SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_011320063.1 NCBI__GCF_000204075.1:WP_011320063.1 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)

2j5sA Structural of abdh, a beta-diketone hydrolase from the cyanobacterium anabaena sp. Pcc 7120 bound to (s)-3-oxocyclohexyl acetic acid (see paper)
97% identity, 99% coverage: 3:252/253 of query aligns to 1:250/250 of 2j5sA

query
sites
2j5sA

L

L

N

N

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active site: I73 (= I75), L78 (= L80), T90 (= T92), K95 (= K97), L118 (= L120), H119 (= H121), E121 (= E123), P141 (= P143), H142 (= H144), G150 (= G152), G235 (= G237)
binding (s)-cyclohexanone-2-acetate: H41 (= H43), F75 (= F77), H119 (= H121), P141 (= P143)

Q93TU6 6-oxocamphor hydrolase; OCH; Beta-diketone hydrolase; EC 3.7.1.18 from Rhodococcus sp. (see paper)
50% identity, 96% coverage: 7:250/253 of query aligns to 10:251/257 of Q93TU6

query
sites
Q93TU6

E

E

Y

Y

F

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K

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Y

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E

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L

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W40 (≠ F38) binding substrate
H122 (= H121) mutation to A: Great decrease of catalytic efficiency, and the binding affinity is five times that of the wild-type.
H145 (= H144) binding substrate; mutation to A: Very large decrease in the catalytic efficiency. 100-fold decrease in the binding affinity.
D154 (= D153) binding substrate; mutation to N: 100-fold decrease in the binding affinity.
E244 (= E243) binding substrate

1szoD Crystal structure analysis of the 6-oxo camphor hydrolase his122ala mutant bound to its natural product (2s,4s)-alpha-campholinic acid (see paper)
50% identity, 96% coverage: 7:250/253 of query aligns to 9:250/251 of 1szoD

query
sites
1szoD

E

E

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active site: I76 (= I75), F81 (≠ L80), I93 (≠ Y93), Q97 (≠ K97), N120 (≠ L120), A121 (≠ H121), E123 (= E123), P143 (= P143), H144 (= H144), G152 (= G152), S237 (≠ G237)
binding (2s,4s)-4-(2,2-dihydroxyethyl)-2,3,3-trimethylcyclopentanone: W39 (≠ F38), F81 (≠ L80), I92 (≠ T92), H144 (= H144), D153 (= D153), E243 (= E243)

6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
30% identity, 89% coverage: 21:244/253 of query aligns to 10:231/257 of 6slbAAA

query
sites
6slbAAA

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active site: Q64 (≠ I75), F69 (≠ L80), L80 (≠ Y93), N84 (≠ K97), A108 (≠ L120), S111 (≠ E123), A130 (≠ P143), F131 (≠ H144), L136 (≠ I149), P138 (= P151), D139 (≠ G152), A224 (≠ G237)
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 (≠ D69), A62 (= A73), Q64 (≠ I75), D65 (= D76), L66 (≠ F77), Y76 (≠ W89), A108 (≠ L120), F131 (≠ H144), D139 (≠ G152)

Sites not aligning to the query:

active site: 234

3rrvB Crystal structure of an enoyl-coa hydratase/isomerase from mycobacterium paratuberculosis (see paper)
29% identity, 75% coverage: 53:243/253 of query aligns to 45:234/254 of 3rrvB

query
sites
3rrvB

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A

G

S

I

L

G
x
D

Y

Y

G

A

L

L

A

S

L

A

E
|
E

active site: G67 (≠ I75), L72 (= L80), G89 (= G96), L114 (= L120), S117 (≠ E123), H137 (= H144), A145 (≠ G152), D228 (≠ G237)
binding calcium ion: H137 (= H144), D146 (= D153), E234 (= E243)

6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
29% identity, 89% coverage: 21:244/253 of query aligns to 7:219/245 of 6slaAAA

query
sites
6slaAAA

E

Q

N

D

G

G

I

V

L

L

E

V

V

L

R

T

M

L

H

N

T

R

N

P

N

E

G

K

S
x
L

L

N

V

A

F

I

T

T

G

G

K

E

T

L

H

L

R

D

E

A

F

L

P

Y

D

A

A

A

F

L

Y

K

D

E

I

G

S

E

R

E

D

D

R

R

D

E

N

V

R

R

V

A

V

L

I

L

L

L

T

T

G

G

T

A

G

G

D

R

A

A

W

F

M

S

A
|
A

E

G

I
x
Q

D
|
D

F
x
L

A

T

S

E

L

-

G

-

D

-

V

-

T

A

N

H

P
x
L

R

R

E

R

W
x
Y

D
x
N

K

R

T

-

Y

-

W

-

E

-

G

-

K

-

V

V

L

V

Q

E

N

A

L

L

L

S

D

G

I

L

E

E

V

K

P

P

V

L

I

V

S

V

A

A

V

V

N

N

G

G

-

V

A

A

A
|
A

L
x
G

L
x
A

H

G

S

M

E
x
S

Y

L

I

A

L

L

T

W

T

G

D

D

I

L

I

R

L

L

A

A

S

A

E

V

N

G

A

A

V

S

F

F

Q

-

D

T

M

T

P
x
A

H
x
F

F

V

N

R

A
x
I

G

G

I
x
L

V

V

P
|
P

G
x
N

D

S

G

G

V

L

H

S

I

F

L

L

W

L

P

P

L

R

A

L

L

V

G

G

L

L

Y

A

R

K

G

A

R

Q

Y

E

F

L

L

L

T

L

Q

S

E

P

K

R

L

L

T

S

A

A

Q

E

A

A

Y

L

E

A

L

L

N

G

V

L

V

V

H

H

E

R

V

V

L

V

P

P

Q

A

S

E

K

K

L

L

M

M

E

E

R

E

A

A

W

L

E

S

I

L

A

A

R

K

T

E

L

L

A

A

K

Q

Q

G

P

P

T

T

L

R

N

A

L

Y

R

A

Y

L

T

T

R

K

V

K

A

L

L

L

T

L

Q

E

R

T

L

Y

K

R

R

L

L

S

V

L

N

T

E

E

G

A

I

L

G
x
A

Y

L

G

E

L

A

A

V

L

L

E

Q

G

G

active site: Q61 (≠ I75), L68 (≠ P86), N72 (≠ D90), A96 (≠ L120), S99 (≠ E123), A118 (≠ P143), F119 (≠ H144), L124 (≠ I149), P126 (= P151), N127 (≠ G152), A212 (≠ G237)
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 (≠ S35), A59 (= A73), Q61 (≠ I75), D62 (= D76), L63 (≠ F77), L68 (≠ P86), Y71 (≠ W89), A94 (= A118), G95 (≠ L119), A96 (≠ L120), F119 (≠ H144), I122 (≠ A147), L124 (≠ I149), N127 (≠ G152)

Sites not aligning to the query:

5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
27% identity, 83% coverage: 37:245/253 of query aligns to 27:230/259 of 5zaiC

query
sites
5zaiC

V

A

F

L

T

N

G

A

K

K

T

L

H

L

R

E

E

E

F

L

P

D

D

R

A

A

F

V

Y

S

D

Q

I

A

S

E

R

S

D

D

R

P

D

E

N

I

R

R

V

V

V

I

I

I

L

I

T

T

G

G

T

K

G

G

D

K

A

A

W

F

M

C

A
|
A

E
x
G

I
x
A

D
|
D

F
x
I

A

T

S

Q

L
x
F

G

N

D

Q

V

L

T

T

N

P

P

A

R

E

E

A

W

W

D

-

K

K

T

F

Y
x
S

W

K

E

K

G

G

K
x
R

K

E

V

I

L

M

Q

D

N

K

L

I

L

E

D

A

I

L

E

S

V

K

P

P

V

T

I

I

S

A

A

M

V

I

N

N

G

G

A

Y

A

A

L

L

L

G

H
x
G

S

G

-

L

E
|
E

Y

L

I

A

L

L

T

A

T

C

D

D

I

I

I

R

L

I

A

A

S

A

E

E

N

E

A

A

V

Q

F

L

Q

-

D

G

M

L

P
|
P

H
x
E

F

I

N

N

A

L

G

G

I
|
I

V

Y

P
|
P

G
|
G

D

Y

G

G

V

G

H

T

I

Q

L

R

W

L

P

T

L

R

A

V

L

I

G

G

L

K

Y

G

R

R

G

A

R

L

Y

E

F

M

L

M

T

T

Q

G

E

D

K
x
R

L

I

T

P

A

G

Q

K

Q

D

A

A

Y

E

E

K

L

Y

N

G

V

L

V

V

H

N

E

R

V

V

L

V

P

P

Q

L

S

A

K

N

L

L

M

E

E

Q

R

E

A

T

W

R

E

K

I

L

A

A

R

E

T

K

L

I

A

A

K

K

Q

K

P

S

T

P

L

I

N

S

L

L

R

A

Y

L

T

-

R

-

V

-

A

-

L

-

T

-

Q

-

R

-

L

I

K

K

R

E

L

V

V

V

N

N

E

R

G

G

I

L

G

D

-

S

-

P

-

L

Y

S

G

G

L

L

A
|
A

L

L

E

E

G

S

I

V

active site: A65 (≠ I75), F70 (≠ L80), S82 (≠ Y93), R86 (≠ K97), G110 (≠ H121), E113 (= E123), P132 (= P143), E133 (≠ H144), I138 (= I149), P140 (= P151), G141 (= G152), A226 (= A241)
binding coenzyme a: A63 (= A73), G64 (≠ E74), A65 (≠ I75), D66 (= D76), I67 (≠ F77), P132 (= P143), R166 (≠ K177)

Sites not aligning to the query:

active site: 236
binding coenzyme a: 24, 25, 248, 251

3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
31% identity, 82% coverage: 46:253/253 of query aligns to 33:220/224 of 3p85A

query
sites
3p85A

F

F

P

F

D

G

A

A

F

L

Y

A

D

D

I

A

S

E

R

T

D
|
D

R

D

D
|
D

N

V

R

D

V

V

I

I

L

I

T

T

G

G

T

A

G

D

D

P

A

V

W

F

M

C

A

A

E

G

I
x
L

D

D

F

L

A

K

S

E

L
|
L

G
x
P

D

D

V

I

T

S

N

-

P

P

R

R

E

-

W

-

D

-

K

-

T

-

Y

-

W

W

E

P

G

A

K

-

V

-

L

-

Q

-

N

-

L

-

D

-

I

L

E

T

V

K

P

P

V

V

I

I

S

G

A

A

V

I

N

N

G

G

A

A

L

V

L

T

H
x
G

S

G

-

L

E
|
E

Y

L

I

A

L

L

T

Y

T

C

D

D

I

I

I

L

L

I

A

A

S

S

E

E

N

N

A

A

V

R

F

F

Q

A

D

D

M
x
T

P

-

H
|
H

F

A

N

R

A

V

G

G

I
x
L

V

L

P
|
P

G
x
T

D

W

G

G

V

L

H

S

I

V

L

R

W

L

P

P

L

Q

A

K

L

V

G

G

L

I

Y

G

R

L

G

A

R

R

Y

R

F

M

L

S

L

L

T

T

Q

G

E

D

K

Y

L

L

T

S

A

A

Q

A

Q

D

A

A

Y

L

E

R

L

A

N

G

V

L

V

V

H

T

E

E

V

V

L

V

P

P

Q

H

S

D

K

Q

L

L

M

L

E

G

R

A

A

A

W

R

E

A

I

V

A

A

R

A

T

S

L

I

A

V

K

G

Q

N

P

-

T

-

L

-

N

N

L

Q

R

N

Y

A

T

V

R

R

V

A

A

L

L

L

T

T

Q

S

R

-

L

Y

K

H

R

R

L

I

V

D

N

D

E

A

G

Q

I

T

G

S

Y

A

G

G

L

L

A
x
W

L

Q

E

E

G

A

I

M

T

A

A

A

T

R

D

Q

L

F

R

R

N
x
T

T

S

active site: L62 (≠ I75), L67 (= L80), P68 (≠ G81), G92 (≠ H121), E95 (= E123), T114 (≠ M142), H115 (= H144), L120 (≠ I149), P122 (= P151), T123 (≠ G152), W208 (≠ A241), T219 (≠ N252)
binding calcium ion: D43 (= D56), D45 (= D58)

3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
25% identity, 90% coverage: 12:238/253 of query aligns to 3:225/255 of 3q0jC

query
sites
3q0jC

Y

Y

E

E

N

T

L

I

H

L

F

V

H

E

R

R

D

D

E

Q

N

R

-

V

G

G

I

I

L

I

E

T

V

L

-

N

R

R

M

P

H
x
Q

T
x
A

N
x
L

N

N

G

-

S

-

L

-

V
x
A

F

L

T

N

G

S

K

Q

T

V

H

M

R

N

E

E

F

V

P

T

D

S

A

A

F

A

Y

T

D

E

I

L

S

D

R

D

D

D

R

P

D

D

N

I

R

G

V

A

V

I

I

I

L

I

T

T

G

G

T

S

G

A

D

K

A

A

W

F

M

A

A
|
A

E
x
G

I
x
A

D
|
D

F
x
I

A
x
K

S

E

L
x
M

G

A

D

D

V

L

T

T

N

F

P

A

R

D

E

A

W

F

D
x
T

K

A

T

D

Y

F

W
x
F

E

A

-

T

-

W

G

G

K

K

K

-

V

-

L

-

Q

-

N

-

L

L

L

A

D

A

I

V

E

R

V

T

P

P

V

T

I

I

S

A

A

A

V

V

N

A

G

G

A

Y

A

A

L

L

L
x
G

H
x
G

-

G

S

C

E
|
E

Y

L

I

A

L

M

T

M

T

C

D

D

I

V

I

L

L

I

A

A

S

A

E

D

N

T

A

A

V

K

F

F

Q

-

D

G

M

Q

P
|
P

H
x
E

F

I

N

K

A

L

G

G

I
x
V

V

L

P
|
P

G
|
G

D
x
M

G

G

V

G

H

S

I

Q

L

R

W

L

P

T

L

R

A

A

L

I

G

G

L

K

Y

A

R

K

G

A

R

M

Y

D

F

L

L

I

L

L

T

T

Q

G

E

R

K

T

L

M

T

D

A

A

Q

A

Q

E

A

A

Y

E

E

R

L

S

N

G

V

L

V

V

H

S

E

R

V

V

L

V

P

P

Q

A

S

D

K

D

L

L

M

L

E

T

R

E

A

A

W

R

E

A

I

T

A

A

R

T

T

T

L

I

A

S

K

Q

Q

M

P

S

T

A

L

S

N

A

L

A

R

R

Y

M

T

A

R

K

V

E

A

A

L

V

T

N

Q

R

R

A

L

F

K

E

R

S

L

S

V

L

N

S

E

E

G

G

I

L

G
x
L

Y

Y

active site: A65 (≠ I75), M70 (≠ L80), T80 (≠ D90), F84 (≠ W94), G108 (≠ H121), E111 (= E123), P130 (= P143), E131 (≠ H144), V136 (≠ I149), P138 (= P151), G139 (= G152), L224 (≠ G237)
binding acetoacetyl-coenzyme a: Q23 (≠ H30), A24 (≠ T31), L25 (≠ N32), A27 (≠ V37), A63 (= A73), G64 (≠ E74), A65 (≠ I75), D66 (= D76), I67 (≠ F77), K68 (≠ A78), M70 (≠ L80), F84 (≠ W94), G107 (≠ L120), G108 (≠ H121), E111 (= E123), P130 (= P143), E131 (≠ H144), P138 (= P151), G139 (= G152), M140 (≠ D153)

Sites not aligning to the query:

active site: 234

3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
25% identity, 90% coverage: 12:238/253 of query aligns to 3:225/255 of 3q0gC

query
sites
3q0gC

Y

Y

E

E

N

T

L

I

H

L

F

V

H

E

R

R

D

D

E

Q

N

R

-

V

G

G

I

I

L

I

E

T

V

L

-

N

R

R

M

P

H

Q

T

A

N
x
L

N

N

G

-

S

-

L

-

V

A

F

L

T

N

G

S

K

Q

T

V

H

M

R

N

E

E

F

V

P

T

D

S

A

A

F

A

Y

T

D

E

I

L

S

D

R

D

D

D

R

P

D

D

N

I

R

G

V

A

V

I

I

I

L

I

T

T

G

G

T

S

G

A

D

K

A

A

W

F

M

A

A
|
A

E

G

I
x
A

D

D

F
x
I

A
x
K

S

E

L
x
M

G

A

D

D

V

L

T

T

N

F

P

A

R

D

E

A

W

F

D
x
T

K

A

T

D

Y

F

W
x
F

E

A

-

T

-

W

G

G

K

K

K

-

V

-

L

-

Q

-

N

-

L

L

L

A

D

A

I

V

E

R

V

T

P

P

V

T

I

I

S

A

A

A

V

V

N

A

G

G

A
x
Y

A

A

L

L

L

G

H
x
G

-

G

S

C

E
|
E

Y

L

I

A

L

M

T

M

T

C

D

D

I

V

I

L

L

I

A

A

S

A

E

D

N

T

A

A

V

K

F

F

Q

-

D

G

M

Q

P
|
P

H
x
E

F

I

N

K

A
x
L

G

G

I
x
V

V

L

P
|
P

G
|
G

D

M

G

G

V

G

H

S

I

Q

L

R

W

L

P

T

L

R

A

A

L

I

G

G

L

K

Y

A

R

K

G

A

R

M

Y

D

F

L

L

I

L

L

T

T

Q

G

E

R

K

T

L

M

T

D

A

A

Q

A

Q

E

A

A

Y

E

E

R

L

S

N

G

V

L

V

V

H

S

E

R

V

V

L

V

P

P

Q

A

S

D

K

D

L

L

M

L

E

T

R

E

A

A

W

R

E

A

I

T

A

A

R

T

T

T

L

I

A

S

K

Q

Q

M

P

S

T

A

L

S

N

A

L

A

R

R

Y

M

T

A

R

K

V

E

A

A

L

V

T

N

Q

R

R

A

L

F

K

E

R

S

L

S

V

L

N

S

E

E

G

G

I

L

G
x
L

Y

Y

active site: A65 (≠ I75), M70 (≠ L80), T80 (≠ D90), F84 (≠ W94), G108 (≠ H121), E111 (= E123), P130 (= P143), E131 (≠ H144), V136 (≠ I149), P138 (= P151), G139 (= G152), L224 (≠ G237)
binding coenzyme a: L25 (≠ N32), A63 (= A73), I67 (≠ F77), K68 (≠ A78), Y104 (≠ A117), P130 (= P143), E131 (≠ H144), L134 (≠ A147)

Sites not aligning to the query:

active site: 234

3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
25% identity, 90% coverage: 12:238/253 of query aligns to 2:224/256 of 3h81A

query
sites
3h81A

Y

Y

E

E

N

T

L

I

H

L

F

V

H

E

R

R

D

D

E

Q

N

R

-

V

G

G

I

I

L

I

E

T

V

L

-

N

R

R

M

P

H

Q

T

A

N

L

N

N

G

-

S

-

L

-

V

A

F

L

T

N

G

S

K

Q

T

V

H

M

R

N

E

E

F

V

P

T

D

S

A

A

F

A

Y

T

D

E

I

L

S

D

R

D

D

D

R

P

D

D

N

I

R

G

V

A

V

I

I

I

L

I

T

T

G

G

T

S

G

A

D

K

A

A

W

F

M

A

A

A

E

G

I
x
A

D

D

F

I

A

K

S

E

L
x
M

G

A

D

D

V

L

T

T

N

F

P

A

R

D

E

A

W

F

D
x
T

K

A

T

D

Y

F

W
x
F

E

A

-

T

-

W

G

G

K

K

K

-

V

-

L

-

Q

-

N

-

L

L

L

A

D

A

I

V

E

R

V

T

P

P

V

T

I

I

S

A

A

A

V

V

N

A

G

G

A

Y

A

A

L

L

L

G

H
x
G

-

G

S

C

E
|
E

Y

L

I

A

L

M

T

M

T

C

D

D

I

V

I

L

L

I

A

A

S

A

E

D

N

T

A

A

V

K

F

F

Q

-

D

G

M

Q

P
|
P

H
x
E

F

I

N

K

A

L

G

G

I
x
V

V

L

P
|
P

G
|
G

D

M

G

G

V

G

H

S

I

Q

L

R

W

L

P

T

L

R

A

A

L

I

G

G

L

K

Y

A

R

K

G

A

R

M

Y

D

F

L

L

I

L

L

T

T

Q

G

E

R

K

T

L

M

T

D

A

A

Q

A

Q

E

A

A

Y

E

E

R

L

S

N

G

V

L

V

V

H

S

E

R

V

V

L

V

P

P

Q

A

S

D

K

D

L

L

M

L

E

T

R

E

A

A

W

R

E

A

I

T

A

A

R

T

T

T

L

I

A

S

K

Q

Q

M

P

S

T

A

L

S

N

A

L

A

R

R

Y

M

T

A

R

K

V

E

A

A

L

V

T

N

Q

R

R

A

L

F

K

E

R

S

L

S

V

L

N

S

E

E

G

G

I

L

G
x
L

Y

Y

active site: A64 (≠ I75), M69 (≠ L80), T79 (≠ D90), F83 (≠ W94), G107 (≠ H121), E110 (= E123), P129 (= P143), E130 (≠ H144), V135 (≠ I149), P137 (= P151), G138 (= G152), L223 (≠ G237)

Sites not aligning to the query:

active site: 233
binding calcium ion: 233, 238

6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
27% identity, 61% coverage: 53:207/253 of query aligns to 40:200/707 of 6yswA

query
sites
6yswA

I

I

S

K

R

Q

D

L

R

R

D

E

N

N

R

K

-

E

-

L

-

R

-

G

V

V

I

F

L

V

T

S

G

A

T

K

G

P

D

D

A

N

W

F

M

I

A

A

E

G

I
x
A

D
|
D

F
x
I

A

N

S

M

L
x
I

G

G

D

N

V

C

T

K

N

T

P

A

R

Q

E

E

W

A

D

E

K

A

T

L

Y
x
A

W

R

E

Q

G

G

K
x
Q

K

Q

V

L

L

M

Q

A

N

E

L

I

L

H

D

A

I

L

E

P

V

I

P

Q

V

V

I

I

S

A

A

A

V

I

N

H

G

G

A

A

A

C

L

L

L

G

H
x
G

S

G

E

-

Y

-

I

-

L

-

T

-

T

L

D
x
E

I

L

I

A

L

L

A

A

S

C

E

H

N

G

A

R

V

V

F

C

Q

T

D

D

-

D

-

P

-

K

-

T

-

V

-

L

-

G

M

L

P
|
P

H
x
E

F

V

N

Q

A
x
L

G

G

I

L

V

L

P

P

G
|
G

D

S

G

G

V

G

H

T

I

Q

L

R

W

L

P

P

L

R

A

L

L

I

G

G

L

V

Y

S

R

T

G

A

R

L

Y

E

F

M

L

I

L

L

T

T

Q

G

E

K

K

Q

L

L

T

R

A

A

Q

K

Q

Q

A

A

Y

L

E

K

L

L

N

G

V

L

V

V

H

D

E

D

V

V

L

V

P

P

Q

H

S

S

K

I

L

L

M

L

E

E

R

A

A

A

W

V

E

E

I

L

A

A

R

K

active site: A66 (≠ I75), I71 (≠ L80), A84 (≠ Y93), Q88 (≠ K97), G112 (≠ H121), E115 (≠ D129), P136 (= P143), E137 (≠ H144), G145 (= G152)
binding coenzyme a: A66 (≠ I75), D67 (= D76), I68 (≠ F77), P136 (= P143), E137 (≠ H144), L140 (≠ A147)

Sites not aligning to the query:

active site: 264, 422, 443, 455, 493
binding coenzyme a: 23, 25, 290, 293

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)
25% identity, 79% coverage: 21:221/253 of query aligns to 16:220/276 of O69762

query
sites
O69762

E

E

N

D

G

G

I

I

L

A

E

F

V

V

R

I

M

L

H

N

T

R

N

P

N

E

G
x
K

S

R

L

N

V

A

F

M

T

S

G

P

K

T

T

L

H

N

R

R

E

E

F

M

P

I

D

D

A

V

F

L

Y

E

D

T

I

L

S

E

R

Q

D

D

R

P

D

A

N

A

R

G

V

V

V

L

I

V

L

L

T

T

G

G

T

A

G

G

D

E

A

A

W

W

M

T

A
|
A

E

G

I
x
M

D

D

F
x
L

A

-

S

-

L

-

G

-

D

-

V

-

T

-

N

-

P

-

R

K

E

E

W
x
Y

D

F

K

R

T

E

Y

V

W

D

E

A

G

G

K

P

K

E

V

I

L

L

Q

Q

N

E

L

K

L

I

D

R

I

R

E

E

V

A

-

S

-

Q

-

W

-

Q

-

W

-

K

-

L

-

R

-

M

-

Y

-

A

-

K

P

P

V

T

I

I

S

A

A

M

V

V

N

N

G

G

A

W

A

C

L

F

L

G

H
x
G

S

G

-

F

E
x
S

Y

P

I

L

L

V

T

A

T

C

D

D

I

L

I

A

L

I

A

C

S

A

E

D

N

E

A

A

V

T

F

F

Q

-

D

G

M

L

P
x
S

H
x
E

F

I

N

N

A
x
W

G

G

I

I

V

P

P

P

G
|
G

D

N

G

L

V

V

H

S

I

K

L

A

W

M

P

A

L

D

A

T

L

V

G

G

L

H

Y

R

R

Q

G

S

R

L

Y

Y

F

Y

L

I

L

M

T

T

Q

G

E

K

K

T

L

F

T

G

A

G

Q

Q

Q

K

A

A

Y

A

E

E

L

M

N

G

V

L

V

V

H

N

E

E

V

S

L

V

P

P

Q

L

S

A

K

Q

L

L

M

R

E

E

R

V

A

T

W

I

E

E

I

L

A

A

R

R

T

N

L

L

A

L

K

E

Q

K

P

N

T

P

L

V

N

V

L

L

R

R

Y

A

T

A

R

K

K29 (≠ G34) binding acetyl-CoA
A68 (= A73) binding acetyl-CoA
M70 (≠ I75) binding acetyl-CoA
L72 (≠ F77) binding acetyl-CoA
Y75 (≠ W89) binding vanillin
G120 (≠ H121) binding acetyl-CoA
S123 (≠ E123) mutation to A: Reduced kcat compared to wild-type but not markerdly.
S142 (≠ P143) binding acetyl-CoA
E143 (≠ H144) mutation to A: Abolishes catalytic activity.
W146 (≠ A147) binding acetyl-CoA
G151 (= G152) binding vanillin

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
239 binding vanillin; Y→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)
25% identity, 79% coverage: 21:221/253 of query aligns to 13:217/247 of 2vssB

query
sites
2vssB

E

E

N

D

G

G

I

I

L

A

E

F

V

V

R

I

M

L

H

N

T

R

N

P

N
x
E

G
x
K

S
x
R

L

N

V
x
A

F

M

T

S

G

P

K

T

T

L

H

N

R

R

E

E

F

M

P

I

D

D

A

V

F

L

Y

E

D

T

I

L

S

E

R

Q

D

D

R

P

D

A

N

A

R

G

V

V

V

L

I

V

L

L

T

T

G

G

T

A

G

G

D

E

A

A

W

W

M

T

A
|
A

E

G

I
x
M

D
|
D

F

L

A

-

S

-

L

-

G

-

D

-

V

-

T

-

N

-

P

-

R

K

E

E

W
x
Y

D

F

K

R

T

E

Y

V

W
x
D

E

A

G

G

K

P

K

E

V

I

L

L

Q

Q

N

E

L

K

L

I

D

R

I
x
R

E

E

V

A

-

S

-
x
Q

-

W

-

Q

-

W

-

K

-

L

-

R

-

M

-

Y

-

A

-

K

P

P

V

T

I

I

S

A

A

M

V

V

N

N

G

G

A
x
W

A

C

L
x
F

L

G

H
x
G

S

G

-

F

E
x
S

Y

P

I

L

L

V

T

A

T

C

D

D

I

L

I

A

L

I

A

C

S

A

E

D

N

E

A

A

V

T

F

F

Q

-

D

G

M

L

P
x
S

H
x
E

F

I

N

N

A

W

G

G

I
|
I

V

P

P
|
P

G
|
G

D

N

G

L

V

V

H

S

I

K

L

A

W

M

P

A

L

D

A

T

L

V

G

G

L

H

Y

R

R

Q

G

S

R

L

Y

Y

F

Y

L

I

L

M

T

T

Q

G

E

K

K

T

L

F

T

G

A

G

Q

Q

Q

K

A

A

Y

A

E

E

L

M

N

G

V

L

V

V

H

N

E

E

V

S

L

V

P

P

Q

L

S

A

K

Q

L

L

M

R

E

E

R

V

A

T

W

I

E

E

I

L

A

A

R

R

T

N

L

L

A

L

K

E

Q

K

P

N

T

P

L

V

N

V

L

L

R

R

Y

A

T

A

R

K

active site: M67 (≠ I75), Y72 (≠ W89), D77 (≠ W94), R89 (≠ I106), Q93 (vs. gap), G117 (≠ H121), S120 (≠ E123), S139 (≠ P143), E140 (≠ H144), I145 (= I149), P147 (= P151), G148 (= G152)
binding acetyl coenzyme *a: E25 (≠ N33), K26 (≠ G34), R27 (≠ S35), A29 (≠ V37), A65 (= A73), M67 (≠ I75), D68 (= D76), W113 (≠ A117), F115 (≠ L119), G117 (≠ H121), S139 (≠ P143), E140 (≠ H144)

Sites not aligning to the query:

active site: 236, 246

2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
25% identity, 79% coverage: 21:221/253 of query aligns to 14:218/246 of 2vssD

query
sites
2vssD

E

E

N

D

G

G

I

I

L

A

E

F

V

V

R

I

M

L

H

N

T

R

N

P

N
x
E

G
x
K

S
x
R

L

N

V
x
A

F

M

T

S

G

P

K

T

T

L

H

N

R

R

E

E

F

M

P

I

D

D

A

V

F

L

Y

E

D

T

I

L

S

E

R

Q

D

D

R

P

D

A

N

A

R

G

V

V

V

L

I

V

L

L

T

T

G

G

T

A

G

G

D

E

A

A

W

W

M

T

A
|
A

E

G

I
x
M

D
|
D

F
x
L

A

-

S

-

L

-

G

-

D

-

V

-

T

-

N

-

P

-

R

K

E

E

W
x
Y

D
x
F

K

R

T

E

Y

V

W
x
D

E

A

G

G

K

P

K

E

V

I

L

L

Q

Q

N

E

L

K

L

I

D

R

I
x
R

E

E

V

A

-

S

-
x
Q

-

W

-
x
Q

-

W

-

K

-

L

-

R

-

M

-

Y

-

A

-

K

P

P

V

T

I

I

S

A

A

M

V

V

N

N

G

G

A
x
W

A

C

L
x
F

L

G

H
x
G

S

G

-

F

E
x
S

Y

P

I

L

L

V

T

A

T

C

D

D

I

L

I

A

L

I

A

C

S

A

E

D

N

E

A

A

V

T

F

F

Q

-

D

G

M

L

P
x
S

H
x
E

F

I

N

N

A

W

G

G

I
|
I

V

P

P
|
P

G
|
G

D
x
N

G

L

V

V

H

S

I

K

L

A

W

M

P

A

L

D

A

T

L

V

G

G

L

H

Y

R

R

Q

G

S

R

L

Y

Y

F

Y

L

I

L

M

T

T

Q

G

E

K

K

T

L

F

T

G

A

G

Q

Q

Q

K

A

A

Y

A

E

E

L

M

N

G

V

L

V

V

H

N

E

E

V

S

L

V

P

P

Q

L

S

A

K

Q

L

L

M

R

E

E

R

V

A

T

W

I

E

E

I

L

A

A

R

R

T

N

L

L

A

L

K

E

Q

K

P

N

T

P

L

V

N

V

L

L

R

R

Y

A

T

A

R

K

active site: M68 (≠ I75), Y73 (≠ W89), D78 (≠ W94), R90 (≠ I106), Q94 (vs. gap), G118 (≠ H121), S121 (≠ E123), S140 (≠ P143), E141 (≠ H144), I146 (= I149), P148 (= P151), G149 (= G152)
binding acetyl coenzyme *a: E26 (≠ N33), K27 (≠ G34), R28 (≠ S35), A30 (≠ V37), A66 (= A73), M68 (≠ I75), D69 (= D76), L70 (≠ F77), F74 (≠ D90), W114 (≠ A117), F116 (≠ L119), S140 (≠ P143)
binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ I75), Y73 (≠ W89), F74 (≠ D90), Q96 (vs. gap), E141 (≠ H144), G149 (= G152), N150 (≠ D153)

Sites not aligning to the query:

active site: 237

1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
27% identity, 78% coverage: 18:214/253 of query aligns to 7:207/269 of 1jxzB

query
sites
1jxzB

H

H

R

R

D

V

E

E

N

D

G

G

I

V

L

A

E

E

V

I

R

T

M

I

H

K

T

L

N

P

N
x
R

G
x
H

S
x
R

L

N

V

A

F

L

T

S

G

V

K

K

T

A

H

M

R

Q

E

E

F

V

P

T

D

D

A

A

F

L

Y

N

D

R

I

A

S

E

R

E

D

D

R

D

D

S

N

V

R
x
G

V

A

V

V

I

M

L

I

T

T

G

G

T

A

G

E

D

D

A

A

W

F

M
x
C

A
|
A

-

G

-
x
F

-
x
Y

-
x
L

-
x
R

E

E

I
|
I

D

P

F

L

-

D

A

K

S

G

L

V

G

A

D

G

V

V

T

R

N

D

P

H

R

F

E

R

W

I

D

A

K
x
A

T

L

Y

W

W
|
W

E
x
Q

G

-

K

-

K

Q

V

M

L

I

Q

H

N

K

L

I

D

R

I

V

E

K

V

R

P

P

V

V

I

L

S

A

A

A

V

I

N

N

G

G

A

V

A

A

L

A

L
x
G

H
x
G

S

G

E

L

Y
x
G

I

I

-

S

L

L

T

A

T

S

D

D

I

M

I

A

L

I

A

C

S

A

E

D

N

S

A

A

V

K

F

F

Q

V

D

C

M
x
A

P
x
W

H

H

F

-

N

T

A

I

G

G

I
|
I

V

-

P

-

G

G

D
x
N

G
x
D

V
x
T

H

A

I

T

L

S

W

Y

P

S

L

L

A

A

-

R

-

I

L

V

G

G

L

M

Y

R

R

R

G

A

R

M

Y

E

F

L

L

M

L

L

T

T

Q

N

E

R

K

T

L

L

T

Y

A

P

Q

E

A

A

Y

K

E

D

L

W

N

G

V

L

V

V

H

S

E

R

V

V

L

Y

P

P

Q

K

S

D

K

E

L

F

M

R

E

E

R

V

A

A

W

W

E

K

I

V

A

A

R

R

T

E

L
|
L

A
|
A

K

A

Q
x
A

P

P

T
|
T

active site: C61 (≠ M72), F64 (vs. gap), I69 (= I75), A86 (≠ K91), Q90 (≠ E95), G113 (≠ L120), G114 (≠ H121), G117 (≠ Y124), A136 (≠ M142), W137 (≠ P143), I142 (= I149), N144 (≠ D153), D145 (≠ G154)
binding 4-hydroxybenzoyl coenzyme a: R22 (≠ N33), H23 (≠ G34), R24 (≠ S35), A62 (= A73), F64 (vs. gap), Y65 (vs. gap), L66 (vs. gap), R67 (vs. gap), W89 (= W94), G113 (≠ L120), A136 (≠ M142), W137 (≠ P143), I142 (= I149), D145 (≠ G154), T146 (≠ V155)
binding calcium ion: G49 (≠ R60), L202 (= L209), A203 (= A210), A205 (≠ Q212), T207 (= T214)

Sites not aligning to the query:

active site: 230
binding 4-hydroxybenzoyl coenzyme a: 252, 257
binding calcium ion: 210

1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
27% identity, 78% coverage: 18:214/253 of query aligns to 7:207/269 of 1nzyB

query
sites
1nzyB

H

H

R

R

D

V

E

E

N

D

G

G

I

V

L

A

E

E

V

I

R

T

M

I

H

K

T

L

N

P

N
x
R

G
x
H

S
x
R

L

N

V

A

F

L

T

S

G

V

K

K

T

A

H

M

R

Q

E

E

F

V

P

T

D

D

A

A

F

L

Y

N

D

R

I

A

S

E

R

E

D

D

R

D

D

S

N

V

R
x
G

V

A

V

V

I

M

L

I

T

T

G

G

T

A

G
x
E

D

D

A

A

W

F

M
x
C

A
|
A

-

G

-
x
F

-
x
Y

-
x
L

-
x
R

E

E

I
|
I

D

P

F

L

-

D

A

K

S

G

L

V

G

A

D

G

V

V

T

R

N

D

P

H

R

F

E

R

W

I

D

A

K
x
A

T

L

Y

W

W
|
W

E
x
H

G

-

K

-

K

Q

V

M

L

I

Q

H

N

K

L

I

D

R

I

V

E

K

V

R

P

P

V

V

I

L

S

A

A

A

V

I

N
|
N

G

G

A

V

A

A

L

A

L
x
G

H
x
G

S

G

E

L

Y
x
G

I

I

-

S

L

L

T

A

T

S

D

D

I

M

I

A

L

I

A

C

S

A

E

D

N

S

A

A

V

K

F

F

Q

V

D

C

M
x
A

P
x
W

H

H

F

-

N

T

A

I

G

G

I
|
I

V

-

P

-

G

G

D
x
N

G
x
D

V
x
T

H

A

I

T

L

S

W

Y

P

S

L

L

A

A

-

R

-

I

L

V

G

G

L

M

Y

R

R

R

G

A

R

M

Y

E

F

L

L

M

L

L

T

T

Q

D

E

R

K

T

L

L

T

Y

A

P

Q

E

A

A

Y

K

E

D

L

W

N

G

V

L

V

V

H

S

E

R

V

V

L

Y

P

P

Q
x
K

S

D

K

E

L

F

M
x
R

E

E

R

V

A

A

W

W

E

K

I

V

A

A

R

R

T

E

L
|
L

A
|
A

K

A

Q
x
A

P

P

T
|
T

active site: C61 (≠ M72), F64 (vs. gap), I69 (= I75), A86 (≠ K91), H90 (≠ E95), G114 (≠ H121), G117 (≠ Y124), A136 (≠ M142), W137 (≠ P143), I142 (= I149), N144 (≠ D153), D145 (≠ G154)
binding 4-hydroxybenzoyl coenzyme a: R22 (≠ N33), H23 (≠ G34), R24 (≠ S35), A62 (= A73), F64 (vs. gap), Y65 (vs. gap), L66 (vs. gap), R67 (vs. gap), W89 (= W94), G113 (≠ L120), G114 (≠ H121), A136 (≠ M142), W137 (≠ P143), D145 (≠ G154), T146 (≠ V155)
binding calcium ion: G49 (≠ R60), L202 (= L209), A203 (= A210), A205 (≠ Q212), T207 (= T214)
binding phosphate ion: E57 (≠ G68), N108 (= N115), K188 (≠ Q195), R192 (≠ M199)

Sites not aligning to the query:

active site: 230
binding 4-hydroxybenzoyl coenzyme a: 252, 257
binding calcium ion: 210

3pe8A Crystal structure of enoyl-coa hydratase from mycobacterium smegmatis (see paper)
37% identity, 42% coverage: 105:209/253 of query aligns to 74:178/219 of 3pe8A

query
sites
3pe8A

D

D

I

M

E

T

V

K

P

P

V

V

I

I

S

G

A

A

V

I

N

N

G

G

A

A

L

V

L

T

H
x
G

S

G

-

L

E
|
E

Y

L

I

A

L

L

T

Y

T

C

D

D

I

I

I

L

L

I

A

A

S

S

E

E

N

N

A

A

V

K

F

F

Q

A

D

D

M
x
T

P

-

H
|
H

F

A

N

R

A

V

G

G

I
x
L

V

M

P
|
P

G
x
T

D

W

G

G

V

L

H

S

I

V

L

R

W

L

P

P

L

Q

A

K

L

V

G

G

L

V

Y

G

R

L

G

A

R

R

Y

R

F

M

L

S

L

L

T

T

Q

G

E

D

K

Y

L

L

T

S

A

A

Q

Q

Q

D

A

A

Y

L

E

R

L

A

N

G

V

L

V

V

H

T

E

E

V

V

L

V

P

A

Q

H

S

D

K

D

L

L

M

L

E

T

R

A

A

A

W

R

E

R

I

V

A

A

R

A

T

S

L

I

active site: G90 (≠ H121), E93 (= E123), T112 (≠ M142), H113 (= H144), L118 (≠ I149), P120 (= P151), T121 (≠ G152)
binding zinc ion: E93 (= E123), H113 (= H144)

Sites not aligning to the query:

active site: 63, 68, 206, 219

A5JTM5 4-chlorobenzoyl coenzyme A dehalogenase; 4-CBA-CoA dehalogenase; 4-CBCoA dehalogenase; 4-chlorobenzoyl-CoA dehalogenase; EC 3.8.1.7 from Pseudomonas sp. (strain CBS-3) (see 7 papers)
27% identity, 78% coverage: 18:214/253 of query aligns to 7:207/269 of A5JTM5

query
sites
A5JTM5

H

H

R

R

D

V

E

E

N

D

G

G

I

V

L

A

E

E

V

I

R

T

M

I

H

K

T

L

N

P

N

R

G

H

S
x
R

L

N

V

A

F

L

T

S

G

V

K

K

T

A

H

M

R

Q

E
|
E

F

V

P

T

D

D

A

A

F

L

Y

N

D

R

I

A

S
x
E

R

E

D
|
D

R
x
D

D

S

N

V

R

G

V

A

V

V

I

M

L

I

T

T

G

G

T

A

G

E

D

D

A

A

W

F

M

C

A

A

-
x
G

-
x
F

-
x
Y

-

L

-
x
R

E
|
E

I

I

D

P

F

L

-

D

A

K

S

G

L

V

G

A

D

G

V

V

T

R

N

D

P
x
H

R
x
F

E

R

W

I

D

G

K

A

T

L

Y

W

W
|
W

E
x
H

G

-

K

-

K

Q

V

M

L

I

Q
x
H

N

K

L

I

D

R

I

V

E

K

V

R

P

P

V

V

I

L

S

A

A

A

V

I

N

N

G

G

A

V

A

A

L
x
A

L
x
G

H
x
G

S
x
G

E

L

Y

G

I

I

-

S

L

L

T

A

T

S

D
|
D

I

M

I

A

L

I

A

C

S

A

E
x
D

N

S

A

A

V

K

F

F

Q

V

D

C

M

A

P
x
W

H

H

F

-

N

T

A

I

G

G

I

I

V

-

P

-

G

G

D

N

G
x
D

V

T

H

A

I

T

L

S

W

Y

P

S

L

L

A

A

-

R

-

I

L

V

G

G

L

M

Y

R

R

R

G

A

R

M

Y
x
E

F

L

L

M

L

L

T

T

Q

N

E

R

K

T

L

L

T

Y

A

P

Q

E

Q
x
E

A

A

Y

K

E

D

L
x
W

N

G

V

L

V

V

H

S

E

R

V

V

L

Y

P

P

Q

K

S

D

K

D

L

F

M

R

E

E

R

V

A

A

W

W

E

K

I

V

A

A

R

R

T

E

L

L

A

A

K

A

Q

A

P

P

T

T

R24 (≠ S35) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
E34 (= E45) mutation to T: Forms inclusion bodies.
E43 (≠ S54) mutation to A: No effect on catalytic activity.
D45 (= D56) mutation to A: No effect on catalytic activity.
D46 (≠ R57) mutation to A: No effect on catalytic activity.
G63 (vs. gap) mutation G->A,I,P: Yields insoluble protein.
F64 (vs. gap) mutation to A: 30-fold reduction in catalytic activity, substrate benzoyl group binding is unaffected.; mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to P: Severely reduces catalytic activity. Arylated intermediate does not accumulate.
Y65 (vs. gap) mutation to D: Catalytic activity is almost as efficient as wild type.
R67 (vs. gap) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
E68 (= E74) mutation to T: No effect on catalytic activity.
H81 (≠ P86) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
F82 (≠ R87) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
W89 (= W94) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
H90 (≠ E95) active site, Proton acceptor; mutation to Q: Complete loss of catalytic activity (PubMed:8718880, PubMed:9063883). Significantly reduced activity (PubMed:11695894). Substrate binding is not significantly affected. Reduced arylated intermediate formation.
H94 (≠ Q101) mutation to Q: No effect on catalytic activity.
A112 (≠ L119) mutation to G: Yields insoluble protein.; mutation to S: Protein precipitates upon purification.; mutation to V: Catalytic activity is almost as efficient as wild type.
G113 (≠ L120) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding. Arylated intermediate does not accumulate.; mutation G->N,S: Strongly reduced catalytic activity. Arylated intermediate does not accumulate.; mutation to V: Protein precipitates upon purification.
G114 (≠ H121) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
G115 (≠ S122) mutation G->L,N,S,V: Yields insoluble protein.
D123 (= D129) mutation to T: No effect on catalytic activity.
D129 (≠ E135) mutation to T: No effect on catalytic activity.
W137 (≠ P143) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
D145 (≠ G154) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
E163 (≠ Y170) mutation to T: No effect on catalytic activity.
E175 (≠ Q182) mutation to D: No effect on catalytic activity.
W179 (≠ L186) mutation to F: No effect on catalytic activity.

Sites not aligning to the query:

208 H→Q: No effect on catalytic activity.
216 mutation R->E,K,L: Yields insoluble protein.
232 mutation E->A,N,Q,R: Yields insoluble protein.; E→D: Reduced catalytic activity, increased substrate binding.
257 R→K: Retains catalytic activity and substrate CoA binding.; R→L: Significantly reduces catalytic activity and substrate CoA binding.

2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
26% identity, 75% coverage: 45:235/253 of query aligns to 37:219/254 of 2dubA

query
sites
2dubA

E

E

F

L

P

N

D

Q

A

A

F

L

Y

E

D

T

I

F

S

E

R

E

D

D

R

P

D

A

N

V

R

G

V

A

V

I

I

V

L

L

T

T

G

G

T

G

G

E

D

K

A

A

W

F

M

A

A
|
A

E

G

I
x
A

D
|
D

F
x
I

A
x
K

S

E

L
x
M

G

Q

D

N

V

R

T

T

N

F

P

Q

R

D

E

C

W

Y

D

-

K

-

T
x
S

Y

H

W

W

E

D

G

-

K

-

V

-

L

-

Q

-

N

H

L

I

L

T

D

R

I

I

E

K

V

K

P

P

V

V

I

I

S

A

A

A

V

V

N

N

G

G

A

Y

A

A

L

L

L

G

H
x
G

-

G

S

C

E
|
E

Y

L

I

A

L

M

T

M

T

C

D

D

I

I

L

Y

A

A

S

G

E

E

N

K

A

A

V

Q

F

F

Q

-

D

G

M

Q

P
|
P

H
x
E

F

I

N

L

A

L

G

G

I
x
T

V

I

P
|
P

G
|
G

D
x
A

G

G

V

G

H

T

I

Q

L

R

W

L

P

T

L

R

A

A

L

V

G

G

L

K

Y

S

R

L

G

A

R

M

Y

E

F

M

L

V

L

L

T

T

Q

G

E

D

K

R

L

I

T

S

A

A

Q

Q

Q

D

A

A

Y

K

E

Q

L

A

N

G

V

L

V

V

H

S

E

K

V

I

L

F

P

P

Q

V

S

E

K

T

L

L

M

V

E

E

R

E

A

A

W

I

E

Q

I

C

A

A

R

E

T

K

L

I

A

A

K

N

Q

N

P

S

T

K

L

I

N

I

L

V

R

A

Y

M

T

A

R

K

V

E

A

S

L

V

T

N

Q

A

R

A

L

F

K

E

R

M

L

T

V

L

N

T

E

E

G

G

active site: A67 (≠ I75), M72 (≠ L80), S82 (≠ T92), G105 (≠ H121), E108 (= E123), P127 (= P143), E128 (≠ H144), T133 (≠ I149), P135 (= P151), G136 (= G152)
binding octanoyl-coenzyme a: A65 (= A73), A67 (≠ I75), D68 (= D76), I69 (≠ F77), K70 (≠ A78), G105 (≠ H121), E108 (= E123), P127 (= P143), E128 (≠ H144), G136 (= G152), A137 (≠ D153)

Sites not aligning to the query:

active site: 221, 231
binding octanoyl-coenzyme a: 25, 26, 27, 29

Query Sequence

>WP_011320063.1 NCBI__GCF_000204075.1:WP_011320063.1
MTLNQPEYFTKYENLHFHRDENGILEVRMHTNNGSLVFTGKTHREFPDAFYDISRDRDNR
VVILTGTGDAWMAEIDFASLGDVTNPREWDKTYWEGKKVLQNLLDIEVPVISAVNGAALL
HSEYILTTDIILASENAVFQDMPHFNAGIVPGDGVHILWPLALGLYRGRYFLLTQEKLTA
QQAYELNVVHEVLPQSKLMERAWEIARTLAKQPTLNLRYTRVALTQRLKRLVNEGIGYGL
ALEGITATDLRNT

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