SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 7023117 Shewana3_0355 ketol-acid reductoisomerase (RefSeq) 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)

P05793 Ketol-acid reductoisomerase (NADP(+)); KARI; Acetohydroxy-acid isomeroreductase; AHIR; Alpha-keto-beta-hydroxylacyl reductoisomerase; Ketol-acid reductoisomerase type 2; Ketol-acid reductoisomerase type II; EC 1.1.1.86 from Escherichia coli (strain K12) (see 5 papers)
73% identity, 99% coverage: 1:489/492 of query aligns to 1:487/491 of P05793

query
sites
P05793

M
|
M

A

A

N

N

Y

Y

F

F

N

N

S

T

L

L

N

N

L

L

R

R

Q

Q

L

L

A

A

Q

Q

L

L

G

G

Q

K

C

C

R

R

F

F

M

M

D

G

R

R

S

D

E

E

F

F

S

A

D

D

G

G

C

A

N

S

Y

Y

I

L

K

Q

D

G

W

K

N

K

I

V

V

V

I

I

L

V

G

G

C
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C

G
|
G

A
|
A

Q
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Q

G

G

L

L

N

N

Q

Q

G

G

L

L

N

N

M

M

R

R

D

D

S

S

G

G

L

L

N

D

I

I

A

S

Y

Y

A

A

L

L

R
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R

P
x
K

E

E

A
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A

I

I

A

A

Q

E

K
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K

R
|
R

A

A

S
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S

W

W

Q

R

K

K

A

A

T

T

D

E

N

N

G

G

F

F

K

K

V

V

G

G

T

T

F

Y

E

E

L

L

I

I

P

P

T

Q

A

A

D

D

L

L

V

V

L

I

N

N

L

L

T

T

P

P

D
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D

K
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K

Q
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Q

H

H

S

S

N

D

V

V

S

R

A

T

V

V

M

Q

P

P

L

L

M

M

K

K

Q

D

G

G

A

A

T

A

L

L

S

G

Y

Y

S

S

H
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H

G

G

F

F

N

N

I

I

V

V

E

E

E

V

G

G

M

E

Q

Q

I

I

R

R

P

K

D

D

I

I

T

T

V

V

M

M

V

V

A

A

P

P

K
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K

C

C

P

P

G

G

T

T

E

E

V

V

R

R

E

E

Y

Y

K

K

R

R

G

G

F

F

G

G

V

V

P

P

T

T

L

L

I

I

A

A

V

V

H

H

P

P

E

E

N

N

D

D

P

P

N

K

G

G

D

E

G

G

L

M

E

A

I

I

A

A

K

K

A

A

Y

W

A

A

S

A

A

A

T

T

G

G

D

H

R

R

A

A

G

G

V

V

L

L

Q

E

S

S

F

F

I

V

A

A

E
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E

V

V

K

K

S

S

D
|
D

L

L

M

M

G

G

E
|
E

Q

Q

T

T

I

I

L

L

C

C

G

G

M

M

L

L

Q

Q

T

A

G

G

A

S

I

L

L

L

G

C

Y

F

D

D

K

K

M

L

V

V

A

E

D

E

G

G

V

T

E

D

P

P

G

A

Y

Y

A

A

A

E

K

K

L

L

I

I

Q

Q

Q

F

G

G

W

W

E

E

T

T

V

I

T

T

E

E

A

A

L

L

K

K

H

Q

G

G

I

I

T

T

N

L

M

M

D

D

R

R

L

L

S

S

N

N

P

P

A

A

K

K

I

L

K

R

A

A

F

Y

E

A

I

L

A

S

E

E

D

Q

L

L

K

K

E

E

I

I

L

M

Q

A

P

P

L

L

F

F

E

Q

K

K

H

H

M

M

D

D

I

I

S

S

G

G

E

E

F

F

S

S

R

S

T

G

M

M

Q

A

D

D

W

W

A

A

N

N

D

D

A

K

N

K

L

L

R

T

W

W

R

R

A

E

E

E

T

T

A

G

E

K

T

T

G

A

F

F

E

E

N

T

A

A

P

P

V

Q

S

Y

S

E

E

G

H

K

I

I

D

G

E

E

Q

Q

T

E

Y

Y

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F

D

D

K

K

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G

I

V

F

L

L

M

V

I

A

A

M

M

I

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K

K

A

A

G

G

V

V

E

E

L

L

A

A

F

F

D

E

T

T

M

M

V

V

S

D

A

S

G

G

I

I

V

I

E

E

S

S

A

A

Y

Y

E
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E

S

S

L

L

H

H

E
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E

T

L

P

P

L

L

I

I

A

A

N

N

T

T

I

I

A

A

R

R

K

K

R

R

L

L

Y

Y

E

E

M

M

N

N

V

V

I

I

S
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S

D

D

T

T

A

A

E

E

Y

Y

G

G

C

N

Y

Y

L

L

F

F

N

S

H

Y

A

A

A

C

V

V

P

P

M

L

L

L

R

K

D

P

Y

F

V

M

N

A

A

E

M

L

S

Q

P

P

E

G

Y

D

L

L

G

G

A

K

G

A

L

I

K

P

D

E

S

G

S

A

N

-

V

V

D

D

N

N

L

G

Q

Q

L

L

I

R

A

D

I

V

N

N

D

E

A

A

I

I

R

R

H

S

T

H

S

A

V

I

E

E

Y

Q

I

V

G

G

A

K

E

K

L

L

R

R

G

G

Y

Y

M

M

T

T

D

D

M

M

K

K

S

R

I

I

M1 (= M1) modified: Initiator methionine, Removed
CGAQ 45:48 (= CGAQ 45:48) binding
R68 (= R68) mutation to D: Inversion of cofactor specificity from NADPH to NADH; when associated with L-69, V-75 and D-76.; mutation to Q: 18-fold decrease of the catalytic efficiency and 3-fold decrease of the affinity for NADPH.
K69 (≠ P69) mutation to L: Does not significantly alter the affinity for NADPH. Slight increase of the catalytic efficiency. Inversion of cofactor specificity from NADPH to NADH; when associated with D-68, V-75 and D-76.
A71 (= A71) mutation to S: 7- and 2.5-fold increase of the reductoisomerase activity with NADH and NADPH, respectively.
K75 (= K75) mutation to Q: 13-fold decrease of the catalytic efficiency and 3-fold increase of the affinity for NADPH.; mutation to V: Inversion of cofactor specificity from NADPH to NADH; when associated with D-68, L-69 and D-76.
R76 (= R76) binding ; mutation to D: 3-fold increase of the reductoisomerase activity with NADH and slight decrease of the reductoisomerase activity with NADPH.; mutation to D: Strong increase of catalytic efficiency and 2.5-fold increase of the affinity for NADH. 4-fold decrease of the catalytic efficiency and strong decrease of the affinity for NADPH. Inversion of cofactor specificity from NADPH to NADH; when associated with D-68, L-69 and V-75.; mutation to Q: 20-fold decrease of the catalytic efficiency and 5-fold decrease of the affinity for NADPH.
S78 (= S78) binding ; mutation to D: 12-fold increase of the reductoisomerase activity with NADH and slight decrease of the reductoisomerase activity with NADPH.
DKQ 108:110 (= DKQ 108:110) binding
Q110 (= Q110) mutation Q->V,A: 12- and 2-fold increase of the reductoisomerase activity with NADH and NADPH, respectively.
H132 (= H132) mutation to K: Loss of reductoisomerase activity.; mutation to Q: Loss of reductoisomerase activity. The reductase activity with 3-hydroxypyruvate and HMKB is nearly normal, and the isomerase activity decreases 24-fold.
K155 (= K155) mutation K->E,Q: Loss of reductoisomerase activity.; mutation to R: Loss of reductoisomerase activity. The reductase activity with 3-hydroxypyruvate and HMKB is nearly normal, and the isomerase activity decreases 40-fold.
E213 (= E213) mutation to D: Loss of reductoisomerase activity. 1.5-fold decrease of the reductase activity with 3-hydroxypyruvate and the isomerase activity decreases 48-fold.
D217 (= D217) binding ; binding ; mutation D->E,N: Loss of reductoisomerase activity.
E221 (= E221) mutation E->D,Q: Loss of reductoisomerase activity.
E389 (= E389) binding ; mutation to D: Loss of reductoisomerase activity. 1.5-fold decrease of the reductase activity with 3-hydroxypyruvate and the isomerase activity decreases 4-fold.; mutation to Q: Loss of reductoisomerase activity.
E393 (= E393) binding ; mutation to D: Loss of reductoisomerase activity. The reductase activity with HMKB is nearly normal.
S414 (= S414) mutation to A: Loss of reductoisomerase activity. The isomerase activity decreases 15-fold.; mutation to T: Loss of reductoisomerase activity. The isomerase activity decreases 24-fold.

3ulkA E. Coli ketol-acid reductoisomerase in complex with NADPH and mg2+ (see paper)
73% identity, 99% coverage: 1:489/492 of query aligns to 1:487/489 of 3ulkA

query
sites
3ulkA

M

M

A

A

N

N

Y

Y

F

F

N

N

S

T

L

L

N

N

L

L

R

R

Q

Q

L

L

A

A

Q

Q

L

L

G

G

Q

K

C

C

R

R

F

F

M

M

D

G

R

R

S

D

E

E

F

F

S

A

D

D

G

G

C

A

N

S

Y

Y

I

L

K

Q

D

G

W

K

N

K

I

V

V

V

I

I

L

V

G

G

C

C

G
|
G

A
|
A

Q
|
Q

G

G

L

L

N

N

Q

Q

G

G

L

L

N

N

M

M

R

R

D

D

S

S

G

G

L

L

N

D

I

I

A

S

Y

Y

A

A

L

L

R
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R

P

K

E

E

A

A

I

I

A

A

Q

E

K

K

R
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R

A

A

S
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S

W

W

Q

R

K

K

A

A

T

T

D

E

N

N

G

G

F

F

K

K

V

V

G

G

T

T

F

Y

E

E

L

L

I

I

P

P

T

Q

A

A

D

D

L

L

V

V

L

I

N

N

L
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L

T
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T

P
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P

D
|
D

K

K

Q
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Q

H

H

S

S

N

D

V
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V

V

V

S

R

A

T

V

V

M

Q

P

P

L

L

M

M

K

K

Q

D

G

G

A

A

T

A

L

L

S

G

Y

Y

S

S

H

H

G

G

F

F

N

N

I

I

V

V

E

E

E

V

G

G

M

E

Q

Q

I

I

R

R

P

K

D

D

I

I

T

T

V

V

M

M

V

V

A

A

P

P

K
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K

C

C

P

P

G

G

T

T

E

E

V

V

R

R

E

E

Y

Y

K

K

R

R

G

G

F

F

G

G

V

V

P

P

T

T

L

L

I

I

A

A

V

V

H

H

P

P

E

E

N

N

D

D

P

P

N

K

G

G

D

E

G

G

L

M

E

A

I

I

A

A

K

K

A

A

Y

W

A

A

S

A

A

A

T

T

G

G

D

H

R

R

A

A

G

G

V

V

L

L

Q

E

S

S

F

F

I

V

A

A

E

E

V

V

K

K

S

S

D
|
D

L

L

M

M

G

G

E
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E

Q

Q

T

T

I

I

L

L

C

C

G

G

M

M

L

L

Q

Q

T

A

G

G

A

S

I

L

L

L

G

C

Y

F

D

D

K

K

M

L

V

V

A

E

D

E

G

G

V

T

E

D

P

P

G

A

Y

Y

A

A

A

E

K

K

L

L

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I

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Q

Q

F

G

G

W

W

E

E

T

T

V

I

T

T

E

E

A

A

L

L

K

K

H

Q

G

G

I

I

T

T

N

L

M

M

D

D

R

R

L

L

S

S

N

N

P

P

A

A

K

K

I

L

K

R

A

A

F

Y

E

A

I

L

A

S

E

E

D

Q

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L

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K

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E

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M

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A

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P

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L

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K

K

H

H

M

M

D

D

I

I

S

S

G

G

E

E

F

F

S

S

R

S

T

G

M

M

Q

A

D

D

W

W

A

A

N

N

D

D

A

K

N

K

L

L

R

T

W

W

R

R

A

E

E

E

T

T

A

G

E

K

T

T

G

A

F

F

E

E

N

T

A

A

P

P

V

Q

S

Y

S

E

E

G

H

K

I

I

D

G

E

E

Q

Q

T

E

Y

Y

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F

D

D

K

K

G

G

I

V

F

L

L

M

V

I

A

A

M

M

I

V

K

K

A

A

G

G

V

V

E

E

L

L

A

A

F

F

D

E

T

T

M

M

V

V

S

D

A

S

G

G

I

I

V

I

E

E

S

S

A

A

Y

Y

E
|
E

S

S

L

L

H

H

E
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E

T

L

P

P

L

L

I

I

A

A

N

N

T

T

I

I

A

A

R

R

K

K

R

R

L

L

Y

Y

E

E

M

M

N

N

V

V

I

I

S

S

D

D

T

T

A

A

E

E

Y

Y

G

G

C

N

Y

Y

L

L

F

F

N

S

H

Y

A

A

A

C

V

V

P

P

M

L

L

L

R

K

D

P

Y

F

V

M

N

A

A

E

M

L

S

Q

P

P

E

G

Y

D

L

L

G

G

A

K

G

A

L

I

K

P

D

E

S

G

S

A

N

-

V

V

D

D

N

N

L

G

Q

Q

L

L

I

R

A

D

I

V

N

N

D

E

A

A

I

I

R

R

H

S

T

H

S

A

V

I

E

E

Y

Q

I

V

G

G

A

K

E

K

L

L

R

R

G

G

Y

Y

M

M

T

T

D

D

M

M

K

K

S

R

I

I

active site: K155 (= K155), D217 (= D217), E221 (= E221)
binding magnesium ion: D217 (= D217), E389 (= E389), E393 (= E393)
binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G46 (= G46), A47 (= A47), Q48 (= Q48), R68 (= R68), R76 (= R76), S78 (= S78), L105 (= L105), T106 (= T106), P107 (= P107), D108 (= D108), Q110 (= Q110), V114 (= V114)

5e4rA Crystal structure of domain-duplicated synthetic class ii ketol-acid reductoisomerase 2ia_kari-dd (see paper)
33% identity, 78% coverage: 35:420/492 of query aligns to 14:395/466 of 5e4rA

query
sites
5e4rA

I

I

K

K

D

N

W

K

N

T

I

I

V

A

I

I

L

L

G

G

C

Y

G
|
G

A
x
S

Q
|
Q

G

G

L

R

N

A

Q

W

G

A

L

L

N

N

M

L

R

R

D

D

S

S

G

G

L

L

N

N

I

V

A

V

Y

V

A

G

L

L

R

E

P

R

E

Q

A

G

I

-

A

-

Q

-

K

-

R

-

A

D

S
|
S

W

W

Q

R

K

R

A

A

T

I

D

D

N

D

G

G

F

F

K

K

V

P

G

M

T

Y

F

T

E

K

E

D

L

A

I

V

P

A

T

I

A

A

D

D

L

I

V

I

L

V

N

F

L
|
L

T
x
V

P
|
P

D
|
D

K

M

-
x
V

Q

Q

H

K

S

S

N

L

V

W

V

L

S

N

A

S

V

V

M

K

P

D

L

F

M

M

K

K

Q

K

G

G

A

A

T

D

L

L

S

V

Y

F

S
x
A

H
|
H

G

G

F

F

N

N

I

I

V

H

E

F

E

K

G

I

M

I

Q

E

I

P

R

P

P

K

D

D

I

S

T

D

V

V

V

Y

M

M

V

I

A

A

P

P

K
|
K

C

S

P
|
P

G

G

T

P

E

I

V

V

R

R

E

R

E

S

Y

Y

K

E

R

M

G

G

F

G

G

G

V

V

P

P

T

A

L

L

I

V

A

A

V

V

H

Y

P

-

E

-

N

Q

D

N

P

V

N

S

G

G

D

E

G

A

L

L

E

Q

I

K

A

A

K

L

A

A

Y

I

A

A

S

K

A

G

T

I

G

G

G

C

D

A

R

R

A

A

G

G

V

V

L

I

Q

E

S

S

S

T

F

F

I

K

A

E

E

E

V

T

K

E

S

T

D
|
D

L

L

M

F

G

G

E
|
E

Q

Q

T

V

I

I

L

L

C

V

G

G

M

G

L

I

Q

M

T

E

G

L

A

I

I

K

L

A

G

S

Y

F

D

E

K

T

M

L

V

V

A

E

D

E

G

G

V

Y

E

Q

P

P

G

E

Y

V

A

A

A

Y

K

F

L

E

I

T

Q

V

Q

N

G

E

W

L

E

K

T

L

V

I

T

V

E

D

A

L

L

I

K

Y

H

E

G

K

G

G

I

L

T

T

N

G

M

M

M

L

D

R

R

A

L

V

S

S

N

D

P

T

A

A

K

K

-

Y

-

G

-

I

-

T

I

V

K

G

A

K

F

F

E

I

I

I

A

D

E

K

D

S

L

V

K

R

E

D

I

K

L

M

Q

K

P

I

L

V

F

L

E

E

K

R

H

-

M

-

D

-

I

I

I

R

S

S

G

G

E

E

F

F

S

A

R

R

T

E

M

W

M

I

Q

K

D

E

W

Y

A

E

N

R

D

G

D

M

A

P

N

T

L

V

L

F

R

K

W

E

R

L

A

S

E

E

T

L

A

E

E

G

T

S

G

T

F

I

E

E

N

T

A

V

P

G

V

R

S

K

-

L

S

R

E

E

H

M

I

M

D

F

E

R

Q

G

T

M

Y

L

F

F

D

G

K

E

G

Q

I

V

F

I

L

L

V

V

A

G

M

G

I

I

K

M

A

E

G

L

V

I

E

K

L

A

A

S

F

F

D

E

T

T

M

L

V

V

S

E

A

E

G

G

I

Y

V

Q

E

P

E

E

S

V

A

A

Y

Y

Y

F

E

E

S

T

L

V

H

N

E

E

T

L

P

K

L

L

I

I

A

V

N

D

T

L

I

I

A

Y

R

E

K

K

R

G

L

L

Y

T

E

G

M

M

N

L

V

R

V
x
A

I
x
V

S
|
S

D

D

T

T

A
|
A

E

K

Y

Y

G

G

active site: K130 (= K155), D190 (= D217), E194 (= E221)
binding oxo(propan-2-ylamino)acetic acid: P132 (= P157), D190 (= D217), E194 (= E221), V388 (≠ I413), S389 (= S414), A392 (= A417)
binding magnesium ion: D190 (= D217), E194 (= E221)
binding nadp nicotinamide-adenine-dinucleotide phosphate: G25 (= G46), S26 (≠ A47), Q27 (= Q48), S52 (= S78), L79 (= L105), V80 (≠ T106), P81 (= P107), D82 (= D108), V84 (vs. gap), A106 (≠ S131), H107 (= H132), P132 (= P157), A387 (≠ V412), V388 (≠ I413), S389 (= S414)

7q03A Ketol-acid reductoisomerase from methanothermococcus thermolithotrophicus in the close state with NADP and mg2+ (see paper)
39% identity, 54% coverage: 35:302/492 of query aligns to 14:288/328 of 7q03A

query
sites
7q03A

I

V

K

K

D

D

W

K

N

T

I

I

V

A

I

V

L

I

G

G

C
x
Y

G
|
G

A
x
S

Q
|
Q

G

G

L

R

N

A

Q

Q

G

S

L

L

N

N

M

M

R

K

D

D

S

S

G

G

L

L

N

K

I

V

A

V

Y

V

A

G

L

L

R
|
R

P

P

E

N

A

G

I

-

A

-

Q

-

K

-

R

-

A

A

S
|
S

W

W

Q

N

K

K

A

A

T

K

D

E

N

D

G

G

F

H

K

E

V

V

G

L

T

S

F

I

E

E

L

A

I

A

P

E

T

K

A

A

D

D

L

I

V

I

L

H

N

I

L
|
L

T
x
I

P
|
P

D
|
D

K

E

Q
x
I

H

Q

S

G

N

D

V

V

V

Y

S

N

A

K

-

Q

V

I

M

K

P

P

L

Y

M

L

K

K

Q

E

G

G

A

K

T

T

L

L

S

S

Y

F

S

S

H
|
H

G

G

F

Y

N

N

I

I

V

-

E

H

E

Y

G

G

M

Y

Q

I

I

V

R

P

P

P

D

E

-

G

I

V

T

N

V

V

M

M

V

V

A

A

P

P

K

K

C

S

P
|
P

G

G

T

A

E

M

V

V

R

R

E

R

E

T

Y

Y

K

E

R

E

G

G

F

F

G

G

V

V

P

P

T

G

L

L

I

V

A

C

V

V

H

-

P

-

E

E

N

K

D

D

P

A

N

T

G

G

D

D

G

A

L

L

E

D

I

I

A

A

K

L

A

G

Y

M

A

A

S

K

A

G

T

V

G

G

G

L

D

T

R

R

A

A

G

G

V

V

L

I

Q

Q

S

T

F

F

I

R

A

E

E

E

V

T

K

E

S

T

D
|
D

L

L

M

F

G

G

E
|
E

Q

Q

T

A

I

V

L

L

C

C

G

G

M

G

L

V

Q

T

T

E

G

L

A

I

I

K

L

A

G

G

Y

F

D

E

K

T

M

L

V

V

A

E

D

A

G

G

V

Y

E

S

P

P

G

E

Y

M

A

A

-

Y

-

F

-

E

-

T

-

C

-

H

-

E

A

L

K

K

L

L

I

I

-

I

-

D

-

L

-

I

-

Y

Q

Q

Q

K

G

G

-

F

-

A

-

G

-

M

W

W

E

N

T

D

V

V

T

S

E

N

A

T

L

A

K

E

H

Y

G

G

I

L

T

T

N

R

M

R

M

S

D

R

R

V

L

I

S

N

N

E

P

Q

A

S

K

R

I

Q

K

-

A

-

F

-

E

E

I

M

A

R

E

K

D

I

L

L

K

K

E

E

I

I

L

Q

Q

D

P

G

L

R

F

F

E

T

K

K

binding magnesium ion: D190 (= D217), E194 (= E221)
binding nadp nicotinamide-adenine-dinucleotide phosphate: Y24 (≠ C45), G25 (= G46), S26 (≠ A47), Q27 (= Q48), R47 (= R68), S52 (= S78), L79 (= L105), I80 (≠ T106), P81 (= P107), D82 (= D108), I84 (≠ Q110), H107 (= H132), P132 (= P157)

7rduA Crystal structure of campylobacter jejuni keto said reductoisomerase in complex with magnesium and oxidixized and reduced NADPH
32% identity, 61% coverage: 33:333/492 of query aligns to 13:305/329 of 7rduA

query
sites
7rduA

N

N

Y

L

I

I

K

K

D

S

W

K

N

K

I

V

V

A

I

I

L

I

G
|
G

C
x
F

G
|
G

A
x
S

Q
|
Q

G

G

L

H

N

A

Q

H

G

A

L

M

N

N

M

L

R

R

D

D

S

N

G

G

L

V

N

N

I

V

A

T

Y

I

A

G

L

L

R
|
R

P

E

E

G

A
x
S

I

V

A

-

Q

-

K

-

R

-

A

-

S
|
S

W

A

Q

V

K

K

A

A

T

K

D

N

N

A

G

G

F

F

K

E

V

V

G

M

T

S

F

V

E

S

E

E

L

A

I

S

P

K

T

I

A

A

D

D

L

V

V

I

L

M

N

I

L
|
L

T
x
A

P
|
P

D
|
D

K

E

Q

I

H

Q

S

A

N

D

V
x
I

V

F

S

N

A

V

-

E

V

I

M

K

P

P

L

N

M

L

K

S

Q

E

G

G

A

K

T

A

L

I

S

A

Y

F

S
x
A

H
|
H

G

G

F

F

N

N

I

I

V

H

E

Y

E

G

G

Q

M

I

Q

V

I

V

R

P

P

K

D

G

I

V

T

D

V

V

V

I

M

M

V

I

A

A

P
|
P

K
|
K

C
x
A

P

P

G

G

T

H

E

T

V

V

R

R

E

N

E

E

Y

F

K

T

R

L

G

G

F

G

G

G

V

T

P

P

T

C

L

L

I

I

A

A

V

I

H

H

P

Q

E

D

N

E

D

S

P

K

N

N

G

A

D

K

G

N

L

L

E

-

I

-

A

A

K

L

A

S

Y

Y

A

A

S

S

A

A

T

I

G

G

D

G

R

R

A

T

G

G

V

I

L

I

Q

E

S

T

F

F

I

K

A

A

E

E

V

T

K

E

S

T

D

D

L

L

M

F

G

G

E

E

Q

Q

T

A

I

V

L

L

C

C

G

G

M

G

L

L

Q

S

T

A

G

L

A

I

I

Q

L

A

G

G

Y

F

D

E

K

T

M

L

V

V

A

E

D

A

G

G

V

Y

E

E

P

P

G

E

Y

M

A

A

A

Y

K

F

L

E

I

C

Q

L

Q

H

G

E

W

M

E

K

T

L

V

I

T

V

E

D

A

L

L

I

K

Y

H

Q

G

G

I

I

T

A

N

D

M

M

M

R

D

Y

R

S

L

I

S

S

N

N

P

T

A

A

K

E

I

Y

K

G

A

D

F

Y

-

I

-

T

-

G

-

P

-

K

E

I

I

I

A

T

E

E

D

E

L

T

K

K

E

K

I

A

L

M

Q

K

P

G

L

V

F

-

E

-

K

-

H

-

M

L

D

K

D

D

I

I

I

Q

S

N

G

G

E

V

F

F

S

A

R

K

T

D

M

F

M

I

Q

L

D

E

W

R

A

-

N

-

D

-

D

R

A

A

N

G

L

F

L

A

R

R

W

M

R

H

A

A

E

E

binding nadp nicotinamide-adenine-dinucleotide phosphate: G24 (= G44), G26 (= G46), S27 (≠ A47), Q28 (= Q48), R48 (= R68), S51 (≠ A71), S53 (= S78), A81 (≠ T106), P82 (= P107), D83 (= D108), I89 (≠ V114), A107 (≠ S131), H108 (= H132), P130 (= P154), K131 (= K155), A132 (≠ C156)
binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G24 (= G44), F25 (≠ C45), G26 (= G46), S27 (≠ A47), Q28 (= Q48), S51 (≠ A71), S53 (= S78), L80 (= L105), P82 (= P107), D83 (= D108), I89 (≠ V114), A107 (≠ S131), H108 (= H132)

7latA Campylobacter jejuni keto-acid reductoisomerase in complex with mg2+
32% identity, 61% coverage: 33:333/492 of query aligns to 13:305/329 of 7latA

query
sites
7latA

N

N

Y

L

I

I

K

K

D

S

W

K

N

K

I

V

V

A

I

I

L

I

G

G

C

F

G

G

A

S

Q

Q

G

G

L

H

N

A

Q

H

G

A

L

M

N

N

M

L

R

R

D

D

S

N

G

G

L

V

N

N

I

V

A

T

Y

I

A

G

L

L

R

R

P

E

E

G

A

S

I

V

A

-

Q

-

K

-

R

-

A

-

S

S

W

A

Q

V

K

K

A

A

T

K

D

N

N

A

G

G

F

F

K

E

V

V

G

M

T

S

F

V

E

S

E

E

L

A

I

S

P

K

T

I

A

A

D

D

L

V

V

I

L

M

N

I

L

L

T

A

P

P

D

D

K

E

Q

I

H

Q

S

A

N

D

V

I

V

F

S

N

A

V

-

E

V

I

M

K

P

P

L

N

M

L

K

S

Q

E

G

G

A

K

T

A

L

I

S

A

Y

F

S

A

H

H

G

G

F

F

N

N

I

I

V

H

E

Y

E

G

G

Q

M

I

Q

V

I

V

R

P

P

K

D

G

I

V

T

D

V

V

V

I

M

M

V

I

A

A

P

P

K

K

C

A

P

P

G

G

T

H

E

T

V

V

R

R

E

N

E

E

Y

F

K

T

R

L

G

G

F

G

G

G

V

T

P

P

T

C

L

L

I

I

A

A

V

I

H

H

P

Q

E

D

N

E

D

S

P

K

N

N

G

A

D

K

G

N

L

L

E

-

I

-

A

A

K

L

A

S

Y

Y

A

A

S

S

A

A

T

I

G

G

D

G

R

R

A

T

G

G

V

I

L

I

Q

E

S

T

F

F

I

K

A

A

E

E

V

T

K

E

S

T

D
|
D

L

L

M

F

G

G

E
|
E

Q

Q

T

A

I

V

L

L

C

C

G

G

M

G

L

L

Q

S

T

A

G

L

A

I

I

Q

L

A

G

G

Y

F

D

E

K

T

M

L

V

V

A

E

D

A

G

G

V

Y

E

E

P

P

G

E

Y

M

A

A

A

Y

K

F

L

E

I

C

Q

L

Q

H

G

E

W

M

E

K

T

L

V

I

T

V

E

D

A

L

L

I

K

Y

H

Q

G

G

I

I

T

A

N

D

M

M

M

R

D

Y

R

S

L

I

S

S

N

N

P

T

A

A

K

E

I

Y

K

G

A

D

F

Y

-

I

-

T

-

G

-

P

-

K

E

I

I

I

A

T

E

E

D

E

L

T

K

K

E

K

I

A

L

M

Q

K

P

G

L

V

F

-

E

-

K

-

H

-

M

L

D

K

D

D

I

I

I

Q

S

N

G

G

E

V

F

F

S

A

R

K

T

D

M

F

M

I

Q

L

D

E

W

R

A

-

N

-

D

-

D

R

A

A

N

G

L

F

L

A

R

R

W

M

R

H

A

A

E

E

binding magnesium ion: D191 (= D217), E195 (= E221)

E0SRA9 Ketol-acid reductoisomerase (NAD(P)(+)); KARI; Acetohydroxy-acid isomeroreductase; AHIR; Alpha-keto-beta-hydroxylacyl reductoisomerase; Ketol-acid reductoisomerase type 1; Ketol-acid reductoisomerase type I; EC 1.1.1.383 from Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1) (see paper)
35% identity, 58% coverage: 35:320/492 of query aligns to 15:295/335 of E0SRA9

query
sites
E0SRA9

I

I

K

K

D

N

W

K

N

T

I

I

V

A

I

I

L

L

G

G

C
x
Y

G
|
G

A
x
S

Q
|
Q

G

G

L

R

N

A

Q

W

G

A

L

L

N

N

M

L

R

R

D

D

S

S

G

G

L

L

N

N

I

V

A

V

Y

V

A

G

L

L

R

E

P
x
R

E

Q

A

G

I

-

A

-

Q

-

K

-

R

-

A

D

S
|
S

W

W

Q

R

K

R

A

A

T

I

D

D

N

D

G

G

F

F

K

K

V

P

G

M

T

Y

F

T

E

K

E

D

L

A

I

V

P

A

T

I

A

A

D

D

L

I

V

I

L

V

N

F

L

L

T

V

P

P

D
|
D

K
x
M

-
x
V

Q
|
Q

H

K

S

S

N

L

V

W

V

L

S

N

A

S

V

V

M

K

P

D

L

F

M

M

K

K

Q

K

G

G

A

A

T

D

L

L

S

V

Y

F

S

A

H

H

G

G

F

F

N

N

I

I

V

H

E

F

E

K

G

I

M

I

Q

E

I

P

R

P

P

K

D

D

I

S

T

D

V

V

V

Y

M

M

V

I

A

A

P

P

K

K

C

S

P

P

G
|
G

T

P

E

I

V

V

R

R

E

R

E

S

Y

Y

K

E

R

M

G

G

F

G

G

G

V

V

P

P

T

A

L

L

I

V

A

A

V

V

H

Y

P

-

E

-

N

Q

D

N

P

V

N

S

G

G

D

E

G

A

L

L

E

Q

I

K

A

A

K

L

A

A

Y

I

A

A

S

K

A

G

T

I

G

G

G

C

D

A

R

R

A

A

G

G

V

V

L

I

Q

E

S

S

S

T

F

F

I

K

A

E

E

E

V

T

K

E

S

T

D
|
D

L

L

M

F

G

G

E
|
E

Q

Q

T

V

I

I

L

L

C

V

G

G

M

G

L

I

Q

M

T

E

G

L

A

I

I

K

L

A

G

S

Y

F

D

E

K

T

M

L

V

V

A

E

D

E

G

G

V

Y

E

Q

P

P

G

E

Y

V

A

A

A

Y

K

F

L

E

I

T

Q

V

Q

N

G

E

W

L

E

K

T

L

V

I

T

V

E

D

A

L

L

I

K

Y

H

E

G

K

G

G

I

L

T

T

N

G

M

M

M

L

D

R

R

A

L

V

S

S

N

D

P

T

A

A

K

K

-

Y

-

G

-

I

-

T

I

V

K

G

A

K

F

F

E

I

I

I

A

D

E

K

D

S

L

V

K

R

E

D

I

K

L

M

Q

K

P

I

L

V

F

L

E

E

K

R

H

-

M

-

D

-

I

I

I

R

S

S

G

G

E

E

F

F

S

A

R

R

T

E

M

W

M

I

Q

K

D

E

W

Y

YGSQ 25:28 (≠ CGAQ 45:48) binding
R49 (≠ P69) binding
S53 (= S78) binding
DMVQ 83:86 (≠ DK-Q 108:110) binding
G134 (= G158) binding
D191 (= D217) binding
E195 (= E221) binding

4xdzA Holo structure of ketol-acid reductoisomerase from ignisphaera aggregans (see paper)
35% identity, 58% coverage: 35:320/492 of query aligns to 14:294/328 of 4xdzA

query
sites
4xdzA

I

I

K

K

D

N

W

K

N

T

I

I

V

A

I

I

L

L

G
|
G

C

Y

G
|
G

A
x
S

Q
|
Q

G

G

L

R

N

A

Q

W

G

A

L

L

N

N

M

L

R

R

D

D

S

S

G

G

L

L

N

N

I

V

A

V

Y

V

A

G

L

L

R
x
E

P
x
R

E

Q

A

G

I

-

A

-

Q

-

K

-

R

-

A

D

S
|
S

W

W

Q

R

K

R

A

A

T

I

D

D

N

D

G

G

F

F

K

K

V

P

G

M

T

Y

F

T

E

K

E

D

L

A

I

V

P

A

T

I

A

A

D

D

L

I

V

I

L

V

N

F

L
|
L

T
x
V

P
|
P

D
|
D

K

M

-
x
V

Q

Q

H

K

S

S

N

L

V

W

V

L

S

N

A

S

V

V

M

K

P

D

L

F

M

M

K

K

Q

K

G

G

A

A

T

D

L

L

S

V

Y

F

S
x
A

H
|
H

G

G

F

F

N

N

I

I

V

H

E

F

E

K

G

I

M

I

Q

E

I

P

R

P

P

K

D

D

I

S

T

D

V

V

V

Y

M

M

V

I

A

A

P

P

K
|
K

C

S

P
|
P

G

G

T

P

E

I

V

V

R

R

E

R

E

S

Y

Y

K

E

R

M

G

G

F

G

G

G

V

V

P

P

T

A

L

L

I

V

A

A

V

V

H

Y

P

-

E

-

N

Q

D

N

P

V

N

S

G

G

D

E

G

A

L

L

E

Q

I

K

A

A

K

L

A

A

Y

I

A

A

S

K

A

G

T

I

G

G

G

C

D

A

R

R

A

A

G

G

V

V

L

I

Q

E

S

S

S

T

F

F

I

K

A

E

E

E

V

T

K

E

S

T

D
|
D

L

L

M

F

G

G

E
|
E

Q

Q

T

V

I

I

L
|
L

C

V

G

G

M

G

L

I

Q

M

T

E

G

L

A

I

I

K

L

A

G

S

Y

F

D

E

K

T

M

L

V

V

A

E

D

E

G

G

V

Y

E

Q

P

P

G

E

Y

V

A

A

A

Y

K

F

L

E

I

T

Q

V

Q

N

G
x
E

W

L

E

K

T

L

V

I

T

V

E

D

A

L

L

I

K

Y

H

E

G

K

G

G

I

L

T

T

N

G

M

M

M

L

D

R

R

A

L
x
V

S
|
S

N

D

P

T

A
|
A

K

K

-

Y

-

G

-

I

-

T

I

V

K

G

A

K

F

F

E

I

I

I

A

D

E

K

D

S

L

V

K

R

E

D

I

K

L

M

Q

K

P

I

L

V

F

L

E

E

K

R

H

-

M

-

D

-

I

I

I

R

S

S

G

G

E

E

F

F

S

A

R

R

T

E

M

W

M

I

Q

K

D

E

W

Y

active site: K130 (= K155), D190 (= D217), E194 (= E221)
binding oxo(propan-2-ylamino)acetic acid: P132 (= P157), D190 (= D217), E194 (= E221), L198 (= L225), E230 (≠ G257), V250 (≠ L277), S251 (= S278), A254 (= A281)
binding magnesium ion: D190 (= D217), E194 (= E221)
binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G23 (= G44), G25 (= G46), S26 (≠ A47), Q27 (= Q48), E47 (≠ R68), R48 (≠ P69), S52 (= S78), L79 (= L105), V80 (≠ T106), P81 (= P107), D82 (= D108), V84 (vs. gap), A106 (≠ S131), H107 (= H132), P132 (= P157)

4xiyA Crystal structure of ketol-acid reductoisomerase from azotobacter (see paper)
31% identity, 61% coverage: 35:335/492 of query aligns to 14:309/328 of 4xiyA

query
sites
4xiyA

I

I

K

Q

D

S

W

K

N

K

I

V

V

A

I

I

L

I

G

G

C

Y

G

G

A

S

Q

Q

G

G

L

H

N

A

Q

H

G

A

L

C

N

N

M

L

R

K

D

D

S

S

G

G

L

V

N

D

I

V

A

Y

Y

V

A

G

L

L

R

R

P

A

E

G

A

S

I

-

A

-

Q

-

K

-

R

-

A

A

S

S

W

V

Q

A

K

K

A

A

T

E

D

A

N

H

G

G

F

L

K

T

V

V

G

K

T

S

F

V

E

K

E

D

L

A

I

V

P

A

T

A

A

A

D

D

L

V

V

V

L

M

N

I

L

L

T

T

P

P

D

D

K

E

Q

F

H

Q

S

G

N

R

V

L

V

Y

S

K

-

D

A

E

V

I

M

E

P

P

L

N

M

L

K

K

Q

K

G

G

A

A

T

T

L

L

S

A

Y

F

S

A

H

H

G

G

F

F

N

S

I

I

V

H

E

Y

E

N

G

Q

M

V

Q

V

I

P

R

R

P

A

D

D

I

L

T

D

V

V

V

I

M

M

V

I

A

A

P

P

K
|
K

C

A

P

P

G

G

T

H

E

T

V

V

R

R

E

S

E

E

Y

F

K

V

R

R

G

G

F

G

G

G

V

I

P

P

T

D

L

L

I

I

A

A

V

V

H

Y

P

-

E

-

N

Q

D

D

P

A

N

S

G

G

D

N

G

A

L

K

E

N

I

L

A

A

K

L

A

S

Y

Y

A

A

S

C

A

G

T

V

G

G

D

G

R

R

A

T

G

G

V

I

L

I

Q

E

S

T

F

F

I

K

A

D

E

E

V

T

K

E

S

T

D
|
D

L

L

M

F

G

G

E
|
E

Q

Q

T

A

I

V

L

L

C

C

G

G

M

G

L

C

Q

V

T

E

G

L

A

V

I

K

L

A

G

G

Y

F

D

E

K

T

M

L

V

V

A

E

D

A

G

G

V

Y

E

A

P

P

G

E

Y

M

A

A

A

Y

K

F

L
x
E

I

C

Q

L

Q

H

G
x
E

W

L

E

K

T

L

V

I

T

V

E

D

A

L

L

M

K

F

H

E

G

G

I

I

T

A

N

N

M

M

M

N

D

Y

R

S

L

I

S

S

N

N

P

N

A

A

K

E

I

Y

K

G

A

E

F

Y

E

V

I

T

A

G

-

P

E

E

D

V

L

I

K

N

E

E

I

Q

L

S

Q

R

P

Q

L

A

F

M

E

R

K

N

H

A

M

L

D

K

D

R

I

I

I

Q

S

D

G

G

E

E

F

Y

S

A

R

K

T

M

M

F

M

I

Q

T

D

E

W

G

A

A

N

A

D

N

D

Y

A

P

N

S

L

M

L

T

R

A

W

Y

R

R

A

R

E

N

T

N

A

A

active site: K130 (= K155), D190 (= D217), E194 (= E221)
binding fe (iii) ion: D190 (= D217), E194 (= E221)
binding magnesium ion: E226 (≠ L253), E230 (≠ G257)

C1DFH7 Ketol-acid reductoisomerase (NADP(+)); KARI; Acetohydroxy-acid isomeroreductase; AHIR; Alpha-keto-beta-hydroxylacyl reductoisomerase; Ketol-acid reductoisomerase type 1; Ketol-acid reductoisomerase type I; EC 1.1.1.86 from Azotobacter vinelandii (strain DJ / ATCC BAA-1303) (see paper)
31% identity, 61% coverage: 35:335/492 of query aligns to 14:309/338 of C1DFH7

query
sites
C1DFH7

I

I

K

Q

D

S

W

K

N

K

I

V

V

A

I

I

L

I

G

G

C

Y

G

G

A

S

Q

Q

G

G

L

H

N

A

Q

H

G

A

L

C

N

N

M

L

R

K

D

D

S

S

G

G

L

V

N

D

I

V

A

Y

Y

V

A

G

L

L

R

R

P

A

E

G

A

S

I

-

A

-

Q

-

K

-

R

-

A

A

S

S

W

V

Q

A

K

K

A

A

T

E

D

A

N

H

G

G

F

L

K

T

V

V

G

K

T

S

F

V

E

K

E

D

L

A

I

V

P

A

T

A

A

A

D

D

L

V

V

V

L

M

N

I

L

L

T

T

P

P

D

D

K

E

Q

F

H

Q

S

G

N

R

V

L

V

Y

S

K

-

D

A

E

V

I

M

E

P

P

L

N

M

L

K

K

Q

K

G

G

A

A

T

T

L

L

S

A

Y

F

S

A

H

H

G

G

F

F

N

S

I

I

V

H

E

Y

E

N

G

Q

M

V

Q

V

I

P

R

R

P

A

D

D

I

L

T

D

V

V

V

I

M

M

V

I

A

A

P

P

K

K

C

A

P

P

G

G

T

H

E

T

V

V

R

R

E

S

E

E

Y

F

K

V

R

R

G

G

F

G

G

G

V

I

P

P

T

D

L

L

I

I

A

A

V

V

H

Y

P

-

E

-

N

Q

D

D

P

A

N

S

G

G

D

N

G

A

L

K

E

N

I

L

A

A

K

L

A

S

Y

Y

A

A

S

C

A

G

T

V

G

G

D

G

R

R

A

T

G

G

V

I

L

I

Q

E

S

T

F

F

I

K

A

D

E

E

V

T

K

E

S

T

D
|
D

L

L

M

F

G

G

E

E

Q

Q

T

A

I

V

L

L

C

C

G

G

M

G

L

C

Q

V

T

E

G

L

A

V

I

K

L

A

G

G

Y

F

D

E

K

T

M

L

V

V

A

E

D

A

G

G

V

Y

E

A

P

P

G

E

Y

M

A

A

A

Y

K

F

L
x
E

I

C

Q

L

Q

H

G
x
E

W

L

E

K

T

L

V

I

T

V

E

D

A

L

L

M

K

F

H

E

G

G

I

I

T

A

N

N

M

M

M

N

D

Y

R

S

L

I

S

S

N

N

P

N

A

A

K

E

I

Y

K

G

A

E

F

Y

E

V

I

T

A

G

-

P

E

E

D

V

L

I

K

N

E

E

I

Q

L

S

Q

R

P

Q

L

A

F

M

E

R

K

N

H

A

M

L

D

K

D

R

I

I

I

Q

S

D

G

G

E

E

F

Y

S

A

R

K

T

M

M

F

M

I

Q

T

D

E

W

G

A

A

N

A

D

N

D

Y

A

P

N

S

L

M

L

T

R

A

W

Y

R

R

A

R

E

N

T

N

A

A

D190 (= D217) binding
E226 (≠ L253) binding
E230 (≠ G257) binding

4tskA Ketol-acid reductoisomerase from alicyclobacillus acidocaldarius (see paper)
34% identity, 59% coverage: 35:322/492 of query aligns to 14:296/333 of 4tskA

query
sites
4tskA

I

L

K

A

D

D

W

K

N

R

I

I

V

A

I

V

L

I

G

G

C
x
Y

G
|
G

A
x
S

Q
|
Q

G

G

L

H

N

A

Q

H

G

A

L

Q

N

N

M

L

R

R

D

D

S

S

G

G

L

F

N

D

I

V

A

V

Y

I

A

G

L
|
L

R
|
R

P

P

E

G

A

S

I

-

A

-

Q

-

K

-

R

-

A

-

S
|
S

W

W

Q

A

K

K

A

A

T

E

D

A

N

D

G

G

F

F

K

R

V

V

G

M

T

A

F

V

E

G

E

E

L

A

I

V

P

E

T

E

A

S

D

D

L

V

V

I

L

M

N

I

L
|
L

T
x
L

P
|
P

D
|
D

K

E

Q

R

H

Q

S

P

N

A

V

V

V

Y

S

E

-

R

A

E

V

I

M

R

P

P

L

Y

M

L

K

T

Q

A

G

G

A

K

T

A

L

L

S

A

Y

F

S

A

H
|
H

G

G

F

F

N

N

I

I

V

H

E

F

E

S

G

Q

M

I

Q

Q

I

P

R

P

P

K

D

D

I

V

T

D

V

V

V

F

M

M

V

V

A

A

P

P

K
|
K

C

G

P
|
P

G

G

T

H

E

L

V

V

R

R

E

R

E

V

Y

Y

K

E

R

A

G

G

F

G

G

G

V

V

P

P

T

A

L

L

I

I

A

A

V

V

H

H

P

-

E

-

N

Q

D

D

P

A

N

S

G

G

D

Q

G

A

L

K

E

D

I

L

A

A

K

L

A

A

Y

Y

A

A

S

R

A

G

T

I

G

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G

A

D

G

R

R

A

A

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L

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F

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A

E

E

E

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E

S

T

D
|
D

L

L

M

F

G

G

E
|
E

Q

Q

T

A

I

V

L

L

C

C

G

G

M

G

L

L

Q

S

T

A

G

L

A

I

I

K

L

A

G

G

Y

F

D

E

K

T

M

L

V

V

A

E

D

A

G

G

V

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E

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P

P

G

E

Y

I

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A

A

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F

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E

I

C

Q

L

Q

H

G

E

W

M

E

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I

T

V

E

D

A

L

L

I

K

Y

H

E

G

G

I

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E

N

Y

M

M

M
x
R

D
x
Y

R

S

L
x
I

S

S

N
x
D

P

T

A

A

K
x
Q

I

W

K

G

A

D

F

F

E

T

-

S

-

G

-

P

-

R

-

I

I

I

A

N

E

E

D

E

L

T

K

K

E

K

I

E

L

M

Q

R

P

R

L

I

F

-

E

-

K

-

H

-

M

L

D

A

D

D

I

I

I

Q

S

S

G

G

E

A

F

F

S

A

R

K

T

S

-

W

M

I

M

L

Q

E

D

N

W

Q

A

A

N

N

active site: K129 (= K155), D189 (= D217), E193 (= E221)
binding magnesium ion: D189 (= D217), D189 (= D217), E193 (= E221), E193 (= E221), R246 (≠ M274), Y247 (≠ D275), I249 (≠ L277), D251 (≠ N279), Q254 (≠ K282)
binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: Y24 (≠ C45), G25 (= G46), S26 (≠ A47), Q27 (= Q48), L46 (= L67), R47 (= R68), S51 (= S78), L78 (= L105), L79 (≠ T106), P80 (= P107), D81 (= D108), H106 (= H132), P131 (= P157)

C8WR67 Ketol-acid reductoisomerase (NADP(+)); KARI; Acetohydroxy-acid isomeroreductase; AHIR; Alpha-keto-beta-hydroxylacyl reductoisomerase; Ketol-acid reductoisomerase type 1; Ketol-acid reductoisomerase type I; EC 1.1.1.86 from Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA) (Bacillus acidocaldarius) (see paper)
34% identity, 59% coverage: 35:322/492 of query aligns to 15:297/344 of C8WR67

query
sites
C8WR67

I

L

K

A

D

D

W

K

N

R

I

I

V

A

I

V

L

I

G

G

C
x
Y

G
|
G

A
x
S

Q
|
Q

G

G

L

H

N

A

Q

H

G

A

L

Q

N

N

M

L

R

R

D

D

S

S

G

G

L

F

N

D

I

V

A

V

Y

I

A

G

L

L

R
|
R

P

P

E

G

A

S

I

-

A

-

Q

-

K

-

R

-

A

-

S
|
S

W

W

Q

A

K

K

A

A

T

E

D

A

N

D

G

G

F

F

K

R

V

V

G

M

T

A

F

V

E

G

E

E

L

A

I

V

P

E

T

E

A

S

D

D

L

V

V

I

L

M

N

I

L

L

T

L

P

P

D
|
D

K
x
E

Q
x
R

H
x
Q

S

P

N

A

V

V

V

Y

S

E

-

R

A

E

V

I

M

R

P

P

L

Y

M

L

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T

Q

A

G

G

A

K

T

A

L

L

S

A

Y

F

S

A

H

H

G

G

F

F

N

N

I

I

V

H

E

F

E

S

G

Q

M

I

Q

Q

I

P

R

P

P

K

D

D

I

V

T

D

V

V

V

F

M

M

V

V

A

A

P

P

K

K

C

G

P

P

G
|
G

T

H

E

L

V

V

R

R

E

R

E

V

Y

Y

K

E

R

A

G

G

F

G

G

G

V

V

P

P

T

A

L

L

I

I

A

A

V

V

H

H

P

-

E

-

N

Q

D

D

P

A

N

S

G

G

D

Q

G

A

L

K

E

D

I

L

A

A

K

L

A

A

Y

Y

A

A

S

R

A

G

T

I

G

G

G

A

D

G

R

R

A

A

G

G

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I

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L

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S

T

F

F

I

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A

E

E

E

V

T

K

E

S

T

D
|
D

L

L

M

F

G

G

E
|
E

Q

Q

T

A

I

V

L

L

C

C

G

G

M

G

L

L

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S

T

A

G

L

A

I

I

K

L

A

G

G

Y

F

D

E

K

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M

L

V

V

A

E

D

A

G

G

V

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E

Q

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P

G

E

Y

I

A

A

A

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F

L
x
E

I

C

Q

L

Q

H

G

E

W

M

E

K

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L

V

I

T

V

E

D

A

L

L

I

K

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G

I

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M

M

M

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Y

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D

P

T

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Q

I

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G

A

D

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F

E

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S

-

G

-

P

-

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-

I

I

I

A

N

E

E

D

E

L

T

K

K

E

K

I

E

L

M

Q

R

P

R

L

I

F

-

E

-

K

-

H

-

M

L

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A

D

D

I

I

I

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S

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G

E

A

F

F

S

A

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M

I

M

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E

D

N

W

Q

A

A

N

N

YGSQ 25:28 (≠ CGAQ 45:48) binding
R48 (= R68) binding ; mutation to P: Inversion of the cofactor specificity from NADPH to NADH.
S52 (= S78) binding ; mutation to D: Inversion of the cofactor specificity from NADPH to NADH.
DERQ 82:85 (≠ DKQH 108:111) binding
G133 (= G158) binding
D190 (= D217) binding
E194 (= E221) binding
E226 (≠ L253) binding

4xdyA Structure of nadh-preferring ketol-acid reductoisomerase from an uncultured archean (see paper)
33% identity, 58% coverage: 35:320/492 of query aligns to 14:299/331 of 4xdyA

query
sites
4xdyA

I

L

K

R

D

D

W

K

N

T

I

I

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I

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G

C

Y

G
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G

A
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A

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G

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D

N

A

Q

Q

G

A

L

N

N

C

M

L

R

K

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D

S

S

G

G

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I

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N

I

V

A

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Y

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A

G

L
x
E

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E

E

I

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x
L

I

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G

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N

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K

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x
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A

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S
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S

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W

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E

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K

A

A

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K

D

E

N

D

G

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G

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F

I

E

D

E

K

L

A

I

A

P

E

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K

A

G

D

D

L

V

V

V

L

H

N

I

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L

T
x
L

P
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P

D
|
D

K

E

-

V

Q

Q

H

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S

A

N
x
I

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S

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A

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P

P

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M

L

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A

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G

A

K

T

A

L

L

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H
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H

G

G

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F

N

N

I

I

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C

E

F

E

K

G

R

M

I

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I

P

R

P

P

E

D

D

I

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T

D

V

V

V

I

M

M

V

V

A

A

P

P

K
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K

C

A

P
|
P

G

G

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T

E

E

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E

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R

E

K

E

A

Y

Y

K

L

R

E

G

G

F

F

G

G

V

V

P

P

T

G

L

L

I

V

A

A

V

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H

-

P

-

E

K

N

Q

D

N

P

P

N

S

G

G

D

E

G

A

L

R

E

E

I

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A

A

K

L

A

A

Y

M

A

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K

A

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A

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F

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A

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E

E

V

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S

E

D
|
D

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G

G

E
|
E

Q

Q

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C

I

V

L

L

C

C

G

G

M

G

L

L

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V

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E

G

L

A

M

I

R

L

N

G

G

Y

F

D

E

K

V

M

L

V

V

A

E

D

A

G

G

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Y

E

P

P

P

G

E

Y

M

A

A

A

Y

K

F

L

E

I

C

Q

V

Q

H

G
x
E

W

M

E

K

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L

V
x
I

T

V

E

D

A

L

L

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W

H

Q

G

G

I

I

T

K

N

R

M

M

M

A

D

E

R

V

L
x
I

S
|
S

N

N

P

T

A
|
A

K

E

I

Y

K

G

A

M

F

W

E

A

I

V

A

G

E

H

D

-

L

-

K

-

E

Q

I

I

L

I

Q

G

P

P

L

E

F

V

E

K

K

E

H

K

M

M

D

K

D

E

I

A

I

L

-

K

-

R

-

V

-

E

S

N

G

G

E

E

F

F

S

A

R

N

T

E

M

W

M

V

Q

D

D

E

W

Y

active site: K135 (= K155), D195 (= D217), E199 (= E221)
binding n-hydroxy-n-isopropyloxamic acid: P137 (= P157), D195 (= D217), E199 (= E221), E235 (≠ G257), I239 (≠ V261), I255 (≠ L277), S256 (= S278), A259 (= A281)
binding magnesium ion: D195 (= D217), E199 (= E221)
binding 1,4-dihydronicotinamide adenine dinucleotide: G25 (= G46), A26 (= A47), Q27 (= Q48), E46 (≠ L67), L50 (≠ A71), N55 (≠ R76), S57 (= S78), L84 (= L105), L85 (≠ T106), P86 (= P107), D87 (= D108), I93 (≠ N113), H112 (= H132), P137 (= P157)

Q64BR7 Ketol-acid reductoisomerase (NAD(+)); KARI; Acetohydroxy-acid isomeroreductase; AHIR; Alpha-keto-beta-hydroxylacyl reductoisomerase; Ketol-acid reductoisomerase type 1; Ketol-acid reductoisomerase type I; EC 1.1.1.382 from Uncultured archaeon GZfos26G2 (see paper)
33% identity, 58% coverage: 35:320/492 of query aligns to 14:299/332 of Q64BR7

query
sites
Q64BR7

I

L

K

R

D

D

W

K

N

T

I

I

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A

I

V

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M

G

G

C
x
Y

G
|
G

A
|
A

Q
|
Q

G

G

L

D

N

A

Q

Q

G

A

L

N

N

C

M

L

R

K

D

D

S

S

G

G

L

I

N

N

I

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V

Y

I

A

G

L
x
E

R

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P

E

E

I

A

L

I

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A

G

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K

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x
N

A

P

S
|
S

W

W

Q

E

K

K

A

A

T

K

D

E

N

D

G

G

F

F

K

E

V

V

G

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P

F

I

E

D

E

K

L

A

I

A

P

E

T

K

A

G

D

D

L

V

V

V

L

H

N

I

L

L

T

L

P

P

D
|
D

K
x
E

-
x
V

Q
|
Q

H

P

S

A

N

I

V

Y

V

E

S

N

A

Q

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I

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K

P

P

L

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M

L

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K

Q

A

G

G

A

K

T

A

L

L

S

C

Y

F

S

S

H

H

G

G

F

F

N

N

I

I

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C

E

F

E

K

G

R

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I

Q

V

I

P

R

P

P

E

D

D

I

V

T

D

V

V

V

I

M

M

V

V

A

A

P

P

K

K

C

A

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P

G
|
G

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E

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V

E

R

R

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K

E

A

Y

Y

K

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E

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G

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F

G

G

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V

P

P

T

G

L

L

I

V

A

A

V

V

H

-

P

-

E

K

N

Q

D

N

P

P

N

S

G

G

D

E

G

A

L

R

E

E

I

V

A

A

K

L

A

A

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M

A

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A

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D

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A

A

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F

I

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A

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E

E

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D
|
D

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L

M

F

G

G

E
|
E

Q

Q

T

C

I

V

L

L

C

C

G

G

M

G

L

L

Q

V

T

E

G

L

A

M

I

R

L

N

G

G

Y

F

D

E

K

V

M

L

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V

A

E

D

A

G

G

V

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E

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P

P

G

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Y

M

A

A

A

Y

K

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L

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I

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Q

H

G

E

W

M

E

K

T

L

V

I

T

V

E

D

A

L

L

V

K

W

H

Q

G

G

I

I

T

K

N

R

M

M

M

A

D

E

R

V

L

I

S

S

N

N

P

T

A

A

K

E

I

Y

K

G

A

M

F

W

E

A

I

V

A

G

E

H

D

-

L

-

K

-

E

Q

I

I

L

I

Q

G

P

P

L

E

F

V

E

K

K

E

H

K

M

M

D

K

D

E

I

A

I

L

-

K

-

R

-

V

-

E

S

N

G

G

E

E

F

F

S

A

R

N

T

E

M

W

M

V

Q

D

D

E

W

Y

YGAQ 24:27 (≠ CGAQ 45:48) binding
E46 (≠ L67) binding
N55 (≠ R76) binding
S57 (= S78) binding
DEVQ 87:90 (≠ DK-Q 108:110) binding
G138 (= G158) binding
D195 (= D217) binding
E199 (= E221) binding

4ypoA Crystal structure of mycobacterium tuberculosis ketol-acid reductoisomerase in complex with mg2+ (see paper)
32% identity, 63% coverage: 33:340/492 of query aligns to 10:312/325 of 4ypoA

query
sites
4ypoA

N

S

Y

I

I

I

K

Q

D

G

W

R

N

K

I

V

V

G

I

V

L

I

G

G

C

Y

G

G

A

S

Q

Q

G

G

L

H

N

A

Q

H

G

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L

L

N

S

M

L

R

R

D

D

S

S

G

G

L

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N

Q

I

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A

R

Y

V

A

G

L

L

R

K

P

-

E

-

A

-

I

-

A

-

Q

Q

K

G

R

S

A

R

S

S

W

R

Q

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K

K

A

V

T

E

D

E

N

Q

G

G

F

L

K

D

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V

G

D

T

T

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P

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A

E

E

L

V

I

A

P

K

T

W

A

A

D

D

L

V

V

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L

M

N

V

L

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A

P

P

D

D

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A

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A

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V

I

V

F

S

A

A

G

-

D

V

I

M

E

P

P

L

N

M

L

K

K

Q

P

G

G

A

D

T

A

L

L

S

F

Y

F

S

G

H

H

G

G

F

L

N

N

I

V

V

H

E

F

E

G

G

L

M

I

Q

K

I

P

R

P

P

A

D

D

I

V

T

A

V

V

V

A

M

M

V

V

A

A

P

P

K
|
K

C

G

P

P

G

G

T

H

E

L

V

V

R

R

E

R

E

Q

Y

F

K

V

R

D

G

G

F

K

G

G

V

V

P

P

T

C

L

L

I

V

A

A

V

V

H

-

P

-

E

E

N

Q

D

D

P

P

N

R

G

G

D

D

G

G

L

L

E

A

I

L

A

A

K

L

A

S

Y

Y

A

A

S

K

A

A

T

I

G

G

D

T

R

R

A

A

G

G

V

V

L

I

Q

K

S

T

F

F

I

K

A

D

E

E

V

T

K

E

S

T

D
|
D

L

L

M

F

G

G

E
|
E

Q

Q

T

T

I

V

L

L

C

C

G

G

M

G

L

T

Q

E

T

E

G

L

A

V

I

K

L

A

G

G

Y

F

D

E

K

V

M

M

V

-

A

-

D

-

G

-

V

V

E

E

P

A

G

G

Y

Y

A

P

A

A

K

E

L

L

-

A

-

Y

-

F

-
x
E

I

V

Q

L

Q

H

G
x
E

W

L

E

K

T

L

V

I

T

V

E

D

A

L

L

M

K

Y

H

E

G

G

I

L

T

A

N

R

M

M

M

Y

D

Y

R

S

L

V

S

S

N

D

P

T

A

A

K

E

I

F

K

G

A

G

F

Y

E

L

I

S

A

G

E

-

D

-

L

-

K

P

E

R

I

V

L

I

Q

D

P

A

L

G

F

T

E

K

K

E

H

R

M

M

D

R

D

D

I

I

I

L

-

R

-

E

-

I

-

Q

S

D

G

G

E

S

F

F

S

V

R

H

T

K

M

L

M

V

Q

A

D

D

W

V

A

E

N

G

D

G

D

N

A

K

N

Q

L

L

L

E

R

E

W

L

R

R

A

R

E

Q

T

N

A

A

E

E

T

H

G

P

F

I

E

E

active site: K128 (= K155), D188 (= D217), E192 (= E221)
binding magnesium ion: D188 (= D217), E192 (= E221), E224 (vs. gap), E228 (≠ G257)

P9WKJ7 Ketol-acid reductoisomerase (NADP(+)); KARI; Acetohydroxy-acid isomeroreductase; AHIR; Alpha-keto-beta-hydroxylacyl reductoisomerase; Ketol-acid reductoisomerase type 1; Ketol-acid reductoisomerase type I; EC 1.1.1.86 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
32% identity, 63% coverage: 33:340/492 of query aligns to 14:316/337 of P9WKJ7

query
sites
P9WKJ7

N

S

Y

I

I

I

K

Q

D

G

W

R

N

K

I

V

V

G

I

V

L

I

G

G

C

Y

G

G

A

S

Q

Q

G

G

L

H

N

A

Q

H

G

S

L

L

N

S

M

L

R

R

D

D

S

S

G

G

L

V

N

Q

I

V

A

R

Y

V

A

G

L

L

R

K

P

-

E

-

A

-

I

-

A

-

Q

Q

K

G

R

S

A

R

S

S

W

R

Q

P

K

K

A

V

T

E

D

E

N

Q

G

G

F

L

K

D

V

V

G

D

T

T

F

P

E

A

E

E

L

V

I

A

P

K

T

W

A

A

D

D

L

V

V

V

L

M

N

V

L

L

T

A

P

P

D

D

K

T

Q

A

H

Q

S

A

N

E

V

I

V

F

S

A

A

G

-

D

V

I

M

E

P

P

L

N

M

L

K

K

Q

P

G

G

A

D

T

A

L

L

S

F

Y

F

S

G

H

H

G

G

F

L

N

N

I

V

V

H

E

F

E

G

G

L

M

I

Q

K

I

P

R

P

P

A

D

D

I

V

T

A

V

V

V

A

M

M

V

V

A

A

P

P

K

K

C

G

P

P

G

G

T

H

E

L

V

V

R

R

E

R

E

Q

Y

F

K

V

R

D

G

G

F

K

G

G

V

V

P

P

T

C

L

L

I

V

A

A

V

V

H

-

P

-

E

E

N

Q

D

D

P

P

N

R

G

G

D

D

G

G

L

L

E

A

I

L

A

A

K

L

A

S

Y

Y

A

A

S

K

A

A

T

I

G

G

D

T

R

R

A

A

G

G

V

V

L

I

Q

K

S

T

F

F

I

K

A

D

E

E

V

T

K

E

S

T

D
|
D

L

L

M

F

G

G

E
|
E

Q

Q

T

T

I

V

L

L

C

C

G

G

M

G

L

T

Q

E

T

E

G

L

A

V

I

K

L

A

G

G

Y

F

D

E

K

V

M

M

V

-

A

-

D

-

G

-

V

V

E

E

P

A

G

G

Y

Y

A

P

A

A

K

E

L

L

-

A

-

Y

-

F

-
x
E

I

V

Q

L

Q

H

G
x
E

W

L

E

K

T

L

V

I

T

V

E

D

A

L

L

M

K

Y

H

E

G

G

I

L

T

A

N

R

M

M

M

Y

D

Y

R

S

L

V

S

S

N

D

P

T

A

A

K

E

I

F

K

G

A

G

F

Y

E

L

I

S

A

G

E

-

D

-

L

-

K

P

E

R

I

V

L

I

Q

D

P

A

L

G

F

T

E

K

K

E

H

R

M

M

D

R

D

D

I

I

I

L

-

R

-

E

-

I

-

Q

S

D

G

G

E

S

F

F

S

V

R

H

T

K

M

L

M

V

Q

A

D

D

W

V

A

E

N

G

D

G

D

N

A

K

N

Q

L

L

L

E

R

E

W

L

R

R

A

R

E

Q

T

N

A

A

E

E

T

H

G

P

F

I

E

E

D192 (= D217) binding ; binding
E196 (= E221) binding
E228 (vs. gap) binding
E232 (≠ G257) binding

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

8cy8A Apo form cryo-em structure of campylobacter jejune ketol-acid reductoisommerase crosslinked by glutaraldehyde
30% identity, 61% coverage: 33:333/492 of query aligns to 12:288/312 of 8cy8A

query
sites
8cy8A

N

N

Y

L

I

I

K

K

D

S

W

K

N

K

I

V

V

A

I

I

L

I

G

G

C

F

G

G

A

S

Q

Q

G

G

L

H

N

A

Q

H

G

A

L

M

N

N

M

L

R

R

D

D

S

N

G

G

L

V

N

N

I

V

A

T

Y

I

A

G

L

L

R

R

P

-

E

-

A

-

I

-

A

-

Q

-

K

-

R

-

A

-

S

-

W

-

Q

-

K

-

A

-

T

-

D

N

N

A

G

G

F

F

K

E

V

V

G

M

T

S

F

V

E

S

E

E

L

A

I

S

P

K

T

I

A

A

D

D

L

V

V

I

L

M

N

I

L

L

T

A

P

P

D

D

K

E

Q

I

H

Q

S

A

N

D

V

I

V

F

S

N

A

V

-

E

V

I

M

K

P

P

L

N

M

L

K

S

Q

E

G

G

A

K

T

A

L

I

S

A

Y

F

S

A

H

H

G

G

F

F

N

N

I

I

V

H

E

Y

E

G

G

Q

M

I

Q

V

I

V

R

P

P

K

D

G

I

V

T

D

V

V

V

I

M

M

V

I

A

A

P

P

K

K

C

A

P

P

G

G

T

H

E

T

V

V

R

R

E

N

E

E

Y

-

K

-

R

-

G

-

F

-

G

-

V

T

P

P

T

C

L

L

I

I

A

A

V

I

H

H

P

Q

E

D

N

E

D

S

P

K

N

N

G

A

D

K

G

N

L

L

E

-

I

-

A

A

K

L

A

S

Y

Y

A

A

S

S

A

A

T

I

G

G

D

G

R

R

A

T

G

G

V

I

L

I

Q

E

S

T

F

F

I

K

A

A

E

E

V

T

K

E

S

T

D
|
D

L

L

M

F

G

G

E
|
E

Q

Q

T

A

I

V

L
|
L

C

C

G

G

M

G

L

L

Q

S

T

A

G

L

A

I

I

Q

L

A

G

G

Y

F

D

E

K

T

M

L

V

V

A

E

D

A

G

G

V

Y

E

E

P

P

G

E

Y

M

A

A

A

Y

K

F

L

E

I

C

Q

L

Q

H

G

E

W

M

E

K

T

L

V

I

T

V

E

D

A

L

L

I

K

Y

H

Q

G

G

I

I

T

A

N

D

M

M

M

R

D

Y

R

S

L

I

S

S

N

N

P

T

A

A

K

E

I

Y

K

G

A

D

F

Y

-

I

-

T

-

G

-

P

-

K

E

I

I

I

A

T

E

E

D

E

L

T

K

K

E

K

I

A

L

M

Q

K

P

G

L

V

F

-

E

-

K

-

H

-

M

L

D

K

D

D

I

I

I

Q

S

N

G

G

E

V

F

F

S

A

R

K

T

D

M

F

M

I

Q

L

D

E

W

R

A

-

N

-

D

-

D

R

A

A

N

G

L

F

L

A

R

R

W

M

R

H

A

A

E

E

binding pentanedial: D174 (= D217), E178 (= E221), L182 (= L225)

8ep7C Crystal structure of the ketol-acid reductoisomerase from bacillus anthracis in complex with NADP
34% identity, 56% coverage: 39:314/492 of query aligns to 18:287/328 of 8ep7C

query
sites
8ep7C

N

T

I

V

V

A

I

V

L

I

G

G

C
x
Y

G
|
G

A
x
S

Q
|
Q

G

G

L

H

N

A

Q

Q

G

A

L

Q

N

N

M

L

R

R

D

D

S

S

G

G

L

V

N

E

I

V

A

V

Y

V

A

G

L

V

R
|
R

P

P

E

-

A

-

I

-

A

-

Q

-

K

-

R

G

A

K

S
|
S

W

F

Q

E

K

V

A

A

T

K

D

A

N

D

G

G

F

F

K

E

V

V

G

M

T

S

F

V

E

S

E

E

L

A

I

V

P

R

T

T

A

A

D

Q

L

V

V

V

L

Q

N

M

L
|
L

T
x
L

P
|
P

D
|
D

K

E

Q
|
Q

H

Q

S

A

N

H

V
|
V

V

Y

S

K

A

A

-

E

V

V

M

E

P

E

L

N

M

L

K

R

Q

E

G

G

A

Q

T

M

L

L

S

L

Y

F

S

S

H
|
H

G

G

F

F

N

N

I

I

V

-

E

-

E

H

G

F

M

G

Q

Q

I

I

R

N

P

P

D

P

-

S

-

Y

I

V

T

D

V

V

V

A

M

M

V

V

A

A

P

P

K

K

C

S

P

P

G

G

T

H

E

L

V

V

R

R

E

R

E

V

Y

F

K

Q

R

E

G

G

F

N

G

G

V

V

P

P

T

A

L

L

I

V

A

A

V

V

H

H

P

-

E

-

N

Q

D

D

P

A

N

T

G

G

D

T

G

A

L

L

E

H

I

V

A

A

K

L

A

A

Y

Y

A

A

S

K

A

G

T

V

G

G

G

C

D

T

R

R

A

A

G

G

V

V

L

I

Q

E

S

T

F

F

I

Q

A

E

E

E

V

T

K

E

S

T

D

D

L

L

M

F

G

G

E

E

Q

Q

T

A

I

V

L

L

C

C

G

G

M

G

L

V

Q

T

T

A

G

L

A

V

I

K

L

A

G

G

Y

F

D

E

K

T

M

L

V

T

A

E

D

G

G

G

V

Y

E

R

P

P

G

E

Y

I

A

A

A

Y

K

F

L

E

I

C

Q

L

Q

H

G

E

W

L

E

K

T

L

V

I

T

V

E

D

A

L

L

M

K

Y

H

E

G

G

I

L

T

T

N

N

M

M

M

R

D

H

R

S

L

I

S

S

N

D

P

T

A

A

-

E

-

F

-

G

-

D

-

Y

-

V

-

T

-

G

-

S

K

R

I

I

K

V

A

T

F

D

E

E

I

T

A

K

E

K

D

E

L

M

K

K

E

R

I

V

L

L

Q

-

P

-

L

-

F

-

E

-

K

-

H

-

M

-

D

T

D

E

I

I

I

Q

S

Q

G

G

E

E

F

F

S

A

R

K

binding nadp nicotinamide-adenine-dinucleotide phosphate: Y24 (≠ C45), G25 (= G46), S26 (≠ A47), Q27 (= Q48), R47 (= R68), S51 (= S78), L78 (= L105), L79 (≠ T106), P80 (= P107), D81 (= D108), Q83 (= Q110), V87 (= V114), H106 (= H132)

5yeqB The structure of sac-kari protein (see paper)
31% identity, 59% coverage: 32:322/492 of query aligns to 11:296/329 of 5yeqB

query
sites
5yeqB

C

L

N

D

Y

V

I

I

K

K

D

E

W

K

N

R

I

V

V

A

I

V

L

L

G

G

C

Y

G

G

A

S

Q

Q

G

G

L

R

N

A

Q

W

G

A

L

L

N

N

M

L

R

R

D

D

S

S

G

G

L

I

N

K

I

V

A

S

Y

V

A

G

L

L

R

E

P

R

E

E

A

G

I

-

A

-

Q

-

K

-

R

-

A

N

S

S

W

W

Q

K

K

Q

A

A

T

E

D

N

N

D

G

G

F

F

K

K

V

P

G

L

T

R

F

T

E

E

L

A

I

V

P

R

T

N

A

S

D

D

L

I

V

I

L

I

N

F

L

L

T

L

P

P

D

D

K

M

-

I

Q

Q

H

R

S

T

N

V

V

Y

V

L

S

E

A

R

V

V

M

K

P

P

L

Y

M

L

K

K

Q

E

G

G

A

M

T

D

L

L

S

V

Y

F

S

A

H

H

G

G

F

F

N

N

I

I

V

H

E

Y

E

R

G

L

M

I

Q

E

I

P

R

P

P

S

D

N

I

V

T

D

V

V

V

Y

M

M

V

I

A

A

P

P

K

K

C

A

P

P

G

G

T

P

E

I

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V

R

R

E

E

E

Y

Y

F

K

A

R

K

G

G

F

G

G

G

V

V

P

P

T

A

L

L

I

V

A

A

V

T

H

Y

P

-

E

-

N

Q

D

D

P

H

N

S

G

G

D

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G

A

L

L

E

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I

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A

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L

A

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A

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I

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D

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G

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T

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L

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V

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P

G

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A

A

A

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F

L
x
E

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T

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I

Q

N

G
x
E

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M

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T

L

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I

T

V

E

D

A

L

L

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Y

H

E

G

K

G

G

I

F

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N

G

M

M

M

L

D

T

R

A

L

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S

N

D

P

T

A

A

K

K

I

Y

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G

A

G

F

M

E

T

I

V

A

G

E

K

-

M

D

V

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K

D

E

E

I

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L

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Q

K

P

E

L

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F

M

E

K

K

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A

M

L

D

D

D

N

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I

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binding magnesium ion: E226 (≠ L253), E230 (≠ G257)

6l2iB Ilvc, a ketol-acid reductoisomerase, from streptococcus pneumoniae_wt
30% identity, 60% coverage: 39:335/492 of query aligns to 18:308/323 of 6l2iB

query
sites
6l2iB

N

K

I

I

V

A

I

V

L

I

G

G

C
x
Y

G
|
G

A
x
S

Q
|
Q

G

G

L

H

N

A

Q

H

G

A

L

Q

N

N

M

L

R

R

D

D

S

S

G

G

L

R

N

D

I

V

A

I

Y

I

A

G

L
x
V

R
|
R

P

P

E

-

A

-

I

-

A

-

Q

-

K

-

R

G

A

K

S
|
S

W

F

Q

D

K

K

A

A

T

K

D

E

N

D

G

G

F

F

K

D

V

T

G

Y

T

T

F

V

E

A

E

E

L

A

I

T

P

K

T

L

A

A

D

D

L

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I

L

M

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L

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T

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P
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P

D
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D

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E

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x
I

H

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Q

N

E

V
x
L

V

Y

S

E

A

A

-

E

V

I

M

A

P

P

L

N

M

L

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E

Q

A

G

G

A

N

T

A

L

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Y

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H
|
H

G

G

F

F

N

N

I

I

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H

E

F

E

E

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F

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I

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I

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D

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D

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F

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M

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A

A

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C

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|
P

G

G

T

H

E

L

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V

R

R

E

R

E

T

Y

Y

K

E

R

E

G

G

F

F

G

G

V

V

P

P

T

A

L

L

I

Y

A

A

V

V

H

Y

P

-

E

-

N

Q

D

D

P

A

N

T

G

G

D

N

G

A

L

K

E

N

I

I

A

A

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M

A

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Y

W

A

C

S

K

A

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G

G

G

A

D

A

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R

A

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G

V

L

L

L

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E

E

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D

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L

M

F

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E
|
E

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A

I

V

L

L

C

C

G

G

M

G

L

L

Q

T

T

A

G

L

A

I

I

E

L

A

G

G

Y

F

D

E

K

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M

L

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A

E

D

A

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P

G

E

Y

L

A

A

A

Y

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F

L

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L

Q

H

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E

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T

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D

A

L

L

I

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H

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K

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K

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R

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L

I

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S

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N

P

T

A

A

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E

I

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K

G

A

D

F

Y

-

V

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-

G

-

P

-

R

E

V

I

I

A

T

E

E

D

Q

L

V

K

K

E

E

I

N

L

M

Q

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P

A

L

V

F

-

E

-

K

-

H

-

M

L

D

A

D

D

I

I

I

Q

S

N

G

G

E

K

F

F

S

A

R

N

T

D

M

F

M

V

Q

N

D

D

W

Y

A

K

N

A

D

G

D

R

A

P

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L

L

L

T

R

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W

Y

R

R

A

E

E

Q

T

A

A

A

binding magnesium ion: D189 (= D217), D189 (= D217), E193 (= E221), E193 (= E221)
binding nadp nicotinamide-adenine-dinucleotide phosphate: Y24 (≠ C45), G25 (= G46), S26 (≠ A47), Q27 (= Q48), V46 (≠ L67), R47 (= R68), S51 (= S78), P80 (= P107), D81 (= D108), I83 (≠ Q110), L87 (≠ V114), H106 (= H132), P131 (= P157)

Query Sequence

>7023117 Shewana3_0355 ketol-acid reductoisomerase (RefSeq)
MANYFNSLNLRQQLAQLGQCRFMDRSEFSDGCNYIKDWNIVILGCGAQGLNQGLNMRDSG
LNIAYALRPEAIAQKRASWQKATDNGFKVGTFEELIPTADLVLNLTPDKQHSNVVSAVMP
LMKQGATLSYSHGFNIVEEGMQIRPDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPE
NDPNGDGLEIAKAYASATGGDRAGVLQSSFIAEVKSDLMGEQTILCGMLQTGAILGYDKM
VADGVEPGYAAKLIQQGWETVTEALKHGGITNMMDRLSNPAKIKAFEIAEDLKEILQPLF
EKHMDDIISGEFSRTMMQDWANDDANLLRWRAETAETGFENAPVSSEHIDEQTYFDKGIF
LVAMIKAGVELAFDTMVSAGIVEESAYYESLHETPLIANTIARKRLYEMNVVISDTAEYG
CYLFNHAAVPMLRDYVNAMSPEYLGAGLKDSSNNVDNLQLIAINDAIRHTSVEYIGAELR
GYMTDMKSIVGA

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