SitesBLAST

Q8WNV7 Dehydrogenase/reductase SDR family member 4; NADPH-dependent carbonyl reductase; CR; PHCR; NADPH-dependent retinol dehydrogenase/reductase; NDRD; Peroxisomal carbonyl reductase; PerCR; Peroxisomal short-chain alcohol dehydrogenase; PSCD; Short chain dehydrogenase/reductase family 25C member 2; Protein SDR25C2; EC 1.1.1.184; EC 1.1.1.300 from Sus scrofa (Pig) (see 2 papers)
35% identity, 98% coverage: 4:247/250 of query aligns to 31:274/279 of Q8WNV7

query
sites
Q8WNV7

F

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G

37:61 (vs. 10:34, 48% identical) binding NADP(+)
F177 (≠ G150) Responsible for the stereoselective reduction of 3-ketosteroids into 3alpha-hydroxysteroids and benzil into S-benzoin; mutation to S: Change in stereoselective activity by the reduction of 3-ketosteroids and benzil into 3beta-hydroxysteroid and R-benzoin, respectively; when associated with F-180.
L180 (≠ Q153) Responsible for the stereoselective reduction of 3-ketosteroids into 3alpha-hydroxysteroids and benzil into S-benzoin; mutation to F: Change in stereoselective activity by the reduction of 3-ketosteroids and benzil into 3beta-hydroxysteroid and R-benzoin, respectively; when associated with S-177.
Y183 (= Y156) active site, Proton acceptor
K187 (= K160) binding NADP(+)
N196 (≠ S169) Important for the maintenance of the quaternary structure, the catalytic activity and cold stability

Sites not aligning to the query:

277:279 Peroxisomal targeting signal

2zatA Crystal structure of a mammalian reductase (see paper)
35% identity, 98% coverage: 4:247/250 of query aligns to 3:246/251 of 2zatA

query
sites
2zatA

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active site: G16 (= G17), S142 (= S143), L152 (≠ Q153), Y155 (= Y156), K159 (= K160), K200 (≠ E201)
binding nadp nicotinamide-adenine-dinucleotide phosphate: A12 (≠ G13), T14 (≠ S15), D15 (≠ R16), G16 (= G17), I17 (= I18), S36 (= S37), R37 (= R38), K38 (≠ S39), N41 (≠ G42), H62 (= H63), N89 (= N90), A91 (= A92), V140 (≠ T141), S142 (= S143), Y155 (= Y156), K159 (= K160), P185 (= P186), G186 (= G187), I188 (≠ T189), T190 (= T191), F192 (= F193), S193 (≠ A194)

C1DMX5 L-rhamnose 1-dehydrogenase (NAD(P)(+)); RhaDH; AvLRA1; EC 1.1.1.378 from Azotobacter vinelandii (strain DJ / ATCC BAA-1303) (see paper)
39% identity, 98% coverage: 6:249/250 of query aligns to 5:252/256 of C1DMX5

query
sites
C1DMX5

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G12 (= G13) binding NADP(+)
S14 (= S15) binding NADP(+)
R15 (= R16) binding NADP(+); mutation to T: Increases specificity toward NAD(+). Shows a strong decrease in catalytic efficiency with NADP(+).
I17 (= I18) binding NADP(+)
S37 (vs. gap) binding NADP(+); mutation to H: Increases specificity toward NAD(+). Shows a strong decrease in catalytic efficiency with NADP(+) and an increase in catalytic efficiency with NAD(+).
D66 (≠ H63) binding NADP(+)
A67 (≠ N64) binding NADP(+)
N93 (= N90) binding NADP(+)
F99 (= F97) mutation F->A,Y: Shows a strong decrease in catalytic efficiency with L-rhamnose, L-lyxose and L-mannose.
S146 (= S143) binding beta-L-rhamnose
S148 (≠ N145) binding beta-L-rhamnose
Q156 (= Q153) binding beta-L-rhamnose; mutation to A: Almost loss of activity with L-rhamnose as substrate.
Y159 (= Y156) binding beta-L-rhamnose; binding NADP(+)
K163 (= K160) binding NADP(+)
T191 (≠ L188) binding beta-L-rhamnose; mutation to F: Retains 4% of wild-type activity with L-rhamnose as substrate.
I192 (≠ T189) binding NADP(+)
I196 (≠ F193) mutation to A: Shows a strong decrease in catalytic efficiency with L-rhamnose as substrate, but does not affect catalytic efficiency with L-lyxose and L-mannose.
N197 (vs. gap) binding beta-L-rhamnose
D200 (vs. gap) mutation to A: Retains 16% of wild-type activity with L-rhamnose as substrate.; mutation to H: Retains 22% of wild-type activity with L-rhamnose as substrate.

7do7A Crystal structure of azotobacter vinelandii l-rhamnose 1- dehydrogenase(NAD and l-rhamnose bound-form) (see paper)
39% identity, 98% coverage: 6:249/250 of query aligns to 5:252/256 of 7do7A

query
sites
7do7A

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F

active site: G16 (= G17), S146 (= S143), Y159 (= Y156)
binding nicotinamide-adenine-dinucleotide: G12 (= G13), R15 (= R16), G16 (= G17), I17 (= I18), S37 (vs. gap), D66 (≠ H63), A67 (≠ N64), N93 (= N90), A94 (= A91), G95 (≠ A92), I96 (≠ A93), V144 (≠ T141), S145 (= S142), S146 (= S143), Y159 (= Y156), K163 (= K160), P189 (= P186), G190 (= G187), I192 (≠ T189), T194 (= T191), I196 (≠ F193)
binding beta-L-rhamnopyranose: F99 (= F97), S146 (= S143), S148 (≠ N145), Q156 (= Q153), Y159 (= Y156), N197 (vs. gap), D235 (= D232), M236 (≠ A233), R238 (≠ K235)

7b81A Crystal structure of azotobacter vinelandii l-rhamnose 1-dehydrogenase (NAD bound-form) (see paper)
39% identity, 98% coverage: 6:249/250 of query aligns to 5:252/256 of 7b81A

query
sites
7b81A

N

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K

T

A

A

G

I

A

A

I

V

T

G

C

A

H
x
D

N
x
A

G

A

D

D

K

L

A

D

S

S

R

G

D

E

G

K

L

L

I

V

K

A

Q

A

T

A

I

V

E

E

Q

A

Y

F

G

G

Q

S

L

V

D

D

V

V

M

L

I

V

N

N

N
|
N

A
|
A

A
x
G

A
x
I

N

C

P

P

Y

-

F

F

G

H

N

S

V

F

L

L

D

D

M

M

G

P

F

R

E

E

A

L

I

Y

K

L

K

K

T

T

I

V

E

G

V
x
T

N

N

I

L

E

N

G

G

Y

A

F

Y

H

F

M

T

S

V

Q

Q

L

A

A

A

G

A

Q

R

M

M

R

K

K

E

Q

Q

G

G

-

R

A

G

G

G

V

A

I

I

N

A

T
x
V

S

S

S
|
S

V

I

N

S

G

A

R

L

V

V

A

G

G

G

F

A

N

M

Q

Q

S

T

L

H

Y
|
Y

S

T

A

P

S

T

K
|
K

A

A

A

G

I

L

S

S

M

L

T

M

E

Q

S

S

F

C

A

A

K

I

E

A

C

L

A

G

Q

P

F

Y

G

G

I

I

R

R

V

C

N

N

A

A

V

V

L

L

P
|
P

G
|
G

L

T

T
x
I

D

A

T
|
T

K

D

F
x
I

-

N

-

K

-

E

-

D

A

L

S

S

A

D

L

L

T

E

Q

K

N

R

E

E

A

R

M

M

L

T

K

S

M

-

I

-

L

-

P

-

Q

R

I

V

P

P

L

L

G

G

R

R

I

L

A

G

Q

E

P

P

E

D

I

L

A

A

P

G

A

P

Y

I

L

V

F

F

L

L

A

A

S

S

D

D

A

M

A

A

K

R

Y

Y

I

V

T

T

G

G

V

A

S

S

L

L

P

L

I

V

D

D

G

G

L

L

L

F

active site: G16 (= G17), S146 (= S143), Y159 (= Y156)
binding nicotinamide-adenine-dinucleotide: G12 (= G13), S14 (= S15), R15 (= R16), I17 (= I18), D66 (≠ H63), A67 (≠ N64), N93 (= N90), A94 (= A91), G95 (≠ A92), I96 (≠ A93), T116 (≠ V114), V144 (≠ T141), S146 (= S143), Y159 (= Y156), K163 (= K160), P189 (= P186), G190 (= G187), I192 (≠ T189), T194 (= T191), I196 (≠ F193)

4nbuB Crystal structure of fabg from bacillus sp (see paper)
38% identity, 100% coverage: 1:249/250 of query aligns to 2:243/244 of 4nbuB

query
sites
4nbuB

M

M

T

S

Q

R

F

L

E

Q

N

D

K

K

V

V

V

A

L

I

I

I

T

T

G
|
G

A

A

S

A

R
x
N

G
|
G

I
|
I

G

G

E

L

A

E

I

A

A

A

H

R

Q

V

F

F

A

M

A

K

Q

E

G

G

A

A

Q

K

V

V

I

V

V

I

S

A

S
x
D

R
x
F

S

N

Q

E

E

A

G

-

I

-

D

-

A

A

V

G

A

K

N

E

A

A

I

V

K

E

Q

A

N

N

G

P

G

G

K

V

A

V

G

-

A

F

I

I

T

R

C
x
V

H
x
D

N
x
V

G

S

D

D

K

R

A

E

S

S

R

V

D

H

G

R

L

L

I

V

K

E

Q

N

T

V

I

A

E

E

Q

R

Y

F

G

G

Q

K

L

I

D

D

V

I

M

L

I

I

N

N

N
|
N

A
|
A

A
x
G

A
x
I

N

T

P

R

Y
x
D

F

-

G

S

N

M

V

L

L

S

D
x
K

M

M

G

T

F

V

E

D

A

Q

I

F

K

Q

T

V

I

I

E

N

V

V

N
|
N

I

L

E

T

G

G

Y

V

F

F

H

H

M

C

S

T

Q

Q

L

A

A

V

G

L

Q

P

Q

Y

M

M

R

A

K

E

Q

Q

G

G

A

K

G

G

V

K

I

I

N

N

T
|
T

S

S

S
|
S

V

V

N

T

G

G

R

T

V

Y

A

G

G
x
N

F
x
V

N

G

Q
|
Q

S

T

L

N

Y
|
Y

S

A

A

A

S

A

K
|
K

A

A

A

G

I

V

I

I

S

G

M

M

T

T

E

K

S

T

F

W

A

A

K

K

E

E

C

L

A

A

Q

R

F

K

G

G

I

I

R

N

V

V

N

N

A

A

V

V

L

A

P
|
P

G

G

L
x
F

T
|
T

D

E

T
|
T

K

A

F
x
M

A

V

S

A

A

E

L

V

T

P

Q

-

N

-

E

E

A

K

M

V

L

I

K

E

M
x
K

I

M

L

K

P

A

Q

Q

I

V

P

P

L

M

G

G

R

R

I

L

A

G

Q

K

P

P

E

E

E

D

I

I

A

A

P

N

A

A

Y

Y

L

L

F

F

L

L

A

A

S

S

D

H

A

E

A

S

K

D

Y

Y

I

V

T

N

G

G

V

H

S

V

L

L

P

H

I

V

D

D

G

G

L

I

L

M

active site: G18 (= G17), N111 (= N115), S139 (= S143), Q149 (= Q153), Y152 (= Y156), K156 (= K160)
binding acetoacetyl-coenzyme a: D93 (≠ Y96), K98 (≠ D102), S139 (= S143), N146 (≠ G150), V147 (≠ F151), Q149 (= Q153), Y152 (= Y156), F184 (≠ L188), M189 (≠ F193), K200 (≠ M206)
binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G13), N17 (≠ R16), G18 (= G17), I19 (= I18), D38 (≠ S37), F39 (≠ R38), V59 (≠ C62), D60 (≠ H63), V61 (≠ N64), N87 (= N90), A88 (= A91), G89 (≠ A92), I90 (≠ A93), T137 (= T141), S139 (= S143), Y152 (= Y156), K156 (= K160), P182 (= P186), F184 (≠ L188), T185 (= T189), T187 (= T191), M189 (≠ F193)

7do6A Crystal structure of azotobacter vinelandii l-rhamnose 1- dehydrogenase(NADP bound-form) (see paper)
39% identity, 98% coverage: 6:249/250 of query aligns to 5:243/247 of 7do6A

query
sites
7do6A

N

D

K

K

V

T

V

V

L

I

I

V

T

T

G
|
G

A

A

S
|
S

R
|
R

G
|
G

I
|
I

G

G

E

R

A

A

I

A

A

A

H

R

Q

E

F

C

A

A

A

R

Q

Q

G

G

A

A

Q

R

V

V

I

V

V

I

-

G

-
x
H

-
x
S

-

G

S

S

S

D

R

E

S
x
G

Q

R

E

A

G

G

I

A

D

L

A

S

V

L

A

A

N

E

A

E

I

I

K

A

Q

A

N

F

G

G

K

T

A

A

G

I

A

A

I

V

T

G

C

A

H
x
D

N
x
A

G

A

D

D

K

L

A

D

S

S

R

G

D

E

G

K

L

L

I

V

K

A

Q

A

T

A

I

V

E

E

Q

A

Y

F

G

G

Q

S

L

V

D

D

V

V

M

L

I

V

N

N

N
|
N

A
|
A

A
x
G

A
x
I

N

C

P

P

Y

-

F

F

G

H

N

S

V

F

L

L

D

D

M

M

G

P

F

R

E

E

A

L

I

Y

K

L

K

K

T

T

I

V

E

G

V
x
T

N

N

I

L

E

N

G

G

Y

A

F

Y

H

F

M

T

S

V

Q

Q

L

A

A

A

G

A

Q

R

M

M

R

K

K

E

Q

Q

G

G

-

R

A

G

G

G

V

A

I

I

N

A

T

V

S

S

S
|
S

V

I

N

S

G

A

R

L

V

V

A

G

G

G

F

A

N

M

Q

Q

S

T

L

H

Y
|
Y

S

T

A

P

S

T

K
|
K

A

A

A

G

I

L

S

S

M

L

T

M

E

Q

S

S

F

C

A

A

K

I

E

A

C

L

A

G

Q

P

F

Y

G

G

I

I

R

R

V

C

N

N

A

A

V

V

L

L

P

P

G

G

L

T

T
x
I

D

-

T

-

K

-

F

-

A

-

S

A

A

D

L

L

T

E

Q

K

N

R

E

E

A

R

M

M

L

T

K

S

M

-

I

-

L

-

P

-

Q

R

I

V

P

P

L

L

G

G

R

R

I

L

A

G

Q

E

P

P

E

D

I

L

A

A

P

G

A

P

Y

I

L

V

F

F

L

L

A

A

S

S

D

D

A

M

A

A

K

R

Y

Y

I

V

T

T

G

G

V

A

S

S

L

L

P

L

I

V

D

D

G

G

L

L

L

F

active site: G16 (= G17), S146 (= S143), Y159 (= Y156)
binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G13), S14 (= S15), R15 (= R16), G16 (= G17), I17 (= I18), H36 (vs. gap), S37 (vs. gap), G42 (≠ S39), D66 (≠ H63), A67 (≠ N64), N93 (= N90), A94 (= A91), G95 (≠ A92), I96 (≠ A93), T116 (≠ V114), S146 (= S143), Y159 (= Y156), K163 (= K160), I192 (≠ T189)

Q9BTZ2 Dehydrogenase/reductase SDR family member 4; NADPH-dependent carbonyl reductase; CR; NADPH-dependent retinol dehydrogenase/reductase; NRDR; humNRDR; Peroxisomal short-chain alcohol dehydrogenase; PSCD; SCAD-SRL; Short chain dehydrogenase/reductase family 25C member 2; Protein SDR25C2; Short-chain dehydrogenase/reductase family member 4; EC 1.1.1.184 from Homo sapiens (Human) (see 2 papers)
33% identity, 97% coverage: 6:247/250 of query aligns to 32:273/278 of Q9BTZ2

query
sites
Q9BTZ2

N

N

K

K

V

V

V

A

L

L

I

V

T

T

G

A

A

S

S

T

R

D

G

G

I

I

G

G

E

F

A

A

I

I

A

A

H

R

Q

R

F

L

A

A

A

Q

Q

D

G

G

A

A

Q

H

V

V

I

V

V

V

S

S

R

R

S

K

Q

Q

E

Q

G

N

I

V

D

D

A

Q

V

A

A

V

N

A

A

T

I

L

K

Q

Q

G

N

E

G

G

G

L

K

S

A

V

G

T

A

G

I

T

T

V

C

C

H

H

N

V

G

G

D

K

K

A

A

E

S

D

R

R

D

E

G

R

L

L

I

V

K

A

Q

T

T

A

I

V

E

K

Q

L

Y

H

G

G

Q

G

L

I

D

D

V

I

M

L

I

V

N

S

N

N

A

A

A

V

N

N

P

P

Y

F

F

F

G

G

N

S

V

I

L

M

D

D

M

V

G

T

F

E

E

E

A

V

I

W

K

D

K

K

T

T

I

L

E

D

V

I

N

N

I

V

E

K

G

A

Y

P

F

A

H

L

M

M

S

T

Q

K

L

A

A

V

G

V

Q

P

Q

E

M

M

R

E

K

K

Q

R

G

G

A

G

G

G

V

S

I

V

N

I

T

V

S

S

V

I

N

A

G

A

R

F

V

S

A

P

G
x
S

F

P

N

G

Q
x
F

S

S

L

P

Y

Y

S

N

A

V

S

S

K

K

A

T

A

A

I

L

S

G

M

L

T

T

E

K

S
x
T

F

L

A

A

K

I

E

E

C

L

A

A

Q

P

F

R

G

N

I

I

R

R

V

V

N

N

A

C

V

L

L

A

P

P

G

G

L

L

T

I

D

K

T

T

K

S

F

F

A

S

S

R

A

M

L

L

T

W

Q

M

N

D

E

K

A

E

M

K

L

E

K

E

M

S

I

M

L

K

P

E

Q

T

I

L

P

R

L

I

G

R

R

R

I

L

A

G

Q

E

P

P

E

E

E

D

I

C

A

A

P

G

A

I

Y

V

L

S

F

F

L

L

A

C

S

S

D

E

A

D

A

A

K

S

Y

Y

I

I

T

T

G

G

V

E

S

T

L

V

P

V

I

V

D

G

G

G

S176 (≠ G150) Responsible for the stereoselective reduction of 3-ketosteroids into 3beta-hydroxysteroids and benzil into R-benzoin; mutation to F: Decreased reduction activity for benzil, isatin and retinal and increased activity for 5beta-Pregnane-3,20-dione and 5beta-Dihydrotestosterone. No change of stereoselectivity in 3-ketosteroids reduction and no change in 3beta-hydroxysteroid oxidation. Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with L-179. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with L-179. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with L-179. Loss of cold catalytic inactivation; when associated with L-179 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with L-179 and N-195.
F179 (≠ Q153) Responsible for the stereoselective reduction of 3-ketosteroids into 3beta-hydroxysteroids and benzil into R-benzoin; mutation to L: Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with F-176. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with F-176. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176. Loss of cold catalytic inactivation; when associated with F-176 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and N-195.
T195 (≠ S169) mutation to N: Loss of cold catalytic inactivation. Loss of cold catalytic inactivation; when associated with F-176 and L-179. Switch in stereoselective activity from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176 and L-179. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and L-179.

3o4rA Crystal structure of human dehydrogenase/reductase (sdr family) member 4 (dhrs4)
33% identity, 97% coverage: 6:247/250 of query aligns to 8:249/254 of 3o4rA

query
sites
3o4rA

N

N

K

K

V

V

V

A

L

L

I

V

T

T

G
x
A

A

S

S
x
T

R
x
D

G
|
G

I
|
I

G

G

E

F

A

A

I

I

A

A

H

R

Q

R

F

L

A

A

A

Q

Q

D

G

G

A

A

Q

H

V

V

I

V

V

V

S

S

S
|
S

R
|
R

S
x
K

Q

Q

E

Q

G
x
N

I

V

D

D

A

Q

V

A

A

V

N

A

A

T

I

L

K

Q

Q

G

N

E

G

G

G

L

K

S

A

V

G

T

A

G

I

T

T

V

C

C

H
|
H

N
x
V

G

G

D

K

K

A

A

E

S

D

R

R

D

E

G

R

L

L

I

V

K

A

Q

T

T

A

I

V

E

K

Q

L

Y

H

G

G

Q

G

L

I

D

D

V

I

M

L

I

V

N

S

N
|
N

A

A

A
|
A

A

V

N

N

P

P

Y

F

F

F

G

G

N

S

V

I

L

M

D

D

M

V

G

T

F

E

E

E

A

V

I

W

K

D

K

K

T

T

I

L

E

D

V

I

N

N

I

V

E

K

G

A

Y

P

F

A

H

L

M

M

S

T

Q

K

L

A

A

V

G

V

Q

P

Q

E

M

M

R

E

K

K

Q

R

G

G

A

G

G

G

V

S

I

V

N

I

T

V

S

S

S
|
S

V

I

N

A

G

A

R

F

V

S

A

P

G

S

F

P

N

G

Q
x
F

S

S

L

P

Y
|
Y

S

N

A

V

S

S

K
|
K

A

T

A

A

I

L

S

G

M

L

T

T

E

K

S

T

F

L

A

A

K

I

E

E

C

L

A

A

Q

P

F

R

G

N

I

I

R

R

V

V

N

N

A

C

V

L

L

A

P
|
P

G
|
G

L
|
L

T
x
I

D

K

T
|
T

K

S

F
|
F

A
x
S

S

R

A

M

L

L

T

W

Q

M

N

D

E
x
K

A

E

M

K

L

E

K

E

M

S

I

M

L

K

P

E

Q

T

I

L

P

R

L

I

G

R

R

R

I

L

A

G

Q

E

P

P

E

E

E

D

I

C

A

A

P

G

A

I

Y

V

L

S

F

F

L

L

A

C

S

S

D

E

A

D

A

A

K

S

Y

Y

I

I

T

T

G

G

V

E

S

T

L

V

P

V

I

V

D

G

G

G

active site: G19 (= G17), S145 (= S143), F155 (≠ Q153), Y158 (= Y156), K162 (= K160), K203 (≠ E201)
binding nadp nicotinamide-adenine-dinucleotide phosphate: A15 (≠ G13), T17 (≠ S15), D18 (≠ R16), G19 (= G17), I20 (= I18), S39 (= S37), R40 (= R38), K41 (≠ S39), N44 (≠ G42), H65 (= H63), V66 (≠ N64), N92 (= N90), A94 (= A92), S145 (= S143), Y158 (= Y156), K162 (= K160), P188 (= P186), G189 (= G187), L190 (= L188), I191 (≠ T189), T193 (= T191), F195 (= F193), S196 (≠ A194)

3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
41% identity, 97% coverage: 7:248/250 of query aligns to 5:244/246 of 3osuA

query
sites
3osuA

K

K

V

S

V

A

L

L

I

V

T

T

G

G

A

A

S

S

R

R

G
|
G

I

I

G

G

E

R

A

S

I

I

A

A

H

L

Q

Q

F

L

A

A

A

E

Q

E

G

G

A

Y

Q

N

V

V

I

A

V

V

S

N

-

Y

S

A

R

G

S

S

Q

K

E

E

G

K

I

A

D

E

A

A

V

V

A

V

N

E

A

E

I

I

K

K

Q

A

N

K

G

G

G

V

K

D

A

S

G

F

A

A

I

I

T

Q

C

A

H

N

N

V

G

A

D

D

K

A

A

D

S

E

R

V

D

K

G

A

L

M

I

I

K

K

Q

E

T

V

I

V

E

S

Q

Q

Y

F

G

G

Q

S

L

L

D

D

V

V

M

L

I

V

N

N

N
|
N

A

A

A

G

A

I

N

T

P

R

Y

-

F

-

G

D

N

N

V

L

L

L

-

M

D

R

M

M

G

K

F

E

E

Q

A

E

I

W

K

D

T

V

I

I

E

D

V

T

N

N

I

L

E

K

G

G

Y

V

F

F

H

N

M

C

S

I

Q

Q

L

K

A

A

G

T

Q

P

Q

Q

M

M

R

L

K

R

Q

Q

G

R

A

S

G

G

V

A

I

I

N

N

T

L

S

S

S
|
S

V

V

N

V

G

G

R

A

V

V

A

G

G

N

F

P

N

G

Q
|
Q

S

A

L

N

Y
|
Y

S

V

A

A

S

T

K
|
K

A

A

A

G

I

V

I

I

S

G

M

L

T

T

E

K

S

S

F

A

A

A

K

R

E

E

C

L

A

A

Q

S

F

R

G

G

I

I

R

T

V

V

N

N

A

A

V

V

L

A

P

P

G

G

L

F

T

I

D

V

T

S

K

D

F

M

A

T

S

D

A

A

L

L

T

S

Q

-

N

-

E

D

A

E

M

L

L

K

K

E

M

Q

I

M

L

L

P

T

Q

Q

I

I

P

P

L

L

G

A

R

R

I

F

A

G

Q

Q

P

D

E

T

E

D

I

I

A

A

P

N

A

T

Y

V

L

A

F

F

L

L

A

A

S

S

D

D

A

K

A

A

K

K

Y

Y

I

I

T

T

G

G

V

Q

S

T

L

I

P

H

I

V

D

N

G

G

L

M

active site: G15 (= G17), S141 (= S143), Q151 (= Q153), Y154 (= Y156), K158 (= K160)
binding magnesium ion: N89 (= N90), K158 (= K160)

6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
35% identity, 99% coverage: 3:250/250 of query aligns to 2:243/251 of 6vspA

query
sites
6vspA

Q

R

F

F

E

D

N

N

K

K

V

V

L

V

I

I

T

T

G
|
G

A

A

S

G

R
x
N

G
|
G

I
x
M

G

G

E

E

A

A

I

A

A

A

H

R

Q

R

F

F

A

S

A

A

Q

E

G

G

A

A

Q

I

V

V

I

V

V

L

S

A

S
x
D

R
x
W

S
x
A

Q

K

E

E

G

A

I

V

D

D

A

K

V

V

A

A

N

A

A

S

I

L

K

P

Q

K

N

-

G

-

G

G

K

R

A

A

G

M

A

A

I

V

T

H

C
x
I

H
x
D

N
x
V

G

S

D

D

K

H

A

V

S

A

R

V

D

E

G

K

L

M

I

M

K

N

Q

E

T

V

I

A

E

E

Q

K

Y

L

G

G

Q

R

L

I

D

D

V

V

M

L

I

L

N

N

N
|
N

A
|
A

A
x
G

A
x
V

N

H

P

-

Y

V

F

A

G

G

N

S

V

V

L

L

D

E

M

T

G

S

F

I

E

D

A

D

I

W

K

R

T

I

I

A

E

G

V
|
V

N

D

I

I

E

D

G

G

Y

V

F

V

H

F

M

C

S

S

Q

K

L

F

A

A

G

L

Q

P

Q

H

M

L

R

L

K

K

Q

T

G

-

A

K

G

G

V

C

I

I

I

V

N

N

T
|
T

S

A

S
|
S

V

V

N

S

G

G

R

L

V

G

A

G

G

D

F

W

N

G

Q

A

S

A

L

Y

Y
|
Y

S

C

A

A

S

A

K
|
K

A

G

A

A

I

V

S

N

M

L

T

T

E

R

S

A

F

M

A

A

K

L

E

D

C

H

A

G

Q

G

F

D

G

G

I

V

R

R

V

I

N

N

A

S

V

V

L

C

P
|
P

G
x
S

L
|
L

T
x
V

D

K

T
|
T

K
x
N

F
x
M

A
x
T

S

N

A

G

L

W

T

P

Q

Q

N

E

E

-

A

-

M

I

L

R

K

D

M

K

I

F

L

N

P

E

Q

R

I

I

P

A

L

L

G

G

R

R

I

A

A

A

Q

E

P

P

E

E

I

V

A

A

P

A

A

V

Y

M

L

A

F

F

L

L

A

A

S

S

D

D

A

D

A

A

K

S

Y

F

I

I

T

N

G

G

V

A

S

N

L

I

P

P

I

V

D

D

G

G

L

A

L

T

A

A

active site: G16 (= G17), S138 (= S143), Y151 (= Y156)
binding nicotinamide-adenine-dinucleotide: G12 (= G13), N15 (≠ R16), G16 (= G17), M17 (≠ I18), D36 (≠ S37), W37 (≠ R38), W37 (≠ R38), A38 (≠ S39), I59 (≠ C62), D60 (≠ H63), V61 (≠ N64), N87 (= N90), A88 (= A91), G89 (≠ A92), V90 (≠ A93), V110 (= V114), T136 (= T141), S138 (= S143), Y151 (= Y156), K155 (= K160), P181 (= P186), S182 (≠ G187), L183 (= L188), V184 (≠ T189), T186 (= T191), N187 (≠ K192), M188 (≠ F193), T189 (≠ A194)

6xewA Structure of serratia marcescens 2,3-butanediol dehydrogenase (see paper)
35% identity, 99% coverage: 3:250/250 of query aligns to 2:243/251 of 6xewA

query
sites
6xewA

Q

R

F

F

E

D

N

N

K

K

V

V

L

V

I

I

T

T

G
|
G

A

A

S

G

R
x
N

G
|
G

I
x
M

G

G

E

E

A

A

I

A

A

A

H

R

Q

R

F

F

A

S

A

A

Q

E

G

G

A

A

Q

I

V

V

I

V

V

L

S

A

S
x
D

R
x
W

S
x
A

Q

K

E

E

G

A

I

V

D

D

A

K

V

V

A

A

N

A

A

S

I

L

K

P

Q

K

N

-

G

-

G

G

K

R

A

A

G

M

A

A

I

V

T

H

C
x
I

H
x
D

N
x
V

G

S

D

D

K

H

A

V

S

A

R

V

D

E

G

K

L

M

I

M

K

N

Q

E

T

V

I

A

E

E

Q

K

Y

L

G

G

Q

R

L

I

D

D

V

V

M

L

I

L

N

N

N
|
N

A
|
A

A
x
G

A

V

N

H

P

-

Y

V

F

A

G

G

N

S

V

V

L

L

D

E

M

T

G

S

F

I

E

D

A

D

I

W

K

R

T

I

I

A

E

G

V
|
V

N

D

I

I

E

D

G

G

Y

V

F

V

H

F

M

C

S

S

Q

K

L

F

A

A

G

L

Q

P

Q

H

M

L

R

L

K

K

Q

T

G

-

A

K

G

G

V

C

I

I

I

V

N

N

T
|
T

S

A

S
|
S

V

V

N
x
S

G

G

R

L

V

G

A

G

G

D

F

W

N

G

Q

A

S

A

L

Y

Y
|
Y

S

C

A

A

S

A

K
|
K

A

G

A

A

I

V

S

N

M

L

T

T

E

R

S

A

F

M

A

A

K

L

E

D

C

H

A

G

Q

G

F

D

G

G

I

V

R

R

V

I

N

N

A

S

V

V

L

C

P

P

G
x
S

L
|
L

T
x
V

D

K

T
|
T

K
x
N

F
x
M

A
x
T

S

N

A

G

L

W

T

P

Q

Q

N

E

E

-

A

-

M

I

L

R

K

D

M

K

I

F

L

N

P

E

Q

R

I

I

P

A

L

L

G

G

R

R

I

A

A

A

Q

E

P

P

E

E

I

V

A

A

P

A

A

V

Y

M

L

A

F

F

L

L

A

A

S

S

D

D

A

D

A

A

K

S

Y

F

I

I

T

N

G

G

V

A

S

N

L

I

P

P

I

V

D

D

G

G

L

A

L

T

A

A

active site: G16 (= G17), S138 (= S143), Y151 (= Y156)
binding r,3-hydroxybutan-2-one: S138 (= S143), S140 (≠ N145), Y151 (= Y156)
binding s,3-hydroxybutan-2-one: S138 (= S143), Y151 (= Y156), S182 (≠ G187)
binding nicotinamide-adenine-dinucleotide: G12 (= G13), N15 (≠ R16), G16 (= G17), M17 (≠ I18), D36 (≠ S37), W37 (≠ R38), W37 (≠ R38), A38 (≠ S39), I59 (≠ C62), D60 (≠ H63), V61 (≠ N64), N87 (= N90), A88 (= A91), G89 (≠ A92), V110 (= V114), T136 (= T141), S138 (= S143), Y151 (= Y156), K155 (= K160), S182 (≠ G187), L183 (= L188), V184 (≠ T189), T186 (= T191), N187 (≠ K192), M188 (≠ F193), T189 (≠ A194)

6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
35% identity, 99% coverage: 3:250/250 of query aligns to 4:245/252 of 6vspB

query
sites
6vspB

Q

R

F

F

E

D

N

N

K

K

V

V

L

V

I

I

T

T

G
|
G

A

A

S

G

R
x
N

G
|
G

I

M

G

G

E

E

A

A

I

A

A

A

H

R

Q

R

F

F

A

S

A

A

Q

E

G

G

A

A

Q

I

V

V

I

V

V

L

S

A

S
x
D

R
x
W

S

A

Q

K

E

E

G

A

I

V

D

D

A

K

V

V

A

A

N

A

A

S

I

L

K

P

Q

K

N

-

G

-

G

G

K

R

A

A

G

M

A

A

I

V

T

H

C
x
I

H
x
D

N
x
V

G

S

D

D

K

H

A

V

S

A

R

V

D

E

G

K

L

M

I

M

K

N

Q

E

T

V

I

A

E

E

Q

K

Y

L

G

G

Q

R

L

I

D

D

V

V

M

L

I

L

N

N

A

A

A
x
G

A

V

N

H

P

-

Y

V

F

A

G

G

N

S

V

V

L

L

D

E

M

T

G

S

F

I

E

D

A

D

I

W

K

R

T

I

I

A

E

G

V

V

N

D

I

I

E

D

G

G

Y

V

F

V

H

F

M

C

S

S

Q

K

L

F

A

A

G

L

Q

P

Q

H

M

L

R

L

K

K

Q

T

G

-

A

K

G

G

V

C

I

I

I

V

N

N

T

T

S

A

S
|
S

V

V

N

S

G

G

R

L

V

G

A

G

G

D

F

W

N

G

Q

A

S

A

L

Y

Y
|
Y

S

C

A

A

S

A

K

K

A

G

A

A

I

V

S

N

M

L

T

T

E

R

S

A

F

M

A

A

K

L

E

D

C

H

A

G

Q

G

F

D

G

G

I

V

R

R

V

I

N

N

A

S

V

V

L

C

P

P

G

S

L

L

T

V

D

K

T

T

K

N

F

M

A

T

S

N

A

G

L

W

T

P

Q

Q

N

E

E

-

A

-

M

I

L

R

K

D

M

K

I

F

L

N

P

E

Q

R

I

I

P

A

L

L

G

G

R

R

I

A

A

A

Q

E

P

P

E

E

I

V

A

A

P

A

A

V

Y

M

L

A

F

F

L

L

A

A

S

S

D

D

A

D

A

A

K

S

Y

F

I

I

T

N

G

G

V

A

S

N

L

I

P

P

I

V

D

D

G

G

L

A

L

T

A

A

active site: G18 (= G17), S140 (= S143), Y153 (= Y156)
binding adenosine-5'-diphosphate: G14 (= G13), N17 (≠ R16), D38 (≠ S37), W39 (≠ R38), I61 (≠ C62), D62 (≠ H63), V63 (≠ N64), G91 (≠ A92)

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)
35% identity, 99% coverage: 3:250/250 of query aligns to 2:243/251 of H9XP47

query
sites
H9XP47

Q

R

F

F

E

D

N

N

K

K

V

V

L

V

I

I

T

T

G

G

A

A

S

G

R
x
N

G

G

I
x
M

G

G

E

E

A

A

I

A

A

A

H

R

Q

R

F

F

A

S

A

A

Q

E

G

G

A

A

Q

I

V

V

I

V

V

L

S

A

S
x
D

R

W

S

A

Q

K

E

E

G

A

I

V

D

D

A

K

V

V

A

A

N

A

A

S

I

L

K

P

Q

K

N

-

G

-

G

G

K

R

A

A

G

M

A

A

I

V

T

H

C

I

H
x
D

N
x
V

G

S

D

D

K

H

A

V

S

A

R

V

D

E

G

K

L

M

I

M

K

N

Q

E

T

V

I

A

E

E

Q

K

Y

L

G

G

Q

R

L

I

D

D

V

V

M

L

I

L

N

N

N
|
N

A

A

A

G

A

V

N

H

P

-

Y

V

F

A

G

G

N

S

V

V

L

L

D

E

M

T

G

S

F

I

E

D

A

D

I

W

K

R

T

I

I

A

E

G

V

V

N

D

I

I

E

D

G

G

Y

V

F

V

H

F

M

C

S

S

Q

K

L

F

A

A

G

L

Q

P

Q

H

M

L

R

L

K

K

Q

T

G

-

A

K

G

G

V

C

I

I

I

V

N

N

T

T

S

A

S
|
S

V
|
V

N
x
S

G

G

R

L

V

G

A

G

G

D

F

W

N

G

Q

A

S

A

L

Y

Y
|
Y

S

C

A

A

S

A

K
|
K

A

G

A

A

I

V

S

N

M

L

T

T

E

R

S

A

F

M

A

A

K

L

E

D

C

H

A

G

Q

G

F

D

G

G

I

V

R

R

V

I

N

N

A

S

V

V

L

C

P

P

G

S

L

L

T
x
V

D

K

T
|
T

K

N

F

M

A

T

S

N

A

G

L

W

T

P

Q

Q

N

E

E

-

A

-

M

I

L
x
R

K
x
D

M
x
K

I

F

L

N

P

E

Q

R

I

I

P

A

L

L

G

G

R

R

I

A

A

A

Q

E

P

P

E

E

I

V

A

A

P

A

A

V

Y

M

L

A

F

F

L

L

A

A

S

S

D

D

A

D

A

A

K

S

Y

F

I

I

T

N

G

G

V

A

S

N

L

I

P

P

I

V

D

D

G

G

L

A

L

T

A

A

N15 (≠ R16) binding NAD(+)
M17 (≠ I18) binding NAD(+)
D36 (≠ S37) binding NAD(+)
D60 (≠ H63) binding NAD(+)
V61 (≠ N64) binding NAD(+)
N87 (= N90) binding NAD(+)
S138 (= S143) binding (R)-acetoin; binding (S)-acetoin
V139 (= V144) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
S140 (≠ N145) binding (R)-acetoin
Y151 (= Y156) binding (R)-acetoin; binding (S)-acetoin; binding NAD(+)
K155 (= K160) binding NAD(+)
V184 (≠ T189) binding NAD(+)
T186 (= T191) binding NAD(+)
RDK 197:199 (≠ LKM 204:206) 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.

P0AEK2 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 3-ketoacyl-acyl carrier protein reductase; Beta-Ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; EC 1.1.1.100 from Escherichia coli (strain K12) (see 2 papers)
38% identity, 98% coverage: 3:248/250 of query aligns to 2:241/244 of P0AEK2

query
sites
P0AEK2

Q

N

F

F

E

E

N

G

K

K

V

I

V

A

L

L

I

V

T

T

G
|
G

A
|
A

S
|
S

R
|
R

G

G

I

I

G

G

E

R

A

A

I

I

A

A

H

E

Q

T

F

L

A

A

Q

R

G

G

A

A

Q

K

V

V

I

I

V

G

S

T

S

A

R
x
T

S

S

Q

E

E

N

G

G

I

A

D

Q

A

A

V

I

A

S

N

D

A

Y

I

L

K

G

Q

A

N

N

G

G

G

K

K

-

A

-

G

-

A

G

I

L

T

M

C

L

H
x
N

N
x
V

G

T

D

D

K

P

A

A

S

S

R

I

D

E

G

S

L

V

I

L

K

E

Q

K

T

I

I

R

E

A

Q

E

Y

F

G

G

Q

E

L

V

D

D

V

I

M

L

I

V

N

N

N
|
N

A

A

A

G

A

I

N

T

P

R

Y

-

F

-

G

D

N

N

V

L

L

L

-

M

D

R

M

M

G

K

F

D

E

E

A

E

I

W

K

N

K

D

T

I

I

I

E

E

V

T

N

N

I

L

E

S

G

S

Y

V

F

F

H

R

M

L

S

S

Q

K

L

A

A

V

G

M

Q

R

Q

A

M

M

R

M

K

K

Q

K

G

R

A

H

G

G

V

R

I

I

N

T

T

I

S

G

S

S

V

V

N

V

G

G

R

T

V

M

A

G

G

N

F

G

N

G

Q

Q

S

A

L

N

Y
|
Y

S
x
A

A
|
A

S
x
A

K
|
K

A

A

A

G

I

L

I

I

S

G

M

F

T

S

E

K

S

S

F

L

A

A

K

R

E

E

C

V

A

A

Q

S

F

R

G

G

I

I

R

T

V

V

N

N

A

V

V

V

L

A

P

P

G

G

L

F

T
x
I

D

E

T

T

K

D

F

M

A

T

S

R

A

A

L

L

T

S

Q

D

N

D

E

Q

A

R

M

-

L

-

K

A

M

G

I

I

L

L

P

A

Q

Q

I

V

P

P

L

A

G

G

R

R

I

L

A

G

Q

G

P

A

E

Q

E

E

I

I

A

A

P

N

A

A

Y

V

L

A

F

F

L

L

A

A

S

S

D

D

A

E

A

A

K

A

Y

Y

I

I

T

T

G

G

V
x
E

S

T

L

L

P

H

I

V

D

N

G

G

L

M

GASR 12:15 (= GASR 13:16) binding NADP(+)
T37 (≠ R38) binding NADP(+)
NV 59:60 (≠ HN 63:64) binding NADP(+)
N86 (= N90) binding NADP(+)
Y151 (= Y156) mutation to F: Defect in the affinity for NADPH.
YAAAK 151:155 (≠ YSASK 156:160) binding NADP(+)
A154 (≠ S159) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
K155 (= K160) mutation to A: Defect in the affinity for NADPH.
I184 (≠ T189) binding NADP(+)
E233 (≠ V240) mutation to K: Decreases in the thermolability of the reductase; when associated with T-154.

1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
38% identity, 98% coverage: 3:248/250 of query aligns to 1:240/243 of 1q7bA

query
sites
1q7bA

Q

N

F

F

E

E

N

G

K

K

V

I

V

A

L

L

I

V

T

T

G
|
G

A

A

S
|
S

R
|
R