SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing Pf1N1B4_5593 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5593 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)

O69762 Hydroxycinnamoyl-CoA hydratase-lyase; HCHL; P-hydroxycinnamoyl CoA hydratase/lyase; Trans-feruloyl-CoA hydratase/vanillin synthase; EC 4.1.2.61 from Pseudomonas fluorescens (see 2 papers)
98% identity, 100% coverage: 1:276/276 of query aligns to 1:276/276 of O69762

query
sites
O69762

M
|
M

S

S

N

T

Y

Y

E

E

G

G

R

R

W

W

T

K

T

T

V

V

K

K

V

V

E

E

I

I

E

E

E

D

G

G

I

I

A

A

W

F

V

V

I

I

L

L

N

N

R

R

P

P

E

E

K
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K

R

R

N

N

A

A

M

M

S

S

P

P

T

T

L

L

N

N

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R

E

E

M

M

I

I

D

D

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V

L

L

E

E

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T

L

L

E

E

Q

Q

D

D

P

P

D

A

A

A

G

G

V

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L

L

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V

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L

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T

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G

A

A

G

G

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E

A

A

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W

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T

A
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A

G

G

M
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M

D

D

L
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L

K

K

E

E

Y
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Y

F

F

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R

E

E

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V

D

D

A

A

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G

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P

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E

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I

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L

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E

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E

A

A

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S

Q

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W

W

Q

Q

W

W

K

K

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L

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R

M

M

Y

Y

A

A

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K

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P

T

T

I

I

A

A

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M

V

V

N

N

G

G

W

W

C

C

F

F

G

G

G
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G

G

G

F

F

S
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S

P

P

L

L

V

V

A

A

C

C

D

D

L

L

A

A

I

I

C

C

A

A

D

D

E

E

A

A

T

T

F

F

G

G

L

L

S
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S

E
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E

I

I

N

N

W
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W

G

G

I

I

P

P

G
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G

N

N

L

L

V

V

S

S

K

K

A

A

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M

A

A

D

D

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H

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Y

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G

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T

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F

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G

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Q

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K

A

A

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E

M

M

G

G

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L

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V

N

N

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E

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S

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V

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P

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L

A

A

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Q

L

L

R

R

E

E

V

V

T

T

I

I

E

E

L

L

A

A

R

R

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N

L

L

E

E

K

K

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N

P

P

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V

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L

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R

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A

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K

H

H

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G

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F

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K

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R

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C

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E

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T

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W

E

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N

N

E

E

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D

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Y

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Y
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Y

A

A

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L

D

D

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R

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L

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D

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T

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G

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M

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D

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K

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A

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Y

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R

M1 (= M1) modified: Initiator methionine, Removed
K29 (= K29) binding
A68 (= A68) binding
M70 (= M70) binding
L72 (= L72) binding
Y75 (= Y75) binding
G120 (= G120) binding
S123 (= S123) mutation to A: Reduced kcat compared to wild-type but not markerdly.
S142 (= S142) binding
E143 (= E143) mutation to A: Abolishes catalytic activity.
W146 (= W146) binding
G151 (= G151) binding
Y239 (= Y239) binding ; mutation to F: Increased KM for feruloyl-CoA but retains a significant amount of catalytic activity with a kcat 10 times less than that of the wild-type.

2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
98% identity, 89% coverage: 4:250/276 of query aligns to 1:247/247 of 2vssB

query
sites
2vssB

Y

Y

E

E

G

G

R

R

W

W

T

K

T

T

V

V

K

K

V

V

E

E

I

I

E

E

E

D

G

G

I

I

A

A

W

F

V

V

I

I

L

L

N

N

R

R

P

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E
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E

K
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K

R
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R

N

N

A
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A

M

M

S

S

P

P

T

T

L

L

N

N

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R

E

E

M

M

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I

D

D

V

V

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L

E

E

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Q

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D

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P

D

A

A

A

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G

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L

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V

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L

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T

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G

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A

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E

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A

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G

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M

D
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D

L

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K

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Y
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Y

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F

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R

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D
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D

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A

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G

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P

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E

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I

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E

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K

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I

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R
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E

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A

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W

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Q

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M

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Y

A

A

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K

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P

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I

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A

M

M

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V

N

N

G

G

W
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W

C

C

F
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F

G

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G
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G

G

G

F

F

S
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S

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P

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L

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V

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A

C

C

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D

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L

A

A

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I

C

C

A

A

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D

E

E

A

A

T

T

F

F

G

G

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L

S
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S

E
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E

I

I

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N

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W

G

G

I
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I

P

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P
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P

G
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G

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N

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L

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V

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S

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K

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A

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M

A

A

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D

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V

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L

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Y

I

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M

M

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G

G

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K

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T

F

F

G

G

Q

Q

K

K

A

A

E

E

M

M

G

G

L

L

V

V

N

N

E

E

S

S

V

V

P

P

L

L

A

A

Q

Q

L

L

R

R

E

E

V

V

T

T

I

I

E

E

L

L

A

A

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R

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N

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L

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E

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K

N

N

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P

V

V

L

L

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A

A

K

K

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H

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G

F

F

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K

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C

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E

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L

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T

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W

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E

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Q

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N

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E

D

D

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Y
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A

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K

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L

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D

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Q

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D
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T

active site: M67 (= M70), Y72 (= Y75), D77 (= D80), R89 (= R92), Q93 (= Q96), G117 (= G120), S120 (= S123), S139 (= S142), E140 (= E143), I145 (= I148), P147 (= P150), G148 (= G151), Y236 (= Y239), D246 (= D249)
binding acetyl coenzyme *a: E25 (= E28), K26 (= K29), R27 (= R30), A29 (= A32), A65 (= A68), M67 (= M70), D68 (= D71), W113 (= W116), F115 (= F118), G117 (= G120), S139 (= S142), E140 (= E143)

2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
98% identity, 89% coverage: 3:248/276 of query aligns to 1:246/246 of 2vssD

query
sites
2vssD

N

T

Y

Y

E

E

G

G

R

R

W

W

T

K

T

T

V

V

K

K

V

V

E

E

I

I

E

E

E

D

G

G

I

I

A

A

W

F

V

V

I

I

L

L

N

N

R

R

P

P

E
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E

K
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K

R
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R

N

N

A
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A

M

M

S

S

P

P

T

T

L

L

N

N

R

R

E

E

M

M

I

I

D

D

V

V

L

L

E

E

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T

L

L

E

E

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Q

D

D

P

P

D

A

A

A

G

G

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V

L

L

V

V

L

L

T

T

G

G

A

A

G

G

E

E

A

A

W

W

T

T

A
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A

G

G

M
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M

D
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D

L
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L

K

K

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E

Y
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Y

F
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F

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R

E

E

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V

D
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D

A

A

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G

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P

E

E

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I

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L

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Q

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E

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K

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R
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R

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E

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A

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S

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Q

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Q
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Q

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W

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K

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R

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M

Y

Y

A

A

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K

P

P

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A

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M

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N

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G

W
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W

C

C

F
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F

G

G

G
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G

G

G

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F

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S

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P

L

L

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V

A

A

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C

D

D

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L

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A

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I

C

C

A

A

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D

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E

A

A

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T

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F

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E
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E

I

I

N

N

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W

G

G

I
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I

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P
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P

G
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G

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N

L

L

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V

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S

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K

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A

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M

A

A

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D

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T

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V

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G

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H

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L

Y

Y

I

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M

M

T

T

G

G

K

K

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T

F

F

G

G

Q

Q

K

K

A

A

E

E

M

M

G

G

L

L

V

V

N

N

E

E

S

S

V

V

P

P

L

L

A

A

Q

Q

L

L

R

R

E

E

V

V

T

T

I

I

E

E

L

L

A

A

R

R

N

N

L

L

E

E

K

K

N

N

P

P

V

V

L

L

R

R

A

A

K

K

H

H

G

G

F

F

K

K

R

R

C

C

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R

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E

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L

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T

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W

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E

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Q

N

N

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E

D

D

Y

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Y
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Y

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A

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L

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D

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Q

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S

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R

L

L

active site: M68 (= M70), Y73 (= Y75), D78 (= D80), R90 (= R92), Q94 (= Q96), G118 (= G120), S121 (= S123), S140 (= S142), E141 (= E143), I146 (= I148), P148 (= P150), G149 (= G151), Y237 (= Y239)
binding acetyl coenzyme *a: E26 (= E28), K27 (= K29), R28 (= R30), A30 (= A32), A66 (= A68), M68 (= M70), D69 (= D71), L70 (= L72), F74 (= F76), W114 (= W116), F116 (= F118), S140 (= S142)
binding 4-hydroxy-3-methoxybenzaldehyde: M68 (= M70), Y73 (= Y75), F74 (= F76), Q96 (= Q98), E141 (= E143), G149 (= G151), N150 (= N152)

6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
91% identity, 90% coverage: 2:250/276 of query aligns to 1:244/244 of 6l3pA

query
sites
6l3pA

S

S

N

K

Y

Y

E

E

G

G

R

R

W

W

T

T

V

V

K

K

V

V

E

E

I

L

E

E

E

A

G

G

I

I

A

A

W

W

V

V

I

T

L

L

N

N

R

R

P

P

E

E

K
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K

R
|
R

N

N

A
|
A

M

M

S

S

P

P

T

T

L

L

N

N

R

R

E

E

M

M

I

V

D

D

V

V

L

L

E

E

T

T

L

L

E

E

Q

Q

D

D

P

A

D

D

A

A

G

G

V

V

L

L

V

V

L

L

T

T

G

G

A

A

G

G

E

E

A

S

W

W

T

T

A
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A

G

G

M
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M

D
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D

L
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L

K

K

E

E

Y
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Y

F

F

R

R

E

E

V

-

D

-

A

-

G

-

P

-

E

E

I

I

L

L

Q

Q

E

E

K

K

I

I

R

R

R
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R

E

E

A

A

S

S

Q
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Q

W

W

Q

Q

W

W

K

K

L

L

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R

M

L

Y

Y

A

A

K

K

P

P

T

T

I

I

A

A

M

M

V

V

N

N

G

G

W

W

C

C

F

F

G
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G

G

G

F

F

S
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S

P

P

L

L

V

V

A

A

C

C

D

D

L

L

A

A

I

I

C

C

A

A

D

N

E

E

A

A

T

T

F

F

G

G

L

L

S
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S

E
|
E

I

I

N

N

W

W

G

G

I
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I

P

P

P
|
P

G
|
G

N

N

L

L

V

V

S

S

K

K

A

A

M

M

A

A

D

D

T

T

V

V

G

G

H

H

R

R

Q

Q

S

S

L

L

Y

Y

I

I

M

M

T

T

G

G

K

K

T

T

F

F

G

D

G

G

Q

R

K

K

A

A

E

E

M

M

G

G

L

L

V

V

N

N

E

D

S

S

V

V

P

P

L

L

A

A

Q

E

L

L

R

R

E

E

V

T

T

T

I

R

E

E

L

L

A

A

R

L

N

N

L

L

E

E

K

K

N

N

P

P

V

V

L

L

R

R

A

A

K

K

H

N

G

G

F

F

K

K

R

R

C

C

R

R

E

E

L

L

T

T

W

W

E

E

Q

Q

N

N

E

E

D

D

Y

Y

L

L

Y
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Y

A

A

K

K

L

L

D

D

Q

Q

S

S

R

R

L

L

D
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D

T

T

active site: M69 (= M70), Y74 (= Y75), R86 (= R92), Q90 (= Q96), G114 (= G120), S117 (= S123), S136 (= S142), E137 (= E143), I142 (= I148), P144 (= P150), G145 (= G151), Y233 (= Y239), D243 (= D249)
binding coenzyme a: K28 (= K29), R29 (= R30), A31 (= A32), A67 (= A68), M69 (= M70), D70 (= D71), L71 (= L72), G113 (= G119)

6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
66% identity, 87% coverage: 9:249/276 of query aligns to 6:246/246 of 6p5uE

query
sites
6p5uE

T

T

V

V

K

K

V

V

E

Q

I

F

E

D

E

E

G

G

I

I

A

A

W

W

V

V

I

S

L

L

N

N

R

R

P

P

E
x
D

K
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K

R
|
R

N

N

A
|
A

M

M

S

S

P

P

T

T

L

L

N

N

R

R

E

E

M

M

I

L

D

Q

V

V

L

L

E

E

T

A

L

L

E

E

Q

F

D

D

P

D

D

R

A

C

G

G

V

V

L

V

V

V

L

L

T

T

G

G

A

E

G

G

E

D

A

S

W

F

T

S

A
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A

G

G

M
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M

D
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D

L
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L

K

K

E

E

Y
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Y

F

F

R

R

E

E

V

T

D
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D

A

N

G

A

P

P

E

A

I

L

L

I

Q

K

E

A

K

Q

I

I

R

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R
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R

E

A

A

A

S

G

Q
x
A

W

W

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Q

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W

K

R

L

K

L

L

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R

M

F

Y

Y

A

A

K

K

P

P

T

T

I

I

A

A

M

M

V

V

N

N

G

G

W
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W

C

C

F
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F

G

G

G
|
G

G

A

F

F

S
x
T

P

P

L

L

V

I

A

A

C

C

D

D

L

L

A

A

I

V

C

A

A

A

D

D

E

E

A

A

T

T

F

F

G

G

L

L

S
|
S

E
|
E

I

I

N

N

W
|
W

G

G

I
|
I

P

I

P
|
P

G
x
A

N

G

L

N

V

V

S

T

K

K

A

A

M

V

A

S

D

Q

T

V

V

C

G

G

H

E

R

R

Q

A

S

A

L

L

Y

Y

I

I

M

M

T

S

G

G

K

E

T

P

F

F

G

G

Q

Q

K

K

A

A

A

R

E

E

M

I

G

G

L

L

V

V

N

N

E

E

S

S

V

V

P

P

L

L

A

A

Q

A

L

L

R

R

E

E

V

R

T

T

I

R

E

E

L

L

A

A

R

K

N

T

L

L

E

G

K

K

N

N

P

P

V

T

V

V

L

L

R

R

A

Q

A

A

K

K

H

H

G

A

F

L

K

R

R

R

C

V

R

E

E

P

L

M

T

D

W

W

E

D

Q

L

N

S

E

E

D

E

Y

Y

L

L

Y
x
A

A

A

K

K

L

A

D

E

Q

Q

S

T

R

A

L

A

L

I

D
|
D

active site: M67 (= M70), Y72 (= Y75), D77 (= D80), R89 (= R92), A93 (≠ Q96), G117 (= G120), T120 (≠ S123), E140 (= E143), I145 (= I148), P147 (= P150), A148 (≠ G151), A236 (≠ Y239), D246 (= D249)
binding coenzyme a: D25 (≠ E28), K26 (= K29), R27 (= R30), A29 (= A32), A65 (= A68), M67 (= M70), D68 (= D71), L69 (= L72), W113 (= W116), F115 (= F118), S139 (= S142), W143 (= W146)

7xwtB Crystal structure of feruoyl-coa hydratase/lyase complexed with coa from sphingomonas paucimobilis (see paper)
51% identity, 97% coverage: 10:276/276 of query aligns to 7:272/277 of 7xwtB

query
sites
7xwtB

T

T

V

V

K

R

V

Y

E

E

I

I

E

V

E

N

G

N

I

V

A

A

W

W

V

V

I

Y

L

Y

N

N

R

R

P

P

E
x
T

K
|
K

R
|
R

N

N

A
|
A

M

Q

S

S

P

P

T

K

L

L

N

N

R

R

E

Q

M

M

I

L

D

K

V

V

L

L

E

T

T

E

L

L

E

E

Q

F

D

R

P

D

D

D

A

V

G

G

V

V

L

L

V

V

L

L

T

G

G

G

A

E

G

G

E

P

A

A

W

W

T

C

A
|
A

G
|
G

M
|
M

D
|
D

L
|
L

K

K

E

E

Y

Y

F
|
F

R

R

E

E

V

T

D

E

A

A

G

E

P

G

E

L

I

A

L

G

Q

T

E

R

K

K

I

A

R

Q

R

R

E

E

A

A

S

Y

Q

T

W

W

Q

-

W

W

K

E

L

R

L

L

R

R

M

W

Y

Y

A

Q

K

K

P

P

T

T

I

I

A

A

M

M

V

V

N

H

G

G

W

W

C

C

F
|
F

G

G

G
|
G

G

A

F

Y

S

G

P

P

L

L

V

F

A

A

C

C

D

D

L

L

A

A

I

F

C

A

A

A

D

D

E

E

A

A

T

Q

F

F

G

G

L

L

S
|
S

E

E

I

V

N

N

W
|
W

G

G

I

I

P

L

P

P

G

G

N

G

L

G

V

A

S

T

K

K

A

V

M

A

A

V

D

D

T

L

V

M

G

P

H

M

R

R

Q

V

S

A

L

M

Y

Y

Y

H

I

A

M

M

T

M

G

G

K

E

T

N

F

L

G

S

G

G

Q

Q

K

D

A

A

E

R

M

Y

G

N

L

L

V

V

N

N

E

E

S

S

V

M

P

P

L

A

A

D

Q

Q

L

L

R

K

E

A

V

R

T

V

I

K

E

Q

L

V

A

A

R

E

N

T

L

L

L

I

E

Q

K

K

N

N

P

W

V

A

V

T

L

V

R

K

A

Y

A

T

K

K

H

D

G

A

F

V

K

R

R

R

C

V

R

K

E

E

L

M

T

T

W

Y

E

D

Q

N

N

A

E

E

D

D

Y

Y

L

L

Y

I

A

R

K

L

L

Q

D

E

Q

G

S

L

R

N

L

W

L

F

D

D

T

K

E

S

G

D

G

G

R

R

E

H

Q

V

G

A

M

M

K

K

Q

Q

F

F

L

L

D

D

K

K

S

T

I

F

K

K

P

P

G

G

L

L

Q

G

A

H

Y

Y

K

D

R

K

binding acetyl coenzyme *a: T25 (≠ E28), K26 (= K29), R27 (= R30), A29 (= A32), A65 (= A68), G66 (= G69), M67 (= M70), D68 (= D71), L69 (= L72), F73 (= F76), F114 (= F118), G116 (= G120), S138 (= S142), W142 (= W146)

7xwvA Feruloyl-coa hydratase/lyase complexed with vanillin and coenzyme a (see paper)
52% identity, 83% coverage: 10:238/276 of query aligns to 6:233/244 of 7xwvA

query
sites
7xwvA

T

T

V

V

K

R

V

Y

E

E

I

I

E

V

E

N

G

N

I

V

A

A

W

W

V

V

I

Y

L

Y

N

N

R

R

P

P

E
x
T

K
|
K

R
|
R

N

N

A

A

M

Q

S

S

P

P

T

K

L

L

N

N

R

R

E

Q

M

M

I

L

D

K

V

V

L

L

E

T

T

E

L

L

E

E

Q

F

D

R

P

D

D

D

A

V

G

G

V

V

L

L

V

V

L

L

T

G

G

G

A

E

G

G

E

P

A

A

W

W

T

C

A
|
A

G
|
G

M
|
M

D
|
D

L
|
L

K

K

E

E

Y
|
Y

F
|
F

R

R

E

E

V

T

D

E

A

A

G

E

P

G

E

L

I

A

L

G

Q

T

E

R

K

K

I

A

R

Q

R

R

E

E

A

A

S

Y

Q

T

W

W

Q

-

W

W

K

E

L

R

L

L

R

R

M

W

Y

Y

A

Q

K

K

P

P

T

T

I

I

A

A

M

M

V

V

N

H

G

G

W
|
W

C

C

F
|
F

G
|
G

G

A

F

Y

S

G

P

P

L

L

V

F

A

A

C

C

D

D

L

L

A

A

I

F

C

A

A

A

D

D

E

E

A

A

T

Q

F

F

G

G

L

L

S
|
S

E
|
E

I

V

N

N

W

W

G

G

I

I

P

L

P

P

G
|
G

N
x
G

L

G

V

A

S

T

K

K

A

V

M

A

A

V

D

D

T

L

V

M

G

P

H

M

R

R

Q

V

S

A

L

M

Y

Y

Y

H

I

A

M

M

T

M

G

G

K

E

T

N

F

L

G

S

G

G

Q

Q

K

D

A

A

E

R

M

Y

G

N

L

L

V

V

N

N

E

E

S

S

V

M

P

P

L

A

A

D

Q

Q

L

L

R

K

E

A

V

R

T

V

I

K

E

Q

L

V

A

A

R

E

N

T

L

L

L

I

E

Q

K

K

N

N

P

W

V

A

V

T

L

V

R

K

A

Y

A

T

K

K

H

D

G

A

F

V

K

R

R

R

C

V

R

K

E

E

L

M

T

T

W

Y

E

D

Q

N

N

A

E

E

D

D

Y

Y

L

L

binding coenzyme a: T24 (≠ E28), K25 (= K29), R26 (= R30), A64 (= A68), G65 (= G69), M66 (= M70), D67 (= D71), L68 (= L72), W111 (= W116), F113 (= F118), G114 (= G119), G115 (= G120), S137 (= S142)
binding 4-hydroxy-3-methoxybenzaldehyde: M66 (= M70), Y71 (= Y75), F72 (= F76), E138 (= E143), G146 (= G151), G147 (≠ N152)

5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
35% identity, 79% coverage: 8:225/276 of query aligns to 3:215/259 of 5zaiC

query
sites
5zaiC

W

F

T

E

T

T

V

I

K

E

V

T

E

K

I

K

E

E

E

G

G

N

I

L

A

F

W

W

V

I

I

T

L

L

N

N

R

R

P

P

E

D

K
|
K

R
x
L

N

N

A

A

M

L

S

N

P

A

T

K

L

L

N

L

R

E

E

E

M

L

I

D

D

R

V

A

L

V

E

S

T

Q

L

A

E

E

Q

S

D

D

P

P

D

E

A

I

G

R

V

V

L

I

V

I

L

I

T

T

G

G

A

K

G

G

E

K

A

A

W

F

T

C

A
|
A

G
|
G

M
x
A

D
|
D

L
x
I

K

T

E

Q

Y
x
F

F

N

R

Q

E

L

V

T

D

P

A

A

G

E

P

A

E

W

I

K

L

F

Q
x
S

E

K

K

K

I

G

R
|
R

R

E

E

I

A

M

S

D

Q

K

W

-

Q

-

W

-

K

-

L

-

L

I

R

E

M

A

Y

L

A

S

K

K

P

P

T

T

I

I

A

A

M

M

V

I

N

N

G

G

W

Y

C

A

F

L

G

G

G
|
G

G

G

F

L

S
x
E

P

L

L

A

V

L

A

A

C

C

D

D

L

I

A

R

I

I

C

A

A

A

D

E

E

E

A

A

T

Q

F

L

G

G

L

L

S
x
P

E
|
E

I

I

N

N

W

L

G

G

I
|
I

P

Y

P
|
P

G
|
G

N

Y

L

G

V

G

S

T

K

Q

A

R

M

L

A

T

D

R

T

V

V

I

G

G

H

K

R

G

Q

R

S

A

L

L

Y

E

Y

M

I

M

M

M

T

T

G

G

K

D

T
x
R

F

I

G

P

G

G

Q

K

K

D

A

A

A

E

E

K

M

Y

G

G

L

L

V

V

N

N

E

R

S

V

V

V

P

P

L

L

A

A

Q

N

L

L

R

E

E

Q

V

E

T

T

I

R

E

K

L

L

A

A

R

E

N

K

L

I

L

A

E

K

K

K

N

S

P

P

V

I

V

S

L

L

R

A

A

L

A

I

K

K

H

E

G

V

F

V

K

N

R

R

active site: A65 (≠ M70), F70 (≠ Y75), S82 (≠ Q87), R86 (= R91), G110 (= G120), E113 (≠ S123), P132 (≠ S142), E133 (= E143), I138 (= I148), P140 (= P150), G141 (= G151)
binding coenzyme a: K24 (= K29), L25 (≠ R30), A63 (= A68), G64 (= G69), A65 (≠ M70), D66 (= D71), I67 (≠ L72), P132 (≠ S142), R166 (≠ T176)

Sites not aligning to the query:

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

Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
36% identity, 77% coverage: 8:220/276 of query aligns to 12:221/273 of Q5HH38

query
sites
Q5HH38

W

Y

T

D

T

E

V

I

K

K

V

Y

E

E

I

F

E

Y

E

E

G

G

I

I

A

A

W

K

V

V

I

T

L

I

N

N

R

R

P

P

E

E

K

V

R
|
R

N

N

A

A

M

F

S

T

P

P

T

K

L

T

N

V

R

A

E

E

M

M

I

I

D

D

V

A

L

F

E

S

T

R

L

A

E

R

Q

D

D

D

P

Q

D

N

A

V

G

S

V

V

L

I

V

V

L

L

T

T

G

G

A

E

G

G

E

D

-

L

A

A

W

F

T

C

A
x
S

G
|
G

M
x
G

D
|
D

L
x
Q

K

K

E

K

Y

R

F

G

R

H

E

-

V

-

D

-

A

-

G

G

P

G

E

Y

I

V

L

G

Q

E

E

D

K

Q

I

I

R

P

R

R

E

L

A

N

S

V

Q

L

W

D

Q

L

W

Q

K

R

L

L

L

I

R

R

M

I

Y

I

A

P

K

K

P

P

T

V

I

I

A

A

M

M

V

V

N

K

G

G

W

Y

C

A

F

V

G

G

F

N

S

V

P

L

L

N

V

V

A

V

C

C

D

D

L

L

A

T

I

I

C

A

A

A

D

D

E

N

A

A

T

I

F

F

G

G

L

Q

S

T

E

G

I

P

N

K

W

V

G

G

I
x
S

P

F

P

D

G

A

N

G

L

Y

V

G

S

S

K

G

A

Y

M

L

A

A

D

R

T

I

V

V

G

G

H

H

R

K

Q

K

S

A

L

R

Y

E

Y

I

I

W

M

Y

T

L

G

C

K

R

T

Q

F

Y

G

N

G

A

Q

Q

K

E

A

A

A

L

E

D

M

M

G

G

L

L

V

V

N

N

E

T

S

V

V

V

P

P

L

L

A

E

Q

K

L

V

R

E

E

D

V

E

T

T

I

V

E

Q

L

W

A

C

R

K

N

E

L

I

L

M

E

K

K

H

N

S

P

P

V

T

V

A

L

L

R

R

A

F

A

L

K

K

R34 (= R30) binding in other chain
SGGDQ 73:77 (≠ AGMDL 68:72) binding in other chain
S149 (≠ I148) binding in other chain

2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
35% identity, 77% coverage: 8:220/276 of query aligns to 7:208/260 of 2uzfA

query
sites
2uzfA

W

Y

T

D

T

E

V

I

K

K

V

Y

E

E

I

F

E

Y

E

E

G

G

I

I

A

A

W

K

V

V

I

T

L

I

N

N

R

R

P

P

E

E

K
x
V

R
|
R

N

N

A

A

M

F

S

T

P

P

T

K

L

T

N

V

R

A

E

E

M

M

I

I

D

D

V

A

L

F

E

S

T

R

L

A

E

R

Q

D

D

D

P

Q

D

N

A

V

G

S

V

V

L

I

V

V

L

L

T

T

G

G

A

E

G

G

E

D

-

L

A

A

W

F

T

C

A
x
S

G
|
G

M
x
G

D
|
D

L

Q

K

K

E

G

Y

-

F

-

R

-

E

-

V

-

D

-

A

-

G

-

P

-

E

-

I

-

L

-

Q

E

E

D

K

Q

I

I

R

P

R
|
R

E

L

A

N

S

V

Q
x
L

W

D

Q

L

W

Q

K

R

L

L

L

I

R

R

M

I

Y

I

A

P

K

K

P

P

T

V

I

I

A

A

M

M

V

V

N

K

G

G

W
x
Y

C

A

F

V

G

G

G
|
G

G

G

F

N

S
x
V

P

L

L

N

V

V

A

V

C

C

D

D

L

L

A

T

I

I

C

A

A

A

D

D

E

N

A

A

T

I

F

F

G

G

L

Q

S
x
T

E
x
G

I

P

N

K

W

V

G

G

I
x
S

P

F

P
x
D

G
x
A

N

G

L

Y

V

G

S

S

K

G

A

Y

M

L

A

A

D

R

T

I

V

V

G

G

H

H

R

K

Q

K

S

A

L

R

Y

E

Y

I

I

W

M

Y

T

L

G

C

K

R

T

Q

F

Y

G

N

G

A

Q

Q

K

E

A

A

A

L

E

D

M

M

G

G

L

L

V

V

N

N

E

T

S

V

V

V

P

P

L

L

A

E

Q

K

L

V

R

E

E

D

V

E

T

T

I

V

E

Q

L

W

A

C

R

K

N

E

L

I

L

M

E

K

K

H

N

S

P

P

V

T

V

A

L

L

R

R

A

F

A

L

K

K

active site: G70 (≠ M70), R80 (= R92), L84 (≠ Q96), G108 (= G120), V111 (≠ S123), T130 (≠ S142), G131 (≠ E143), S136 (≠ I148), D138 (≠ P150), A139 (≠ G151)
binding acetoacetyl-coenzyme a: V28 (≠ K29), R29 (= R30), S68 (≠ A68), G69 (= G69), G70 (≠ M70), D71 (= D71), Y104 (≠ W116), G108 (= G120)

Sites not aligning to the query:

active site: 225, 233

4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
35% identity, 74% coverage: 17:220/276 of query aligns to 29:216/268 of 4elxA

query
sites
4elxA

E

D

G

G

I

I

A

A

W

K

V

I

I

T

L

I

N

N

R

R

P

P

E

Q

K

V

R

R

N

N

A

A

M

F

S

R

P

P

T

L

L

T

N

V

R

K

E

E

M

M

I

I

D

Q

V

A

L

L

E

A

T

D

L

A

E

R

Q

Y

D

D

P

D

D

N

A

I

G

G

V

V

L

I

V

I

L

L

T

T

G

G

A

A

G

G

E

D

-

K

A

A

W

F

T

C

A

S

G

G

M
x
G

D

D

L

Q

K

K

E

H

Y
x
H

F

L

R

N

E

V

V
x
L

D

D

A

-

G

-

P

-

E

-

I

-

L

F

Q

Q

E

R

K

Q

I

I

R

R

R

-

E

-

A

-

S

-

Q

-

W

-

Q

-

W

-

K

-

L

-

R

-

M

T

Y

C

A

P

K

K

P

P

T

V

I

V

A

A

M

M

V

V

N

A

G

G

W

Y

C

S

F

I

G
|
G

G

G

F

H

S
x
V

P

L

L

H

V

M

A

M

C

C

D

D

L

L

A

T

I

I

C

A

A

A

D

D

E

N

A

A

T

I

F

F

G

G

L

Q

S

T

E
x
G

I

P

N

K

W

V

G

G

I
x
S

P

F

P
x
D

G
|
G

N

G

L

W

V

G

S

A

K

S

A

Y

M

M

A

A

D

R

T

I

V

V

G

G

H

Q

R

K

Q

K

S

A

L

R

Y

E

Y

I

I
x
W

M

F

T

L

G

C

K

R

T

Q

F

Y

G

D

G

A

Q

K

K

Q

A

A

A

L

E

D

M

M

G

G

L

L

V

V

N

N

E

T

S

V

V

V

P

P

L

L

A

A

Q

D

L

L

R

E

E

K

V

E

T

T

I

V

E

R

L

W

A

C

R

R

N

E

L

M

L

L

E

Q

K

N

N

S

P

P

V

M

V

A

L

L

R

R

A

C

A

L

K

K

active site: G83 (≠ M70), H88 (≠ Y75), L92 (≠ V79), G116 (= G120), V119 (≠ S123), G139 (≠ E143), S144 (≠ I148), D146 (≠ P150), G147 (= G151)
binding chloride ion: G115 (= G119), G139 (≠ E143), W167 (≠ I171)

Sites not aligning to the query:

active site: 233, 241

3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 94% coverage: 8:266/276 of query aligns to 2:246/250 of 3q0gD

query
sites
3q0gD

W

Y

T

E

T

T

V

I

K

L

V

V

E

E

I

R

E

D

E

Q

G

R

I

V

A

G

W

I

V

I

I

T

L

L

N

N

R

R

P

P

E

Q

K

A

R

L

N

N

A

A

M

L

S

N

P

S

T

Q

L

V

N

M

R

N

E

E

M

V

I

T

D

S

V

A

L

A

E

T

T

E

L

L

E

D

Q

D

D

D

P

P

D

D

A

I

G

G

V

A

L

I

V

I

L

I

T

T

G

G

A

S

G

A

E

K

A

A

W

F

T

A

A

A

G

G

M
x
A

D

D

L

I

K

K

E

E

Y
x
M

F

F

R

A

E

D

V

A

D

F

A
x
T

G

A

P

D

E

F

I
x
F

L

-

Q

-

E

-

K

-

I

-

R

-

E

-

A

-

S

-

Q

-

W

A

Q

T

W

W

K

G

L

K

L

L

R

A

M

A

Y

V

A

R

K

T

P

P

T

T

I

I

A

A

M

A

V

V

N

A

G

G

W

Y

C

A

F

L

G

G

G
|
G

G

G

F

C

S
x
E

P

L

L

A

V

M

A

M

C

C

D

D

L

V

A

L

I

I

C

A

A

A

D

D

E

T

A

A

T

K

F

F

G

G

L

Q

S
x
P

E
|
E

I

I

N

K

W

L

G

G

I
x
V

P

L

P
|
P

G
|
G

N

M

L

G

V

G

S

S

K

Q

A

R

M

L

A

T

D

R

T

A

V

I

G

G

H

K

R

A

Q

K

S

A

L

M

Y

D

Y

L

I

I

M

L

T

T

G

G

K

R

T

T

F

M

G

D

G

A

Q

A

K

E

A

A

A

E

E

R

M

S

G

G

L

L

V

V

N

S

E

R

S

V

V

V

P

P

L

A

A

D

Q

D

L

L

R

L

E

T

V

E

T

A

I

R

E

A

L

T

A

A

R

T

N

T

L

I

L

S

E

Q

K

M

N

S

P

A

V

S

V

A

L

A

R

R

A

M

A

A

K

K

H

E

G

A

F

V

K

N

R

R

C

A

R

F

E

E

L

S

T

S

W

L

E

-

Q

-

N

S

E

E

D

G

Y

L

L
|
L

Y

Y

A

E

K

R

L

R

D

L

Q
x
F

S

H

R

S

L

A

L
x
F

D

A

T

T

E

E

G

-

G

D

R

Q

E

S

Q

E

G

G

M

M

K

A

Q

A

F
|
F

L

I

D

E

D

K

K

R

S

A

active site: A64 (≠ M70), M69 (≠ Y75), T75 (≠ A81), F79 (≠ I85), G103 (= G120), E106 (≠ S123), P125 (≠ S142), E126 (= E143), V131 (≠ I148), P133 (= P150), G134 (= G151), L219 (= L238), F229 (≠ L248)
binding Butyryl Coenzyme A: F225 (≠ Q244), F241 (= F261)

2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
30% identity, 89% coverage: 19:265/276 of query aligns to 16:247/254 of 2dubA

query
sites
2dubA

I

V

A

G

W

L

V

I

I

Q

L

L

N

N

R

R

P

P

E
x
K

K
x
A

R
x
L

N

N

A
|
A

M

L

S

C

P

N

T

G

L

L

N

I

R

E

E

E

M

L

I

N

D

Q

V

A

L

L

E

E

T

T

L

F

E

E

Q

E

D

D

P

P

D

A

A

V

G

G

V

A

L

I

V

V

L

L

T

T

G

G

A

G

G

E

E

K

A

A

W

F

T

A

A
|
A

G

G

M
x
A

D
|
D

L
x
I

K
|
K

E

E

Y

-

F

-

R

-

E

-

V

-

D

-

A

-

G

-

P

-

E

-

I

-

L
x
M

Q

Q

E

N

K

R

I

T

R

F

R

Q

E

D

A

C

S

Y

Q
x
S

W

-

Q

H

W

W

K

D

L

H

L

I

R

T

M

R

Y

I

A

K

K

K

P

P

T

V

I

I

A

A

M

A

V

V

N

N

G

G

W

Y

C

A

F

L

G

G

G
|
G

G

G

F

C

S
x
E

P

L

L

A

V

M

A

M

C

C

D

D

L

I

A

I

I

Y

C

A

A

G

D

E

E

K

A

A

T

Q

F

F

G

G

L

Q

S
x
P

E
|
E

I

I

N

L

W

L

G

G

I
x
T

P

I

P
|
P

G
|
G

N
x
A

L

G

V

G

S

T

K

Q

A

R

M

L

A

T

D

R

T

A

V

V

G

G

H

K

R

S

Q

L

S

A

L

M

Y

E

Y

M

I

V

M

L

T

T

G

G

K

D

T

R

F

I

G

S

G

A

Q

Q

K

D

A

A

A

K

E

Q

M

A

G

G

L

L

V

V

N

S

E

K

S

I

V

F

P

P

L

V

A

E

Q

T

L

L

R

V

E

E

V

E

T

A

I

I

E

Q

L

C

A

A

R

E

N

K

L

I

L

A

E

N

K

N

N

S

P

K

V

I

L

V

R

A

A

M

A

A

K

K

H

E

G

S

F

V

K

N

R

A

C

A

R

F

E

E

L

M

T

T

W

L

E

T

Q

E

N

G

E

-

D

N

Y
x
K

L

L

Y

E

A

K

K

K

L

L

D

F

Q

Y

S

S

R

T

L
x
F

L

A

D

T

T

D

E

D

G

-

R

R

E

R

Q

E

G

G

M

M

K

S

Q

A

F

F

L

V

D

E

D

K

K

R

active site: A67 (≠ M70), M72 (≠ L86), S82 (≠ Q96), G105 (= G120), E108 (≠ S123), P127 (≠ S142), E128 (= E143), T133 (≠ I148), P135 (= P150), G136 (= G151), K221 (≠ Y237), F231 (≠ L247)
binding octanoyl-coenzyme a: K25 (≠ E28), A26 (≠ K29), L27 (≠ R30), A29 (= A32), A65 (= A68), A67 (≠ M70), D68 (= D71), I69 (≠ L72), K70 (= K73), G105 (= G120), E108 (≠ S123), P127 (≠ S142), E128 (= E143), G136 (= G151), A137 (≠ N152)

1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
29% identity, 89% coverage: 19:265/276 of query aligns to 17:253/260 of 1dubA

query
sites
1dubA

I

V

A

G

W

L

V

I

I

Q

L

L

N

N

R

R

P

P

E
x
K

K
x
A

R
x
L

N

N

A
|
A

M

L

S

C

P

N

T

G

L

L

N

I

R

E

E

E

M

L

I

N

D

Q

V

A

L

L

E

E

T

T

L

F

E

E

Q

E

D

D

P

P

D

A

A

V

G

G

V

A

L

I

V

V

L

L

T

T

G

G

A

G

G

E

E

K

A

A

W

F

T

A

A
|
A

G

G

M
x
A

D
|
D

L
x
I

K

K

E

E

Y
x
M

-

Q

-

N

-

R

-

T

F

F

R

Q

E

D

V

C

D

Y

A
x
S

G

G

P

K

E

F

I
x
L

L

-

Q

-

E

-

K

-

I

-

R

-

E

-

A

-

S

-

Q

-

W

S

Q

H

W

W

K

D

L

H

L

I

R

T

M

R

Y

I

A

K

K

K

P

P

T

V

I

I

A

A

M

A

V

V

N

N

G

G

W
x
Y

C

A

F

L

G
|
G

G

G

F

C

S
x
E

P

L

L

A

V

M

A

M

C

C

D

D

L

I

A

I

I

Y

C

A

A

G

D

E

E

K

A

A

T

Q

F

F

G

G

L

Q

S
x
P

E
|
E

I

I

N

L

W
x
L

G

G

I
x
T

P

I

P
|
P

G
|
G

N

A

L

G

V

G

S

T

K

Q

A

R

M

L

A

T

D

R

T

A

V

V

G

G

H

K

R

S

Q

L

S

A

L

M

Y

E

Y

M

I

V

M

L

T

T

G

G

K

D

T

R

F

I

G

S

G

A

Q

Q

K

D

A

A

A

K

E

Q

M

A

G

G

L

L

V

V

N

S

E

K

S

I

V

F

P

P

L

V

A

E

Q

T

L

L

R

V

E

E

V

E

T

A

I

I

E

Q

L

C

A

A

R

E

N

K

L

I

L

A

E

N

K

N

N

S

P

K

V

I

L

V

R

A

A

M

A

A

K

K

H

E

G

S

F

V

K

N

R

A

C

A

R

F

E

E

L

M

T

T

W

L

E

T

Q

E

N

G

E

-

D

N

Y
x
K

L

L

Y

E

A

K

K

K

L

L

D
x
F

Q

Y

S

S

R

T

L
x
F

L

A

D

T

T

D

E

D

G

-

R

R

E

R

Q

E

G

G

M

M

K

S

Q

A

F
|
F

L

V

D

E

D

K

K

R

active site: A68 (≠ M70), M73 (≠ Y75), S83 (≠ A81), L87 (≠ I85), G111 (= G120), E114 (≠ S123), P133 (≠ S142), E134 (= E143), T139 (≠ I148), P141 (= P150), G142 (= G151), K227 (≠ Y237), F237 (≠ L247)
binding acetoacetyl-coenzyme a: K26 (≠ E28), A27 (≠ K29), L28 (≠ R30), A30 (= A32), A66 (= A68), A68 (≠ M70), D69 (= D71), I70 (≠ L72), Y107 (≠ W116), G110 (= G119), G111 (= G120), E114 (≠ S123), P133 (≠ S142), E134 (= E143), L137 (≠ W146), G142 (= G151), F233 (≠ D243), F249 (= F261)

1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
29% identity, 89% coverage: 19:265/276 of query aligns to 15:251/258 of 1ey3A

query
sites
1ey3A

I

V

A

G

W

L

V

I

I

Q

L

L

N

N

R

R

P

P

E
x
K

K

A

R
x
L

N

N

A
|
A

M

L

S

C

P

N

T

G

L

L

N

I

R

E

E

E

M

L

I

N

D

Q

V

A

L

L

E

E

T

T

L

F

E

E

Q

E

D

D

P

P

D

A

A

V

G

G

V

A

L

I

V

V

L

L

T

T

G

G

A

G

G

E

E

K

A

A

W

F

T

A

A
|
A

G
|
G

M
x
A

D
|
D

L
x
I

K

K

E

E

Y
x
M

-

Q

-

N

-

R

-

T

F

F

R

Q

E

D

V

C

D

Y

A
x
S

G

G

P

K

E

F

I
x
L

L

-

Q

-

E

-

K

-

I

-

R

-

E

-

A

-

S

-

Q

-

W

S

Q

H

W
|
W

K

D

L

H

L

I

R

T

M

R

Y

I

A

K

K

K

P

P

T

V

I

I

A

A

M

A

V

V

N

N

G

G

W

Y

C

A

F

L

G

G

G
|
G

G

G

F

C

S
x
E

P

L

L

A

V

M

A

M

C

C

D

D

L

I

A

I

I

Y

C

A

A

G

D

E

E

K

A

A

T

Q

F

F

G

G

L

Q

S
x
P

E
|
E

I

I

N

L

W
x
L

G

G

I
x
T

P

I

P
|
P

G
|
G

N

A

L

G

V

G

S

T

K

Q

A

R

M

L

A

T

D

R

T

A

V

V

G

G

H

K

R

S

Q

L

S

A

L

M

Y

E

Y

M

I

V

M

L

T

T

G

G

K

D

T

R

F

I

G

S

G

A

Q

Q

K

D

A

A

A

K

E

Q

M

A

G

G

L

L

V

V

N

S

E

K

S

I

V

F

P

P

L

V

A

E

Q

T

L

L

R

V

E

E

V

E

T

A

I

I

E

Q

L

C

A

A

R

E

N

K

L

I

L

A

E

N

K

N

N

S

P

K

V

I

L

V

R

A

A

M

A

A

K

K

H

E

G

S

F

V

K

N

R

A

C

A

R

F

E

E

L

M

T

T

W

L

E

T

Q

E

N

G

E

-

D

N

Y
x
K

L

L

Y

E

A

K

K

K

L

L

D

F

Q

Y

S

S

R

T

L
x
F

L

A

D

T

T

D

E

D

G

-

R

R

E

R

Q

E

G

G

M

M

K

S

Q

A

F

F

L

V

D

E

D

K

K

R

active site: A66 (≠ M70), M71 (≠ Y75), S81 (≠ A81), L85 (≠ I85), G109 (= G120), E112 (≠ S123), P131 (≠ S142), E132 (= E143), T137 (≠ I148), P139 (= P150), G140 (= G151), K225 (≠ Y237), F235 (≠ L247)
binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E28), L26 (≠ R30), A28 (= A32), A64 (= A68), G65 (= G69), A66 (≠ M70), D67 (= D71), I68 (≠ L72), L85 (≠ I85), W88 (= W99), G109 (= G120), P131 (≠ S142), L135 (≠ W146), G140 (= G151)

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)
29% identity, 89% coverage: 19:265/276 of query aligns to 47:283/290 of P14604

query
sites
P14604

I

V

A

G

W

L

V

I

I

Q

L

L

N

N

R

R

P

P

E

K

K

A

R

L

N

N

A

A

M

L

S

C

P

N

T

G

L

L

N

I

R

E

E

E

M

L

I

N

D

Q

V

A

L

L

E

E

T

T

L

F

E

E

Q

E

D

D

P

P

D

A

A

V

G

G

V

A

L

I

V

V

L

L

T

T

G

G

A

G

G

E

E

K

A

A

W

F

T

A

A

A

G

G

M

A

D

D

L

I

K

K

E

E

Y

M

-

Q

-

N

-

R

-

T

F

F

R

Q

E

D

V

C

D

Y

A

S

G

G

P

K

E

F

I

L

L

-

Q

-

E

-

K

-

I

-

R

-

E

-

A

-

S

-

Q

-

W

S

Q

H

W

W

K

D

L

H

L

I

R

T

M

R

Y

I

A

K

K

K

P

P

T

V

I

I

A

A

M

A

V

V

N

N

G

G

W

Y

C

A

F

L

G

G

F

C

S
x
E

P

L

L

A

V

M

A

M

C

C

D

D

L

I

A

I

I

Y

C

A

A

G

D

E

E

K

A

A

T

Q

F

F

G

G

L

Q

S

P

E
|
E

I

I

N

L

W

L

G

G

I

T

P

I

P

P

G

G

N

A

L

G

V

G

S

T

K

Q

A

R

M

L

A

T

D

R

T

A

V

V

G

G

H

K

R

S

Q

L

S

A

L

M

Y

E

Y

M

I

V

M

L

T

T

G

G

K

D

T

R

F

I

G

S

G

A

Q

Q

K

D

A

A

A

K

E

Q

M

A

G

G

L

L

V

V

N

S

E

K

S

I

V

F

P

P

L

V

A

E

Q

T

L

L

R

V

E

E

V

E

T

A

I

I

E

Q

L

C

A

A

R

E

N

K

L

I

L

A

E

N

K

N

N

S

P

K

V

I

L

V

R

A

A

M

A

A

K

K

H

E

G

S

F

V

K

N

R

A

C

A

R

F

E

E

L

M

T

T

W

L

E

T

Q

E

N

G

E

-

D

N

Y

K

L

L

Y

E

A

K

K

K

L

L

D

F

Q

Y

S

S

R

T

L

F

L

A

D

T

T

D

E

D

G

-

R

R

E

R

Q

E

G

G

M

M

K

S

Q

A

F

F

L

V

D

E

D

K

K

R

E144 (≠ S123) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
E164 (= E143) 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)
29% identity, 89% coverage: 19:265/276 of query aligns to 17:251/258 of 1mj3A

query
sites
1mj3A

I

V

A

G

W

L

V

I

I

Q

L

L

N

N

R

R

P

P

E
x
K

K
x
A

R
x
L

N

N

A
|
A

M

L

S

C

P

N

T

G

L

L

N

I

R

E

E

E

M

L

I

N

D

Q

V

A

L

L

E

E

T

T

L

F

E

E

Q

E

D

D

P

P

D

A

A

V

G

G

V

A

L

I

V

V

L

L

T

T

G

G

A

G

G

E

E

K

A

A

W

F

T

A

A
|
A

G
|
G

M
x
A

D
|
D

L
x
I

K

K

E

E

Y
x
M

-

Q

-

N

-

R

-

T

F

F

R

Q

E

D

V

C

D

Y

A
x
S

G

G

P
x
L

E

S

I

-

L

-

Q

-

E

-

K

-

I

-

R

-

E

-

A

-

S

-

Q

-

W

-

Q

H

W

W

K

D

L

H

L

I

R

T

M

R

Y

I

A

K

K

K

P

P

T

V

I

I

A

A

M

A

V

V

N

N

G

G

W

Y

C

A

F

L

G

G

G
|
G

G

G

F

C

S
x
E

P

L

L

A

V

M

A

M

C

C

D

D

L

I

A

I

I

Y

C

A

A

G

D

E

E

K

A

A

T

Q

F

F

G

G

L

Q

S
x
P

E
|
E

I

I

N

L

W
x
L

G

G

I
x
T

P

I

P
|
P

G
|
G

N

A

L

G

V

G

S

T

K

Q

A

R

M

L

A

T

D

R

T

A

V

V

G

G

H

K

R

S

Q

L

S

A

L

M

Y

E

Y

M

I

V

M

L

T

T

G

G

K

D

T

R

F

I

G

S

G

A

Q

Q

K

D

A

A

A

K

E

Q

M

A

G

G

L

L

V

V

N

S

E

K

S

I

V

F

P

P

L

V

A

E

Q

T

L

L

R

V

E

E

V

E

T

A

I

I

E

Q

L

C

A

A

R

E

N

K

L

I

L

A

E

N

K

N

N

S

P

K

V

I

L

V

R

A

A

M

A

A

K

K

H

E

G

S

F

V

K

N

R

A

C

A

R

F

E

E

L

M

T

T

W

L

E

T

Q

E

N

G

E

-

D

N

Y
x
K

L

L

Y

E

A

K

K

K

L

L

D

F

Q

Y

S

S

R

T

L
x
F

L

A

D

T

T

D

E

D

G

-

R

R

E

R

Q

E

G

G

M

M

K

S

Q

A

F

F

L

V

D

E

D

K

K

R

active site: A68 (≠ M70), M73 (≠ Y75), S83 (≠ A81), L85 (≠ P83), G109 (= G120), E112 (≠ S123), P131 (≠ S142), E132 (= E143), T137 (≠ I148), P139 (= P150), G140 (= G151), K225 (≠ Y237), F235 (≠ L247)
binding hexanoyl-coenzyme a: K26 (≠ E28), A27 (≠ K29), L28 (≠ R30), A30 (= A32), A66 (= A68), G67 (= G69), A68 (≠ M70), D69 (= D71), I70 (≠ L72), G109 (= G120), P131 (≠ S142), E132 (= E143), L135 (≠ W146), G140 (= G151)

4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
35% identity, 74% coverage: 17:220/276 of query aligns to 29:215/267 of 4elwA

query
sites
4elwA

E

D

G

G

I

I

A

A

W

K

V

I

I

T

L

I

N

N

R

R

P

P

E

Q

K

V

R

R

N

N

A

A

M

F

S

R

P

P

T

L

L

T

N

V

R

K

E

E

M

M

I

I

D

Q

V

A

L

L

E

A

T

D

L

A

E

R

Q

Y

D

D

P

D

D

N

A

I

G

G

V

V

L

I

V

I

L

L

T

T

G

G

A

A

G

G

E

D

-

K

A

A

W

F

T

C

A

S

G

G

M
x
G

D

D

L

Q

K

K

E

-

Y

H

F

L

R

N

E

V

V
x
L

D

D

A

-

G

-

P

-

E

-

I

-

L

F

Q

Q

E

R

K

Q

I

I

R

R

R

-

E

-

A

-

S

-

Q

-

W

-

Q

-

W

-

K

-

L

-

R

-

M

T

Y

C

A

P

K

K

P

P

T

V

I

V

A

A

M

M

V

V

N

A

G

G

W

Y

C

S

F

I

G
|
G

G

G

F

H

S
x
V

P

L

L

H

V

M

A

M

C

C

D

D

L

L

A

T

I

I

C

A

A

A

D

D

E

N

A

A

T

I

F

F

G

G

L

Q

S
x
T

E
x
G

I

P

N

K

W

V

G

G

I
x
S

P
x
F

P
x
D

G
|
G

N

G

L

W

V

G

S

A

K

S

A

Y

M

M

A

A

D

R

T

I

V

V

G

G

H

Q

R

K

Q

K

S

A

L

R

Y

E

Y

I

I
x
W

M

F

T

L

G

C

K

R

T

Q

F

Y

G

D

G

A

Q

K

K

Q

A

A

A

L

E

D

M

M

G

G

L

L

V

V

N

N

E

T

S

V

V

V

P

P

L

L

A

A

Q

D

L

L

R

E

E

K

V

E

T

T

I

V

E

R

L

W

A

C

R

R

N

E

L

M

L

L

E

Q

K

N

N

S

P

P

V

M

V

A

L

L

R

R

A

C

A

L

K

K

active site: G83 (≠ M70), L91 (≠ V79), G115 (= G120), V118 (≠ S123), G138 (≠ E143), S143 (≠ I148), D145 (≠ P150), G146 (= G151)
binding nitrate ion: G114 (= G119), T137 (≠ S142), G138 (≠ E143), F144 (≠ P149), W166 (≠ I171)

Sites not aligning to the query:

active site: 232, 240

4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
35% identity, 74% coverage: 17:220/276 of query aligns to 32:233/285 of 4i42A

query
sites
4i42A

E

D

G

G

I

I

A

A

W

K

V

I

I

T

L

I

N

N

R

R

P

P

E

Q

K
x
V

R
|
R

N

N

A

A

M

F

S

R

P

P

T

L

L

T

N

V

R

K

E

E

M

M

I

I

D

Q

V

A

L

L

E

A

T

D

L

A

E

R

Q

Y

D

D

P

D

D

N

A

I

G

G

V

V

L

I

V

I

L

L

T

T

G

G

A

A

G

G

E

D

-

K

A

A

W

F

T

C

A
x
S

G
|
G

M
x
G

D
|
D

L
x
Q

K
|
K

E

V

Y

-

F

-

R

-

E
x
R

V

G

D

D

A

Y

G

G

P

G

E
x
Y

I

K

L

D

Q

D

E

S

K

G

I

V

R

H

R
x
H

E

L

A

N

S
x
V

Q
x
L

W

D

Q

F

W

Q

K

R

L

Q

L

I

R

R

M

T

Y

C

A

P

K

K

P

P

T

V

I

V

A

A

M

M

V

V

N

A

G

G

W
x
Y

C

S

F

I

G

G

G
|
G

G

G

F

H

S
x
V

P

L

L

H

V

M

A

M

C

C

D

D

L

L

A

T

I

I

C

A

A

A

D

D

E

N

A

A

T

I

F

F

G

G

L

Q

S
x
T

E
x
G

I

P

N

K

W

V

G

G

I
x
S

P

F

P
x
D

G
|
G

N

G

L

W

V

G

S

A

K

S

A

Y

M

M

A

A

D

R

T

I

V

V

G

G

H

Q

R

K

Q

K

S

A

L

R

Y

E

Y

I

I

W

M

F

T

L

G

C

K

R

T

Q

F

Y

G

D

G

A

Q

K

K

Q

A

A

A

L

E

D

M

M

G

G

L

L

V

V

N

N

E

T

S

V

V

V

P

P

L

L

A

A

Q

D

L

L

R

E

E

K

V

E

T

T

I

V

E

R

L

W

A

C

R

R

N

E

L

M

L

L

E

Q

K

N

N

S

P

P

V

M

V

A

L

L

R

R

A

C

A

L

K

K

active site: G86 (≠ M70), R91 (≠ E78), Y97 (≠ E84), H105 (≠ R92), L109 (≠ Q96), G133 (= G120), V136 (≠ S123), G156 (≠ E143), S161 (≠ I148), D163 (≠ P150), G164 (= G151)
binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ K29), R45 (= R30), S84 (≠ A68), G85 (= G69), G86 (≠ M70), D87 (= D71), Q88 (≠ L72), K89 (= K73), Y97 (≠ E84), V108 (≠ S95), Y129 (≠ W116), G133 (= G120), T155 (≠ S142), S161 (≠ I148)

Sites not aligning to the query:

active site: 250, 258
binding 1-hydroxy-2-naphthoyl-CoA: 254, 270, 273

P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
35% identity, 74% coverage: 17:220/276 of query aligns to 32:233/285 of P0ABU0

query
sites
P0ABU0

E

D

G

G

I

I

A

A

W

K

V

I

I

T

L

I

N

N

R

R

P

P

E

Q

K

V

R
|
R

N

N

A

A

M

F

S

R

P

P

T

L

L

T

N

V

R

K

E

E

M

M

I

I

D

Q

V

A

L

L

E

A

T

D

L

A

E

R

Q

Y

D

D

P

D

D

N

A

I

G

G

V

V

L

I

V

I

L

L

T

T

G

G

A

A

G

G

E

D

-

K

A

A

W

F

T

C

A
x
S

G
|
G

M
x
G

D
|
D

L
x
Q

K
|
K

E

V

Y

-

F

-

R

-

E
x
R

V

G

D

D

A

Y

G

G

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G

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Y

I

K

L

D

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D

E

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R

R

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M

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G

G

W
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Y

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x
S

F
x
I

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|
G

G

G

F

H

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L

L

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M

A

M

C

C

D

D

L

L

A

T

I

I

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A

A

A

D

D

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N

A

A

T

I

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F

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G

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G

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N

K

W

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G

G

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x
S

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F

P

D

G

G

N

G

L

W

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S

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K

S

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Y

M

M

A

A

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R

T

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W

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D

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D

M

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G

G

L

L

V

V

N

N

E

T

S

V

V

V

P

P

L

L

A

A

Q

D

L

L

R

E

E

K

V

E

T

T

I

V

E

R

L

W

A

C

R

R

N

E

L

M

L

L

E

Q

K

N

N

S

P

P

V

M

V

A

L

L

R

R

A

C

A

L

K

K

R45 (= R30) binding in other chain
SGGDQK 84:89 (≠ AGMDLK 68:73) binding in other chain
K89 (= K73) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
R91 (≠ E78) mutation to A: Loss of DHNA-CoA synthase activity.
Y97 (≠ E84) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
YSIGG 129:133 (≠ WCFGG 116:120) binding in other chain
Q154 (≠ L141) 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 (≠ LSE 141:143) binding
T155 (≠ S142) binding in other chain
G156 (≠ E143) mutation to D: Loss of DHNA-CoA synthase activity.
S161 (≠ I148) binding in other chain
W184 (≠ I171) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.

Sites not aligning to the query:

258 binding
267 R→A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
270 F→A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
273 binding ; K→A: Impairs protein folding.

Query Sequence

>Pf1N1B4_5593 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5593
MSNYEGRWTTVKVEIEEGIAWVILNRPEKRNAMSPTLNREMIDVLETLEQDPDAGVLVLT
GAGEAWTAGMDLKEYFREVDAGPEILQEKIRREASQWQWKLLRMYAKPTIAMVNGWCFGG
GFSPLVACDLAICADEATFGLSEINWGIPPGNLVSKAMADTVGHRQSLYYIMTGKTFGGQ
KAAEMGLVNESVPLAQLREVTIELARNLLEKNPVVLRAAKHGFKRCRELTWEQNEDYLYA
KLDQSRLLDTEGGREQGMKQFLDDKSIKPGLQAYKR

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