SitesBLAST

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)
36% identity, 99% coverage: 4:255/255 of query aligns to 25:276/278 of Q9BTZ2

query
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Q9BTZ2

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S176 (≠ G155) 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 (≠ Q158) 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 (≠ V174) 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.

2zatA Crystal structure of a mammalian reductase (see paper)
37% identity, 97% coverage: 9:255/255 of query aligns to 3:249/251 of 2zatA

query
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2zatA

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active site: G16 (= G22), S142 (= S148), L152 (≠ Q158), Y155 (= Y161), K159 (= K165), K200 (≠ E206)
binding nadp nicotinamide-adenine-dinucleotide phosphate: A12 (≠ G18), T14 (≠ S20), D15 (≠ R21), G16 (= G22), I17 (= I23), S36 (= S42), R37 (= R43), K38 (= K44), N41 (≠ G47), H62 (= H68), N89 (= N95), A91 (= A97), V140 (= V146), S142 (= S148), Y155 (= Y161), K159 (= K165), P185 (= P191), G186 (= G192), I188 (≠ T194), T190 (= T196), F192 (= F198), S193 (≠ A199)

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)
37% identity, 97% coverage: 9:255/255 of query aligns to 31:277/279 of Q8WNV7

query
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Q8WNV7

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S

37:61 (vs. 15:39, 56% identical) binding NADP(+)
F177 (≠ G155) 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 (≠ Q158) 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 (= Y161) active site, Proton acceptor
K187 (= K165) binding NADP(+)
N196 (≠ V174) 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

7do7A Crystal structure of azotobacter vinelandii l-rhamnose 1- dehydrogenase(NAD and l-rhamnose bound-form) (see paper)
37% identity, 95% coverage: 12:254/255 of query aligns to 6:252/256 of 7do7A

query
sites
7do7A

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active site: G16 (= G22), S146 (= S148), Y159 (= Y161)
binding nicotinamide-adenine-dinucleotide: G12 (= G18), R15 (= R21), G16 (= G22), I17 (= I23), S37 (vs. gap), D66 (≠ H68), A67 (≠ I69), N93 (= N95), A94 (= A96), G95 (≠ A97), I96 (≠ T98), V144 (= V146), S145 (≠ A147), S146 (= S148), Y159 (= Y161), K163 (= K165), P189 (= P191), G190 (= G192), I192 (≠ T194), T194 (= T196), I196 (≠ F198)
binding beta-L-rhamnopyranose: F99 (= F102), S146 (= S148), S148 (≠ N150), Q156 (= Q158), Y159 (= Y161), N197 (≠ A199), D235 (= D237), M236 (≠ A238), R238 (≠ S240)

7b81A Crystal structure of azotobacter vinelandii l-rhamnose 1-dehydrogenase (NAD bound-form) (see paper)
37% identity, 95% coverage: 12:254/255 of query aligns to 6:252/256 of 7b81A

query
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7b81A

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K

G

L

R

E

A

G

G

C

A

Q

L

H

S

V

L

A

A

D

E

A

E

I

I

I

A

A

A

A

F

G

G

K

T

A

A

T

I

A

A

I

V

A

G

C

A

H
x
D

I
x
A

G

A

E

D

M

L

E

D

Q

S

I

G

S

E

Q

K

V

L

F

V

A

A

G

A

I

A

K

V

E

E

Q

A

F

F

G

G

R

S

L

V

D

D

I

V

L

L

V

V

N

N

N
|
N

A
|
A

A
x
G

T
x
I

N

C

P

P

Q

-

F

F

C

H

N

S

V

F

L

L

D

D

T

M

D

P

L

R

S

E

A

L

F

Y

Q

L

K

K

T

T

V

V

D

G

V
x
T

N

N

I

L

R

N

G

G

Y

A

F

Y

F

F

M

T

S

V

V

Q

E

A

A

A

G

A

K

R

L

R

M

M

R

K

E

E

N

Q

G

G

-

R

G

G

S

A

I

I

N

A

V
|
V

A

S

S
|
S

I

I

N

S

G

A

V

L

S

V

P

G

G

G

I

A

F

M

Q

Q

G

T

I

H

Y
|
Y

S

T

V

P

T

T

K
|
K

A

A

A

G

V

L

I

L

N

S

M

L

T

M

K

Q

V

S

F

C

A

A

K

I

E

A

C

L

A

G

Q

P

F

Y

G

G

I

I

R

R

C

C

N

N

A

A

L

V

L

L

P
|
P

G
|
G

L

T

T
x
I

D

A

T
|
T

K

D

F
x
I

A

N

S

K

A

E

L

D

V

L

K

S

N

D

E

L

A

E

I

K

L

R

N

E

T

R

A

M

L

T

Q

S

Q

R

I

V

P

P

L

L

K

G

R

R

V

L

A

G

D

E

P

P

S

D

E

D

M

L

A

A

G

G

A

P

V

I

L

V

Y

F

L

L

A

A

S

S

D

D

A

M

S

A

S

R

Y

Y

T

V

T

T

G

G

V

A

S

S

L

L

N

L

V

V

D

D

G

G

F

L

L

F

active site: G16 (= G22), S146 (= S148), Y159 (= Y161)
binding nicotinamide-adenine-dinucleotide: G12 (= G18), S14 (= S20), R15 (= R21), I17 (= I23), D66 (≠ H68), A67 (≠ I69), N93 (= N95), A94 (= A96), G95 (≠ A97), I96 (≠ T98), T116 (≠ V119), V144 (= V146), S146 (= S148), Y159 (= Y161), K163 (= K165), P189 (= P191), G190 (= G192), I192 (≠ T194), T194 (= T196), I196 (≠ F198)

7do6A Crystal structure of azotobacter vinelandii l-rhamnose 1- dehydrogenase(NADP bound-form) (see paper)
38% identity, 95% coverage: 12:254/255 of query aligns to 6:243/247 of 7do6A

query
sites
7do6A

K

K

I

T

A

V

F

I

V

V

S

T

G
|
G

A

A

S
|
S

R
|
R

G
|
G

I
|
I

G

G

E

R

A

A

I

A

A

A

K

R

L

E

L

C

A

A

Q

R

Q

Q

G

G

A

A

H

R

V

V

I

V

V

I

-

G

-
x
H

-
x
S

-

G

S

S

S

D

R

E

K
x
G

L

R

E

A

G

G

C

A

Q

L

H

S

V

L

A

A

D

E

A

E

I

I

I

A

A

A

A

F

G

G

K

T

A

A

T

I

A

A

I

V

A

G

C

A

H
x
D

I
x
A

G

A

E

D

M

L

E

D

Q

S

I

G

S

E

Q

K

V

L

F

V

A

A

G

A

I

A

K

V

E

E

Q

A

F

F

G

G

R

S

L

V

D

D

I

V

L

L

V

V

N

N

N
|
N

A
|
A

A
x
G

T
x
I

N

C

P

P

Q

-

F

F

C

H

N

S

V

F

L

L

D

D

T

M

D

P

L

R

S

E

A

L

F

Y

Q

L

K

K

T

T

V

V

D

G

V
x
T

N

N

I

L

R

N

G

G

Y

A

F

Y

F

F

M

T

S

V

V

Q

E

A

A

A

G

A

K

R

L

R

M

M

R

K

E

E

N

Q

G

G

-

R

G

G

S

A

I

I

N

A

V

V

A

S

S
|
S

I

I

N

S

G

A

V

L

S

V

P

G

G

G

I

A

F

M

Q

Q

G

T

I

H

Y
|
Y

S

T

V

P

T

T

K
|
K

A

A

A

G

V

L

I

L

N

S

M

L

T

M

K

Q

V

S

F

C

A

A

K

I

E

A

C

L

A

G

Q

P

F

Y

G

G

I

I

R

R

C

C

N

N

A

A

L

V

L

L

P

P

G

G

L

T

T
x
I

D

-

T

-

K

-

F

-

A

-

S

A

A

D

L

L

V

E

K

K

N

R

E

E

A

R

I

M

L

T

N

S

T

-

A

-

L

-

Q

-

Q

R

I

V

P

P

L

L

K

G

R

R

V

L

A

G

D

E

P

P

S

D

E

D

M

L

A

A

G

G

A

P

V

I

L

V

Y

F

L

L

A

A

S

S

D

D

A

M

S

A

S

R

Y

Y

T

V

T

T

G

G

V

A

S

S

L

L

N

L

V

V

D

D

G

G

F

L

L

F

active site: G16 (= G22), S146 (= S148), Y159 (= Y161)
binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G18), S14 (= S20), R15 (= R21), G16 (= G22), I17 (= I23), H36 (vs. gap), S37 (vs. gap), G42 (≠ K44), D66 (≠ H68), A67 (≠ I69), N93 (= N95), A94 (= A96), G95 (≠ A97), I96 (≠ T98), T116 (≠ V119), S146 (= S148), Y159 (= Y161), K163 (= K165), I192 (≠ T194)

3op4A Crystal structure of putative 3-ketoacyl-(acyl-carrier-protein) reductase from vibrio cholerae o1 biovar eltor str. N16961 in complex with NADP+ (see paper)
35% identity, 98% coverage: 4:253/255 of query aligns to 1:244/247 of 3op4A

query
sites
3op4A

T

S

Q

Q

L

F

F

M

D

N

L

L

D

E

G

G

K

K

I

V

A

A

F

L

V

V

S

T

G
|
G

A

A

S
|
S

R
|
R

G

G

I
|
I

G

G

E

K

A

A

I

I

A

A

K

E

L

L

A

A

Q

E

Q

R

G

G

A

A

H

K

V

V

I

I

V

G

S

T

S

A

R
x
T

K

S

L

E

E

S

G

G

C

A

Q

Q

H

A

V

I

A

S

D

D

A

Y

I

L

I

-

A

-

G

G

G

D

K

N

A

G

T

K

A

G

I

M

A

A

C

L

H
x
N

I
x
V

G

T

E

N

M

P

E

E

Q

S

I

I

S

E

Q

A

V

V

F

L

A

K

G

A

I

I

K

T

E

D

Q

E

F

F

G

G

R

G

L

V

D

D

I

I

L

L

V

V

N

N

N
|
N

A
|
A

A

G

-
x
I

-

T

-

R

-

D

-

N

-

L

-

M

-

R

-

M

T

K

N

E

P

E

Q

E

F

W

C

S

N

D

V

I

L

M

D

E

T

T

D

N

L

L

S

T

A

S

F

I

Q

F

K

R

T

L

V

S

D

K

V

A

N

V

I

L

R

R

G

G

Y

-

F

-

M

-

S

-

V

-

E

-

A

-

G

-

K

-

L

-

M

M

R

M

E

K

N

K

G

R

G

Q

G

G

S

R

I

I

N

N

V
|
V

A

G

S
|
S

I

V

N

V

G

G

V

T

S

M

P

G

G

N

I

A

F

G

Q

Q

G

A

I

N

Y
|
Y

S

A

V

A

T

A

K
|
K

A

A

A

G

V

V

I

I

N

G

M

F

T

T

K

K

V

S

F

M

A

A

K

R

E

E

C

V

A

A

Q

S

F

R

G

G

I

V

R

T

C

V

N

N

A

T

L

V

L

A

P
|
P

G
|
G

L

F

T
x
I

D

E

T
|
T

K

D

F
x
M

A

T

S

K

A

A

L

L

V

-

K

-

N

N

E

D

A

E

I

Q

L

R

N

T

T

A

A

T

L

L

Q

A

Q

Q

I

V

P

P

L

A

K

G

R

R

V

L

A

G

D

D

P

P

S

R

E

E

M

I

A

A

G

S

A

A

V

V

L

A

Y

F

L

L

A

A

S

S

D

P

A

E

S

A

Y

Y

T

I

T

T

G

G

V

E

S

T

L

L

N

H

V

V

D

N

G

G

F

M

binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G18), S17 (= S20), R18 (= R21), I20 (= I23), T40 (≠ R43), N62 (≠ H68), V63 (≠ I69), N89 (= N95), A90 (= A96), I92 (vs. gap), V139 (= V146), S141 (= S148), Y154 (= Y161), K158 (= K165), P184 (= P191), G185 (= G192), I187 (≠ T194), T189 (= T196), M191 (≠ F198)

7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
36% identity, 97% coverage: 7:254/255 of query aligns to 4:246/247 of 7tzpG

query
sites
7tzpG

F

M

D

K

L

L

D

A

G

S

K

K

I

T

A

A

F

I

V

V

S

T

G
|
G

A

A

S

A

R
|
R

G
|
G

I
|
I

G

G

E

F

A

G

I

I

A

A

K

Q

L

V

L

L

A

A

Q

R

Q

E

G

G

A

A

H

R

V

V

I

I

V

I

S

A

S
x
D

R
|
R

K

D

L

A

E

H

G

G

C

-

Q

E

H

A

V

A

A

A

D

A

A

S

I

L

I

R

A

E

A

S

G

G

G

A

K

Q

A

A

T

L

A

F

I

I

A

S

C
|
C

H

N

I
|
I

G

A

E

E

M

K

E

T

Q

Q

I

V

S

E

Q

A

V

L

F

F

A

S

G

Q

I

A

K

E

E

E

Q

A

F

F

G

G

R

P

L

V

D

D

I

I

L

L

V

V

N

N

N
|
N

A

A

A
x
G

T
x
I

N

N

-

R

-

D

P

A

Q

M

F

L

C

H

N

K

V

L

L

T

D

E

T

A

D

D

L

-

S

-

A

-

F

W

Q

D

K

T

T

V

V

I

D

D

V
|
V

N

N

I

L

R

K

G

G

Y

T

F

F

F

L

M

C

S

M

V

Q

E

Q

A

A

G

A

K

I

L

R

M

M

R

R

E

E

N

R

G

G

G

A

G

G

S

R

I

I

N

N

V

I

A

A

S

S

I

A

N

S

G

W

V

L

S

G

P

-

G

N

I

V

F

G

Q

Q

G

T

I

N

Y
|
Y

S

S

V

A

T

S

K
|
K

A

A

A

G

V

V

I

V

N

G

M

M

T

T

K

K

V

T

F

A

A

C

K

R

E

E

C

L

A

A

Q

K

F

K

G

G

I

V

R

T

C

V

N

N

A

A

L

I

L

C

P

P

G

G

L

F

T
x
I

D

D

T
|
T

K

D

F

M

A
x
T

S

R

A

G

L

V

V

P

K

E

N

N

E

-

A

-

I

V

L

W

N

Q

T

I

A

M

L

V

Q

S

Q

K

I

I

P

P

L

A

K

G

R

Y

V

A

A

G

D

E

P

A

S

K

E

D

M

V

A

G

G

E

A

C

V

V

L

A

Y

F

L

L

A

A

S

S

D

D

A

G

S

A

S

R

Y

Y

T

I

T

N

G

G

V

E

S

V

L

I

N

N

V

V

D

G

G

G

F

M

L

V

binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G18), R18 (= R21), G19 (= G22), I20 (= I23), D39 (≠ S42), R40 (= R43), C63 (= C67), I65 (= I69), N91 (= N95), G93 (≠ A97), I94 (≠ T98), V114 (= V119), Y155 (= Y161), K159 (= K165), I188 (≠ T194), T190 (= T196), T193 (≠ A199)

4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
35% identity, 98% coverage: 4:253/255 of query aligns to 1:240/243 of 4i08A

query
sites
4i08A

T

S

Q

Q

L

F

F

M

D

N

L

L

D

E

G

G

K

K

I

V

A

A

F

L

V

V

S

T

G
|
G

A

A

S
|
S

R
|
R

G
|
G

I
|
I

G

G

E

K

A

A

I

I

A

A

K

E

L

L

A

A

Q

E

Q

R

G

G

A

A

H

K

V

V

I

I

V

G

S

T

S

A

R
x
T

K

S

L

E

E

S

G

G

C

A

Q

Q

H

A

V

I

A

S

D

D

A

Y

I

L

I

-

A

-

G

G

G

D

K

N

A

G

T

K

A

G

I

M

A

A

C

L

H
x
N

I
x
V

G

T

E

N

M

P

E

E

Q

S

I

I

S

E

Q

A

V

V

F

L

A

K

G

A

I

I

K

T

E

D

Q

E

F

F

G

G

R

G

L

V

D

D

I

I

L

L

V

V

N

N

N
|
N

A
|
A

A

G

-

I

-

T

-

R

-

D

-

N

-

L

-

M

-

R

-

M

T

K

N

E

P

E

Q

E

F

W

C

S

N

D

V

I

L

M

D

E

T

T

D
x
N

L

L

S

T

A

S

F

I

Q

F

K

R

T

L

V

S

D

K

V

A

N

V

I

L

R

R

G

G

Y

-

F

-

M

-

S

-

V

-

E

-

A

-

G

-

K

-

L

-

M

M

R

M

E

K

N

K

G

R

G

Q

G

G

S

R

I

I

N

N

V

V

A
x
G

S
|
S

I

V

N

V

G

G

V

T

S

M

P

G

G

N

I

A

F

G

Q
|
Q

G

A

I

N

Y
|
Y

S

A

V

A

T

A

K
|
K

A

A

A

G

V

V

I

I

N

G

M

F

T

T

K

K

V

S

F

M

A

A

K

R

E

E

C

V

A

A

Q

S

F

R

G

G

I

V

R

T

C

V

N

N

A

T

L

V

L

A

P
|
P

G
|
G

L

F

T

I

D

E

T
|
T

K

D

F

M

A

-

S

-

A

-

L

-

V

-

K

-

N

N

E

D

A

E

I

Q

L

R

N

T

T

A

A

T

L

L

Q

A

Q

Q

I

V

P

P

L

A

K

G

R

R

V

L

A

G

D

D

P

P

S

R

E

E

M

I

A

A

G

S

A

A

V

V

L

A

Y

F

L

L

A

A

S

S

D

P

A

E

S

A

Y

Y

T

I

T

T

G

G

V

E

S

T

L

L

N

H

V

V

D

N

G

G

F

M

active site: G19 (= G22), N113 (≠ D109), S141 (= S148), Q151 (= Q158), Y154 (= Y161), K158 (= K165)
binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G18), S17 (= S20), R18 (= R21), I20 (= I23), T40 (≠ R43), N62 (≠ H68), V63 (≠ I69), N89 (= N95), A90 (= A96), G140 (≠ A147), S141 (= S148), Y154 (= Y161), K158 (= K165), P184 (= P191), G185 (= G192), T189 (= T196)

7krmC Putative fabg bound to nadh from acinetobacter baumannii
38% identity, 96% coverage: 9:254/255 of query aligns to 3:242/244 of 7krmC

query
sites
7krmC

L

L

D

Q

G

G

K

K

I

V

A

A

F

L

V

I

S

T

G
|
G

A

A

S

A

-
x
S

-

E

R

R

G
|
G

I
|
I

G

G

E

R

A

A

I

T

A

A

K

E

L

I

L

F

A

A

Q

Q

G

G

A

A

H

K

V

V

I

I

V

I

S

V

S
x
D

R
x
L

K

D

L

L

E

A

G

Q

C

S

Q

Q

H

N

V

A

A

A

D

K

A

A

I

L

I

-

A

-

G

G

G

E

K

G

A

H

T

M

A

G

I

L

A

A

C
x
A

H
x
N

I
x
V

G

A

E

N

M

E

E

E

Q

Q

I

V

S

K

Q

A

V

A

F

V

A

E

G

Q

I

A

K

L

E

Q

Q

H

F

Y

G

G

R

K

L

I

D

D

I

I

L

L

V

I

N

N

N
|
N

A

A

A

G

T

I

N

T

P

-

Q

Q

F

P

C

I

N

K

V

T

L

L

D

D

T

I

D

Q

L

R

S

S

A

D

F

Y

Q

D

K

R

T

V

V

L

D

D

V
|
V

N

S

I

L

R

R

G

G

Y

T

F

L

F

I

M

M

S

S

V

Q

E

A

A

V

G

I

K

P

L

S

M

M

R

K

E

A

N

N

G

G

S

S

I

I

I

V

N

C

V

L

A

S

S
|
S

I

V

N

S

G

A

-

Q

V

R

S

G

P

G

G

G

I

I

F

F

Q

G

G

G

I

P

-

H

Y
|
Y

S

S

V

A

T

A

K
|
K

A

A

A

G

V

V

I

L

N

G

M

L

T

A

K

K

V

A

F

M

A

A

K

R

E

E

C

F

A

G

Q

G

F

D

G

Q

I

I

R

R

C

V

N

N

A

S

L

L

L

T

P

P

G

G

L

L

T
x
I

D

Q

T
|
T

K

D

F

M

A

-

S

-

A

-

L

-

V

-

K

-

N

N

E

D

A

D

I

R

L

R

N

H

T

D

A

I

L

L

Q

A

Q

G

I

I

P

P

L

L

K

G

R

R

V

L

A

G

D

K

P

A

S

Q

E

D

M

V

A

A

G

N

A

A

V

A

L

L

Y

F

L

L

A

A

S

S

D

D

A

L

S

S

S

A

Y

Y

T

L

T

T

G

G

V

V

S

T

L

L

N

D

V

V

D

N

G

G

F

M

L

L

active site: G18 (= G22), S140 (= S148), Y155 (= Y161)
binding nicotinamide-adenine-dinucleotide: G12 (= G18), S15 (vs. gap), G18 (= G22), I19 (= I23), D38 (≠ S42), L39 (≠ R43), A60 (≠ C67), N61 (≠ H68), V62 (≠ I69), N88 (= N95), V111 (= V119), S140 (= S148), Y155 (= Y161), K159 (= K165), I188 (≠ T194), T190 (= T196)

G9FRD7 7alpha-hydroxysteroid dehydrogenase; 7alpha-HSDH; NADP-dependent 7alpha-hydroxysteroid dehydrogenase; EC 1.1.1.- from Clostridium sardiniense (Clostridium absonum) (see 2 papers)
38% identity, 96% coverage: 9:253/255 of query aligns to 4:249/262 of G9FRD7

query
sites
G9FRD7

L

L

D

E

G

G

K

K

I

V

A

A

F

I

V

V

S

T

G
x
S

A
x
S

S
x
T

R
|
R

G
|
G

I
|
I

G

G

E

R

A

A

I

S

A

A

K

E

L

A

L

L

A

A

Q

K

Q

E

G

G

A

A

H

L

V

V

I

Y

V

L

S

A

R
|
R

K

S

L

E

E

E

G

L

C

A

Q

N

H

E

V

V

A

I

D

A

A

D

I

I

I

K

A

K

A

Q

G

G

K

V

A

A

T

K

A

F

I

V

A

Y

C

F

H
x
N

I
x
A

G

R

E

E

M

E

E

E

Q

T

I

Y

S

T

Q

S

V

M

F

V

A

E

G

K

I

V

K

A

E

E

Q

A

F

E

G

G

R

R

L

I

D

D

I

I

L

L

V

V

N

N

N
|
N

-

Y

A

G

T

T

N

N

P

V

Q

N

F

L

-

D

C

K

N

N

V

L

L

T

D

A

T

G

D

D

L

T

S

D

A

E

F

F

Q

F

K

R

T

I

V

L

D

K

V

D

N

N

I

V

R

Q

G

S

Y

V

F

Y

F

L

M

P

S

A

V

K

E

A

A

A

G

I

K

P

L

H

M

M

R

E

E

K

N

V

G

G

S

S

I

I

I

V

N

N

V

I

A

S

S
x
T

I

I

N

G

G

S

V

V

S

V

P

P

G

D

I

I

F

S

Q

R

G

I

I

A

Y
|
Y

S

C

V

V

T

S

K
|
K

A

S

A

A

V

I

I

N

N

S

M

L

T

T

K

Q

V

N

F

I

A

A

K

L

E

Q

C

Y

A

A

Q

R

F

K

G

N

I

I

R

R

C

C

N

N

A

A

L

V

L

L

P

P

G

G

L

L

T
x
I

D
x
G

T
|
T

K
x
R

F
x
A

A

A

S

L

A

E

L

N

V

M

K

T

N

D

E

E

A

-

I

F

L

R

N

D

T

S

A

F

L

L

Q

G

Q

H

I

V

P

P

L

L

K

N

R

R

V

V

A

G

D

R

P

P

S

E

E

D

M

I

A

A

G

N

A

A

V

V

L

L

Y

Y

L

Y

A

A

S

S

D

D

A

D

S

S

S

G

Y

Y

T

V

T

T

G

G

V

M

S

I

L

H

N

E

V

V

D

A

G

G

F

F

SSTRGI 13:18 (≠ GASRGI 18:23) binding NADP(+)
R38 (= R43) binding NADP(+); mutation to D: Loss of catalytic activity.
NA 63:64 (≠ HI 68:69) binding NADP(+)
N90 (= N95) binding NADP(+)
T145 (≠ S148) binding taurochenodeoxycholate
Y158 (= Y161) binding NADP(+); binding taurochenodeoxycholate
K162 (= K165) binding NADP(+)
IGTRA 191:195 (≠ TDTKF 194:198) binding NADP(+)

Sites not aligning to the query:

261:262 mutation Missing: 5-fold reduction in catalytic efficiency.

5epoA The three-dimensional structure of clostridium absonum 7alpha- hydroxysteroid dehydrogenase (see paper)
38% identity, 96% coverage: 9:253/255 of query aligns to 3:248/261 of 5epoA

query
sites
5epoA

L

L

D

E

G

G

K

K

I

V

A

A

F

I

V

V

S

T

G
x
S

A

S

S
x
T

R
|
R

G
|
G

I
|
I

G

G

E

R

A

A

I

S

A

A

K

E

L

A

L

L

A

A

Q

K

Q

E

G

G

A

A

H

L

V

V

I

Y

V

L

S

A

R
|
R

K

S

L

E

E

E

G

L

C

A

Q

N

H

E

V

V

A

I

D

A

A

D

I

I

I

K

A

K

A

Q

G

G

K

V

A

A

T

K

A

F

I

V

A

Y

C
x
F

H
x
N

I

A

G

R

E

E

M

E

E

E

Q

T

I

Y

S

T

Q

S

V

M

F

V

A

E

G

K

I

V

K

A

E

E

Q

A

F

E

G

G

R

R

L

I

D

D

I

I

L

L

V

V

N

N

N
|
N

-
x
Y

A
x
G

A

G

T
|
T

N

N

P

V

Q

N

F

L

-

D

C

K

N

N

V

L

L

T

D

A

T

G

D

D

L

T

S

D

A

E

F

F

Q

F

K

R

T

I

V

L

D

K

V

D

N

N

I

V

R

Q

G

S

Y

V

F

Y

F

L

M

P

S

A

V

K

E

A

A

A

G

I

K

P

L

H

M

M

R

E

E

K

N

V

G

G

S

S

I

I

I

V

N

N

V

I

A

S

S
x
T

I

I

N
x
G

G

S

V

V

S

V

P

P

G

D

I
|
I

F

S

Q
x
R

G

I

I

A

Y
|
Y

S

C

V

V

T

S

K
|
K

A

S

A

A

V

I

I

N

N

S

M

L

T

T

K

Q

V

N

F

I

A

A

K

L

E

Q

C

Y

A

A

Q

R

F

K

G

N

I

I

R

R

C

C

N

N

A

A

L

V

L

L

P
|
P

G
|
G

L

L

T
x
I

D

G

T
|
T

K
x
R

F
x
A

A
|
A

S

L

A

E

L
x
N

V
x
M

K

T

N

D

E

E

A

-

I
x
F

L

R

N

D

T

S

A

F

L

L

Q

G

Q

H

I

V

P

P

L

L

K

N

R

R

V

V

A

G

D

R

P

P

S

E

E

D

M

I

A

A

G

N

A

A

V

V

L

L

Y

Y

L

Y

A

A

S

S

D

D

A

D

S

S

S

G

Y

Y

T

V

T

T

G

G

V

M

S

I

L

H

N

E

V

V

D

A

G

G

F

F

active site: G16 (= G22), T144 (≠ S148), I152 (= I156), Y157 (= Y161), K161 (= K165), R193 (≠ K197)
binding nadp nicotinamide-adenine-dinucleotide phosphate: S12 (≠ G18), T14 (≠ S20), R15 (= R21), G16 (= G22), I17 (= I23), R37 (= R43), F61 (≠ C67), N62 (≠ H68), N89 (= N95), Y90 (vs. gap), G91 (≠ A96), Y157 (= Y161), K161 (= K165), P187 (= P191), G188 (= G192), I190 (≠ T194), T192 (= T196), R193 (≠ K197), A194 (≠ F198), A195 (= A199)
binding taurochenodeoxycholic acid: T93 (= T98), T144 (≠ S148), G146 (≠ N150), R154 (≠ Q158), Y157 (= Y161), G188 (= G192), N198 (≠ L202), M199 (≠ V203), F203 (≠ I208)

P73574 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-acyl carrier protein reductase; EC 1.1.1.100 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
38% identity, 96% coverage: 9:254/255 of query aligns to 4:245/247 of P73574

query
sites
P73574

L

L

D

T

G

A

K

Q

I

V

A

A

F

L

V

V

S

T

G

G

A
|
A

S

S

R

R

G

G

I

I

G

G

E

K

A

A

I

T

A

A

K

L

L

A

L

L

A

A

Q

A

Q

T

G

G

A

M

H

K

V

V

I

V

V

V

S

N

-

Y

S

A

R

Q

K

S

L

S

E

T

G

A

C

A

Q

D

H

A

V

V

A

V

D

A

A

E

I

I

A

A

A

N

G

G

K

E

A

A

T

I

A

A

I

V

A

Q

C

A

H

N

I

V

G

A

E

N

M

A

E

D

Q

E

I

V

S

D

Q

Q

V

L

F

I

A

K

G

T

I

T

K

L

E

D

Q

K

F

F

G

S

R

R

L

I

D

D

I

V

L

L

V

V

N

N

A

A

A

G

T

I

N

T

P

R

Q

D

F

T

C

L

N

-

V

L

L

L

D

R

T

M

D

K

L

L

S

E

A

D

F

W

Q

Q

K

A

T

V

V

I

D

D

V

L

N

N

I

L

R

T

G

G

Y

V

F

F

F

L

M

C

S

T

V

K

E

A

A

V

G

S

K

K

L

L

M

M

R

L

E

K

N

Q

G

K

G

S

G

G

S

R

I

I

N

N

V

I

A

T

S

S

I

V

N

A

G

G

V

M

-

M

-

G

S

N

P
|
P

G

G

I

-

F

-

Q

Q

G

A

I

N

Y

Y

S

S

V

A

T

A

K
|
K

A

A

A

G

V

V

I

I

N

G

M

F

T

T

K

K

V

T

F

V

A

A

K

K

E

E

C

L

A

A

Q

S

F

R

G

G

I

V

R

T

C

V

N

N

A

A

L

V

L

A

P

P

G

G

L
x
F

T

I

D

A

T

T

K

D

F

M

A

T

S

E

A

N

L

L

V

-

K
x
N

N

A

E

E

A

P

I

I

L

-

N

-

T

-

A

-

L

L

Q

Q

Q

F

I

I

P

P

L

L

K

A

R

R

V

Y

A

G

D

Q

P

P

S

E

E

E

M

V

A

A

G

G

A

T

V

I

L

R

Y

F

L

L

A

A

S

T

D

D

-

P

A

A

S

A

Y

Y

T

I

T

T

G

G

V

Q

S

T

L

F

N

N

V

V

D

D

G

G

F

M

L

V

A14 (= A19) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
P151 (= P154) mutation to F: 2.7-fold increase in activity on acetoacetyl-CoA.; mutation to V: 5.7-fold increase in activity on acetoacetyl-CoA.
K160 (= K165) mutation to A: Almost no activity on acetoacetyl-CoA.
F188 (≠ L193) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
N198 (≠ K204) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.

6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
35% identity, 96% coverage: 9:253/255 of query aligns to 3:245/248 of 6ixmC

query
sites
6ixmC

L

L

D

D

G

N

K

K

I

V

A

A

F

L

V

V

S

T

G
|
G

A

A

S

G

R
x
S

G
|
G

I
|
I

G

G

E

L

A

A

I

V

A

A

K

H

L

S

L

Y

A

A

Q

K

Q

E

G

G

A

A

H

K

V

V

I

I

V

V

S

S

S
x
D

R
x
I

K

N

L

E

E

D

G

H

C

G

Q

N

H

K

V

A

A

V

D

E

A

D

I

I

I

K

A

A

A

Q

G

G

K

E

A

A

T

S

A

F

I

V

A

K

C
x
A

H
x
D

I
x
T

G

S

E

N

M

P

E

E

Q

E

I

V

S

E

Q

A

V

L

F

V

A

K

G

R

I

T

K

V

E

E

Q

I

F

Y

G

G

R

R

L

L

D

D

I

I

L

A

V

C

N

N

N
|
N

A
|
A

A

G

T

I

N

G

P

G

Q

E

F

Q

C

A

N

L

V

A

L

G

D

D

T

Y

D

G

L

L

S

D

A

S

F

W

Q

R

K

K

T

V

V

L

D

S

V

I

N

N

I

L

R

D

G

G

Y

V

F

F

F

Y

M

G

S

C

V

K

E

Y

A

E

G

L

K

E

L

Q

M

M

R

E

E

K

N

N

G

G

S

V

I

I

I

V

N

N

V
x
M

A

A

S
|
S

I

I

N

H

G

G

V

I

S

V

P

A

G

A

I

P

F

L

Q

S

G

S

I

A

Y
|
Y

S

T

V

S

T

A

K
|
K

A

H

A

A

V

V

I

V

N

G

M

L

T

T

K

K

V

N

F

I

A

G

K

A

E

E

C

Y

A

G

Q

Q

F

K

G

N

I

I

R

R

C

C

N

N

A

A

L

V

L

G

P
|
P

G
x
A

L
x
Y

T
x
I

D

E

T

T

K

P

F
x
L

A

L

S

E

A

S

L

L

V

T

K

K

N

E

E

-

A

-

I

M

L

K

N

E

T

A

A

L

L

I

Q

S

Q

K

I

H

P

P

L

M

K

G

R

R

V

L

A

G

D

K

P

P

S

E

E

E

M

V

A

A

G

E

A

L

V

V

L

L

Y

F

L

L

A

S

S

S

D

E

A

K

S

S

Y

F

T

M

T

T

G

G

V

G

S

Y

L

Y

N

L

V

V

D

D

G

G

F

Y

active site: G16 (= G22), S142 (= S148), Y155 (= Y161), K159 (= K165)
binding nicotinamide-adenine-dinucleotide: G12 (= G18), S15 (≠ R21), G16 (= G22), I17 (= I23), D36 (≠ S42), I37 (≠ R43), A61 (≠ C67), D62 (≠ H68), T63 (≠ I69), N89 (= N95), A90 (= A96), M140 (≠ V146), S142 (= S148), Y155 (= Y161), K159 (= K165), P185 (= P191), A186 (≠ G192), Y187 (≠ L193), I188 (≠ T194), L192 (≠ F198)

4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
36% identity, 96% coverage: 9:254/255 of query aligns to 3:246/247 of 4jroC

query
sites
4jroC

L

L

D

Q

G

G

K

K

I

V

A

A

F

V

V

V

S

T