SitesBLAST

Q9LBG2 Levodione reductase; (6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase; EC 1.1.1.- from Leifsonia aquatica (Corynebacterium aquaticum) (see paper)
36% identity, 97% coverage: 8:271/273 of query aligns to 1:267/267 of Q9LBG2

query
sites
Q9LBG2

L

M

P

T

A

A

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T

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S

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S

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P

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Y

-

G

-

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N

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L

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N

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N

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Y

17:42 (vs. 26:51, 35% identical) binding NAD(+)
E103 (≠ N110) mutation E->A,D,N,Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products.

1iy8A Crystal structure of levodione reductase (see paper)
36% identity, 93% coverage: 19:271/273 of query aligns to 1:258/258 of 1iy8A

query
sites
1iy8A

R

R

L

F

N

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G

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L

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x
M

N

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L

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-

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D

P

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A

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-

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Y

active site: G15 (= G33), S143 (= S158), Q153 (≠ C168), Y156 (= Y171), K160 (= K175)
binding nicotinamide-adenine-dinucleotide: G11 (= G29), S14 (≠ Q32), G15 (= G33), L16 (≠ I34), D35 (= D53), V36 (≠ I54), A62 (≠ V78), D63 (= D79), V64 (≠ I80), N90 (≠ C106), G92 (= G108), I93 (≠ V109), T141 (≠ I156), S143 (= S158), Y156 (= Y171), K160 (= K175), P186 (= P201), G187 (= G202), T191 (= T206), P192 (≠ Q207), M193 (≠ L208)

4urfB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 90% coverage: 20:266/273 of query aligns to 3:244/248 of 4urfB

query
sites
4urfB

L

L

N

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G

G

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K

V

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G

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x
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I

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T

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L

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N

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S

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G

active site: G16 (= G33), S142 (= S158), I152 (≠ C168), Y155 (= Y171), K159 (= K175)
binding 3-pyridinium-1-ylpropane-1-sulfonate: L210 (≠ P232), R211 (≠ K233), R212 (= R234)
binding bicarbonate ion: I92 (≠ V109), G94 (vs. gap), R109 (= R125), R179 (= R195), S228 (≠ T250)
binding nicotinamide-adenine-dinucleotide: G12 (= G29), G14 (≠ A31), N15 (≠ Q32), G16 (= G33), I17 (= I34), D36 (= D53), I37 (= I54), D62 (= D79), T63 (≠ I80), N89 (≠ C106), A90 (= A107), G91 (= G108), I140 (= I156), Y155 (= Y171), K159 (= K175), P185 (= P201), A186 (≠ G202), I188 (= I204), T190 (= T206)

4urfA Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 90% coverage: 20:266/273 of query aligns to 3:244/248 of 4urfA

query
sites
4urfA

L

L

N

E

G

G

K

K

V

T

V

A

I

L

I

V

T

T

G
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G

A

A

A
x
G

Q
x
N

G
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G

I
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I

G

G

E

R

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I

I

V

A

A

L

C

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A

A

A

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G

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C

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N

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x
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A
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I

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x
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V
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E

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x
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R

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I

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K

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G
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T

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T

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L

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Q

N

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D

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Y

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A

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R

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L

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Q

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E

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A

A

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N

T

L

A

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L

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L

L

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S

D

D

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K

A

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S

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F

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T
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L

Y

M

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D

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G

active site: G16 (= G33), S142 (= S158), I152 (≠ C168), Y155 (= Y171), K159 (= K175)
binding 3-pyridinium-1-ylpropane-1-sulfonate: I92 (≠ V109), S93 (≠ N110), G94 (vs. gap), E95 (≠ V111), T97 (≠ R113), E101 (= E117), T103 (= T119), Q106 (≠ D122), R109 (= R125), S175 (≠ P191), G177 (= G193)
binding magnesium ion: S237 (≠ T259), Y238 (≠ C260)
binding nicotinamide-adenine-dinucleotide: G12 (= G29), G14 (≠ A31), N15 (≠ Q32), G16 (= G33), I17 (= I34), D36 (= D53), I37 (= I54), W41 (≠ K58), D62 (= D79), T63 (≠ I80), N89 (≠ C106), A90 (= A107), G91 (= G108), I140 (= I156), Y155 (= Y171), K159 (= K175), P185 (= P201), I188 (= I204), T190 (= T206)

4ureB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
35% identity, 90% coverage: 20:266/273 of query aligns to 3:244/248 of 4ureB

query
sites
4ureB

L

L

N

E

G

G

K

K

V

T

V

A

I

L

I

V

T

T

G

G

A

A

A

G

Q
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N

G
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I
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I

G

G

E

R

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T

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I

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A

A

L

C

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Y

Q

A

A

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Q

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A

A

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L

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D

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E

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A

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H

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D

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A

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L

L

V

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N

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L

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A

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E

R

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A

F

F

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G

R

R

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L

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D

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L

A

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C

N

N

C
x
N

A

A

G
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G

V

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N

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-

G

V

E

F

F

R

T

D

P

P

T

L

A

E

E

M

T

T

T

D

D

E

A

D

Q

W

W

R

Q

R

R

C

V

F

I

A

G

I

I

D

N

L

L

D

S

G

G

A

V

W

F

F

Y

G

G

C

V

R

R

A

A

V

Q

L

I

P

R

H

A

M

M

I

L

E

E

Q

T

G

G

I

G

G

G

N

A

I

I

I

V

N

N

I

I

A

S

S
|
S

T

I

H

A

S

G

S

Q

H

I

I

G

I

I

P

E

G

G

C
x
I

F

T

P

P

Y
|
Y

P

T

V

A

A

A

K
|
K

H

H

G

G

L

V

G

G

L

L

T

T

R

K

A

T

L

V

G

A

I

W

E

E

Y

Y

A

G

P

S

K

K

G

G

I

I

R

R

V

I

N

N

A

S

I

V

A

G

P
|
P

G
x
A

Y

F

I

I

E

N

T

T

Q

T

L

L

-

V

-

Q

N

N

V

V

D

-

Y

-

W

-

N

-

G

-

F

-

P

-

D

-

P

P

H

L

A

E

E

T

R

R

Q

R

R

Q

A

L

F

E

D

Q

L

M

H

H

P

A

P

L

K

R

R

R

I

L

G

G

Q

E

P

T

I

E

E

E

V

V

A

A

M

N

T

L

A

V

L

A

F

W

L

L

A

S

T

S

D

D

E

K

A

A

P

S

F

F

I

V

N

T

A

G

T

S

C

Y

L

Y

M

A

I

V

D

D

G

G

active site: G16 (= G33), S142 (= S158), I152 (≠ C168), Y155 (= Y171), K159 (= K175)
binding 3-pyridinium-1-ylpropane-1-sulfonate: N15 (≠ Q32), G16 (= G33), I17 (= I34), N89 (≠ C106), G91 (= G108), Y155 (= Y171), P185 (= P201), A186 (≠ G202)

6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
33% identity, 92% coverage: 20:270/273 of query aligns to 3:248/248 of 6ixmC

query
sites
6ixmC

L

L

N

D

G

N

K

K

V

V

V

A

I

L

I

V

T

T

G
|
G

A

A

A

G

Q
x
S

G
|
G

I
|
I

G

G

E

L

A

A

I

V

V

A

A

H

C

S

F

Y

Q

A

A

K

Q

E

Q

G

A

A

R

K

L

V

I

I

I

V

A

S

D
|
D

I
|
I

Q

N

G

E

E

D

K

H

V

G

E

N

K

K

V

A

A

V

A

E

H

D

W

I

R

K

E

A

R

Q

G

G

A

G

D

E

I

A

Y

S

A

F

Q

V

A

K

V
x
A

D
|
D

I
x
T

T

S

S

N

K

P

D

E

Q

E

W

V

Q

E

A

A

L

L

V

V

N

K

L

R

A

T

I

V

E

E

R

I

F

Y

G

G

R

R

V

L

D

D

V

I

L

A

V

C

N

N

C
x
N

A
|
A

G

G

V

I

N

G

V

G

F

E

R

Q

D

A

-

L

P

A

L

G

E

D

M

Y

T

G

D

L

E

D

D

S

W

W

R

R

R

K

C

V

F

L

A

S

I

I

D

N

L

L

D

D

G

G

A

V

W

F

F

Y

G

G

C

C

R

K

A

Y

V

E

L

L

P

E

H

Q

M

M

I

E

E

K

Q

N

G

G

I

G

G

G

N

V

I

I

I

V

N

N

I
x
M

A

A

S
|
S

T

I

H

H

S

G

S

I

H

V

I

A

P

P

G

L

C

S

F

S

P

A

Y
|
Y

P

T

V

S

A

A

K
|
K

H

H

G

A

L

V

G

G

L

L

T

T

R

K

A

N

L

I

G

G

I

A

E

E

Y

Y

A

G

P

Q

K

K

G

N

I

I

R

R

V

C

N

N

A

A

I

V

A

G

P
|
P

G
x
A

Y
|
Y

I
|
I

E

E

T

T

Q

P

L
|
L

N

-

V

-

D

-

Y

-

W

-

N

-

G

-

F

L

P

E

D

S

P

L

H

T

A

K

E

E

R

M

Q

K

R

E

A

A

F

L

-

I

D

S

L

K

H

H

P

P

P

M

K

G

R

R

I

L

G

G

Q

K

P

P

I

E

E

E

V

V

A

A

M

E

T

L

A

V

L

L

F

F

L

L

A

S

T

S

D

E

E

K

A

S

P

S

F

F

I

M

N

T

A

G

T

G

C

Y

L

Y

M

L

I

V

D

D

G

G

R

Y

S

T

V

A

M

V

active site: G16 (= G33), S142 (= S158), Y155 (= Y171), K159 (= K175)
binding nicotinamide-adenine-dinucleotide: G12 (= G29), S15 (≠ Q32), G16 (= G33), I17 (= I34), D36 (= D53), I37 (= I54), A61 (≠ V78), D62 (= D79), T63 (≠ I80), N89 (≠ C106), A90 (= A107), M140 (≠ I156), S142 (= S158), Y155 (= Y171), K159 (= K175), P185 (= P201), A186 (≠ G202), Y187 (= Y203), I188 (= I204), L192 (= L208)

Q9KJF1 (2S)-[(R)-hydroxy(phenyl)methyl]succinyl-CoA dehydrogenase subunit BbsD; (S,R)-2-(alpha-hydroxybenzyl)succinyl-CoA dehydrogenase subunit BbsD; EC 1.1.1.429 from Thauera aromatica (see 2 papers)
35% identity, 92% coverage: 20:270/273 of query aligns to 3:246/248 of Q9KJF1

query
sites
Q9KJF1

L

I

N

Q

G

N

K

R

V

V

V

A

I

L

I

I

T

T

G

G

A

S

A

A

Q
x
S

G

G

I

M

G

G

E

K

A

Q

I

T

V

A

A

L

C

R

F

F

Q

A

A

E

Q

Q

Q

G

A

A

R

A

L

V

I

V

I

I

A

N

D
|
D

I

I

Q

D

G

A

E

E

K

K

V

V

E

R

K

A

V

T

A

V

A

D

H

E

W

F

R

S

E

A

R

R

G

G

A

H

D

R

I

V

Y

L

A

G

Q

A

A

V

V

A

D
|
D

I
|
I

T

G

S

N

K

K

D

A

Q

A

W

V

Q

D

A

G

L

M

V

V

N

K

L

Q

A

T

I

I

E

D

R

A

F

F

G

G

R

R

V

I

D

D

V

I

L

L

V

V

N

N

C
x
N

A

A

G

G

V

M

N

E

V

R

F

A

R

G

D

A

P

L

L

R

E

K

M

L

T

S

D

E

E

A

D

D

W

W

R

D

R

V

C

T

F

I

A

N

I

V

D

N

L

L

D

K

G

G

A

T

W

F

F

L

G

C

C

T

R

Q

A

A

V

V

L

H

P

G

H

H

M

M

I

V

E

E

Q

N

G

K

I

H

G

G

N

R

I

I

I

V

N

N

I

I

A

A

S

S

T

-

H

R

S

A

S

W

H

L

I

G

P

A

G

G

C

Q

F

T

P

P

Y
|
Y

P

S

V

S

A

A

K
|
K

H

A

G

G

L

V

G

G

L

M

T

T

R

R

A

A

L

L

G

A

I

I

E

E

Y

L

A

G

P

R

K

A

G

G

I

I

R

T

V

V

N

N

A

C

I

V

A

A

P

P

G

G

Y

L

I

I

E

H

T

T

Q

P

L

M

N

-

V

-

D

-

Y

-

W

W

N

D

G

E

F

L

P

P

D

E

P

K

H

-

A

-

E

D

R

Q

Q

Q

R

F

A

L

F

L

D

S

L

R

H

Q

P

P

P

T

K

G

R

K

I

L

G

G

Q

E

P

P

I

D

E

D

V

I

A

A

M

N

T

T

A

L

L

L

F

F

L

L

A

A

T

D

D

D

E

D

A

S

P

G

F

F

I

V

N

T

A

G

T

Q

C

V

L

L

M

Y

I

V

D

C

G

G

R

R

S

S

V

L

M

F

S15 (≠ Q32) binding NAD(+)
D36 (= D53) binding NAD(+)
D62 (= D79) binding NAD(+)
I63 (= I80) binding NAD(+)
N89 (≠ C106) binding NAD(+)
Y153 (= Y171) binding NAD(+)
K157 (= K175) binding NAD(+)

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
35% identity, 92% coverage: 20:270/273 of query aligns to 2:245/247 of 7pcsB

query
sites
7pcsB

L

I

N

Q

G

N

K

R

V

V

V

A

I

L

I

I

T

T

G
|
G

A

S

A

A

Q

S

G

G

I
x
M

G

G

E

K

A

Q

I

T

V

A

A

L

C

R

F

F

Q

A

A

E

Q

Q

Q

G

A

A

R

A

L

V

I

V

I

I

A

N

D
|
D

I
|
I

Q

D

G

A

E

E

K

K

V

V

E

R

K

A

V

T

A

V

A

D

H

E

W

F

R

S

E

A

R

R

G

G

A

H

D

R

I

V

Y

L

A

G

Q

A

A

V

V

A

D

D

I
|
I

T

G

S

N

K

K

D

A

Q

A

W

V

Q

D

A

G

L

M

V

V

N

K

L

Q

A

T

I

I

E

D

R

A

F

F

G

G

R

R

V

I

D

D

V

I

L

L

V

V

N

N

C
x
N

A

A

G
|
G

V

M

N

E

V

R

F

A

R

G

D

A

P

L

L

R

E

K

M

L

T

S

D

E

E

A

D

D

W

W

R

D

R

V

C

T

F

I

A

N

I

V

D

N

L

L

D

K

G

G

A

T

W

F

F

L

G

C

C

T

R

Q

A

A

V

V

L

H

P

G

H

H

M

M

I

V

E

E

Q

N

G

K

I

H

G

G

N

R

I

I

I

V

N

N

I
|
I

A

A

S
|
S

T

-

H

R

S

A

S

W

H

L

I

G

P

A

G

G

C

Q

F

T

P

P

Y
|
Y

P

S

V

S

A

A

K
|
K

H

A

G

G

L

V

G

G

L

M

T

T

R

R

A

A

L

L

G

A

I

I

E

E

Y

L

A

G

P

R

K

A

G

G

I

I

R

T

V

V

N

N

A

C

I

V

A

A

P

P

G

G

Y

L

I
|
I

E

H

T

T

Q

P

L

M

N

-

V

-

D

-

Y

-

W

W

N

D

G

E

F

L

P

P

D

E

P

K

H

-

A

-

E

D

R

Q

Q

Q

R

F

A

L

F

L

D

S

L

R

H

Q

P

P

P

T

K

G

R

K

I

L

G

G

Q

E

P

P

I

D

E

D

V

I

A

A

M

N

T

T

A

L

L

L

F

F

L

L

A

A

T

D

D

D

E

D

A

S

P

G

F

F

I

V

N

T

A

G

T

Q

C

V

L

L

M

Y

I

V

D

C

G

G

R

R

S

S

V

L

M

F

binding nicotinamide-adenine-dinucleotide: G11 (= G29), M16 (≠ I34), D35 (= D53), I36 (= I54), I62 (= I80), N88 (≠ C106), G90 (= G108), I138 (= I156), S140 (= S158), Y152 (= Y171), K156 (= K175), I185 (= I204)

4nbuB Crystal structure of fabg from bacillus sp (see paper)
36% identity, 91% coverage: 19:266/273 of query aligns to 4:241/244 of 4nbuB

query
sites
4nbuB

R

R

L

L

N

Q

G

D

K

K

V

V

V

A

I

I

T

T

G
|
G

A

A

Q
x
N

G
|
G

I
|
I

G

G

E

L

A

E

I

A

V

A

A

R

C

V

F

F

Q

M

A

K

Q

E

Q

G

A

A

R

K

L

V

I

V

I

I

A

A

D
|
D

I
x
F

Q

N

G

-

E

-

K

-

V

-

E

E

K

A

V

A

A

G

A

K

H

E

W

A

R

V

E

E

R

A

G

N

A

P

D

G

I

V

Y

V

A

F

Q

I

A

R

V
|
V

D
|
D

I
x
V

T

S

S

D

K

R

D

E

Q

S

W

V

Q

H

A

R

L

L

V

V

N

E

L

N

A

V

I

A

E

E

R

R

F

F

G

G

R

K

V

I

D

D

V

I

L

L

V

I

N

N

C
x
N

A
|
A

G
|
G

V
x
I

N

T

V

-

F

-

R

R

D
|
D

P

S

L

M

-

L

-

S

E
x
K

M

M

T

T

D

V

E

D

D

Q

W

F

R

Q

C

V

F

I

A

N

I

V

D
x
N

L

L

D

T

G

G

A

V

W

F

F

H

G

C

C

T

R

Q

A

A

V

V

L

L

P

P

H

Y

M

M

I

A

E

E

Q

Q

G

G

I

K

G

G

N

K

I

I

N

N

I
x
T

A

S

S
|
S

T

V

H

T

S

G

S

T

H

Y

I

G

I
x
N

P
x
V

G

G

C
x
Q

F

T

P

N

Y
|
Y

P

A

V

A

A

A

K
|
K

H

A

G

G

L

V

L

I

G

G

L

M

T

T

R

K

A

T

L

W

G

A

I

K

E

E

Y

L

A

A

P

R

K

K

G

G

I

I

R

N

V

V

N

N

A

A

I

V

A

A

P
|
P

G

G

Y
x
F

I
x
T

E

E

T
|
T

Q

A

L
x
M

N

V

V

A

D

E

Y

-

W

-

N

-

G

-

F

V

P

P

D

E

P

K

H

V

A

I

E

E

R
x
K

Q

M

R

K

A

A

F

-

D

-

L

Q

H

V

P

P

P

M

K

G

R

R

I

L

G

G

Q

K

P

P

I

E

E

D

V

I

A

A

M

N

T

A

A

Y

L

L

F

F

L

L

A

A

T

S

D

H

E

E

A

S

P

D

F

Y

I

V

N

N

A

G

T

H

C

V

L

L

M

H

I

V

D

D

G

G

active site: G18 (= G33), N111 (≠ D130), S139 (= S158), Q149 (≠ C168), Y152 (= Y171), K156 (= K175)
binding acetoacetyl-coenzyme a: D93 (= D114), K98 (≠ E117), S139 (= S158), N146 (≠ I165), V147 (≠ P166), Q149 (≠ C168), Y152 (= Y171), F184 (≠ Y203), M189 (≠ L208), K200 (≠ R223)
binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G29), N17 (≠ Q32), G18 (= G33), I19 (= I34), D38 (= D53), F39 (≠ I54), V59 (= V78), D60 (= D79), V61 (≠ I80), N87 (≠ C106), A88 (= A107), G89 (= G108), I90 (≠ V109), T137 (≠ I156), S139 (= S158), Y152 (= Y171), K156 (= K175), P182 (= P201), F184 (≠ Y203), T185 (≠ I204), T187 (= T206), M189 (≠ L208)

P40288 Glucose 1-dehydrogenase; EC 1.1.1.47 from Priestia megaterium (Bacillus megaterium) (see 2 papers)
34% identity, 91% coverage: 20:268/273 of query aligns to 5:251/261 of P40288

query
sites
P40288

L

L

N

E

G

G

K

K

V

V

I
x
V

I
|
I

T
|
T

G
|
G

A
x
S

Q
x
T

G
|
G

I
x
L

G
|
G

E
x
K

A
x
S

I
x
M

V
x
A

A
x
I

C
x
R

F
|
F

Q
x
A

A
x
T

Q
x
E

Q
x
K

A
|
A

R
x
K

L
x
V

I
x
V

I

V

A

N

D

Y

I

R

Q

S

G

K

E

E

-

D

K

E

V

A

E

N

K

S

V

V

A

L

A

E

H

E

W

I

R

K

E

K

R

V

G

G

A

G

D

E

I

A

Y

I

A

A

Q

V

A

K

V

G

D

D

I

V

T

T

S

V

K

E

D

S

Q

D

W

V

Q

I

A

N

L

L

V

V

N

Q

L

S

A

A

I

I

E

K

R

E

F

F

G

G

R

K

V

L

D

D

V

V

L

M

V

I

N

N

C

N

A

A

G

G

V

L

N
x
E

V

N

F

P

R

V

D

S

P

S

L

H

E

E

M

M

T

S

D

L

E

S

D
|
D

W

W

R

N

R

K

C
x
V

F

I

A

D

I

T

D

N

L

L

D

T

G

G

A

A

W

F

F

L

G

G

C

S

R

R

A

E

V

A

L

I

P

K

H

Y

M

F

I

V

E
|
E

Q

N

G

D

I

I

-

K

G

G

N

T

I

V

I

I

N

N

I

M

A

S

S

S

T

V

H

H

S

E

S

K

H

I

I

P

I

W

P

P

G

L

C

F

F

V

P

H

Y

Y

P

A

V

A

A

S

K

K

H

G

G

G

L

M

L

K

G

L

L

M

T

T

R

E

A

T

L

L

G

A

I

L

E

E

Y

Y

A

A

P

P

K

K

G

G

I

I

R

R

V
|
V

N

N

A

N

I

I

A

G

P

P

G

G

Y

A

I

I

E

N

T

T

Q
x
P

L

I

N

N

V

A

D

E

Y

K

W

-

N

-

G

-

F

F

P

A

D

D

P

P

H

E

A

-

E

Q

R

R

Q

A

R

D

A

V

F
x
E

D

S

L

M

H

I

P

P

P

M

K

G

R
x
Y

I

I

G

G

Q

E

P

P

I

E

E

E

V

I

A

A

M

A

T

V

A

A

L

A

F

W

L

L

A

A

T

S

D

S

E

E

A

A

P

S

F

Y

I

V

N

T

A

G

T

I

C

T

L

L

M

F

I

A

D

D

G

G

R

M

S

T

11:35 (vs. 26:50, 28% identical) binding NADP(+)
E96 (≠ N110) mutation E->A,G,K: Heat stable.
D108 (= D122) mutation to N: Heat stable.
V112 (≠ C126) mutation to A: Heat stable.
E133 (= E147) mutation to K: Heat stable.
V183 (= V196) mutation to I: Heat stable.
P194 (≠ Q207) mutation to Q: Heat stable.
E210 (≠ F227) mutation to K: Heat stable.
Y217 (≠ R234) mutation to H: Heat stable.

Sites not aligning to the query:

252 Q→L: Heat stable.
253 Y→C: Heat stable.
258 A→G: Heat stable.

1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
34% identity, 91% coverage: 20:268/273 of query aligns to 5:251/261 of 1g6kA

query
sites
1g6kA

L

L

N

E

G

G

K

K

V

V

I

V

I

I

T

T

G

G

A

S

Q
x
T

G
|
G

I
x
L

G

G

E

K

A

S

I

M

V

A

A

I

C

R

F

F

Q

A

A

T

Q

E

Q

K

A

A

R

K

L

V

I

V

A

N

D

Y

I
x
R

Q

S

G

K

E

E

-

D

K

E

V

A

E

N

K

S

V

V

A

L

A

E

H

E

W

I

R

K

E

K

R

V

G

G

A

G

D

E

I

A

Y

I

A

A

Q

V

A

K

V

G

D
|
D

I
x
V

T

T

S

V

K

E

D

S

Q

D

W

V

Q

I

A

N

L

L

V

V

N

Q

L

S

A

A

I

I

E

K

R

E

F

F

G

G

R

K

V

L

D

D

V

V

L

M

V

I

N

N

C
x
N

A
|
A

G
|
G

V

L

N

A

V

N

F

P

R

V

D

S

P

S

L

H

E

E

M

M

T

S

D

L

E

S

D

D

W

W

R

N

R

K

C

V

F

I

A

D

I

T

D

N

L

L

D

T

G

G

A

A

W

F

F

L

G

G

C

S

R

R

A

E

V

A

L

I

P

K

H

Y

M

F

I

V

E

E

Q

N

G

D

I

I

-

K

G

G

N

T

I

V

I

I

N

N

I
x
M

A

S

S
|
S

T

V

H

H

S

E

S

K

H

I

I

P

I

W

P

P

G

L

C

F

F

V

P

H

Y
|
Y

P

A

V

A

A

S

K
|
K

H

G

G

G

L

M

L

K

G

L

L

M

T

T

R

E

A

T

L

L

G

A

I

L

E

E

Y

Y

A

A

P

P

K

K

G

G

I

I

R

R

V

V

N

N

A

N

I

I

A

G

P
|
P

G
|
G

Y

A

I
|
I

E

N

T
|
T

Q

P

L

I

N

N

V

A

D

E

Y

K

W

-

N

-

G

-

F

F

P

A

D

D

P

P

H

E

A

-

E

Q

R

R

Q

A

R

D

A

V

F

E

D

S

L

M

H

I

P

P

P

M

K

G

R

Y

I

I

G

G

Q

E

P

P

I

E

E

E

V

I

A

A

M

A

T

V

A

A

L

A

F

W

L

L

A

A

T

S

D

S

E

E

A

A

P

S

F

Y

I

V

N

T

A

G

T

I

C

T

L

L

M

F

I

A

D

D

G

G

R

M

S

T

active site: G18 (= G33), S145 (= S158), Y158 (= Y171), K162 (= K175)
binding nicotinamide-adenine-dinucleotide: T17 (≠ Q32), G18 (= G33), L19 (≠ I34), R39 (≠ I54), D65 (= D79), V66 (≠ I80), N92 (≠ C106), A93 (= A107), G94 (= G108), M143 (≠ I156), S145 (= S158), Y158 (= Y171), P188 (= P201), G189 (= G202), I191 (= I204), T193 (= T206)

2cfcA Structural basis for stereo selectivity in the (r)- and (s)- hydroxypropylethane thiosulfonate dehydrogenases (see paper)
36% identity, 89% coverage: 23:265/273 of query aligns to 3:245/250 of 2cfcA

query
sites
2cfcA

K

R

V

V

V

A

I

I

I

V

T

T

G
|
G

A

A

A

S

Q
x
S

G
|
G

I
x
N

G

G

E

L

A

A

I

I

V

A

A

T

C

R

F

F

Q

L

A

A

Q

R

Q

G

A

D

R

R

L

V

I

A

A

L

D
|
D

I
x
L

Q

S

G

A

E

E

K

T

V

L

E

E

K

E

V

T

A

A

-

R

A

T

H

H

W

W

R

H

E

A

R

Y

G

A

A

D

D

K

I

V

Y

L

A

R

Q

V

A

R

V
x
A

D
|
D

I
x
V

T

A

S

D

K

E

D

G

Q

D

W

V

Q

N

A

A

L

A

V

I

N

A

L

A

A

T

I

M

E

E

R

Q

F

F

G

G

R

A

V

I

D

D

V

V

L

L

V

V

N

N

C
x
N

A
|
A

G
|
G

V

I

-

T

-

G

N

N

V

S

F

E

R

A

D

G

P

V

L

L

E

H

M

T

T

T

D

P

-

V

E

E

D

Q

W

F

R

D

R

K

C

V

F

M

A

A

I

V

D

N

L

V

D

R

G

G

A

I

W

F

F

L

G

G

C

C

R

R

A

A

V

V

L

L

P

P

H

H

M

M

I

L

E

L

Q

Q

G

G

I

A

G

G

N

V

I

I

I

V

N

N

I
|
I

A

A

S
|
S

T

V

H

A

S

S

S

L

H

V

I

A

I
x
F

P

P

G

G

C
x
R

F

S

P

A

Y
|
Y

P

T

V

T

A

S

K
|
K

H

G

G

A

L

V

L

L

G

Q

L

L

T

T

R

K

A

S

L

V

G

A

I

V

E

D

Y

Y

A

A

P

G

K

S

G

G

I

I

R

R

V

C

N

N

A

A

I

V

A

C

P
|
P

G
|
G

Y
x
M

I
|
I

E

E

T
|
T

Q
x
P

L
x
M

N
x
T

V

-

D

-

Y

Q

W
|
W

N
x
R

G

-

F

-

P

L

D

D

P

Q

H

P

A

E

E

L

R

R

Q

D

R

Q

A

V

F

L

D

A

L

R

H

I

P

P

P

Q

K

K

R

E

I

I

G

G

Q

T

P

A

I

A

E

Q

V

V

A

A

M

D

T

A

A

V

L

M

F

F

L

L

A

A

T

G

D

E

E

D

A

A

P

T

F

Y

I

V

N

N

A

G

T

A

C

A

L

L

M

V

I

M

D

D

G

G

active site: G13 (= G33), S142 (= S158), Y155 (= Y171), K159 (= K175)
binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ I165), R152 (≠ C168), Y155 (= Y171), W195 (= W213), R196 (≠ N214)
binding nicotinamide-adenine-dinucleotide: G9 (= G29), S12 (≠ Q32), G13 (= G33), N14 (≠ I34), D33 (= D53), L34 (≠ I54), A59 (≠ V78), D60 (= D79), V61 (≠ I80), N87 (≠ C106), A88 (= A107), G89 (= G108), I140 (= I156), P185 (= P201), G186 (= G202), M187 (≠ Y203), I188 (= I204), T190 (= T206), P191 (≠ Q207), M192 (≠ L208), T193 (≠ N209)

Q56840 2-(R)-hydroxypropyl-CoM dehydrogenase; R-HPCDH; 2-[(R)-2-hydroxypropylthio]ethanesulfonate dehydrogenase; Aliphatic epoxide carboxylation component III; Epoxide carboxylase component III; RHPCDH1; EC 1.1.1.268 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 4 papers)
36% identity, 89% coverage: 23:265/273 of query aligns to 3:245/250 of Q56840

query
sites
Q56840

K

R

V

V

V

A

I

I

I

V

T

T

G

G

A

A

A

S

Q
x
S

G
|
G

I
x
N

G

G

E

L

A

A

I

I

V

A

A

T

C

R

F

F

Q

L

A

A

Q

R

Q

G

A

D

R

R

L

V

I

A

A

L

D
|
D

I

L

Q

S

G

A

E

E

K

T

V

L

E

E

K

E

V

T

A

A

-

R

A

T

H

H

W

W

R

H

E

A

R

Y

G

A

A

D

D

K

I

V

Y

L

A

R

Q

V

A

R

V

A

D
|
D

I
x
V

T

A

S

D

K

E

D

G

Q

D

W

V

Q

N

A

A

L

A

V

I

N

A

L

A

A

T

I

M

E

E

R

Q

F

F

G

G

R

A

V

I

D

D

V

V

L

L

V

V

N

N

C
x
N

A

A

G

G

V

I

-

T

-

G

N

N

V

S

F

E

R

A

D

G

P

V

L

L

E

H

M

T

T

T

D

P

-

V

E

E

D

Q

W

F

R

D

R

K

C

V

F

M

A

A

I

V

D

N

L

V

D

R

G

G

A

I

W

F

F

L

G

G

C

C

R

R

A

A

V

V

L

L

P

P

H

H

M

M

I

L

E

L

Q

Q

G

G

I

A

G

G

N

V

I

I

I

V

N

N

I

I

A

A

S
|
S

T

V

H

A

S

S

S

L

H

V

I

A

I

F

P

P

G

G

C
x
R

F

S

P

A

Y
|
Y

P

T

V

T

A

S

K
|
K

H

G

G

A

L

V

L

L

G

Q

L

L

T

T

R

K

A

S

L

V

G

A

I

V

E

D

Y

Y

A

A

P

G

K

S

G

G

I

I

R
|
R

V

C

N

N

A

A

I

V

A

C

P

P

G

G

Y

M

I
|
I

E
|
E

T
|
T

Q
x
P

L
x
M

N

T

V

-

D

-

Y

Q

W
|
W

N
x
R

G

-

F

-

P

L

D

D

P

Q

H

P

A

E

E

L

R
|
R

Q

D

R

Q

A

V

F

L

D

A

L
x
R

H

I

P

P

P

Q

K

K

R

E

I

I

G

G

Q

T

P

A

I

A

E

Q

V

V

A

A

M

D

T

A

A

V

L

M

F

F

L

L

A

A

T

G

D

E

E

D

A

A

P

T

F

Y

I

V

N

N

A

G

T

A

C

A

L

L

M

V

I

M

D

D

G

G

SGN 12:14 (≠ QGI 32:34) binding NAD(+)
D33 (= D53) binding NAD(+)
DV 60:61 (≠ DI 79:80) binding NAD(+)
N87 (≠ C106) binding NAD(+)
S142 (= S158) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
R152 (≠ C168) binding 2-oxopropyl-coenzyme M; mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
Y155 (= Y171) mutation Y->E,F: Loss of activity.
K159 (= K175) mutation to A: Loss of activity.
R179 (= R195) mutation to A: Loss of activity.
IETPM 188:192 (≠ IETQL 204:208) binding NAD(+)
WR 195:196 (≠ WN 213:214) binding 2-oxopropyl-coenzyme M
R196 (≠ N214) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
R203 (= R223) mutation to A: Slight decrease in catalytic efficiency.
R209 (≠ L229) mutation to A: Does not affect catalytic efficiency.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

H9XP47 Meso-2,3-butanediol dehydrogenase; BDH; meso-2,3-BDH; (R,S)-butane-2,3-diol dehydrogenase; NAD(H)-dependent meso-2,3-BDH; SmBdh; EC 1.1.1.- from Serratia marcescens (see paper)
36% identity, 92% coverage: 19:268/273 of query aligns to 2:242/251 of H9XP47

query
sites
H9XP47

R

R

L

F

N

D

G

N

K

K

V

V

I

V

I

I

T

T

G

G

A

A

A

G

Q
x
N

G

G

I
x
M

G

G

E

E

A

A

I

A

V

A

A

R

C

R

F

F

Q

S

A

A

Q

E

Q

G

A

A

R

I

L

V

I

V

I

L

A

A

D
|
D

I

W

Q

A

G

K

E

E

K

A

V

V

E

D

K

K

V

V

A

A

H

S

W

L

R

P

E

K

R

G

G

R

A

A

D

-

I

-

Y

M

A

A

Q

V

A

H

V

I

D
|
D

I
x
V

T

S

S

D

K

H

D

V

Q

A

W

V

Q

E

A

K

L

M

V

M

N

N

L

E

A

V

I

A

E

E

R

K

F

L

G

G

R

R

V

I

D

D

V

V

L

L

V

L

N

N

C
x
N

A

A

G

G

V

V

N

H

V

V

F

A

R

G

D

S

P

V

L

L

E

E

M

T

T

S

D

I

E

D

D

D

W

W

R

R

C

I

F

A

A

G

I

V

D

D

L

I

D

D

G

G

A

V

W

V

F

F

G

C

C

S

R

K

A

F

V

A

L

L

P

P

H

H

M

L

I

L

E

K

Q

T

G

K

I

-

G

G

N

C

I

I

I

V

N

N

I

T

A

A

S
|
S

T
x
V

H
x
S

S

G

S

L

H

G

I

G

I

D

P

W

G

G

C

A

F

A

P

Y

Y
|
Y

P

C

V

A

A

A

K
|
K

H

G

G

A

L

V

G

N

L

L

T

T

R

R

A

A

L

M

G

A

I

L

E

D

Y

H

A

G

P

G

K

D

G

G

I

V

R

R

V

I

N

N

A

S

I

V

A

C

P

P

G

S

Y

L

I
x
V

E

K

T
|
T

Q

N

L

M

N

T

V

-

D

-

Y

-

W

-

N

N

G

G

F

W

P

-

D

-

P

P

H

Q

A

E

E

I

R
|
R

Q
x
D

R
x
K

A

F

F

N

D

E

L

R

H

I

P

A

P

L

K

G

R

R

I

A

G

A

Q

E

P

P

I

E

E

E

V

V

A

A

M

A

T

V

A

M

L

A

F

F

L

L

A

A

T

S

D

D

E

D

A

A

P

S

F

F

I

I

N

N

A

G

T

A

C

N

L

I

M

P

I

V

D

D

G

G

R

A

S

T

N15 (≠ Q32) binding NAD(+)
M17 (≠ I34) binding NAD(+)
D36 (= D53) binding NAD(+)
D60 (= D79) binding NAD(+)
V61 (≠ I80) binding NAD(+)
N87 (≠ C106) binding NAD(+)
S138 (= S158) binding (R)-acetoin; binding (S)-acetoin
V139 (≠ T159) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
S140 (≠ H160) binding (R)-acetoin
Y151 (= Y171) binding (R)-acetoin; binding (S)-acetoin; binding NAD(+)
K155 (= K175) binding NAD(+)
V184 (≠ I204) binding NAD(+)
T186 (= T206) binding NAD(+)
RDK 197:199 (≠ RQR 223:225) mutation to SEAAGKPLGYGTET: Mimics longer alpha6 helix. Retains 3% of activity with acetoin as substrate.

Sites not aligning to the query:

247 Q→A: Retains 10% of activity with acetoin as substrate. Retains 50% of activity with acetoin as substrate; when associated with Q-139.

6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
36% identity, 92% coverage: 19:268/273 of query aligns to 4:244/252 of 6vspB

query
sites
6vspB

R

R

L

F

N

D

G

N

K

K

V

V

I

V

I

I

T

T

G
|
G

A

A

A

G

Q
x
N

G
|
G

I

M

G

G

E

E

A

A

I

A

V

A

A

R

C

R

F

F

Q

S

A

A

Q

E

Q

G

A

A

R

I

L

V

I

V

I

L

A

A

D
|
D

I
x
W

Q

A

G

K

E

E

K

A

V

V

E

D

K

K

V

V

A

A

H

S

W

L

R

P

E

K

R

G

G

R

A

A

D

-

I

-

Y

M

A

A

Q

V

A

H

V
x
I

D
|
D

I
x
V

T

S

S

D

K

H

D

V

Q

A

W

V

Q

E

A

K

L

M

V

M

N

N

L

E

A

V

I

A

E

E

R

K

F

L

G

G

R

R

V

I

D

D

V

V

L

L

V

L

N

N

C

N

A

A

G
|
G

V

V

N

H

V

V

F

A

R

G

D

S

P

V

L

L

E

E

M

T

T

S

D

I

E

D

D

D

W

W

R

R

C

I

F

A

A

G

I

V

D

D

L

I

D

D

G

G

A

V

W

V

F

F

G

C

C

S

R

K

A

F

V

A

L

L

P

P

H

H

M

L

I

L

E

K

Q

T

G

K

I

-

G

G

N

C

I

I

I

V

N

N

I

T

A

A

S
|
S

T

V

H

S

S

G

S

L

H

G

I

G

I

D

P

W

G

G

C

A

F

A

P

Y

Y
|
Y

P

C

V

A

A

A

K

K

H

G

G

A

L

V

G

N

L

L

T

T

R

R

A

A

L

M

G

A

I

L

E

D

Y

H

A

G

P

G

K

D

G

G

I

V

R

R

V

I

N

N

A

S

I

V

A

C

P

P

G

S

Y

L

I

V

E

K

T

T

Q

N

L

M

N

T

V

-

D

-

Y

-

W

-

N

N

G

G

F

W

P

-

D

-

P

P

H

Q

A

E

E

I

R

R

Q

D

R

K

A

F

F

N

D

E

L

R

H

I

P

A

P

L

K

G

R

R

I

A

G

A

Q

E

P

P

I

E

E

E

V

V

A

A

M

A

T

V

A

M

L

A

F

F

L

L

A

A

T

S

D

D

E

D

A

A

P

S

F

F

I

I

N

N

A

G

T

A

C

N

L

I

M

P

I

V

D

D