SitesBLAST

Q56268 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans) (see paper)
64% identity, 99% coverage: 3:358/358 of query aligns to 2:354/358 of Q56268

query
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Q56268

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R95 (= R97) binding substrate
R105 (= R107) binding substrate
R133 (= R135) binding substrate
D222 (= D225) binding Mg(2+); binding substrate
D246 (= D249) 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)
62% identity, 99% coverage: 5:358/358 of query aligns to 45:397/405 of P93832

query
sites
P93832

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114:129 (vs. 74:90, 53% identical) binding NAD(+)
L132 (= L93) mutation to A: Reduced activity toward 3-isopropylmalate.
L133 (= L94) 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 (= R97) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
R146 (= R107) binding substrate; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
R174 (= R135) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
Y181 (= Y142) Important for catalysis; mutation Y->A,F,H: Reduced activity toward 3-isopropylmalate.
K232 (= K193) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
N234 (= N195) binding NAD(+); mutation N->A,D: Loss of activity toward 3-isopropylmalate.
V235 (= V196) mutation to A: Reduced activity toward 3-isopropylmalate.
D264 (= D225) binding Mg(2+); binding substrate; mutation to N: Loss of activity toward 3-isopropylmalate.
N265 (= N226) binding NAD(+)
D288 (= D249) binding Mg(2+); mutation to N: Loss of activity toward 3-isopropylmalate.
D292 (= D253) binding Mg(2+); mutation to N: Reduced activity toward 3-isopropylmalate.
318:334 (vs. 279:295, 82% identical) binding NAD(+)

5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
62% identity, 99% coverage: 5:358/358 of query aligns to 5:357/360 of 5j33A

query
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active site: Y141 (= Y142), K192 (= K193), D224 (= D225), D248 (= D249), D252 (= D253)
binding magnesium ion: D248 (= D249), D252 (= D253)
binding nicotinamide-adenine-dinucleotide: I74 (≠ V74), E89 (= E90), L92 (= L93), I261 (= I262), E278 (= E279), H281 (= H282), G282 (= G283), S283 (= S284), A284 (= A285), I287 (= I288), N294 (= N295), D335 (= D336)

5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
62% identity, 99% coverage: 5:358/358 of query aligns to 15:367/369 of 5j32A

query
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5j32A

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V

V

V

R
|
R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

Q

E

P

P

R

R

G

G

I

I

R

K

T

T

L

N

E

E

N

N

G

G

E

E

R

E

E

V

G

G

Y

F

N

N

T

T

Y

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V

V

Y

Y

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A

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A

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H

E

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V

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F

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A

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K

R

K

K

R

R

G

R

G

G

K

K

L

L

C

C

S

S

V

V

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D

K
|
K

A

A

N

N

V

V

L

L

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A

T

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I

L

L

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W

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V

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L

L

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S

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H

M

M

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Y

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V

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|
D

N

N

A

A

M

M

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Q

L

L

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V

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P

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K

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Q

F

F

D

D

V

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I

V

V

T

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N

N

N

M

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F

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G

D
|
D

I

I

L

L

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S

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|
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

D

S

K

D

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K

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G

G

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G

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S

A

A

P

P

D

D

I

I

A

A

G

G

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Q

G

D

I

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

Y

Y

S

G

L

L

G

G

E

E

N

E

A

K

A

A

D

K

A

R

I

I

E

E

K

D

A

A

V

V

S

L

D

V

V

A

L

L

D

N

Q

N

N

G

L

F

R

R

T

T

P

G

D

D

I

I

Y

Y

S

S

E

A

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G

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T

T

K

K

L

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V

S

G

T

C

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E

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A

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V

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K

A

S

L

V

active site: L18 (= L8), Y151 (= Y142), K202 (= K193), D234 (= D225), D258 (= D249), D262 (= D253)
binding 3-isopropylmalic acid: R106 (= R97), R144 (= R135), Y151 (= Y142), D258 (= D249)
binding magnesium ion: D258 (= D249), D262 (= D253)

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)
62% identity, 99% coverage: 5:358/358 of query aligns to 46:398/404 of Q9SA14

query
sites
Q9SA14

V

I

L

T

I

L

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

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I

T

S

E

V

A

A

E

K

N

N

V

V

L

L

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Q

A

-

V

-

N

K

A

A

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F

N

L

L

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G

L

L

E

E

F

F

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D

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Q

L

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M

-

P

-

F

G

G

A

A

G

A

Y

L

D

D

A

L

N

V

G

G

H

V

P

P

L

L

P

P

A

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E

E

T

T

M

S

E

T

K

A

A

A

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K

T

Q

A

S

D

D

A

A

I

I

L

L

G

G

A

A

V

I

G

G

P

Y

K

K

W

W

D

D

A

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L

N

E

E

D

-

R

K

E

H

M

L

R

R

P

P

E

E

K

M

G

G

L

L

L
|
L

G

N

L

I

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D

L

L

E

N

L

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F

F

G

A

N

N

L

L

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P

A

A

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Y

L

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Q

L

L

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D

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K

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G

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M

L

M

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T

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L

N

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V

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D

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K

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V

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L

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D

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A

A

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P

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K

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Q

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F

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D

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T

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I

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N

N

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D

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D

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Q

G

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K

A

A

N

N

P

P

L

L

A

A

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T

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L

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S

A

A

M

M

M

L

L

L

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K

Y

Y

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L

L

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G

E

E

N

E

A

K

A

A

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K

A

M

I

I

E

E

K

D

A

A

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V

S

V

D

D

V

A

L

L

D

N

Q

K

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G

L

F

R

R

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T

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G

D

D

I

I

Y

Y

S

S

E

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G

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M

N

T

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K

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L134 (= L94) Confers substrate specificity; mutation to F: Enhanced activity toward 3-(2'-methylthio)-ethylmalate, but reduced catalytic efficiency with 3-isopropylmalate.

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)
61% identity, 99% coverage: 5:358/358 of query aligns to 49:401/409 of Q9FMT1

query
sites
Q9FMT1

V

I

L

A

I

L

L

L

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D

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I

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A

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G

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F

F

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A

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G

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A

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K

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D

A

A

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L

L

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G

A

A

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I

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G

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Y

K

K

W

W

D

D

A

K

L

N

E

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D

-

R

K

E

H

M

L

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R

P

P

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K

M

G

A

L

L

L
x
F

G

Y

L

L

R

R

S

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D

L

L

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K

L

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F

F

G

A

N

N

L

L

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R

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P

A

A

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T

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Y

L

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P

Q

Q

L

L

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D

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S

S

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L

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K

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K

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G

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D

D

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M

L

M

I

I

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V

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R

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L

L

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G

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F

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T

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N

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K

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R

G

G

K

K

L

L

C
|
C

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S

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V

D

D

K

K

A

A

N

N

V

V

L

L

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D

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A

T

S

V

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L

L

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W

R

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M

L

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Y

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P

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V

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L

L

S

S

H

H

M

M

Y

Y

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V

D

D

N

N

A

A

M

M

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Q

L

L

V

I

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R

A

D

P

P

K

K

Q

Q

F

F

D

D

V

T

I

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

D

G

K

E

D

S

N

G

K

P

G

G

M

L

Y

F

E

E

P

P

C

I

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

Q

Q

G

D

I

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

Y

Y

S

G

L

L

G

G

E

E

N

E

A

K

A

A

D

K

A

R

I

I

E

E

K

D

A

A

V

V

S

V

D

D

V

A

L

L

D

N

Q

K

N

G

L

F

R

R

T

T

P

G

D

D

I

I

Y

Y

S

S

E

P

G

G

M

N

T

K

K

L

V

V

S

G

T
x
C

S

K

E

E

M

M

G

G

A

E

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V

V

L

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K

A

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L

V

F137 (≠ L94) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
C232 (= C189) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
C390 (≠ T347) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.

6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
55% identity, 100% coverage: 2:358/358 of query aligns to 3:358/358 of 6xxyA

query
sites
6xxyA

S

S

K

Y

K

N

V

I

L

A

I

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L

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A

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G

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D

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A

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L

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A

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V

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A

E

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K

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F

N

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L

F

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L

L

E

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L

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V

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A

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C

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A

A

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D

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A

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L

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F

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G

A
x
S

V
|
V

G
|
G

G

G

P

P

K

K

W

W

D

T

A

N

L

L

E

P

D

P

R

-

E

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M

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R

Q

P

P

E
|
E

K

R

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G

-

A

L
|
L

L

L

G

P

L

L

R

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K

G

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E

K

L

L

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C

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N

L

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|
R

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L

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A

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K

G

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I

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L

V

I

V

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|
R

E

E

L

L

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G

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I

Y
|
Y

F

F

G

G

Q

Q

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K

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L

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A

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A

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K

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R

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G

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K

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L

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C

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S

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V

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D

K
|
K

A

A

N

N

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|
V

L

L

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Q

V

S

T

S

V

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L

L

W

W

R

R

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M

M

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A

K

K

D

D

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Y

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P

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V

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T

L

L

S

E

H

H

M

I

Y
|
Y

V

I

D
|
D

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|
N

A

A

A

T

M
|
M

Q

Q

L

L

V

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K

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P

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F

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D

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L

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L

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G

S

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N

M

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F

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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

D

N

K

E

D

E

N

G

K

F

G

G

M

L

Y

Y

E
|
E

P

P

C

A

H
x
G

G
|
G

S
|
S

A
|
A

P
|
P

D
|
D

I
|
I

A

A

G

G

Q

K

G

G

I

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

Y

Y

S

S

L

F

G

N

E

L

N

N

A

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A

A

D

D

A

A

I

I

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V

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L

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|
D

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L

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-

S

A

E

D

G

D

M

S

T

T

K

P

V

V

S

S

T

T

S

A

E

E

M

M

G

G

A

T

A

L

V

I

V

T

K

Q

A

A

L

I

active site: Y144 (= Y142), K194 (= K193), D226 (= D225), D250 (= D249)
binding magnesium ion: D250 (= D249), D254 (= D253)
binding nicotinamide-adenine-dinucleotide: S74 (≠ A73), V75 (= V74), G76 (= G75), E90 (= E90), L94 (= L93), Y224 (= Y223), N227 (= N226), M230 (= M229), M263 (≠ I262), G264 (= G263), E280 (= E279), G283 (≠ H282), G284 (= G283), S285 (= S284), A286 (= A285), P287 (= P286), D288 (= D287), I289 (= I288), N296 (= N295), D337 (= D336)
binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E90), R108 (= R107), R137 (= R135), K194 (= K193), V197 (= V196), D226 (= D225), D250 (= D249)

1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
53% identity, 99% coverage: 1:356/358 of query aligns to 1:357/363 of 1cnzA

query
sites
1cnzA

M

M

S

S

K

K

K

N

-

Y

-

H

V

I

L

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

T

A

E

Q

A

A

E

L

N

K

V

V

L

M

V

D

A

A

V

V

N

R

A

S

K

R

F

F

N

D

L

M

G

R

L

I

E

T

F

T

D

S

H

H

G

Y

L

D

V

V

G

G

A

I

G

A

Y

I

D

D

A

N

N

H

G

G

H

H

P

P

L

L

P

P

A

K

E

A

T

T

M

V

E

E

K

G

A

C

R

E

T

Q

A

A

D

D

A

A

I

I

L

L

L

F

G

G

A

S

V

V

G

G

P

P

K

K

W

W

D

E

A

N

L

L

E

P

D

P

R

-

E

E

M

S

R

Q

P

P

E

E

K

R

G

G

-

A

L

L

G

P

L

L

R

R

S

K

G

H

L

F

E

K

L

L

F

F

G

S

N

N

L

L

R

R

P

P

A

A

I

K

L

L

Y

Y

P

Q

Q

G

L

L

A

E

D

A

A

F

S

C

S

P

L

L

K

R

P

A

E

D

V

I

V

A

S

A

-

N

G

G

L

F

D

D

I

I

L

L

I

C

V

V

R

R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

Q

Q

P

P

R

K

G

G

I

-

R

R

T

E

L

G

E

S

N

G

G

Q

E

Y

R

E

E

K

G

A

Y

F

N

D

T

T

Y

E

V

V

Y

Y

R

H

E

R

S

F

E

E

I

I

R

E

R

R

I

I

G

A

K

R

V

I

A

A

F

F

E

E

A

S

A

A

K

R

K

K

R

R

G

R

K

K

L

V

C

T

S

S

V

I

D

D

K
|
K

A

A

N

N

V

V

L

L

E

Q

V

S

T

S

V

I

L

L

W

W

R

R

E

E

I

I

M

V

T

N

E

D

M

V

A

A

K

K

D

T

Y

Y

P

P

E

D

V

V

E

E

L

L

S

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

Q

Q

F

F

D

D

V

V

I

L

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

D

N

K

E

D

Q

N

G

K

F

G

G

M

L

Y

Y

E

E

P

P

C

A

H

G

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

Q

K

G

N

I

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

Y

Y

S

S

L

L

G

D

E

A

N

N

A

D

A

A

D

T

A

A

I

I

E

E

K

Q

A

A

V

I

S

N

D

R

V

A

L

L

D

E

Q

E

N

G

L

V

R

R

T

T

P

G

D

D

I

L

Y

-

S

A

E

R

G

G

M

A

T

A

K

A

V

V

S

S

T

T

S

D

E

E

M

M

G

G

A

D

A

I

V

I

V

A

K

R

active site: Y145 (= Y142), K195 (= K193), D227 (= D225), D251 (= D249)
binding manganese (ii) ion: D251 (= D249), D255 (= D253)

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)
53% identity, 99% coverage: 1:356/358 of query aligns to 1:357/363 of P37412

query
sites
P37412

M

M

S

S

K

K

K

N

-

Y

-

H

V

I

L

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

T

A

E

Q

A

A

E

L

N

K

V

V

L

M

V

D

A

A

V

V

N

R

A

S

K

R

F

F

N

D

L

M

G

R

L

I

E

T

F

T

D

S

H

H

G

Y

L

D

V

V

G

G

A

I

G

A

Y

I

D

D

A

N

N

H

G

G

H

H

P

P

L

L

P

P

A

K

E

A

T

T

M

V

E

E

K

G

A

C

R

E

T

Q

A

A

D

D

A

A

I

I

L

L

L

F

G

G

A

S

V

V

G

G

P

P

K

K

W

W

D

E

A

N

L

L

E

P

D

P

R

-

E

E

M

S

R

Q

P

P

E

E

K

R

G

G

-

A

L

L

G

P

L

L

R

R

S

K

G

H

L

F

E

K

L

L

F

F

G

S

N

N

L

L

R

R

P

P

A

A

I

K

L

L

Y

Y

P

Q

Q

G

L

L

A

E

D

A

A

F

S

C

S

P

L

L

K

R

P

A

E

D

V

I

V

A

S

A

-

N

G

G

L

F

D

D

I

I

L

L

I

C

V

V

R

R

E

E

L

L

T

T

G

G

I

I

Y

Y

F

F

G

G

Q

Q

P

P

R

K

G

G

I

-

R

R

T

E

L

G

E

S

N

G

G

Q

E

Y

R

E

E

K

G

A

Y

F

N

D

T

T

Y

E

V

V

Y

Y

R

H

E

R

S

F

E

E

I

I

R

E

R

R

I

I

G

A

K

R

V

I

A

A

F

F

E

E

A

S

A

A

K

R

K

K

R

R

G

R

K

K

L

V

C

T

S

S

V

I

D

D

K

K

A

A

N

N

V

V

L

L

E

Q

V

S

T

S

V

I

L

L

W

W

R

R

E

E

I

I

M

V

T

N

E

D

M

V

A

A

K

K

D

T

Y

Y

P

P

E

D

V

V

E

E

L

L

S

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

Q

Q

F

F

D

D

V

V

I

L

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

D

N

K

E

D

Q

N

G

K

F

G

G

M

L

Y

Y

E

E

P

P

C

A

H

G

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

Q

K

G

N

I

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

Y

Y

S

S

L

L

G

D

E

A

N

N

A

D

A

A

D

T

A

A

I

I

E

E

K

Q

A

A

V

I

S

N

D

R

V

A

L

L

D

E

Q

E

N

G

L

V

R

R

T

T

P

G

D

D

I

L

Y

-

S

A

E

R

G

G

M

A

T

A

K

A

V

V

S

S

T

T

S

D

E

E

M

M

G

G

A

D

A

I

V

I

V

A

K

R

D227 (= D225) binding Mn(2+)
D251 (= D249) binding Mn(2+)
D255 (= D253) binding Mn(2+)

3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
53% identity, 100% coverage: 2:358/358 of query aligns to 8:366/369 of 3vmkA

query
sites
3vmkA

S

S

K

Y

K

Q

V

I

L

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

T

A

E

E

A

A

E

R

N

K

V

V

L

L

V

A

A

A

V

V

N

E

A

K

K

R

F

F

N

D

L

L

G

S

L

I

E

E

F

Y

D

S

H

E

G

Y

L

D

V

V

G

G

A

A

G

A

Y

I

D

D

A

N

N

H

G

G

H

C

P

P

L

L

P

P

A

E

E

A

T

T

M

L

E

K

K

G

A

C

R

E

T

A

A

A

D

D

A

A

I

V

L

L

L

F

G

G

A

S

V

V

G

G

P

P

K

K

W

W

D

E

A

H

L

L

E

P

D

P

R

N

E

D

M

-

R

Q

P

P

E

E

K

R

G

G

-

A

L

L

G

P

L

L

R
|
R

S

G

G

H

L

F

E

E

L

L

F

F

G

C

N

N

L

M

R

R

P

P

A

A

I

K

L

L

Y

H

P

P

Q

G

L

L

A

E

D

H

A

M

S

S

S

P

L

L

K

R

P

S

E

D

V

I

V

S

-

E

S

K

G

G

L

F

D

D

I

I

L

L

I

C

V

V

R
|
R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

Q

K

P

P

R

K

G

G

I

-

R

R

T

Q

L

G

E

E

N

G

G

E

E

N

R

E

E

E

G

A

Y

F

N

D

T

T

Y

M

V

R

Y

Y

R

S

E

R

S

K

E

E

I

I

R

R

I

I

G

A

K

K

V

I

A

A

F

F

E

E

A

S

A

A

K

Q

K

G

R

R

G

R

G

K

K

K

L

V

C

T

S

S

V

V

D

D

K
|
K

A

A

N
|
N

V

V

L

L

E

A

V

C

T

S

V

V

L

L

W

W

R

R

E

E

I

V

M

V

T

E

E

E

M

V

A

A

K

K

D

D

Y

Y

P

P

E

D

V

V

E

E

L

L

S

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

N

Q

E

F

F

D

D

V

V

I

M

V

L

T

C

G

S

N

N

M

L

F

F

G

G

D
|
D

I

I

L

V

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

A

S

S

A

I

S

S

L

M

D

N

K

S

D

Q

N

G

K

F

G

G

M

M

Y

Y

E

E

P

P

C

A

H

G

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

Q

Q

G

G

I

I

A

A

N

N

P

P

L

V

A

A

T

Q

I

I

L

L

S

S

A

A

M

L

L

L

R

R

Y

H

S

S

L

L

G

K

E

L

N

E

A

D

A

A

D

L

A

A

I

I

E

E

K

A

A

A

V

V

S

S

D

K

V

A

L

L

D

S

Q

D

N

G

L

Y

R

L

T

T

P

C

D

E

I

L

Y

L

-

P

-

A

S

S

E

E

G

R

M

S

T

Q

K

A

V

K

S

S

T

T

S

S

E

Q

M

M

G

G

A

D

A

Y

V

I

V

A

K

Q

A

A

L

I

active site: Y149 (= Y142), K199 (= K193), D231 (= D225), D255 (= D249), D259 (= D253)
binding 3-isopropylmalic acid: R103 (= R97), R142 (= R135), Y149 (= Y142), K199 (= K193), N201 (= N195), D255 (= D249)

3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
52% identity, 99% coverage: 2:357/358 of query aligns to 2:362/364 of 3vkzA

query
sites
3vkzA

S

S

K

Y

K

Q

V

I

L

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

T

A

E

E

A

A

E

R

N

K

V

V

L

L

V

K

A

A

V

V

N

E

A

A

K

R

F

F

N

G

L

L

G

N

L

I

E

E

F

Y

D

T

H

E

G

Y

L

D

V

V

G

G

A

I

G

A

Y

I

D

D

A

N

N

H

G

G

H

C

P

P

L

L

P

P

A

E

E

A

T

T

M

L

E

K

K

G

A

C

R

E

T

A

A

A

D

D

A

A

I

I

L

L

L

F

G

G

A

S

V

V

G

G

P

P

K

K

W

W

D

E

A

K

L

L

E

P

D

P

R

N

E

E

M

-

R

Q

P

P

E

E

K

R

G

G

-

A

L

L

G

P

L

L

R
|
R

S

G

G

H

L

F

E

E

L

L

F

F

G

C

N

N

L

L

R

R

P

P

A

A

I

K

L

L

Y

H

P

D

Q

G

L

L

A

E

D

H

A

M

S

S

S

P

L

L

K

R

P

S

E

D

V

I

V

S

S

A

-

R

G

G

L

F

D

D

I

V

L

L

I

C

V

V

R
|
R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

Q

K

P

P

R

K

G

G

I

-

R

R

T

Q

L

G

E

E

N

G

G

E

E

S

R

E

E

E

G

A

Y

F

N

D

T

T

Y

M

V

R

Y

Y

R

S

E

R

S

R

E

E

I

I

R

S

R

R

I

I

G

A

K

R

V

I

A

A

F

F

E

E

A

A

K

R

K

G

R

R

G

R

G

K

K

K

L

V

C

T

S

S

V

V

D

D

K
|
K

A

A

N

N

V

V

L

L

E

A

V

C

T

S

V

V

L

L

W

W

R

R

E

Q

I

V

M

V

T

E

E

E

M

V

A

A

K

V

D

D

Y

F

P

P

E

D

V

V

E

E

L

L

S

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

Q

E

F

F

D

D

V

V

I

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

D

N

K

S

D

T

N

G

K

F

G

G

M

L

Y

F

E

E

P

P

C

A

H

G

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

Q

K

G

G

I

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

Y

H

S

S

L

L

G

K

E

Q

N

E

A

E

A

A

D

S

A

A

I

I

E

E

K

R

A

A

V

V

S

T

D

K

V

A

L

L

D

N

Q

S

N

G

L

Y

R

L

T

T

P

G

D

E

I

L

Y

L

S

S

-

S

-

D

-

Q

-

R

-

H

E

K

G

A

M

K

T

T

K

T

V

V

S

Q

T

M

S

G

E

D

M

F

G

I

A

A

A

D

V

A

V

V

K

K

A

A

active site: Y143 (= Y142), K193 (= K193), D225 (= D225), D249 (= D249), D253 (= D253)
binding calcium ion: D249 (= D249), D253 (= D253)
binding 3-isopropylmalic acid: R97 (= R97), R136 (= R135), Y143 (= Y142), D249 (= D249)

2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
54% identity, 93% coverage: 2:335/358 of query aligns to 1:324/346 of 2y41A

query
sites
2y41A

S

S

K

M

K

K

V

V

L

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

T

E

E

A

A

A

E

L

N

K

V

V

L

L

V

R

A

A

V

L

N

D

A

E

K

A

F

E

N

G

L

L

G

G

L

L

E

A

F

Y

D

E

H

V

G

F

L

P

V

F

G

G

A

A

G

A

Y

I

D

D

A

A

N

F

G

G

H

E

P

P

L

F

P

P

A

E

E

P

T

T

M

R

E

K

K

G

A

V

R

E

T

E

A

A

D

E

A

A

I

V

L

L

G

G

A

S

V

V

G

G

P

P

K

K

W

W

D

D

A

G

L

L

E

-

D

P

R

R

E

K

M

I

R

R

P

P

E

E

K

T

G

G

L

L

G

S

L

L

R
|
R

S

K

G

S

L

Q

E

D

L

L

F

F

G

A

N

N

L

L

R
|
R

P

P

A

A

I

K

L

V

Y

F

P

P

Q

G

L

L

A

E

D

R

A

L

S

S

S

P

L

L

K

K

P

E

E

E

V

I

V

A

S

R

G

G

L

V

D

D

I

V

L

L

I

I

V

V

R
|
R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

Q

E

P

P

R

R

G

G

I

M

R

-

T

-

L

-

E

-

N

-

G

S

E

E

R

A

E

E

G

A

Y

W

N

N

T

T

Y

E

V

R

Y

Y

R

S

E

K

S

P

E

E

I

V

R

E

R

R

I

V

G

A

K

R

V

V

A

A

F

F

E

E

A

A

K

R

K

K

R

R

G

R

G

K

K

H

L

V

C

V

S

S

V

V

D

D

K
|
K

A

A

N

N

V

V

L

L

E

E

V

V

T

G

V

E

L

F

W

W

R

R

E

K

I

T

M

V

T

E

E

E

M

V

A

G

K

R

D

G

Y

Y

P

P

E

D

V

V

E

A

L

L

S

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

Q

R

F

F

D

D

V

V

I

V

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

D

G

K

R

D

G

N

T

K

P

G

-

M

V

Y

F

E

E

P

P

C

V

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

Q

K

G

G

I

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

Y

H

S

A

L

F

G

G

E

L

N

V

A

E

A

L

A

A

D

R

A

K

I

V

E

E

K

D

A

A

V

V

S

A

D

K

V

A

L

L

D

-

Q

-

N

-

L

L

R

E

T

T

P

P

active site: Y140 (= Y142), K186 (= K193), D218 (= D225), D242 (= D249), D246 (= D253)
binding 3-isopropylmalic acid: R95 (= R97), R105 (= R107), R133 (= R135), Y140 (= Y142), D242 (= D249)

2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
54% identity, 93% coverage: 2:335/358 of query aligns to 1:324/355 of 2y42D

query
sites
2y42D

S

S

K

M

K

K

V

V

L

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

T

E

E

A

A

A

E

L

N

K

V

V

L

L

V

R

A

A

V

L

N

D

A

E

K

A

F

E

N

G

L

L

G

G

L

L

E

A

F

Y

D

E

H

V

G

F

L

P

V

F

G

G

A

A

G

A

Y

I

D

D

A

A

N

F

G

G

H

E

P

P

L

F

P

P

A

E

E

P

T

T

M

R

E

K

K

G

A

V

R

E

T

E

A

A

D

E

A

A

I

V

L

L

G

G

A

S

V

V

G

G

P

P

K

K

W

W

D
|
D

A

G

L

L

E

-

D

P

R

R

E

K

M

I

R

R

P

P

E

E

K

T

G

G

L

L

G

S

L

L

R

R

S

K

G

S

L

Q

E

D

L

L

F

F

G

A

N

N

L

L

R

R

P

P

A

A

I

K

L

V

Y

F

P

P

Q

G

L

L

A

E

D

R

A

L

S

S

S

P

L

L

K

K

P

E

E

E

V

I

V

A

S

R

G

G

L

V

D

D

I

V

L

L

I

I

V

V

R

R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

Q

E

P

P

R

R

G

G

I

M

R

-

T

-

L

-

E

-

N

-

G

S

E

E

R

A

E

E

G

A

Y

W

N

N

T

T

Y

E

V

R

Y

Y

R

S

E

K

S

P

E

E

I

V

R

E

R

R

I

V

G

A

K

R

V

V

A

A

F

F

E

E

A

A

K

R

K

K

R

R

G

R

G

K

K

H

L

V

C

V

S

S

V

V

D

D

K
|
K

A

A

N

N

V

V

L

L

E

E

V

V

T

G

V

E

L

F

W

W

R

R

E

K

I

T

M

V

T

E

E

E

M

V

A

G

K

R

D

G

Y

Y

P

P

E

D

V

V

E

A

L

L

S

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

Q

R

F

F

D

D

V

V

I

V

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

D

G

K

R

D

G

N

T

K

P

G

-

M

V

Y

F

E

E

P

P

C

V

H
|
H

G
|
G

S

S

A
|
A

P

P

D
|
D

I
|
I

A

A

G

G

Q

K

G

G

I

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

Y

H

S

A

L

F

G

G

E

L

N

V

A

E

A

L

A

A

D

R

A

K

I

V

E

E

K

D

A

A

V

V

S

A

D

K

V

A

L

L

D

-

Q

-

N

-

L

L

R

E

T

T

P

P

active site: Y140 (= Y142), K186 (= K193), D218 (= D225), D242 (= D249), D246 (= D253)
binding manganese (ii) ion: D242 (= D249), D246 (= D253)
binding nicotinamide-adenine-dinucleotide: I12 (= I13), D79 (= D80), H274 (= H282), G275 (= G283), A277 (= A285), D279 (= D287), I280 (= I288), N287 (= N295)

2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
55% identity, 93% coverage: 4:335/358 of query aligns to 2:323/345 of 2ztwA

query
sites
2ztwA

K

K

V

V

L

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

T

E

E

A

A

A

E

L

N

K

V

V

L

L

V

R

A

A

V

L

N

D

A

E

K

A

F

E

N

G

L

L

G

G

L

L

E

A

F

Y

D

E

H

V

G

F

L

P

V

F

G

G

A

A

G

A

Y

I

D

D

A

A

N

F

G

G

H

E

P

P

L

F

P

P

A

E

E

P

T

T

M

R

E

K

K

G

A

V

R

E

T

E

A

A

D

E

A

A

I

V

L

L

G

G

A

S

V

V

G

G

P

P

K

K

W

W

D

D

A

G

L

L

E

-

D

P

R

R

E

K

M

I

R

R

P

P

E

E

K

T

G

G

L

L

G

S

L

L

R

R

S

K

G

S

L

Q

E

D

L

L

F

F

G

A

N

N

L

L

R

R

P

P

A

A

I

K

L

V

Y

F

P

P

Q

G

L

L

A

E

D

R

A

L

S

S

S

P

L

L

K

K

P

E

E

E

V

I

V

A

S

R

G

G

L

V

D

D

I

V

L

L

I

I

V

V

R

R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

Q

E

P

P

R

R

G

G

I

M

R

-

T

-

L

-

E

-

N

-

G

S

E

E

R

A

E

E

G

A

Y

W

N

N

T

T

Y

E

V

R

Y

Y

R

S

E

K

S

P

E

E

I

V

R

E

R

R

I

V

G

A

K

R

V

V

A

A

F

F

E

E

A

A

K

R

K

K

R

R

G

R

G

K

K

H

L

V

C

V

S

S

V

V

D

D

K
|
K

A

A

N

N

V

V

L

L

E

E

V

V

T

G

V

E

L

F

W

W

R

R

E

K

I

T

M

V

T

E

E

E

M

V

A
x
G

K

R

D

G

Y
|
Y

P

P

E

D

V
|
V

E

A

L

L

S

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

Q

R

F

F

D

D

V

V

I

V

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

D

G

K

R

D

G

N

T

K

P

G

-

M

V

Y

F

E

E

P

P

C

V

H
|
H

G
|
G

S

S

A
|
A

P

P

D
|
D

I
|
I

A

A

G

G

Q

K

G

G

I

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

Y

H

S

A

L

F

G

G

E

L

N

V

A

E

A

L

A

A

D

R

A

K

I

V

E

E

K

D

A

A

V

V

S

A

D

K

V

A

L

L

D

-

Q

-

N

-

L

L

R

E

T

T

P

P

active site: Y139 (= Y142), K185 (= K193), D217 (= D225), D241 (= D249), D245 (= D253)
binding magnesium ion: G203 (≠ A211), Y206 (= Y214), V209 (= V217)
binding nicotinamide-adenine-dinucleotide: I11 (= I13), H273 (= H282), G274 (= G283), A276 (= A285), D278 (= D287), I279 (= I288), A285 (= A294), N286 (= N295)

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)
55% identity, 93% coverage: 4:335/358 of query aligns to 2:323/345 of Q5SIY4

query
sites
Q5SIY4

K

K

V

V

L

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

T

E

E

A

A

A

E

L

N

K

V

V

L

L

V

R

A

A

V

L

N

D

A

E

K

A

F

E

N

G

L

L

G

G

L

L

E

A

F

Y

D

E

H

V

G

F

L

P

V

F

G

G

A

A

G

A

Y

I

D

D

A

A

N

F

G

G

H

E

P

P

L

F

P

P

A

E

E

P

T

T

M

R

E

K

K

G

A

V

R

E

T

E

A

A

D

E

A

A

I

V

L

L

G

G

A

S

V

V

G

G

G
|
G

P
|
P

K
|
K

W
|
W

D
|
D

A
x
G

L
|
L

E

-

D
x
P

R
|
R

E
x
K

M
x
I

R
|
R

P
|
P

E
|
E

K

T

G

G

L

L

G

S

L

L

R

R

S

K

G

S

L

Q

E

D

L

L

F

F

G

A

N

N

L

L

R

R

P

P

A

A

I

K

L

V

Y

F

P

P

Q

G

L

L

A

E

D

R

A

L

S

S

S

P

L

L

K

K

P

E

E

E

V

I

V

A

S

R

G

G

L

V

D

D

I

V

L

L

I

I

V

V

R

R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

Q

E

P

P

R

R

G

G

I

M

R

-

T

-

L

-

E

-

N

-

G

S

E

E

R

A

E

E

G

A

Y

W

N

N

T

T

Y

E

V

R

Y

Y

R

S

E

K

S

P

E

E

I

V

R

E

R

R

I

V

G

A

K

R

V

V

A

A

F

F

E

E

A

A

K

R

K

K

R

R

G

R

G

K

K

H

L

V

C

V

S

S

V

V

D

D

K

K

A

A

N

N

V

V

L

L

E

E

V

V

T

G

V

E

L

F

W

W

R

R

E

K

I

T

M

V

T

E

E

E

M

V

A

G

K

R

D

G

Y

Y

P

P

E

D

V

V

E

A

L

L

S

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

Q

R

F

F

D

D

V

V

I

V

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

D

G

K

R

D

G

N

T

K

P

G

-

M

V

Y

F

E

E

P

P

C

V

H

H

G
|
G

S
|
S

A
|
A

P
|
P

D
|
D

I
|
I

A
|
A

G
|
G

Q
x
K

G
|
G

I
|
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

Y

H

S

A

L

F

G

G

E

L

N

V

A

E

A

L

A

A

D

R

A

K

I

V

E

E

K

D

A

A

V

V

S

A

D

K

V

A

L

L

D

-

Q

-

N

-

L

L

R

E

T

T

P

P

74:87 (vs. 76:90, 67% identical) binding NAD(+)
Y139 (= Y142) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
274:286 (vs. 283:295, 92% identical) binding NAD(+)

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)
44% identity, 100% coverage: 1:358/358 of query aligns to 2:367/371 of P18869

query
sites
P18869

M

C

S

A

K

K

V

I

L

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

T

A

E

S

A

A

E

L

N

E

V

V

L

L

V

K

A

V

V

V

N

E

A

K

K

K

F

R

-

P

N

E

L

L

G

K

L

L

E

E

F

F

D

E

H

E

G

H

L

K

V

I

G

G

A

A

G

S

Y

I

D

D

A

A

N

Y

G

G

H
x
T

P

P

L

L

P

T

A

D

E

E

T

T

M

V

E

K

K

A

A

C

R

L

T

E

A

A

D

D

A

G

I

V

L

L

G

G

A

A

V

V

G

G

P

P

K

E

W

W

D

T

A

-

L

-

E

-

D

N

R

P

E

N

M

C

R

R

P

P

E

E

K

Q

G

G

L

L

G

K

L

L

R

R

S

K

G

S

L

M

E

G

L

V

F

W

G

A

N

N

L

L

R

R

P

P

A

C

I

N

L

F

Y

A

P

S

Q

K

-

S

L

L

A

V

D

K

A

Y

S

S

S

P

L

L

K

K

P

P

E

E

V

I

V

V

S

E

G

G

L

V

D

D

I

F

L

C

I

V

V

V

R

R

E

E

L

L

T

T

G

G

I

C

Y

Y

F

F

G

G

Q

E

P

-

R

-

G

-

I

-

R

R

T

T

L

E

E

D

N

N

G

G

E

S

R

G

E

Y

G

A

Y

M

N

D

T

T

Y

W

V

P

Y

Y

R

S

E

L

S

E

E

E

I

V

R

S

R

R

I

I

G

A

K

R

V

L

A

A

F

A

E

W

A

L

A

A

K

E

K

T

R

S

G

N

-

P

G

A

K

P

L

V

C

T

S

L

V

L

D

D

K

K

A

A

N

N

V

V

L

L

E

A

V

T

T

S

V

R

L

L

W

W

R

R

E

K

I

T

M

V

T

A

E

K

M

I

A

F

K

K

D

E

-

E

Y

Y

P

P

E

H

V

L

E

T

L

L

S

K

H

N

M

Q

Y

L

V

I

D

D

N

S

A

A

M

M

Q

L

L

L

V

V

R

K

A

S

P

P

K

R

Q

T

F

L

D

N

-

G

V

V

I

V

V

L

T

T

G

D

N

N

M

L

F

F

G

G

D

D

I

I

L

I

S

S

D

D

A

E

A

A

A

S

M

V

L

I

T

P

G

G

S

S

I

L

G

G

M

L

L

L

P

P

S

S

A

A

S

S

L

L

-

S

-

G

-

V

-

G

-

K

-

S

D

E

K

E

D

K

N

V

K

H

G

C

M

L

Y

V

E

E

P

P

C

I

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

Q

K

G

G

I

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

Y

Y

S

G

L

L

G

N

E

A

N

P

A

K

A

E

A

A

D

E

A

A

I

I

E

E

K

A

A

A

V

V

S

R

D

K

V

V

L

L

D

D

-

D

-

T

-

S

-

I

-

G

Q

R

N

G

L

L

R

Y

T

T

P

R

D

D

I

L

Y

G

S

G

E

E

G

A

M

-

T

-

K

-

V

-

S

S

T

T

S

A

E

D

M

I

G

T

A

K

A

A

V

V

K

E

A

E

L

L

T55 (≠ H53) 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)
42% identity, 100% coverage: 1:358/358 of query aligns to 1:331/334 of Q72IW9

query
sites
Q72IW9

M

M

S

A

K

Y

K

R

V

I

L

C

I

L

L

I

P

E

G

G

D

D

G

G

I

I

G

G

P

H

E

E

I

V

V

I

T

P

E

A

A

A

E

R

N

R

V

V

L

L

V

E

A

A

V

T

N

G

A

-

K

-

F

-

N

-

L

L

G

P

L

L

E

E

F

F

D

V

H

E

G

A

L

E

V

A

G

G

G

W

A

E

G

T

Y

F

D

E

A

R

N

R

G

G

H

T

P

S

L

V

P

P

A

E

E

E

T

T

M

V

E
|
E

K

K

A

I

R

L

T

S

A

C

D

H

A

A

I

T

L

L

L

F

G

G

A

A

V
x
A

G
x
T

G
x
S

P

P

K

-

W

-

D

-

A

-

L

-

E

-

D

-

R

-

E

-

M

T

R

R

P

K

E

V

K

P

G

G

L

F

G

G

-

A

-

I

-
x
R

-
x
Y

L

L

R
|
R

S

R

G

R

L

L

E

D

L

L

F

Y

G

A

N

N

L

V

R
|
R

P

P

A

A

I

K

L

S

Y

R

P

P

Q

V

L

-

A

-

D

-

A

-

S

-

L

-

K

-

P

P

E

G

V

S

V

R

S

P

G

G

L

V

D

D

I

L

L

V

I

I

V

V

R
|
R

E

E

L

N

T

T

G

E

G

G

I

L

Y
|
Y

F

V

G

E

Q

Q

P

E

R

R

G

-

I

-

R

R

T

Y

L

L

E

D

N
x
V

G

A

E

I

R

A

E

D

G

A

Y

-

N

-

T

-

Y

-

V

V

Y

I

R

S

E

K

S

K

E

A

I

S

R

E

R

R

I

I

G

G

K

R

V

A

A

A

F

L

E

R

A

I

A

A

K

E

K

G

R

R

G

P

G

R

K

K

L

T

C

L

S

H

V

I

-

A

D

H

K
|
K

A

A

N
|
N

V

V

L

L

E

P

V

L

T

T

V

Q

-

G

L

L

W

F

R

L

E

D

I

T

M

V

T

K

E

E

M

V

A

A

K

K

D

D

Y

F

P

P

E

L

V

V

E

N

L

V

S

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

Q

R

F
|
F

D

D

V

V

I

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

D

G

K

-

D

D

N

T

K

T

G

A

M

V

Y

F

E

E

P

P

C

V

H

H

G
|
G

S
|
S

A
|
A

P
|
P

D
|
D

I

I

A

A

G

G

Q

K

G

G

I

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

Y

Y

S

-

L

L

G

G

E

E

N

K

A

E

A

A

D

K

A

R

I

V

E

E

K

K

A

A

V

V

S

D

D

L

V

V

L

L

D

E

Q

R

N

G

L

P

R
|
R

T

T

P

P

D

D

I

L

Y

G

S

G

E

D

G

A

M

T

T

T

K

E

V

A

S

F

T

T

S

E

E

-

M

-

G

-

A

-

A

A

V

V

K

E

A

A

L

L

E57 (= E61) 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 (≠ VGG 74:76) binding NADH
S72 (≠ G76) 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 (= R97) binding in other chain
R98 (= R107) binding in other chain
R118 (= R135) binding in other chain
Y125 (= Y142) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
V135 (≠ N154) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
K171 (= K193) binding (2R,3S)-homoisocitrate
N173 (= N195) binding (2R,3S)-homoisocitrate; binding NADH
D204 (= D225) binding Mg(2+)
M208 (= M229) 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 (= F238) 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 (= D249) binding Mg(2+)
D232 (= D253) binding Mg(2+)
V238 (≠ T259) 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 283:287) binding NADH
N273 (= N295) binding NADH
R310 (= R333) 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_046009012.1 NCBI__GCF_000967895.1:WP_046009012.1
MSKKVLILPGDGIGPEIVTEAENVLVAVNAKFNLGLEFDHGLVGGAGYDANGHPLPAETM
EKARTADAILLGAVGGPKWDALEDREMRPEKGLLGLRSGLELFGNLRPAILYPQLADASS
LKPEVVSGLDILIVRELTGGIYFGQPRGIRTLENGEREGYNTYVYRESEIRRIGKVAFEA
AKKRGGKLCSVDKANVLEVTVLWREIMTEMAKDYPEVELSHMYVDNAAMQLVRAPKQFDV
IVTGNMFGDILSDAAAMLTGSIGMLPSASLDKDNKGMYEPCHGSAPDIAGQGIANPLATI
LSAAMMLRYSLGENAAADAIEKAVSDVLDQNLRTPDIYSEGMTKVSTSEMGAAVVKAL

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