SitesBLAST

4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
40% identity, 98% coverage: 1:255/260 of query aligns to 1:245/247 of 4jroC

query
sites
4jroC

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active site: G16 (= G16), S142 (= S150), Q152 (= Q160), Y155 (= Y163), K159 (= K167)
binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G12), S14 (= S14), R15 (= R15), G16 (= G16), I17 (= I17), N35 (= N35), Y36 (= Y36), N37 (≠ W37), G38 (= G38), S39 (≠ D39), A62 (≠ G69), N63 (= N70), V64 (= V71), N90 (= N97), A91 (= A98), G92 (= G99), I93 (= I100), I113 (≠ V120), A141 (≠ S149), S142 (= S150), Y155 (= Y163), K159 (= K167), P185 (= P193), G186 (= G194), I188 (= I196), T190 (= T198)

3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
40% identity, 97% coverage: 6:257/260 of query aligns to 5:246/246 of 3osuA

query
sites
3osuA

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active site: G15 (= G16), S141 (= S150), Q151 (= Q160), Y154 (= Y163), K158 (= K167)
binding magnesium ion: N89 (= N97), K158 (= K167)

3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
40% identity, 97% coverage: 6:257/260 of query aligns to 2:239/239 of 3sj7A

query
sites
3sj7A

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active site: G12 (= G16), S138 (= S150), Q148 (= Q160), Y151 (= Y163), K155 (= K167)
binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G12), S10 (= S14), R11 (= R15), G12 (= G16), I13 (= I17), N31 (= N35), Y32 (= Y36), A33 (≠ Y44), G34 (= G45), S35 (≠ R46), A58 (≠ G69), N59 (= N70), V60 (= V71), N86 (= N97), A87 (= A98), G88 (= G99), I89 (= I100), T109 (≠ V120), L136 (≠ T148), S137 (= S149), S138 (= S150), Y151 (= Y163), K155 (= K167), P181 (= P193), G182 (= G194), F183 (≠ T195), I184 (= I196)

3ay6B Crystal structure of bacillus megaterium glucose dehydrogenase 4 a258f mutant in complex with nadh and d-glucose (see paper)
36% identity, 97% coverage: 3:255/260 of query aligns to 11:256/267 of 3ay6B

query
sites
3ay6B

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active site: G24 (= G16), S151 (= S150), Y164 (= Y163), K168 (= K167)
binding beta-D-glucopyranose: E102 (vs. gap), S151 (= S150), V152 (≠ I151), H153 (≠ S152), W158 (≠ G157), Y164 (= Y163), G195 (= G194), A196 (≠ T195), I201 (≠ L200), N202 (= N201), K205 (≠ D204), M256 (≠ L255)
binding 1,4-dihydronicotinamide adenine dinucleotide: G20 (= G12), T23 (≠ R15), G24 (= G16), L25 (≠ I17), Y45 (= Y44), G70 (= G69), D71 (≠ N70), V72 (= V71), N98 (= N97), A99 (= A98), G100 (= G99), V101 (≠ I100), T121 (≠ S116), M149 (≠ T148), S150 (= S149), S151 (= S150), Y164 (= Y163), K168 (= K167), P194 (= P193), G195 (= G194), A196 (≠ T195), M197 (≠ I196), T199 (= T198), P200 (≠ D199), I201 (≠ L200), N202 (= N201)

1g6kA Crystal structure of glucose dehydrogenase mutant e96a complexed with NAD+
33% identity, 97% coverage: 3:255/260 of query aligns to 5:250/261 of 1g6kA

query
sites
1g6kA

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S

V

D

L

W

E

N

S

K

T

V

V

I

A

D

V
x
T

N

N

L

L

N

T

G

G

A

A

F

F

Y

L

V

G

T

S

Q

R

A

E

A

A

A

I

Q

K

Q

Y

M

F

K

V

L

E

Q

N

G

D

T

I

G

K

G

G

A

T

I

V

V

I

A

N

T
x
M

S
|
S

I

V

S

H

A

E

L

K

V

I

G

P

G

W

G

P

M

L

Q

F

T

V

H

H

Y
|
Y

T

A

P

A

T

S

K
|
K

A

G

G

G

V

M

H

K

S

L

L

M

M

T

Q

E

S

T

C

L

A

A

V

L

A

E

L

Y

G

A

P

P

Y

K

G

G

I

I

R

R

C

V

N

N

S

N

V

I

M

G

P
|
P

G
|
G

T
x
A

I
|
I

A

N

T
|
T

D

P

L
x
I

N
|
N

A

A

Q

E

D

K

L

F

A

A

D

D

E

P

A

E

K

Q

K

R

A

A

Y

D

F

V

E

E

K

S

R

M

I

I

P

P

L

M

G

G

R

Y

L

I

G

G

R

E

P

P

E

E

D

E

V

I

A

A

D

A

C

V

V

A

T

A

F

W

L

L

A

A

S

S

D

S

R

E

A

A

R

S

Y

Y

V

V

T

T

G

G

A

I

A

T

L

L

L

F

V

A

D

D

G

G

L

M

active site: G18 (= G16), S145 (= S150), Y158 (= Y163), K162 (= K167)
binding nicotinamide-adenine-dinucleotide: G14 (= G12), T17 (≠ R15), G18 (= G16), L19 (≠ I17), N37 (= N35), R39 (≠ W37), G64 (= G69), D65 (≠ N70), V66 (= V71), N92 (= N97), A93 (= A98), G94 (= G99), T115 (≠ V120), M143 (≠ T148), S144 (= S149), S145 (= S150), Y158 (= Y163), K162 (= K167), P188 (= P193), G189 (= G194), A190 (≠ T195), I191 (= I196), T193 (= T198), I195 (≠ L200), N196 (= N201)

P40288 Glucose 1-dehydrogenase; EC 1.1.1.47 from Priestia megaterium (Bacillus megaterium) (see 2 papers)
33% identity, 97% coverage: 3:255/260 of query aligns to 5:250/261 of P40288

query
sites
P40288

L

L

K

E

D

G

K

K

V

V

I
x
V

V
x
I

T
|
T

G
|
G

G
x
S

S
|
S

R
x
T

G
|
G

I
x
L

G
|
G

R
x
K

A
x
S

I
x
M

A
|
A

V
x
I

A
x
R

C
x
F

A
|
A

A
x
T

E
|
E

G
x
K

A
|
A

D
x
K

V
|
V

A
x
V

I

V

N

N

Y

Y

W

R

G

S

D

K

N

E

D

D

V

-

S

-

Y

-

G

-

R

-

S

-

A

E

V

A

A

N

E

S

V

V

V

L

A

E

E

E

I

I

E

K

A

K

L

V

G

G

R

G

R

E

V

A

I

I

A

A

I

V

E

K

G

G

N

D

V

V

A

T

A

V

R

E

E

S

T

D

G

V

Q

I

Q

N

L

L

V

V

R

Q

H

S

T

A

V

I

E

K

A

E

F

F

G

G

K

K

V

L

D

D

V

V

L

M

A

I

S

N

N

N

A

A

G

G

I

L

C
x
E

P

N

F

P

H

V

A

S

F

S

L

H

D

E

M

M

P

S

P

L

E

S

V
x
D

L

W

E

N

S

K

T
x
V

V

I

A

D

V

T

N

N

L

L

N

T

G

G

A

A

F

F

Y

L

V

G

T

S

Q

R

A

E

A

A

A

I

Q

K

Q

Y

M

F

K

V

L
x
E

Q

N

G

D

T

I

G

K

G

G

A

T

I

V

V

I

A

N

T

M

S

S

I

V

S

H

A

E

L

K

V

I

G

P

G

W

G

P

M

L

Q

F

T

V

H

H

Y

Y

T

A

P

A

T

S

K

K

A

G

G

G

V

M

H

K

S

L

L

M

M

T

Q

E

S

T

C

L

A

A

V

L

A

E

L

Y

G

A

P

P

Y

K

G

G

I

I

R

R

C
x
V

N

N

S

N

V

I

M

G

P

P

G

G

T

A

I

I

A

N

T

T

D
x
P

L

I

N

N

A

A

Q

E

D

K

L

F

A

A

D

D

E

P

A

E

K

Q

K

R

A

A

Y

D

F

V

E
|
E

K

S

R

M

I

I

P

P

L

M

G

G

R
x
Y

L

I

G

G

R

E

P

P

E

E

D

E

V

I

A

A

D

A

C

V

V

A

T

A

F

W

L

L

A

A

S

S

D

S

R

E

A

A

R

S

Y

Y

V

V

T

T

G

G

A

I

A

T

L

L

L

F

V

A

D

D

G

G

L

M

11:35 (vs. 9:33, 40% identical) binding
E96 (≠ C101) mutation E->A,G,K: Heat stable.
D108 (≠ V113) mutation to N: Heat stable.
V112 (≠ T117) mutation to A: Heat stable.
E133 (≠ L138) mutation to K: Heat stable.
V183 (≠ C188) mutation to I: Heat stable.
P194 (≠ D199) mutation to Q: Heat stable.
E210 (= E215) mutation to K: Heat stable.
Y217 (≠ R222) mutation to H: Heat stable.

Sites not aligning to the query:

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

4cqlI Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD (see paper)
41% identity, 98% coverage: 3:257/260 of query aligns to 6:251/251 of 4cqlI

query
sites
4cqlI

L

L

K

R

D

S

K

A

V

L

V

A

I

L

V

V

T

T

G
|
G

G

A

S
x
G

R
x
S

G
|
G

I
|
I

G

G

R

R

A

A

I

V

A

S

V

V

A

R

C

L

A

A

A

G

E

E

G

G

A

A

D

T

V

V

A

A

I

A

N

C

Y

-

W

-

G

-

D
|
D

N
x
L

D

D

V

-

S

-

Y

-

G

-

R

-

R

R

S

A

A

A

V

A

A

Q

E

E

V

T

V

V

A

R

E

L

I

L

E

G

A

G

L

P

G

G

R

S

R

N

V

H

I

A

A

A

I

F

E

Q

G
x
A

N
x
D

V
|
V

A

S

A

E

R

A

E

R

T

A

G

A

Q

R

Q

C

L

L

V

L

R

E

H

Q

T

V

V

Q

E

A

A

C

F

F

G

S

K

R

V

P

-

P

D

S

V

V

L

V

A

V

S

S

N
x
C

A
|
A

G
|
G

I
|
I

C

T

P

Q

F

D

H

E

A

F

F

L

L

L

D

H

M

M

P

S

P

E

E

D

V

D

L

W

E

D

S

K

T

V

V

I

A

A

V
|
V

N

N

L

L

N

K

G

G

A

T

F

F

Y

L

V

V

T

T

Q

Q

A

A

Q

Q

Q

A

M

L

K

V

L

S

Q

N

G

G

T

C

G

R

G

G

A

S

I

I

V

I

A

N

T
x
I

S

S

S
|
S

I

I

S

V

A

G

L

K

V

V

G

G

G

N

G

V

M

G

Q

Q

T

T

H

N

Y
|
Y

T

A

P

A

T

S

K
|
K

A

A

G

G

V

V

H

I

S

G

L

L

M

T

Q

Q

S

T

C

A

A

A

V

R

A

E

L

L

G

G

P

R

Y

H

G

G

I

I

R

R

C

C

N

N

S

S

V

V

M

L

P
|
P

G
|
G

T
x
F

I
|
I

A

A

T
|
T

D
x
P

L
x
M

N
x
T

-

Q

-

K

-

V

A

P

Q

Q

D

K

L

V

A

V

D

D

E

K

A

-

K

-

A

-

Y

-

F

I

E

T

K

E

R

M

I

I

P

P

L

M

G

G

R

H

L

L

G

G

R

D

P

P

E

E

D

D

V

V

A

A

D

D

C

V

V

V

T

A

F

F

L

L

A

A

S

S

D

E

R

D

A

S

R

G

Y

Y

V

I

T

T

G

G

A

T

A

S

L

V

L

E

V

V

D

T

G

G

L

L

F

F

V

M

active site: G19 (= G16), S146 (= S150), Y159 (= Y163), K163 (= K167)
binding nicotinamide-adenine-dinucleotide: G15 (= G12), G17 (≠ S14), S18 (≠ R15), G19 (= G16), I20 (= I17), D39 (= D39), L40 (≠ N40), A64 (≠ G69), D65 (≠ N70), V66 (= V71), C93 (≠ N97), A94 (= A98), G95 (= G99), I96 (= I100), V116 (= V120), I144 (≠ T148), S146 (= S150), Y159 (= Y163), K163 (= K167), P189 (= P193), G190 (= G194), F191 (≠ T195), I192 (= I196), T194 (= T198), P195 (≠ D199), M196 (≠ L200), T197 (≠ N201)

3pk0B Crystal structure of short-chain dehydrogenase/reductase sdr from mycobacterium smegmatis (see paper)
37% identity, 97% coverage: 3:254/260 of query aligns to 8:250/262 of 3pk0B

query
sites
3pk0B

L

L

K

Q

D

G

K

R

V

S

V

V

I

V

V

V

T

T

G

G

S

T

R

K

G
|
G

I

I

G

G

R

R

A

G

I

I

A

A

V

T

A

V

C

F

A

A

A

R

E

A

G

G

A

A

D

N

V

V

A

A

I

V

N

-

Y

-

W

-

G

-

D

-

N

-

D

-

V

-

S

-

Y

A

G

G

R

R

R

S

S

T

A

A

-

D

V

I

A

D

E

A

V

C

V

V

A

A

E

D

I

L

E
x
D

A

Q

L

L

G
|
G

R

S

-
x
G

R

K

V

V

I

I

A

G

I

V

E

Q

G

T

N

D

V

V

A

S

A

D

R

R

E

A

T

Q

G

C

Q

D

Q

A

L

L

V

A

R

G

H

R

T

A

V

V

E

E

A

E

F

F

G

G

K

G

V

I

D

D

V

V

L

V

A

C

S

A

N

N

A

A

G

G

I

V

C

F

P

P

F

D

H

A

A

P

F

L

L

A

D

T

M

M

P

T

P

P

E

E

V

Q

L

L

E

N

S

G

T

I

V

F

A

A

V

V

N

N

L

V

N

N

G

G

A

T

F

F

Y

Y

V

A

T

V

Q

Q

A

A

A

C

A

L

Q

D

Q

A

M

L

K

I

L

A

Q

S

G

G

T

S

G

G

G

R

A

V

I

V

V

L

A

T

T

S

S
|
S

S

I

I

T

S

G

A

P

L

I

V

T

G

G

G

Y

G

P

M

G

Q
x
W

T

S

H

H

Y
|
Y

T

G

P

A

T

T

K
|
K

A

A

G

A

V

Q

H

L

S

G

L

F

M

M

Q

R

S

T

C

A

A

A

V

I

A

E

L

L

G

A

P

P

Y

H

G

K

I

I

R

T

C

V

N

N

S

A

V

I

M

M

P

P

G

G

T

N

I

I

A

M

T

T

D

E

L

G

N

L

A

L

Q

E

D

N

L

-

A

-

D

G

E

E

A

E

K

Y

K

I

A

A

Y

S

F

M

E

A

K

R

R

S

I

I

P

P

L

A

G

G

R

A

L

L

G

G

R

T

P

P

E

E

D

D

V

I

A

G

D

H

C

L

V

A

T

A

F

F

L

L

A

A

S

T

D

K

R

E

A

A

R

G

Y

Y

V

I

T

T

G

G

A

Q

A

A

L

I

L

A

V

V

D

D

G

G

active site: G21 (= G16), S147 (= S149), W158 (≠ Q160), Y161 (= Y163), K165 (= K167)
binding calcium ion: D55 (≠ E58), G58 (= G61), G60 (vs. gap)

4cqmA Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP (see paper)
41% identity, 98% coverage: 3:257/260 of query aligns to 4:248/248 of 4cqmA

query
sites
4cqmA

L

L

K

R

D

S

K

A

V

L

V

A

I

L

V

V

T

T

G
|
G

G

A

S
x
G

R
x
S

G
|
G

I
|
I

G

G

R

R

A

A

I

V

A

S

V

V

A

R

C

L

A

A

A

G

E

E

G

G

A

A

D

T

V

V

A

A

I

A

N

C

Y

-

W

-

G

-

D
|
D

N
x
L

D

D

V

-

S

-

Y

-

G

-

R

-

R

R

S

A

A

A

V

A

A

Q

E

E

V

T

V

V

A

R

E

L

I

L

E

P

A

P

L

R

G

G

R

N

R

H

V

A

I

-

A

A

I

F

E

Q

G
x
A

N
x
D

V
|
V

A

S

A

E

R

A

E

R

T

A

G

A

Q

R

Q

C

L

L

V

L

R

E

H

Q

T

V

V

Q

E

A

A

C

F

F

G

S

K

R

V

P

-

P

D

S

V

V

L

V

A

V

S

S

N
x
C

A
|
A

G
|
G

I
|
I

C

T

P

Q

F

D

H

E

A

F

F

L

L

L

D

H

M

M

P

S

P

E

E

D

V

D

L

W

E

D

S

K

T

V

V

I

A

A

V
|
V

N

N

L

L

N

K

G

G

A

T

F

F

Y

L

V

V

T

T

Q

Q

A

A

Q

Q

Q

A

M

L

K

V

L

S

Q

N

G

G

T

C

G

R

G

G

A

S

I

I

V

I

A

N

T
x
I

S
|
S

I

I

S

V

A

G

L

K

V

V

G

G

G

N

G

V

M

G

Q

Q

T

T

H

N

Y
|
Y

T

A

P

A

T

S

K
|
K

A

A

G

G

V

V

H

I

S

G

L

L

M

T

Q

Q

S

T

C

A

A

A

V

R

A

E

L

L

G

G

P

R

Y

H

G

G

I

I

R

R

C

C

N

N

S

S

V

V

M

L

P
|
P

G
|
G

T
x
F

I
|
I

A

A

T
|
T

D
x
P

L
x
M

N
x
T

-

Q

-

K

-

V

A

P

Q

Q

D

K

L

V

A

V

D

D

E

K

A

-

K

-

A

-

Y

-

F

I

E

T

K

E

R

M

I

I

P

P

L

M

G

G

R

H

L

L

G

G

R

D

P

P

E

E

D

D

V

V

A

A

D

D

C

V

V

V

T

A

F

F

L

L

A

A

S

S

D

E

R

D

A

S

R

G

Y

Y

V

I

T

T

G

G

A

T

A

S

L

V

L

E

V

V

D

T

G

G

L

L

F

F

V

M

active site: G17 (= G16), S143 (= S150), Y156 (= Y163), K160 (= K167)
binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G12), G15 (≠ S14), S16 (≠ R15), G17 (= G16), I18 (= I17), D37 (= D39), L38 (≠ N40), A61 (≠ G69), D62 (≠ N70), V63 (= V71), C90 (≠ N97), A91 (= A98), G92 (= G99), I93 (= I100), V113 (= V120), I141 (≠ T148), S142 (= S149), S143 (= S150), Y156 (= Y163), K160 (= K167), P186 (= P193), G187 (= G194), F188 (≠ T195), I189 (= I196), T191 (= T198), P192 (≠ D199), M193 (≠ L200), T194 (≠ N201)

Q92506 (3R)-3-hydroxyacyl-CoA dehydrogenase; 17-beta-hydroxysteroid dehydrogenase 8; 17-beta-HSD 8; HSD17B8; 3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit; KAR alpha subunit; 3-oxoacyl-[acyl-carrier-protein] reductase; Estradiol 17-beta-dehydrogenase 8; Protein Ke6; Ke6; Short chain dehydrogenase/reductase family 30C member 1; Testosterone 17-beta-dehydrogenase 8; EC 1.1.1.n12; EC 1.1.1.62; EC 1.1.1.239 from Homo sapiens (Human) (see 2 papers)
40% identity, 98% coverage: 3:257/260 of query aligns to 9:261/261 of Q92506

query
sites
Q92506

L

L

K

R

D

S

K

A

V

L

V

A

I
x
L

V
|
V

T
|
T

G
|
G

G
x
A

S
x
G

R
x
S

G
|
G

I
|
I

G

G

R

R

A

A

I

V

A

S

V

V

A

R

C

L

A

A

A

G

E

E

G

G

A

A

D

T

V

V

A

A

I

A

N

C

Y

-

W

-

G

-

D
|
D

N
x
L

D

D

V

-

S

-

Y

-

G

-

R

-

R

R

S

A

A

A

V

A

A

Q

E

E

V

T

V

V

A

R

E

L

I

L

E

G

A

G

L

P

G

G

R

S

R

K

V

E

I

G

A

P

I

P

E

R

G

G

N

N

V

H

A

A

R

F

E

Q

T
x
A

-
x
D

-
x
V

-

S

-

E

-

A

-

R

-

A

G

A

Q

R

Q

C

L

L

V

L

R

E

H

Q

T

V

V

Q

E

A

A

C

F

F

G

S

K

R

V

P

-

P

D

S

V

V

L

V

A

V

S

S

N

C

A

A

G

G

I

I

C

T

P

Q

F

D

H

E

A

F

F

L

L

L

D

H

M

M

P

S

P

E

E

D

V

D

L

W

E

D

S

K

T

V

V

I

A

A

V

V

N

N

L

L

N

K

G

G

A

T

F

F

Y

L

V

V

T

T

Q

Q

A

A

Q

Q

Q

A

M

L

K

V

L

S

Q

N

G

G

T

C

G
x
R

G

G

A

S

I

I

V

I

A

N

T

I

S

S

I

I

S
x
V

A

G

L

K

V

V

G

G

G

N

G

V

M

G

Q

Q

T

T

H

N

Y
|
Y

T
x
A

P
x
A

T
x
S

K
|
K

A

A

G

G

V

V

H

I

S

G

L

L

M

T

Q

Q

S

T

C

A

A

A

V

R

A

E

L

L

G

G

P
x
R

Y

H

G

G

I

I

R

R

C

C

N

N

S

S

V

V

M

L

P

P

G

G

T

F

I
|
I

A
|
A

T
|
T

D

P

L

M

N

T

-

Q

-

K

-

V

A

P

Q

Q

D

K

L

V

A

V

D

D

E

K

A

-

K

-

A

-

Y

-

F

I

E

T

K

E

R

M

I

I

P

P

L

M

G

G

R

H

L

L

G

G

R

D

P

P

E

E

D

D

V

V

A

A

D

D

C

V

V

V

T

A

F

F

L

L

A

A

S

S

D

E

R

D

A

S

R

G

Y

Y

V

I

T

T

G

G

A

T

A

S

L

V

L

E

V

V

D

T

G

G

L

L

F

F

V

M

15:23 (vs. 9:17, 56% identical) binding
D42 (= D39) mutation to A: Reduced NADH-dependent reductase activity with acetoacetyl-CoA. Reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Increases NADPH-dependent reductase activities. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
DL 42:43 (≠ DN 39:40) binding
ADV 74:76 (≠ T-- 76) binding
R148 (≠ G142) mutation to E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
V158 (≠ S152) to L: in a breast cancer sample; somatic mutation
Y169 (= Y163) mutation to A: Strongly reduced NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
YAASK 169:173 (≠ YTPTK 163:167) binding
K173 (= K167) mutation to A: Abolishes NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Slightly decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
R189 (≠ P183) mutation to E: No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
IAT 202:204 (= IAT 196:198) binding

Q48436 Diacetyl reductase [(S)-acetoin forming]; Acetoin(diacetyl) reductase; AR; Meso-2,3-butanediol dehydrogenase; EC 1.1.1.304 from Klebsiella pneumoniae (see paper)
36% identity, 97% coverage: 6:258/260 of query aligns to 3:256/256 of Q48436

query
sites
Q48436

K

K

V

V

V

A

I
x
L

V
|
V

T
|
T

G
|
G

G
x
A

S
x
G

R
x
Q

G
|
G

I
|
I

G
|
G

R
x
K

A
|
A

I
|
I

A
|
A

V
x
L

A
x
R

C
x
L

A
x
V

A
x
K

E
x
D

G
|
G

A
x
F

D
x
A

V
|
V

A
|
A

I
|
I

N
x
A

Y
x
D

W

Y

G

N

D

D

N

-

D

-

V

-

S

-

Y

-

G

-

R

-

S

-

A

A

V

T

A

A

E

K

V

A

V

V

A

A

-

S

E

E

I

I

E

N

A

Q

L

A

G

G

R

G

R

R

V

A

I

M

A

A

I

V

E

K

G

V

N
x
D

V

V

A

S

A

D

R

R

E

D

T

Q

G

V

Q

F

Q

A

L

A

V

V

R

E

H

Q

T

A

V

R

E

K

A

T

F

L

G

G

K

G

V

F

D

D

V

V

L

I

A

V

S

N

N

N

A

A

G

G

I

V

C

A

P

P

F

S

H

T

A

P

F

I

L

E

D

S

M

I

P

T

P

P

E

E

V

I

L

V

E

D

S

K

T

V

V

Y

A

N

V

I

N

N

L

V

N

K

G

G

A

V

F

I

Y

W

V

G

T

I

Q

Q

A

A

A

V

Q

E

Q

A

M

F

K

K

L

K

Q

E

G

G

T

H

G

G

A

K

I

I

V

I

A

N

T

A

S

C

S

S

I

Q

S

A

A

G

L

H

V

V

G

G

G

N

G

P

M

E

Q

L

T

A

H

V

Y

Y

T

S

P

S

T

S

K
|
K

A

F

G

A

V

V

H

R

S

G

L

L

M

T

Q

Q

S

T

C

A

A

A

V

R

A

D

L

L

G

A

P

P

Y

L

G

G

I

I

R

T

C

V

N

N

S

G

V

Y

M

C

P

P

G

G

T

I

I

V

A

K

T

T

D

P

L

M

N

W

A

A

Q

E

-

I

-

D

-

R

D

Q

L

V

A

S

D

E

E

A

A

A

K

G

K

K

-

P

-

L

-

G

-

Y

-

G

-

T

A

A

Y

E

F

F

E

A

K

K

R

R

I

I

P

T

L

L

G

G

R

R

L

L

G

S

R

E

P

P

E

E

D

D

V

V

A

A

D

A

C

C

V

V

T

S

F

Y

L

L

A

A

S

S

D

P

R

D

A

S

R

D

Y

Y

V

M

T

T

G

G

A

Q

A

S

L

L

V

I

D

D

G

G

L

M

F

V

V

F

N

N

6:33 (vs. 9:36, 46% identical) binding
D59 (≠ N70) binding
K156 (= K167) binding

P73574 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-acyl carrier protein reductase; EC 1.1.1.100 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
39% identity, 97% coverage: 3:255/260 of query aligns to 4:244/247 of P73574

query
sites
P73574

L

L

K

T

D

A

K

Q

V

V

V

A

I

L

V

V

T

T

G

G

G
x
A

S

S

R

R

G

G

I

I

G

G

R

K

A

A

I

T

A

A

V

L

A

A

C

L

A

A

E

T

G

G

A

M

D

K

V

V

A

V

I

V

N

N

Y

Y

W

A

G

Q

D

S

N

S

D

-

V

-

S

-

Y

-

G

-

R

-

S

T

A

A

V

A

A

D

E

A

V

V

A

A

E

E

I

I

E

I

A

A

L

N

G

G

R

G

R

E

V

A

I

I

A

A

I

V

E

Q

G

A

N

N

V

V

A

A

A

N

R

A

E

D

T

E

G

V

Q

D

Q

Q

L

L

V

I

R

K

H

T

T

T

V

L

E

D

A

K

F

F

G

S

K

R

V

I

D

D

V

V

L

L

A

V

S

N

N

N

A

A

G

G

I

I

C

T

P

R

F

D

H

T

A

L

F

L

L

L

D

R

M

M

P

K

P

L

E

E

V

D

L

W

E

Q

S

A

T

V

V

I

A

D

V

L

N

N

L

L

N

T

G

G

A

V

F

F

Y

L

V

C

T

T

Q

K

A

A

A

V

A

S

Q

K

Q

L

M

M

K

-

L

L

Q

K

G

Q

T

K

G

S

G

G

A

R

I

I

V

I

A

N

T

I

S

T

S

S

I

V

S

A

A

G

L

M

V

M

G

G

G

N

G
x
P

M

G

Q

Q

T

A

H

N

Y

Y

T

S

P

A

T

A

K
|
K

A

A

G

G

V

V

H

I

S

G

L

F

M

T

Q

K

S

T

C

V

A

A

V

K

A

E

L

L

G

A

P

S

Y

R

G

G

I

V

R

T

C

V

N

N

S

A

V

V

M

A

P

P

G

G

T
x
F

I

I

A

A

T

T

D

D

L

M

N

T

A

-

Q

E

D

N

L

L

A
x
N

D

A

E

E

A

P

K

I

K

L

A

Q

Y

F

F

-

E

-

K

-

R

-

I

I

P

P

L

L

G

A

R

R

L

Y

G

G

R

Q

P

P

E

E

D

E

V

V

A

A

D

G

C

T

V

I

T

R

F

F

L

L

A

A

S

T

D

D

-

P

R

A

A

A

R

A

Y

Y

V

I

T

T

G

G

A

Q

A

T

L

F

L

N

V

V

D

D

G

G

L

M

A14 (≠ G13) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
P151 (≠ G158) 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 (= K167) mutation to A: Almost no activity on acetoacetyl-CoA.
F188 (≠ T195) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
N198 (≠ A206) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.

4fn4A Short-chain NAD(h)-dependent dehydrogenase/reductase from sulfolobus acidocaldarius (see paper)
37% identity, 98% coverage: 3:257/260 of query aligns to 5:253/254 of 4fn4A

query
sites
4fn4A

L

L

K

K

D

N

K

K

V

V

I

I

V

V

T

T

G
|
G

G

A

S
x
G

R
x
S

G
|
G

I
|
I

G

G

R

R

A

A

I

I

A

A

V

K

A

K

C

F

A

A

A

L

-

N

E

D

G

S

A

I

D

V

V

V

A

A

I

V

N
x
E

Y
x
L

W
x
L

G

E

D

D

N
x
R

D

-

V

-

S

-

Y

-

G

-

R

-

S

-

A

-

V

L

A

N

E

Q

V

I

V

V

A

Q

E

E

I

L

E

R

A

G

L

M

G

G

R

K

R

E

V

V

I

L

A

G

I

V

E

K

G
x
A

N
x
D

V
|
V

A

S

A

K

R

K

E

K

T

D

G

V

Q

E

L

F

V

V

R

R

H

R

T

T

V

F

E

E

A

T

F

Y

G

S

K

R

V

I

D

D

V

V

L

L

A

C

S

N

N
|
N

A
|
A