SitesBLAST

P50162 Tropinone reductase 1; Tropine dehydrogenase; Tropinone reductase I; TR-I; EC 1.1.1.206 from Datura stramonium (Jimsonweed) (Common thornapple) (see paper)
38% identity, 98% coverage: 2:250/254 of query aligns to 17:268/273 of P50162

query
sites
P50162

F

W

S

S

L

L

K

K

N

G

K

T

A

A

V
x
L

V
|
V

T
|
T

G
|
G

G
x
S

S
x
K

G
|
G

I
|
I

G
|
G

K
x
Y

A
|
A

I
|
I

A
x
V

T
x
E

I
x
E

L
|
L

A
|
A

K
x
G

Q
x
L

G
|
G

A
|
A

E
x
R

V
|
V

H
x
Y

I

T

I

C

E

S

L

R

G

N

T

E

E

K

H

E

A

L

Q

D

D

E

T

C

L

L

D

E

E

I

I

W

K

R

T

E

N

K

G

G

G

L

V

N

A

V

F

E

S

G

Y

S

G

V

C

C

D

D

V

L

S

L

D

S

H

R

-

T

-

E

-

R

-

D

-

K

-

L

-

M

Q

Q

A

T

V

V

A

A

A

H

V

V

F

F

N

D

E

-

I

-

G

G

N

K

I

L

N

N

I

I

L

L

I

V

N

N

A

A

G

G

I

V

A

V

H

I

I

H

G

K

K

E

A

A

D

K

T

D

T

F

D

T

E

E

A

K

D

D

F

Y

D

N

R

I

V

I

M

M

R

G

V

T

N

N

V

F

K

E

G

A

V

A

Y

Y

N

H

C

L

L

S

H

Q

A

I

A

A

I

Y

P

P

Q

L

I

L

R

K

L

A

S

S

G

Q

G

N

G

G

V

N

I

V

I

I

N

F

M

L

A

S

S
|
S

I

I

A

A

A

G

L

F

I

S

G

A

L

L

P

P

D

S

R

V

F

S

V

L

Y
|
Y

S

S

A

A

A

S

K

K

G

G

A

A

V

I

K

N

A

Q

I

M

T

T

M

K

S

S

V

L

A

A

K

C

D

E

Y

W

I

A

G

K

E

D

N

N

I

I

R

R

C

V

N

N

S

S

I

V

S

A

P

P

A

G

R

V

V

I

H

L

T

T

P

P

F

L

V

V

D

E

G

T

F

A

L

I

Q

K

K

K

N

N

Y

-

P

P

D

H

N

Q

I

K

P

E

E

E

M

I

F

D

E

N

K

F

L

I

S

V

K

K

T

T

Q

-

P

P

I

M

G

G

R

R

M

A

A

G

K

K

P

P

E

Q

E

E

V

V

G

S

A

A

L

L

A

I

L

A

Y

F

L

L

C

C

S

F

D

P

E

A

A

A

S

S

F

Y

I

I

T

T

G

G

C

Q

D

I

Y

I

P

W

I

A

D

D

G

G

F

F

T

T

25:49 (vs. 10:34, 56% identical) binding
S158 (= S138) binding
Y171 (= Y151) active site, Proton acceptor

1ae1B Tropinone reductase-i complex with NADP (see paper)
38% identity, 98% coverage: 2:250/254 of query aligns to 2:253/258 of 1ae1B

query
sites
1ae1B

F

W

S

S

L

L

K

K

N

G

K

T

A

A

V

L

V

V

T

T

G
|
G

G

G

G
x
S

S
x
K

G
|
G

I
|
I

G

G

K

Y

A

A

I

I

A

V

T

E

I

E

L

L

A

A

K

G

Q

L

G

G

A

A

E

R

V

V

H

Y

I

T

I

C

E
x
S

L
x
R

G

N

T

E

E

K

H

E

A

L

Q

D

D

E

T

C

L

L

D

E

E

I

I

W

K

R

T

E

N

K

G

G

G

L

V

N

A

V

F

E

S

G

Y

S

G

V

C
|
C

D
|
D

V
x
L

S

L

D

S

H

R

-

T

-

E

-

R

-

D

-

K

-

L

-

M

Q

Q

A

T

V

V

A

A

A

H

V

V

F

F

N

D

E

-

I

-

G

G

N

K

I

L

N

N

I

I

L

L

I

V

N

N

N
|
N

A
|
A

G

G

I

V

A

V

H

I

I

H

G

K

K

E

A

A

D

K

T

D

T

F

D

T

E

E

A

K

D

D

F

Y

D

N

R

I

V

I

M

M

R

G

V

T

N

N

V

F

K

E

G

A

V

A

Y

Y

N

H

C

L

L

S

H

Q

A

I

A

A

I

Y

P

P

Q

L

I

L

R

K

L

A

S

S

G

Q

G

N

G

G

V

N

I

V

I

I

N

F

M

L

A

S

S
|
S

I

I

A

A

A

G

L

F

I

S

G

A

L

L

P

P

D

S

R
x
V

F

S

V

L

Y
|
Y

S

S

A

A

A

S

K
|
K

G

G

A

A

V

I

K

N

A

Q

I

M

T

T

M

K

S

S

V

L

A

A

K

C

D

E

Y

W

I

A

G

K

E

D

N

N

I

I

R

R

C

V

N

N

S

S

I

V

S

A

P
|
P

A

G

R

V

V
x
I

H

L

T
|
T

P

P

F
x
L

V
|
V

D

E

G

T

F

A

L

I

Q

K

K

K

N

N

Y

-

P

P

D

H

N

Q

I

K

P

E

E

E

M

I

F

D

E

N

K

F

L

I

S

V

K

K

T

T

Q

-

P

P

I

M

G

G

R

R

M

A

A

G

K

K

P

P

E

Q

E

E

V

V

G

S

A

A

L

L

A

I

L

A

Y

F

L

L

C

C

S

F

D

P

E

A

A

A

S

S

F

Y

I

I

T

T

G

G

C

Q

D

I

Y

I

P

W

I

A

D

D

G

G

F

F

T

T

active site: G17 (= G17), S143 (= S138), V153 (≠ R148), Y156 (= Y151), K160 (= K155)
binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G13), S15 (≠ G15), K16 (≠ S16), G17 (= G17), I18 (= I18), S37 (≠ E37), R38 (≠ L38), C62 (= C62), D63 (= D63), L64 (≠ V64), N91 (= N86), A92 (= A87), S143 (= S138), Y156 (= Y151), K160 (= K155), P186 (= P181), I189 (≠ V184), T191 (= T186), L193 (≠ F188), V194 (= V189)

Q8JZV9 Dehydrogenase/reductase SDR family member 6; (R)-beta-hydroxybutyrate dehydrogenase; 3-hydroxybutyrate dehydrogenase type 2; 4-oxo-L-proline reductase; Oxidoreductase UCPA; Short chain dehydrogenase/reductase family 15C member 1; EC 1.1.1.-; EC 1.1.1.30; EC 1.1.1.104 from Mus musculus (Mouse) (see paper)
36% identity, 98% coverage: 1:250/254 of query aligns to 1:244/245 of Q8JZV9

query
sites
Q8JZV9

M

M

F

G

S

R

L

L

K

D

N

G

K

K

K

V

A

I

V

V

V

L

T

T

G

A

S

Q

G

G

I

I

G

G

K

R

A

A

I

S

A

A

T

L

I

A

L

F

A

A

K

R

Q

E

G

G

A

A

E

K

V

V

H

-

I

-

E

-

L

I

G

A

T

T

E

D

H

I

A

N

Q

E

D

S

T

K

L

L

D

Q

E

E

I

L

K

E

T

S

N

Y

G

R

G

G

V

I

A

Q

F

-

S

T

Y

R

G

V

C

L

D

D

V

V

S

T

D

K

H

K

Q

R

A

Q

V

I

A

D

A

Q

V

F

F

A

N

S

E

E

I

I

G

E

N

R

I

I

N

D

I

V

L

L

I

F

N

N

N

V

A

A

G

G

I

F

A

V

H

H

I

H

G

G

K

T

A

I

D

L

T

D

T

C

D

E

E

E

A

K

D

D

F

W

D

D

R

F

V

S

M

M

R

N

V

L

N

N

V

V

K

R

G

S

V

M

Y

F

N

L

C

M

L

I

H

K

A

A

A

F

I

L

P

P

Q

K

I

M

R

L

L

A

S

Q

G

K

G

S

G

G

V

N

I

I

N

N

M

M

A

S

S

S

I

V

A

A

A

S

L

S

I

I

-

K

G

G

L

V

P

E

D

N

R

R

F

C

V

V

Y
|
Y

S

S

A

A

A

T

K

K

G

A

A

A

V

V

K

I

A

G

I

L

T

T

M

K

S

S

V

V

A

A

K

A

D

D

Y

F

I

I

G

Q

E

Q

N

G

I

I

R

R

C

C

N

N

S

C

I

V

S

C

P

P

A

G

R

T

V

V

H

D

T

T

P

P

F

S

V

L

D

Q

G

E

F

R

L

I

Q

Q

K

A

N

R

Y

-

P

-

D

D

N

N

I

P

P

K

E

E

M

A

F

L

E

K

K

T

L

F

S

L

K

N

T

R

Q

Q

P

K

I

T

G

G

R

R

M

F

A

A

K

S

P

A

E

E

V

V

G

A

A

L

L

L

A

C

L

V

Y

Y

L

L

C

A

S

S

D

D

E

E

A

S

S

A

F

Y

I

V

T

T

G

G

C

N

D

P

Y

V

P

I

I

I

D

D

G

G

F

W

T

S

Y147 (= Y151) active site, Proton acceptor; mutation to F: Loss of function.

D4A1J4 Dehydrogenase/reductase SDR family member 6; (R)-beta-hydroxybutyrate dehydrogenase; 3-hydroxybutyrate dehydrogenase type 2; 4-oxo-L-proline reductase; Oxidoreductase UCPA; Short chain dehydrogenase/reductase family 15C member 1; EC 1.1.1.-; EC 1.1.1.30; EC 1.1.1.104 from Rattus norvegicus (Rat) (see paper)
36% identity, 98% coverage: 1:250/254 of query aligns to 1:244/245 of D4A1J4

query
sites
D4A1J4

M

M

F

G

S

R

L

L

K

E

N

G

K

K

K

V

A

I

V

V

V

L

T

T

G

A

S

Q

G

G

I

I

G

G

K

R

A

A

I

S

A

A

T

L

I

A

L

F

A

A

K

R

Q

E

G

G

A

A

E

K

V

V

H

-

I

-

E

-

L

I

G

A

T

T

E

D

H

I

A

N

Q

E

D

A

T

K

L

L

D

Q

E

E

I

L

K

E

T

N

N

Y

G

P

G

G

V

I

A

Q

F

-

S

T

Y

R

G

V

C

L

D

D

V

V

S

T

D

K

H

K

Q

R

A

Q

V

I

A

D

A

Q

V

F

F

A

N

S

E

E

I

I

G

E

N

K

I

I

N

D

I

V

L

L

I

F

N

N

N

V

A

A

G

G

I

F

A

V

H

H

I

H

G

G

K

T

A

I

D

L

T

D

T

C

D

E

E

E

A

K

D

D

F

W

D

D

R

F

V

S

M

M

R

N

V

L

N

N

V

V

K

R

G

S

V

M

Y

Y

N

L

C

M

L

I

H

K

A

A

A

F

I

L

P

P

Q

K

I

M

R

L

L

A

S

Q

G

K

G

S

G

G

V

N

I

I

N

N

M

M

A

S

S

S

I

V

A

A

A

S

L

S

I

I

-

K

G

G

L

V

P

E

D

N

R

R

F

C

V

V

Y
|
Y

S

S

A

A

A

T

K

K

G

A

A

A

V

V

K

I

A

G

I

L

T

T

M

K

S

S

V

V

A

A

K

A

D

D

Y

F

I

I

G

Q

E

Q

N

G

I

I

R

R

C

C

N

N

S

C

I

V

S

C

P

P

A

G

R

T

V

V

H

D

T

T

P

P

F

S

V

L

D

Q

G

E

F

R

L

I

Q

Q

K

A

N

R

Y

-

P

-

D

D

N

D

I

P

P

K

E

E

M

A

F

L

E

K

K

A

L

F

S

L

K

N

T

R

Q

Q

P

K

I

T

G

G

R

R

M

F

A

A

K

S

P

A

E

E

V

V

G

A

A

L

L

L

A

C

L

V

Y

Y

L

L

C

A

S

S

D

D

E

E

A

S

S

A

F

Y

I

V

T

T

G

G

C

T

D

P

Y

V

P

V

I

I

D

D

G

G

F

W

T

S

Y147 (= Y151) mutation to F: Loss of function.

7djsD Crystal structure of isopiperitenol dehydrogenase from pseudomonas aeruginosa complexed with NAD
39% identity, 98% coverage: 4:252/254 of query aligns to 3:251/251 of 7djsD

query
sites
7djsD

L

L

K

S

N

G

K

Q

K

V

A

A

V

L

V

V

T

T

G
|
G

G

G

G

A

S

A

G
|
G

I
|
I

G

G

K

R

A

A

I

T

A

A

T

Q

I

A

L

F

A

A

K

A

Q

A

G

G

A

V

E

K

V

V

H

V

I

V

I

A

E
x
D

L
|
L

G

D

T

S

E

A

H

G

A

G

Q

E

D

G

T

T

L

V

D

E

E

A

I

I

K

R

T

Q

N

A

G

G

V

E

A

A

F

V

S

F

Y

I

G

R

C
|
C

D
|
D

V
|
V

S

T

D

R

H

D

Q

A

A

E

V

V

A

K

A

A

V

L

F

V

N

E

-

G

-

C

-

A

E

A

I

Y

G

G

N

R

I

L

N

D

I

Y

L

A

I

F

N

N

N
|
N

A
|
A

G

G

I

I

A

E

-

I

H

E

I

Q

G

G

K

K

A

L

D

A

T

D

T

G

D

N

E

E

A

A

D

E

F

F

D

D

R

A

V

I

M

M

R

A

V

V

N

N

V

V

K

K

G

G

V

V

Y

W

N

L

C

C

L

M

H

K

A

H

A

Q

I

I

P

P

Q

L

I

M

R

L

L

A

S

Q

G

G

V

A

I

I

I

V

N

N

M
x
T

A

A

S
|
S

I

V

A

A

A

G

L

L

I

G

G

A

L

A

P

P

D

K

R

M

F

S

V

I

Y
|
Y

S

A

A

A

A

S

K
|
K

G

H

A

A

V

V

K

I

A

G

I

L

T

T

M

K

S

S

V

A

A

A

K

I

D

E

Y

Y

I

A

G

K

E

K

N

G

I

I

R

R

C

V

N

N

S

A

I

V

S

C

P

P

A
|
A

R
x
V

V

I

H

D

T

T

P

-

F

-

V

-

D

D

G

M

F

F

L

R

Q

R

K

A

N

Y

Y

E

P

A

D

D

N

-

I

-

P

P

E

R

M

K

F

A

E

E

K

F

L

A

S

A

K

A

T

M

Q

H

P

P

I

L

G

G

R

R

M

V

A

G

K

R

P

V

E

E

V

I

G

A

A

A

L

A

A

V

L

L

Y

Y

L

L

C

C

S

S

D

D

E

N

A

A

S

G

F

F

I

T

T

T

G

G

C

I

D

A

Y

L

P

P

I

V

D

D

G

G

F

A

T

T

T

A

L

I

binding nicotinamide-adenine-dinucleotide: G12 (= G13), G16 (= G17), I17 (= I18), D36 (≠ E37), L37 (= L38), C61 (= C62), D62 (= D63), V63 (= V64), N89 (= N86), A90 (= A87), T140 (≠ M136), S142 (= S138), Y155 (= Y151), K159 (= K155), A186 (= A182), V187 (≠ R183)

4urfB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
38% identity, 97% coverage: 4:249/254 of query aligns to 3:245/248 of 4urfB

query
sites
4urfB

L

L

K

E

N

G

K

K

K

T

A

A

V

L

V

V

T

T

G
|
G

G

A

G
|
G

S
x
N

G
|
G

I
|
I

G

G

K

R

A

T

I

I

A

A

T

L

I

T

L

Y

A

A

K

A

Q

E

G

G

A

A

E

N

V

V

H

V

I

V

I

S

E
x
D

L
x
I

G

S

T

D

E

E

H

W

A

G

Q

R

D

E

T

T

L

L

D

A

E

L

I

I

K

E

T

G

N

K

G

G

V

K

A

A

F

V

S

F

Y

Q

G

H

C

A

D
|
D

V
x
T

S

A

-

H

-

P

-

E

D

D

H

H

-

D

Q

E

A

L

V

I

A

A

V

A

F

K

N

R

E

A

I

F

G

G

N

R

I

L

N

D

I

I

L

A

I

C

N

N

N
|
N

A
|
A

G
|
G

I
|
I

A

S

-
x
G

-

E

H

F

I

T

G

P

K

T

A

A

D

E

T

T

D

D

E

-

A

A

D

Q

F

W

D

Q

R
|
R

V

V

M

I

R

G

V

I

N

N

V

L

K

S

G

G

V

V

Y

F

N

Y

C

G

L

V

H

R

A

A

A

Q

I

I

P

R

Q

A

I

M

R

L

L

E

S

T

G

G

V

A

I

I

I

V

N

N

M
x
I

A

S

S
|
S

I

I

A

A

A

G

L

Q

I

I

G

G

L

I

P

E

D

G

R
x
I

F

T

V

P

Y
|
Y

S

T

A

A

K
|
K

G

H

A

G

V

V

K

V

A

G

I

L

T

T

M

K

S

T

V

V

A

A

K

W

D

E

Y

Y

I

G

G

S

E

K

N

G

I

I

R
|
R

C

I

N

N

S

S

I

V

S

G

P
|
P

A
|
A

R

F

V
x
I

H

N

T
|
T

P

T

F

L

V

V

D

-

G

-

F

-

L

-

Q

-

K

-

N

-

Y

-

P

-

D

Q

N

N

I

V

P

P

-

L

E

E

M

T

F

R

E

R

K

Q

L

L

S

E

K

Q

T

M

Q

H

P

A

I
x
L

G
x
R

R
|
R

M

L

A

G

K

E

P

T

E

E

V

V

G

A

A

N

L

L

A

V

L

A

Y

W

L

L

C

S

S
|
S

D

D

E

K

A

A

S

S

F

F

I

V

T

T

G

G

C

S

D

Y

Y

Y

P

A

I

V

D

D

G

G

F

Y

active site: G16 (= G17), S142 (= S138), I152 (≠ R148), Y155 (= Y151), K159 (= K155)
binding 3-pyridinium-1-ylpropane-1-sulfonate: L210 (≠ I214), R211 (≠ G215), R212 (= R216)
binding bicarbonate ion: I92 (= I89), G94 (vs. gap), R109 (= R105), R179 (= R175), S228 (= S232)
binding nicotinamide-adenine-dinucleotide: G12 (= G13), G14 (= G15), N15 (≠ S16), G16 (= G17), I17 (= I18), D36 (≠ E37), I37 (≠ L38), D62 (= D63), T63 (≠ V64), N89 (= N86), A90 (= A87), G91 (= G88), I140 (≠ M136), Y155 (= Y151), K159 (= K155), P185 (= P181), A186 (= A182), I188 (≠ V184), T190 (= T186)

4urfA Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
38% identity, 97% coverage: 4:249/254 of query aligns to 3:245/248 of 4urfA

query
sites
4urfA

L

L

K

E

N

G

K

K

K

T

A

A

V

L

V

V

T

T

G
|
G

G

A

G
|
G

S
x
N

G
|
G

I
|
I

G

G

K

R

A

T

I

I

A

A

T

L

I

T

L

Y

A

A

K

A

Q

E

G

G

A

A

E

N

V

V

H

V

I

V

I

S

E
x
D

L
x
I

G

S

T

D

E

E

H
x
W

A

G

Q

R

D

E

T

T

L

L

D

A

E

L

I

I

K

E

T

G

N

K

G

G

V

K

A

A

F

V

S

F

Y

Q

G

H

C

A

D
|
D

V
x
T

S

A

-

H

-

P

-

E

D

D

H

H

-

D

Q

E

A

L

V

I

A

A

V

A

F

K

N

R

E

A

I

F

G

G

N

R

I

L

N

D

I

I

L

A

I

C

N

N

N
|
N

A
|
A

G
|
G

I
|
I

A
x
S

-
x
G

-
x
E

H

F

I
x
T

G

P

K

T

A

A

D
x
E

T

T

T
|
T

D

D

E

-

A

A

D
x
Q

F

W

D

Q

R
|
R

V

V

M

I

R

G

V

I

N

N

V

L

K

S

G

G

V

V

Y

F

N

Y

C

G

L

V

H

R

A

A

A

Q

I

I

P

R

Q

A

I

M

R

L

L

E

S

T

G

G

V

A

I

I

I

V

N

N

M
x
I

A

S

S
|
S

I

I

A

A

A

G

L

Q

I

I

G

G

L

I

P

E

D

G

R
x
I

F

T

V

P

Y
|
Y

S

T

A

A

K
|
K

G

H

A

G

V

V

K

V

A

G

I

L

T

T

M

K

S

T

V

V

A

A

K

W

D

E

Y

Y

I

G

G
x
S

E

K

N
x
G

I

I

R

R

C

I

N

N

S

S

I

V

S

G

P
|
P

A

A

R

F

V
x
I

H

N

T
|
T

P

T

F

L

V

V

D

-

G

-

F

-

L

-

Q

-

K

-

N

-

Y

-

P

-

D

Q

N

N

I

V

P

P

-

L

E

E

M

T

F

R

E

R

K

Q

L

L

S

E

K

Q

T

M

Q

H

P

A

I

L

G

R

R

R

M

L

A

G

K

E

P

T

E

E

V

V

G

A

A

N

L

L

A

V

L

A

Y

W

L

L

C

S

S

S

D

D

E

K

A

A

S

S

F

F

I

V

T

T

G

G

C
x
S

D
x
Y

Y

Y

P

A

I

V

D

D

G

G

F

Y

active site: G16 (= G17), S142 (= S138), I152 (≠ R148), Y155 (= Y151), K159 (= K155)
binding 3-pyridinium-1-ylpropane-1-sulfonate: I92 (= I89), S93 (≠ A90), G94 (vs. gap), E95 (vs. gap), T97 (≠ I92), E101 (≠ D96), T103 (= T98), Q106 (≠ D102), R109 (= R105), S175 (≠ G171), G177 (≠ N173)
binding magnesium ion: S237 (≠ C241), Y238 (≠ D242)
binding nicotinamide-adenine-dinucleotide: G12 (= G13), G14 (= G15), N15 (≠ S16), G16 (= G17), I17 (= I18), D36 (≠ E37), I37 (≠ L38), W41 (≠ H42), D62 (= D63), T63 (≠ V64), N89 (= N86), A90 (= A87), G91 (= G88), I140 (≠ M136), Y155 (= Y151), K159 (= K155), P185 (= P181), I188 (≠ V184), T190 (= T186)

4ureB Molecular genetic and crystal structural analysis of 1-(4- hydroxyphenyl)-ethanol dehydrogenase from aromatoleum aromaticum ebn1 (see paper)
38% identity, 97% coverage: 4:249/254 of query aligns to 3:245/248 of 4ureB

query
sites
4ureB

L

L

K

E

N

G

K

K

K

T

A

A

V

L

V

V

T

T

G

G

G

A

G

G

S
x
N

G
|
G

I
|
I

G

G

K

R

A

T

I

I

A

A

T

L

I

T

L

Y

A

A

K

A

Q

E

G

G

A

A

E

N

V

V

H

V

I

V

I

S

E

D

L

I

G

S

T

D

E

E

H

W

A

G

Q

R

D

E

T

T

L

L

D

A

E

L

I

I

K

E

T

G

N

K

G

G

V

K

A

A

F

V

S

F

Y

Q

G

H

C

A

D

D

V

T

S

A

-

H

-

P

-

E

D

D

H

H

-

D

Q

E

A

L

V

I

A

A

V

A

F

K

N

R

E

A

I

F

G

G

N

R

I

L

N

D

I

I

L

A

I

C

N

N

N
|
N

A

A

G
|
G

I

I

A

S

-

G

-

E

H

F

I

T

G

P

K

T

A

A

D

E

T

T

D

D

E

-

A

A

D

Q

F

W

D

Q

R

R

V

V

M

I

R

G

V

I

N

N

V

L

K

S

G

G

V

V

Y

F

N

Y

C

G

L

V

H

R

A

A

A

Q

I

I

P

R

Q

A

I

M

R

L

L

E

S

T

G

G

V

A

I

I

I

V

N

N

M

I

A

S

S
|
S

I

I

A

A

A

G

L

Q

I

I

G

G

L

I

P

E

D

G

R
x
I

F

T

V

P

Y
|
Y

S

T

A

A

K
|
K

G

H

A

G

V

V

K

V

A

G

I

L

T

T

M

K

S

T

V

V

A

A

K

W

D

E

Y

Y

I

G

G

S

E

K

N

G

I

I

R

R

C

I

N

N

S

S

I

V

S

G

P
|
P

A
|
A

R

F

V

I

H

N

T

T

P

T

F

L

V

V

D

-

G

-

F

-

L

-

Q

-

K

-

N

-

Y

-

P

-

D

Q

N

N

I

V

P

P

-

L

E

E

M

T

F

R

E

R

K

Q

L

L

S

E

K

Q

T

M

Q

H

P

A

I

L

G

R

R

R

M

L

A

G

K

E

P

T

E

E

V

V

G

A

A

N

L

L

A

V

L

A

Y

W

L

L

C

S

S

S

D

D

E

K

A

A

S

S

F

F

I

V

T

T

G

G

C

S

D

Y

Y

Y

P

A

I

V

D

D

G

G

F

Y

active site: G16 (= G17), S142 (= S138), I152 (≠ R148), Y155 (= Y151), K159 (= K155)
binding 3-pyridinium-1-ylpropane-1-sulfonate: N15 (≠ S16), G16 (= G17), I17 (= I18), N89 (= N86), G91 (= G88), Y155 (= Y151), P185 (= P181), A186 (= A182)

2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
34% identity, 97% coverage: 6:252/254 of query aligns to 2:250/250 of 2cfcA

query
sites
2cfcA

N

S

K

R

K

V

A

A

V

I

V

V

T

T

G
|
G

G

A

G

S

S
|
S

G
|
G

I
x
N

G

G

K

L

A

A

I

I

A

A

T

T

I

R

L

F

A

L

K

A

Q

R

G

G

A

D

E

R

V

V

H

A

I

A

I

L

E
x
D

L
|
L

G

S

T

A

E

E

H

-

A

-

Q

-

D

-

T

T

L

L

D

E

E

E

I

T

K

A

T

R

N

T

G

H

G

W

V

H

A

A

F

Y

S

A

-

D

-

K

-

V

-

L

-

R

Y

V

G

R

C
x
A

D
|
D

V
|
V

S

A

D

D

-

E

-

G

-

D

-

V

H

N

Q

A

A

A

V

I

A

A

V

T

F

M

N

E

E

Q

I

F

G

G

N

A

I

I

N

D

I

V

L

L

I

V

N

N

N
|
N

A
|
A

G
|
G

I

I

-

T

-

G

-

N

A

S

H

E

I

A

G

G

K

V

A

L

D

H

T

T

D

P

E

V

A

E

D

Q

F

F

D

D

R

K

V

V

M

M

R

A

V

V

N

N

V

V

K

R

G

G

V

I

Y

F

N

L

C

G

L

C

H

R

A

A

A

V

I

L

P

P

Q

H

I

M

R

L

L

L

S

Q

G

G

G

A

G

G

V

V

I

I

I

V

N

N

M
x
I

A

A

S
|
S

I

V

A

A

A

S

L

L

I

V

G

A

L
x
F

P

P

D

G

R
|
R

F

S

V

A

Y
|
Y

S

T

A

T

A

S

K
|
K

G

G

A

A

V

V

K

L

A

Q

I

L

T

T

M

K

S

S

V

V

A

A

K

V

D

D

Y

Y

I

A

G

G

E

S

N

G

I

I

R

R

C

C

N

N

S

A

I

V

S

C

P
|
P

A
x
G

R
x
M

V
x
I

H

E

T
|
T

P
|
P

F
x
M

V
x
T

D

Q

G
x
W

F
x
R

L

L

Q

D

K

Q

N

-

Y

-

P

-

D

-

N

-

I

-

P

P

E

E

M

L

F

R

E

D

K

Q

L

V

S

L

K

A

T

R

Q

I

P

P

I

Q

G

K

R

E

M

I

A

G

K

T

P

A

E

A

E

Q

V

V

G

A

A

D

L

A

A

V

L

M

Y

F

L

L

C

A

S

G

D

E

E

D

A

A

S

T

F

Y

I

V

T

N

G

G

C

A

D

A

Y

L

P

V

I

M

D

D

G

G

G

A

F

Y

T

T

T

A

L

I

active site: G13 (= G17), S142 (= S138), Y155 (= Y151), K159 (= K155)
binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ L145), R152 (= R148), Y155 (= Y151), W195 (≠ G191), R196 (≠ F192)
binding nicotinamide-adenine-dinucleotide: G9 (= G13), S12 (= S16), G13 (= G17), N14 (≠ I18), D33 (≠ E37), L34 (= L38), A59 (≠ C62), D60 (= D63), V61 (= V64), N87 (= N86), A88 (= A87), G89 (= G88), I140 (≠ M136), P185 (= P181), G186 (≠ A182), M187 (≠ R183), I188 (≠ V184), T190 (= T186), P191 (= P187), M192 (≠ F188), T193 (≠ V189)

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)
34% identity, 97% coverage: 6:252/254 of query aligns to 2:250/250 of Q56840

query
sites
Q56840

N

S

K

R

K

V

A

A

V

I

V

V

T

T

G

G

G

A

G

S

S
|
S

G
|
G

I
x
N

G

G

K

L

A

A

I

I

A

A

T

T

I

R

L

F

A

L

K

A

Q

R

G

G

A

D

E

R

V

V

H

A

I

A

I

L

E
x
D

L

L

G

S

T

A

E

E

H

-

A

-

Q

-

D

-

T

T

L

L

D

E

E

E

I

T

K

A

T

R

N

T

G

H

G

W

V

H

A

A

F

Y

S

A

-

D

-

K

-

V

-

L

-

R

Y

V

G

R

C

A

D
|
D

V
|
V

S

A

D

D

-

E

-

G

-

D

-

V

H

N

Q

A

A

A

V

I

A

A

V

T

F

M

N

E

E

Q

I

F

G

G

N

A

I

I

N

D

I

V

L

L

I

V

N

N

N
|
N

A

A

G

G

I

I

-

T

-

G

-

N

A

S

H

E

I

A

G

G

K

V

A

L

D

H

T

T

D

P

E

V

A

E

D

Q

F

F

D

D

R

K

V

V

M

M

R

A

V

V

N

N

V

V

K

R

G

G

V

I

Y

F

N

L

C

G

L

C

H

R

A

A

A

V

I

L

P

P

Q

H

I

M

R

L

L

L

S

Q

G

G

G

A

G

G

V

V

I

I

I

V

N

N

M

I

A

A

S
|
S

I

V

A

A

A

S

L

L

I

V

G

A

L

F

P

P

D

G

R
|
R

F

S

V

A

Y
|
Y

S

T

A

T

A

S

K
|
K

G

G

A

A

V

V

K

L

A

Q

I

L

T

T

M

K

S

S

V

V

A

A

K

V

D

D

Y

Y

I

A

G

G

E

S

N

G

I

I

R
|
R

C

C

N

N

S

A

I

V

S

C

P

P

A

G

R

M

V
x
I

H
x
E

T
|
T

P
|
P

F
x
M

V

T

D

Q

G
x
W

F
x
R

L

L

Q

D

K

Q

N

-

Y

-

P

-

D

-

N

-

I

-

P

P

E

E

M

L

F
x
R

E

D

K

Q

L

V

S

L

K

A

T
x
R

Q

I

P

P

I

Q

G

K

R

E

M

I

A

G

K

T

P

A

E

A

E

Q

V

V

G

A

A

D

L

A

A

V

L

M

Y

F

L

L

C

A

S

G

D

E

E

D

A

A

S

T

F

Y

I

V

T

N

G

G

C

A

D

A

Y

L

P

V

I

M

D

D

G

G

G

A

F

Y

T

T

T

A

L

I

SGN 12:14 (≠ SGI 16:18) binding
D33 (≠ E37) binding
DV 60:61 (= DV 63:64) binding
N87 (= N86) binding
S142 (= S138) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
R152 (= R148) binding ; mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
Y155 (= Y151) mutation Y->E,F: Loss of activity.
K159 (= K155) mutation to A: Loss of activity.
R179 (= R175) mutation to A: Loss of activity.
IETPM 188:192 (≠ VHTPF 184:188) binding
WR 195:196 (≠ GF 191:192) binding
R196 (≠ F192) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
R203 (≠ F205) mutation to A: Slight decrease in catalytic efficiency.
R209 (≠ T211) mutation to A: Does not affect catalytic efficiency.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

6xewA Structure of serratia marcescens 2,3-butanediol dehydrogenase (see paper)
37% identity, 97% coverage: 4:250/254 of query aligns to 3:242/251 of 6xewA

query
sites
6xewA

L

F

K

D

N

N

K

K

K

V

A

V

V

V

V

I

T

T

G
|
G

G

A

G

G

S
x
N

G
|
G

I
x
M

G

G

K

E

A

A

I

A

A

A

T

R

I

R

L

F

A

S

K

A

Q

E

G

G

A

A

E

I

V

V

H

V

I

L

I

-

E

-

L

-

G

-

T

A

E
x
D

H
x
W

A
|
A

Q

K

D

E

T

A

L

V

D

D

E

K

I

V

K

A

T

A

N

S

-

L

-

P

G

K

G

G

V

R

A

A

F

M

S

A

Y

V

G

H

C
x
I

D
|
D

V
|
V

S

S

D

D

H

H

Q

V

A

A

V

V

A

E

A

K

V

M

F

M

N

N

E

E

I

V

-

A

-

E

-

K

-

L

G

G

N

R

I

I

N

D

I

V

L

L

I

L

N

N

N
|
N

A
|
A

G
|
G

I

V

A

H

H

V

I

A

G

G

K

S

A

V

D

L

T

E

T

T

D

S

E

I

A

D

D

D

F

W

D

R

R

R

V

I

M

A

R

G

V
|
V

N

D

V

I

K

D

G

G

V

V

Y

V

N

F

C

C

L

S

H

K

A

F

A

A

I

L

P

P

Q

H

I

L

R

-

L

L

S

K

G

T

G

K

G

G

V

C

I

I

I

V

N

N

M
x
T

A

A

S
|
S

I

V

A
x
S

A

G

L

L

I

G

G

G

L

D

P

W

D

G

R

A

F

A

V

Y

Y
|
Y

S

C

A

A

K
|
K

G

G

A

A

V

V

K

V

A

N

I

L

T

T

M

R

S

A

V

M

A

A

K

L

D

D

Y

H

I

G

G

G

E

D

N

G

I

V

R

R

C

I

N

N

S

S

I

V

S

C

P

P

A
x
S

R
x
L

V
|
V

H

K

T
|
T

P
x
N

F
x
M

V
x
T

D

N

G

G

F

W

L

P

Q

Q

K

-

N

-

Y

-

P

-

D

-

N

-

I

-

P

-

E

E

M

I

F

R

E

D

K

K

L

F

S

N

K

E

T

R

Q

I

P

A

I

L

G

G

R

R

M

A

A

A

K

E

P

P

E

E

V

V

G

A

A

A

L

V

A

M

L

A

Y

F

L

L

C

A

S

S

D

D

E

D

A

A

S

S

F

F

I

I

T

N

G

G

C

A

D

N

Y

I

P

P

I

V

D

D

G

G

F

A

T

T

active site: G16 (= G17), S138 (= S138), Y151 (= Y151)
binding r,3-hydroxybutan-2-one: S138 (= S138), S140 (≠ A140), Y151 (= Y151)
binding s,3-hydroxybutan-2-one: S138 (= S138), Y151 (= Y151), S182 (≠ A182)
binding nicotinamide-adenine-dinucleotide: G12 (= G13), N15 (≠ S16), G16 (= G17), M17 (≠ I18), D36 (≠ E41), W37 (≠ H42), W37 (≠ H42), A38 (= A43), I59 (≠ C62), D60 (= D63), V61 (= V64), N87 (= N86), A88 (= A87), G89 (= G88), V110 (= V109), T136 (≠ M136), S138 (= S138), Y151 (= Y151), K155 (= K155), S182 (≠ A182), L183 (≠ R183), V184 (= V184), T186 (= T186), N187 (≠ P187), M188 (≠ F188), T189 (≠ V189)

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, 98% coverage: 2:250/254 of query aligns to 1:242/251 of H9XP47

query
sites
H9XP47

F

M

S

R

L

F

K

D

N

N

K

K

K

V

A

V

V

V

V

I

T

T

G

G

G

A

G

G

S
x
N

G

G

I
x
M

G

G

K

E

A

A

I

A

A

A

T

R

I

R

L

F

A

S

K

A

Q

E

G

G

A

A

E

I

V

V

H

V

I

L

I

-

E

-

L

-

G

-

T

A

E
x
D

H

W

A

A

Q

K

D

E

T

A

L

V

D

D

E

K

I

V

K

A

T

A

N

S

-

L

-

P

G

K

G

G

V

R

A

A

F

M

S

A

Y

V

G

H

C

I

D
|
D

V
|
V

S

S

D

D

H

H

Q

V

A

A

V

V

A

E

A

K

V

M

F

M

N

N

E

E

I

V

-

A

-

E

-

K

-

L

G

G

N

R

I

I

N

D

I

V

L

L

I

L

N

N

N
|
N

A

A

G

G

I

V

A

H

H

V

I

A

G

G

K

S

A

V

D

L

T

E

T

T

D

S

E

I

A

D

D

D

F

W

D

R

R

R

V

I

M

A

R

G

V

V

N

D

V

I

K

D

G

G

V

V

Y

V

N

F

C

C

L

S

H

K

A

F

A

A

I

L

P

P

Q

H

I

L

R

-

L

L

S

K

G

T

G

K

G

G

V

C

I

I

I

V

N

N

M

T

A

A

S
|
S

I
x
V

A
x
S

A

G

L

L

I

G

G

G

L

D

P

W

D

G

R

A

F

A

V

Y

Y
|
Y

S

C

A

A

K
|
K

G

G

A

A

V

V

K

V

A

N

I

L

T

T

M

R

S

A

V

M

A

A

K

L

D

D

Y

H

I

G

G

G

E

D

N

G

I

V

R

R

C

I

N

N

S

S

I

V

S

C

P

P

A

S

R

L

V
|
V

H

K

T
|
T

P

N

F

M

V

T

D

N

G

G

F

W

L

P

Q

Q

K

-

N

-

Y

-

P

-

D

-

N

-

I

-

P

-

E

E

M

I

F
x
R

E
x
D

K
|
K

L

F

S

N

K

E

T

R

Q

I

P

A

I

L

G

G

R

R

M

A

A

A

K

E

P

P

E

E

V

V

G

A

A

A

L

V

A

M

L

A

Y

F

L

L

C

A

S

S

D

D

E

D

A

A

S

S

F

F

I

I

T

N

G

G

C

A

D

N

Y

I

P

P

I

V

D

D

G

G

F

A

T

T

N15 (≠ S16) binding
M17 (≠ I18) binding
D36 (≠ E41) binding
D60 (= D63) binding
V61 (= V64) binding
N87 (= N86) binding
S138 (= S138) binding ; binding
V139 (≠ I139) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
S140 (≠ A140) binding
Y151 (= Y151) binding ; binding ; binding
K155 (= K155) binding
V184 (= V184) binding
T186 (= T186) binding
RDK 197:199 (≠ FEK 205:207) 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)
37% identity, 97% coverage: 4:250/254 of query aligns to 5:244/252 of 6vspB

query
sites
6vspB

L

F

K

D

N

N

K

K

K

V

A

V

V

V

V

I

T

T

G
|
G

G

A

G

G

S
x
N

G
|
G

I

M

G

G

K

E

A

A

I

A

A

A

T

R

I

R

L

F

A

S

K

A

Q

E

G

G

A

A

E

I

V

V

H

V

I

L

I

-

E

-

L

-

G

-

T

A

E
x
D

H
x
W

A

A

Q

K

D

E

T

A

L

V

D

D

E

K

I

V

K

A

T

A

N

S

-

L

-

P

G

K

G

G

V

R

A

A

F

M

S

A

Y

V

G

H

C
x
I

D
|
D

V
|
V

S

S

D

D

H

H

Q

V

A

A

V

V

A

E

A

K

V

M

F

M

N

N

E

E

I

V

-

A

-

E

-

K

-

L

G

G

N

R

I

I

N

D

I

V

L

L

I

L

N

N

A

A

G
|
G

I

V

A

H

H

V

I

A

G

G

K

S

A

V

D

L

T

E

T

T

D

S

E

I

A

D

D

D

F

W

D

R

R

R

V

I

M

A

R

G

V

V

N

D

V

I

K

D

G

G

V

V

Y

V

N

F

C

C

L

S

H

K

A

F

A

A

I

L

P

P

Q

H

I

L

R

-

L

L

S

K

G

T

G

K

G

G

V

C

I

I

I

V

N

N

M

T

A

A

S
|
S

I

V

A

S

A

G

L

L

I

G

G

G

L

D

P

W

D

G

R

A

F

A

V

Y

Y
|
Y

S

C

A

A

K

K

G

G

A

A

V

V

K

V

A

N

I

L

T

T

M

R

S

A

V

M

A

A

K

L

D

D

Y

H

I

G

G

G

E

D

N

G

I

V

R

R

C

I

N

N

S

S

I

V

S

C

P

P

A

S

R

L

V

V

H

K

T

T

P

N

F

M

V

T

D

N

G

G

F

W

L

P

Q

Q

K

-

N

-

Y

-

P

-

D

-

N

-

I

-

P

-

E

E

M

I

F

R

E

D

K

K

L

F

S

N

K

E

T

R

Q

I

P

A

I

L

G

G

R

R

M

A

A

A

K

E

P

P

E

E

V

V

G

A

A

A

L

V

A

M

L

A

Y

F

L

L

C

A

S

S

D

D

E

D

A

A

S

S

F

F

I

I

T

N

G

G

C

A

D

N

Y

I

P

P

I

V

D

D

G

G

F

A

T

T

active site: G18 (= G17), S140 (= S138), Y153 (= Y151)
binding adenosine-5'-diphosphate: G14 (= G13), N17 (≠ S16), D38 (≠ E41), W39 (≠ H42), I61 (≠ C62), D62 (= D63), V63 (= V64), G91 (= G88)

6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
37% identity, 97% coverage: 4:250/254 of query aligns to 3:242/251 of 6vspA

query
sites
6vspA

L

F

K

D

N

N

K

K

K

V

A

V

V

V

V

I

T

T

G
|
G

G

A

G

G

S
x
N

G
|
G

I
x
M

G

G

K

E

A

A

I

A

A

A

T

R

I

R

L

F

A

S

K

A

Q

E

G

G

A

A

E

I

V

V

H

V

I

L

I

-

E

-

L

-

G

-

T

A

E
x
D

H
x
W

A
|
A

Q

K

D

E

T

A

L

V

D

D

E

K

I

V

K

A

T

A

N

S

-

L

-

P

G

K

G

G

V

R

A

A

F

M

S

A

Y

V

G

H

C
x
I

D
|
D

V
|
V

S

S

D

D

H

H

Q

V

A

A

V

V

A

E

A

K

V

M

F

M

N

N

E

E

I

V

-

A

-

E

-

K

-

L

G

G

N

R

I

I

N

D

I

V

L

L

I

L

N

N

N
|
N

A
|
A

G
|
G

I
x
V

A

H

H

V

I

A

G

G

K

S

A

V

D

L

T

E

T

T

D

S

E

I

A

D

D

D

F

W

D

R

R

R

V

I

M

A

R

G

V
|
V

N

D

V

I

K

D

G

G

V

V

Y

V

N

F

C

C

L

S

H

K

A

F

A

A

I

L

P

P

Q

H

I

L

R

-

L

L

S

K

G

T

G

K

G

G

V

C

I

I

I

V

N

N

M
x
T

A

A

S
|
S

I

V

A

S

A

G

L

L

I

G

G

G

L

D

P

W

D

G

R

A

F

A

V

Y

Y
|
Y

S

C

A

A

K
|
K

G

G

A

A

V

V

K

V

A

N

I

L

T

T

M

R

S

A

V

M

A

A

K

L

D

D

Y

H

I

G

G

G

E

D

N

G

I

V

R

R

C

I

N

N

S

S

I

V

S

C

P
|
P

A
x
S

R
x
L

V
|
V

H

K

T
|
T

P
x
N

F
x
M

V
x
T

D

N

G

G

F

W

L

P

Q

Q

K

-

N

-

Y

-

P

-

D

-

N

-

I

-

P

-

E

E

M

I

F

R

E

D

K

K

L

F

S

N

K

E

T

R

Q

I

P

A

I

L

G

G

R

R

M

A

A

A

K

E

P

P

E

E

V

V

G

A

A

A

L

V

A

M

L

A

Y

F

L

L

C

A

S

S

D

D

E

D

A

A

S

S

F

F

I

I

T

N

G

G

C

A

D

N

Y

I

P

P

I

V

D

D

G

G

F

A

T

T

active site: G16 (= G17), S138 (= S138), Y151 (= Y151)
binding nicotinamide-adenine-dinucleotide: G12 (= G13), N15 (≠ S16), G16 (= G17), M17 (≠ I18), D36 (≠ E41), W37 (≠ H42), W37 (≠ H42), A38 (= A43), I59 (≠ C62), D60 (= D63), V61 (= V64), N87 (= N86), A88 (= A87), G89 (= G88), V90 (≠ I89), V110 (= V109), T136 (≠ M136), S138 (= S138), Y151 (= Y151), K155 (= K155), P181 (= P181), S182 (≠ A182), L183 (≠ R183), V184 (= V184), T186 (= T186), N187 (≠ P187), M188 (≠ F188), T189 (≠ V189)

A7IQH5 2-(S)-hydroxypropyl-CoM dehydrogenase 3; S-HPCDH 3; 2-[(S)-2-hydroxypropylthio]ethanesulfonate dehydrogenase 3; Aliphatic epoxide carboxylation component IV; Epoxide carboxylase component IV; SHPCDH3; EC 1.1.1.269 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 2 papers)
35% identity, 89% coverage: 28:252/254 of query aligns to 29:255/255 of A7IQH5

query
sites
A7IQH5

K

R

Q

E

G

G

A

A

E

K

V

V

H

A

I

L

I

I

E
x
D

L

L

G

D

T

Q

E

G

H

L

A

A

Q

E

D

R

T

S

L

A

D

A

E

M

I

L

K

S

T

T

N

G

G

G

G

A

V

V

A

A

F

K

S

G

Y

F

G

G

C

A

D
|
D

V
|
V

S

T

D

K

H

A

Q

A

A

D

V

I

A

T

A

A

V

A

F

I

N

T

E

S

-

A

-

E

-

Q

-

T

I

I

G

G

N

S

I

L

N

T

I

G

L

L

I

V

N

N

N
|
N

A

A

G

G

I

I

A

A

H

G

I

F

G

G

K

S

A

V

D

H

T

D

T

A

D

D

E

A

A

A

D

A

F

W

D

D

R

R

V

I

M

M

R

A

V

V

N

N

V

V

K

T

G

G

V

T

Y

F

N

L

C

A

L

S

H

K

A

A

I

L

P

A

Q

G

I

M

R

L

L

E

S

R

G

H

G

K

G

G

V

T

I

I

I

V

N

N

M

F

A

G

S
|
S

I

V

A

A

A

G

L

L

I

V

G

G

L

I

P

P

D

T

R

M

F

A

V

A

Y
|
Y

S

C

A

A

K
|
K

G

G

A

A

V

I

K

V

A

N

I

L

T

T

M

R

S

Q

V

M

A

A

K

A

D

D

Y

Y

I

S

G

G

E

R

N

G

I

V

R

R

C

V

N

N

S

A

I

V

S

C

P

P

A

G

R
x
T

V
|
V

H
x
T

T
x
S

P
x
T

F

-

V

-

D

-

G
|
G

F

M

L

G

Q

Q

K

Q

N

L

Y

L

-

G

P

S

D

D

N

T

I

S

P

P

E

E

M

V

F

Q

E

A

K

R

L
x
R

S

L

K

A

T
x
K

Q
x
Y

P

P

I

I

G

G

R

R

M

F

A

G

K

T

P

P

E

E

E

D

V

I

G

A

A

E

L

A

A

V

L

I

Y

F

L

L

C

L

S

S

D

D

E

Q

A

A

S

A

F

F

I

V

T

T

G

G

C

A

D

A

Y

F

P

A

I

V

D

D

G

G

F

M

T

T

T

A

L

I

D38 (≠ E37) binding
DV 64:65 (= DV 63:64) binding
N91 (= N86) binding
S143 (= S138) binding ; mutation to A: Retains very weak activity.
Y156 (= Y151) binding ; mutation to A: Retains some activity but with more than 2200-fold decrease in catalytic efficiency.; mutation to F: Loss of activity.
K160 (= K155) binding ; mutation to A: Loss of activity.
T188 (≠ R183) binding
VTST---G 189:193 (≠ VHTPFVDG 184:191) binding
R211 (≠ L208) mutation to A: Severely impaired in the oxidation of S-HPC or reduction of 2-KPC but largely unaffected in the oxidation and reduction of aliphatic alcohols and ketones.
K214 (≠ T211) mutation to A: Severely impaired in the oxidation of S-HPC or reduction of 2-KPC but largely unaffected in the oxidation and reduction of aliphatic alcohols and ketones.
Y215 (≠ Q212) binding

Sites not aligning to the query:

19 binding

4ituA Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) bound to s-hpc and nadh (see paper)
35% identity, 89% coverage: 28:252/254 of query aligns to 27:253/253 of 4ituA

query
sites
4ituA

K

R

Q

E

G

G

A

A

E

K

V

V

H

A

I

L

I

I

E
x
D

L
|
L

G

D

T

Q

E

G

H

L

A

A

Q

E

D

R

T

S

L

A

D

A

E

M

I

L

K

S

T

T

N

G

G

G

G

A

V

V

A

A

F

K

S

G

Y

F

G

G

C

A

D
|
D

V
|
V

S

T

D

K

H

A

Q

A

A

D

V

I

A

T

A

A

V

A

F

I

N

T

E

S

-

A

-

E

-

Q

-

T

I

I

G

G

N

S

I

L

N

T

I

G

L

L

I

V

N

N

N
|
N

A

A

G

G

I

I

A

A

H

G

I

F

G

G

K

S

A

V

D

H

T

D

T

A

D

D

E

A

A

A

D

A

F

W

D

D

R

R

V

I

M

M

R

A

V
|
V

N
|
N

V

V

K

T

G

G

V

T

Y

F

N

L

C

A

L

S

H

K

A

A

I

L

P

A

Q

G

I

M

R

L

L

E

S

R

G

H

G

K

G

G

V

T

I

I

I

V

N

N

M
x
F

A

G

S
|
S

I

V

A

A

A

G

L

L

I

V

G

G

L

I

P

P

D

T

R

M

F

A

V

A

Y
|
Y

S

C

A

A

K
|
K

G

G

A

A

V

I

K

V

A

N

I

L

T

T

M

R

S

Q

V

M

A

A

K

A

D

D

Y

Y

I

S

G

G

E

R

N

G

I

V

R

R

C

V

N

N

S

A

I

V

S

C

P
|
P

A

G

R
x
T

V
|
V

H

T

T

S

P
x
T

F

-

V

-

D

-

G

G

F
x
M

L

G

Q

Q

K

Q

N

L

Y

L

-

G

P

S

D

D

N

T

I

S

P

P

E

E

M

V

F

Q

E

A

K

R

L
x
R

S

L

K

A

T

K

Q
x
Y

P

P

I

I

G

G

R

R

M

F

A

G

K

T

P

P

E

E

E

D

V

I

G

A

A

E

L

A

A

V

L

I

Y

F

L

L

C

L

S

S

D

D

E

Q

A

A

S

A

F

F

I

V

T

T

G

G

C

A

D

A

Y

F

P

A

I

V

D

D

G

G

F

M

T

T

T

A

L

I

active site: N113 (= N110), S141 (= S138), Y154 (= Y151), K158 (= K155)
binding 2-{[(2S)-2-hydroxypropyl]sulfanyl}ethanesulfonic acid: S141 (= S138), Y154 (= Y151), T186 (≠ R183), R209 (≠ L208), Y213 (≠ Q212)
binding 1,4-dihydronicotinamide adenine dinucleotide: D36 (≠ E37), L37 (= L38), D62 (= D63), V63 (= V64), N89 (= N86), V112 (= V109), F139 (≠ M136), S141 (= S138), Y154 (= Y151), K158 (= K155), P184 (= P181), T186 (≠ R183), V187 (= V184), T190 (≠ P187), M192 (≠ F192)

Sites not aligning to the query:

active site: 16
binding 1,4-dihydronicotinamide adenine dinucleotide: 12, 16, 17

7v1qA Leifsonia alcohol dehydrogenases lnadh (see paper)
36% identity, 98% coverage: 2:250/254 of query aligns to 4:249/251 of 7v1qA

query
sites
7v1qA

F

Y

S

D

L

V

K

A

N

D

K

R

K

S

A

A

V

I

V

V

T

T

G
|
G

G

G

S
|
S

G
|
G

I
|
I

G

G

K

R

A

A

I

V

A

A

T

L

I

T

L

L

A

A

K

A

Q

S

G

G

A

A

E

A

V

V

H

L

I

V

I

T

E
x
D

L
|
L

G

N

T

E

E

E

H

H

A

A

Q

Q

D

A

T

V

L

V

D

A

E

E

I

I

K

E

T

A

N

A

G

G

V

K

A

A

F

A

S

A

Y

L

G

A

C

G

D
|
D

V
|
V

S

T

D

D

-

P

-

A

-

F

H

G

Q

E

A

A

V

S

A

V

A

A

V

A

F

A

N

N

E

A

I

L

G

A

N

P

I

L

N

K

I

I

L

A

I

V

N

N

N
|
N

A

A

G

G

I

I

A

G

H

-

I

-

G

G

K

E

A

A

D

A

T

T

T

V

D

G

E

D

A

Y

D

S

F

L

D

D

-

S

-

W

-

R

R

K

V

V

M

I

R

E

V

V

N

N

V

L

K

N

G

A

V

V

Y

F

N

Y

C

G

L

M

H

Q

A

P

A

Q

I

L

P

K

Q

A

I

M

R

A

L

A

S

N

G

G

V

A

I

I

I

V

N

N

M
|
M

A

A

S

S

I

I

A

L

A

G

L

S

I

V

G

G

L

F

P

A

D

N

R

S

F

S

V

A

Y
|
Y

S

V

A

T

A

A

K
|
K

G

H

A

A

V

L

K

L

A

G

I

L

T

T

M

Q

S

N

V

A

A

A

K

L

D

E

Y

Y

I

A

G

A

E

D

N

K

I

V

R

R

C

V

N

V

S

A

I

V

S

G

P
|
P

A
x
G

R
x
F

V
x
I

H

R

T

T

P

P

F

L

V

V

D

E

G

A

F

N

L

L

Q

S

K

A

N

-

Y

-

P

-

D

-

N

-

I

-

P

-

E

E

M

A

F

L

E

A

K

F

L

L

S

E

K

G

T

K

Q

H

P

A

I

L

G

G

R

R

M

L

A

G

K

E

P

P

E

E

V

V

G

A

A

S

L

L

A

V

L

A

Y

F

L

L

C

A

S

S

D

D

E

A

A

A

S

S

F

F

I

I

T

T

G

G

C

S

D

Y

Y

H

P

L

I

V

D

D

G

G

F

Y

T

T

binding nicotinamide-adenine-dinucleotide: G15 (= G13), S18 (= S16), G19 (= G17), I20 (= I18), D39 (≠ E37), L40 (= L38), D65 (= D63), V66 (= V64), N91 (= N86), M142 (= M136), Y157 (= Y151), K161 (= K155), P187 (= P181), G188 (≠ A182), F189 (≠ R183), I190 (≠ V184)

2q2qD Structure of d-3-hydroxybutyrate dehydrogenase from pseudomonas putida (see paper)
34% identity, 97% coverage: 3:249/254 of query aligns to 1:252/255 of 2q2qD

query
sites
2q2qD

S

T

L

L

K

K

N

G

K

K

K

T

A

A

V

L

V

V

T

T

G
|
G

G

S

G
x
T

S
|
S

G
|
G

I
|
I

G

G

K

L

A

G

I

I

A

A

T

Q

I

V

L

L

A

A

K

R

Q

A

G

G

A

A

E

-

V

-

H

N

I

I

I

V

E

L

L

N

G

G

T
x
F

E

G

H

D

A

P

Q

A

D

P

T

A

L

L

D

A

E

E

I

I

K

A

T

R

N

H

G

G

G

V

V

K

A

A

F

V

S

H

Y

H

G

P

C

A

D
|
D

V
x
L

S

S

D

D

H

V

Q

A

A

Q

V

I

A

E

A

A

V

L

F

F

-

A

-

L

-

A

-

E

N

R

E

E

I

F

G

G

N

G

I

V

N

D

I

I

L

L

I

V

N

N

N
|
N

A

A

G
|
G

I

I

A

Q

H

H

I

V

G

A

K

P

A

V

D

E

T

Q

T

F

D

P

E

L

A

E

D

S

F

W

D

D

R

K

V

I

M

I

R

A

V
x
L

N

N

V

L

K

S

G

A

V

V

Y

F

N

H

C

G

L

T

H

R

A

L

A

A

I

L

P

P

Q

G

I

M

R

R

L

A

S

R

G

N

G

W

G

G

V

R

I

I

N

N

M
x
I

A

A

S
|
S

I

V

A

H

A

G

L

L

I

V

G

G

L

S

P

T

D

G

R

K

F

A

V

A

Y
|
Y

S

V

A

A

K
|
K

G

H

A

G

V

V

K

V

A

G

I

L

T

T

M

K

S

V

V

V

A

G

K

L

D

E

Y

T

I

A

G

T

E

S

N

N

I

V

R

T

C

C

N

N

S

A

I

I

S

C

P
|
P

A
x
G

R
x
W

V
|
V

H

L

T
|
T

P

P

F
x
L

V
|
V

D

Q

G

K

F

Q

L

I

Q

D

-

D

-
x
R

-

A

K

A

N

N

Y

G

P

G

D

D

N

P

I

L

P

Q

E

A

M

Q

F

H

E

D

K

L

L

L

S

A

K

E

T

K

Q

Q

P

P

I

S

G

L

R

A

M

F

A

V

K

T

P

P

E

E

E

H

V

L

G

G

A

E

L

L

A

V

L

L

Y

F

L

L

C

C

S

S

D

E

E

A

A

G

S

S

F

Q

I

V

T

R

G

G

C

A

D

A

Y

W

P

N

I

V

D

D

G

G

F

W

active site: G15 (= G17), S138 (= S138), Y151 (= Y151), K155 (= K155), R196 (vs. gap)
binding nicotinamide-adenine-dinucleotide: G11 (= G13), T13 (≠ G15), S14 (= S16), G15 (= G17), I16 (= I18), F36 (≠ T40), D59 (= D63), L60 (≠ V64), N86 (= N86), G88 (= G88), L109 (≠ V109), I136 (≠ M136), S138 (= S138), Y151 (= Y151), K155 (= K155), P181 (= P181), G182 (≠ A182), W183 (≠ R183), V184 (= V184), T186 (= T186), L188 (≠ F188), V189 (= V189)

4gh5A Crystal structure of s-2-hydroxypropyl coenzyme m dehydrogenase (s- hpcdh) (see paper)
34% identity, 89% coverage: 28:252/254 of query aligns to 27:248/248 of 4gh5A

query
sites
4gh5A

K

R

Q

E

G

G

A

A

E

K

V

V

H

A

I

L

I

I

E
x
D

L
|
L

G

D

T

Q

E

G

H

L

A

A

Q

E

D

R

T

S

L

A

D

A

E

M

I

L

K

S

T

T

N

G

G

G

G

A

V

V

A

A

F

K

S

G

Y

F

G

G

C
x
A

D
|
D

V
|
V

S

T

D

K

H

A

Q

A

A

D

V

I

A

T

A

A

V

A

F

I

N

T

E

S

-

A

-

E

-

Q

-

T

I

I

G

G

N

S

I

L

N

T

I

G

L

L

I

V

N

N

N
|
N

A
|
A

G

G

I

I

A

A

H

G

I

F

G

G

K

S

A

V

D

H

T

D

T

A

D

D

E

A

A

A

D

A

F

W

D

D

R

R

V

I

M

M

R

A

V
|
V

N
|
N

V

V

K

T

G

G

V

T

Y

F

N

L

C

A

L

S

H

K

A

A

I

L

P

A

Q

G

I

M

R

L

L

E

S

R

G

H

G

K

G

G

V

T

I

I

I

V

N

N

M
x
F

A

G

S
|
S

I

V

A

A

A

G

L

L

I

V

G

G

L

I

P

P

D

T

R

M

F

A

V

A

Y
|
Y

S

C

A

A

K
|
K

G

G

A

A

V

I

K

V

A

N

I

L

T

T

M

R

S

Q

V

M

A

A

K

A

D

D

Y

Y

I

S

G

G

E

R

N

G

I

V

R

R

C

V

N

N

S

A

I

V

S

C

P
|
P

A

G

R

T

V
|
V

H

T

T

S

P
x
T

F

-

V

-

D

-

G
|
G

F
x
M

L

G

Q

Q

K

Q

N

-

Y

-

P

-

D

-

N

L

I

L

P

P

E

E

M

V

F

Q

E

A

K

R

L

R

S

L

K

A

T

K

Q

Y

P

P

I

I

G

G

R

R

M

F

A

G

K

T

P

P

E

E

E

D

V

I

G

A

A

E

L

A

A

V

L

I

Y

F

L

L

C

L

S

S

D

D

E

Q

A

A

S

A

F

F

I

V

T

T

G

G

C

A

D

A

Y

F

P

A

I

V

D

D

G

G

F

M

T

T

T

A

L

I

active site: N113 (= N110), S141 (= S138), Y154 (= Y151), K158 (= K155)
binding nicotinamide-adenine-dinucleotide: D36 (≠ E37), L37 (= L38), A61 (≠ C62), D62 (= D63), V63 (= V64), N89 (= N86), A90 (= A87), V112 (= V109), F139 (≠ M136), S141 (= S138), Y154 (= Y151), K158 (= K155), P184 (= P181), V187 (= V184), T190 (≠ P187), G191 (= G191), M192 (≠ F192)

Sites not aligning to the query:

active site: 16
binding nicotinamide-adenine-dinucleotide: 12, 16, 17

Query Sequence

>CA265_RS08355 CA265_RS08355 short-chain dehydrogenase
MFSLKNKKAVVTGGGSGIGKAIATILAKQGAEVHIIELGTEHAQDTLDEIKTNGGVAFSY
GCDVSDHQAVAAVFNEIGNINILINNAGIAHIGKADTTDEADFDRVMRVNVKGVYNCLHA
AIPQIRLSGGGVIINMASIAALIGLPDRFVYSAAKGAVKAITMSVAKDYIGENIRCNSIS
PARVHTPFVDGFLQKNYPDNIPEMFEKLSKTQPIGRMAKPEEVGALALYLCSDEASFITG
CDYPIDGGFTTLNN

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