SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_085125660.1 NCBI__GCF_900177295.1:WP_085125660.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 96% coverage: 10:267/270 of query aligns to 1:249/250 of 3q0gD

query
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3q0gD

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active site: A64 (≠ G74), M69 (≠ F79), T75 (≠ S94), F79 (≠ A98), G103 (= G122), E106 (≠ G125), P125 (≠ T144), E126 (= E145), V131 (≠ L150), P133 (= P152), G134 (≠ A153), L219 (≠ D237), F229 (≠ W247)
binding Butyryl Coenzyme A: F225 (≠ L243), F241 (= F259)

3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
34% identity, 96% coverage: 10:267/270 of query aligns to 2:254/255 of 3q0jC

query
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3q0jC

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active site: A65 (≠ G74), M70 (≠ F79), T80 (≠ S94), F84 (≠ A98), G108 (= G122), E111 (≠ G125), P130 (≠ T144), E131 (= E145), V136 (≠ L150), P138 (= P152), G139 (≠ A153), L224 (≠ D237), F234 (≠ W247)
binding acetoacetyl-coenzyme a: Q23 (≠ E32), A24 (≠ V33), L25 (≠ H34), A27 (= A36), A63 (= A72), G64 (= G73), A65 (≠ G74), D66 (= D75), I67 (≠ L76), K68 (≠ R77), M70 (≠ F79), F84 (≠ A98), G107 (= G121), G108 (= G122), E111 (≠ G125), P130 (≠ T144), E131 (= E145), P138 (= P152), G139 (≠ A153), M140 (≠ N154)

3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 96% coverage: 10:267/270 of query aligns to 2:254/255 of 3q0gC

query
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3q0gC

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active site: A65 (≠ G74), M70 (≠ F79), T80 (≠ S94), F84 (≠ A98), G108 (= G122), E111 (≠ G125), P130 (≠ T144), E131 (= E145), V136 (≠ L150), P138 (= P152), G139 (≠ A153), L224 (≠ D237), F234 (≠ W247)
binding coenzyme a: L25 (≠ H34), A63 (= A72), I67 (≠ L76), K68 (≠ R77), Y104 (≠ G118), P130 (≠ T144), E131 (= E145), L134 (= L148)

3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
34% identity, 96% coverage: 10:267/270 of query aligns to 1:253/256 of 3h81A

query
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3h81A

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active site: A64 (≠ G74), M69 (≠ F79), T79 (≠ S94), F83 (≠ A98), G107 (= G122), E110 (≠ G125), P129 (≠ T144), E130 (= E145), V135 (≠ L150), P137 (= P152), G138 (≠ A153), L223 (≠ D237), F233 (≠ W247)
binding calcium ion: F233 (≠ W247), Q238 (≠ G252)

5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
31% identity, 96% coverage: 11:269/270 of query aligns to 3:258/259 of 5zaiC

query
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5zaiC

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L

M

A

A

L

V

A

C

C

D

D

V

I

A

R

I

I

G

A

V

A

E

E

G

E

A

A

R

Q

F

L

G

G

L

L

T
x
P

E
|
E

V

I

R

N

L

L

G

G

L
x
I

L

Y

P
|
P

A
x
G

N

Y

I

G

S

G

P

T

F

Q

V

R

I

L

A

T

R

R

-

V

I

I

G

G

A

K

A

G

N

R

A

A

R

L

R

E

V

M

M

M

L

M

S

T

G

G

R

D

R
|
R

F

I

E

P

A

G

S

K

E

D

A

A

V

E

A

K

L

Y

G

G

L

L

L

V

K

N

E

R

A

V

V

V

P

P

A

L

D

A

R

N

L

L

D

E

A

Q

A

E

V

T

E

R

A

K

E

L

V

A

A

E

E

K

L

I

L

A

L

K

A

K

A

S

P

P

G

I

A

S

I

L

A

A

A

-

T

-

K

-

R

-

L

L

I

I

R

K

Q

E

V

V

A

V

T

N

H

R

G

G

L

L

E

D

D

S

N

P

L

L

D

L

Y

S

T

G

A

L

R
x
A

A

L

L

E

A

S

D

V

A

G

W

W

-

G

-

V

-
x
F

E

S

T

T

E

E

E

D

G

K

Q

K

E

E

G

G

I

V

A

S

A

A

F
|
F

L

L

E

E

K
|
K

R

R

K

E

P

P

G

T

W

F

Q

K

G

G

active site: A65 (≠ G74), F70 (= F79), S82 (= S94), R86 (≠ A98), G110 (= G122), E113 (≠ G125), P132 (≠ T144), E133 (= E145), I138 (≠ L150), P140 (= P152), G141 (≠ A153), A226 (≠ R241), F236 (vs. gap)
binding coenzyme a: K24 (≠ V33), L25 (≠ H34), A63 (= A72), G64 (= G73), A65 (≠ G74), D66 (= D75), I67 (≠ L76), P132 (≠ T144), R166 (= R177), F248 (= F259), K251 (= K262)

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)
32% identity, 98% coverage: 4:268/270 of query aligns to 3:272/276 of O69762

query
sites
O69762

S

T

Y

Y

E

E

T

-

P

-

G

G

T

R

F

W

E

K

T

T

L

V

K

K

I

V

E

E

R

I

D

E

A

D

R

-

G

G

V

I

A

A

T

F

L

V

A

I

L

L

D

N

R

R

P

P

E

E

V
x
K

H

R

N

N

A

A

F

M

D

S

E

P

T

T

V

L

I

N

A

R

E

E

L

M

H

I

R

D

A

V

A

L

E

E

A

T

L

L

G

E

A

Q

D

D

P

P

A

A

V

A

R

G

V

V

V

L

V

V

L

L

T

T

G

G

E

A

G

G

R

E

S

A

F

W

S

T

A
|
A

G

G

G
x
M

D

D

L
|
L

R

K

W

E

F
x
Y

R

F

R

R

Q

E

I

V

E

D

S

A

G

G

R

P

E

E

-

I

-

L

-

Q

E

E

R

K

L

I

A

R

G

R

S

E

A

A

A

S

L

-

A

Q

A

W

M

Q

L

W

R

K

A

L

L

L

D

R

E

M

L

Y

P

A

K

K

P

P

L

T

I

I

G

A

R

M

I

V

N

N

G

G

G

W

A

C

Y

F

G

G

G
|
G

G

G

T

F

G
x
S

L

P

M

L

A

V

V

A

C

C

D

D

V

L

A

A

I

I

G

C

V

A

E

D

G

E

A

A

R

T

F

F

G

G

L

L

T
x
S

E
|
E

V

I

R

N

L
x
W

G

G

L

I

L

P

P

P

A
x
G

N

N

-

L

I

V

S

S

P

K

F

A

V

M

I

A

A

D

R

T

I

V

G

G

A

H

A

R

N

Q

A

S

R

L

R

Y

V

Y

M

I

L

M

S

T

G

G

R

K

R

T

F

F

E

G

A

G

S

Q

E

K

A

A

V

A

A

E

L

M

G

G

L

L

L

V

K

N

E

E

A

S

V

V

P

P

A

L

D

A

R

Q

L

L

D

R

A

E

A

V

V

T

E

I

A

E

E

L

V

A

A

R

E

N

L

L

L

E

A

K

A

N

P

P

G

V

A

V

I

L

A

R

A

A

T

A

K

K

R

H

L

G

I

F

R

K

Q

R

V

C

A

R

T

E

H

L

G

T

L

W

E

E

D

Q

N

N

L

E

D

D

Y

Y

T

L

A
x
Y

R

A

A

K

L

L

A

D

D

Q

A

S

-

R

-

L

W

L

E

D

T

T

E

E

E

G

G

G

Q

R

E

E

-

Q

G

G

I

M

A

K

A

Q

F

F

L

L

E

D

K

D

R

K

-

S

-

I

K

K

P

P

G

G

W

L

Q

Q

K29 (≠ V33) binding acetyl-CoA
A68 (= A72) binding acetyl-CoA
M70 (≠ G74) binding acetyl-CoA
L72 (= L76) binding acetyl-CoA
Y75 (≠ F79) binding vanillin
G120 (= G122) binding acetyl-CoA
S123 (≠ G125) mutation to A: Reduced kcat compared to wild-type but not markerdly.
S142 (≠ T144) binding acetyl-CoA
E143 (= E145) mutation to A: Abolishes catalytic activity.
W146 (≠ L148) binding acetyl-CoA
G151 (≠ A153) binding vanillin
Y239 (≠ A240) binding vanillin; 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.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
32% identity, 87% coverage: 4:238/270 of query aligns to 1:235/246 of 2vssD

query
sites
2vssD

S

T

Y

Y

E

E

T

-

P

-

G

G

T

R

F

W

E

K

T

T

L

V

K

K

I

V

E

E

R

I

D

E

A

-

R

D

G

G

V

I

A

A

T

F

L

V

A

I

L

L

D

N

R

R

P

P

E
|
E

V
x
K

H
x
R

N

N

A
|
A

F

M

D

S

E

P

T

T

V

L

I

N

A

R

E

E

L

M

H

I

R

D

A

V

A

L

E

E

A

T

L

L

G

E

A

Q

D

D

P

P

A

A

V

A

R

G

V

V

V

L

V

V

L

L

T

T

G

G

E

A

G

G

R

E

S

A

F

W

S

T

A
|
A

G

G

G
x
M

D
|
D

L
|
L

R

K

W

E

F
x
Y

R
x
F

R

R

Q

E

I

V

E
x
D

S

A

G

G

R

P

E

E

-

I

-

L

-

Q

E

E

R

K

L

I

A

R

G
x
R

S

E

A

A

A

S

L

-

A
x
Q

A

W

M
x
Q

L

W

R

K

A

L

L

L

D

R

E

M

L

Y

P

A

K

K

P

P

L

T

I

I

G

A

R

M

I

V

N

N

G

G

G
x
W

A

C

Y
x
F

G

G

G
|
G

G

G

T

F

G
x
S

L

P

M

L

A

V

V

A

C

C

D

D

V

L

A

A

I

I

G

C

V

A

E

D

G

E

A

A

R

T

F

F

G

G

L

L

T
x
S

E
|
E

V

I

R

N

L

W

G

G

L
x
I

L

P

P
|
P

A
x
G

N
|
N

-

L

I

V

S

S

P

K

F

A

V

M

I

A

A

D

R

T

I

V

G

G

A

H

A

R

N

Q

A

S

R

L

R

Y

V

Y

M

I

L

M

S

T

G

G

R

K

R

T

F

F

E

G

A

G

S

Q

E

K

A

A

V

A

A

E

L

M

G

G

L

L

L

V

K

N

E

E

A

S

V

V

P

P

A

L

D

A

R

Q

L

L

D

R

A

E

A

V

V

T

E

I

A

E

E

L

V

A

A

R

E

N

L

L

L

E

A

K

A

N

P

P

G

V

A

V

I

L

A

R

A

A

T

A

K

K

R

H

L

G

I

F

R

K

Q

R

V

C

A

R

T

E

H

L

G

T

L

W

E

E

D

Q

N

N

L

E

D

D

Y

Y

active site: M68 (≠ G74), Y73 (≠ F79), D78 (≠ E84), R90 (≠ G93), Q94 (≠ A98), G118 (= G122), S121 (≠ G125), S140 (≠ T144), E141 (= E145), I146 (≠ L150), P148 (= P152), G149 (≠ A153)
binding acetyl coenzyme *a: E26 (= E32), K27 (≠ V33), R28 (≠ H34), A30 (= A36), A66 (= A72), M68 (≠ G74), D69 (= D75), L70 (= L76), F74 (≠ R80), W114 (≠ G118), F116 (≠ Y120), S140 (≠ T144)
binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ G74), Y73 (≠ F79), F74 (≠ R80), Q96 (≠ M100), E141 (= E145), G149 (≠ A153), N150 (= N154)

Sites not aligning to the query:

active site: 237

2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
32% identity, 85% coverage: 9:238/270 of query aligns to 3:234/247 of 2vssB

query
sites
2vssB

G

G

T

R

F

W

E

K

T

T

L

V

K

K

I

V

E

E

R

I

D

E

A

-

R

D

G

G

V

I

A

A

T

F

L

V

A

I

L

L

D

N

R

R

P

P

E
|
E

V
x
K

H
x
R

N

N

A
|
A

F

M

D

S

E

P

T

T

V

L

I

N

A

R

E

E

L

M

H

I

R

D

A

V

A

L

E

E

A

T

L

L

G

E

A

Q

D

D

P

P

A

A

V

A

R

G

V

V

V

L

V

V

L

L

T

T

G

G

E

A

G

G

R

E

S

A

F

W

S

T

A
|
A

G

G

G
x
M

D
|
D

L

L

R

K

W

E

F
x
Y

R

F

R

R

Q

E

I

V

E
x
D

S

A

G

G

R

P

E

E

-

I

-

L

-

Q

E

E

R

K

L

I

A

R

G
x
R

S

E

A

A

A

S

L

-

A
x
Q

A

W

M

Q

L

W

R

K

A

L

L

L

D

R

E

M

L

Y

P

A

K

K

P

P

L

T

I

I

G

A

R

M

I

V

N

N

G

G

G
x
W

A

C

Y
x
F

G

G

G
|
G

G

G

T

F

G
x
S

L

P

M

L

A

V

V

A

C

C

D

D

V

L

A

A

I

I

G

C

V

A

E

D

G

E

A

A

R

T

F

F

G

G

L

L

T
x
S

E
|
E

V

I

R

N

L

W

G

G

L
x
I

L

P

P
|
P

A
x
G

N

N

-

L

I

V

S

S

P

K

F

A

V

M

I

A

A

D

R

T

I

V

G

G

A

H

A

R

N

Q

A

S

R

L

R

Y

V

Y

M

I

L

M

S

T

G

G

R

K

R

T

F

F

E

G

A

G

S

Q

E

K

A

A

V

A

A

E

L

M

G

G

L

L

L

V

K

N

E

E

A

S

V

V

P

P

A

L

D

A

R

Q

L

L

D

R

A

E

A

V

V

T

E

I

A

E

E

L

V

A

A

R

E

N

L

L

L

E

A

K

A

N

P

P

G

V

A

V

I

L

A

R

A

A

T

A

K

K

R

H

L

G

I

F

R

K

Q

R

V

C

A

R

T

E

H

L

G

T

L

W

E

E

D

Q

N

N

L

E

D

D

Y

Y

active site: M67 (≠ G74), Y72 (≠ F79), D77 (≠ E84), R89 (≠ G93), Q93 (≠ A98), G117 (= G122), S120 (≠ G125), S139 (≠ T144), E140 (= E145), I145 (≠ L150), P147 (= P152), G148 (≠ A153)
binding acetyl coenzyme *a: E25 (= E32), K26 (≠ V33), R27 (≠ H34), A29 (= A36), A65 (= A72), M67 (≠ G74), D68 (= D75), W113 (≠ G118), F115 (≠ Y120), G117 (= G122), S139 (≠ T144), E140 (= E145)

Sites not aligning to the query:

active site: 236, 246

6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 92% coverage: 22:269/270 of query aligns to 9:244/245 of 6slaAAA

query
sites
6slaAAA

G

G

V

V

A

L

T

V

L

L

A

T

L

L

D

N

R

R

P

P

E

E

V

K

H
x
L

N

N

A

A

F

I

D

T

E

G

T

E

V

L

I

L

A

D

E

A

L

L

H

Y

R

A

A

A

A

L

E

K

A

E

L

G

G

E

A

E

D

D

P

R

A

E

V

V

R

R

V

A

V

L

L

L

T

T

G

G

E

A

G

G

R

R

S

A

F

F

S

S

A
|
A

G

G

G
x
Q

D
|
D

L
|
L

-

T

-

E

-

A

-

H

-
x
L

R

R

W

R

F
x
Y

R
x
N

R

R

Q

V

I

V

E

E

S

-

G

-

R

-

E

-

R

-

L

-

A

-

G

-

S

-

A

-

L

-

A

-

M

-

L

-

R

-

A

A

L

L

D

S

E

G

L

L

P

E

K

K

P

P

L

L

I

V

G

V

R

A

I

V

N

N

G

G

G

V

A

A

Y
x
A

G
|
G

G
x
A

G

G

T

M

G
x
S

L

L

M

A

A

L

V

W

C

G

D

D

V

L

A

R

I

L

G

A

V

A

E

V

G

G

A

A

R

S

F

F

G

T

L

T

T
x
A

E
x
F

V

V

R

R

L
x
I

G

G

L
|
L

L

V

P
|
P

A
x
N

N

S

I

G

S

L

P

S

F

F

V

L

I

L

A

P

R

R

-

L

I

V

G

G

A

L

A

A

N

K

A

A

R

Q

R

E

V

L

M

L

L

L

S

L

G

S

R

P

R

R

F

L

E

S

A

A

S

E

E

E

A

A

V

L

A

A

L

L

G

G

L

L

L

V

K

H

E

R

A

V

V

V

P

P

A

A

D

E

R

K

L

L

D

M

A

E

V

A

E

L

A

S

E

L

V

A

A

K

E

E

L

L

L

A

L

Q

A

G

A

P

P

T

G

R

A

A

I

Y

A

A

A

L

T

T

K

K

R

K

L

L

I

L

R

L

Q

E

V

T

A

Y

T

R

H

L

G

S

L

L

E

T

D

E

N

A

L

L

D
x
A

Y

L

T

E

A

A

R

V

A

L

L

Q

A

G

D

Q

A

A

W
x
G

E

Q

T

T

E

Q

E

D

G

H

Q

E

E

E

G

G

I

V

A

R

A

A

F
|
F

L

R

E

E

K
|
K

R

R

K

P

P

P

G

R

W

F

Q

Q

G

G

active site: Q61 (≠ G74), L68 (vs. gap), N72 (≠ R80), A96 (≠ G122), S99 (≠ G125), A118 (≠ T144), F119 (≠ E145), L124 (= L150), P126 (= P152), N127 (≠ A153), A212 (≠ D237), G222 (≠ W247)
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 (≠ H34), A59 (= A72), Q61 (≠ G74), D62 (= D75), L63 (= L76), L68 (vs. gap), Y71 (≠ F79), A94 (≠ Y120), G95 (= G121), A96 (≠ G122), F119 (≠ E145), I122 (≠ L148), L124 (= L150), N127 (≠ A153), F234 (= F259), K237 (= K262)

6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 92% coverage: 22:269/270 of query aligns to 12:256/257 of 6slbAAA

query
sites
6slbAAA

G

G

V

V

A

L

T

V

L

L

A

T

L

L

D

N

R

R

P

P

E

E

V

K

H

L

N

N

A

A

F

I

D

T

E

G

T

E

V

L

I

L

A

D

E

A

L

L

H

Y

R

A

A

A

A

L

E

K

A

E

L

G

G

E

A

E

D

D

P

R

A

E

V

V

R

R

V

A

V

L

L

L

T

T

G

G

E

A

G

G

R
|
R

S

A

F

F

S

S

A
|
A

G

G

G
x
Q

D
|
D

L
|
L

R

T

W

E

F
|
F

R

G

R

D

Q

R

I

-

E

-

S

-

G

-

R

K

E

P

E

D

R
x
Y

L

E

A

A

G

H

S
x
L

A

R

L

Y

A
x
N

A

R

M

V

L

V

R

E

A

A

L

L

D

S

E

G

L

L

P

E

K

K

P

P

L

L

I

V

G

V

R

A

I

V

N

N

G

G

G

V

A

A

Y

A

G

G

G
x
A

G

G

T

M

G
x
S

L

L

M

A

A

L

V

W

C

G

D

D

V

L

A

R

I

L

G

A

V

A

E

V

G

G

A

A

R

S

F

F

G

T

L

T

T
x
A

E
x
F

V

V

R

R

L

I

G

G

L
|
L

L

V

P
|
P

A
x
D

N

S

I

G

S

L

P

S

F

F

V

L

I

L

A

P

R

R

-

L

I

V

G

G

A

L

A

A

N

K

A

A

R

Q

R

E

V

L

M

L

L

L

S

L

G

S

R

P

R

R

F

L

E

S

A

A

S

E

E

E

A

A

V

L

A

A

L

L

G

G

L

L

L

V

K

H

E

R

A

V

V

V

P

P

A

A

D

E

R

K

L

L

D

M

A

E

V

A

E

L

A

S

E

L

V

A

A

K

E

E

L

L

L

A

L

Q

A

G

A

P

P

T

G

R

A

A

I

Y

A

A

A

L

T

T

K

K

R

K

L

L

I

L

R

L

Q

E

V

T

A

Y

T

R

H

L

G

S

L

L

E

T

D

E

N

A

L

L

D
x
A

Y

L

T

E

A

A

R

V

A

L

L

Q

A

G

D

Q

A

A

W
x
G

E

Q

T

T

E

Q

E

D

G

H

Q

E

E

E

G

G

I

V

A

R

A

A

F

F

L

R

E

E

K

K

R

R

K

P

P

P

G

R

W

F

Q

Q

G

G

active site: Q64 (≠ G74), F69 (= F79), L80 (≠ S94), N84 (≠ A98), A108 (≠ G122), S111 (≠ G125), A130 (≠ T144), F131 (≠ E145), L136 (= L150), P138 (= P152), D139 (≠ A153), A224 (≠ D237), G234 (≠ W247)
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 (= R68), A62 (= A72), Q64 (≠ G74), D65 (= D75), L66 (= L76), Y76 (≠ R90), A108 (≠ G122), F131 (≠ E145), D139 (≠ A153)

Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
29% identity, 98% coverage: 2:265/270 of query aligns to 13:276/285 of Q7CQ56

query
sites
Q7CQ56

T

V

E

E

S

W

Y

H

E

D

T

C

P

S

G

E

T

G

F

Y

E

T

T

D

L

I

K

R

I

Y

E

E

R

K

D

S

A

T

R

D

G

G

V

I

A

A

T

K

L

I

A

T

L

I

D

N

R

R

P

P

E

Q

V

V

H

R

N

N

A

A

F

F

D

R

E

P

T

L

V

T

I

V

A

K

E

E

L

M

H

I

R

Q

A

A

A

L

E

A

A

D

L

A

G

R

A

Y

D

D

P

D

A

N

V

V

R

G

V

V

V

I

L

L

T

T

G

G

E

E

G

G

-

D

R

K

S

A

F

F

S

C

A

A

G

G

D

D

L

Q

R

K

W

-

F

V

R

R

R

G

Q

D

I

Y

E

G

S

G

G

Y

R

Q

E

D

R

S

L

G

A

V

G

H

S

H

A

L

A

N

L

V

A

L

A

D

M

F

L

Q

R

R

A

Q

L

I

D

R

E

T

L

C

P

P

K

K

P

P

L

V

I

V

G

A

R

M

I

V

N

A

G

G

G

Y

A

S

Y

I

G

G

T

H

G

V

L

L

M

H

A

M

V

M

C

C

D

D

V

L

A

T

I

I

G

A

V

A

E

E

G

N

A

A

R

I

F

F

G

G

L
x
Q

T
|
T

E
x
G

V

P

R

K

L

V

G

G

L

S

L

F

P

D

A

G

N

G

I

W

S

G

P

A

F

S

V

Y

I

M

A

A

R

R

I

I

-

V

G

G

A

Q

A

K

N

K

A

A

R

R

R

E

V

I

M

W

L

F

S

L

G

C

R

R

R

Q

F

Y

E

D

A

A

S

Q

E

Q

A

A

V

L

A

D

L

M

G

G

L

L

L

V

K

N

E

T

A

V

V

V

P

P

A

L

D

A

R

D

L

L

D

E

A

K

A

E

V

T

E

V

A

R

E

W

V

C

A

R

E

E

L

M

L

L

L

Q

A

N

A

S

P

P

G

M

A

A

I

L

A

R

A

C

T

L

K

K

R

A

L

A

I

L

R

-

Q

N

V

A

A

D

T

C

H

D

G

G

L

Q

E

A

D

G

N

L

L

Q

D

E

Y

L

T

A

A

G

R

N

A

A

L

T

A

M

D

L

A

F

W

Y

E

M

T

T

E

E

G

G

Q

Q

E

E

G

G

I

R

A

N

A

A

F

F

L

N

E

Q

K

K

R

R

K

Q

P

P

QTG 154:156 (≠ LTE 143:145) binding hydrogencarbonate

Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
32% identity, 98% coverage: 4:267/270 of query aligns to 5:266/273 of Q5HH38

query
sites
Q5HH38

S

Q

Y

W

E

E

T

T

P

L

G

R

T

E

F

Y

E

D

T

E

L

I

K

K

I

Y

E

E

R

F

D

-

A

Y

R

E

G

G

V

I

A

A

T

K

L

V

A

T

L

I

D

N

R

R

P

P

E

E

V

V

H
x
R

N

N

A

A

F

F

D

T

E

P

T

K

V

T

I

V

A

A

E

E

L

M

H

I

R

D

A

A

A

F

E

S

A

R

L

A

G

R

A

D

D

D

P

Q

A

N

V

V

R

S

V

V

V

I

V

V

L

L

T

T

G

G

E

E

G

G

R

D

-

L

S

A

F

F

S

C

A
x
S

G
|
G

D
|
D

L
x
Q

R

K

W

-

F

-

R

K

R

R

Q

G

I

H

E

G

S

G

G

Y

R

V

E

G

E

E

R

D

L

Q

A

I

G

P

S

R

A

L

A

N

L

V

A

L

A

D

M

L

L

Q

R

R

A

L

L

I

D

R

E

I

L

I

P

P

K

K

P

P

L

V

I

I

G

A

R

M

I

V

N

K

G

G

G

Y

A

A

Y

V

G

G

T

N

G

V

L

L

M

N

A

V

V

V

C

C

D

D

V

L

A

T

I

I

G

A

V

A

E

D

G

N

A

A

R

I

F

F

G

G

L

Q

T

T

E

G

V

P

R

K

L

V

G

G

L
x
S

L

F

P

D

A

A

N

G

I

Y

S

G

P

S

F

G

V

Y

I

L

A

A

R

R

I

I

-

V

G

G

A

H

A

K

N

K

A

A

R

R

R

E

V

I

M

W

L

Y

S

L

G

C

R

R

R

Q

F

Y

E

N

A

A

S

Q

E

E

A

A

V

L

A

D

L

M

G

G

L

L

L

V

K

N

E

T

A

V

V

V

P

P

A

L

D

E

R

K

L

V

D

E

A

D

A

E

V

T

E

V

A

Q

E

W

V

C

A

K

E

E

L

I

L

M

L

K

A

H

A

S

P

P

G

T

A

A

I

L

A

R

A

F

T

L

K

K

R

A

L

A

I

M

R

-

Q

N

V

A

A

D

T

T

H

D

G

G

L

L

E

A

D

G

N

L

L

Q

D

Q

Y

M

T

A

A

G

R

D

A

A

L

T

A

L

D

L

A

Y

W

Y

E

T

T

T

E

D

E

E

G

A

Q

K

E

E

G

G

I

R

A

D

A

A

F

F

L

K

E

E

K

K

R

R

K

D

P

P

G

D

W

F

R34 (≠ H34) binding in other chain
SGGDQ 73:77 (≠ AGGDL 72:76) binding in other chain
S149 (≠ L150) 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)
32% identity, 97% coverage: 5:267/270 of query aligns to 1:253/260 of 2uzfA

query
sites
2uzfA

Y

W

E

E

T

T

P

L

G

R

T

E

F

Y

E

D

T

E

L

I

K

K

I

Y

E

E

R

F

D

-

A

Y

R

E

G

G

V

I

A

A

T

K

L

V

A

T

L

I

D

N

R

R

P

P

E

E

V
|
V

H
x
R

N

N

A

A

F

F

D

T

E

P

T

K

V

T

I

V

A

A

E

E

L

M

H

I

R

D

A

A

A

F

E

S

A

R

L

A

G

R

A

D

D

D

P

Q

A

N

V

V

R

S

V

V

V

I

V

V

L

L

T

T

G

G

E

E

G

G

R

D

-

L

S

A

F

F

S

C

A
x
S

G
|
G

D
|
D

L

Q

R

K

W

-

F

-

R

-

Q

-

I

-

E

-

S

-

G

-

R

G

E

E

E

D

R

Q

L

I

A

P

G
x
R

S

L

A

N

A

V

L
|
L

A

D

A

-

M

L

L

Q

R

R

A

L

L

I

D

R

E

I

L

I

P

P

K

K

P

P

L

V

I

I

G

A

R

M

I

V

N

K

G

G

G
x
Y

A

A

Y

V

G

G

G
|
G

G

G

T

N

G
x
V

L

L

M

N

A

V

V

V

C

C

D

D

V

L

A

T

I

I

G

A

V

A

E

D

G

N

A

A

R

I

F

F

G

G

L

Q

T
|
T

E
x
G

V

P

R

K

L

V

G

G

L
x
S

L

F

P
x
D

A
|
A

N

G

I

Y

S

G

P

S

F

G

V

Y

I

L

A

A

R

R

I

I

-

V

G

G

A

H

A

K

N

K

A

A

R

R

R

E

V

I

M

W

L

Y

S

L

G

C

R

R

R

Q

F

Y

E

N

A

A

S

Q

E

E

A

A

V

L

A

D

L

M

G

G

L

L

L

V

K

N

E

T

A

V

V

V

P

P

A

L

D

E

R

K

L

V

D

E

A

D

A

E

V

T

E

V

A

Q

E

W

V

C

A

K

E

E

L

I

L

M

L

K

A

H

A

S

P

P

G

T

A

A

I

L

A

R

A

F

T

L

K

K

R

A

L

A

I

M

R

-

Q

N

V

A

A

D

T

T

H

D

G

G

L

L

E

A

D

G

N

L

L

Q

D

Q

Y

M

T
x
A

A

G

R

D

A

A

L

T

A

L

D

L

A

Y

W
x
Y

E

T

T

T

E

D

E

E

G

A

Q

K

E

E

G

G

I

R

A

D

A

A

F

F

L

K

E

E

K

K

R

R

K

D

P

P

G

D

W

F

active site: G70 (= G74), R80 (≠ G93), L84 (= L97), G108 (= G122), V111 (≠ G125), T130 (= T144), G131 (≠ E145), S136 (≠ L150), D138 (≠ P152), A139 (= A153), A225 (≠ T239), Y233 (≠ W247)
binding acetoacetyl-coenzyme a: V28 (= V33), R29 (≠ H34), S68 (≠ A72), G69 (= G73), G70 (= G74), D71 (= D75), Y104 (≠ G118), G108 (= G122)

4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
28% identity, 98% coverage: 2:265/270 of query aligns to 13:276/285 of 4i42A

query
sites
4i42A

T

V

E

E

S

W

Y

H

E

D

T

C

P

S

G

E

T

G

F

F

E

E

T

D

L

I

K

R

I

Y

E

E

R

K

D

S

A

T

R

D

G

G

V

I

A

A

T

K

L

I

A

T

L

I

D

N

R

R

P

P

E

Q

V
|
V

H
x
R

N

N

A

A

F

F

D

R

E

P

T

L

V

T

I

V

A

K

E

E

L

M

H

I

R

Q

A

A

A

L

E

A

A

D

L

A

G

R

A

Y

D

D

P

D

A

N

V

I

R

G

V

V

V

I

L

L

T

T

G

G

E

A

G

G

-

D

R

K

S

A

F

F

S

C

A
x
S

G
|
G

D
|
D

L
x
Q

R
x
K

W

-

F

V

R
|
R

R

G

Q

D

I

Y

E

G

S

G

G
x
Y

R

K

E

D

R

S

L

G

A

V

G

H

S
x
H

A

L

A

N

L
x
V

A
x
L

A

D

M

F

L

Q

R

R

A

Q

L

I

D

R

E

T

L

C

P

P

K

K

P

P

L

V

I

V

G

A

R

M

I

V

N

A

G

G

G
x
Y

A

S

Y

I

G

G

G
|
G

G

G

T

H

G
x
V

L

L

M

H

A

M

V

M

C

C

D

D

V

L

A

T

I

I

G

A

V

A

E

D

G

N

A

A

R

I

F

F

G

G

L

Q

T
|
T

E
x
G

V

P

R

K

L

V

G

G

L
x
S

L

F

P
x
D

A
x
G

N

G

I

W

S

G

P

A

F

S

V

Y

I

M

A

A

R

R

I

I

-

V

G

G

A

Q

A

K

N

K

A

A

R

R

R

E

V

I

M

W

L

F

S

L

G

C

R

R

R

Q

F

Y

E

D

A

A

S

K

E

Q

A

A

V

L

A

D

L

M

G

G

L

L

L

V

K

N

E

T

A

V

V

V

P

P

A

L

D

A

R

D

L

L

D

E

A

K

A

E

V

T

E

V

A

R

E

W

V

C

A

R

E

E

L

M

L

L

L

Q

A

N

A

S

P

P

G

M

A

A

I

L

A

R

A

C

T

L

K

K

R

A

L

A

I

L

R

-

Q

N

V

A

A

D

T

C

H

D

G

G

L

Q

E

A

D

G

N

L

L

Q

D

E

Y

L

T
x
A

A

G

R

N

A

A

L
x
T

A

M

D

L

A

F

W
x
Y

E

M

T

T

E

E

G

G

Q

Q

E

E

G

G

I

R

A

N

A

A

F
|
F

L

N

E

Q

K
|
K

R

R

K

Q

P

P

active site: G86 (= G74), R91 (= R80), Y97 (≠ G86), H105 (≠ S94), L109 (≠ A98), G133 (= G122), V136 (≠ G125), G156 (≠ E145), S161 (≠ L150), D163 (≠ P152), G164 (≠ A153), A250 (≠ T239), Y258 (≠ W247)
binding 1-hydroxy-2-naphthoyl-CoA: V44 (= V33), R45 (≠ H34), S84 (≠ A72), G85 (= G73), G86 (= G74), D87 (= D75), Q88 (≠ L76), K89 (≠ R77), Y97 (≠ G86), V108 (≠ L97), Y129 (≠ G118), G133 (= G122), T155 (= T144), S161 (≠ L150), T254 (≠ L243), F270 (= F259), K273 (= K262)

P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
28% identity, 98% coverage: 2:265/270 of query aligns to 13:276/285 of P0ABU0

query
sites
P0ABU0

T

V

E

E

S

W

Y

H

E

D

T

C

P

S

G

E

T

G

F

F

E

E

T

D

L

I

K

R

I

Y

E

E

R

K

D

S

A

T

R

D

G

G

V

I

A

A

T

K

L

I

A

T

L

I

D

N

R

R

P

P

E

Q

V

V

H
x
R

N

N

A

A

F

F

D

R

E

P

T

L

V

T

I

V

A

K

E

E

L

M

H

I

R

Q

A

A

A

L

E

A

A

D

L

A

G

R

A

Y

D

D

P

D

A

N

V

I

R

G

V

V

V

I

L

L

T

T

G

G

E

A

G

G

-

D

R

K

S

A

F

F

S

C

A
x
S

G
|
G

D
|
D

L
x
Q

R
x
K

W

-

F

V

R
|
R

R

G

Q

D

I

Y

E

G

S

G

G
x
Y

R

K

E

D

R

S

L

G

A

V

G

H

S

H

A

L

A

N

L

V

A

L

A

D

M

F

L

Q

R

R

A

Q

L

I

D

R

E

T

L

C

P

P

K

K

P

P

L

V

I

V

G

A

R

M

I

V

N

A

G

G

G
x
Y

A
x
S

Y
x
I

G
|
G

G

G

T

H

G

V

L

L

M

H

A

M

V

M

C

C

D

D

V

L

A

T

I

I

G

A

V

A

E

D

G

N

A

A

R

I

F

F

G

G

L
x
Q

T
|
T

E
x
G

V

P

R

K

L

V

G

G

L
x
S

L

F

P

D

A

G

N

G

I

W

S

G

P

A

F

S

V

Y

I

M

A

A

R

R

I

I

-

V

G

G

A

Q

A

K

N

K

A

A

R

R

R

E

V

I

M
x
W

L

F

S

L

G

C

R

R

R

Q

F

Y

E

D

A

A

S

K

E

Q

A

A

V

L

A

D

L

M

G

G

L

L

L

V

K

N

E

T

A

V

V

V

P

P

A

L

D

A

R

D

L

L

D

E

A

K

A

E

V

T

E

V

A

R

E

W

V

C

A

R

E

E

L

M

L

L

L

Q

A

N

A

S

P

P

G

M

A

A

I

L

A

R

A

C

T

L

K

K

R

A

L

A

I

L

R

-

Q

N

V

A

A

D

T

C

H

D

G

G

L

Q

E

A

D

G

N

L

L

Q

D

E

Y

L

T

A

A

G

R

N

A

A

L

T

A

M

D

L

A

F

W
x
Y

E

M

T

T

E

E

G

G

Q

Q

E

E

G

G

I
x
R

A

N

A

A

F
|
F

L

N

E

Q

K
|
K

R

R

K

Q

P

P

R45 (≠ H34) binding in other chain
SGGDQK 84:89 (≠ AGGDLR 72:77) binding in other chain
K89 (≠ R77) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
R91 (= R80) mutation to A: Loss of DHNA-CoA synthase activity.
Y97 (≠ G86) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
YSIGG 129:133 (≠ GAYGG 118:122) binding in other chain
Q154 (≠ L143) mutation to A: Reduces the specific DHNA-CoA synthase activity by 15-fold, whereas its affinity for hydrogencarbonate is reduced by 36-fold.
QTG 154:156 (≠ LTE 143:145) binding hydrogencarbonate
T155 (= T144) binding in other chain
G156 (≠ E145) mutation to D: Loss of DHNA-CoA synthase activity.
S161 (≠ L150) binding in other chain
W184 (≠ M172) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
Y258 (≠ W247) binding substrate
R267 (≠ I256) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
F270 (= F259) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
K273 (= K262) binding substrate; mutation to A: Impairs protein folding.

6l3pA Crystal strcuture of feruloyl-coa hydratase lyase(fchl) complexed with coa
33% identity, 85% coverage: 9:238/270 of query aligns to 5:231/244 of 6l3pA

query
sites
6l3pA

G

G

T

R

F

W

E

T

T

T

L

V

K

K

I

V

E

E

R

L

D

E

A

A

R

-

G

G

V

I

A

A

T

W

L

V

A

T

L

L

D

N

R

R

P

P

E

E

V
x
K

H
x
R

N

N

A
|
A

F

M

D

S

E

P

T

T

V

L

I

N

A

R

E

E

L

M

H

V

R

D

A

V

A

L

E

E

A

T

L

L

G

E

A

Q

D

D

P

A

A

D

V

A

R

G

V

V

V

L

V

V

L

L

T

T

G

G

E

A

G

G

R

E

S

S

F

W

S

T

A
|
A

G

G

G
x
M

D
|
D

L
|
L

R

K

-

E

W
x
Y

F

F

R

R

R

E

Q

E

I

I

E

L

S

Q

G

E

R

K

E

I

E

R

R
|
R

L

E

A

A

G

-

S

S

A
x
Q

A

W

L

Q

A

W

A

K

M

L

L

L

R

R

A

L

L

Y

D

-

E

-

L

-

P

A

K

K

P

P

L

T

I

I

G

A

R

M

I

V

N

N

G

G

G

W

A

C

Y

F

G
|
G

G

G

T

F

G
x
S

L

P

M

L

A

V

V

A

C

C

D

D

V

L

A

A

I

I

G

C

V

A

E

N

G

E

A

A

R

T

F

F

G

G

L

L

T
x
S

E
|
E

V

I

R

N

L

W

G

G

L
x
I

L

P

P
|
P

A
x
G

N

N

-

L

I

V

S

S

P

K

F

A

V

M

I

A

A

D

R

T

I

V

G

G

A

H

A

R

N

Q

A

S

R

L

R

Y

V

Y

M

I

L

M

S

T

G

G

R

K

R

T

F

F

E

D

A

G

S

R

E

K

A

A

V

A

A

E

L

M

G

G

L

L

L

V

K

N

E

D

A

S

V

V

P

P

A

L

D

A

R

E

L

L

D

R

A

E

A

T

V

T

E

R

A

E

E

L

V

A

A

L

E

N

L

L

L

E

A

K

A

N

P

P

G

V

A

V

I

L

A

R

A

A

T

A

K

K

R

N

L

G

I

F

R

K

Q

R

V

C

A

R

T

E

H

L

G

T

L

W

E

E

D

Q

N

N

L

E

D

D

Y

Y

active site: M69 (≠ G74), Y74 (≠ W78), R86 (= R90), Q90 (≠ A95), G114 (= G122), S117 (≠ G125), S136 (≠ T144), E137 (= E145), I142 (≠ L150), P144 (= P152), G145 (≠ A153)
binding coenzyme a: K28 (≠ V33), R29 (≠ H34), A31 (= A36), A67 (= A72), M69 (≠ G74), D70 (= D75), L71 (= L76), G113 (= G121)

Sites not aligning to the query:

active site: 233, 243

3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
28% identity, 98% coverage: 2:265/270 of query aligns to 9:272/281 of 3t88A

query
sites
3t88A

T

V

E

E

S

W

Y

H

E

D

T

C

P

S

G

E

T

G

F

F

E

E

T

D

L

I

K

R

I

Y

E

E

R

K

D

S

A

T

R

D

G

G

V

I

A

A

T

K

L

I

A

T

L

I

D

N

R

R

P

P

E
x
Q

V
|
V

H
x
R

N

N

A
|
A

F

F

D

R

E

P

T

L

V

T

I

V

A

K

E

E

L

M

H

I

R

Q

A

A

A

L

E

A

A

D

L

A

G

R

A

Y

D

D

P

D

A

N

V

I

R

G

V

V

V

I

L

L

T

T

G

G

E

A

G

G

-

D

R

K

S

A

F

F

S

C

A
x
S

G
|
G

D
|
D

L
x
Q

R
x
K

W

-

F

V

R
|
R

R

G

Q

D

I

Y

E

G

S

G

G
x
Y

R

K

E

D

R

S

L

G

A

V

G

H

S
x
H

A

L

A

N

L
x
V

A
x
L

A

D

M

F

L

Q

R

R

A

Q

L

I

D

R

E

T

L

C

P

P

K

K

P

P

L

V

I

V

G

A

R

M

I

V

N

A

G

G

G
x
Y

A

S

Y

I

G

G

G
|
G

G

G

T

H

G
x
V

L

L

M

H

A

M

V

M

C

C

D

D

V

L

A

T

I

I

G

A

V

A

E

D

G

N

A

A

R

I

F

F

G

G

L

Q

T
|
T

E
x
G

V

P

R

K

L
x
V

G

G

L
x
S

L
x
F

P
x
D

A
x
G

N

G

I

W

S

G

P

A

F

S

V

Y

I

M

A

A

R

R

I

I

-

V

G

G

A

Q

A

K

N

K

A

A

R

R

R

E

V

I

M

W

L

F

S

L

G

C

R

R

R

Q

F

Y

E

D

A

A

S

K

E

Q

A

A

V

L

A

D

L

M

G

G

L

L

L

V

K

N

E

T

A

V

V

V

P

P

A

L

D

A

R

D

L

L

D

E

A

K

A

E

V

T

E

V

A

R

E

W

V

C

A

R

E

E

L

M

L

L

L

Q

A

N

A

S

P

P

G

M

A

A

I

L

A

R

A

C

T

L

K

K

R

A

L

A

I

L

R

-

Q

N

V

A

A

D

T

C

H

D

G

G

L

Q

E

A

D

G

N

L

L

Q

D

E

Y

L

T
x
A

A

G

R

N

A

A

L
x
T

A

M

D

L

A

F

W
x
Y

E

M

T

T

E

E

G

G

Q

Q

E

E

G

G

I

R

A

N

A

A

F
|
F

L

N

E

Q

K
|
K

R

R

K

Q

P

P

active site: G82 (= G74), R87 (= R80), Y93 (≠ G86), H101 (≠ S94), L105 (≠ A98), G129 (= G122), V132 (≠ G125), G152 (≠ E145), S157 (≠ L150), D159 (≠ P152), G160 (≠ A153), A246 (≠ T239), Y254 (≠ W247)
binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ E32), V40 (= V33), R41 (≠ H34), A43 (= A36), S80 (≠ A72), G81 (= G73), G82 (= G74), D83 (= D75), Q84 (≠ L76), K85 (≠ R77), Y93 (≠ G86), V104 (≠ L97), L105 (≠ A98), Y125 (≠ G118), G129 (= G122), T151 (= T144), V155 (≠ L148), F158 (≠ L151), D159 (≠ P152), T250 (≠ L243), Y254 (≠ W247), F266 (= F259), K269 (= K262)

3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
29% identity, 97% coverage: 3:265/270 of query aligns to 10:257/266 of 3h02A

query
sites
3h02A

E

E

S

W

Y

H

E

D

T

C

P

S

G

E

T

G

F

Y

E

T

T

D

L

I

K

R

I

Y

E

E

R

K

D

S

A

T

R

D

G

G

V

I

A

A

T

K

L

I

A

T

L

I

D

N

R

R

P

P

E

Q

V

V

H

R

N

N

A

A

F

F

D

R

E

P

T

L

V

T

I

V

A

K

E

E

L

M

H

I

R

Q

A

A

A

L

E

A

A

D

L

A

G

R

A

Y

D

D

P

D

A

N

V

V

R

G

V

V

V

I

L

L

T

T

G

G

E

E

G

G

-

D

R

K

S

A

F

F

S

C

A

A

G

G

G
|
G

D

D

L

Q

R

H

W
x
H

-

L

-

N

-

V

-
x
L

-

D

F

F

R

Q

R

R

Q

Q

I

I

E

R

S

T

G

-

R

-

E

-

R

-

L

-

A

-

G

-

S

-

A

-

L

-

A

-

M

-

L

-

R

-

A

-

L

-

D

-

E

-

L

C

P

P

K

K

P

P

L

V

I

V

G

A

R

M

I

V

N

A

G

G

G

Y

A

S

Y

I

G
|
G

G

G

T

H

G
x
V

L

L

M

H

A

M

V

M

C

C

D

D

V

L

A

T

I

I

G

A

V

A

E

E

G

N

A

A

R

I

F

F

G

G

L
x
Q

T

T

E
x
G

V

P

R

K

L

V

G

G

L
x
S

L

F

P
x
D

A
x
G

N

G

I

W

S

G

P

A

F

S

V

Y

I

M

A

A

R

R

I

I

-

V

G

G

A

Q

A

K

N

K

A

A

R

R

R

E

V

I

M
x
W

L

F

S

L

G

C

R

R

R

Q

F

Y

E

D

A

A

S

Q

E

Q

A

A

V

L

A

D

L

M

G

G

L

L

L

V

K

N

E

T

A

V

V

V

P

P

A

L

D

A

R

D

L

L

D

E

A

K

A

E

V

T

E

V

A

R

E

W

V

C

A

R

E

E

L

M

L

L

L

Q

A

N

A

S

P

P

G

M

A

A

I

L

A

R

A

C

T

L

K

K

R

A

L

A

I

L

R

-

Q

N

V

A

A

D

T

C

H

D

G

G

L

Q

E

A

D

G

N

L

L

Q

D

E

Y

L

T
x
A

A

G

R

N

A

A

L

T

A

M

D

L

A

F

W
x
Y

E

M

T

T

E

E

G

G

Q

Q

E

E

G

G

I

R

A

N

A

A

F

F

L

N

E

Q

K

K

R

R

K

Q

P

P

active site: G82 (= G74), H86 (≠ W78), L90 (vs. gap), G114 (= G122), V117 (≠ G125), G137 (≠ E145), S142 (≠ L150), D144 (≠ P152), G145 (≠ A153), A231 (≠ T239), Y239 (≠ W247)
binding bicarbonate ion: G113 (= G121), Q135 (≠ L143), G137 (≠ E145), W165 (≠ M172)

4elxA Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl (see paper)
28% identity, 98% coverage: 2:265/270 of query aligns to 10:259/268 of 4elxA

query
sites
4elxA

T

V

E

E

S

W

Y

H

E

D

T

C

P

S

G

E

T

G

F

F

E

E

T

D

L

I

K

R

I

Y

E

E

R

K

D

S

A

T

R

D

G

G

V

I

A

A

T

K

L

I

A

T

L

I

D

N

R

R

P

P

E

Q

V

V

H

R

N

N

A

A

F

F

D

R

E

P

T

L

V

T

I

V

A

K

E

E

L

M

H

I

R

Q

A

A

A

L

E

A

A

D

L

A

G

R

A

Y

D

D

P

D

A

N

V

I

R

G

V

V

V

I

L

L

T

T

G

G

E

A

G

G

-

D

R

K

S

A

F

F

S

C

A

S

G

G

G
|
G

D

D

L

Q

R

K

W

H

F
x
H

R

L

R

N

Q

V

I
x
L

E

D

S

F

G

Q

R

R

E

Q

E

I

R

R

L

T

A

C

G

-

S

-

A

-

L

-

A

-

M

-

L

-

R

-

A

-

L

-

D

-

E

-

L

-

P

P

K

K

P

P

L

V

I

V

G

A

R

M

I

V

N

A

G

G

G

Y

A

S

Y

I

G
|
G

G

G

T

H

G
x
V

L

L

M

H

A

M

V

M

C

C

D

D

V

L

A

T

I

I

G

A

V

A

E

D

G

N

A

A

R

I

F

F

G

G

L

Q

T

T

E
x
G

V

P

R

K

L

V

G

G

L
x
S

L

F

P
x
D

A
x
G

N

G

I

W

S

G

P

A

F

S

V

Y

I

M

A

A

R

R

I

I

-

V

G

G

A

Q

A

K

N

K

A

A

R

R

R

E

V

I

M
x
W

L

F

S

L

G

C

R

R

R

Q

F

Y

E

D

A

A

S

K

E

Q

A

A

V

L

A

D

L

M

G

G

L

L

L

V

K

N

E

T

A

V

V

V

P

P

A

L

D

A

R

D

L

L

D

E

A

K

A

E

V

T

E

V

A

R

E

W

V

C

A

R

E

E

L

M

L

L

L

Q

A

N

A

S

P

P

G

M

A

A

I

L

A

R

A

C

T

L

K

K

R

A

L

A

I

L

R

-

Q

N

V

A

A

D

T

C

H

D

G

G

L

Q

E

A

D

G

N

L

L

Q

D

E

Y

L

T
x
A

A

G

R

N

A

A

L

T

A

M

D

L

A

F

W
x
Y

E

M

T

T

E

E

G

G

Q

Q

E

E

G

G

I

R

A

N

A

A

F

F

L

N

E

Q

K

K

R

R

K

Q

P

P

active site: G83 (= G74), H88 (≠ F79), L92 (≠ I83), G116 (= G122), V119 (≠ G125), G139 (≠ E145), S144 (≠ L150), D146 (≠ P152), G147 (≠ A153), A233 (≠ T239), Y241 (≠ W247)
binding chloride ion: G115 (= G121), G139 (≠ E145), W167 (≠ M172)

4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
28% identity, 98% coverage: 2:265/270 of query aligns to 10:258/267 of 4elwA

query
sites
4elwA

T

V

E

E

S

W

Y

H

E

D

T

C

P

S

G

E

T

G

F

F

E

E

T

D

L

I

K

R

I

Y

E

E

R

K

D

S

A

T

R

D

G

G

V

I

A

A

T

K

L

I

A

T

L

I

D

N

R

R

P

P

E

Q

V

V

H

R

N

N

A

A

F

F

D

R

E

P

T

L

V

T

I

V

A

K

E

E

L

M

H

I

R

Q

A

A

A

L

E

A

A

D

L

A

G

R

A

Y

D

D

P

D

A

N

V

I

R

G

V

V

V

I

L

L

T

T

G

G

E

A

G

G

-

D

R

K

S

A

F

F

S

C

A

S

G

G

G
|
G

D

D

L

Q

R

K

W

H

-

L

-

N

-

V

-
x
L

-

D

F

F

R

Q

R

R

Q

Q

I

I

E

R

S

T

G

-

R

-

E

-

R

-

L

-

A

-

G

-

S

-

A

-

L

-

A

-

M

-

L

-

R

-

A

-

L

-

D

-

E

-

L

C

P

P

K

K

P

P

L

V

I

V

G

A

R

M

I

V

N

A

G

G

G

Y

A

S

Y

I

G
|
G

G

G

T

H

G
x
V

L

L

M

H

A

M

V

M

C

C

D

D

V

L

A

T

I

I

G

A

V

A

E

D

G

N

A

A

R

I

F

F

G

G

L

Q

T
|
T

E
x
G

V

P

R

K

L

V

G

G

L
x
S

L
x
F

P
x
D

A
x
G

N

G

I

W

S

G

P

A

F

S

V

Y

I

M

A

A

R

R

I

I

-

V

G

G

A

Q

A

K

N

K

A

A

R

R

R

E

V

I

M
x
W

L

F

S

L

G

C

R

R

R

Q

F

Y

E

D

A

A

S

K

E

Q

A

A

V

L

A

D

L

M

G

G

L

L

L

V

K

N

E

T

A

V

V

V

P

P

A

L

D

A

R

D

L

L

D

E

A

K

A

E

V

T

E

V

A

R

E

W

V

C

A

R

E

E

L

M

L

L

L

Q

A

N

A

S

P

P

G

M

A

A

I

L

A

R

A

C

T

L

K

K

R

A

L

A

I

L

R

-

Q

N

V

A

A

D

T

C

H

D

G

G

L

Q

E

A

D

G

N

L

L

Q

D

E

Y

L

T
x
A

A

G

R

N

A

A

L

T

A

M

D

L

A

F

W
x
Y

E

M

T

T

E

E

G

G

Q

Q

E

E

G

G

I

R

A

N

A

A

F

F

L

N

E

Q

K

K

R

R

K

Q

P

P

active site: G83 (= G74), L91 (vs. gap), G115 (= G122), V118 (≠ G125), G138 (≠ E145), S143 (≠ L150), D145 (≠ P152), G146 (≠ A153), A232 (≠ T239), Y240 (≠ W247)
binding nitrate ion: G114 (= G121), T137 (= T144), G138 (≠ E145), F144 (≠ L151), W166 (≠ M172)

Query Sequence

>WP_085125660.1 NCBI__GCF_900177295.1:WP_085125660.1
MTESYETPGTFETLKIERDARGVATLALDRPEVHNAFDETVIAELHRAAEALGADPAVRV
VVLTGEGRSFSAGGDLRWFRRQIESGREERLAGSAALAAMLRALDELPKPLIGRINGGAY
GGGTGLMAVCDVAIGVEGARFGLTEVRLGLLPANISPFVIARIGAANARRVMLSGRRFEA
SEAVALGLLKEAVPADRLDAAVEAEVAELLLAAPGAIAATKRLIRQVATHGLEDNLDYTA
RALADAWETEEGQEGIAAFLEKRKPGWQGA

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