SitesBLAST

Q56268 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans) (see paper)
63% identity, 100% coverage: 2:354/354 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 (= D221) binding Mg(2+); binding substrate
D246 (= D245) 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)
61% identity, 99% coverage: 3:354/354 of query aligns to 45:397/405 of P93832

query
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P93832

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114:129 (vs. 68:83, 50% identical) binding NAD(+)
L132 (= L86) 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 (= K189) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
N234 (= N191) binding NAD(+); mutation N->A,D: Loss of activity toward 3-isopropylmalate.
V235 (= V192) mutation to A: Reduced activity toward 3-isopropylmalate.
D264 (= D221) binding Mg(2+); binding substrate; mutation to N: Loss of activity toward 3-isopropylmalate.
N265 (= N222) binding NAD(+)
D288 (= D245) binding Mg(2+); mutation to N: Loss of activity toward 3-isopropylmalate.
D292 (= D249) binding Mg(2+); mutation to N: Reduced activity toward 3-isopropylmalate.
318:334 (vs. 275:291, 76% identical) binding NAD(+)

5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
61% identity, 99% coverage: 3:354/354 of query aligns to 5:357/360 of 5j33A

query
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active site: Y141 (= Y135), K192 (= K189), D224 (= D221), D248 (= D245), D252 (= D249)
binding magnesium ion: D248 (= D245), D252 (= D249)
binding nicotinamide-adenine-dinucleotide: I74 (≠ V68), E89 (= E83), L92 (= L86), I261 (= I258), E278 (= E275), H281 (= H278), G282 (= G279), S283 (= S280), A284 (= A281), I287 (= I284), N294 (= N291), D335 (= D332)

5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
61% identity, 99% coverage: 3:354/354 of query aligns to 15:367/369 of 5j32A

query
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5j32A

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V

V

A

S

E

G

G

L

V

D

D

I

L

L

M

I

V

V

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

I

I

E

K

T

T

R

N

E

E

V

-

N

N

G

G

A

-

Q

-

Q

E

R

E

V

V

G

G

W

F

N

N

T

T

M

E

I

V

Y

Y

A

A

E

A

Y

H

E

E

I

I

R

D

R

R

I

I

L

A

K

R

V

V

A

A

F

F

E

E

A

T

A

A

Q

R

K

K

R

R

G

R

K

G

K

K

L

L

C

C

S

S

V

V

D

D

K
|
K

M

A

N

N

V

V

L

L

E

E

T

A

T

S

Q

I

L

L

W

W

R

R

D

K

I

R

A

V

D

T

E

A

M

L

A

A

K

S

D

E

F

Y

P

P

D

D

V

V

E

E

L

L

S

S

H

H

M

M

L

Y

V

V

D
|
D

N

N

A

A

M

M

Q

Q

L

L

V

V

R

R

N

D

P

P

K

K

Q

Q

F

F

D

D

V

T

M

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

E

E

A

A

S

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

A

D

N

S

N

G

K

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

Y

Y

T

G

F

L

N

G

Q

E

E

E

E

K

A

A

V

K

R

R

I

I

E

E

R

D

A

A

V

V

K

L

K

V

V

A

L

L

A

N

Q

N

G

G

F

F

R

R

T

T

G

G

D

D

I

I

Y

Y

E

S

A

A

G

G

T

T

K

K

K

L

V

V

G

G

T

C

R

K

E

E

M

M

G

G

D

E

A

E

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V

L

L

A

K

A

S

L

V

active site: L18 (= L6), Y151 (= Y135), K202 (= K189), D234 (= D221), D258 (= D245), D262 (= D249)
binding 3-isopropylmalic acid: R106 (= R90), R144 (= R128), Y151 (= Y135), D258 (= D245)
binding magnesium ion: D258 (= D245), D262 (= D249)

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)
60% identity, 100% coverage: 2:354/354 of query aligns to 45:398/404 of Q9SA14

query
sites
Q9SA14

K

N

I

I

C

T

V

L

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

T

I

A

S

E

V

A

A

V

K

R

N

V

V

L

L

R

Q

A

K

L

A

D

G

-

F

-

L

-

Q

-

G

L

L

K

E

I

F

E

D

L

F

E

Q

E

E

A

M

L

P

L

F

G

G

S

A

A

A

V

L

D

D

A

L

T

V

G

G

T

V

P

P

Y

L

P

P

E

E

A

E

T

T

Q

S

K

T

L

A

A

A

R

K

A

Q

A

S

D

D

A

A

V

I

L

L

G

G

A

A

V

I

G

G

P

Y

K

K

W

W

D

D

T

K

L

N

P

E

R

K

E

H

Q

L

R

R

P

P

E

E

R

M

G

G

L

L

L
|
L

G

N

I

I

R

R

K

R

D

D

L

L

S

N

L

V

F

F

A

A

N

N

L

L

R

R

P

P

A

A

I

T

L

V

Y

L

P

P

E

Q

L

L

A

V

N

D

A

A

S

S

T

T

L

L

K

K

P

K

E

E

V

V

V

A

S

Q

G

G

L

V

D

D

I

M

L

M

I

I

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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

I

I

E

T

T

I

R

N

E

E

V

-

N

N

G

G

A

-

Q

-

Q

E

R

E

V

V

G

G

W

F

N

N

T

T

M

E

I

I

Y

Y

A

A

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A

Y

H

E

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I

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A

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A

A

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F

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R

K

G

K

K

L

L

C

C

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V

D

D

K

K

M

A

N

N

V

V

L

L

E

D

T

A

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S

Q

I

L

L

W

W

R

R

D

K

I

R

A

V

D

T

E

A

M

L

A

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E

F

Y

P

P

D

D

V

V

E

E

L

L

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S

H

H

M

M

L

Y

V

V

D

D

N

N

A

A

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M

Q

Q

L

L

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V

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R

N

D

P

P

K

K

Q

Q

F

F

D

D

V

T

M

I

V

V

T

T

G

N

N

N

M

I

F

F

G

G

D

D

I

I

L

L

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S

D

D

E

E

A

A

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M

L

I

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T

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I

I

G

G

M

M

L

L

P

P

S

S

A

A

S

S

L

L

D

G

A

E

N

S

N

G

K

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

Y

Y

T

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F

L

N

G

Q

E

E

E

E

K

A

A

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K

R

M

I

I

E

E

R

D

A

A

V

V

K

V

K

D

V

A

L

L

A

N

Q

K

G

G

F

F

R

R

T

T

G

G

D

D

I

I

Y

Y

E

S

A

P

G

G

T

N

K

K

K

L

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V

G

G

T

C

R

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L

L

A

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.

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)
60% identity, 99% coverage: 3:354/354 of query aligns to 49:401/409 of Q9FMT1

query
sites
Q9FMT1

I

I

C

A

V

L

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

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T

I

A

S

E

V

A

A

V

K

R

N

V

V

L

L

R

Q

-

K

-

A

-

G

A

S

L

L

D

E

-

G

L

L

K

E

I

F

E

D

L

F

E

K

E

E

A

M

L

P

L

V

G

G

S

A

A

A

V

L

D

D

A

L

T

V

G

G

T

V

P

P

Y

L

P

P

E

E

A

E

T

T

Q

F

K

T

L

A

A

A

R

K

A

L

A

S

D

D

A

A

V

I

L

L

G

G

A

A

V

I

G

G

P

Y

K

K

W

W

D

D

T

K

L

N

P

E

R

K

E

H

Q

L

R

R

P

P

E

E

R

M

G

A

L

L

L
x
F

G

Y

I

L

R

R

K

R

D

D

L

L

S

K

L

V

F

F

A

A

N

N

L

L

R

R

P

P

A

A

I

T

L

V

Y

L

P

P

E

Q

L

L

A

V

N

D

A

A

S

S

T

T

L

L

K

K

P

K

E

E

V

V

V

A

S

E

G

G

L

V

D

D

I

M

L

M

I

I

V

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

I

I

E

T

T

I

R

N

E

E

V

-

N

N

G

G

A

-

Q

-

Q

E

R

E

V

V

G

G

W

V

N

S

T

T

M

E

I

I

Y

Y

A

A

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A

Y

H

E

E

I

I

R

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I

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L

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F

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E

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T

A

A

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R

K

K

R

R

G

R

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G

K

K

L

L

C
|
C

S

S

V

V

D

D

K

K

M

A

N

N

V

V

L

L

E

D

T

A

T

S

Q

I

L

L

W

W

R

R

D

K

I

R

A

V

D

T

E

A

M

L

A

A

K

S

D

E

F

Y

P

P

D

D

V

V

E

E

L

L

S

S

H

H

M

M

L

Y

V

V

D

D

N

N

A

A

M

M

Q

Q

L

L

V

I

R

R

N

D

P

P

K

K

Q

Q

F

F

D

D

V

T

M

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

E

E

A

A

S

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

A

E

N

S

N

G

K

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

Y

Y

T

G

F

L

N

G

Q

E

E

E

E

K

A

A

V

K

R

R

I

I

E

E

R

D

A

A

V

V

K

V

K

D

V

A

L

L

A

N

Q

K

G

G

F

F

R

R

T

T

G

G

D

D

I

I

Y

Y

E

S

A

P

G

G

T

N

K

K

K

L

V

V

G

G

T
x
C

R

K

E

E

M

M

G

G

D

E

A

E

V

V

L

L

A

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 (= C185) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
C390 (≠ T343) 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: 2:354/354 of query aligns to 5:358/358 of 6xxyA

query
sites
6xxyA

K

N

I

I

C

A

V

V

L

L

P

A

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

T

M

A

A

E

E

A

A

V

I

R

K

V

V

L

L

R

N

-

R

-

V

-

Q

-

E

A

K

L

F

D

G

L

F

K

K

I

L

E

N

L

F

E

N

E

E

A

F

L

F

L

V

G

G

S

A

A

A

V

I

D

E

A

H

T

C

G

G

T

Y

P

P

Y

L

P

P

E

A

A

E

T

T

Q

L

K

K

L

G

A

C

R

D

A

Q

A

A

D

D

A

A

V

I

L

L

L

F

G

G

A
x
S

V
|
V

G
|
G

G

G

P

P

K

K

W

W

D

T

T

N

L

L

P

P

R

P

E

D

Q

Q

R

Q

P

P

E
|
E

R

R

G

G

-

A

L
|
L

L

L

G

P

I

L

R

R

K

K

D

H

L

F

S

K

L

L

F

F

A

C

N

N

L

L

R
|
R

P

P

A

A

I

T

L

L

Y

Y

P

K

E

G

L

L

A

E

N

K

A

F

S

C

T

P

L

L

K

R

P

A

E

D

V

I

V

A

S

A

-

K

G

G

L

F

D

D

I

M

L

V

I

V

V

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

I

-

E

-

T

-

R

R

E

E

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G

N

D

G

G

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V

Q

Q

Q

T

R

K

V

-

G

A

W

F

N

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T

T

M

E

I

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Y

Y

A

Y

E

K

Y

Y

E

E

I

I

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E

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R

I

I

L

A

K

R

V

A

A

A

F

F

E

E

A

A

Q

M

K

K

R

R

G

N

K

K

L

V

C

T

S

S

V

V

D

D

K
|
K

M

A

N

N

V
|
V

L

L

E

Q

T

S

Q

I

L

L

W

W

R

R

D

E

I

T

A

V

D

T

E

E

M

M

A

A

K

K

D

D

F

Y

P

P

D

E

V

V

E

T

L

L

S

E

H

H

M

I

L
x
Y

V

I

D
|
D

N
|
N

A

A

A

T

M
|
M

Q

Q

L

L

V

I

R

K

N

S

P

P

K

E

Q

S

F

F

D

D

V

V

M

L

V

L

T

C

G

S

N

N

M

I

F

F

G

G

D
|
D

I

I

L

I

S

S

D
|
D

E

E

A

A

S

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

A

E

N

E

N

G

K

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

Y

Y

T

S

F

F

N

N

Q

L

E

N

E

E

A

A

V

D

R

A

I

I

E

E

R

S

A

A

V

V

K

Q

K

K

V

V

L

L

A

A

Q

S

G

G

F

H

R

R

T

T

G

A

D
|
D

I

L

Y

A

E

D

A

D

G

S

T

T

K

-

K

P

V

V

G

S

T

T

R

A

E

E

M

M

G

G

D

T

A

L

V

I

L

T

A

Q

A

A

L

I

active site: Y144 (= Y135), K194 (= K189), D226 (= D221), D250 (= D245)
binding magnesium ion: D250 (= D245), D254 (= D249)
binding nicotinamide-adenine-dinucleotide: S74 (≠ A67), V75 (= V68), G76 (= G69), E90 (= E83), L94 (= L86), Y224 (≠ L219), N227 (= N222), M230 (= M225), M263 (≠ I258), G264 (= G259), E280 (= E275), G283 (≠ H278), G284 (= G279), S285 (= S280), A286 (= A281), P287 (= P282), D288 (= D283), I289 (= I284), N296 (= N291), D337 (= D332)
binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E83), R108 (= R100), R137 (= R128), K194 (= K189), V197 (= V192), D226 (= D221), D250 (= D245)

1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
53% identity, 99% coverage: 2:350/354 of query aligns to 6:355/363 of 1cnzA

query
sites
1cnzA

K

H

I

I

C

A

V

V

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

T

M

A

A

E

Q

A

A

V

L

R

K

V

V

L

M

R

D

A

A

-

V

-

R

-

S

-

R

L

F

D

D

L

M

K

R

I

I

E

T

L

T

E

S

E

H

A

Y

L

D

L

V

G

G

S

I

A

A

V

I

D

D

A

N

T

H

G

G

T

H

P

P

Y

L

P

P

E

K

A

A

T

T

Q

V

K

E

L

G

A

C

R

E

A

Q

A

A

D

D

A

A

V

I

L

L

L

F

G

G

A

S

V

V

G

G

P

P

K

K

W

W

D

E

T

N

L

L

P

P

R

P

E

E

Q

S

R

Q

P

P

E

E

R

R

G

G

-

A

L

L

G

P

I

L

R

R

K

K

D

H

L

F

S

K

L

L

F

F

A

S

N

N

L

L

R

R

P

P

A

A

I

K

L

L

Y

Y

P

Q

E

G

L

L

A

E

N

A

A

F

S

C

T

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

D

G

I

I

Y
|
Y

F

F

G

G

Q

Q

P

P

R

K

G

G

I

-

E

-

T

-

R

R

E

E

V

G

N

S

G

G

A

-

Q

Q

Q

Y

R

E

V

K

G

A

W

F

N

D

T

T

M

E

I

V

Y

Y

A

H

E

R

Y

F

E

E

I

I

R

E

R

R

I

I

L

A

K

R

V

I

A

A

F

F

E

E

A

S

A

A

Q

R

K

K

R

R

G

R

K

R

K

K

L

V

C

T

S

S

V

I

D

D

K
|
K

M

A

N

N

V

V

L

L

E

Q

T

S

Q

I

L

L

W

W

R

R

D

E

I

I

A

V

D

N

E

D

M

V

A

A

K

K

D

T

F

Y

P

P

D

D

V

V

E

E

L

L

S

A

H

H

M

M

L

Y

V

I

D
|
D

N

N

A

A

A

T

M

M

Q

Q

L

L

V

I

R

K

N

D

P

P

K

S

Q

Q

F

F

D

D

V

V

M

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

E

E

A

C

S

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

A

E

N

Q

N

G

K

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

Y

Y

T

S

F

L

N

D

Q

A

E

N

E

D

A

A

V

T

R

A

I

I

E

E

R

Q

A

A

V

I

K

N

K

R

V

A

L

L

A

E

Q

E

G

G

F

V

R

R

T

T

G

G

D

D

I

L

Y

A

E

R

A

-

G

G

T

A

K

A

V

V

G

S

T

T

R

D

E

E

M

M

G

G

D

D

A

I

V

I

active site: Y145 (= Y135), K195 (= K189), D227 (= D221), D251 (= D245)
binding manganese (ii) ion: D251 (= D245), D255 (= D249)

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: 2:350/354 of query aligns to 6:355/363 of P37412

query
sites
P37412

K

H

I

I

C

A

V

V

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

T

M

A

A

E

Q

A

A

V

L

R

K

V

V

L

M

R

D

A

A

-

V

-

R

-

S

-

R

L

F

D

D

L

M

K

R

I

I

E

T

L

T

E

S

E

H

A

Y

L

D

L

V

G

G

S

I

A

A

V

I

D

D

A

N

T

H

G

G

T

H

P

P

Y

L

P

P

E

K

A

A

T

T

Q

V

K

E

L

G

A

C

R

E

A

Q

A

A

D

D

A

A

V

I

L

L

L

F

G

G

A

S

V

V

G

G

P

P

K

K

W

W

D

E

T

N

L

L

P

P

R

P

E

E

Q

S

R

Q

P

P

E

E

R

R

G

G

-

A

L

L

G

P

I

L

R

R

K

K

D

H

L

F

S

K

L

L

F

F

A

S

N

N

L

L

R

R

P

P

A

A

I

K

L

L

Y

Y

P

Q

E

G

L

L

A

E

N

A

A

F

S

C

T

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

D

G

I

I

Y

Y

F

F

G

G

Q

Q

P

P

R

K

G

G

I

-

E

-

T

-

R

R

E

E

V

G

N

S

G

G

A

-

Q

Q

Q

Y

R

E

V

K

G

A

W

F

N

D

T

T

M

E

I

V

Y

Y

A

H

E

R

Y

F

E

E

I

I

R

E

R

R

I

I

L

A

K

R

V

I

A

A

F

F

E

E

A

S

A

A

Q

R

K

K

R

R

G

R

K

R

K

K

L

V

C

T

S

S

V

I

D

D

K

K

M

A

N

N

V

V

L

L

E

Q

T

S

Q

I

L

L

W

W

R

R

D

E

I

I

A

V

D

N

E

D

M

V

A

A

K

K

D

T

F

Y

P

P

D

D

V

V

E

E

L

L

S

A

H

H

M

M

L

Y

V

I

D
|
D

N

N

A

A

A

T

M

M

Q

Q

L

L

V

I

R

K

N

D

P

P

K

S

Q

Q

F

F

D

D

V

V

M

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

E

E

A

C

S

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

A

E

N

Q

N

G

K

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

Y

Y

T

S

F

L

N

D

Q

A

E

N

E

D

A

A

V

T

R

A

I

I

E

E

R

Q

A

A

V

I

K

N

K

R

V

A

L

L

A

E

Q

E

G

G

F

V

R

R

T

T

G

G

D

D

I

L

Y

A

E

R

A

-

G

G

T

A

K

A

V

V

G

S

T

T

R

D

E

E

M

M

G

G

D

D

A

I

V

I

D227 (= D221) binding Mn(2+)
D251 (= D245) binding Mn(2+)
D255 (= D249) binding Mn(2+)

3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
53% identity, 100% coverage: 2:354/354 of query aligns to 10:366/369 of 3vmkA

query
sites
3vmkA

K

Q

I

I

C

A

V

V

L

L

P

A

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

T

M

A

A

E

E

A

A

V

R

R

K

V

V

L

L

R

A

A

A

-

V

-

E

-

K

-

R

L

F

D

D

L

L

K

S

I

I

E

E

L

Y

E

S

E

E

A

Y

L

D

L

V

G

G

S

A

A

A

V

I

D

D

A

N

T

H

G

G

T

C

P

P

Y

L

P

P

E

E

A

A

T

T

Q

L

K

K

L

G

A

C

R

E

A

A

D

D

A

A

V

V

L

L

L

F

G

G

A

S

V

V

G

G

P

P

K

K

W

W

D

E

T

H

L

L

P

P

R

P

E

N

Q

D

R

Q

P

P

E

E

R

R

G

G

-

A

L

L

G

P

I

L

R
|
R

K

G

D

H

L

F

S

E

L

L

F

F

A

C

N

N

L

M

R

R

P

P

A

A

I

K

L

L

Y

H

P

P

E

G

L

L

A

E

N

H

A

M

S

S

T

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

D

G

I

I

Y
|
Y

F

F

G

G

Q

K

P

P

R

K

G

G

I

-

E

-

T

-

R

R

E

Q

V

G

N

E

G

G

A

E

Q

N

Q

E

R

E

V

A

G

-

W

F

N

D

T

T

M

M

I

R

Y

Y

A

S

E

R

Y

K

E

E

I

I

R

R

I

I

L

A

K

K

V

I

A

A

F

F

E

E

A

S

A

A

Q

Q

K

G

R

R

G

R

K

K

L

V

C

T

S

S

V

V

D

D

K
|
K

M

A

N
|
N

V

V

L

L

E

A

T

C

T

S

Q

V

L

L

W

W

R

R

D

E

I

V

A

V

D

E

E

E

M

V

A

A

K

K

D

D

F

Y

P

P

D

D

V

V

E

E

L

L

S

E

H

H

M

I

L

Y

V

I

D
|
D

N

N

A

A

A

T

M

M

Q

Q

L

L

V

L

R

R

N

R

P

P

K

N

Q

E

F

F

D

D

V

V

M

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

E

E

A

I

S

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

A

S

N

Q

N

G

K

F

G

G

L

M

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

Q

G

G

V

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

T

S

F

L

N

K

Q

L

E

E

E

D

A

A

V

L

R

A

I

I

E

E

R

A

A

A

V

V

K

S

K

K

V

A

L

L

A

S

Q

D

G

G

F

Y

R

L

T

T

G

C

D

E

I

L

Y

L

E

P

A

A

G

S

-

E

-

R

T

S

K

Q

K

A

V

K

G

S

T

T

R

S

E

Q

M

M

G

G

D

D

A

Y

V

I

L

A

A

Q

A

A

L

I

active site: Y149 (= Y135), K199 (= K189), D231 (= D221), D255 (= D245), D259 (= D249)
binding 3-isopropylmalic acid: R103 (= R90), R142 (= R128), Y149 (= Y135), K199 (= K189), N201 (= N191), D255 (= D245)

3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
53% identity, 100% coverage: 2:354/354 of query aligns to 4:360/364 of 3vkzA

query
sites
3vkzA

K

Q

I

I

C

A

V

V

L

L

P

A

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

T

M

A

A

E

E

A

A

V

R

R

K

V

V

L

L

R

K

A

A

L

V

D

E

-

A

-

R

-

F

-

G

L

L

K

N

I

I

E

E

L

Y

E

T

E

E

A

Y

L

D

L

V

G

G

S

I

A

A

V

I

D

D

A

N

T

H

G

G

T

C

P

P

Y

L

P

P

E

E

A

A

T

T

Q

L

K

K

L

G

A

C

R

E

A

A

D

D

A

A

V

I

L

L

L

F

G

G

A

S

V

V

G

G

P

P

K

K

W

W

D

E

T

K

L

L

P

P

R

P

E

N

Q

E

R

Q

P

P

E

E

R

R

G

G

-

A

L

L

G

P

I

L

R
|
R

K

G

D

H

L

F

S

E

L

L

F

F

A

C

N

N

L

L

R

R

P

P

A

A

I

K

L

L

Y

H

P

D

E

G

L

L

A

E

N

H

A

M

S

S

T

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

D

G

I

I

Y
|
Y

F

F

G

G

Q

K

P

P

R

K

G

G

I

-

E

-

T

-

R

R

E

Q

V

G

N

E

G

G

A

E

Q

S

Q

E

R

E

V

A

G

-

W

F

N

D

T

T

M

M

I

R

Y

Y

A

S

E

R

Y

R

E

E

I

I

R

S

R

R

I

I

L

A

K

R

V

I

A

A

F

F

E

E

A

A

Q

R

K

G

R

R

G

R

K

K

L

V

C

T

S

S

V

V

D

D

K
|
K

M

A

N

N

V

V

L

L

E

A

T

C

T

S

Q

V

L

L

W

W

R

R

D

Q

I

V

A

V

D

E

E

E

M

V

A

A

K

V

D

D

F

F

P

P

D

D

V

V

E

E

L

L

S

E

H

H

M

I

L

Y

V

I

D
|
D

N

N

A

A

A

T

M

M

Q

Q

L

L

V

L

R

R

N

R

P

P

K

D

Q

E

F

F

D

D

V

V

M

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

E

E

A

I

S

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

A

S

N

T

N

G

K

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

Y

H

T

S

F

L

N

K

Q

Q

E

E

A

A

V

S

R

A

I

I

E

E

R

R

A

A

V

V

K

T

K

K

V

A

L

L

A

N

Q

S

G

G

F

Y

R

L

T

T

G

G

D

E

I

L

Y

L

E

S

A

S

G

D

T

Q

K

R

K

H

V

K

G

A

-

K

-

T

T

T

R

V

E

Q

M

M

G

G

D

D

A

F

V

I

L

A

A

D

A

A

L

V

active site: Y143 (= Y135), K193 (= K189), D225 (= D221), D249 (= D245), D253 (= D249)
binding calcium ion: D249 (= D245), D253 (= D249)
binding 3-isopropylmalic acid: R97 (= R90), R136 (= R128), Y143 (= Y135), D249 (= D245)

2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
57% identity, 92% coverage: 1:326/354 of query aligns to 2:322/346 of 2y41A

query
sites
2y41A

M

M

K

K

I

V

C

A

V

V

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

T

T

A

E

E

A

A

A

V

L

R

K

V

V

L

L

R

R

A

A

L

L

D

D

-

E

-

A

-

E

-

G

L

L

K

G

I

L

E

A

L

Y

E

E

E

V

A

F

L

P

L

F

G

G

S

A

A

A

V

I

D

D

A

A

T

F

G

G

T

E

P

P

Y

F

P

P

E

E

A

P

T

T

Q

R

K

K

L

G

A

V

R

E

A

E

A

A

D

E

A

A

V

V

L

L

G

G

A

S

V

V

G

G

P

P

K

K

W

W

D

D

T

G

L

L

P

P

R

R

E

K

Q

I

R

R

P

P

E

E

R

T

G

G

L

L

G

S

I

L

R
|
R

K

K

D

S

L

Q

S

D

L

L

F

F

A

A

N

N

L

L

R
|
R

P

P

A

A

I

K

L

V

Y

F

P

P

E

G

L

L

A

E

N

R

A

L

S

S

T

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

D

G

I

I

Y
|
Y

F

F

G

G

Q

E

P

P

R

R

G

G

I

M

E

S

T

E

R

A

E

E

V

A

N

-

G

-

A

-

Q

-

R

-

V

-

G

-

W

W

N

N

T

T

M

E

I

R

Y

Y

A

S

E

K

Y

P

E

E

I

V

R

E

R

R

I

V

L

A

K

R

V

V

A

A

F

F

E

E

A

A

Q

R

K

K

R

R

G

R

K

K

K

H

L

V

C

V

S

S

V

V

D

D

K
|
K

M

A

N

N

V

V

L

L

E

E

T

V

T

G

Q

E

L

F

W

W

R

R

D

K

I

T

A

V

D

E

E

E

M

V

A

G

K

R

D

G

F

Y

P

P

D

D

V

V

E

A

L

L

S

E

H

H

M

Q

L

Y

V

V

D
|
D

N

A

A

M

A

A

M

M

Q

H

L

L

V

V

R

R

N

S

P

P

K

A

Q

R

F

F

D

D

V

V

M

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

E

L

A

A

S

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

A

R

N

G

N

T

K

P

G

-

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

Y

H

T

A

F

F

N

G

Q

L

E

V

E

E

A

L

A

A

V

R

R

K

I

V

E

E

R

D

A

A

V

V

K

A

K

K

V

A

L

L

A

L

Q

E

active site: Y140 (= Y135), K186 (= K189), D218 (= D221), D242 (= D245), D246 (= D249)
binding 3-isopropylmalic acid: R95 (= R90), R105 (= R100), R133 (= R128), Y140 (= Y135), D242 (= D245)

2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
57% identity, 92% coverage: 1:326/354 of query aligns to 1:321/345 of 2ztwA

query
sites
2ztwA

M

M

K

K

I

V

C

A

V

V

L

L

P

P

G

G

D

D

G

G

I
|
I

G

G

P

P

E

E

I

V

T

T

A

E

E

A

A

A

V

L

R

K

V

V

L

L

R

R

A

A

L

L

D

D

-

E

-

A

-

E

-

G

L

L

K

G

I

L

E

A

L

Y

E

E

E

V

A

F

L

P

L

F

G

G

S

A

A

A

V

I

D

D

A

A

T

F

G

G

T

E

P

P

Y

F

P

P

E

E

A

P

T

T

Q

R

K

K

L

G

A

V

R

E

A

E

A

A

D

E

A

A

V

V

L

L

G

G

A

S

V

V

G

G

P

P

K

K

W

W

D

D

T

G

L

L

P

P

R

R

E

K

Q

I

R

R

P

P

E

E

R

T

G

G

L

L

G

S

I

L

R

R

K

K

D

S

L

Q

S

D

L

L

F

F

A

A

N

N

L

L

R

R

P

P

A

A

I

K

L

V

Y

F

P

P

E

G

L

L

A

E

N

R

A

L

S

S

T

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

D

G

I

I

Y
|
Y

F

F

G

G

Q

E

P

P

R

R

G

G

I

M

E

S

T

E

R

A

E

E

V

A

N

-

G

-

A

-

Q

-

R

-

V

-

G

-

W

W

N

N

T

T

M

E

I

R

Y

Y

A

S

E

K

Y

P

E

E

I

V

R

E

R

R

I

V

L

A

K

R

V

V

A

A

F

F

E

E

A

A

Q

R

K

K

R

R

G

R

K

K

K

H

L

V

C

V

S

S

V

V

D

D

K
|
K

M

A

N

N

V

V

L

L

E

E

T

V

T

G

Q

E

L

F

W

W

R

R

D

K

I

T

A

V

D

E

E

E

M

V

A
x
G

K

R

D

G

F
x
Y

P

P

D

D

V
|
V

E

A

L

L

S

E

H

H

M

Q

L

Y

V

V

D
|
D

N

A

A

M

A

A

M

M

Q

H

L

L

V

V

R

R

N

S

P

P

K

A

Q

R

F

F

D

D

V

V

M

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

E

L

A

A

S

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

-

A

G

N

R

N

G

K

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

Y

H

T

A

F

F

N

G

Q

L

E

V

E

E

A

L

A

A

V

R

R

K

I

V

E

E

R

D

A

A

V

V

K

A

K

K

V

A

L

L

A

L

Q

E

active site: Y139 (= Y135), K185 (= K189), D217 (= D221), D241 (= D245), D245 (= D249)
binding magnesium ion: G203 (≠ A207), Y206 (≠ F210), V209 (= V213)
binding nicotinamide-adenine-dinucleotide: I11 (= I11), H273 (= H278), G274 (= G279), A276 (= A281), D278 (= D283), I279 (= I284), A285 (= A290), N286 (= N291)

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)
57% identity, 92% coverage: 1:326/354 of query aligns to 1:321/345 of Q5SIY4

query
sites
Q5SIY4

M

M

K

K

I

V

C

A

V

V

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

T

T

A

E

E

A

A

A

V

L

R

K

V

V

L

L

R

R

A

A

L

L

D

D

-

E

-

A

-

E

-

G

L

L

K

G

I

L

E

A

L

Y

E

E

E

V

A

F

L

P

L

F

G

G

S

A

A

A

V

I

D

D

A

A

T

F

G

G

T

E

P

P

Y

F

P

P

E

E

A

P

T

T

Q

R

K

K

L

G

A

V

R

E

A

E

A

A

D

E

A

A

V

V

L

L

G

G

A

S

V

V

G

G

G
|
G

P
|
P

K
|
K

W
|
W

D
|
D

T
x
G

L
|
L

P
|
P

R
|
R

E
x
K

Q
x
I

R
|
R

P
|
P

E
|
E

R

T

G

G

L

L

G

S

I

L

R

R

K

K

D

S

L

Q

S

D

L

L

F

F

A

A

N

N

L

L

R

R

P

P

A

A

I

K

L

V

Y

F

P

P

E

G

L

L

A

E

N

R

A

L

S

S

T

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

D

G

I

I

Y
|
Y

F

F

G

G

Q

E

P

P

R

R

G

G

I

M

E

S

T

E

R

A

E

E

V

A

N

-

G

-

A

-

Q

-

R

-

V

-

G

-

W

W

N

N

T

T

M

E

I

R

Y

Y

A

S

E

K

Y

P

E

E

I

V

R

E

R

R

I

V

L

A

K

R

V

V

A

A

F

F

E

E

A

A

Q

R

K

K

R

R

G

R

K

K

K

H

L

V

C

V

S

S

V

V

D

D

K

K

M

A

N

N

V

V

L

L

E

E

T

V

T

G

Q

E

L

F

W

W

R

R

D

K

I

T

A

V

D

E

E

E

M

V

A

G

K

R

D

G

F

Y

P

P

D

D

V

V

E

A

L

L

S

E

H

H

M

Q

L

Y

V

V

D

D

N

A

A

M

A

A

M

M

Q

H

L

L

V

V

R

R

N

S

P

P

K

A

Q

R

F

F

D

D

V

V

M

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

E

L

A

A

S

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

-

A

G

N

R

N

G

K

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

Y

H

T

A

F

F

N

G

Q

L

E

V

E

E

A

L

A

A

V

R

R

K

I

V

E

E

R

D

A

A

V

V

K

A

K

K

V

A

L

L

A

L

Q

E

74:87 (vs. 70:83, 79% identical) binding NAD(+)
Y139 (= Y135) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
274:286 (vs. 279:291, 92% identical) binding NAD(+)

2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
57% identity, 92% coverage: 1:326/354 of query aligns to 2:322/355 of 2y42D

query
sites
2y42D

M

M

K

K

I

V

C

A

V

V

L

L

P

P

G

G

D

D

G

G

I
|
I

G

G

P

P

E

E

I

V

T

T

A

E

E

A

A

A

V

L

R

K

V

V

L

L

R

R

A

A

L

L

D

D

-

E

-

A

-

E

-

G

L

L

K

G

I

L

E

A

L

Y

E

E

E

V

A

F

L

P

L

F

G

G

S

A

A

A

V

I

D

D

A

A

T

F

G

G

T

E

P

P

Y

F

P

P

E

E

A

P

T

T

Q

R

K

K

L

G

A

V

R

E

A

E

A

A

D

E

A

A

V

V

L

L

G

G

A

S

V

V

G

G

P

P

K

K

W

W

D
|
D

T

G

L

L

P

P

R

R

E

K

Q

I

R

R

P

P

E

E

R

T

G

G

L

L

G

S

I

L

R

R

K

K

D

S

L

Q

S

D

L

L

F

F

A

A

N

N

L

L

R

R

P

P

A

A

I

K

L

V

Y

F

P

P

E

G

L

L

A

E

N

R

A

L

S

S

T

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

D

G

I

I

Y
|
Y

F

F

G

G

Q

E

P

P

R

R

G

G

I

M

E

S

T

E

R

A

E

E

V

A

N

-

G

-

A

-

Q

-

R

-

V

-

G

-

W

W

N

N

T

T

M

E

I

R

Y

Y

A

S

E

K

Y

P

E

E

I

V

R

E

R

R

I

V

L

A

K

R

V

V

A

A

F

F

E

E

A

A

Q

R

K

K

R

R

G

R

K

K

K

H

L

V

C

V

S

S

V

V

D

D

K
|
K

M

A

N

N

V

V

L

L

E

E

T

V

T

G

Q

E

L

F

W

W

R

R

D

K

I

T

A

V

D

E

E

E

M

V

A

G

K

R

D

G

F

Y

P

P

D

D

V

V

E

A

L

L

S

E

H

H

M

Q

L

Y

V

V

D
|
D

N

A

A

M

A

A

M

M

Q

H

L

L

V

V

R

R

N

S

P

P

K

A

Q

R

F

F

D

D

V

V

M

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

E

L

A

A

S

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

A

R

N

G

N

T

K

P

G

-

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

Y

H

T

A

F

F

N

G

Q

L

E

V

E

E

A

L

A

A

V

R

R

K

I

V

E

E

R

D

A

A

V

V

K

A

K

K

V

A

L

L

A

L

Q

E

active site: Y140 (= Y135), K186 (= K189), D218 (= D221), D242 (= D245), D246 (= D249)
binding manganese (ii) ion: D242 (= D245), D246 (= D249)
binding nicotinamide-adenine-dinucleotide: I12 (= I11), D79 (= D74), H274 (= H278), G275 (= G279), A277 (= A281), D279 (= D283), I280 (= I284), N287 (= N291)

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, 98% coverage: 2:347/354 of query aligns to 5:351/371 of P18869

query
sites
P18869

K

K

I

I

C

V

V

V

L

L

P

P

G

G

D

D

G

H

I

I

G

G

P

P

E

E

I

I

T

V

A

A

E

S

A

A

V

L

R

E

V

V

L

L

R

K

A

V

L

V

D

E

-

K

-

R

-

P

-

E

L

L

K

K

I

L

E

E

L

F

E

E

A

H

L

K

L

I

G

G

S

A

A

S

V

I

D

D

A

A

T

Y

G

G

T
|
T

P

P

Y

L

P

T

E

D

A

E

T

T

Q

V

K

K

L

A

A

C

R

L

A

E

A

A

D

D

A

G

V

V

L

L

G

G

A

A

V

V

G

G

P

P

K

E

W

W

D

-

T

T

L

N

P

P

R

N

E

-

Q

C

R

R

P

P

E

E

R

Q

G

G

L

L

G

K

I

L

R

R

K

K

D

S

L

M

S

G

L

V

F

W

A

A

N

N

L

L

R

R

P

P

A

C

-

N

I

F

L

A

Y

S

P

K

E

S

L

L

A

V

N

K

A

Y

S

S

T

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

D

G

I

C

Y

Y

F

F

G

G

Q

-

P

-

R

-

G

-

I

-

E

E

T

R

R

T

E

E

V

D

N

N

G

G

A

S

Q

G

Q

Y

R

A

V

M

G

-

W

-

N

D

T

T

M

W

I

P

Y

Y

A

S

E

L

Y

E

E

E

I

V

R

S

R

R

I

I

L

A

K

R

V

L

A

A

F

A

E

W

A

L

A

A

Q

E

K

T

R

S

G

N

K

P

-

A

-

P

L

V

C

T

S

L

V

L

D

D

K

K

M

A

N

N

V

V

L

L

E

A

T

T

T

S

Q

R

L

L

W

W

R

R

D

K

-

T

I

V

A

A

D

K

E

I

M

F

A

K

K

E

D

E

F

Y

P

P

D

H

V

L

E

T

L

L

S

K

H

N

M

Q

L

L

V

I

D

D

N

S

A

A

M

M

Q

L

L

L

V

V

R

K

N

S

P

P

K

R

Q

T

F

L

D

N

-

G

V

V

M

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

E

E

A

A

S

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

A

E

N

K

N

V

K

H

G

C

L

L

Y

V

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

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

Y

Y

T

G

F

L

N

N

Q

A

E

P

E

K

A

E

A

A

V

E

R

A

I

I

E

E

R

A

A

A

V

V

K

R

K

K

V

V

L

L

A

-

Q

-

G

-

F

-

R

-

T

-

G

-

D

D

I

D

Y

T

E

S

A

I

G

G

T

G

K

R

K

G

V

L

G

Y

T

T

R

R

E

D

M

L

G

G

T55 (= T47) modified: Phosphothreonine

2g4oA Anomalous substructure of 3-isopropylmalate dehydrogenase (see paper)
38% identity, 100% coverage: 2:354/354 of query aligns to 3:337/337 of 2g4oA

query
sites
2g4oA

K

K

I

L

C

A

V

I

L

I

P

A

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

T

T

A

A

E

E

A

A

V

V

R

K

V

V

L

L

R

D

A

A

L

V

D

V

L

P

K

G

I

V

E

Q

L

K

E

T

E

S

A

Y

L

D

L

L

G

G

G

A

S

R

A

R

V

F

D

H

A

A

T

T

G

G

T
x
E

P

V

Y
x
L

P
|
P

E

D

A

S

T

V

Q

V

K

A

L

E

A

L

R

R

A

N

A

H

D

D

A

A

V

I

L

L

G

G

A

A

V

I

G

G

G

D

P

P

K

-

W

-

D

-

T

S

L

V

P

P

R

S

E

G

Q

V

R

L

P

E

E

R

R

G

G

L

L

L

G

R

I

L

R

R

K

F

D

E

L

L

S

D

L

H

F

H

A

I

N

N

L

L

R

R

P

P

A

A

I

R

L

L

Y

Y

P

P

E

G

L

V

A

A

N

S

A

P

S

L

T

S

L

G

K

N

P

P

E

-

V

-

S

-

G

G

L

I

D

D

I

F

L

V

I

V

V

V

R

R

E

E

L

G

T

T

G

E

D

G

I

P

Y
|
Y

F

T

G

G

Q

N

P

G

R

G

G

A

I

I

E

R

T

V

R

G

E

T

V

P

N

N

G

E

A

V

Q

A

Q

T

R

E

V

V

G

S

W

V

N

N

T

T

M

A

I

-

Y

-

A

-

E

-

Y

F

E

G

I

V

R

R

I

V

L

V

K

A

V

D

A

A

F

F

E

E

A

R

A

A

Q

R

K

R

R

R

G

R

K

K

K

H

L

L

C

T

S

L

V

V

D

H

K
|
K

M

T

N

N

V

V

L

L

E

T

-

F

T

A

T

G

Q

G

L

L

W

W

R

L

D

R

I

T

A

V

D

D

E

E

M

V

A

G

K

E

D

C

F

Y

P

P

D

D

V

V

E

E

L

V

S

A

H

Y

M

Q

L

H

V

V

D
|
D

N

A

A

A

A

T

M

I

Q

H

L

M

V

I

R

T

N

D

P

P

K

G

Q

R

F

F

D

D

V

V

M

I

V

V

T

T

G

D

N

N

M

L

F

F

G

G

D
|
D

I

I

L

I

S

T

D
|
D

E

L

A

A

S

A

M

A

L

V

T

C

G

G

S

G

I

I

G

G

M

L

L

A

P

A

S

S

A

G

S

N

L

I

D

D

A

A

N

T

-

R

-

A

N

N

K

P

G

S

L

M

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

Q

G

G

V

I

A

A

N

D

P

P

L

T

A

A

T

A

I

I

L

M

S

S

A

V

A

A

M

L

L

L

R

S

Y

H

T

-

F

L

N

G

Q

E

E

H

E

D

A

A

V

A

R

R

I

V

E

D

R

R

A

A

V

V

K

E

K

A

V

H

L

L

A

A

Q

T

G

-

F

-

R

-

T

-

G

-

D

-

I

-

Y

-

E

-

A

R

G

G

T

S

K

E

K

R

V

L

G

A

T

T

R

S

E

D

M

V

G

G

D

E

A

R

V

I

L

A

A

A

L

L

active site: Y129 (= Y135), K179 (= K189), D212 (= D221), D236 (= D245), D240 (= D249)
binding sulfate ion: E48 (≠ T47), L50 (≠ Y49), P51 (= P50)

Query Sequence

>WP_011764775.1 NCBI__GCF_000061505.1:WP_011764775.1
MKICVLPGDGIGPEITAEAVRVLRALDLKIELEEALLGGSAVDATGTPYPEATQKLARAA
DAVLLGAVGGPKWDTLPREQRPERGLLGIRKDLSLFANLRPAILYPELANASTLKPEVVS
GLDILIVRELTGDIYFGQPRGIETREVNGAQQRVGWNTMIYAEYEIRRILKVAFEAAQKR
GKKLCSVDKMNVLETTQLWRDIADEMAKDFPDVELSHMLVDNAAMQLVRNPKQFDVMVTG
NMFGDILSDEASMLTGSIGMLPSASLDANNKGLYEPSHGSAPDIAGKGVANPLATILSAA
MMLRYTFNQEEAAVRIERAVKKVLAQGFRTGDIYEAGTKKVGTREMGDAVLAAL

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