SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_011319729.1 NCBI__GCF_000204075.1:WP_011319729.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

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)
68% identity, 99% coverage: 3:360/362 of query aligns to 41:398/405 of P93832

query
sites
P93832

Q

K

N

R

Y

Y

R

T

I

I

T

T

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

M

V

A

S

V

I

A

A

V

K

D

N

V

V

L

L

K

Q

V

Q

V

A

G

G

Q

S

Q

L

F

E

D

G

I

V

Q

E

F

F

D

N

F

F

Q

R

E

E

A

M

L

P

I

I

G

G

A

A

I

L

D

D

A

L

T

V

G

G

E

V

P

P

L

L

P

P

S

E

A

E

T

T

L

I

D

S

T

A

C

A

R

K

Q

E

S

S

D

D

A

A

V

V

L

L

A

G

A

A

I
|
I

G
|
G

Y
|
Y

K
|
K

W
|
W

D
|
D

S
x
N

L
x
N

P
x
E

P
x
K

H
|
H

Q
x
L

R
|
R

P
|
P

E
|
E

G

K

G

G

L
|
L

G

Q

L

I

R
|
R

A

A

G

A

L

L

E

K

L

V

F

F

A

A

N

N

L

L

R
|
R

P

P

A

A

Q

T

I

V

L

L

P

P

Q

Q

L

L

I

V

D

D

A

A

S

S

T

T

L

L

K

K

R

R

E

E

V

V

V

A

E

E

G

G

V

V

D

D

I

L

M

M

V

V

R
|
R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

K

E

P

P

R

R

G

G

I

I

F

K

T

T

T

N

E

E

T

N

G

G

E

E

K

E

R

V

G

G

V

F

N

N

T

T

M

E

V

V

Y

Y

T

A

E

A

S

H

E

E

I

I

D

D

R

R

I

I

G

A

R

R

I

V

A

A

F

F

E

E

T

T

A

A

R

R

K

K

R

R

G

G

K

K

L

L

C

C

S

S

V

V

D

D

K
|
K

A

A

N
|
N

V
|
V

L

L

D

E

V

A

S

S

Q

I

L

L

W

W

R

R

D

K

R

R

I

V

T

T

K

A

L

L

S

A

Q

S

E

E

Y

Y

P

P

D

D

V

V

E

E

L

L

S

S

H

H

L

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

Q

Q

F

F

D

D

T

T

I

I

V

V

T

T

G

N

N

N

L

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

G

S

A

D

S

S

G

G

P

P

G

G

V

L

F

F

E
|
E

P
|
P

V
x
I

H
|
H

G
|
G

S
|
S

A
|
A

P
|
P

D
|
D

I
|
I

A
|
A

G
|
G

L
x
Q

D
|
D

K
|
K

A
|
A

N
|
N

P

P

L

L

A

A

Q

T

V

I

L

L

S

S

A

A

M

M

M

L

L

L

R

K

Y

Y

A

G

L

L

N

G

Q

E

P

E

Q

K

A

A

D

K

K

R

I

I

E

E

Q

D

A

A

V

V

L

L

Q

V

V

A

L

L

E

N

Q

N

G

G

D

F

R

R

T

T

G

G

D

D

I

I

M

Y

S

S

V

A

G

G

M

T

N

K

L

L

L

V

G

G

C

C

R

K

A

E

M

M

G

G

D

E

S

E

L

V

I

L

K

K

A

S

L

V

E

D

114:129 (vs. 76:91, 69% identical) binding NAD(+)
L132 (= L94) mutation to A: Reduced activity toward 3-isopropylmalate.
L133 (= L95) 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 (= R98) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
R146 (= R108) binding substrate; mutation to A: Reduced activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
R174 (= R136) binding substrate; mutation to A: Loss of activity toward 3-isopropylmalate.; mutation to K: Reduced activity toward 3-isopropylmalate.
Y181 (= Y143) Important for catalysis; mutation Y->A,F,H: Reduced activity toward 3-isopropylmalate.
K232 (= K194) Important for catalysis; mutation to M: Loss of activity toward 3-isopropylmalate.
N234 (= N196) binding NAD(+); mutation N->A,D: Loss of activity toward 3-isopropylmalate.
V235 (= V197) mutation to A: Reduced activity toward 3-isopropylmalate.
D264 (= D226) binding Mg(2+); binding substrate; mutation to N: Loss of activity toward 3-isopropylmalate.
N265 (= N227) binding NAD(+)
D288 (= D250) binding Mg(2+); mutation to N: Loss of activity toward 3-isopropylmalate.
D292 (= D254) binding Mg(2+); mutation to N: Reduced activity toward 3-isopropylmalate.
318:334 (vs. 280:296, 88% identical) binding NAD(+)

5j33A Isopropylmalate dehydrogenase in complex with NAD+ (see paper)
68% identity, 99% coverage: 3:360/362 of query aligns to 1:358/360 of 5j33A

query
sites
5j33A

Q

K

N

R

Y

Y

R

T

I

I

T

T

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

M

V

A

S

V

I

A

A

V

K

D

N

V

V

L

L

K

Q

V

Q

V

A

G

G

Q

S

Q

L

F

E

D

G

I

V

Q

E

F

F

D

N

F

F

Q

R

E

E

A

M

L

P

I

I

G

G

A

A

I

L

D

D

A

L

T

V

G

G

E

V

P

P

L

L

P

P

S

E

A

E

T

T

L

I

D

S

T

A

C

A

R

K

Q

E

S

S

D

D

A

A

V

V

L

L

A

G

A

A

I
|
I

G

G

Y

Y

K

K

W

W

D

D

S

N

L

N

P

E

P

K

H

H

Q

L

R

R

P

P

E
|
E

G

K

G

G

L
|
L

L

L

G

Q

L

I

R

R

A

A

G

A

L

L

E

K

L

V

F

F

A

A

N

N

L

L

R

R

P

P

A

A

Q

T

I

V

L

L

P

P

Q

Q

L

L

I

V

D

D

A

A

S

S

T

T

L

L

K

K

R

R

E

E

V

V

V

A

E

E

G

G

V

V

D

D

I

L

M

M

V

V

R

R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

K

E

P

P

R

R

G

G

I

I

F

K

T

T

T

N

E

E

T

N

G

G

E

E

K

E

R

V

G

G

V

F

N

N

T

T

M

E

V

V

Y

Y

T

A

E

A

S

H

E

E

I

I

D

D

R

R

I

I

G

A

R

R

I

V

A

A

F

F

E

E

T

T

A

A

R

R

K

K

R

R

G

G

K

K

L

L

C

C

S

S

V

V

D

D

K
|
K

A

A

N

N

V

V

L

L

D

E

V

A

S

S

Q

I

L

L

W

W

R

R

D

K

R

R

I

V

T

T

K

A

L

L

S

A

Q

S

E

E

Y

Y

P

P

D

D

V

V

E

E

L

L

S

S

H

H

L

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

Q

Q

F

F

D

D

T

T

I

I

V

V

T

T

G

N

N

N

L

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

G

S

A

D

S

S

G

G

P

P

G

G

V

L

F

F

E
|
E

P

P

V

I

H
|
H

G
|
G

S
|
S

A
|
A

P

P

D

D

I
|
I

A

A

G

G

L

Q

D

D

K

K

A

A

N
|
N

P

P

L

L

A

A

Q

T

V

I

L

L

S

S

A

A

M

M

M

L

L

L

R

K

Y

Y

A

G

L

L

N

G

Q

E

P

E

Q

K

A

A

D

K

K

R

I

I

E

E

Q

D

A

A

V

V

L

L

Q

V

V

A

L

L

E

N

Q

N

G

G

D

F

R

R

T

T

G

G

D
|
D

I

I

M

Y

S

S

V

A

G

G

M

T

N

K

L

L

L

V

G

G

C

C

R

K

A

E

M

M

G

G

D

E

S

E

L

V

I

L

K

K

A

S

L

V

E

D

active site: Y141 (= Y143), K192 (= K194), D224 (= D226), D248 (= D250), D252 (= D254)
binding magnesium ion: D248 (= D250), D252 (= D254)
binding nicotinamide-adenine-dinucleotide: I74 (= I76), E89 (= E91), L92 (= L94), I261 (= I263), E278 (= E280), H281 (= H283), G282 (= G284), S283 (= S285), A284 (= A286), I287 (= I289), N294 (= N296), D335 (= D337)

5j32A Isopropylmalate dehydrogenase in complex with isopropylmalate (see paper)
68% identity, 99% coverage: 3:360/362 of query aligns to 11:368/369 of 5j32A

query
sites
5j32A

Q

K

N

R

Y

Y

R

T

I

I

T

T

L

L

L
|
L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

M

V

A

S

V

I

A

A

V

K

D

N

V

V

L

L

K

Q

V

Q

V

A

G

G

Q

S

Q

L

F

E

D

G

I

V

Q

E

F

F

D

N

F

F

Q

R

E

E

A

M

L

P

I

I

G

G

A

A

I

L

D

D

A

L

T

V

G

G

E

V

P

P

L

L

P

P

S

E

A

E

T

T

L

I

D

S

T

A

C

A

R

K

Q

E

S

S

D

D

A

A

V

V

L

L

A

G

A

A

I

I

G

G

Y

Y

K

K

W

W

D

D

S

N

L

N

P

E

P

K

H

H

Q

L

R

R

P

P

E

E

G

K

G

G

L

L

G

Q

L

I

R
|
R

A

A

G

A

L

L

E

K

L

V

F

F

A

A

N

N

L

L

R

R

P

P

A

A

Q

T

I

V

L

L

P

P

Q

Q

L

L

I

V

D

D

A

A

S

S

T

T

L

L

K

K

R

R

E

E

V

V

V

A

E

E

G

G

V

V

D

D

I

L

M

M

V

V

R
|
R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

K

E

P

P

R

R

G

G

I

I

F

K

T

T

T

N

E

E

T

N

G

G

E

E

K

E

R

V

G

G

V

F

N

N

T

T

M

E

V

V

Y

Y

T

A

E

A

S

H

E

E

I

I

D

D

R

R

I

I

G

A

R

R

I

V

A

A

F

F

E

E

T

T

A

A

R

R

K

K

R

R

G

G

K

K

L

L

C

C

S

S

V

V

D

D

K
|
K

A

A

N

N

V

V

L

L

D

E

V

A

S

S

Q

I

L

L

W

W

R

R

D

K

R

R

I

V

T

T

K

A

L

L

S

A

Q

S

E

E

Y

Y

P

P

D

D

V

V

E

E

L

L

S

S

H

H

L

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

Q

Q

F

F

D

D

T

T

I

I

V

V

T

T

G

N

N

N

L

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

G

S

A

D

S

S

G

G

P

P

G

G

V

L

F

F

E

E

P

P

V

I

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

L

Q

D

D

K

K

A

A

N

N

P

P

L

L

A

A

Q

T

V

I

L

L

S

S

A

A

M

M

M

L

L

L

R

K

Y

Y

A

G

L

L

N

G

Q

E

P

E

Q

K

A

A

D

K

K

R

I

I

E

E

Q

D

A

A

V

V

L

L

Q

V

V

A

L

L

E

N

Q

N

G

G

D

F

R

R

T

T

G

G

D

D

I

I

M

Y

S

S

V

A

G

G

M

T

N

K

L

L

L

V

G

G

C

C

R

K

A

E

M

M

G

G

D

E

S

E

L

V

I

L

K

K

A

S

L

V

E

D

active site: L18 (= L10), Y151 (= Y143), K202 (= K194), D234 (= D226), D258 (= D250), D262 (= D254)
binding 3-isopropylmalic acid: R106 (= R98), R144 (= R136), Y151 (= Y143), D258 (= D250)
binding magnesium ion: D258 (= D250), D262 (= D254)

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)
67% identity, 99% coverage: 1:360/362 of query aligns to 40:399/404 of Q9SA14

query
sites
Q9SA14

M

V

T

K

Q

K

N

R

Y

Y

R

N

I

I

T

T

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

M

I

A

S

V

V

A

A

V

K

D

N

V

V

L

L

K

Q

V

K

V

A

G

G

Q

F

Q

L

F

Q

D

G

I

L

Q

E

F

F

D

D

F

F

Q

Q

E

E

A

M

L

P

I

F

G

G

A

A

I

L

D

D

A

L

T

V

G

G

E

V

P

P

L

L

P

P

S

E

A

E

T

T

L

S

D

T

T

A

C

A

R

K

Q

Q

S

S

D

D

A

A

V

I

L

L

A

G

A

A

I

I

G

G

Y

Y

K

K

W

W

D

D

S

K

L

N

P

E

P

K

H

H

Q

L

R

R

P

P

E

E

G

M

G

G

L

L

L
|
L

G

N

L

I

R

R

A

R

G

D

L

L

E

N

L

V

F

F

A

A

N

N

L

L

R

R

P

P

A

A

Q

T

I

V

L

L

P

P

Q

Q

L

L

I

V

D

D

A

A

S

S

T

T

L

L

K

K

R

K

E

E

V

V

V

A

E

Q

G

G

V

V

D

D

I

M

M

M

V

I

V

V

R

R

E

E

L

L

T

T

G

G

I

I

Y

Y

F

F

G

G

K

E

P

P

R

R

G

G

I

I

F

T

T

I

T

N

E

E

T

N

G

G

E

E

K

E

R

V

G

G

V

F

N

N

T

T

M

E

V

I

Y

Y

T

A

E

A

S

H

E

E

I

I

D

D

R

R

I

I

G

A

R

R

I

V

A

A

F

F

E

E

T

T

A

A

R

R

K

K

R

R

G

G

K

K

L

L

C

C

S

S

V

V

D

D

K

K

A

A

N

N

V

V

L

L

D

D

V

A

S

S

Q

I

L

L

W

W

R

R

D

K

R

R

I

V

T

T

K

A

L

L

S

A

Q

S

E

E

Y

Y

P

P

D

D

V

V

E

E

L

L

S

S

H

H

L

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

Q

Q

F

F

D

D

T

T

I

I

V

V

T

T

G

N

N

N

L

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

G

G

A

E

S

S

G

G

P

P

G

G

V

L

F

F

E

E

P

P

V

I

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

L

Q

D

D

K

K

A

A

N

N

P

P

L

L

A

A

Q

T

V

I

L

L

S

S

A

A

M

M

M

L

L

L

R

K

Y

Y

A

G

L

L

N

G

Q

E

P

E

Q

K

A

A

D

K

K

M

I

I

E

E

Q

D

A

A

V

V

L

V

Q

D

V

A

L

L

E

N

Q

K

G

G

D

F

R

R

T

T

G

G

D

D

I

I

M

Y

S

S

V

P

G

G

M

N

N

K

L

L

L

V

G

G

C

C

R

K

A

E

M

M

G

G

D

E

S

E

L

V

I

L

K

K

A

S

L

V

E

D

L134 (= L95) 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)
66% identity, 99% coverage: 3:360/362 of query aligns to 45:402/409 of Q9FMT1

query
sites
Q9FMT1

Q

K

N

R

Y

Y

R

N

I

I

T

A

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

M

I

A

S

V

V

A

A

V

K

D

N

V

V

L

L

K

Q

V

K

V

A

G

G

Q

S

Q

L

F

E

D

G

I

L

Q

E

F

F

D

D

F

F

Q

K

E

E

A

M

L

P

I

V

G

G

A

A

I

L

D

D

A

L

T

V

G

G

E

V

P

P

L

L

P

P

S

E

A

E

T

T

L

F

D

T

T

A

C

A

R

K

Q

L

S

S

D

D

A

A

V

I

L

L

A

G

A

A

I

I

G

G

Y

Y

K

K

W

W

D

D

S

K

L

N

P

E

P

K

H

H

Q

L

R

R

P

P

E

E

G

M

G

A

L

L

L
x
F

G

Y

L

L

R

R

A

R

G

D

L

L

E

K

L

V

F

F

A

A

N

N

L

L

R

R

P

P

A

A

Q

T

I

V

L

L

P

P

Q

Q

L

L

I

V

D

D

A

A

S

S

T

T

L

L

K

K

R

K

E

E

V

V

V

A

E

E

G

G

V

V

D

D

I

M

M

M

V

I

V

V

R

R

E

E

L

L

T

T

G

G

I

I

Y

Y

F

F

G

G

K

E

P

P

R

R

G

G

I

I

F

T

T

I

T

N

E

E

T

N

G

G

E

E

K

E

R

V

G

G

V

V

N

S

T

T

M

E

V

I

Y

Y

T

A

E

A

S

H

E

E

I

I

D

D

R

R

I

I

G

A

R

R

I

V

A

A

F

F

E

E

T

T

A

A

R

R

K

K

R

R

G

G

K

K

L

L

C
|
C

S

S

V

V

D

D

K

K

A

A

N

N

V

V

L

L

D

D

V

A

S

S

Q

I

L

L

W

W

R

R

D

K

R

R

I

V

T

T

K

A

L

L

S

A

Q

S

E

E

Y

Y

P

P

D

D

V

V

E

E

L

L

S

S

H

H

L

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

Q

Q

F

F

D

D

T

T

I

I

V

V

T

T

G

N

N

N

L

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

G

G

A

E

S

S

G

G

P

P

G

G

V

L

F

F

E

E

P

P

V

I

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

L

Q

D

D

K

K

A

A

N

N

P

P

L

L

A

A

Q

T

V

I

L

L

S

S

A

A

M

M

M

L

L

L

R

K

Y

Y

A

G

L

L

N

G

Q

E

P

E

Q

K

A

A

D

K

K

R

I

I

E

E

Q

D

A

A

V

V

L

V

Q

D

V

A

L

L

E

N

Q

K

G

G

D

F

R

R

T

T

G

G

D

D

I

I

M

Y

S

S

V

P

G

G

M

N

N

K

L

L

L

V

G

G

C
|
C

R

K

A

E

M

M

G

G

D

E

S

E

L

V

I

L

K

K

A

S

L

V

E

E

F137 (≠ L95) Confers substrate specificity; mutation to L: Reduced activity toward 3-(2'-methylthio)-ethylmalate, but enhanced catalytic efficiency with 3-isopropylmalate.
C232 (= C190) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.
C390 (= C348) Essential for redox regulation; mutation to S: Reduced sensitivity to oxidation on enzyme activity regulation.

1a05A Crystal structure of the complex of 3-isopropylmalate dehydrogenase from thiobacillus ferrooxidans with 3-isopropylmalate (see paper)
59% identity, 98% coverage: 6:360/362 of query aligns to 3:355/357 of 1a05A

query
sites
1a05A

R

K

I

I

T

A

L

I

L

F

P

A

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

I

M

V

A

A

V

A

A

A

V

R

D

Q

V

V

L

L

K

D

V

A

V

V

G

D

Q

Q

Q

A

F

A

D

H

I

L

Q

G

F

L

D

R

F

C

Q

T

E

E

A

G

L

L

I

V

G

G

A

A

I

L

D

D

A

A

T

S

G

D

E

D

P

P

L

L

P

P

S

A

A

A

T

S

L

L

D

Q

T

L

C

A

R

M

Q

A

S

A

D

D

A

A

V

V

L

I

L

L

A

G

A

A

I

V

G

G

Y

P

K

R

W

W

D

D

S

A

L

Y

P

P

H

A

Q

K

R

R

P

P

E

E

G

Q

G

G

L

L

G

R

L

L

R
|
R

A

K

G

G

L

L

E

D

L

L

F

Y

A

A

N

N

L

L

R
|
R

P

P

A

A

Q

Q

I

I

L

F

P

P

Q

Q

L

L

I

L

D

D

A

A

S

S

T

P

L

L

K

R

R

P

E

E

V

L

V

V

E

R

G

D

V

V

D

D

I

I

M

L

V

V

R
|
R

E

E

L

L

T

T

G

G

G

D

I

I

Y
|
Y

F

F

G

G

K

Q

P

P

R

R

G

G

I

L

F

E

T

V

T

I

E

D

T

-

G

G

E

K

K

R

R

R

G

G

V

F

N

N

T

T

M

M

V

V

Y

Y

T

D

E

E

S

D

E

E

I

I

D

R

R

R

I

I

G

A

R

H

I

V

A

A

F

F

E

R

T

A

A

A

R

Q

K

G

R

R

G

K

K

Q

L

L

C

C

S

S

V

V

D

D

K
|
K

A

A

N

N

V

V

L

L

D

E

V

T

S

T

Q

R

L

L

W

W

R

R

D

E

R

V

I

V

T

T

K

E

L

V

S

A

Q

R

E

D

Y

Y

P

P

D

D

V

V

E

R

L

L

S

S

H

H

L

M

Y

Y

V

V

D
|
D

N

N

A

A

M

M

Q

Q

L

L

V

I

R

R

A

A

P

P

K

A

Q

Q

F

F

D

D

T

V

I

L

V

L

T

T

G

G

N

N

L

M

F

F

G

G

D
|
D

I

I

L

L

S

S

D
|
D

A

E

A

A

A

S

M

Q

L

L

T

T

G

G

S

S

I

I

G

G

M

M

L

L

P

P

S

S

A

A

S

S

L

L

G

G

A

-

S

E

G

G

P

R

G

A

V

M

F

Y

E

E

P

P

V

I

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

L

Q

D

D

K

K

A

A

N

N

P

P

L

L

A

A

Q

T

V

I

L

L

S

S

A

V

A

A

M

M

L

L

R

R

Y

H

A

S

L

L

N

N

Q

A

P

E

Q

P

A

W

A

A

D

Q

K

R

I

V

E

E

Q

A

A

A

V

V

L

Q

Q

R

V

V

L

L

E

D

Q

Q

G

G

D

L

R

R

T

T

G

A

D

D

I

I

M

A

S

A

V

P

G

G

M

T

N

P

L

V

L

I

G

G

C

T

R

K

A

A

M

M

G

G

D

A

S

A

L

V

I

V

K

N

A

A

L

L

E

N

active site: Y140 (= Y143), K190 (= K194), D222 (= D226), D246 (= D250), D250 (= D254)
binding 3-isopropylmalic acid: R95 (= R98), R105 (= R108), R133 (= R136), Y140 (= Y143), D246 (= D250)

Q56268 3-isopropylmalate dehydrogenase; 3-IPM-DH; Beta-IPM dehydrogenase; IMDH; EC 1.1.1.85 from Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans) (see paper)
59% identity, 98% coverage: 6:360/362 of query aligns to 3:355/358 of Q56268

query
sites
Q56268

R

K

I

I

T

A

L

I

L

F

P

A

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

I

M

V

A

A

V

A

A

A

V

R

D

Q

V

V

L

L

K

D

V

A

V

V

G

D

Q

Q

Q

A

F

A

D

H

I

L

Q

G

F

L

D

R

F

C

Q

T

E

E

A

G

L

L

I

V

G

G

A

A

I

L

D

D

A

A

T

S

G

D

E

D

P

P

L

L

P

P

S

A

A

A

T

S

L

L

D

Q

T

L

C

A

R

M

Q

A

S

A

D

D

A

A

V

V

L

I

L

L

A

G

A

A

I

V

G

G

Y

P

K

R

W

W

D

D

S

A

L

Y

P

P

H

A

Q

K

R

R

P

P

E

E

G

Q

G

G

L

L

G

R

L

L

R
|
R

A

K

G

G

L

L

E

D

L

L

F

Y

A

A

N

N

L

L

R
|
R

P

P

A

A

Q

Q

I

I

L

F

P

P

Q

Q

L

L

I

L

D

D

A

A

S

S

T

P

L

L

K

R

R

P

E

E

V

L

V

V

E

R

G

D

V

V

D

D

I

I

M

L

V

V

R
|
R

E

E

L

L

T

T

G

G

G

D

I

I

Y

Y

F

F

G

G

K

Q

P

P

R

R

G

G

I

L

F

E

T

V

T

I

E

D

T

-

G

G

E

K

K

R

R

R

G

G

V

F

N

N

T

T

M

M

V

V

Y

Y

T

D

E

E

S

D

E

E

I

I

D

R

R

R

I

I

G

A

R

H

I

V

A

A

F

F

E

R

T

A

A

A

R

Q

K

G

R

R

G

K

K

Q

L

L

C

C

S

S

V

V

D

D

K

K

A

A

N

N

V

V

L

L

D

E

V

T

S

T

Q

R

L

L

W

W

R

R

D

E

R

V

I

V

T

T

K

E

L

V

S

A

Q

R

E

D

Y

Y

P

P

D

D

V

V

E

R

L

L

S

S

H

H

L

M

Y

Y

V

V

D
|
D

N

N

A

A

M

M

Q

Q

L

L

V

I

R

R

A

A

P

P

K

A

Q

Q

F

F

D

D

T

V

I

L

V

L

T

T

G

G

N

N

L

M

F

F

G

G

D
|
D

I

I

L

L

S

S

D

D

A

E

A

A

A

S

M

Q

L

L

T

T

G

G

S

S

I

I

G

G

M

M

L

L

P

P

S

S

A

A

S

S

L

L

G

G

A

-

S

E

G

G

P

R

G

A

V

M

F

Y

E

E

P

P

V

I

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

L

Q

D

D

K

K

A

A

N

N

P

P

L

L

A

A

Q

T

V

I

L

L

S

S

A

V

A

A

M

M

L

L

R

R

Y

H

A

S

L

L

N

N

Q

A

P

E

Q

P

A

W

A

A

D

Q

K

R

I

V

E

E

Q

A

A

A

V

V

L

Q

Q

R

V

V

L

L

E

D

Q

Q

G

G

D

L

R

R

T

T

G

A

D

D

I

I

M

A

S

A

V

P

G

G

M

T

N

P

L

V

L

I

G

G

C

T

R

K

A

A

M

M

G

G

D

A

S

A

L

V

I

V

K

N

A

A

L

L

E

N

R95 (= R98) binding substrate
R105 (= R108) binding substrate
R133 (= R136) binding substrate
D222 (= D226) binding Mg(2+); binding substrate
D246 (= D250) binding Mg(2+)

4iwhA Crystal structure of a 3-isopropylmalate dehydrogenase from burkholderia pseudomallei
58% identity, 99% coverage: 3:359/362 of query aligns to 2:358/358 of 4iwhA

query
sites
4iwhA

Q

H

N

H

Y

M

R

K

I

I

T

A

L

V

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

I

M

V

A

N

V

E

A

A

V

V

D

K

V

V

L

L

K

N

V

A

V

L

G

-

Q

-

F

-

D

D

I

E

Q

K

F

F

D

E

F

L

Q

E

E

H

A

A

L

P

I

V

G

G

A

A

A

G

I

Y

D

E

A

A

T

S

G

G

E

H

P

P

L

L

P

P

S

D

A

A

T

T

L

L

D

A

T

L

C

A

R

K

Q

E

S

A

D

D

A

A

V

I

L

L

L

F

A

G

A

A

I

V

G

G

G

D

Y

W

K

K

W

Y

D

D

S

S

L

L

P

E

P

R

H

A

Q

L

R

R

P

P

E

E

G

Q

G

A

L

I

L

L

G

G

L

L

R

R

A

K

G

H

L

L

E

E

L

L

F

F

A

A

N

N

L

F

R

R

P

P

A

A

Q

I

I

C

L

Y

P

P

Q

Q

L

L

I

V

D

D

A

A

S

S

T

P

L

L

K

K

R

P

E

E

V

L

V

V

E

A

G

G

V

L

D

D

I

I

M

L

V

I

V

V

R

R

E

E

L

L

T

N

G

G

G

D

I

I

Y
|
Y

F

F

G

G

K

Q

P

P

R

R

G

G

I

V

F

R

T

A

E

P

-

D

-

G

-

P

-

F

T

A

G

G

E

E

K

R

R

E

G

G

V

F

N

D

T

T

M

M

V

R

Y

Y

T

S

E

E

S

P

E

E

I

V

D

R

R

R

I

I

G

A

R

H

I

V

A

A

F

F

E

Q

T

A

A

A

R

Q

K

K

R

R

R

A

G

K

K

K

L

L

C

L

S

S

V

V

D

D

K
|
K

A

S

N

N

V

V

L

L

D

E

V

T

S

S

Q

Q

L

F

W

W

R

R

D

D

R

V

I

M

T

I

K

D

L

V

S

S

Q

K

E

E

Y

Y

P

A

D

D

V

V

E

E

L

L

S

S

H

H

L

M

Y

Y

V

V

D
|
D

N

N

A

A

M

M

Q

Q

L

L

V

A

R

K

A

A

P

P

K

K

Q

Q

F

F

D

D

T

V

I

I

V

V

T

T

G

G

N

N

L

M

F

F

G

G

D
|
D

I

I

L

L

S

S

D
|
D

A

E

A

A

A

S

M

M

L

L

T

T

G

G

S

S

I

I

G

G

M

M

L

L

P

P

S

S

A

A

S

S

L

L

G

D

A

K

S

N

G

N

P

K

G

G

V

L

F

Y

E

E

P

P

V

S

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

L

K

D

G

K

I

A

A

N

N

P

P

L

L

A

A

Q

T

V

I

L

L

S

S

A

A

M

M

M

L

L

L

R

R

Y

Y

A

S

L

L

N

N

Q

R

P

A

Q

E

A

Q

A

A

D

D

K

R

I

I

E

E

Q

R

A

A

V

V

L

K

Q

T

V

V

L

L

E

E

Q

Q

G

G

D

Y

R

R

T

T

G

G

D

D

I

I

M

A

S

T

V

P

G

G

M

C

N

R

L

Q

L

V

G

G

C

T

R

A

A

A

M

M

G

G

D

D

S

A

L

V

I

V

K

A

A

A

L

L

active site: Y138 (= Y143), K193 (= K194), D225 (= D226), D249 (= D250), D253 (= D254)
binding magnesium ion: D249 (= D250), D253 (= D254)

4xxvA Crystal structure of 3-isopropylmalate dehydrogenase from burkholderia thailandensis in complex with NAD
58% identity, 98% coverage: 4:359/362 of query aligns to 1:356/356 of 4xxvA

query
sites
4xxvA

N

H

Y

M

R

K

I

I

T

A

L

V

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

I

M

V

A

N

V

E

A

A

V

V

D

K

V

V

L

L

K

N

V

A

V

L

G

-

Q

-

F

-

D

D

I

E

Q

K

F

F

D

E

F

L

Q

E

E

H

A

A

L

P

I

V

G

G

A

A

A

G

I

Y

D

E

A

A

T

S

G

G

E

H

P

P

L

L

P

P

S

D

A

A

T

T

L

L

D

A

T

L

C

A

R

K

Q

E

S

A

D

D

A

A

V

I

L

L

L

F

A

G

A

A

I

V

G

G

G

D

Y

W

K

K

W

Y

D

D

S

S

L

L

P

E

P

R

H

A

Q

L

R

R

P

P

E

E

G

Q

G

A

L

I

L

L

G

G

L

L

R

R

A

K

G

H

L

L

E

E

L

L

F

F

A

A

N

N

L

F

R

R

P

P

A

A

Q

I

I

C

L

Y

P

P

Q

Q

L

L

I

V

D

D

A

A

S

S

T

P

L

L

K

K

R

P

E

E

V

L

V

V

E

A

G

G

V

L

D

D

I

I

M

L

V

I

V

V

R

R

E

E

L

L

T

N

G

G

G

D

I

I

Y
|
Y

F

F

G

G

K

Q

P

P

R

R

G

G

I

V

F

R

T

A

E

P

-

D

-

G

-

P

-

F

T

A

G

G

E

E

K

R

R

E

G

G

V

F

N

D

T

T

M

M

V

R

Y

Y

T

S

E

E

S

P

E

E

I

V

D

R

R

R

I

I

G

A

R

H

I

V

A

A

F

F

E

Q

T

A

A

A

R

Q

K

K

R

R

R

A

G

K

K

K

L

L

C

L

S

S

V

V

D

D

K
|
K

A

S

N
|
N

V

V

L

L

D

E

V

T

S

S

Q

Q

L

F

W

W

R

R

D

D

R

V

I

M

T

I

K

D

L

V

S

S

Q

K

E

E

Y

Y

P

A

D

D

V

V

E

E

L

L

S

S

H

H

L

M

Y
|
Y

V

V

D
|
D

N
|
N

A

A

M

M

Q

Q

L

L

V

A

R

K

A

A

P

P

K

K

Q

Q

F

F

D

D

T

V

I

I

V

V

T

T

G

G

N

N

L

M

F

F

G

G

D
|
D

I

I

L

L

S

S

D
|
D

A

E

A

A

A

S

M

M

L

L

T

T

G

G

S

S

I

I

G

G

M

M

L

L

P

P

S

S

A

A

S

S

L

L

G

D

A

K

S

N

G

N

P

K

G

G

V

L

F

Y

E

E

P

P

V

S

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

L

K

D

G

K

I

A

A

N

N

P

P

L

L

A

A

Q

T

V

I

L

L

S

S

A

A

M

M

M

L

L

L

R

R

Y

Y

A

S

L

L

N

N

Q

R

P

A

Q

E

A

Q

A

A

D

D

K

R

I

I

E

E

Q

R

A

A

V

V

L

K

Q

T

V

V

L

L

E

E

Q

Q

G

G

D

Y

R

R

T

T

G

G

D

D

I

I

M

A

S

T

V

P

G

G

M

C

N

R

L

Q

L

V

G

G

C

T

R

A

A

A

M

M

G

G

D

D

S

A

L

V

I

V

K

A

A

A

L

L

active site: Y136 (= Y143), K191 (= K194), D223 (= D226), D247 (= D250), D251 (= D254)
binding nicotinamide-adenine-dinucleotide: N193 (= N196), Y221 (= Y224), N224 (= N227)

1cnzA 3-isopropylmalate dehydrogenase (ipmdh) from salmonella typhimurium (see paper)
52% identity, 99% coverage: 1:357/362 of query aligns to 1:357/363 of 1cnzA

query
sites
1cnzA

M

M

T

S

Q

K

N

N

Y

Y

R

H

I

I

T

A

L

V

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

M

M

A

A

V

Q

A

A

V

L

D

K

V

V

L

M

K

D

V

A

V

V

G

R

Q

S

Q

R

F

F

D

D

I

M

Q

R

F

I

D

T

F

T

Q

S

E

H

A

Y

L

D

I

V

G

G

A

I

A

A

I

I

D

D

A

N

T

H

G

G

E

H

P

P

L

L

P

P

S

K

A

A

T

T

L

V

D

E

T

G

C

C

R

E

Q

Q

S

A

D

D

A

A

V

I

L

L

L

F

A

G

A

S

I

V

G

G

Y

P

K

K

W

W

D

E

S

N

L

L

P

P

H

E

Q

S

R

Q

P

P

E

E

-

R

G

G

G

A

L

L

G

P

L

L

R

R

A

K

G

H

L

F

E

K

L

L

F

F

A

S

N

N

L

L

R

R

P

P

A

A

Q

K

I

L

L

Y

P

Q

Q

G

L

L

I

E

D

A

A

F

S

C

T

P

L

L

K

R

R

A

E

D

V

I

V

A

-

A

E

N

G

G

V

F

D

D

I

I

M

L

V

C

V

V

R

R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

K

Q

P

P

R

K

G

G

I

R

F

E

T

G

T

S

E

G

T

Q

G

Y

E

E

K

K

R

-

G

A

V

F

N

D

T

T

M

E

V

V

Y

Y

T

H

E

R

S

F

E

E

I

I

D

E

R

R

I

I

G

A

R

R

I

I

A

A

F

F

E

E

T

S

A

A

R

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

D

Q

V

S

S

S

Q

I

L

L

W

W

R

R

D

E

R

I

I

V

T

N

K

D

L

V

S

A

Q

K

E

T

Y

Y

P

P

D

D

V

V

E

E

L

L

S

A

H

H

L

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

T

V

I

L

V

L

T

C

G

S

N

N

L

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

G

N

A

E

S

Q

G

G

P

F

G

G

V

L

F

Y

E

E

P

P

V

A

H

G

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

L

K

D

N

K

I

A

A

N

N

P

P

L

I

A

A

Q

Q

V

I

L

L

S

S

A

L

A

A

M

L

L

L

R

R

Y

Y

A

S

L

L

N

D

Q

A

P

N

Q

D

A

A

D

T

K

A

I

I

E

E

Q

Q

A

A

V

I

L

N

Q

R

V

A

L

L

E

E

Q

E

G

G

D

V

R

R

T

T

G

G

D

D

I

-

M

L

S

A

V

R

G

G

M

A

N

A

L

A

L

V

G

S

C

T

R

D

A

E

M

M

G

G

D

D

S

I

L

I

I

A

K

R

active site: Y145 (= Y143), K195 (= K194), D227 (= D226), D251 (= D250)
binding manganese (ii) ion: D251 (= D250), D255 (= D254)

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: 1:357/362 of query aligns to 1:357/363 of P37412

query
sites
P37412

M

M

T

S

Q

K

N

N

Y

Y

R

H

I

I

T

A

L

V

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

M

M

A

A

V

Q

A

A

V

L

D

K

V

V

L

M

K

D

V

A

V

V

G

R

Q

S

Q

R

F

F

D

D

I

M

Q

R

F

I

D

T

F

T

Q

S

E

H

A

Y

L

D

I

V

G

G

A

I

A

A

I

I

D

D

A

N

T

H

G

G

E

H

P

P

L

L

P

P

S

K

A

A

T

T

L

V

D

E

T

G

C

C

R

E

Q

Q

S

A

D

D

A

A

V

I

L

L

L

F

A

G

A

S

I

V

G

G

Y

P

K

K

W

W

D

E

S

N

L

L

P

P

H

E

Q

S

R

Q

P

P

E

E

-

R

G

G

G

A

L

L

G

P

L

L

R

R

A

K

G

H

L

F

E

K

L

L

F

F

A

S

N

N

L

L

R

R

P

P

A

A

Q

K

I

L

L

Y

P

Q

Q

G

L

L

I

E

D

A

A

F

S

C

T

P

L

L

K

R

R

A

E

D

V

I

V

A

-

A

E

N

G

G

V

F

D

D

I

I

M

L

V

C

V

V

R

R

E

E

L

L

T

T

G

G

I

I

Y

Y

F

F

G

G

K

Q

P

P

R

K

G

G

I

R

F

E

T

G

T

S

E

G

T

Q

G

Y

E

E

K

K

R

-

G

A

V

F

N

D

T

T

M

E

V

V

Y

Y

T

H

E

R

S

F

E

E

I

I

D

E

R

R

I

I

G

A

R

R

I

I

A

A

F

F

E

E

T

S

A

A

R

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

D

Q

V

S

S

S

Q

I

L

L

W

W

R

R

D

E

R

I

I

V

T

N

K

D

L

V

S

A

Q

K

E

T

Y

Y

P

P

D

D

V

V

E

E

L

L

S

A

H

H

L

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

T

V

I

L

V

L

T

C

G

S

N

N

L

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

G

N

A

E

S

Q

G

G

P

F

G

G

V

L

F

Y

E

E

P

P

V

A

H

G

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

L

K

D

N

K

I

A

A

N

N

P

P

L

I

A

A

Q

Q

V

I

L

L

S

S

A

L

A

A

M

L

L

L

R

R

Y

Y

A

S

L

L

N

D

Q

A

P

N

Q

D

A

A

D

T

K

A

I

I

E

E

Q

Q

A

A

V

I

L

N

Q

R

V

A

L

L

E

E

Q

E

G

G

D

V

R

R

T

T

G

G

D

D

I

-

M

L

S

A

V

R

G

G

M

A

N

A

L

A

L

V

G

S

C

T

R

D

A

E

M

M

G

G

D

D

S

I

L

I

I

A

K

R

D227 (= D226) binding Mn(2+)
D251 (= D250) binding Mn(2+)
D255 (= D254) binding Mn(2+)

6xxyA Crystal structure of haemophilus influenzae 3-isopropylmalate dehydrogenase in complex with o-isobutenyl oxalylhydroxamate. (see paper)
53% identity, 93% coverage: 3:338/362 of query aligns to 2:338/358 of 6xxyA

query
sites
6xxyA

Q

E

N

S

Y

Y

R

N

I

I

T

A

L

V

L

L

P

A

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

M

M

A

A

V

E

A

A

V

I

D

K

V

V

L

L

K

N

V

R

V

V

G

Q

Q

E

Q

K

F

F

D

G

I

F

Q

K

F

L

D

N

F

F

Q

N

E

E

A

F

L

F

I

V

G

G

A

A

I

I

D

E

A

H

T

C

G

G

E

Y

P

P

L

L

P

P

S

A

A

E

T

T

L

L

D

K

T

G

C

C

R

D

Q

Q

S

A

D

D

A

A

V

I

L

L

L

F

A

G

A
x
S

I
x
V

G
|
G

G

G

Y

P

K

K

W

W

D

T

S

N

L

L

P

P

H

D

Q

Q

R

Q

P

P

E
|
E

-

R

G

G

G

A

L
|
L

L

L

G

P

L

L

R

R

A

K

G

H

L

F

E

K

L

L

F

F

A

C

N

N

L

L

R
|
R

P

P

A

A

Q

T

I

L

L

Y

P

K

Q

G

L

L

I

E

D

K

A

F

S

C

T

P

L

L

K

R

R

A

E

D

V

I

V

A

-

A

E

K

G

G

V

F

D

D

I

M

M

V

V

V

R
|
R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

K

Q

P

P

R

K

G

G

I

R

F

-

T

E

T

G

E

D

T

G

G

V

E

Q

K

T

R

K

G

A

V

F

N

D

T

T

M

E

V

V

Y

Y

T

Y

E

K

S

Y

E

E

I

I

D

E

R

R

I

I

G

A

R

R

I

A

A

A

F

F

E

E

T

A

A

A

R

M

K

K

R

R

R

N

G

K

K

K

L

V

C

T

S

S

V

V

D

D

K
|
K

A

A

N

N

V
|
V

L

L

D

Q

V

S

S

S

Q

I

L

L

W

W

R

R

D

E

R

T

I

V

T

T

K

E

L

M

S

A

Q

K

E

D

Y

Y

P

P

D

E

V

V

E

T

L

L

S

E

H

H

L

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

Q

S

F

F

D

D

T

V

I

L

V

L

T

C

G

S

N

N

L

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

G

N

A

E

S

E

G

G

P

F

G

G

V

L

F

Y

E
|
E

P

P

V

A

H
x
G

G
|
G

S
|
S

A
|
A

P
|
P

D
|
D

I
|
I

A

A

G

G

L

K

D

G

K

I

A

A

N
|
N

P

P

L

I

A

A

Q

Q

V

I

L

L

S

S

A

A

M

M

L

L

R

R

Y

Y

A

S

L

F

N

N

Q

L

P

N

Q

E

A

A

D

D

K

A

I

I

E

E

Q

S

A

A

V

V

L

Q

Q

K

V

V

L

L

E

A

Q

S

G

G

D

H

R

R

T

T

G

A

D
|
D

I

L

active site: Y144 (= Y143), K194 (= K194), D226 (= D226), D250 (= D250)
binding magnesium ion: D250 (= D250), D254 (= D254)
binding nicotinamide-adenine-dinucleotide: S74 (≠ A75), V75 (≠ I76), G76 (= G77), E90 (= E91), L94 (= L94), Y224 (= Y224), N227 (= N227), M230 (= M230), M263 (≠ I263), G264 (= G264), E280 (= E280), G283 (≠ H283), G284 (= G284), S285 (= S285), A286 (= A286), P287 (= P287), D288 (= D288), I289 (= I289), N296 (= N296), D337 (= D337)
binding 2-(2-methylprop-2-enoxyamino)-2-oxidanylidene-ethanoic acid: E90 (= E91), R108 (= R108), R137 (= R136), K194 (= K194), V197 (= V197), D226 (= D226), D250 (= D250)

3vkzA 3-isopropylmalate dehydrogenase from shewanella oneidensis mr-1 at atmospheric pressure (see paper)
53% identity, 93% coverage: 4:340/362 of query aligns to 2:339/364 of 3vkzA

query
sites
3vkzA

N

S

Y

Y

R

Q

I

I

T

A

L

V

L

L

P

A

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

M

M

A

A

V

E

A

A

V

R

D

K

V

V

L

L

K

K

V

A

V

V

G

E

Q

A

Q

R

F

F

D

G

I

L

Q

N

F

I

D

E

F

Y

Q

T

E

E

A

Y

L

D

I

V

G

G

A

I

A

A

I

I

D

D

A

N

T

H

G

G

E

C

P

P

L

L

P

P

S

E

A

A

T

T

L

L

D

K

T

G

C

C

R

E

Q

A

S

A

D

D

A

A

V

I

L

L

L

F

A

G

A

S

I

V

G

G

Y

P

K

K

W

W

D

E

S

K

L

L

P

P

H

N

Q

E

R

Q

P

P

E

E

-

R

G

G

G

A

L

L

G

P

L

L

R
|
R

A

G

G

H

L

F

E

E

L

L

F

F

A

C

N

N

L

L

R

R

P

P

A

A

Q

K

I

L

L

H

P

D

Q

G

L

L

I

E

D

H

A

M

S

S

T

P

L

L

K

R

R

S

E

D

V

I

-

S

V

A

E

R

G

G

V

F

D

D

I

V

M

L

V

C

V

V

R
|
R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

K

K

P

P

R

K

G

G

I

-

F

R

T

Q

T

G

E

E

T

G

G

E

E

S

K

E

R

E

G

A

V

F

N

D

T

T

M

M

V

R

Y

Y

T

S

E

R

S

R

E

E

I

I

D

S

R

R

I

I

G

A

R

R

I

I

A

A

F

F

E

E

T

A

A

A

R

R

K

G

R

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

D

A

V

C

S

S

Q

V

L

L

W

W

R

R

D

Q

R

V

I

V

T

E

K

E

L

V

S

A

Q

V

E

D

Y

F

P

P

D

D

V

V

E

E

L

L

S

E

H

H

L

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

T

V

I

M

V

L

T

C

G

S

N

N

L

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

G

N

A

S

S

T

G

G

P

F

G

G

V

L

F

F

E

E

P

P

V

A

H

G

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

L

K

D

G

K

I

A

A

N

N

P

P

L

I

A

A

Q

Q

V

I

L

L

S

S

A

A

M

L

M

M

L

L

R

R

Y

H

A

S

L

L

N

K

Q

Q

P

E

Q

E

A

A

D

S

K

A

I

I

E

E

Q

R

A

A

V

V

L

T

Q

K

V

A

L

L

E

N

Q

S

G

G

D

Y

R

L

T

T

G

G

D

E

I

L

M

L

S

S

active site: Y143 (= Y143), K193 (= K194), D225 (= D226), D249 (= D250), D253 (= D254)
binding calcium ion: D249 (= D250), D253 (= D254)
binding 3-isopropylmalic acid: R97 (= R98), R136 (= R136), Y143 (= Y143), D249 (= D250)

3vmkA 3-isopropylmalate dehydrogenase from shewanella benthica db21 mt-2 (see paper)
51% identity, 98% coverage: 4:359/362 of query aligns to 8:366/369 of 3vmkA

query
sites
3vmkA

N

S

Y

Y

R

Q

I

I

T

A

L

V

L

L

P

A

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

M

M

A

A

V

E

A

A

V

R

D

K

V

V

L

L

K

A

V

A

V

V

G

E

Q

K

Q

R

F

F

D

D

I

L

Q

S

F

I

D

E

F

Y

Q

S

E

E

A

Y

L

D

I

V

G

G

A

A

I

I

D

D

A

N

T

H

G

G

E

C

P

P

L

L

P

P

S

E

A

A

T

T

L

L

D

K

T

G

C

C

R

E

Q

A

S

A

D

D

A

A

V

V

L

L

L

F

A

G

A

S

I

V

G

G

Y

P

K

K

W

W

D

E

S

H

L

L

P

P

H

N

Q

D

R

Q

P

P

E

E

-

R

G

G

G

A

L

L

G

P

L

L

R
|
R

A

G

G

H

L

F

E

E

L

L

F

F

A

C

N

N

L

M

R

R

P

P

A

A

Q

K

I

L

L

H

P

P

Q

G

L

L

I

E

D

H

A

M

S

S

T

P

L

L

K

R

R

S

E

D

V

I

V

S

E

E

-

K

G

G

V

F

D

D

I

I

M

L

V

C

V

V

R
|
R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

K

K

P

P

R

K

G

G

I

-

F

R

T

Q

T

G

E

E

T

G

G

E

E

N

K

E

R

E

G

A

V

F

N

D

T

T

M

M

V

R

Y

Y

T

S

E

R

S

K

E

E

I

I

D

R

R

R

I

I

G

A

R

K

I

I

A

A

F

F

E

E

T

S

A

A

R

Q

K

G

R

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

D

A

V

C

S

S

Q

V

L

L

W

W

R

R

D

E

R

V

I

V

T

E

K

E

L

V

S

A

Q

K

E

D

Y

Y

P

P

D

D

V

V

E

E

L

L

S

E

H

H

L

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

T

V

I

M

V

L

T

C

G

S

N

N

L

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

G

N

A

S

S

Q

G

G

P

F

G

G

V

M

F

Y

E

E

P

P

V

A

H

G

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

L

Q

D

G

K

I

A

A

N

N

P

P

L

V

A

A

Q

Q

V

I

L

L

S

S

A

A

M

L

L

L

R

R

Y

H

A

S

L

L

N

K

Q

L

P

E

Q

D

A

A

D

L

K

A

I

I

E

E

Q

A

A

A

V

V

L

S

Q

K

V

A

L

L

E

S

Q

D

G

G

D

Y

R

L

T

T

G

C

D

E

I

L

M

L

-

P

-

A

S

S

V

E

G

R

M

S

N

Q

L

A

L

K

G

S

C

T

R

S

A

Q

M

M

G

G

D

D

S

Y

L

I

I

A

K

Q

A

A

L

I

active site: Y149 (= Y143), K199 (= K194), D231 (= D226), D255 (= D250), D259 (= D254)
binding 3-isopropylmalic acid: R103 (= R98), R142 (= R136), Y149 (= Y143), K199 (= K194), N201 (= N196), D255 (= D250)

2y41A Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with ipm and mn (see paper)
53% identity, 90% coverage: 4:329/362 of query aligns to 1:320/346 of 2y41A

query
sites
2y41A

N

S

Y

M

R

K

I

V

T

A

L

V

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

M

T

A

E

V

A

A

A

V

L

D

K

V

V

L

L

K

R

V

A

V

L

G

D

Q

E

Q

A

F

E

D

G

I

L

Q

G

F

L

D

A

F

Y

Q

E

E

V

A

F

L

P

I

F

G

G

A

A

I

I

D

D

A

A

T

F

G

G

E

E

P

P

L

F

P

P

S

E

A

P

T

T

L

R

D

K

T

G

C

V

R

E

Q

E

S

A

D

E

A

A

V

V

L

L

A

G

A

S

I

V

G

G

Y

P

K

K

W

W

D

D

S

G

L

L

P

P

P

R

H

K

Q

I

R

R

P

P

E

E

G

T

G

G

L

L

G

S

L

L

R
|
R

A

K

G

S

L

Q

E

D

L

L

F

F

A

A

N

N

L

L

R
|
R

P

P

A

A

Q

K

I

V

L

F

P

P

Q

G

L

L

I

E

D

R

A

L

S

S

T

P

L

L

K

K

R

E

E

E

V

I

V

A

E

R

G

G

V

V

D

D

I

V

M

L

V

I

V

V

R
|
R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

K

E

P

P

R

R

G

G

I

M

F

-

T

-

E

-

T

-

G

S

E

E

K

A

R

E

G

A

V

W

N

N

T

T

M

E

V

R

Y

Y

T

S

E

K

S

P

E

E

I

V

D

E

R

R

I

V

G

A

R

R

I

V

A

A

F

F

E

E

T

A

A

A

R

R

K

K

R

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

D

E

V

V

S

G

Q

E

L

F

W

W

R

R

D

K

R

T

I

V

T

E

K

E

L

V

S

G

Q

R

E

G

Y

Y

P

P

D

D

V

V

E

A

L

L

S

E

H

H

L

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

T

V

I

V

V

V

T

T

G

G

N

N

L

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

G

G

A

R

S

G

G

T

P

P

G

-

V

V

F

F

E

E

P

P

V

V

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

L

K

D

G

K

I

A

A

N

N

P

P

L

T

A

A

Q

A

V

I

L

L

S

S

A

A

M

M

L

L

R

E

Y

H

A

A

L

F

N

G

Q

L

P

V

Q

E

A

L

A

A

D

R

K

K

I

V

E

E

Q

D

A

A

V

V

L

A

Q

K

V

A

L

L

active site: Y140 (= Y143), K186 (= K194), D218 (= D226), D242 (= D250), D246 (= D254)
binding 3-isopropylmalic acid: R95 (= R98), R105 (= R108), R133 (= R136), Y140 (= Y143), D242 (= D250)

2y42D Structure of isopropylmalate dehydrogenase from thermus thermophilus - complex with nadh and mn (see paper)
53% identity, 90% coverage: 4:329/362 of query aligns to 1:320/355 of 2y42D

query
sites
2y42D

N

S

Y

M

R

K

I

V

T

A

L

V

L

L

P

P

G

G

D

D

G

G

I
|
I

G

G

P

P

E

E

I

V

M

T

A

E

V

A

A

A

V

L

D

K

V

V

L

L

K

R

V

A

V

L

G

D

Q

E

Q

A

F

E

D

G

I

L

Q

G

F

L

D

A

F

Y

Q

E

E

V

A

F

L

P

I

F

G

G

A

A

I

I

D

D

A

A

T

F

G

G

E

E

P

P

L

F

P

P

S

E

A

P

T

T

L

R

D

K

T

G

C

V

R

E

Q

E

S

A

D

E

A

A

V

V

L

L

A

G

A

S

I

V

G

G

Y

P

K

K

W

W

D
|
D

S

G

L

L

P

P

P

R

H

K

Q

I

R

R

P

P

E

E

G

T

G

G

L

L

G

S

L

L

R

R

A

K

G

S

L

Q

E

D

L

L

F

F

A

A

N

N

L

L

R

R

P

P

A

A

Q

K

I

V

L

F

P

P

Q

G

L

L

I

E

D

R

A

L

S

S

T

P

L

L

K

K

R

E

E

E

V

I

V

A

E

R

G

G

V

V

D

D

I

V

M

L

V

I

V

V

R

R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

K

E

P

P

R

R

G

G

I

M

F

-

T

-

E

-

T

-

G

S

E

E

K

A

R

E

G

A

V

W

N

N

T

T

M

E

V

R

Y

Y

T

S

E

K

S

P

E

E

I

V

D

E

R

R

I

V

G

A

R

R

I

V

A

A

F

F

E

E

T

A

A

A

R

R

K

K

R

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

D

E

V

V

S

G

Q

E

L

F

W

W

R

R

D

K

R

T

I

V

T

E

K

E

L

V

S

G

Q

R

E

G

Y

Y

P

P

D

D

V

V

E

A

L

L

S

E

H

H

L

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

T

V

I

V

V

V

T

T

G

G

N

N

L

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

G

G

A

R

S

G

G

T

P

P

G

-

V

V

F

F

E

E

P

P

V

V

H
|
H

G
|
G

S

S

A
|
A

P

P

D
|
D

I
|
I

A

A

G

G

L

K

D

G

K

I

A

A

N
|
N

P

P

L

T

A

A

Q

A

V

I

L

L

S

S

A

A

M

M

L

L

R

E

Y

H

A

A

L

F

N

G

Q

L

P

V

Q

E

A

L

A

A

D

R

K

K

I

V

E

E

Q

D

A

A

V

V

L

A

Q

K

V

A

L

L

active site: Y140 (= Y143), K186 (= K194), D218 (= D226), D242 (= D250), D246 (= D254)
binding manganese (ii) ion: D242 (= D250), D246 (= D254)
binding nicotinamide-adenine-dinucleotide: I12 (= I15), D79 (= D82), H274 (= H283), G275 (= G284), A277 (= A286), D279 (= D288), I280 (= I289), N287 (= N296)

2ztwA Structure of 3-isopropylmalate dehydrogenase in complex with the inhibitor and NAD+ (see paper)
53% identity, 90% coverage: 6:329/362 of query aligns to 2:319/345 of 2ztwA

query
sites
2ztwA

R

K

I

V

T

A

L

V

L

L

P

P

G

G

D

D

G

G

I
|
I

G

G

P

P

E

E

I

V

M

T

A

E

V

A

A

A

V

L

D

K

V

V

L

L

K

R

V

A

V

L

G

D

Q

E

Q

A

F

E

D

G

I

L

Q

G

F

L

D

A

F

Y

Q

E

E

V

A

F

L

P

I

F

G

G

A

A

I

I

D

D

A

A

T

F

G

G

E

E

P

P

L

F

P

P

S

E

A

P

T

T

L

R

D

K

T

G

C

V

R

E

Q

E

S

A

D

E

A

A

V

V

L

L

A

G

A

S

I

V

G

G

Y

P

K

K

W

W

D

D

S

G

L

L

P

P

P

R

H

K

Q

I

R

R

P

P

E

E

G

T

G

G

L

L

G

S

L

L

R

R

A

K

G

S

L

Q

E

D

L

L

F

F

A

A

N

N

L

L

R

R

P

P

A

A

Q

K

I

V

L

F

P

P

Q

G

L

L

I

E

D

R

A

L

S

S

T

P

L

L

K

K

R

E

E

E

V

I

V

A

E

R

G

G

V

V

D

D

I

V

M

L

V

I

V

V

R

R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

K

E

P

P

R

R

G

G

I

M

F

-

T

-

E

-

T

-

G

S

E

E

K

A

R

E

G

A

V

W

N

N

T

T

M

E

V

R

Y

Y

T

S

E

K

S

P

E

E

I

V

D

E

R

R

I

V

G

A

R

R

I

V

A

A

F

F

E

E

T

A

A

A

R

R

K

K

R

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

D

E

V

V

S

G

Q

E

L

F

W

W

R

R

D

K

R

T

I

V

T

E

K

E

L

V

S
x
G

Q

R

E

G

Y
|
Y

P

P

D

D

V
|
V

E

A

L

L

S

E

H

H

L

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

T

V

I

V

V

V

T

T

G

G

N

N

L

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

G

G

A

R

S

G

G

T

P

P

G

-

V

V

F

F

E

E

P

P

V

V

H
|
H

G
|
G

S

S

A
|
A

P

P

D
|
D

I
|
I

A

A

G

G

L

K

D

G

K

I

A
|
A

N
|
N

P

P

L

T

A

A

Q

A

V

I

L

L

S

S

A

A

M

M

L

L

R

E

Y

H

A

A

L

F

N

G

Q

L

P

V

Q

E

A

L

A

A

D

R

K

K

I

V

E

E

Q

D

A

A

V

V

L

A

Q

K

V

A

L

L

active site: Y139 (= Y143), K185 (= K194), D217 (= D226), D241 (= D250), D245 (= D254)
binding magnesium ion: G203 (≠ S212), Y206 (= Y215), V209 (= V218)
binding nicotinamide-adenine-dinucleotide: I11 (= I15), H273 (= H283), G274 (= G284), A276 (= A286), D278 (= D288), I279 (= I289), A285 (= A295), N286 (= N296)

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)
53% identity, 90% coverage: 6:329/362 of query aligns to 2:319/345 of Q5SIY4

query
sites
Q5SIY4

R

K

I

V

T

A

L

V

L

L

P

P

G

G

D

D

G

G

I

I

G

G

P

P

E

E

I

V

M

T

A

E

V

A

A

A

V

L

D

K

V

V

L

L

K

R

V

A

V

L

G

D

Q

E

Q

A

F

E

D

G

I

L

Q

G

F

L

D

A

F

Y

Q

E

E

V

A

F

L

P

I

F

G

G

A

A

I

I

D

D

A

A

T

F

G

G

E

E

P

P

L

F

P

P

S

E

A

P

T

T

L

R

D

K

T

G

C

V

R

E

Q

E

S

A

D

E

A

A

V

V

L

L

A

G

A

S

I

V

G

G

G
|
G

Y
x
P

K
|
K

W
|
W

D
|
D

S
x
G

L
|
L

P
|
P

P
x
R

H
x
K

Q
x
I

R
|
R

P
|
P

E
|
E

G

T

G

G

L

L

G

S

L

L

R

R

A

K

G

S

L

Q

E

D

L

L

F

F

A

A

N

N

L

L

R

R

P

P

A

A

Q

K

I

V

L

F

P

P

Q

G

L

L

I

E

D

R

A

L

S

S

T

P

L

L

K

K

R

E

E

E

V

I

V

A

E

R

G

G

V

V

D

D

I

V

M

L

V

I

V

V

R

R

E

E

L

L

T

T

G

G

I

I

Y
|
Y

F

F

G

G

K

E

P

P

R

R

G

G

I

M

F

-

T

-

E

-

T

-

G

S

E

E

K

A

R

E

G

A

V

W

N

N

T

T

M

E

V

R

Y

Y

T

S

E

K

S

P

E

E

I

V

D

E

R

R

I

V

G

A

R

R

I

V

A

A

F

F

E

E

T

A

A

A

R

R

K

K

R

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

D

E

V

V

S

G

Q

E

L

F

W

W

R

R

D

K

R

T

I

V

T

E

K

E

L

V

S

G

Q

R

E

G

Y

Y

P

P

D

D

V

V

E

A

L

L

S

E

H

H

L

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

T

V

I

V

V

V

T

T

G

G

N

N

L

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

G

G

A

R

S

G

G

T

P

P

G

-

V

V

F

F

E

E

P

P

V

V

H

H

G
|
G

S
|
S

A
|
A

P
|
P

D
|
D

I
|
I

A
|
A

G
|
G

L
x
K

D
x
G

K
x
I

A
|
A

N
|
N

P

P

L

T

A

A

Q

A

V

I

L

L

S

S

A

A

M

M

L

L

R

E

Y

H

A

A

L

F

N

G

Q

L

P

V

Q

E

A

L

A

A

D

R

K

K

I

V

E

E

Q

D

A

A

V

V

L

A

Q

K

V

A

L

L

74:87 (vs. 78:91, 64% identical) binding NAD(+)
Y139 (= Y143) mutation to F: Large decrease in activity and a small decrease in substrate affinity.
274:286 (vs. 284:296, 77% 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)
46% identity, 90% coverage: 6:330/362 of query aligns to 5:336/371 of P18869

query
sites
P18869

R

K

I

I

T

V

L

V

L

L

P

P

G

G

D

D

G

H

I

I

G

G

P

P

E

E

I

I

M

V

A

A

V

S

A

A

V

L

D

E

V

V

L

L

K

K

V

V

G

E

Q

K

F

R

-

P

D

E

I

L

Q

K

F

L

D

E

F

F

Q

E

E

E

A

H

L

K

I

I

G

G

A

A

A

S

I

I

D

D

A

A

T

Y

G

G

E
x
T

P

P

L

L

P

T

S

D

A

E

T

T

L

V

D

K

T

A

C

C

R

L

Q

E

S

A

D

D

A

G

V

V

L

L

A

G

A

A

I

V

G

G

Y

P

K

E

W

W

D

T

S

N

L

-

P

-

P

P

H

N

Q

C

R

R

P

P

E

E

G

Q

G

G

L

L

G

K

L

L

R

R

A

K

G

S

L

M

E

G

L

V

F

W

A

A

N

N

L

L

R

R

P

P

A

C

Q

N

I

F

L

A

P

S

Q

K

-

S

L

L

I

V

D

K

A

Y

S

S

T

P

L

L

K

K

R

P

E

E

V

I

V

V

E

E

G

G

V

V

D

D

I

F

M

C

V

V

R

R

E

E

L

L

T

T

G

G

I

C

Y

Y

F

F

G

G

K

E

P

-

R

-

G

-

I

-

F

R

T

T

T

E

E

D

T

N

G

G

E

S

K

G

R

Y

G

A

V

M

N

D

T

T

M

W

V

P

Y

Y

T

S

E

L

S

E

E

E

I

V

D

S

R

R

I

I

G

A

R

R

I

L

A

A

F

A

E

W

T

L

A

A

R

E

K

T

R

S

R

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

D

A

V

T

S

S

Q

R

L

L

W

W

R

R

D

K

R

T

I

V

T

A

K

K

L

I

-

F

S

K

Q

E

E

E

Y

Y

P

P

D

H

V

L

E

T

L

L

S

K

H

N

L

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

T

G

I

V

V

V

-

L

T

T

G

D

N

N

L

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

G

A

V

S

V

G

G

P

K

G

S

-

E

-

K

-

V

-

H

-

C

V

L

F

V

E

E

P

P

V

I

H

H

G

G

S

S

A

A

P

P

D

D

I

I

A

A

G

G

L

K

D

G

K

I

A

V

N

N

P

P

L

V

A

G

Q

T

V

I

L

L

S

S

A

A

A

S

M

L

L

L

R

R

Y

Y

A

G

L

L

N

N

Q

A

P

P

Q

K

A

E

A

A

D

E

K

A

I

I

E

E

Q

A

A

A

V

V

L

R

Q

K

V

V

L

L

E

D

T55 (≠ E55) 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, 92% coverage: 5:338/362 of query aligns to 3:314/334 of Q72IW9

query
sites
Q72IW9

Y

Y

R

R

I

I

T

C

L

L

L

I

P

E

G

G

D

D

G

G

I

I

G

G

P

H

E

E

I

V

M

I

A

P

V

A

A

A

V

R

D

R

V

V

L

L

K

E

V

A

V

T

G

G

Q

-

F

-

D

-

I

L

Q

P

F

L

D

E

F

F

Q

V

E

E

A

A

L

E

I

A

G

G

G

W

A

E

A

T

I

F

D

E

A

R

T

R

G

G

E

T

P

S

L

V

P

P

S

E

A

E

T

T

L

V

D
x
E

T

K

C

I

R

L

Q

S

S

C

D

H

A

A

V

T

L

L

L

F

A

G

A

A

I
x
A

G

-

Y

-

K

-

W

-

D

-

S
x
T

L
x
S

P

P

P

T

H

R

Q

K

R

V

P

P

E

G

-

F

G

G

G

A

L

I

L
x
R

G
x
Y

L

L

R
|
R

A

R

G

R

L

L

E

D

L

L

F

Y

A

A

N

N

L

V

R
|
R

P

P

A

A

Q

K

I

S

L

R

P

P

Q

-

L

-

I

V

D

P

A

G

S

S

T

R

L

-

K

-

R

-

E

-

V

-

E

P

G

G

V

V

D

D

I

L

M

V

V

I

V

V

R
|
R

E

E

L

N

T

T

G

E

G

G

I

L

Y
|
Y

F

V

G

E

K

Q

P

E

R

R

G

R

I

Y

F

L

T

D

T
x
V

E

-

T

-

G

-

E

-

K

-

R

-

G

A

V

I

N

A

T

D

M

A

V

V

Y

I

T

S

E

K

S

K

E

A

I

S

D

E

R

R

I

I

G

G

R

R

I

A

A

A

F

L

E

R

T

I

A

A

R

E

K

G

R

R

-

P

R

R

G

K

K

T

L

L

C

H

S

I

V

A

D

H

K
|
K

A

A

N
|
N

V

V

L

L

D

P

V

L

S

T

Q

Q

-

G

L

L

W

F

R

L

D

D

R

T

I

V

T

K

K

E

L

V

S

A

Q

K

E

D

Y

F

P

P

D

L

V

V

E

N

L

V

S

Q

H

D

L

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

T

V

I

I

V

V

T

T

G

T

N

N

L

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

G

G

A

D

S

T

G

-

P

T

G

A

V

V

F

F

E

E

P

P

V

V

H

H

G
|
G

S
|
S

A
|
A

P
|
P

D
|
D

I

I

A

A

G

G

L

K

D

G

K

I

A

A

N
|
N

P

P

L

T

A

A

Q

A

V

I

L

L

S

S

A

A

M

M

L

L

R

D

Y

Y

A

-

L

L

N

G

Q

E

P

K

Q

E

A

A

D

K

K

R

I

V

E

E

Q

K

A

A

V

V

L

D

Q

L

V

V

L

L

E

E

Q

R

G

G

D

P

R
|
R

T

T

G

P

D

D

I

L

E57 (≠ D63) 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.
A------TS 70:72 (≠ IGGYKWDSL 76:84) binding NADH
S72 (≠ L84) 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 (≠ L95) 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 (≠ G96) 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 (= R98) binding in other chain
R98 (= R108) binding in other chain
R118 (= R136) binding in other chain
Y125 (= Y143) binding in other chain; mutation to A: Reduces catalytic efficiency with isocitrate.
V135 (≠ T153) mutation to M: Formation of homodimers instead of homotetramers. Increased affinity for isocitrate. Reduces enzyme activity with isocitrate.
K171 (= K194) binding (2R,3S)-homoisocitrate
N173 (= N196) binding (2R,3S)-homoisocitrate; binding NADH
D204 (= D226) binding Mg(2+)
M208 (= M230) 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 (= F239) 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 (= D250) binding Mg(2+)
D232 (= D254) binding Mg(2+)
V238 (≠ T260) 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 284:288) binding NADH
N273 (= N296) binding NADH
R310 (= R334) 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_011319729.1 NCBI__GCF_000204075.1:WP_011319729.1
MTQNYRITLLPGDGIGPEIMAVAVDVLKVVGQQFDIQFDFQEALIGGAAIDATGEPLPSA
TLDTCRQSDAVLLAAIGGYKWDSLPPHQRPEGGLLGLRAGLELFANLRPAQILPQLIDAS
TLKREVVEGVDIMVVRELTGGIYFGKPRGIFTTETGEKRGVNTMVYTESEIDRIGRIAFE
TARKRRGKLCSVDKANVLDVSQLWRDRITKLSQEYPDVELSHLYVDNAAMQLVRAPKQFD
TIVTGNLFGDILSDAAAMLTGSIGMLPSASLGASGPGVFEPVHGSAPDIAGLDKANPLAQ
VLSAAMMLRYALNQPQAADKIEQAVLQVLEQGDRTGDIMSVGMNLLGCRAMGDSLIKALE
KS

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