SitesBLAST

P0DJA2 Alcohol dehydrogenase 2; Alcohol dehydrogenase II; ADH II; EC 1.1.1.1 from Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) (see 2 papers)
52% identity, 98% coverage: 10:393/393 of query aligns to 6:383/383 of P0DJA2

query
sites
P0DJA2

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D39 (= D43) binding NAD(+)
N71 (= N75) binding NAD(+)
G98 (= G102) binding NAD(+)
S99 (= S103) binding NAD(+)
T138 (= T142) binding NAD(+)
T139 (= T143) binding NAD(+)
T147 (= T151) binding NAD(+)
F149 (= F153) binding NAD(+)
K160 (= K164) binding NAD(+)
L179 (= L183) binding NAD(+)
G182 (= G186) binding NAD(+)
M183 (= M187) binding NAD(+)
D194 (= D198) binding Fe(2+)
H198 (= H202) binding Fe(2+)
H263 (= H267) binding Fe(2+)
H267 (= H271) binding NAD(+)
H277 (= H281) binding Fe(2+); binding NAD(+)

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 3 papers)
51% identity, 98% coverage: 10:393/393 of query aligns to 4:381/381 of P31005

query
sites
P31005

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G13 (= G19) mutation to A: Shows a reduced dehydrogenase activity.
G15 (= G21) mutation to A: Shows almost the same dehydrogenase activity as the wild-type.
D88 (= D94) mutation to N: Shows almost the same dehydrogenase activity as the wild-type.
G95 (= G101) mutation to A: Shows a 10-fold decreased affinity for NAD and NADH and a strongly reduced dehydrogenase activity. Completely insensitive to the stimulating effect of the activator protein Act.
S97 (= S103) mutation to G: Shows an increase of the dehydrogenase activity and a decrease of the affinity for NAD and NADH. Completely insensitive to the stimulating effect of the activator protein Act. It does not bind NAD.; mutation to T: Shows an increase of the dehydrogenase activity and affinity for NAD and NADH.
D100 (= D106) mutation to N: Loss of dehydrogenase activity. It still binds NADH.
K103 (= K109) mutation to R: Loss of dehydrogenase activity. It does not bind NADH.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

2bi4A Lactaldehyde:1,2-propanediol oxidoreductase of escherichia coli (see paper)
42% identity, 96% coverage: 17:393/393 of query aligns to 12:382/382 of 2bi4A

query
sites
2bi4A

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binding fe (iii) ion: D195 (= D198), H199 (= H202), H262 (= H267), H276 (= H281)
binding nicotinamide-adenine-dinucleotide: D38 (= D43), T40 (≠ G45), L41 (≠ I46), G96 (= G101), G97 (= G102), S98 (= S103), T139 (= T142), T140 (= T143), V152 (≠ I155), K161 (= K164), G183 (= G186), M184 (= M187), L188 (= L191), D195 (= D198), H199 (= H202), H262 (= H267), H276 (= H281)

P0A9S1 Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli (strain K12) (see paper)
42% identity, 96% coverage: 17:393/393 of query aligns to 12:382/382 of P0A9S1

query
sites
P0A9S1

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V

I

Y

Y

D

D

E

G

T

V

I

V

P

P

N

N

P

P

T

T

D

I

I

T

N

V

V

V

H

K

D

E

G

G

V

L

D

G

V

V

Y

F

K

Q

E

N

N

S

N

G

C

A

D

D

S

Y

L

L

I

I

T

A

L

I

G

G

G
|
G

G

G

S

S

S

P

H

Q

D

D

C

T

G

C

K

K

G

A

I

I

G

G

L

I

V

I

V

S

A

N

N

N

G

P

-

E

-

F

G

A

K

D

I

V

H

R

D

S

F

L

E

E

G

G

V

L

D

S

Q

P

S

T

T

N

K

K

P

P

M

S

P

V

P

P

Y

I

V

L

A

A

V

I

N

P

T

T

A

A

G

G

T

T

A

A

S

A

E

E

M

V

T

T

R

I

F

N

C

Y

I

V

I

I

T

T

D

D

T

E

S

E

R

K

K

R

V

R

K

K

M

F

A

V

I

C

V

V

D

D

W

P

R

H

V

D

T

I

P

P

G

Q

I

V

A

A

L

F

D

I

D

D

P

A

L

D

L

M

M

M

M

D

G

G

M

M

P

P

A

A

L

L

T

K

A

A

T

T

G

G

M

V

D
|
D

A

A

L

L

T

T

H
|
H

A

A

V

I

E

E

A

G

Y

Y

V

I

S

T

T

R

I

G

A

A

T

W

P

A

M

L

T

T

D

D

S

A

A

L

A

H

E

I

K

K

A

A

I

I

E

E

L

I

I

I

A

A

Q

G

H

A

L

L

R

R

P

G

A

S

V

V

A

A

N

G

G

D

D

K

D

D

I

-

V

-

A

A

R

G

E

E

G

E

M

M

C

A

Y

L

A

G

Q

Q

Y

Y

L

V

A

A

G

G

M

M

A

G

F

F

N

S

N

N

A

V

S

G

L

L

G

G

H

L

V

V

H

H

A

G

M

M

A

A

H

H

Q

P

L

L

G

G

G

A

F

F

Y

Y

D

N

L

T

P

P

H

H

G

G

E

V

C

A

N

N

A

A

I

I

L

L

P

P

H

H

V

V

S

M

R

R

F

Y

N

N

L

A

I

D

A

F

K

T

M

G

D

E

R

K

F

Y

I

R

K

D

I

I

A

A

E

R

L

V

M

M

G

G

E

V

N

K

V

V

D

E

G

G

L

M

A

S

P

L

R

E

D

E

A

A

A

R

E

N

L

A

A

A

L

V

E

E

A

A

I

V

Q

F

K

A

L

L

S

N

A

R

D

D

I

V

G

G

I

I

P

P

S

P

G

H

L

L

I

R

E

D

L

V

G

G

K

-

R

-

Y

-

G

-

K

-

E

-

V

V

K

R

A

K

E

E

D

D

I

I

E

P

T

A

M

L

T

A

G

Q

N

A

A

A

Q

L

K

D

D

D

A

V

C

C

G

T

L

G

T

G

N

N

P

P

R

R

R

E

P

A

K

T

D

L

M

E

D

D

V

I

A

V

A

E

I

L

Y

Y

T

H

A

T

A

A

L

W

G16 (= G21) mutation to D: No effect on enzyme activity.
D38 (= D43) mutation to G: Enzyme can now use NADP.
G96 (= G101) mutation to E: Loss of NAD binding and enzyme activity.
D195 (= D198) mutation to L: Complete loss of iron-binding.
H199 (= H202) mutation H->A,F: Complete loss of iron-binding.

Sites not aligning to the query:

1:9 MANRMILNE→M: Loss of enzyme activity, loss of dimerization.

1rrmA Crystal structure of lactaldehyde reductase
42% identity, 96% coverage: 17:393/393 of query aligns to 12:382/385 of 1rrmA

query
sites
1rrmA

L

W

I

F

G

G

I

R

G

G

A

A

A

V

K

G

E

A

I

L

P

T

A

D

K

E

I

V

K

K

D

R

L

R

G

G

G

Y

S

Q

K

K

P

A

L

L

I

I

V

V

T

T

D
|
D

K

K

G
x
T

I
x
L

T

V

A

Q

A

C

G

G

I

V

T

V

K

A

E

K

I

V

T

T

D

D

L

K

L

M

D

D

G

A

A

A

E

G

M

L

A

A

Y

W

V

A

V

I

Y

Y

D

D

E

G

T

V

I

V

P

P

N
|
N

P

P

T

T

D

I

I

T

N

V

V

V

H

K

D

E

G

G

V

L

D

G

V

V

Y

F

K

Q

E

N

N

S

N

G

C

A

D

D

S

Y

L

L

I

I

T

A

L

I

G

G

G
|
G

S
|
S

S

P

H

Q

D

D

C

T

G

C

K

K

G

A

I

I

G

G

L

I

V

I

V

S

A

N

N

N

G

P

-

E

-

F

G

A

K

D

I

V

H

R

D

S

F

L

E

E

G

G

V

L

D

S

Q

P

S

T

T

N

K

K

P

P

M

S

P

V

P

P

Y

I

V

L

A

A

V

I

N

P

T
|
T

A

A

G

G

T
|
T

A

A

S

A

E

E

M

V

T

T

R

I

F

N

C

Y

I
x
V

I

I

T

T

D

D

T

E

S

E

R

K

K

R

V

R

K
|
K

M

F

A

V

I

C

V

V

D

D

W

P

R

H

V

D

T

I

P

P

G

Q

I

V

A

A

L

F

D

I

D

D

P

A

L

D

L

M

M

M

M

D

G
|
G

M
|
M

P

P

A

A

L
|
L

T

K

A

A

T

T

G

G

M

V

D
|
D

A

A

L

L

T

T

H
|
H

A

A

V

I

E

E

A

G

Y

Y

V

I

S

T

T

R

I

G

A

A

T

W

P

A

M

L

T

T

D

D

S

A

A

L

A

H

E

I

K

K

A

A

I

I

E

E

L

I

I

I

A

A

Q

G

H

A

L

L

R

R

P

G

A

S

V

V

A

A

N

G

G

D

D

K

D

D

I

-

V

-

A

A

R

G

E

E

G

E

M

M

C

A

Y

L

A

G

Q

Q

Y

Y

L

V

A

A

G

G

M

M

A

G

F

F

N

S

N

N

A

V

S

G

L
|
L

G

G

H

L

V

V

H
|
H

A

G

M

M

A

A

H

H

Q

P

L

L

G

G

G

A

F

F

Y

Y

D

N

L

T

P

P

H
|
H

G

G

E

V

C

A

N

N

A

A

I

I

L

L

P

P

H

H

V

V

S

M

R

R

F

Y

N

N

L

A

I

D

A

F

K

T

M

G

D

E

R

K

F

Y

I

R

K

D

I

I

A

A

E

R

L

V

M

M

G

G

E

V

N

K

V

V

D

E

G

G

L

M

A

S

P

L

R

E

D

E

A

A

A

R

E

N

L

A

A

A

L

V

E

E

A

A

I

V

Q

F

K

A

L

L

S

N

A

R

D

D

I

V

G

G

I

I

P

P

S

P

G

H

L

L

I

R

E

D

L

V

G

G

K

-

R

-

Y

-

G

-

K

-

E

-

V

V

K

R

A

K

E

E

D

D

I

I

E

P

T

A

M

L

T

A

G

Q

N

A

A

A

Q

L

K

D

D

D

A

V

C
|
C

G

T

L

G

T

G

N

N

P

P

R

R

R

E

P

A

K

T

D

L

M

E

D

D

V

I

A

V

A

E

I

L

Y

Y

T

H

A

T

A

A

L

W

binding adenosine-5-diphosphoribose: D38 (= D43), T40 (≠ G45), L41 (≠ I46), N70 (= N75), G96 (= G101), G97 (= G102), S98 (= S103), T139 (= T142), T140 (= T143), T143 (= T146), V152 (≠ I155), K161 (= K164), G183 (= G186), M184 (= M187), L188 (= L191), H276 (= H281)
binding fe (ii) ion: L258 (= L263), C361 (= C372)
binding zinc ion: D195 (= D198), H199 (= H202), H262 (= H267), H276 (= H281)

7qlqAAA Lactaldehyde reductase (see paper)
42% identity, 96% coverage: 17:393/393 of query aligns to 11:381/383 of 7qlqAAA

query
sites
7qlqAAA

L

W

I

F

G

G

I

R

G

G

A

A

A

V

K

G

E

A

I

L

P

T

A

D

K

E

I

V

K

K

D

R

L

R

G

G

G

Y

S

Q

K

K

P

A

L

L

I

I

V

V

T

T

D
|
D

K

K

G
x
T

I
x
L

T

V

A

Q

A

C

G

G

I

V

T

V

K

A

E

K

I

V

T

T

D

D

L

K

L

M

D

D

G

A

A

A

E

G

M

L

A

A

Y

W

V

A

V

I

Y

Y

D

D

E

G

T

V

I

V

P

P

N

N

P

P

T

T

D

I

I

T

N

V

V

V

H

K

D

E

G

G

V

L

D

G

V

V

Y

F

K

Q

E

N

N

S

N

G

C

A

D

D

S

Y

L

L

I

I

T

A

L

I

G

G

G
|
G

S
|
S

S

P

H

Q

D

D

C

T

G

C

K

K

G

A

I

I

G

G

L

I

V

I

V

S

A

N

N

N

G

P

-

E

-

F

G

A

K

D

I

V

H

R

D

S

F

L

E

E

G

G

V

L

D

S

Q

P

S

T

T

N

K

K

P

P

M

S

P

V

P

P

Y

I

V

L

A

A

V

I

N

P

T
|
T

A

A

G

G

T
|
T

A

A

S

A

E

E

M

V

T

T

R

I

F
x
G

C

Y

I

V

I

I

T

T

D

D

T

E

S

E

R

K

K

R

V

R

K
|
K

M

F

A

V

I

C

V
|
V

D

D

W

P

R

H

V

D

T

I

P

P

G

Q

I

V

A

A

L

F

D

I

D

D

P

A

L

D

L

M

M

M

M

D

G
|
G

M
|
M

P

P

A

A

L
|
L

T

K

A

A

T

T

G

G

M

V

D
|
D

A

A

L

L

T

T

H
|
H

A

A

V

I

E

E

A

G

Y

Y

V

I

S

T

T

R

I

G

A

A

T

W

P

A

M

L

T

T

D

D

S

A

A

L

A

H

E

I

K

K

A

A

I

I

E

E

L

I

I

I

A

A

Q

G

H

A

L

L

R

R

P

G

A

S

V

V

A

A

N

G

G

D

D

K

D

D

I

-

V

-

A

A

R

G

E

E

G

E

M

M

C

A

Y

L

A

G

Q

Q

Y

Y

L

V

A

A

G

G

M

M

A

G

F
|
F

N
x
S

N

N

A

V

S

G

L

V

G

G

H

L

V

V

H
|
H

A

G

M

M

A

A

H

H

Q

P

L

L

G

G

G

A

F

F

Y

Y

D

N

L

T

P

P

H
|
H

G

G

E

V

C

A

N

N

A

A

I

I

L

L

P

P

H

H

V

V

S

M

R

R

F

Y

N

N

L

A

I

D

A

F

K

T

M

G

D

E

R

K

F

Y

I

R

K

D

I

I

A

A

E

R

L

V

M

M

G

G

E

V

N

K

V

V

D

E

G

G

L

M

A

S

P

L

R

E

D

E

A

A

A

R

E

N

L

A

A

A

L

V

E

E

A

A

I

V

Q

F

K

A

L

L

S

N

A

R

D

D

I

V

G

G

I

I

P

P

S

P

G

H

L

L

I

R

E

D

L

V

G

G

K

-

R

-

Y

-

G

-

K

-

E

-

V

V

K

R

A

K

E

E

D

D

I

I

E

P

T

A

M

L

T

A

G

Q

N

A

A

A

Q

L

K

D

D

D

A

V

C
|
C

G

T

L

G

T

G

N

N

P

P

R

R

R

E

P

A

K

T

D

L

M

E

D

D

V

I

A

V

A

E

I

L

Y

Y

T

H

A

T

A

A

L

W

binding adenosine-5-diphosphoribose: D37 (= D43), T39 (≠ G45), L40 (≠ I46), G95 (= G101), G96 (= G102), S97 (= S103), T138 (= T142), T139 (= T143), T142 (= T146), K160 (= K164), G182 (= G186), M183 (= M187), L187 (= L191), H275 (= H281)
binding 2-(3,4-dimethoxyphenyl)ethanamide: G149 (≠ F153), V164 (= V168), H198 (= H202), F252 (= F258), S253 (≠ N259), H261 (= H267), C360 (= C372)
binding fe (iii) ion: D194 (= D198), H198 (= H202), H261 (= H267), H275 (= H281)

7qlgAAA Lactaldehyde reductase (see paper)
42% identity, 96% coverage: 17:393/393 of query aligns to 11:381/383 of 7qlgAAA

query
sites
7qlgAAA

L

W

I

F

G

G

I

R

G

G

A

A

A

V

K

G

E

A

I

L

P

T

A

D

K

E

I

V

K

K

D

R

L

R

G

G

G

Y

S

Q

K

K

P

A

L

L

I

I

V

V

T

T

D
|
D

K

K

G
x
T

I
x
L

T

V

A

Q

A

C

G

G

I

V

T

V

K

A

E

K

I

V

T

T

D

D

L

K

L

M

D

D

G

A

A

A

E

G

M

L

A

A

Y

W

V

A

V

I

Y

Y

D

D

E

G

T

V

I

V

P

P

N
|
N

P

P

T

T

D

I

I

T

N

V

V

V

H

K

D

E

G

G

V

L

D

G

V

V

Y

F

K

Q

E

N

N

S

N

G

C

A

D

D

S

Y

L

L

I

I

T

A

L

I

G

G

G
|
G

S
|
S

S

P

H

Q

D
|
D

C

T

G

C

K

K

G

A

I

I

G

G

L

I

V

I

V

S

A

N

N

N

G

P

-

E

-

F

G

A

K

D

I

V

H

R

D

S

F

L

E

E

G

G

V

L

D

S

Q

P

S

T

T

N

K

K

P

P

M

S

P

V

P

P

Y

I

V

L

A

A

V

I

N

P

T
|
T

A

A

G

G

T
|
T

A

A

S

A

E

E

M

V

T
|
T

R

I

F
x
N

C

Y

I

V

I

I

T

T

D

D

T

E

S

E

R

K

K

R

V

R

K
|
K

M

F

A

V

I

C

V

V

D

D

W

P

R

H

V

D

T

I

P

P

G

Q

I

V

A

A

L

F

D

I

D

D

P

A

L

D

L

M

M

M

M

D

G

G

M

M

P

P

A

A

L
|
L

T

K

A

A

T

T

G

G

M

V

D
|
D

A

A

L

L

T

T

H
|
H

A

A

V

I

E

E

A

G

Y

Y

V

I

S

T

T

R

I

G

A

A

T

W

P

A

M

L

T

T

D

D

S

A

A

L

A

H

E

I

K

K

A

A

I

I

E

E

L

I

I

I

A

A

Q

G

H

A

L

L

R

R

P

G

A

S

V

V

A

A

N

G

G

D

D

K

D

D

I

-

V

-

A

A

R

G

E

E

G

E

M

M

C

A

Y

L

A

G

Q

Q

Y

Y

L

V

A

A

G

G

M

M

A

G

F

F

N

S

N

N

A

V

S

G

L

V

G

G

H

L

V

V

H
|
H

A

G

M

M

A

A

H

H

Q

P

L

L

G

G

G

A

F

F

Y

Y

D

N

L

T

P

P

H
|
H

G

G

E

V

C

A

N

N

A

A

I

I

L

L

P

P

H

H

V

V

S

M

R

R

F

Y

N

N

L

A

I

D

A

F

K

T

M

G

D

E

R

K

F

Y

I

R

K

D

I

I

A

A

E

R

L

V

M

M

G

G

E

V

N

K

V

V

D

E

G

G

L

M

A

G

P

L

R

E

D

E

A

A

A

R

E

N

L

A

A

A

L

V

E

E

A

A

I

V

Q

F

K

A

L

L

S

N

A

R

D

D

I

V

G

G

I

I

P

P

S

P

G

H

L

L

I

R

E

D

L

V

G

G

K

-

R

-

Y

-

G

-

K

-

E

-

V

V

K

R

A

K

E

E

D

D

I

I

E

P

T

A

M

L

T

A

G

Q

N

A

A

A

Q

L

K

D

D

D

A

V

C

C

G

T

L

G

T

G

N

N

P

P

R

R

R

E

P

A

K

T

D

L

M

E

D

D

V

I

A

V

A

E

I

L

Y

Y

T

H

A

T

A

A

L

W

binding fe (iii) ion: D194 (= D198), H198 (= H202), H261 (= H267), H275 (= H281)
binding 1,4-dihydronicotinamide adenine dinucleotide: D37 (= D43), T39 (≠ G45), L40 (≠ I46), N69 (= N75), G95 (= G101), G96 (= G102), S97 (= S103), D100 (= D106), T138 (= T142), T139 (= T143), T142 (= T146), T147 (= T151), N149 (≠ F153), K160 (= K164), L187 (= L191), H198 (= H202), H275 (= H281)

5br4A E. Coli lactaldehyde reductase (fuco) m185c mutant (see paper)
42% identity, 96% coverage: 17:393/393 of query aligns to 13:383/385 of 5br4A

query
sites
5br4A

L

W

I

F

G

G

I

R

G

G

A

A

A

V

K

G

E

A

I

L

P

T

A

D

K

E

I

V

K

K

D

R

L

R

G

G

G

Y

S

Q

K

K

P

A

L

L

I

I

V

V

T

T

D
|
D

K

K

G
x
T

I
x
L

T

V

A

Q

A

C

G

G

I

V

T

V

K

A

E

K

I

V

T

T

D

D

L

K

L

M

D

D

G

A

A

A

E

G

M

L

A

A

Y

W

V

A

V

I

Y

Y

D

D

E

G

T

V

I

V

P
|
P

N

N

P

P

T

T

D

I

I

T

N

V

V

V

H

K

D

E

G

G

V

L

D

G

V

V

Y

F

K

Q

E

N

N

S

N

G

C

A

D

D

S

Y

L

L

I

I

T

A

L

I

G

G

G
|
G

S
|
S

S

P

H

Q

D
|
D

C

T

G

C

K

K

G

A

I

I

G

G

L

I

V

I

V

S

A

N

N

N

G

P

-

E

-

F

G

A

K

D

I

V

H

R

D

S

F

L

E

E

G

G

V

L

D

S

Q

P

S

T

T

N

K

K

P

P

M

S

P

V

P

P

Y

I

V

L

A

A

V

I

N

P

T
|
T

A

A

G

G

T
|
T

A

A

S

A

E

E

M

V

T
|
T

R

I

F
x
N

C

Y

I
x
V

I

I

T

T

D

D

T

E

S

E

R

K

K

R

V

R

K
|
K

M

F

A

V

I

C

V

V

D

D

W

P

R

H

V

D

T

I

P

P

G

Q

I

V

A

A

L

F

D

I

D

D

P

A

L

D

L

M

M

M

M

D

G
|
G

M
x
C

P

P

A

A

L
|
L

T

K

A

A

T

T

G

G

M

V

D
|
D

A

A

L

L

T

T

H
|
H

A

A

V

I

E

E

A

G

Y

Y

V

I

S

T

T

R

I

G

A

A

T

W

P

A

M

L

T

T

D

D

S

A

A

L

A

H

E

I

K

K

A

A

I

I

E

E

L

I

I

I

A

A

Q

G

H

A

L

L

R

R

P

G

A

S

V

V

A

A

N

G

G

D

D

K

D

D

I

-

V

-

A

A

R

G

E

E

G

E

M

M

C

A

Y

L

A

G

Q

Q

Y

Y

L

V

A

A

G

G

M

M

A

G

F

F

N

S

N

N

A

V

S

G

L

L

G

G

H

L

V

V

H
|
H

A

G

M

M

A

A

H

H

Q

P

L

L

G

G

G

A

F

F

Y

Y

D

N

L

T

P

P

H
|
H

G

G

E

V

C

A

N

N

A

A

I

I

L

L

P

P

H

H

V

V

S

M

R

R

F

Y

N

N

L

A

I

D

A

F

K

T

M

G

D

E

R

K

F

Y

I

R

K

D

I

I

A

A

E

R

L

V

M

M

G

G

E

V

N

K

V

V

D

E

G

G

L

M

A

S

P

L

R

E

D

E

A

A

A

R

E

N

L

A

A

A

L

V

E

E

A

A

I

V

Q

F

K

A

L

L

S

N

A

R

D

D

I

V

G

G

I

I

P

P

S

P

G

H

L

L

I

R

E

D

L

V

G

G

K

-

R

-

Y

-

G

-

K

-

E

-

V

V

K

R

A

K

E

E

D

D

I

I

E

P

T

A

M

L

T

A

G

Q

N

A

A

A

Q

L

K

D

D

D

A

V

C

C

G

T

L

G

T

G

N

N

P

P

R

R

R

E

P

A

K

T

D

L

M

E

D

D

V

I

A

V

A

E

I

L

Y

Y

T

H

A

T

A

A

L

W

binding nicotinamide-adenine-dinucleotide: D39 (= D43), T41 (≠ G45), L42 (≠ I46), P70 (= P74), G97 (= G101), G98 (= G102), S99 (= S103), D102 (= D106), T140 (= T142), T141 (= T143), T144 (= T146), T149 (= T151), N151 (≠ F153), V153 (≠ I155), K162 (= K164), G184 (= G186), C185 (≠ M187), L189 (= L191), H277 (= H281)
binding zinc ion: D196 (= D198), H200 (= H202), H263 (= H267), H277 (= H281)

3zdrA Structure of the alcohol dehydrogenase (adh) domain of a bifunctional adhe dehydrogenase from geobacillus thermoglucosidasius ncimb 11955 (see paper)
35% identity, 93% coverage: 28:393/393 of query aligns to 22:400/403 of 3zdrA

query
sites
3zdrA

A

A

K

K

I

M

K

P

D

D

L

I

G

-

S

S

K

R

P

A

L

F

I

I

V

V

T

T

D

D

K

P

G

G

I

M

T

V

A

K

A

L

G

G

I

Y

T

V

K

D

E

K

I

V

T

L

D

Y

L

Y

L

L

D

R

G

R

A

R

E

P

M

-

A

D

Y

Y

V

V

-

H

-

S

-

E

V

I

Y

F

D

S

E

E

T

V

I

E

P

P

N

D

P

P

T

S

D

I

I

E

N

T

V

V

H

M

D

K

G

G

V

V

D

D

V

M

Y

M

K

R

E

S

N

F

N

E

C

P

D

D

S

V

L

I

I

I

T

A

L

L

G

G

S

S

S

P

H

M

D

D

C

A

G

A

K

K

G

A

I

M

G

W

L

L

V

F

V

Y

A

E

N

H

-

P

-

T

-

A

-

D

-

F

-

N

-

A

-

L

-

K

-

Q

-

K

-

F

-

L

-

D

-

I

G

R

G

K

K

R

I

V

H

Y

D

K

F

Y

E

P

G

K

V

L

D

G

Q

Q

S

K

T

A

K

K

P

-

M

-

P

-

Y

F

V

V

A

A

V

I

N

P

T

T

A

S

G

G

T

T

A

G

S

S

E

E

M

V

T

T

R

S

F

F

C

A

I

V

I

I

T

T

D

D

T

K

S

K

R

T

K

N

V

I

K

K

M

Y

A

P

I

L

V

A

D

D

W

Y

R

E

V

L

T

T

P

P

G

D

I

V

A

A

L

I

D

V

D

D

P

P

L

Q

L

F

M

V

M

M

G

T

M

V

P

P

P

K

A

H

L

V

T

T

A

A

A

D

T

T

G

G

M

M

D
|
D

A

V

L

L

T

T

H
|
H

A

A

V

I

E

E

A

A

Y

Y

V

V

S

S

T

N

I

M

A

A

T

N

P

D

M

Y

T

T

D

D

S

G

A

L

A

A

E

M

K

K

A

A

I

I

E

Q

L

L

I

V

A

F

Q

E

H

Y

L

L

R

P

P

R

A

A

V

Y

A

Q

N

N

G

G

D

A

D

D

I

E

V

L

A

A

R

R

E

E

G

K

M

M

C

H

Y

N

A

A

Q

S

Y

T

L

I

A

A

G

G

M

M

A

A

F

F

N

A

N

N

A

A

S

F

L

L

G

G

H

I

V

N

H
|
H

A

S

M

L

A

A

H

H

Q

K

L

L

G

G

G

A

F

E

Y

F

D

H

L

I

P

P

H
|
H

G

G

E

R

C

A

N

N

A

T

I

I

L

L

L

M

P

P

H

H

V

V

S

I

R

R

F

Y

N

N

L

-

I

A

A

A

K

K

M

P

D

K

R

K

F

Y

I

F

K

K

I

A

A

D

E

Q

L

R

M

Y

G

A

E

E

-

I

-

A

N

R

V

M

D

L

G

G

L

L

A

P

P

A

R

R

-

T

-

E

D

E

A

G

A

V

E

E

L

S

A

L

L

V

E

Q

A

A

I

I

Q

I

K

K

L

L

S

A

A

K

D

Q

I

L

G

D

I

M

P

P

S

L

G

S

L

I

I

E

E

A

L

C

G

G

K

-

R

-

Y

V

G

S

K

K

E

Q

V

E

K

F

A

E

E

S

D

K

I

V

E

E

T

K

M

L

T

A

G

E

N

L

A

A

Q

F

K

E

D

D

A

Q

C

C

G

T

L

T

T

A

N

N

P

P

R

K

R

L

P

P

K

L

D

V

M

S

D

D

V

L

A

V

A

H

I

I

Y

Y

T

R

A

Q

A

A

L

F

binding zinc ion: D203 (= D198), H207 (= H202), H272 (= H267), H286 (= H281)

Q59104 4-hydroxybutyrate dehydrogenase; 4HbD; Gamma-hydroxybutyrate dehydrogenase; GHBDH; EC 1.1.1.61 from Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha) (see paper)
33% identity, 95% coverage: 10:384/393 of query aligns to 5:373/382 of Q59104

query
sites
Q59104

Y

Y

F

Y

I

L

P

T

S

H

V

I

T

H

L

L

I

-

G

D

I

F

G

G

A

A

A

V

K

S

E

L

I

L

P

K

A

S

K

E

I

C

K

E

D

R

L

I

G

G

G

I

S

R

K

R

P

P

L

L

I

L

V

V

T

T

D

D

K

K

G

G

I

V

T

V

A

A

G

G

I

V

T

A

K

Q

E

R

I

A

T

I

D

D

L

A

L

M

D

Q

G

G

A

L

E

Q

M

V

A

A

Y

-

V

-

V

V

Y

F

D

D

E

E

T

T

I

P

P

S

N

N

P

P

T

T

D

E

I

A

N

M

V

V

H

R

D

K

G

A

V

A

D

A

V

Q

Y

Y

K

R

E

E

N

A

N

G

C

C

D

D

S

G

L

L

I

V

T

A

L

V

G

G

S

S

H

I

D

D

C

L

G

A

K

K

G

G

I

I

G

A

L

I

V

L

V

A

A

T

N

H

G

E

G

G

K

E

I

L

H

T

D

T

F

Y

E

A

G

T

V

I

D

E

-

G

-

S

-

A

Q

R

S

I

T

T

K

D

P

K

M

A

P

A

P

P

Y

L

V

I

A

A

V

V

N

P

T

T

A

S

G

G

T

T

A

G

S

S

E

E

M

V

T

A

R

R

F

G

C

A

I

I

T

I

-

L

D

D

T

D

S

G

R

R

K

K

V

-

K

-

M

L

A

G

I

F

V

H

D

S

W

W

R

H

V

L

T

L

P

P

G

K

I

S

A

A

L

V

D

C

D

D

P

P

L

E

L

L

M

T

M

L

G

G

M

L

P

P

P

A

A

G

L

L

T

T

A

A

T

T

G

G

M

M

D
|
D

A

A

L

I

T

A

H
|
H

A

C

V

I

E

E

A

T

Y

F

V

L

S

A

T

P

I

A

A

F

T

N

P

P

M

P

T

A

D

D

S

G

A

I

A

A

E

L

K

D

A

G

I

L

E

E

L

R

I

G

A

W

Q

G

H

H

L

I

R

E

P

R

A

A

V

T

A

R

N

D

G

G

D

Q

D

D

I

R

V

D

A

A

R

R

E

L

G

N

M

M

C

M

Y

S

A

A

Q

S

Y

M

L

Q

A

G

G

A

M

M

A

A

F

F

N

Q

N

K

A

G

S

-

L

L

G

G

H

C

V

V

H
|
H

A

S

M

L

A

S

H
|
H

Q

P

L

L

G

G

F

L

Y

K

-

I

-

D

-

G

-

R

-

T

D

G

L

L

P

H

H
|
H

G

G

E

T

C

L

N

N

A

A

I

V

L

V

L

M

P

P

H

A

V

V

S

L

R

R

F

F

N

N

-

A

-

D

-

A

-

P

L

T

I

V

A

V

K

R

M

D

D

D

R

R

F

Y

I

A

K

R

I

L

A

R

E

R

L

A

M

M

G

H

E

L

N

P

V

-

D

-

G

-

L

-

A

-

P

-

R

-

D

D

A

G

A

A

E

D

L

I

A

A

L

-

E

Q

A

A

I

V

Q

H

K

D

L

M

S

T

A

V

D

R

I

L

G

G

I

L

P

P

S

T

G

G

L

L

I

R

E

Q

L

M

G

G

K

-

R

-

Y

-

G

-

K

-

E

-

V

V

K

T

A

E

E

D

D

M

I

F

E

D

T

K

M

V

T

I

G

A

N

G

A

A

Q

L

K

V

D

D

A

H

C

C

G

H

L

K

T

T

N

N

P

P

R

K

R

E

P

A

K

S

D

A

M

A

D

D

D193 (= D198) mutation to A: Retains very low activity.
H197 (= H202) mutation to A: Loss of activity.
H261 (= H267) mutation to A: Loss of activity.
H265 (= H271) mutation to A: 75% decrease in Vmax. Optimum pH is 9.5.; mutation to C: 95% decrease in Vmax. Optimum pH is 8.5.; mutation to D: Retains very low activity.; mutation to Y: Loss of activity.
H280 (= H281) mutation to A: Retains very low activity.

6scgA Structure of adhe form 1 (see paper)
34% identity, 88% coverage: 34:380/393 of query aligns to 29:386/406 of 6scgA

query
sites
6scgA

G

G

G

H

S

K

K

R

P

A

L

L

I

I

V

V

T

T

D
|
D

K

R

G
x
F

I

L

T

F

A

N

G

G

I

Y

T

A

K

D

E

Q

I

I

T

T

D

S

L

V

L

L

D

K

G

A

A

A

E

G

M

V

A

E

Y

T

V

E

V

V

Y

F

D

F

E

E

T

V

I

E

P
x
A

N
x
D

P

P

T

T

D

L

I

S

N

I

V

V

H

R

D

K

G

G

V

A

D

E

V

L

Y

A

K

N

E

S

N

F

N

K

C

P

D

D

S

V

L

I

I

I

T

A

L

L

G

G

G
|
G

S
|
S

S

P

H

M

D

D

C

A

G

A

K

K

G

-

I

I

G

M

L

W

V

V

V

M

A

Y

N

E

G

H

G

P

K

E

I

T

H

H

-

F

-

E

-

L

-

A

-

L

D

R

F

F

E

M

G

D

V

I

D

R

Q

K

S

R

T

I

K

Y

P

K

M

F

P

P

P

K

Y

M

-

G

-

V

-

K

-

A

-

K

-

M

V

I

A

A

V

V

N

T

T
|
T

A

S

G

G

T
|
T

A

G

S

S

E

E

M

V

T

T

R

P

F

F

C

A

I
x
V

I

V

T

T

D

D

T

D

S

A

R

T

K

G

V

Q

K

K

M

Y

A

P

I

L

V

A

D

D

W

Y

R

A

V

L

T

T

P

P

G

D

I

M

A

A

L

I

D

V

D

D

P

A

L

N

L

L

M

V

M

M

G

D

M

M

P

P

P

K

A

S

L
|
L

T

C

A

A

A

F

T

G

G

G

M

L

D
|
D

A

A

L

V

T

T

H
|
H

A

A

V

M

E

E

A

A

Y

Y

V

V

S

S

T

V

I

L

A

A

T

S

P

E

M

F

T

S

D

D

S

G

A

Q

A

A

E

L

K

Q

A

A

I

L

E

K

L

L

I

L

A

K

Q

E

H

Y

L

L

R

P

P

A

A

S

V

Y

A

H

N

E

G

G

D

S

-

K

D

N

I

P

V

V

A

A

R

R

E

E

G

R

M

V

C

H

Y

S

A

A

Q

A

Y

T

L

I

A

A

G

G

M

I

A

A

F

F

N

A

N

N

A

A

S

F

L

L

G

G

H

V

V

C

H
|
H

A

S

M

M

A

A

H
|
H

Q

K

L

L

G

G

G

S

F

Q

Y

F

D

H

L

I

P

P

H
|
H

G

G

E

L

C

A

N

N

A

A

I

L

L

L

L

I

P

C

H

N

V

V

S

I

R

R

F

Y

N

N

L

A

I

N

A

P

K

Q

-

A

M

R

D

R

R

R

F

Y

I

A

K

E

I

I

A

A

E

D

L

H

M

L

G

G

E

L

N

S

V

A

D

P

G

G

L

D

A

R

P

T

R

A

D

A

A

K

A

I

E

E

L

K

A

L

L

L

E

A

A

W

I

L

Q

E

K

T

L

L

S

K

A

A

D

E

I

L

G

G

I

I

P

P

S

K

G

S

L

I

I

R

E

E

L

A

G

G

K

V

R

Q

Y

E

G

A

K

D

E

F

V

L

K

A

A

-

E

-

D

N

I

V

E

D

T

K

M

L

T

S

G

E

N

D

A

A

Q

F

K

D

D

D

A

Q

C

C

G

T

L

G

T

A

N

N

P

P

R

R

R

Y

P

P

binding fe (iii) ion: D204 (= D198), H208 (= H202), H274 (= H267), H288 (= H281)
binding nicotinamide-adenine-dinucleotide: D38 (= D43), F40 (≠ G45), A69 (≠ P74), D70 (≠ N75), G96 (= G101), G97 (= G102), S98 (= S103), T148 (= T142), T149 (= T143), T152 (= T146), V161 (≠ I155), L197 (= L191), H278 (= H271)

7bvpA Adhe spirosome in extended conformation (see paper)
33% identity, 88% coverage: 34:380/393 of query aligns to 478:849/869 of 7bvpA

query
sites
7bvpA

G

G

G

H

S

K

K

R

P

A

L

L

I

I

V

V

T

T

D
|
D

K

R

G
x
F

I

L

T

F

A

N

G

G

I

Y

T

A

K

D

E

Q

I

I

T

T

D

S

L

V

L

L

D

K

G

A

A

A

E

G

M

V

A

E

Y

T

V

E

V

V

Y

F

D

F

E

E

T

V

I

E

P

A

N
x
D

P

P

T

T

D

L

I

S

N

I

V

V

H

R

D

K

G

G

V

A

D

E

V

L

Y

A

K

N

E

S

N

F

N

K

C

P

D

D

S

V

L

I

I

I

T

A

L

L

G

G

S
|
S

S

P

H

M

D
|
D

C

A

G

A

K

K

G

-

I

I

G

M

L

W

V

V

V

M

A

Y

N

E

G

H

G

P

K

E

I

T

H

H

-

F

-

E

-

L

-

A

-

L

D

R

F

F

E

M

G

D

V

I

D

R

Q

K

S

R

T

I

K

Y

P

K

M

F

P

P

P

K

Y

M

-

G

-

V

-

K

-

A

-

K

-

M

V

I

A

A

V

V

N

T

T
|
T

A

S

G

G

T
|
T

A

G

S

S

E

E

M

V

T

T

R

P

F

F

C

A

I
x
V

I

V

T

T

D

D

T

D

S

A

R

T

K

G

V

Q

K
|
K

M

Y

A

P

I

L

V

A

D

D

W

Y

R

A

V

L

T

T

P

P

G

D

I

M

A

A

L

I

D

V

D

D

P

A

L

N

L

L

M

V

M

M

G

D

M

M

P

P

P

K

A

S

L
|
L

T

C

A

A

A

F

T

G

G

G

M

L

D
|
D

A

A

L

V

T

T

H
|
H

A

A

V

M

E

E

A

A

Y

Y

V

V

S

S

T

V

I

L

A

A

T

S

P

E

M

F

T

S

D

D

S

G

A

Q

A

A

E

L

K

Q

A

A

I

L

E

K

L

L

I

L

A

K

Q

E

H

Y

L

L

R

P

P

A

A

S

V

Y

A

H

N

E

G

G

D

S

-

K

D

N

I

P

V

V

A

A

R

R

E

E

G

R

M

V

C

H

Y

S

A

A

Q

A

Y

T

L

I

A

A

G

G

M

I

A

A

F

F

N

A

N

N

A

A

S

F

L

L

G

G

H

V

V

C

H
|
H

A

S

M

M

A

A

H

H

Q

K

L

L

G

G

G

S

F

Q

Y

F

D

H

L

I

P

P

H
|
H

G

G

E

L

C

A

N

N

A

A

I

L

L

L

L

I

P

C

H

N

V

V

S

I

R

R

F

Y

N

N

-

A

-

N

-

D

-

N

-

P

-

T

-

K

-

Q

-

T

L

A

I

F

A

S

K

Q

M

Y

D

D

-

R

-

P

-

Q

-

A

-

R

R

R

F

Y

I

A

K

E

I

I

A

A

E

D

L

H

M

L

G

G

E

L

N

S

V

A

D

P

G

G

L

D

A

R

P

T

R

A

D

A

A

K

A

I

E

E

L

K

A

L

L

L

E

A

A

W

I

L

Q

E

K

T

L

L

S

K

A

A

D

E

I

L

G

G

I

I

P

P

S

K

G

S

L

I

I

R

E

E

L

A

G

G

K

V

R

Q

Y

E

G

A

K

D

E

F

V

L

K

A

A

-

E

-

D

N

I

V

E

D

T

K

M

L

T

S

G

E

N

D

A

A

Q

F

K

D

D

D

A

Q

C

C

G

T

L

G

T

A

N

N

P

P

R

R

R

Y

P

P

binding nicotinamide-adenine-dinucleotide: D487 (= D43), F489 (≠ G45), D519 (≠ N75), S547 (= S103), D550 (= D106), T597 (= T142), T598 (= T143), T601 (= T146), V610 (≠ I155), K619 (= K164), L646 (= L191), H737 (= H281)
binding zinc ion: D653 (= D198), H657 (= H202), H723 (= H267), H737 (= H281)

Sites not aligning to the query:

binding nicotinamide-adenine-dinucleotide: 112, 113, 139, 194, 195, 198, 212, 213, 214, 246, 335, 337, 367, 418, 419

6tqmA Escherichia coli adhe structure in its compact conformation (see paper)
33% identity, 88% coverage: 34:380/393 of query aligns to 478:849/869 of 6tqmA

query
sites
6tqmA

G

G

G

H

S

K

K

R

P

A

L

L

I

I

V

V

T

T

D
|
D

K

R

G

F

I
x
L

T

F

A

N

G

G

I

Y

T

A

K

D

E

Q

I

I

T

T

D

S

L

V

L

L

D

K

G

A

A

A

E

G

M

V

A

E

Y

T

V

E

V

V

Y

F

D

F

E

E

T

V

I

E

P

A

N

D

P

P

T

T

D

L

I

S

N

I

V

V

H

R

D

K

G

G

V

A

D

E

V

L

Y

A

K

N

E

S

N

F

N

K

C

P

D

D

S

V

L

I

I

I

T

A

L

L

G

G

G
|
G

G

G

S
|
S

S

P

H

M

D
|
D

C

A

G

A

K

K

G

-

I

I

G

M

L

W

V

V

V

M

A

Y

N

E

G

H

G

P

K

E

I

T

H

H

-

F

-

E

-

L

-

A

-

L

D

R

F

F

E

M

G

D

V

I

D

R

Q

K

S

R

T

I

K

Y

P

K

M

F

P

P

P

K

Y

M

-

G

-

V

-

K

-

A

-

K

-

M

V

I

A

A

V

V

N

T

T
|
T

T

T

A

S

G

G

T

T

A

G

S
|
S

E

E

M

V

T

T

R

P

F
|
F

C

A

I

V

T

T

D

D

T

D

S

A

R

T

K

G

V

Q

K

K

M

Y

A

P

I

L

V

A

D

D

W

Y

R

A

V

L

T

T

P

P

G

D

I

M

A

A

L

I

D

V

D

D

P

A

L

N

L

L

M

V

M

M

G

D

M

M

P

P

P

K

A

S

L
|
L

T

C

A

A

A

F

T

G

G

G

M

L

D
|
D

A

A

L

V

T

T

H
|
H

A

A

V

M

E

E

A

A

Y

Y

V

V

S

S

T

V

I

L

A

A

T

S

P

E

M

F

T

S

D

D

S

G

A

Q

A

A

E

L

K

Q

A

A

I

L

E

K

L

L

I

L

A

K

Q

E

H

Y

L

L

R

P

P

A

A

S

V

Y

A

H

N

E

G

G

D

S

-

K

D

N

I

P

V

V

A

A

R

R

E

E

G

R

M

V

C

H

Y

S

A

A

Q

A

Y

T

L

I

A

A

G

G

M

I

A

A

F

F

N

A

N

N

A

A

S

F

L

L

G

G

H

V

V

C

H
|
H

A

S

M

M

A

A

H
|
H

Q

K

L

L

G

G

G

S

F

Q

Y

F

D

H

L

I

P

P

H
|
H

G

G

E

L

C

A

N

N

A

A

I

L

L

L

L

I

P

C

H

N

V

V

S

I

R

R

F

Y

N

N

-

A

-

N

-

D

-

N

-

P

-

T

-

K

-

Q

-

T

L

A

I

F

A

S

K

Q

M

Y

D

D

-

R

-

P

-

Q

-

A

-

R

R

R

F

Y

I

A

K

E

I

I

A

A

E

D

L

H

M

L

G

G

E

L

N

S

V

A

D

P

G

G

L

D

A

R

P

T

R

A

D

A

A

K

A

I

E

E

L

K

A

L

L

L

E

A

A

W

I

L

Q

E

K

T

L

L

S

K

A

A

D

E

I

L

G

G

I

I

P

P

S

K

G

S

L

I

I

R

E

E

L

A

G

G

K

V

R

Q

Y

E

G

A

K

D

E

F

V

L

K

A

A

-

E

-

D

N

I

V

E

D

T

K

M

L

T

S

G

E

N

D

A

A

Q

F

K

D

D

D

A

Q

C

C

G

T

L

G

T

A

N

N

P

P

R

R

R

Y

P

P

binding fe (iii) ion: D653 (= D198), H657 (= H202), H723 (= H267), H737 (= H281)
binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: D487 (= D43), L490 (≠ I46), G545 (= G101), S547 (= S103), D550 (= D106), T597 (= T142), S603 (= S148), F608 (= F153), L646 (= L191), H727 (= H271)

P0A9Q7 Bifunctional aldehyde-alcohol dehydrogenase AdhE; Alcohol dehydrogenase E; EC 1.2.1.10; EC 1.1.1.1 from Escherichia coli (strain K12) (see 8 papers)
33% identity, 88% coverage: 34:380/393 of query aligns to 478:849/891 of P0A9Q7

query
sites
P0A9Q7

G

G

G

H

S

K

K

R

P

A

L

L

I

I

V

V

T

T

D
|
D

K

R

G

F

I

L

T

F

A

N

G

G

I

Y

T

A

K

D

E

Q

I

I

T

T

D

S

L

V

L

L

D

K

G

A

A

A

E

G

M

V

A

E

Y

T

V

E

V

V

Y

F

D

F

E

E

T

V

I

E

P

A

N
x
D

P

P

T

T

D

L

I

S

N

I

V

V

H

R

D

K

G

G

V

A

D

E

V

L

Y

A

K

N

E

S

N

F

N

K

C

P

D

D

S

V

L

I

I

I

T

A

L

L

G

G

G
|
G

S
|
S

S
x
P

H
x
M

D
|
D

C

A

G

A

K

K

G

-

I

I

G

M

L

W

V

V

V

M

A

Y

N

E

G

H

G

P

K

E

I

T

H

H

-

F

-

E

-
x
E

-

L

-

A

-

L

D

R

F

F

E

M

G

D

V

I

D

R

Q

K

S

R

T

I

K

Y

P

K

M

F

P

P

P

K

Y

M

-

G

-

V

-

K

-

A

-

K

-

M

V

I

A

A

V

V

N

T

T

T

A

S

G

G

T

T

A

G

S

S

E

E

M

V

T

T

R

P

F

F

C

A

I
x
V

I

V

T

T

D

D

T

D

S

A

R

T

K

G

V

Q

K
|
K

M

Y

A

P

I

L

V

A

D

D

W

Y

R

A

V

L

T

T

P

P

G

D

I

M

A

A

L

I

D

V

D

D

P

A

L

N

L

L

M

V

M

M

G

D

M

M

P

P

P

K

A

S

L

L

T

C

A

A

A

F

T

G

G

G

M

L

D
|
D

A

A

L

V

T

T

H
|
H

A

A

V

M

E

E

A

A

Y

Y

V

V

S

S

T

V

I

L

A

A

T

S

P

E

M
x
F

T

S

D

D

S

G

A

Q

A

A

E

L

K

Q

A

A

I

L

E

K

L

L

I

L

A

K

Q

E

H

Y

L

L

R

P

P

A

A

S

V

Y

A

H

N

E

G

G

D

S

-

K

D

N

I

P

V

V

A

A

R

R

E

E

G

R

M

V

C

H

Y

S

A

A

Q

A

Y

T

L

I

A

A

G

G

M

I

A

A

F

F

N

A

N

N

A

A

S

F

L

L

G

G

H

V

V

C

H
|
H

A

S

M

M

A

A

H

H

Q

K

L

L

G

G

G

S

F

Q

Y

F

D

H

L

I

P

P

H
|
H

G

G

E

L

C

A

N

N

A

A

I

L

L

L

L

I

P

C

H

N

V

V

S

I

R

R

F

Y

N

N

-

A

-

N

-

D

-

N

-

P

-

T

-

K

-

Q

-

T

L

A

I

F

A

S

K

Q

M

Y

D

D

-

R

-

P

-

Q

-

A

-

R

R

R

F

Y

I

A

K

E

I

I

A

A

E

D

L

H

M

L

G

G

E

L

N

S

V

A

D

P

G

G

L

D

A

R

P

T

R

A

D

A

A

K

A

I

E

E

L

K

A

L

L

L

E

A

A

W

I

L

Q

E

K

T

L

L

S

K

A

A

D

E

I

L

G

G

I

I

P

P

S

K

G

S

L

I

I

R

E

E

L

A

G

G

K

V

R

Q

Y

E

G

A

K

D

E

F

V

L

K

A

A

-

E

-

D

N

I

V

E

D

T

K

M

L

T

S

G

E

N

D

A

A

Q

F

K

D

D

D

A

Q

C

C

G

T

L

G

T

A

N

N

P

P

R

R

R

Y

P

P

D487 (= D43) binding NAD(+)
D519 (≠ N75) binding NAD(+)
GSPMD 546:550 (≠ GSSHD 102:106) binding NAD(+)
E568 (vs. gap) mutation to K: Partially restores protein stability and resistance to MCO damage; when associated with T-267.
V610 (≠ I155) binding NAD(+)
K619 (= K164) binding NAD(+)
D653 (= D198) binding Fe cation
H657 (= H202) binding Fe cation
F670 (≠ M215) mutation F->A,E,V: Disrupts spirosome formation. Affects the forward activity of ALDH.
H723 (= H267) binding Fe cation
H737 (= H281) binding Fe cation

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
110:115 binding NAD(+)
195 binding NAD(+)
213 binding NAD(+)
267 A→T: Shows aerobic growth ability on ethanol. Shows 5-6 fold increase in acetaldehyde dehydrogenase activity, but does not affect ethanol dehydrogenase activity. Shows decreased thermal enzyme stability and increased sensitivity to MCO damage. Shows increased protein stability and resistance to MCO; when associated with K-568.
335 binding NAD(+)
358 modified: N6-acetyllysine
419 binding NAD(+)
446:449 mutation Missing: Can form dimers, but does not assemble into long filaments. Strongly affects ALDH activity, but not ADH activity.

P0A9Q8 Bifunctional aldehyde-alcohol dehydrogenase AdhE; Alcohol dehydrogenase E; EC 1.2.1.10; EC 1.1.1.1 from Escherichia coli O157:H7 (see paper)
33% identity, 88% coverage: 34:380/393 of query aligns to 478:849/891 of P0A9Q8

query
sites
P0A9Q8

G

G

G

H

S

K

K

R

P

A

L

L

I

I

V

V

T

T

D
|
D

K

R

G

F

I

L

T

F

A

N

G

G

I

Y

T

A

K

D

E

Q

I

I

T

T

D

S

L

V

L

L

D

K

G

A

A

A

E

G

M

V

A

E

Y

T

V

E

V

V

Y

F

D

F

E

E

T

V

I

E

P

A

N
x
D

P

P

T

T

D

L

I

S

N

I

V

V

H

R

D

K

G

G

V

A

D

E

V

L

Y

A

K

N

E

S

N

F

N

K

C

P

D

D

S

V

L

I

I

I

T

A

L

L

G

G

G
|
G

S
|
S

S
x
P

H
x
M

D
|
D

C

A

G

A

K

K

G

-

I

I

G

M

L

W

V

V

V

M

A

Y

N

E

G

H

G

P

K

E

I

T

H

H

-

F

-

E

-

L

-

A

-

L

D

R

F

F

E

M

G

D

V

I

D

R

Q

K

S

R

T

I

K

Y

P

K

M

F

P

P

P

K

Y

M

-

G

-

V

-

K

-

A

-

K

-

M

V

I

A

A

V

V

N

T

T
|
T

A

S

G

G

T

T

A

G

S

S

E

E

M

V

T

T

R

P

F

F

C

A

I

V

T

T

D

D

T

D

S

A

R

T

K

G

V

Q

K

K

M

Y

A

P

I

L

V

A

D

D

W

Y

R

A

V

L

T

T

P

P

G

D

I

M

A

A

L

I

D

V

D

D

P

A

L

N

L
|
L

M

V

M

M

G

D

M

M

P

P

P

K

A

S

L

L

T

C

A

A

A

F

T

G

G

G

M

L

D
|
D

A

A

L

V

T

T

H
|
H

A

A

V

M

E

E

A

A

Y

Y

V

V

S

S

T

V

I

L

A

A

T

S

P

E

M

F

T

S

D

D

S

G

A

Q

A

A

E

L

K

Q

A

A

I

L

E

K

L

L

I

L

A

K

Q

E

H

Y

L

L

R

P

P

A

A

S

V

Y

A

H

N

E

G

G

D

S

-

K

D

N

I

P

V

V

A

A

R

R

E

E

G

R

M

V

C

H

Y

S

A

A

Q

A

Y

T

L

I

A

A

G

G

M

I

A

A

F

F

N

A

N

N

A

A

S

F

L

L

G

G

H

V

V

C

H
|
H

A

S

M

M

A

A

H

H

Q

K

L

L

G

G

G

S

F

Q

Y

F

D

H

L

I

P

P

H
|
H

G

G

E

L

C

A

N

N

A

A

I

L

L

L

L

I

P

C

H

N

V

V

S

I

R

R

F

Y

N

N

-

A

-

N

-

D

-

N

-

P

-

T

-

K

-

Q

-

T

L

A

I

F

A

S

K

Q

M

Y

D

D

-

R

-

P

-

Q

-

A

-

R

R

R

F

Y

I

A

K

E

I

I

A

A

E

D

L

H

M

L

G

G

E

L

N

S

V

A

D

P

G

G

L

D

A

R

P

T

R

A

D

A

A

K

A

I

E

E

L

K

A

L

L

L

E

A

A

W

I

L

Q

E

K

T

L

L

S

K

A

A

D

E

I

L

G

G

I

I

P

P

S

K

G

S

L

I

I

R

E

E

L

A

G

G

K

V

R

Q

Y

E

G

A

K

D

E

F

V

L

K

A

A

-

E

-

D

N

I

V

E

D

T

K

M

L

T

S

G

E

N

D

A

A

Q

F

K

D

D

D

A

Q

C

C

G

T

L

G

T

A

N

N

P

P

R

R

R

Y

P

P

D487 (= D43) binding NAD(+)
D519 (≠ N75) binding NAD(+)
GSPMD 546:550 (≠ GSSHD 102:106) binding NAD(+)
TT 597:598 (= TT 142:143) binding NAD(+)
L638 (= L183) binding NAD(+)
D653 (= D198) binding Fe cation
H657 (= H202) binding Fe cation
H723 (= H267) binding Fe cation
H737 (= H281) binding Fe cation

6jkpA Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense in complex with NAD+ (see paper)
32% identity, 87% coverage: 7:347/393 of query aligns to 3:334/376 of 6jkpA

query
sites
6jkpA

V

L

Y

W

G

D

Y

Y

F

A

I

Q

P

P

S

V

V

T

T

I

L

R

I

F

G

G

I

K

G

G

A

R

A

A

K

M

E

E

I

I

P

K

A

D

K

I

I

A

K

E

D

A

L

M

G

G

G

L

S

H

K

D

P

G

L

I

I

M

V

V

T

T

D

P

K

K

G

F

I
x
F

T

V

A

D

A

S

G

G

I

E

T

A

K

Q

E

R

I

L

T

I

D

D

L

A

L

S

D

D

G

G

A

A

E

-

M

-

A

V

Y

S

V

T

V

V

Y

F

D

T

E

D

T

F

I

S

P

P

N

N

P

P

T

D

D

V

I

T

N

E

V

V

H

D

D

A

G

C

V

A

D

E

V

I

Y

I

K

R

E

K

N

N

N

H

C

C

D

E

S

F

L

V

I

V

T

A

L

M

G

G

G
|
G

S

S

S

A

H

M

D
|
D

C

V

G

S

K

K

G

A

I

A

G

A

L

S

V

I

V

C

A

L

N

T

G

D

K

S

I

I

H

A

D

D

F

Y

E

H

G

G

V

-

D

-

Q

-

S

T

T

G

K

K

P

A

M

M

P

P

-

Q

-

K

-

H

-

L

P

P

Y

I

V

I

A

A

V

L

N

P

T
|
T

A

A

G

G

T
|
T

A

G

S
|
S

E

E

M

V

T
|
T

R

C

F

V

C

S

I

V

I

L

T

T

D

N

T

R

S

K

R

L

K

G

V

K

K

K

M

A

A

P

I

I

V

V

D

S

W

D

R

G

V

F

T

F

P

P

G

S

I

V

A

A

L

I

D

V

D

D

P

P

L

E

L

L

M

T

M

Y

G
x
S

M
x
V

P
|
P

P

P

A

K

L

I

T

T

A

A

A

S

T

T

G

G

M

M

D

D

A

V

L

L

T

S

H

Q

A

A

V

I

E

E

A

G

Y

F

V

W

S

S

T

K

I

G

A

H

T

Q

P

P

M

I

T

C

D

D

S

S

A

C

A

A

E

A

K

H

A

A

I

A

E

K

L

L

I

V

A

F

Q

K

H

Y

L

L

R

P

P

I

A

A

V

V

A

A

N

E

G

P

D

H

D

N

I

E

V

E

A

A

R

R

E

E

G

K

M

M

C

C

Y

E

A

A

Q

S

Y

V

L

I

A

A

G

G

M

L

A

A

F

F

N

T

N

L

A

P

S

K

L

T

G

T

H

S

V

S

H

H

A

A

M

C

A

S

H

F

Q

P

L

L

G

T

G

N

F

I

Y

H

D

G

L

I

P

P

H

H

G

G

E

E

C

A

N

C

A

G

I

L

L

T

L

L

P

D

H

Y

V

F

S

A

R

R

F

I

N

N

L

K

I

D

A

A

K

Q

M

H

D

G

R

R

F

V

I

Q

K

E

I

F

A

A

E

R

L

G

M

I

G

G

-

F

E

K

N

D

V

V

D

D

G

A

L

M

A

A

P

-

R

-

D

-

A

-

E

-

L

-

A

-

L

-

E

D

A

A

I

I

Q

H

K

D

L

L

S

K

A

V

D

R

I

I

G

G

I

M

P

R

S

T

G

G

L

L

I

K

E

D

L

L

binding nicotinamide-adenine-dinucleotide: F42 (≠ I46), G96 (= G102), D100 (= D106), T137 (= T142), T138 (= T143), T141 (= T146), S143 (= S148), T146 (= T151), S181 (≠ G186), V182 (≠ M187), P183 (= P188)

6jkoA Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense (see paper)
32% identity, 87% coverage: 7:347/393 of query aligns to 3:334/376 of 6jkoA

query
sites
6jkoA

V

L

Y

W

G

D

Y

Y

F

A

I

Q

P

P

S

V

V

T

T

I

L

R

I

F

G

G

I

K

G

G

A

R

A

A

K

M

E

E

I

I

P

K

A

D

K

I

I

A

K

E

D

A

L

M

G

G

G

L

S

H

K

D

P

G

L

I

I

M

V

V

T

T

D

P

K

K

G

F

I

F

T

V

A

D

A

S

G

G

I

E

T

A

K

Q

E

R

I

L

T

I

D

D

L

A

L

S

D

D

G

G

A

A

E

-

M

-

A

V

Y

S

V

T

V

V

Y

F

D

T

E

D

T

F

I

S

P

P

N

N

P

P

T

D

D

V

I

T

N

E

V

V

H

D

D

A

G

C

V

A

D

E

V

I

Y

I

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R

E

K

N

N

N

H

C

C

D

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F

L

V

I

V

T

A

L

M

G

G

S

S

S

A

H

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D

D

C

V

G

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K

K

G

A

I

A

G

A

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S

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I

V

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A

L

N

T

G

D

K

S

I

I

H

A

D

D

F

Y

E

H

G

G

V

-

D

-

Q

-

S

T

T

G

K

K

P

A

M

M

P

P

-

Q

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K

-

H

-

L

P

P

Y

I

V

I

A

A

V

L

N

P

T

T

A

A

G

G

T

T

A

G

S

S

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E

M

V

T

T

R

C

F

V

C

S

I

V

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L

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T

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N

T

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R

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A

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A

K

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I

T

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A

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S

T

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G

G

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M

D
|
D

A

V

L

L

T

S

H

Q

A

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I

E

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F

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I

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H

A

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A

E

K

L

L

I

V

A

F

Q

K

H

Y

L

L

R

P

P

I

A

A

V

V

A

A

N

E

G

P

D

H

D

N

I

E

V

E

A

A

R

R

E

E

G

K

M

M

C

C

Y

E

A

A

Q

S

Y

V

L

I

A

A

G

G

M

L

A

A

F

F

N

T

N

L

A

P

S

K

L

T

G

T

H

S

V

S

H
|
H

A

A

M

C

A

S

H

F

Q

P

L

L

G

T

G

N

F

I

Y

H

D

G

L

I

P

P

H
|
H

G

G

E

E

C

A

N

C

A

G

I

L

L

T

L

L

P

D

H

Y

V

F

S

A

R

R

F

I

N

N

L

K

I

D

A

A

K

Q

M

H

D

G

R

R

F

V

I

Q

K

E

I

F

A

A

E

R

L

G

M

I

G

G

-

F

E

K

N

D

V

V

D

D

G

A

L

M

A

A

P

-

R

-

D

-

A

-

E

-

L

-

A

-

L

-

E

D

A

A

I

I

Q

H

K

D

L

L

S

K

A

V

D

R

I

I

G

G

I

M

P

R

S

T

G

G

L

L

I

K

E

D

L

L

binding zinc ion: D193 (= D198), H262 (= H267), H276 (= H281)

Query Sequence

>WP_028584568.1 NCBI__GCF_000429965.1:WP_028584568.1
MAIREEVYGYFIPSVTLIGIGAAKEIPAKIKDLGGSKPLIVTDKGITAAGITKEITDLLD
GAEMAYVVYDETIPNPTDINVHDGVDVYKENNCDSLITLGGGSSHDCGKGIGLVVANGGK
IHDFEGVDQSTKPMPPYVAVNTTAGTASEMTRFCIITDTSRKVKMAIVDWRVTPGIALDD
PLLMMGMPPALTAATGMDALTHAVEAYVSTIATPMTDSAAEKAIELIAQHLRPAVANGDD
IVAREGMCYAQYLAGMAFNNASLGHVHAMAHQLGGFYDLPHGECNAILLPHVSRFNLIAK
MDRFIKIAELMGENVDGLAPRDAAELALEAIQKLSADIGIPSGLIELGKRYGKEVKAEDI
ETMTGNAQKDACGLTNPRRPKDMDVAAIYTAAL

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