SitesBLAST

Q56268 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans) (see paper)
62% identity, 99% coverage: 2:355/356 of query aligns to 3:354/358 of Q56268

query
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Q56268

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R95 (= R90) binding substrate
R105 (= R100) binding substrate
R133 (= R128) binding substrate
D222 (= D222) binding Mg(2+); binding substrate
D246 (= D246) binding Mg(2+)

P93832 3-isopropylmalate dehydrogenase 2, chloroplastic; 3-IPM-DH 2; AtIMDH2; AtIMDH3; IMDH 2; Beta-IPM dehydrogenase 2; Isopropylmalate dehydrogenase 2; AtIMD2; EC 1.1.1.85 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
56% identity, 99% coverage: 3:355/356 of query aligns to 45:397/405 of P93832

query
sites
P93832

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114:129 (vs. 68:83, 44% identical) binding NAD(+)
L132 (≠ I86) mutation to A: Reduced activity toward 3-isopropylmalate.
L133 (= L87) Confers substrate specificity; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.
R136 (= R90) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
R146 (= R100) binding substrate; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
R174 (= R128) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
Y181 (= Y135) Important for catalysis; mutation Y->A,F,H: Reduced activity toward 3-isopropylmalate.
K232 (= K190) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
N234 (= N192) binding NAD(+); mutation N->A,D: Loss of activity toward 3-isopropylmalate.
V235 (= V193) mutation to A: Reduced activity toward 3-isopropylmalate.
D264 (= D222) binding Mg(2+); binding substrate; mutation to N: Loss of activity toward 3-isopropylmalate.
N265 (= N223) binding NAD(+)
D288 (= D246) binding Mg(2+); mutation to N: Loss of activity toward 3-isopropylmalate.
D292 (= D250) binding Mg(2+); mutation to N: Reduced activity toward 3-isopropylmalate.
318:334 (vs. 276:292, 76% identical) binding NAD(+)

5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
56% identity, 99% coverage: 3:355/356 of query aligns to 5:357/360 of 5j33A

query
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5j33A

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active site: Y141 (= Y135), K192 (= K190), D224 (= D222), D248 (= D246), D252 (= D250)
binding magnesium ion: D248 (= D246), D252 (= D250)
binding nicotinamide-adenine-dinucleotide: I74 (≠ V68), E89 (= E83), L92 (≠ I86), I261 (= I259), E278 (= E276), H281 (= H279), G282 (= G280), S283 (= S281), A284 (= A282), I287 (= I285), N294 (= N292), D335 (= D333)

5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
56% identity, 99% coverage: 3:355/356 of query aligns to 15:367/369 of 5j32A

query
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5j32A

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A

S

S

S

T

L

L

K

K

R

R

E

E

L

V

V

A

S

E

G

G

L

V

D

D

I

L

L

M

I

V

R
|
R

E

E

L

L

T

T

G

G

D

G

I

I

Y
|
Y

F

F

G

G

Q

E

P

P

R

R

G

G

R

I

R

K

I

T

A

N

T

E

D

N

G

G

H

E

F

-

P

-

G

-

A

-

E

E

E

V

A

G

F

F

D

N

T

T

M

E

R

V

Y

Y

S

A

R

A

P

H

E

E

I

I

E

D

R

R

I

I

A

A

H

R

V

V

A

A

F

F

Q

E

A

T

A

A

R

R

K

K

R

R

G

R

K

G

R

K

V

L

T

C

S

S

V

V

D

D

K
|
K

A

A

N

N

V

V

L

L

E

E

T

A

F

S

Q

I

L

L

W

W

K

R

D

K

V

R

V

V

T

T

E

A

I

L

G

A

L

S

Q

E

Y

Y

P

P

D

D

V

V

A

E

L

L

D

S

H

H

M

M

Y

Y

V

V

D
|
D

N

N

A

A

M

M

Q

Q

L

L

V

V

R

R

A

D

P

P

K

K

K

Q

F

F

D

D

V

T

V

I

V

V

T

T

G

N

N

N

M

I

F

F

G

G

D
|
D

I

I

L

L

S

S

D
|
D

A

E

A

A

A

S

M

M

L

I

T

T

G

G

S

S

I

I

G

G

M

M

L

L

P

P

S

S

A

A

S

S

L

L

N

S

D

D

K

S

N

G

Q

P

G

G

L

L

Y

F

E

E

P

P

S

I

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

K

Q

G

D

V

K

A

A

N

N

P

P

L

L

A

A

T

T

I

I

L

L

S

S

A

A

M

M

M

L

L

L

R

K

F

Y

S

G

L

L

N

G

Q

E

P

E

E

K

A

A

A

K

R

R

I

I

E

E

Q

D

A

A

V

V

D

L

K

V

V

A

L

L

S

N

Q

N

G

G

L

F

R

R

T

T

P

G

D

D

I

I

Y

Y

S

S

D

A

G

G

T

T

T

K

R

L

I

V

G

G

T

C

V

K

E

E

M

M

G

G

D

E

A

E

V

V

V

L

K

K

A

S

L

V

active site: L18 (= L6), Y151 (= Y135), K202 (= K190), D234 (= D222), D258 (= D246), D262 (= D250)
binding 3-isopropylmalic acid: R106 (= R90), R144 (= R128), Y151 (= Y135), D258 (= D246)
binding magnesium ion: D258 (= D246), D262 (= D250)

Q9FMT1 3-isopropylmalate dehydrogenase 1, chloroplastic; 3-IPM-DH 1; AtIMDH1; IMDH 1; Beta-IPM dehydrogenase 1; Isopropylmalate dehydrogenase 1; AtIMD1; Methylthioalkylmalate dehydrogenase 1; EC 1.1.1.85 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
56% identity, 99% coverage: 3:355/356 of query aligns to 49:401/409 of Q9FMT1

query
sites
Q9FMT1

I

I

A

A

I

L

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

V

I

A

S

E

V

A

A

V

K

K

N

V

V

L

L

K

Q

-

K

-

A

-

G

-

S

V

L

L

E

D

G

L

L

N

E

F

F

E

D

T

F

E

K

T

E

A

M

L

P

V

V

G

G

A

A

F

L

E

D

A

L

Y

V

G

G

H

V

P

P

L

L

P

P

E

E

A

E

T

T

L

F

Q

T

L

A

A

A

K

K

D

L

A

S

D

D

A

A

V

I

L

L

F

L

G

G

A

A

V

I

G

G

D

G

W

Y

K

K

Y

W

D

D

T

K

L

N

D

E

R

K

P

H

L

L

R

R

P

P

E

E

Q

M

A

A

I

L

L
x
F

G

Y

L

L

R

R

K

R

N

D

L

L

G

K

L

V

F

F

A

A

N

N

F

L

R

R

P

P

A

A

I

T

C

V

Y

L

P

P

Q

Q

L

L

V

V

D

D

A

A

S

S

S

T

L

L

K

K

R

K

E

E

L

V

V

A

S

E

G

G

L

V

D

D

I

M

L

M

I

I

I

V

R

R

E

E

L

L

T

T

G

G

D

G

I

I

Y

Y

F

F

G

G

Q

E

P

P

R

R

G

G

R

I

R

T

I

I

A

N

T

E

D

N

G

G

H

E

F

-

P

-

G

-

A

-

E

E

E

V

A

G

F

V

D

S

T

T

M

E

R

I

Y

Y

S

A

R

A

P

H

E

E

I

I

E

D

R

R

I

I

A

A

H

R

V

V

A

A

F

F

Q

E

A

T

A

A

R

R

K

K

R

R

G

R

K

G

R

K

V

L

T
x
C

S

S

V

V

D

D

K

K

A

A

N

N

V

V

L

L

E

D

T

A

F

S

Q

I

L

L

W

W

K

R

D

K

V

R

V

V

T

T

E

A

I

L

G

A

L

S

Q

E

Y

Y

P

P

D

D

V

V

A

E

L

L

D

S

H

H

M

M

Y

Y

V

V

D

D

N

N

A

A

M

M

Q

Q

L

L

V

I

R

R

A

D

P

P

K

K

K

Q

F

F

D

D

V

T

V

I

V

V

T

T

G

N

N

N

M

I

F

F

G

G

D

D

I

I

L

L

S

S

D

D

A

E

A

A

A

S

M

M

L

I

T

T

G

G

S

S

I

I

G

G

M

M

L

L

P

P

S

S

A

A

S

S

L

L

N

G

D

E

K

S

N

G

Q

P

G

G

L

L

Y

F

E

E

P

P

S

I

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

K

Q

G

D

V

K

A

A

N

N

P

P

L

L

A

A

T

T

I

I

L

L

S

S

A

A

M

M

M

L

L

L

R

K

F

Y

S

G

L

L

N

G

Q

E

P

E

E

K

A

A

A

K

R

R

I

I

E

E

Q

D

A

A

V

V

D

V

K

D

V

A

L

L

S

N

Q

K

G

G

L

F

R

R

T

T

P

G

D

D

I

I

Y

Y

S

S

D

P

G

G

T

N

T

K

R

L

I

V

G

G

T
x
C

V

K

E

E

M

M

G

G

D

E

A

E

V

V

V

L

K

K

A

S

L

V

F137 (≠ L87) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
C232 (≠ T186) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
C390 (≠ T344) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.

Q9SA14 3-isopropylmalate dehydrogenase 3, chloroplastic; 3-IPM-DH 3; AtIMDH2; AtIMDH3; IMDH 3; Beta-IPM dehydrogenase 3; Isopropylmalate dehydrogenase 3; AtIMD3; EC 1.1.1.85 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
55% identity, 99% coverage: 2:355/356 of query aligns to 45:398/404 of Q9SA14

query
sites
Q9SA14

K

N

I

I

A

T

I

L

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

V

I

A

S

E

V

A

A

V

K

K

N

V

V

L

L

K

Q

-

K

-

A

-

G

-

F

V

L

L

Q

D

G

L

L

N

E

F

F

E

D

T

F

E

Q

T

E

A

M

L

P

V

F

G

G

A

A

F

L

E

D

A

L

Y

V

G

G

H

V

P

P

L

L

P

P

E

E

A

E

T

T

L

S

Q

T

L

A

A

A

K

K

D

Q

A

S

D

D

A

A

V

I

L

L

F

L

G

G

A

A

V

I

G

G

D

G

W

Y

K

K

Y

W

D

D

T

K

L

N

D

E

R

K

P

H

L

L

R

R

P

P

E

E

Q

M

A

G

I

L

L
|
L

G

N

L

I

R

R

K

R

N

D

L

L

G

N

L

V

F

F

A

A

N

N

F

L

R

R

P

P

A

A

I

T

C

V

Y

L

P

P

Q

Q

L

L

V

V

D

D

A

A

S

S

S

T

L

L

K

K

R

K

E

E

L

V

V

A

S

Q

G

G

L

V

D

D

I

M

L

M

I

I

I

V

R

R

E

E

L

L

T

T

G

G

D

G

I

I

Y

Y

F

F

G

G

Q

E

P

P

R

R

G

G

R

I

R

T

I

I

A

N

T

E

D

N

G

G

H

E

F

-

P

-

G

-

A

-

E

E

E

V

A

G

F

F

D

N

T

T

M

E

R

I

Y

Y

S

A

R

A

P

H

E

E

I

I

E

D

R

R

I

I

A

A

H

R

V

V

A

A

F

F

Q

E

A

T

A

A

R

R

K

K

R

R

G

R

K

G

R

K

V

L

T

C

S

S

V

V

D

D

K

K

A

A

N

N

V

V

L

L

E

D

T

A

F

S

Q

I

L

L

W

W

K

R

D

K

V

R

V

V

T

T

E

A

I

L

G

A

L

S

Q

E

Y

Y

P

P

D

D

V

V

A

E

L

L

D

S

H

H

M

M

Y

Y

V

V

D

D

N

N

A

A

M

M

Q

Q

L

L

V

V

R

R

A

D

P

P

K

K

K

Q

F

F

D

D

V

T

V

I

V

V

T

T

G

N

N

N

M

I

F

F

G

G

D

D

I

I

L

L

S

S

D

D

A

E

A

A

A

S

M

M

L

I

T

T

G

G

S

S

I

I

G

G

M

M

L

L

P

P

S

S

A

A

S

S

L

L

N

G

D

E

K

S

N

G

Q

P

G

G

L

L

Y

F

E

E

P

P

S

I

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

K

Q

G

D

V

K

A

A

N

N

P

P

L

L

A

A

T

T

I

I

L

L

S

S

A

A

M

M

M

L

L

L

R

K

F

Y

S

G

L

L

N

G

Q

E

P

E

E

K

A

A

A

K

R

M

I

I

E

E

Q

D

A

A

V

V

D

V

K

D

V

A

L

L

S

N

Q

K

G

G

L

F

R

R

T

T

P

G

D

D

I

I

Y

Y

S

S

D

P

G

G

T

N

T

K

R

L

I

V

G

G

T

C

V

K

E

E

M

M

G

G

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E

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L

K

K

A

S

L

V

L134 (= L87) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.

6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
54% identity, 99% coverage: 2:355/356 of query aligns to 5:358/358 of 6xxyA

query
sites
6xxyA

K

N

I

I

A

A

I

V

L

L

P

A

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

V

M

A

A

E

E

A

A

V

I

K

K

V

V

L

L

K

N

V

R

L

V

D

Q

-

E

-

K

-

F

-

G

-

F

-

K

L

L

N

N

F

F

E

N

T

E

E

-

T

-

A

F

L

F

V

V

G

G

A

A

F

I

E

E

A

H

Y

C

G

G

H

Y

P

P

L

L

P

P

E

A

A

E

T

T

L

L

Q

K

L

G

A

C

K

D

D

Q

A

A

D

D

A

A

V

I

L

L

F

F

G

G

A
x
S

V
|
V

G
|
G

D

G

W

P

K

K

Y

W

D

T

T

N

L

L

D

P

R

P

P

D

L

Q

R

Q

P

P

E
|
E

Q

R

-

G

A

A

I
x
L

L

L

G

P

L

L

R

R

K

K

N

H

L

F

G

K

L

L

F

F

A

C

N

N

F

L

R
|
R

P

P

A

A

I

T

C

L

Y

Y

P

K

Q

G

L

L

V

E

D

K

A

F

S

C

S

P

L

L

K

R

R

A

E

D

L

I

V

A

S

A

-

K

G

G

L

F

D

D

I

M

L

V

I

V

R
|
R

E

E

L

L

T

T

G

G

D

G

I

I

Y
|
Y

F

F

G

G

Q

Q

P

P

R

K

G

G

R

R

R

E

I

-

A

-

T

G

D

D

G

G

H

V

F

-

P

-

G

-

A

Q

E

T

E

K

A

A

F

F

D

D

T

T

M

E

R

V

Y

Y

S

Y

R

K

P

Y

E

E

I

I

E

E

R

R

I

I

A

A

H

R

V

A

A

A

F

F

Q

E

A

A

R

M

K

K

R

R

G

N

K

K

R

K

V

V

T

T

S

S

V

V

D

D

K
|
K

A

A

N

N

V
|
V

L

L

E

Q

T

S

F

S

Q

I

L

L

W

W

K

R

D

E

V

T

V

V

T

T

E

E

I

M

G

A

L

K

Q

D

Y

Y

P

P

D

E

V

V

A

T

L

L

D

E

H

H

M

I

Y
|
Y

V

I

D
|
D

N
|
N

A

A

A

T

M
|
M

Q

Q

L

L

V

I

R

K

A

S

P

P

K

E

K

S

F

F

D

D

V

V

V

L

T

C

G

S

N

N

M

I

F

F

G

G

D
|
D

I

I

L

I

S

S

D
|
D

A

E

A

A

M

M

L

I

T

T

G

G

S

S

I
x
M

G
|
G

M

M

L

L

P

P

S

S

A

A

S

S

L

L

N

N

D

E

K

E

N

G

Q

F

G

G

L

L

Y

Y

E
|
E

P

P

S

A

H
x
G

G
|
G

S
|
S

A
|
A

P
|
P

D
|
D

I
|
I

A

A

G

G

K

K

G

G

V

I

A

A

N
|
N

P

P

L

I

A

A

T

Q

I

I

L

L

S

S

A

A

M

M

L

L

R

R

F

Y

S

S

L

F

N

N

Q

L

P

N

E

E

A

A

A

D

R

A

I

I

E

E

Q

S

A

A

V

V

D

Q

K

K

V

V

L

L

S

A

Q

S

G

G

L

H

R

R

T

T

P

A

D
|
D

I

L

Y

-

S

A

D

D

G

D

T

S

T

T

R

P

I

V

G

S

T

T

V

A

E

E

M

M

G

G

D

T

A

L

V

I

V

T

K

Q

A

A

L

I

active site: Y144 (= Y135), K194 (= K190), D226 (= D222), D250 (= D246)
binding magnesium ion: D250 (= D246), D254 (= D250)
binding nicotinamide-adenine-dinucleotide: S74 (≠ A67), V75 (= V68), G76 (= G69), E90 (= E83), L94 (≠ I86), Y224 (= Y220), N227 (= N223), M230 (= M226), M263 (≠ I259), G264 (= G260), E280 (= E276), G283 (≠ H279), G284 (= G280), S285 (= S281), A286 (= A282), P287 (= P283), D288 (= D284), I289 (= I285), N296 (= N292), D337 (= D333)
binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E83), R108 (= R100), R137 (= R128), K194 (= K190), V197 (= V193), D226 (= D222), D250 (= D246)

1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
52% identity, 99% coverage: 3:353/356 of query aligns to 7:357/363 of 1cnzA

query
sites
1cnzA

I

I

A

A

I

V

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

V

M

A

A

E

Q

A

A

V

L

K

K

V

V

L

M

K

D

V

A

L

V

-

R

-

S

-

R

-

F

D

D

L

M

N

R

F

I

E

T

T

T

E

S

T

H

A

Y

L

D

V

V

G

G

A

I

A

A

F

I

E

D

A

N

Y

H

G

G

H

H

P

P

L

L

P

P

E

K

A

A

T

T

L

V

Q

E

L

G

A

C

K

E

D

Q

A

A

D

D

A

A

V

I

L

L

F

F

G

G

A

S

V

V

G

G

D

G

W

P

K

K

Y

W

D

E

T

N

L

L

D

P

R

P

P

E

L

S

R

Q

P

P

E

E

Q

R

-

G

A

A

I

L

L

L

G

P

L

L

R

R

K

K

N

H

L

F

G

K

L

L

F

F

A

S

N

N

F

L

R

R

P

P

A

A

I

K

C

L

Y

Y

P

Q

Q

G

L

L

V

E

D

A

A

F

S

C

S

P

L

L

K

R

R

A

E

D

L

I

V

A

-

A

S

N

G

G

L

F

D

D

I

I

L

L

I

C

I

V

R

R

E

E

L

L

T

T

G

G

D

G

I

I

Y
|
Y

F

F

G

G

Q

Q

P

P

R

K

G

G

R

R

R

E

I

-

A

-

T

G

D

S

G

G

H

Q

F

Y

P

-

G

-

A

-

E

E

E

K

A

A

F

F

D

D

T

T

M

E

R

V

Y

Y

S

H

R

R

P

F

E

E

I

I

E

E

R

R

I

I

A

A

H

R

V

I

A

A

F

F

Q

E

A

S

A

A

R

R

K

K

R

R

G

R

K

R

R

K

V

V

T

T

S

S

V

I

D

D

K
|
K

A

A

N

N

V

V

L

L

E

Q

T

S

F

S

Q

I

L

L

W

W

K

R

D

E

V

I

V

V

T

N

E

D

I

V

G

A

L

K

Q

T

Y

Y

P

P

D

D

V

V

A

E

L

L

D

A

H

H

M

M

Y

Y

V

I

D
|
D

N

N

A

A

A

T

M

M

Q

Q

L

L

V

I

R

K

A

D

P

P

K

S

K

Q

F

F

D

D

V

V

V

L

T

C

G

S

N

N

M

L

F

F

G

G

D
|
D

I

I

L

L

S

S

D
|
D

A

E

A

C

A

A

M

M

L

I

T

T

G

G

S

S

I

M

G

G

M

M

L

L

P

P

S

S

A

A

S

S

L

L

N

N

D

E

K

Q

N

G

Q

F

G

G

L

L

Y

Y

E

E

P

P

S

A

H

G

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

K

K

G

N

V

I

A

A

N

N

P

P

L

I

A

A

T

Q

I

I

L

L

S

S

A

L

A

A

M

L

L

L

R

R

F

Y

S

S

L

L

N

D

Q

A

P

N

E

D

A

A

A

T

R

A

I

I

E

E

Q

Q

A

A

V

I

D

N

K

R

V

A

L

L

S

E

Q

E

G

G

L

V

R

R

T

T

P

G

D

D

I

L

Y

-

S

A

D

R

G

G

T

A

R

A

I

V

G

S

T

T

V

D

E

E

M

M

G

G

D

D

A

I

V

I

V

A

K

R

active site: Y145 (= Y135), K195 (= K190), D227 (= D222), D251 (= D246)
binding manganese (ii) ion: D251 (= D246), D255 (= D250)

P37412 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
52% identity, 99% coverage: 3:353/356 of query aligns to 7:357/363 of P37412

query
sites
P37412

I

I

A

A

I

V

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

V

M

A

A

E

Q

A

A

V

L

K

K

V

V

L

M

K

D

V

A

L

V

-

R

-

S

-

R

-

F

D

D

L

M

N

R

F

I

E

T

T

T

E

S

T

H

A

Y

L

D

V

V

G

G

A

I

A

A

F

I

E

D

A

N

Y

H

G

G

H

H

P

P

L

L

P

P

E

K

A

A

T

T

L

V

Q

E

L

G

A

C

K

E

D

Q

A

A

D

D

A

A

V

I

L

L

F

F

G

G

A

S

V

V

G

G

D

G

W

P

K

K

Y

W

D

E

T

N

L

L

D

P

R

P

P

E

L

S

R

Q

P

P

E

E

Q

R

-

G

A

A

I

L

L

L

G

P

L

L

R

R

K

K

N

H

L

F

G

K

L

L

F

F

A

S

N

N

F

L

R

R

P

P

A

A

I

K

C

L

Y

Y

P

Q

Q

G

L

L

V

E

D

A

A

F

S

C

S

P

L

L

K

R

R

A

E

D

L

I

V

A

-

A

S

N

G

G

L

F

D

D

I

I

L

L

I

C

I

V

R

R

E

E

L

L

T

T

G

G

D

G

I

I

Y

Y

F

F

G

G

Q

Q

P

P

R

K

G

G

R

R

R

E

I

-

A

-

T

G

D

S

G

G

H

Q

F

Y

P

-

G

-

A

-

E

E

E

K

A

A

F

F

D

D

T

T

M

E

R

V

Y

Y

S

H

R

R

P

F

E

E

I

I

E

E

R

R

I

I

A

A

H

R

V

I

A

A

F

F

Q

E

A

S

A

A

R

R

K

K

R

R

G

R

K

R

R

K

V

V

T

T

S

S

V

I

D

D

K

K

A

A

N

N

V

V

L

L

E

Q

T

S

F

S

Q

I

L

L

W

W

K

R

D

E

V

I

V

V

T

N

E

D

I

V

G

A

L

K

Q

T

Y

Y

P

P

D

D

V

V

A

E

L

L

D

A

H

H

M

M

Y

Y

V

I

D
|
D

N

N

A

A

A

T

M

M

Q

Q

L

L

V

I

R

K

A

D

P

P

K

S

K

Q

F

F

D

D

V

V

V

L

T

C

G

S

N

N

M

L

F

F

G

G

D
|
D

I

I

L

L

S

S

D
|
D

A

E

A

C

A

A

M

M

L

I

T

T

G

G

S

S

I

M

G

G

M

M

L

L

P

P

S

S

A

A

S

S

L

L

N

N

D

E

K

Q

N

G

Q

F

G

G

L

L

Y

Y

E

E

P

P

S

A

H

G

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

K

K

G

N

V

I

A

A

N

N

P

P

L

I

A

A

T

Q

I

I

L

L

S

S

A

L

A

A

M

L

L

L

R

R

F

Y

S

S

L

L

N

D

Q

A

P

N

E

D

A

A

A

T

R

A

I

I

E

E

Q

Q

A

A

V

I

D

N

K

R

V

A

L

L

S

E

Q

E

G

G

L

V

R

R

T

T

P

G

D

D

I

L

Y

-

S

A

D

R

G

G

T

A

R

A

I

V

G

S

T

T

V

D

E

E

M

M

G

G

D

D

A

I

V

I

V

A

K

R

D227 (= D222) binding Mn(2+)
D251 (= D246) binding Mn(2+)
D255 (= D250) binding Mn(2+)

3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
54% identity, 99% coverage: 2:355/356 of query aligns to 4:360/364 of 3vkzA

query
sites
3vkzA

K

Q

I

I

A

A

I

V

L

L

P

A

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

V

M

A

A

E

E

A

A

V

R

K

K

V

V

L

L

K

K

V

A

L

V

D

E

-

A

-

R

-

F

-

G

L

L

N

N

F

I

E

E

T

Y

E

T

T

E

A

Y

L

D

V

V

G

G

A

I

A

A

F

I

E

D

A

N

Y

H

G

G

H

C

P

P

L

L

P

P

E

E

A

A

T

T

L

L

Q

K

L

G

A

C

K

E

D

A

A

A

D

D

A

A

V

I

L

L

F

F

G

G

A

S

V

V

G

G

D

G

W

P

K

K

Y

W

D

E

T

K

L

L

D

P

R

P

P

N

L

E

R

Q

P

P

E

E

Q

R

-

G

A

A

I

L

L

L

G

P

L

L

R
|
R

K

G

N

H

L

F

G

E

L

L

F

F

A

C

N

N

F

L

R

R

P

P

A

A

I

K

C

L

Y

H

P

D

Q

G

L

L

V

E

D

H

A

M

S

S

S

P

L

L

K

R

R

S

E

D

L

I

V

S

S

A

-

R

G

G

L

F

D

D

I

V

L

L

I

C

I

V

R
|
R

E

E

L

L

T

T

G

G

D

G

I

I

Y
|
Y

F

F

G

G

Q

K

P

P

R

K

G

G

R

R

R

Q

I

G

A

E

T

G

D

E

G

-

H

-

F

-

P

-

G

-

A

S

E

E

A

A

F

F

D

D

T

T

M

M

R

R

Y

Y

S

S

R

R

P

R

E

E

I

I

E

S

R

R

I

I

A

A

H

R

V

I

A

A

F

F

Q

E

A

A

R

R

K

G

R

R

G

R

K

K

R

K

V

V

T

T

S

S

V

V

D

D

K
|
K

A

A

N

N

V

V

L

L

E

A

T

C

F

S

Q

V

L

L

W

W

K

R

D

Q

V

V

T

E

E

E

I

V

G

A

L

V

Q

D

Y

F

P

P

D

D

V

V

A

E

L

L

D

E

H

H

M

I

Y

Y

V

I

D
|
D

N

N

A

A

A

T

M

M

Q

Q

L

L

V

L

R

R

A

R

P

P

K

D

K

E

F

F

D

D

V

V

V

M

V

L

T

C

G

S

N

N

M

L

F

F

G

G

D
|
D

I

I

L

L

S

S

D
|
D

A

E

A

I

A

A

M

M

L

L

T

T

G

G

S

S

I

M

G

G

M

L

L

L

P

S

S

S

A

A

S

S

L

M

N

N

D

S

K

T

N

G

Q

F

G

G

L

L

Y

F

E

E

P

P

S

A

H

G

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

K

K

G

G

V

I

A

A

N

N

P

P

L

I

A

A

T

Q

I

I

L

L

S

S

A

A

M

L

M

M

L

L

R

R

F

H

S

S

L

L

N

K

Q

Q

P

E

E

E

A

A

A

S

R

A

I

I

E

E

Q

R

A

A

V

V

D

T

K

K

V

A

L

L

S

N

Q

S

G

G

L

Y

R

L

T

T

P

G

D

E

I

L

Y

L

S

S

D

S

G

D

T

Q

T

R

R

H

I

K

G

A

-

K

-

T

T

T

V

V

E

Q

M

M

G

G

D

D

A

F

V

I

V

A

K

D

A

A

L

V

active site: Y143 (= Y135), K193 (= K190), D225 (= D222), D249 (= D246), D253 (= D250)
binding calcium ion: D249 (= D246), D253 (= D250)
binding 3-isopropylmalic acid: R97 (= R90), R136 (= R128), Y143 (= Y135), D249 (= D246)

2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
56% identity, 93% coverage: 1:332/356 of query aligns to 2:324/346 of 2y41A

query
sites
2y41A

M

M

K

K

I

V

A

A

I

V

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

V

T

A

E

E

A

A

A

V

L

K

K

V

V

L

L

K

R

V

A

L

L

D

D

-

E

-

A

-

E

-

G

L

L

N

G

F

L

E

A

T

Y

E

E

T

V

A

F

L

P

V

F

G

G

A

A

F

I

E

D

A

A

Y

F

G

G

H

E

P

P

L

F

P

P

E

E

A

P

T

T

L

R

Q

K

L

G

A

V

K

E

D

E

A

A

D

E

A

A

V

V

L

L

F

L

G

G

A

S

V

V

G

G

D

G

W

P

K

K

Y

W

D

D

T

G

L

L

D

P

R

R

P

K

L

I

R

R

P

P

E

E

Q

T

A

G

I

L

L

L

G

S

L

L

R
|
R

K

K

N

S

L

Q

G

D

L

L

F

F

A

A

N

N

F

L

R
|
R

P

P

A

A

I

K

C

V

Y

F

P

P

Q

G

L

L

V

E

D

R

A

L

S

S

S

P

L

L

K

K

R

E

E

E

L

I

V

A

S

R

G

G

L

V

D

D

I

V

L

L

I

I

I

V

R
|
R

E

E

L

L

T

T

G

G

D

G

I

I

Y
|
Y

F

F

G

G

Q

E

P

P

R

R

G

G

R

M

R

S

I

E

A

A

T

-

D

-

G

-

H

-

F

-

P

-

G

-

A

-

E

-

E

E

A

A

F

W

D

N

T

T

M

E

R

R

Y

Y

S

S

R

K

P

P

E

E

I

V

E

E

R

R

I

V

A

A

H

R

V

V

A

A

F

F

Q

E

A

A

R

R

K

K

R

R

G

R

K

K

R

H

V

V

T

V

S

S

V

V

D

D

K
|
K

A

A

N

N

V

V

L

L

E

E

T

V

F

G

Q

E

L

F

W

W

K

R

D

K

V

T

V

V

T

E

E

E

I

V

G

G

L

R

Q

G

Y

Y

P

P

D

D

V

V

A

A

L

L

D

E

H

H

M

Q

Y

Y

V

V

D
|
D

N

A

A

M

A

A

M

M

Q

H

L

L

V

V

R

R

A

S

P

P

K

A

K

R

F

F

D

D

V

V

T

T

G

G

N

N

M

I

F

F

G

G

D
|
D

I

I

L

L

S

S

D
|
D

A

L

A

A

A

S

M

V

L

L

T

P

G

G

S

S

I

L

G

G

M

L

L

L

P

P

S

S

A

A

S

S

L

L

N

G

D

-

K

R

N

G

Q

T

G

P

L

V

Y

F

E

E

P

P

S

V

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

K

K

G

G

V

I

A

A

N

N

P

P

L

T

A

A

T

A

I

I

L

L

S

S

A

A

M

M

L

L

R

E

F

H

S

A

L

F

N

G

Q

L

P

V

E

E

A

L

A

A

A

R

R

K

I

V

E

E

Q

D

A

A

V

V

D

A

K

K

V

A

L

L

S

-

Q

-

G

-

L

L

R

E

T

T

P

P

active site: Y140 (= Y135), K186 (= K190), D218 (= D222), D242 (= D246), D246 (= D250)
binding 3-isopropylmalic acid: R95 (= R90), R105 (= R100), R133 (= R128), Y140 (= Y135), D242 (= D246)

2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
56% identity, 93% coverage: 1:332/356 of query aligns to 1:323/345 of 2ztwA

query
sites
2ztwA

M

M

K

K

I

V

A

A

I

V

L

L

P

P

G

G

D

D

G

G

I
|
I

G

G

P

P

E

E

I

V

V

T

A

E

E

A

A

A

V

L

K

K

V

V

L

L

K

R

V

A

L

L

D

D

-

E

-

A

-

E

-

G

L

L

N

G

F

L

E

A

T

Y

E

E

T

V

A

F

L

P

V

F

G

G

A

A

F

I

E

D

A

A

Y

F

G

G

H

E

P

P

L

F

P

P

E

E

A

P

T

T

L

R

Q

K

L

G

A

V

K

E

D

E

A

A

D

E

A

A

V

V

L

L

F

L

G

G

A

S

V

V

G

G

D

G

W

P

K

K

Y

W

D

D

T

G

L

L

D

P

R

R

P

K

L

I

R

R

P

P

E

E

Q

T

A

G

I

L

L

L

G

S

L

L

R

R

K

K

N

S

L

Q

G

D

L

L

F

F

A

A

N

N

F

L

R

R

P

P

A

A

I

K

C

V

Y

F

P

P

Q

G

L

L

V

E

D

R

A

L

S

S

S

P

L

L

K

K

R

E

E

E

L

I

V

A

S

R

G

G

L

V

D

D

I

V

L

L

I

I

I

V

R

R

E

E

L

L

T

T

G

G

D

G

I

I

Y
|
Y

F

F

G

G

Q

E

P

P

R

R

G

G

R

M

R

S

I

E

A

A

T

-

D

-

G

-

H

-

F

-

P

-

G

-

A

-

E

-

E

E

A

A

F

W

D

N

T

T

M

E

R

R

Y

Y

S

S

R

K

P

P

E

E

I

V

E

E

R

R

I

V

A

A

H

R

V

V

A

A

F

F

Q

E

A

A

R

R

K

K

R

R

G

R

K

K

R

H

V

V

T

V

S

S

V

V

D

D

K
|
K

A

A

N

N

V

V

L

L

E

E

T

V

F

G

Q

E

L

F

W

W

K

R

D

K

V

T

V

V

T

E

E

E

I

V

G
|
G

L

R

Q

G

Y
|
Y

P

P

D

D

V
|
V

A

A

L

L

D

E

H

H

M

Q

Y

Y

V

V

D
|
D

N

A

A

M

A

A

M

M

Q

H

L

L

V

V

R

R

A

S

P

P

K

A

K

R

F

F

D

D

V

V

T

T

G

G

N

N

M

I

F

F

G

G

D
|
D

I

I

L

L

S

S

D
|
D

A

L

A

A

A

S

M

V

L

L

T

P

G

G

S

S

I

L

G

G

M

L

L

L

P

P

S

S

A

A

S

S

L

L

N

G

D

-

K

R

N

G

Q

T

G

P

L

V

Y

F

E

E

P

P

S

V

H
|
H

G
|
G

S

S

A
|
A

P

P

D
|
D

I
|
I

A

A

G

G

K

K

G

G

V

I

A
|
A

N
|
N

P

P

L

T

A

A

T

A

I

I

L

L

S

S

A

A

M

M

L

L

R

E

F

H

S

A

L

F

N

G

Q

L

P

V

E

E

A

L

A

A

A

R

R

K

I

V

E

E

Q

D

A

A

V

V

D

A

K

K

V

A

L

L

S

-

Q

-

G

-

L

L

R

E

T

T

P

P

active site: Y139 (= Y135), K185 (= K190), D217 (= D222), D241 (= D246), D245 (= D250)
binding magnesium ion: G203 (= G208), Y206 (= Y211), V209 (= V214)
binding nicotinamide-adenine-dinucleotide: I11 (= I11), H273 (= H279), G274 (= G280), A276 (= A282), D278 (= D284), I279 (= I285), A285 (= A291), N286 (= N292)

Q5SIY4 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see 2 papers)
56% identity, 93% coverage: 1:332/356 of query aligns to 1:323/345 of Q5SIY4

query
sites
Q5SIY4

M

M

K

K

I

V

A

A

I

V

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

V

T

A

E

E

A

A

A

V

L

K

K

V

V

L

L

K

R

V

A

L

L

D

D

-

E

-

A

-

E

-

G

L

L

N

G

F

L

E

A

T

Y

E

E

T

V

A

F

L

P

V

F

G

G

A

A

F

I

E

D

A

A

Y

F

G

G

H

E

P

P

L

F

P

P

E

E

A

P

T

T

L

R

Q

K

L

G

A

V

K

E

D

E

A

A

D

E

A

A

V

V

L

L

F

L

G

G

A

S

V

V

G

G

D
x
G

W
x
P

K
|
K

Y
x
W

D
|
D

T
x
G

L
|
L

D
x
P

R
|
R

P
x
K

L
x
I

R
|
R

P
|
P

E
|
E

Q

T

A

G

I

L

L

L

G

S

L

L

R

R

K

K

N

S

L

Q

G

D

L

L

F

F

A

A

N

N

F

L

R

R

P

P

A

A

I

K

C

V

Y

F

P

P

Q

G

L

L

V

E

D

R

A

L

S

S

S

P

L

L

K

K

R

E

E

E

L

I

V

A

S

R

G

G

L

V

D

D

I

V

L

L

I

I

I

V

R

R

E

E

L

L

T

T

G

G

D

G

I

I

Y
|
Y

F

F

G

G

Q

E

P

P

R

R

G

G

R

M

R

S

I

E

A

A

T

-

D

-

G

-

H

-

F

-

P

-

G

-

A

-

E

-

E

E

A

A

F

W

D

N

T

T

M

E

R

R

Y

Y

S

S

R

K

P

P

E

E

I

V

E

E

R

R

I

V

A

A

H

R

V

V

A

A

F

F

Q

E

A

A

R

R

K

K

R

R

G

R

K

K

R

H

V

V

T

V

S

S

V

V

D

D

K

K

A

A

N

N

V

V

L

L

E

E

T

V

F

G

Q

E

L

F

W

W

K

R

D

K

V

T

V

V

T

E

E

E

I

V

G

G

L

R

Q

G

Y

Y

P

P

D

D

V

V

A

A

L

L

D

E

H

H

M

Q

Y

Y

V

V

D

D

N

A

A

M

A

A

M

M

Q

H

L

L

V

V

R

R

A

S

P

P

K

A

K

R

F

F

D

D

V

V

T

T

G

G

N

N

M

I

F

F

G

G

D

D

I

I

L

L

S

S

D

D

A

L

A

A

A

S

M

V

L

L

T

P

G

G

S

S

I

L

G

G

M

L

L

L

P

P

S

S

A

A

S

S

L

L

N

G

D

-

K

R

N

G

Q

T

G

P

L

V

Y

F

E

E

P

P

S

V

H

H

G
|
G

S
|
S

A
|
A

P
|
P

D
|
D

I
|
I

A
|
A

G
|
G

K
|
K

G
|
G

V
x
I

A
|
A

N
|
N

P

P

L

T

A

A

T

A

I

I

L

L

S

S

A

A

M

M

L

L

R

E

F

H

S

A

L

F

N

G

Q

L

P

V

E

E

A

L

A

A

A

R

R

K

I

V

E

E

Q

D

A

A

V

V

D

A

K

K

V

A

L

L

S

-

Q

-

G

-

L

L

R

E

T

T

P

P

74:87 (vs. 70:83, 50% identical) binding NAD(+)
Y139 (= Y135) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
274:286 (vs. 280:292, 92% identical) binding NAD(+)

2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
56% identity, 93% coverage: 1:332/356 of query aligns to 2:324/355 of 2y42D

query
sites
2y42D

M

M

K

K

I

V

A

A

I

V

L

L

P

P

G

G

D

D

G

G

I
|
I

G

G

P

P

E

E

I

V

V

T

A

E

E

A

A

A

V

L

K

K

V

V

L

L

K

R

V

A

L

L

D

D

-

E

-

A

-

E

-

G

L

L

N

G

F

L

E

A

T

Y

E

E

T

V

A

F

L

P

V

F

G

G

A

A

F

I

E

D

A

A

Y

F

G

G

H

E

P

P

L

F

P

P

E

E

A

P

T

T

L

R

Q

K

L

G

A

V

K

E

D

E

A

A

D

E

A

A

V

V

L

L

F

L

G

G

A

S

V

V

G

G

D

G

W

P

K

K

Y

W

D
|
D

T

G

L

L

D

P

R

R

P

K

L

I

R

R

P

P

E

E

Q

T

A

G

I

L

L

L

G

S

L

L

R

R

K

K

N

S

L

Q

G

D

L

L

F

F

A

A

N

N

F

L

R

R

P

P

A

A

I

K

C

V

Y

F

P

P

Q

G

L

L

V

E

D

R

A

L

S

S

S

P

L

L

K

K

R

E

E

E

L

I

V

A

S

R

G

G

L

V

D

D

I

V

L

L

I

I

I

V

R

R

E

E

L

L

T

T

G

G

D

G

I

I

Y
|
Y

F

F

G

G

Q

E

P

P

R

R

G

G

R

M

R

S

I

E

A

A

T

-

D

-

G

-

H

-

F

-

P

-

G

-

A

-

E

-

E

E

A

A

F

W

D

N

T

T

M

E

R

R

Y

Y

S

S

R

K

P

P

E

E

I

V

E

E

R

R

I

V

A

A

H

R

V

V

A

A

F

F

Q

E

A

A

R

R

K

K

R

R

G

R

K

K

R

H

V

V

T

V

S

S

V

V

D

D

K
|
K

A

A

N

N

V

V

L

L

E

E

T

V

F

G

Q

E

L

F

W

W

K

R

D

K

V

T

V

V

T

E

E

E

I

V

G

G

L

R

Q

G

Y

Y

P

P

D

D

V

V

A

A

L

L

D

E

H

H

M

Q

Y

Y

V

V

D
|
D

N

A

A

M

A

A

M

M

Q

H

L

L

V

V

R

R

A

S

P

P

K

A

K

R

F

F

D

D

V

V

T

T

G

G

N

N

M

I

F

F

G

G

D
|
D

I

I

L

L

S

S

D
|
D

A

L

A

A

A

S

M

V

L

L

T

P

G

G

S

S

I

L

G

G

M

L

L

L

P

P

S

S

A

A

S

S

L

L

N

G

D

-

K

R

N

G

Q

T

G

P

L

V

Y

F

E

E

P

P

S

V

H
|
H

G
|
G

S

S

A
|
A

P

P

D
|
D

I
|
I

A

A

G

G

K

K

G

G

V

I

A

A

N
|
N

P

P

L

T

A

A

T

A

I

I

L

L

S

S

A

A

M

M

L

L

R

E

F

H

S

A

L

F

N

G

Q

L

P

V

E

E

A

L

A

A

A

R

R

K

I

V

E

E

Q

D

A

A

V

V

D

A

K

K

V

A

L

L

S

-

Q

-

G

-

L

L

R

E

T

T

P

P

active site: Y140 (= Y135), K186 (= K190), D218 (= D222), D242 (= D246), D246 (= D250)
binding manganese (ii) ion: D242 (= D246), D246 (= D250)
binding nicotinamide-adenine-dinucleotide: I12 (= I11), D79 (= D74), H274 (= H279), G275 (= G280), A277 (= A282), D279 (= D284), I280 (= I285), N287 (= N292)

3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
53% identity, 99% coverage: 2:355/356 of query aligns to 10:366/369 of 3vmkA

query
sites
3vmkA

K

Q

I

I

A

A

I

V

L

L

P

A

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

V

M

A

A

E

E

A

A

V

R

K

K

V

V

L

L

-

A

-

V

-

E

K

K

V

R

L

F

D

D

L

L

N

S

F

I

E

E

T

Y

E

S

T

E

A

Y

L

D

V

V

G

G

A

A

F

I

E

D

A

N

Y

H

G

G

H

C

P

P

L

L

P

P

E

E

A

A

T

T

L

L

Q

K

L

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A

C

K

E

D

A

A

A

D

D

A

A

V

V

L

L

F

F

G

G

A

S

V

V

G

G

D

G

W

P

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K

Y

W

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E

T

H

L

L

D

P

R

P

P

N

L

D

R

Q

P

P

E

E

Q

R

-

G

A

A

I

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L

L

G

P

L

L

R
|
R

K

G

N

H

L

F

G

E

L

L

F

F

A

C

N

N

F

M

R

R

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A

A

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H

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P

Q

G

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L

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E

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A

M

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S

P

L

L

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R

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E

D

L

I

V

S

S

E

-

K

G

G

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F

D

D

I

I

L

L

I

C

I

V

R
|
R

E

E

L

L

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T

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G

D

G

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I

Y
|
Y

F

F

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G

Q

K

P

P

R

K

G

G

R

R

R

Q

I

G

A

E

T

G

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E

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N

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-

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-

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-

G

-

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-

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E

A

A

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M

M

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Y

Y

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E

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A

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A

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F

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E

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R

G

R

K

K

R

K

V

V

T

T

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S

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D

K
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K

A

A

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N

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V

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L

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W

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D

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V

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E

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D

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N

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Q

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D

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S

I

M

G

G

M

L

L

L

P

A

S

S

A

I

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N

D

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Q

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G

G

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Y

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E

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A

A

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P

D

D

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I

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A

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Q

G

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I

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A

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N

P

P

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A

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S

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M

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L

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K

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L

P

E

E

D

A

A

A

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A

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I

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E

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A

A

A

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V

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S

K

K

V

A

L

L

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S

Q

D

G

G

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T

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C

D

E

I

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Y

L

-

P

-

A

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S

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R

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S

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Q

R

A

I

K

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T

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A

Y

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L

I

active site: Y149 (= Y135), K199 (= K190), D231 (= D222), D255 (= D246), D259 (= D250)
binding 3-isopropylmalic acid: R103 (= R90), R142 (= R128), Y149 (= Y135), K199 (= K190), N201 (= N192), D255 (= D246)

P18869 3-isopropylmalate dehydrogenase; 3-IPM-DH; IMDH; Beta-IPM dehydrogenase; EC 1.1.1.85 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
45% identity, 95% coverage: 2:340/356 of query aligns to 5:356/371 of P18869

query
sites
P18869

K

K

I

I

A

V

I

V

L

L

P

P

G

G

D

D

G

H

I

I

G

G

P

P

E

E

I

I

V

V

A

A

E

S

A

A

V

L

K

E

V

V

L

L

K

K

V

V

L

V

D

E

-

K

-

R

-

P

-

E

L

L

N

K

F

L

E

E

T

F

E

E

T

E

A

H

L

K

V

I

G

G

A

A

A

S

F

I

E

D

A

A

Y

Y

G

G

H
x
T

P

P

L

L

P

T

E

D

A

E

T

T

L

V

Q

K

L

A

A

C

K

L

D

E

A

A

D

D

A

G

V

V

L

L

F

L

G

G

A

A

V

V

G

G

D

G

W

P

K

E

Y

W

D

T

T

N

L

P

D

N

R

-

P

-

L

C

R

R

P

P

E

E

Q

Q

A

G

I

L

L

L

G

K

L

L

R

R

K

K

N

S

L

M

G

G

L

V

F

W

A

A

N

N

F

L

R

R

P

P

A

C

-

N

I

F

C

A

Y

S

P

K

Q

S

L

L

V

V

D

K

A

Y

S

S

S

P

L

L

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K

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P

E

E

L

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V

S

E

G

G

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D

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I

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R

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E

L

L

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T

G

G

D

G

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C

Y

Y

F

F

G

G

Q

E

P

-

R

-

G

-

R

-

R

R

I

T

A

E

T

D

D

N

G

G

H

-

F

-

P

-

G

-

A

S

E

G

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Y

A

A

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M

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D

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M

W

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Y

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E

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R

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I

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H

R

V

L

A

A

F

A

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W

A

L

A

A

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K

T

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G

N

-

P

K

A

R

P

V

V

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T

S

L

V

L

D

D

K

K

A

A

N

N

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V

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L

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S

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R

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L

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W

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R

D

K

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T

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I

-

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E

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D

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M

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L

L

L

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V

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K

A

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P

K

R

K

T

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N

-

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N

M

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F

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D

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D

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A

A

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S

I

L

G

G

M

L

L

L

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P

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S

A

A

S

S

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L

N

S

-

G

-

V

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G

-

K

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D

E

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V

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Y

V

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H

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G

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S

A

A

P

P

D

D

I

I

A

A

G

G

K

K

G

G

V

I

A

V

N

N

P

P

L

V

A

G

T

T

I

I

L

L

S

S

A

A

A

S

M

L

L

L

R

R

F

Y

S

G

L

L

N

N

Q

A

P

P

E

K

A

E

A

A

A

E

R

A

I

I

E

E

Q

A

A

A

V

V

D

R

K

K

V

V

L

L

-

D

-

T

-

S

-

I

-

G

S

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L

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Y

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G

D

E

G

A

T

S

T

T

T55 (≠ H47) modified: Phosphothreonine

Q72IW9 Isocitrate/homoisocitrate dehydrogenase; Homoisocitrate dehydrogenase; HICDH; EC 1.1.1.286 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see 4 papers)
41% identity, 99% coverage: 2:355/356 of query aligns to 4:331/334 of Q72IW9

query
sites
Q72IW9

K

R

I

I

A

C

I

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L

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E

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G

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D

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V

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A

A

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K

R

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L

K

E

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A

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L

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T

E

A

A

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V

A

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G

G

W

A

E

A

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F

E

E

A

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Y

R

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G

H

T

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S

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P

P

E

E

A

E

T

T

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Q
x
E

L

K

A

I

K

L

D

S

A

C

D

H

A

A

V

T

L

L

F

F

G

G

A

A

V
x
A

G
x
T

D
x
S

W

-

K

-

Y

-

D

-

T

-

L

-

D

-

R

-

P

P

L

T

R

R

P

K

E

V

Q

P

A

G

I

F

L

F

G

G

-

A

-

I

-
x
R

-
x
Y

L

L

R
|
R

K

R

N

R

L

L

G

D

L

L

F

Y

A

A

N

N

F

V

R
|
R

P

P

A

A

I

K

C

S

Y

R

P

P

Q

-

L

-

V

V

D

P

A

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S

S

R

L

-

K

-

R

-

E

-

L

-

V

-

S

P

G

G

L

V

D

D

I

L

L

V

I

I

I

V

R
|
R

E

E

L

N

T

T

G

E

D

G

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Y
|
Y

F

V

G

E

Q

Q

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E

R

R

G

-

R

R

R

Y

I

L

A

-

T

-

D

-

G

-

H

-

F

-

P

-

G

-

A

-

E

D

E
x
V

A

A

F

I

D

A

T

D

M

A

R

V

Y

I

S

S

R

K

P

K

E

A

I

S

E

E

R

R

I

I

A

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H

R

V

A

A

A

F

L

Q

R

A

I

A

A

R

E

K

G

R

R

G

P

K

R

R

K

V

T

T

L

S

H

V

I

-

A

D

H

K
|
K

A

A

N
|
N

V

V

L

L

E

P

T

L

F

T

Q

Q

-

G

L

L

W

F

K

L

D

D

V

T

V

V

T

K

E

E

I

V

G

A

L

K

Q

D

Y

F

P

P

D

L

V

V

A

N

L

V

D

Q

H

D

M

I

Y

I

V

V

D
|
D

N

N

A

C

A

A

M
|
M

Q

Q

L

L

V

V

R

M

A

R

P

P

K

E

K

R

F
|
F

D

D

V

V

V

I

V

V

T

T

G

T

N

N

M

L

F

L

G

G

D
|
D

I

I

L

L

S

S

D
|
D

A

L

A

A

M

G

L

L

T
x
V

G

G

S

G

I

L

G

G

M

L

L

A

P

P

S

S

A

G

S

N

L

I

N

G

D

D

K

-

N

T

Q

T

G

A

L

V

Y

F

E

E

P

P

S

V

H

H

G
|
G

S
|
S

A
|
A

P
|
P

D
|
D

I

I

A

A

G

G

K

K

G

G

V

I

A

A

N
|
N

P

P

L

T

A

A

T

A

I

I

L

L

S

S

A

A

M

M

L

L

R

D

F

Y

S

-

L

L

N

G

Q

E

P

K

E

E

A

A

A

K

R

R

I

V

E

E

Q

K

A

A

V

V

D

D

K

L

V

V

L

L

S

E

Q

R

G

G

L

P

R
|
R

T

T

P

P

D

D

I

L

Y

G

S

G

D

D

G

A

T

T

R

E

I

A

G

F

T

T

V

-

E

-

M

-

G

-

D

E

A

A

V

V

K

E

A

A

L

L

E57 (≠ Q55) mutation to V: Confers enzyme activity with 3-isopropylmalate; when associated with I-72; M-85; A-86; T-208; Y-217; M-238 and M-310.
ATS 70:72 (≠ VGD 68:70) binding NADH
S72 (≠ D70) binding in other chain; mutation to I: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; M-85; A-86; T-208; Y-217; M-238 and M-310.
R85 (vs. gap) binding in other chain; mutation to M: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; A-86; T-208; Y-217; M-238 and M-310.; mutation to V: Confers low enzyme activity with 3-isopropylmalate. Reduces activity with homoisocitrate. Abolishes activity with isocitrate.
Y86 (vs. gap) mutation to A: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; T-208; Y-217; M-238 and M-310.
R88 (= R90) binding in other chain
R98 (= R100) binding in other chain
R118 (= R128) binding in other chain
Y125 (= Y135) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
V135 (≠ E155) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
K171 (= K190) binding (2R,3S)-homoisocitrate
N173 (= N192) binding (2R,3S)-homoisocitrate; binding NADH
D204 (= D222) binding Mg(2+)
M208 (= M226) mutation to T: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; Y-217; M-238 and M-310.
F217 (= F235) mutation to Y: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; M-238 and M-310.
D228 (= D246) binding Mg(2+)
D232 (= D250) binding Mg(2+)
V238 (≠ T256) mutation to M: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; Y-217; and M-310.
GSAPD 261:265 (= GSAPD 280:284) binding NADH
N273 (= N292) binding NADH
R310 (= R330) mutation to M: Confers enzyme activity with 3-isopropylmalate; when associated with V-57; I-72; M-85; A-86; T-208; Y-217; and M-238.

Query Sequence

>WP_011802412.1 NCBI__GCF_000015505.1:WP_011802412.1
MKIAILPGDGIGPEIVAEAVKVLKVLDLNFETETALVGGAAFEAYGHPLPEATLQLAKDA
DAVLFGAVGDWKYDTLDRPLRPEQAILGLRKNLGLFANFRPAICYPQLVDASSLKRELVS
GLDILIIRELTGDIYFGQPRGRRIATDGHFPGAEEAFDTMRYSRPEIERIAHVAFQAARK
RGKRVTSVDKANVLETFQLWKDVVTEIGLQYPDVALDHMYVDNAAMQLVRAPKKFDVVVT
GNMFGDILSDAAAMLTGSIGMLPSASLNDKNQGLYEPSHGSAPDIAGKGVANPLATILSA
AMMLRFSLNQPEAAARIEQAVDKVLSQGLRTPDIYSDGTTRIGTVEMGDAVVKALG

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