARALEIAAFDERIPAEKALEWGLV
TRLAEDGAARDEALDMLNRLAERSLHSFARCKDLFNRAFQNDFETQAERERRALAACARH
EDGREGLRAFVEKRPPKFV

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