SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing CA265_RS15825 FitnessBrowser__Pedo557:CA265_RS15825 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)
72% identity, 100% coverage: 1:493/493 of query aligns to 1:490/491 of P05793

query
sites
P05793

M
|
M

A

A

N

N

Y

Y

F

F

N

N

T

T

L

L

P

N

L

L

R

R

E

Q

K

Q

L

L

N

A

Q

Q

L

L

G

G

V

K

C

C

D

R

F

F

M

M

D

G

S

R

S

D

E

E

F

F

L

A

D

D

G

G

V

A

N

S

A

Y

L

L

K

Q

G

G

K

K

L

V

V

V

I

I

V

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

L

M

R

R

D

D

S

S

G

G

L

L

D

D

V

I

S

S

Y

Y

T

A

L

L

R
|
R

K
|
K

E

E

A
|
A

I

I

E

A

G

E

K
|
K

R
|
R

D

A

S
|
S

W

W

K

R

N

K

A

A

T

T

E

E

N

N

N

G

F

F

T

K

V

V

G

G

T

T

Y

Y

E

E

L

L

I

I

P

P

N

Q

A

A

D

D

V

L

V

V

I

I

N

N

L

L

T

T

P

P

D
|
D

K
|
K

Q
|
Q

H

H

T

S

A

D

V

V

N

R

A

T

I

V

M

Q

P

P

L

L

M

M

K

K

E

D

G

G

A

A

T

A

L

L

L

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

K

K

D

D

L

I

T

T

V

V

I

V

M

M

V

V

A

A

P

P

K
|
K

C

C

P

P

G

G

S

T

E

E

V

V

R

R

A

E

E

E

Y

Y

V

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

Q

K

G

G

K

E

G

G

L

M

A

A

Q

I

A

A

K

K

A

A

Y

W

C

A

A

A

G

A

T

T

G

G

H

H

R

R

A

A

G

G

V

V

L

L

K

E

S

S

F

F

V

V

A

A

E
|
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

L

M

L

L

Q

Q

T

A

G

G

S

S

I

L

L

L

S

C

F

F

D

D

K

K

M

L

V

V

E

E

K

E

G

G

I

T

D

D

A

P

G

A

Y

Y

A

A

S

E

K

K

L

L

V

I

Q

Q

Y

F

G

G

V

W

E

E

V

T

I

I

T

T

E

E

A

A

L

L

K

K

Q

Q

G

G

I

I

T

T

A

L

M

M

D

D

R

R

L

L

S

S

N

N

V

P

A

A

K

K

I

L

K

R

A

A

F

Y

E

A

I

L

S

S

E

E

E

Q

L

L

K

K

D

E

I

I

M

M

R

A

P

P

L

L

F

F

Q

Q

K

K

H

H

Q

M

D

D

I

I

M

I

S

S

G

G

E

E

F

F

S

S

R

S

T

G

M

M

E

A

D

D

W

W

A

A

N

N

G

D

D

D

K

K

N

K

L

L

K

T

W

W

R

R

A

E

E

E

T

T

G

G

E

K

T

T

A

A

F

F

E

E

K

T

T

A

P

P

A

Q

G

Y

D

E

V

G

K

K

I

I

G

G

E

E

Q

Q

E

E

Y

Y

F

F

D

D

N

K

Y

G

T

V

L

L

M

M

V

I

A

A

F

M

V

V

R

K

A

A

G

G

V

V

E

E

L

L

A

A

F

F

E

E

T

T

M

M

V

V

Q

D

A

S

G

G

I

I

K

I

P

E

E

E

S

S

A

A

Y

Y

E
|
E

S

S

L

L

H

H

E
|
E

T

L

P

P

L

L

I

I

A

A

N

N

T

T

I

I

A

A

R

R

K

K

K

R

L

L

F

Y

E

E

M

M

N

N

R

V

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

D

S

Q

Y

A

A

C

C

K

V

P

P

L

L

G

K

D

P

F

F

M

M

K

A

K

E

V

L

D

Q

T

P

D

G

L

D

V

L

G

G

K

K

N

A

F

I

N

P

E

E

G

-

K

-

D

-

G

G

A

A

V

V

D

D

N

N

R

G

K

Q

L

L

I

R

D

D

I

V

N

N

E

E

A

A

I

I

R

R

S

S

H

H

E

A

V

I

E

E

Q

Q

I

V

G

G

A

K

T

K

L

L

R

R

K

G

A

Y

M

M

T

T

A

D

M

M

K

K

A

R

I

I

K

A

T

V

A

A

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 (= K69) 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)
72% identity, 99% coverage: 1:490/493 of query aligns to 1:487/489 of 3ulkA

query
sites
3ulkA

M

M

A

A

N

N

Y

Y

F

F

N

N

T

T

L

L

P

N

L

L

R

R

E

Q

K

Q

L

L

N

A

Q

Q

L

L

G

G

V

K

C

C

D

R

F

F

M

M

D

G

S

R

S

D

E

E

F

F

L

A

D

D

G

G

V

A

N

S

A

Y

L

L

K

Q

G

G

K

K

L

V

V

V

I

I

V

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

L

M

R

R

D

D

S

S

G

G

L

L

D

D

V

I

S

S

Y

Y

T

A

L

L

R
|
R

K

K

E

E

A

A

I

I

E

A

G

E

K

K

R
|
R

D

A

S
|
S

W

W

K

R

N

K

A

A

T

T

E

E

N

N

N

G

F

F

T

K

V

V

G

G

T

T

Y

Y

E

E

L

L

I

I

P

P

N

Q

A

A

D

D

V

L

V

V

I

I

N

N

L
|
L

T
|
T

P
|
P

D
|
D

K

K

Q
|
Q

H

H

T

S

A

D

V
|
V

V

V

N

R

A

T

I

V

M

Q

P

P

L

L

M

M

K

K

E

D

G

G

A

A

T

A

L

L

L

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

K

K

D

D

L

I

T

T

V

V

I

V

M

M

V

V

A

A

P

P

K
|
K

C

C

P

P

G

G

S

T

E

E

V

V

R

R

A

E

E

E

Y

Y

V

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

Q

K

G

G

K

E

G

G

L

M

A

A

Q

I

A

A

K

K

A

A

Y

W

C

A

A

A

G

A

T

T

G

G

H

H

R

R

A

A

G

G

V

V

L

L

K

E

S

S

F

F

V

V

A

A

E

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

L

M

L

L

Q

Q

T

A

G

G

S

S

I

L

L

L

S

C

F

F

D

D

K

K

M

L

V

V

E

E

K

E

G

G

I

T

D

D

A

P

G

A

Y

Y

A

A

S

E

K

K

L

L

V

I

Q

Q

Y

F

G

G

V

W

E

E

V

T

I

I

T

T

E

E

A

A

L

L

K

K

Q

Q

G

G

I

I

T

T

A

L

M

M

D

D

R

R

L

L

S

S

N

N

V

P

A

A

K

K

I

L

K

R

A

A

F

Y

E

A

I

L

S

S

E

E

E

Q

L

L

K

K

D

E

I

I

M

M

R

A

P

P

L

L

F

F

Q

Q

K

K

H

H

Q

M

D

D

I

I

M

I

S

S

G

G

E

E

F

F

S

S

R

S

T

G

M

M

E

A

D

D

W

W

A

A

N

N

G

D

D

D

K

K

N

K

L

L

K

T

W

W

R

R

A

E

E

E

T

T

G

G

E

K

T

T

A

A

F

F

E

E

K

T

T

A

P

P

A

Q

G

Y

D

E

V

G

K

K

I

I

G

G

E

E

Q

Q

E

E

Y

Y

F

F

D

D

N

K

Y

G

T

V

L

L

M

M

V

I

A

A

F

M

V

V

R

K

A

A

G

G

V

V

E

E

L

L

A

A

F

F

E

E

T

T

M

M

V

V

Q

D

A

S

G

G

I

I

K

I

P

E

E

E

S

S

A

A

Y

Y

E
|
E

S

S

L

L

H

H

E
|
E

T

L

P

P

L

L

I

I

A

A

N

N

T

T

I

I

A

A

R

R

K

K

K

R

L

L

F

Y

E

E

M

M

N

N

R

V

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

D

S

Q

Y

A

A

C

C

K

V

P

P

L

L

G

K

D

P

F

F

M

M

K

A

K

E

V

L

D

Q

T

P

D

G

L

D

V

L

G

G

K

K

N

A

F

I

N

P

E

E

G

-

K

-

D

-

G

G

A

A

V

V

D

D

N

N

R

G

K

Q

L

L

I

R

D

D

I

V

N

N

E

E

A

A

I

I

R

R

S

S

H

H

E

A

V

I

E

E

Q

Q

I

V

G

G

A

K

T

K

L

L

R

R

K

G

A

Y

M

M

T

T

A

D

M

M

K

K

A

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, 81% coverage: 32:429/493 of query aligns to 11:409/466 of 5e4rA

query
sites
5e4rA

V

L

N

E

A

P

L

I

K

K

G

N

K

K

K

T

L

I

V

A

I

I

V

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

L

L

R

R

D

D

S

S

G

G

L

L

D

N

V

V

S

V

Y

V

T

G

L

L

R

E

K

R

E

Q

A

G

I

-

E

-

G

-

K

-

R

-

D

D

S
|
S

W

W

K

R

N

R

A

A

T

I

E

D

N

D

N

G

F

F

T

K

V

P

G

M

T

Y

Y

T

E

K

E

D

L

A

I

V

P

A

N

I

A

A

D

D

V

I

I

V

N

F

L
|
L

T
x
V

P
|
P

D
|
D

K

M

-
x
V

Q

Q

H

K

T

S

A

L

V

W

V

L

N

N

A

S

I

V

M

K

P

D

L

F

M

M

K

K

E

K

G

G

A

A

T

D

L

L

L

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

K

K

D

D

L

S

T

D

V

V

I

Y

M

M

V

I

A

A

P

P

K
|
K

C

S

P
|
P

G

G

S

P

E

I

V

V

R

R

A

R

E

S

Y

Y

V

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

Q

S

G

G

K

E

G

A

L

L

A

Q

Q

K

A

A

K

L

A

A

Y

I

C

A

A

K

G

G

T

I

G

G

G

C

H

A

R

R

A

A

G

G

V

V

L

I

K

E

S

S

S

T

F

F

V

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

L

G

L

I

Q

M

T

E

G

L

S

I

I

K

L

A

S

S

F

F

D

E

K

T

M

L

V

V

E

E

K

E

G

G

I

Y

D

Q

A

P

G

E

Y

V

A

A

S

Y

K

F

L

E

V

T

Q

V

Y

N

G

E

V

L

E

K

V

L

I

I

T

V

E

D

A

L

L

I

K

Y

Q

E

G

K

G

G

I

L

T

T

A

G

M

M

M

L

D

R

R

A

L

V

S

S

N

D

V

T

A

A

K

K

-

Y

-

G

-

I

-

T

I

V

K

G

A

K

F

F

E

I

I

I

S

D

E

K

E

S

L

V

K

R

D

D

I

K

M

M

R

K

P

I

L

V

F

L

Q

E

K

R

H

-

Q

-

D

-

I

I

M

R

S

S

G

G

E

E

F

F

S

A

R

R

T

E

M

W

M

I

E

K

D

E

W

Y

A

E

N

R

G

G

D

M

K

P

N

T

L

V

L

F

K

K

W

E

R

L

A

S

E

E

T

L

G

E

E

G

T

S

A

T

F

I

E

E

K

T

T

V

P

G

A

R

G

-

D

-

V

-

K

K

I

L

G

R

E

E

Q

M

E

M

Y

F

-

R

-

G

-

M

-

L

F

F

D

G

N

E

Y

Q

T

V

L

I

M

L

V

V

A

G

F

G

V

I

R

M

A

E

G

L

V

I

E

K

L

A

A

S

F

F

E

E

T

T

M

L

V

V

Q

E

A

E

G

G

I

Y

K

Q

P

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

K

G

L

L

F

T

E

G

M

M

N

L

R

R

V
x
A

I
x
V

S
|
S

D

D

T

T

A
|
A

E

K

Y

Y

G

G

C

G

-

I

-

T

-

V

-

G

-

K

Y

F

L

I

F

I

D

D

Q

K

A

S

C

V

K

R

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)

4xdzA Holo structure of ketol-acid reductoisomerase from ignisphaera aggregans (see paper)
34% identity, 60% coverage: 32:329/493 of query aligns to 11:303/328 of 4xdzA

query
sites
4xdzA

V

L

N

E

A

P

L

I

K

K

G

N

K

K

K

T

L

I

V

A

I

I

V

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

L

L

R

R

D

D

S

S

G

G

L

L

D

N

V

V

S

V

Y

V

T

G

L

L

R
x
E

K
x
R

E

Q

A

G

I

-

E

-

G

-

K

-

R

-

D

D

S
|
S

W

W

K

R

N

R

A

A

T

I

E

D

N

D

N

G

F

F

T

K

V

P

G

M

T

Y

Y

T

E

K

E

D

L

A

I

V

P

A

N

I

A

A

D

D

V

I

I

V

N

F

L
|
L

T
x
V

P
|
P

D
|
D

K

M

-
x
V

Q

Q

H

K

T

S

A

L

V

W

V

L

N

N

A

S

I

V

M

K

P

D

L

F

M

M

K

K

E

K

G

G

A

A

T

D

L

L

L

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

K

K

D

D

L

S

T

D

V

V

I

Y

M

M

V

I

A

A

P

P

K
|
K

C

S

P
|
P

G

G

S

P

E

I

V

V

R

R

A

R

E

S

Y

Y

V

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

Q

S

G

G

K

E

G

A

L

L

A

Q

Q

K

A

A

K

L

A

A

Y

I

C

A

A

K

G

G

T

I

G

G

G

C

H

A

R

R

A

A

G

G

V

V

L

I

K

E

S

S

S

T

F

F

V

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

L

G

L

I

Q

M

T

E

G

L

S

I

I

K

L

A

S

S

F

F

D

E

K

T

M

L

V

V

E

E

K

E

G

G

I

Y

D

Q

A

P

G

E

Y

V

A

A

S

Y

K

F

L

E

V

T

Q

V

Y

N

G
x
E

V

L

E

K

V

L

I

I

T

V

E

D

A

L

L

I

K

Y

Q

E

G

K

G

G

I

L

T

T

A

G

M

M

M

L

D

R

R

A

L
x
V

S
|
S

N

D

V

T

A
|
A

K

K

-

Y

-

G

-

I

-

T

I

V

K

G

A

K

F

F

E

I

I

I

S

D

E

K

E

S

L

V

K

R

D

D

I

K

M

M

R

K

P

I

L

V

F

L

Q

E

K

R

H

-

Q

-

D

-

I

I

M

R

S

S

G

G

E

E

F

F

S

A

R

R

T

E

M

W

M

I

E

K

D

E

W

Y

A

E

N

R

G

G

D

M

K

P

N

T

L

V

L

F

K

K

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 (≠ K69), S52 (= S78), L79 (= L105), V80 (≠ T106), P81 (= P107), D82 (= D108), V84 (vs. gap), A106 (≠ S131), H107 (= H132), P132 (= P157)

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)
34% identity, 60% coverage: 32:329/493 of query aligns to 12:304/335 of E0SRA9

query
sites
E0SRA9

V

L

N

E

A

P

L

I

K

K

G

N

K

K

K

T

L

I

V

A

I

I

V

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

L

L

R

R

D

D

S

S

G

G

L

L

D

N

V

V

S

V

Y

V

T

G

L

L

R

E

K
x
R

E

Q

A

G

I

-

E

-

G

-

K

-

R

-

D

D

S
|
S

W

W

K

R

N

R

A

A

T

I

E

D

N

D

N

G

F

F

T

K

V

P

G

M

T

Y

Y

T

E

K

E

D

L

A

I

V

P

A

N

I

A

A

D

D

V

I

I

V

N

F

L

L

T

V

P

P

D
|
D

K
x
M

-
x
V

Q
|
Q

H

K

T

S

A

L

V

W

V

L

N

N

A

S

I

V

M

K

P

D

L

F

M

M

K

K

E

K

G

G

A

A

T

D

L

L

L

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

K

K

D

D

L

S

T

D

V

V

I

Y

M

M

V

I

A

A

P

P

K

K

C

S

P

P

G
|
G

S

P

E

I

V

V

R

R

A

R

E

S

Y

Y

V

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

Q

S

G

G

K

E

G

A

L

L

A

Q

Q

K

A

A

K

L

A

A

Y

I

C

A

A

K

G

G

T

I

G

G

G

C

H

A

R

R

A

A

G

G

V

V

L

I

K

E

S

S

S

T

F

F

V

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

L

G

L

I

Q

M

T

E

G

L

S

I

I

K

L

A

S

S

F

F

D

E

K

T

M

L

V

V

E

E

K

E

G

G

I

Y

D

Q

A

P

G

E

Y

V

A

A

S

Y

K

F

L

E

V

T

Q

V

Y

N

G

E

V

L

E

K

V

L

I

I

T

V

E

D

A

L

L

I

K

Y

Q

E

G

K

G

G

I

L

T

T

A

G

M

M

M

L

D

R

R

A

L

V

S

S

N

D

V

T

A

A

K

K

-

Y

-

G

-

I

-

T

I

V

K

G

A

K

F

F

E

I

I

I

S

D

E

K

E

S

L

V

K

R

D

D

I

K

M

M

R

K

P

I

L

V

F

L

Q

E

K

R

H

-

Q

-

D

-

I

I

M

R

S

S

G

G

E

E

F

F

S

A

R

R

T

E

M

W

M

I

E

K

D

E

W

Y

A

E

N

R

G

G

D

M

K

P

N

T

L

V

L

F

K

K

YGSQ 25:28 (≠ CGAQ 45:48) binding
R49 (≠ K69) binding
S53 (= S78) binding
DMVQ 83:86 (≠ DK-Q 108:110) binding
G134 (= G158) binding
D191 (= D217) binding
E195 (= E221) binding

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)
35% identity, 63% coverage: 32:340/493 of query aligns to 13:316/337 of P9WKJ7

query
sites
P9WKJ7

V

L

N

S

A

I

L

I

K

Q

G

G

K

R

K

K

L

V

V

G

I

V

V

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

L

L

R

R

D

D

S

S

G

G

L

V

D

Q

V

V

S

R

Y

V

T

G

L

L

R

K

K

-

E

-

A

-

I

-

E

Q

G

G

K

S

R

R

D

-

S

S

W

R

K

P

N

K

A

V

T

E

E

E

N

Q

N

G

F

L

T

D

V

V

G

D

T

T

Y

P

E

A

E

E

L

V

I

A

P

K

N

W

A

A

D

D

V

V

I

M

N

V

L

L

T

A

P

P

D

D

K

T

Q

A

H

Q

T

A

A

E

V

I

V

F

N

A

A

G

-

D

I

I

M

E

P

P

L

N

M

L

K

K

E

P

G

G

A

D

T

A

L

L

L

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

K

A

D

D

L

V

T

A

V

V

I

A

M

M

V

V

A

A

P

P

K

K

C

G

P

P

G

G

S

H

E

L

V

V

R

R

A

R

E

Q

Y

F

V

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

Q

R

G

G

K

D

G

G

L

L

A

A

Q

L

A

A

K

L

A

S

Y

Y

C

A

A

K

G

A

T

I

G

G

H

T

R

R

A

A

G

G

V

V

L

I

K

K

S

T

F

F

V

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

L

G

L

T

Q

E

T

E

G

L

S

V

I

K

L

A

S

G

F

F

D

E

K

V

M

M

V

V

E

E

K

A

G

G

I

Y

D

P

A

A

G

E

Y

L

A

A

S

Y

K

F

L
x
E

V

V

Q

L

Y

H

G
x
E

V

L

E

K

V

L

I

I

T

V

E

D

A

L

L

M

K

Y

Q

E

G

G

I

L

T

A

A

R

M

M

M

Y

D

Y

R

S

L

V

S

S

N

D

V

T

A

A

K

E

I

F

K

G

A

G

F

Y

-

L

-

S

-

G

-

P

-

R

E

V

I

I

S

D

E

A

E

G

L

T

K

K

D

E

I

R

M

M

R

R

P

D

L

I

F

L

Q

R

K

E

H

I

Q

Q

D

D

D

-

I

-

M

-

S

-

G

G

E

S

F

F

S

V

R

H

T

K

M

L

M

V

E

A

D

D

W

V

A

E

N

G

G

G

D

N

K

K

N

Q

L

L

L

E

K

E

W

L

R

R

A

R

E

Q

T

N

G

A

E

E

T

H

A

P

F

I

E

E

D192 (= D217) binding ; binding
E196 (= E221) binding
E228 (≠ L253) binding
E232 (≠ G257) binding

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

4ypoA Crystal structure of mycobacterium tuberculosis ketol-acid reductoisomerase in complex with mg2+ (see paper)
35% identity, 63% coverage: 32:340/493 of query aligns to 9:312/325 of 4ypoA

query
sites
4ypoA

V

L

N

S

A

I

L

I

K

Q

G

G

K

R

K

K

L

V

V

G

I

V

V

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

L

L

R

R

D

D

S

S

G

G

L

V

D

Q

V

V

S

R

Y

V

T

G

L

L

R

K

K

-

E

-

A

-

I

-

E

Q

G

G

K

S

R

R

D

-

S

S

W

R

K

P

N

K

A

V

T

E

E

E

N

Q

N

G

F

L

T

D

V

V

G

D

T

T

Y

P

E

A

E

E

L

V

I

A

P

K

N

W

A

A

D

D

V

V

I

M

N

V

L

L

T

A

P

P

D

D

K

T

Q

A

H

Q

T

A

A

E

V

I

V

F

N

A

A

G

-

D

I

I

M

E

P

P

L

N

M

L

K

K

E

P

G

G

A

D

T

A

L

L

L

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

K

A

D

D

L

V

T

A

V

V

I

A

M

M

V

V

A

A

P

P

K
|
K

C

G

P

P

G

G

S

H

E

L

V

V

R

R

A

R

E

Q

Y

F

V

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

Q

R

G

G

K

D

G

G

L

L

A

A

Q

L

A

A

K

L

A

S

Y

Y

C

A

A

K

G

A

T

I

G

G

H

T

R

R

A

A

G

G

V

V

L

I

K

K

S

T

F

F

V

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

L

G

L

T

Q

E

T

E

G

L

S

V

I

K

L

A

S

G

F

F

D

E

K

V

M

M

V

V

E

E

K

A

G

G

I

Y

D

P

A

A

G

E

Y

L

A

A

S

Y

K

F

L
x
E

V

V

Q

L

Y

H

G
x
E

V

L

E

K

V

L

I

I

T

V

E

D

A

L

L

M

K

Y

Q

E

G

G

I

L

T

A

A

R

M

M

M

Y

D

Y

R

S

L

V

S

S

N

D

V

T

A

A

K

E

I

F

K

G

A

G

F

Y

-

L

-

S

-

G

-

P

-

R

E

V

I

I

S

D

E

A

E

G

L

T

K

K

D

E

I

R

M

M

R

R

P

D

L

I

F

L

Q

R

K

E

H

I

Q

Q

D

D

D

-

I

-

M

-

S

-

G

G

E

S

F

F

S

V

R

H

T

K

M

L

M

V

E

A

D

D

W

V

A

E

N

G

G

G

D

N

K

K

N

Q

L

L

L

E

K

E

W

L

R

R

A

R

E

Q

T

N

G

A

E

E

T

H

A

P

F

I

E

E

active site: K128 (= K155), D188 (= D217), E192 (= E221)
binding magnesium ion: D188 (= D217), E192 (= E221), E224 (≠ L253), E228 (≠ 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)
35% identity, 60% coverage: 35:331/493 of query aligns to 14:305/338 of C1DFH7

query
sites
C1DFH7

L

I

K

Q

G

S

K

K

L

V

V

A

I

I

V

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

L

L

R

K

D

D

S

S

G

G

L

V

D

D

V

V

S

Y

Y

V

T

G

L

L

R

R

K

A

E

G

A

S

I

A

E

-

G

-

K

-

R

-

D

-

S

S

W

V

K

A

N

K

A

A

T

E

E

A

N

H

N

G

F

L

T

T

V

V

G

K

T

S

Y

V

E

K

E

D

L

A

I

V

P

A

N

A

A

A

D

D

V

V

I

M

N

I

L

L

T

T

P

P

D

D

K

E

-

F

Q

Q

H

G

T

R

A

L

V

Y

V

K

N

D

A

E

I

I

M

E

P

P

L

N

M

L

K

K

E

K

G

G

A

A

T

T

L

L

L

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

K

A

D

D

L

L

T

D

V

V

I

I

M

M

V

I

A

A

P

P

K

K

C

A

P

P

G

G

S

H

E

T

V

V

R

R

A

S

E

E

Y

F

V

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

Q

E

D

N

A

D

S

P

G

Q

N

G

A

K

K

G

N

L

L

A

A

Q

L

A

-

K

-

A

S

Y

Y

C

A

A

C

G

G

T

V

G

G

H

G

R

R

A

T

G

G

V

I

L

I

K

E

S

T

F

F

V

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

-

G

-

C

-

V

-

E

L

L

L

V

Q

K

T

A

G

G

S

-

I

-

L

-

S

-

F

F

D

E

K

T

M

L

V

V

E

E

K

-

G

-

I

-

D

-

A

A

G

G

Y

Y

A

A

S

P

K

E

L

M

V

A

Q

Y

Y

F

-
x
E

-

C

-

L

-

H

G
x
E

V

L

E

K

V

L

I

I

T

V

E

D

A

L

L

M

K

F

Q

E

G

G

I

I

T

A

A

N

M

M

M

N

D

Y

R

S

L

I

S

S

N

N

V

N

A

A

K

E

I

Y

K

G

A

E

F

Y

-

V

-

T

-

G

-

P

-

E

E

V

I

I

S

N

E

E

E

Q

L

S

K

R

D

Q

I

A

M

M

R

R

P

N

L

A

F

L

Q

K

K

R

H

I

Q

Q

D

D

D

-

I

-

M

-

S

-

G

G

E

E

F

Y

S

A

R

K

T

M

M

F

M

I

E

T

D

E

W

G

A

A

N

A

G

N

D

Y

K

P

N

S

L

M

L

T

K

A

W

Y

R

R

D190 (= D217) binding
E226 (vs. gap) binding
E230 (≠ G257) binding

4xiyA Crystal structure of ketol-acid reductoisomerase from azotobacter (see paper)
35% identity, 60% coverage: 35:331/493 of query aligns to 14:305/328 of 4xiyA

query
sites
4xiyA

L

I

K

Q

G

S

K

K

L

V

V

A

I

I

V

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

L

L

R

K

D

D

S

S

G

G

L

V

D

D

V

V

S

Y

Y

V

T

G

L

L

R

R

K

A

E

G

A

S

I

A

E

-

G

-

K

-

R

-

D

-

S

S

W

V

K

A

N

K

A

A

T

E

E

A

N

H

N

G

F

L

T

T

V

V

G

K

T

S

Y

V

E

K

E

D

L

A

I

V

P

A

N

A

A

A

D

D

V

V

I

M

N

I

L

L

T

T

P

P

D

D

K

E

-

F

Q

Q

H

G

T

R

A

L

V

Y

V

K

N

D

A

E

I

I

M

E

P

P

L

N

M

L

K

K

E

K

G

G

A

A

T

T

L

L

L

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

K

A

D

D

L

L

T

D

V

V

I

I

M

M

V

I

A

A

P

P

K
|
K

C

A

P

P

G

G

S

H

E

T

V

V

R

R

A

S

E

E

Y

F

V

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

Q

E

D

N

A

D

S

P

G

Q

N

G

A

K

K

G

N

L

L

A

A

Q

L

A

-

K

-

A

S

Y

Y

C

A

A

C

G

G

T

V

G

G

H

G

R

R

A

T

G

G

V

I

L

I

K

E

S

T

F

F

V

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

-

G

-

C

-

V

-

E

L

L

L

V

Q

K

T

A

G

G

S

-

I

-

L

-

S

-

F

F

D

E

K

T

M

L

V

V

E

E

K

-

G

-

I

-

D

-

A

A

G

G

Y

Y

A

A

S

P

K

E

L

M

V

A

Q

Y

Y

F

-
x
E

-

C

-

L

-

H

G
x
E

V

L

E

K

V

L

I

I

T

V

E

D

A

L

L

M

K

F

Q

E

G

G

I

I

T

A

A

N

M

M

M

N

D

Y

R

S

L

I

S

S

N

N

V

N

A

A

K

E

I

Y

K

G

A

E

F

Y

-

V

-

T

-

G

-

P

-

E

E

V

I

I

S

N

E

E

E

Q

L

S

K

R

D

Q

I

A

M

M

R

R

P

N

L

A

F

L

Q

K

K

R

H

I

Q

Q

D

D

D

-

I

-

M

-

S

-

G

G

E

E

F

Y

S

A

R

K

T

M

M

F

M

I

E

T

D

E

W

G

A

A

N

A

G

N

D

Y

K

P

N

S

L

M

L

T

K

A

W

Y

R

R

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

7rduA Crystal structure of campylobacter jejuni keto said reductoisomerase in complex with magnesium and oxidixized and reduced NADPH
33% identity, 63% coverage: 32:342/493 of query aligns to 12:317/329 of 7rduA

query
sites
7rduA

V

L

N

N

A

L

L

I

K

K

G

S

K

K

L

V

V

A

I

I

V

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

L

L

R

R

D

D

S

N

G

G

L

V

D

N

V

V

S

T

Y

I

T

G

L

L

R
|
R

K

E

E

G

A
x
S

I

V

E
x
S

G

A

K

V

R

K

D

-

S

-

W

A

K

K

N

N

A

A

T

-

E

-

N

-

N

G

F

F

T

E

V

V

G

M

T

S

Y

V

E

S

E

E

L

A

I

S

P

K

N

I

A

A

D

D

V

V

V

I

I

M

N

I

L
|
L

T
x
A

P
|
P

D
|
D

K

E

Q

I

H

Q

T

A

A

D

V
x
I

V

F

N

N

A

V

-

E

I

I

M

K

P

P

L

N

M

L

K

S

E

E

G

G

A

K

T

A

L

I

L

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

K

K

D

G

L

V

T

D

V

V

I

I

M

M

V

I

A

A

P
|
P

K
|
K

C
x
A

P

P

G

G

S

H

E

T

V

V

R

R

A

N

E

E

Y

F

V

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

Q

N

G

A

K

K

G

N

L

L

A

A

Q

L

A

-

K

-

A

S

Y

Y

C

A

A

S

G

A

T

I

G

G

H

G

R

R

A

T

G

G

V

I

L

I

K

E

S

T

F

F

V

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

L

G

L

L

Q

S

T

A

G

L

S

I

I

Q

L

A

S

G

F

F

D

E

K

T

M

L

V

V

E

E

K

A

G

G

I

Y

D

E

A

P

G

E

Y

M

A

A

S

Y

K

F

L

E

V

C

Q

L

Y

H

G

E

V

M

E

K

V

L

I

I

T

V

E

D

A

L

L

I

K

Y

Q

Q

G

G

I

I

T

A

A

D

M

M

M

R

D

Y

R

S

L

I

S

S

N

N

V

T

A

A

K

E

I

Y

K

G

A

D

F

Y

-

I

-

T

-

G

-

P

-

K

E

I

I

I

S

T

E

E

L

T

K

K

D

K

I

A

M

M

R

K

P

G

L

V

F

L

Q

K

K

-

H

-

Q

-

D

-

D

D

I

I

M

Q

S

N

G

G

E

V

F

F

S

A

R

K

T

D

M

F

M

I

E

L

D

E

W

R

A

R

N

A

G

G

D

F

K

A

N

R

L

M

L

H

K

A

W

E

R

R

A

K

E

N

T

M

G

N

E

D

T

S

A

L

F

I

E

E

K

K

T

T

binding nadp nicotinamide-adenine-dinucleotide phosphate: G24 (= G44), G26 (= G46), S27 (≠ A47), Q28 (= Q48), R48 (= R68), S51 (≠ A71), S53 (≠ E73), 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 (≠ E73), L80 (= L105), P82 (= P107), D83 (= D108), I89 (≠ V114), A107 (≠ S131), H108 (= H132)

7latA Campylobacter jejuni keto-acid reductoisomerase in complex with mg2+
33% identity, 63% coverage: 32:342/493 of query aligns to 12:317/329 of 7latA

query
sites
7latA

V

L

N

N

A

L

L

I

K

K

G

S

K

K

L

V

V

A

I

I

V

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

L

L

R

R

D

D

S

N

G

G

L

V

D

N

V

V

S

T

Y

I

T

G

L

L

R

R

K

E

E

G

A

S

I

V

E

S

G

A

K

V

R

K

D

-

S

-

W

A

K

K

N

N

A

A

T

-

E

-

N

-

N

G

F

F

T

E

V

V

G

M

T

S

Y

V

E

S

E

E

L

A

I

S

P

K

N

I

A

A

D

D

V

V

V

I

I

M

N

I

L

L

T

A

P

P

D

D

K

E

Q

I

H

Q

T

A

A

D

V

I

V

F

N

N

A

V

-

E

I

I

M

K

P

P

L

N

M

L

K

S

E

E

G

G

A

K

T

A

L

I

L

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

K

K

D

G

L

V

T

D

V

V

I

I

M

M

V

I

A

A

P

P

K

K

C

A

P

P

G

G

S

H

E

T

V

V

R

R

A

N

E

E

Y

F

V

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

Q

N

G

A

K

K

G

N

L

L

A

A

Q

L

A

-

K

-

A

S

Y

Y

C

A

A

S

G

A

T

I

G

G

H

G

R

R

A

T

G

G

V

I

L

I

K

E

S

T

F

F

V

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

L

G

L

L

Q

S

T

A

G

L

S

I

I

Q

L

A

S

G

F

F

D

E

K

T

M

L

V

V

E

E

K

A

G

G

I

Y

D

E

A

P

G

E

Y

M

A

A

S

Y

K

F

L

E

V

C

Q

L

Y

H

G

E

V

M

E

K

V

L

I

I

T

V

E

D

A

L

L

I

K

Y

Q

Q

G

G

I

I

T

A

A

D

M

M

M

R

D

Y

R

S

L

I

S

S

N

N

V

T

A

A

K

E

I

Y

K

G

A

D

F

Y

-

I

-

T

-

G

-

P

-

K

E

I

I

I

S

T

E

E

L

T

K

K

D

K

I

A

M

M

R

K

P

G

L

V

F

L

Q

K

K

-

H

-

Q

-

D

-

D

D

I

I

M

Q

S

N

G

G

E

V

F

F

S

A

R

K

T

D

M

F

M

I

E

L

D

E

W

R

A

R

N

A

G

G

D

F

K

A

N

R

L

M

L

H

K

A

W

E

R

R

A

K

E

N

T

M

G

N

E

D

T

S

A

L

F

I

E

E

K

K

T

T

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

4kqxB Mutant slackia exigua kari ddv in complex with NAD and an inhibitor (see paper)
34% identity, 63% coverage: 35:344/493 of query aligns to 16:320/335 of 4kqxB

query
sites
4kqxB

L

I

K

Q

G

G

K

L

K

K

L

V

V

G

I

I

V

I

G

G

C
x
Y

G
|
G

A
x
S

Q
|
Q

G
|
G

L

H

N

A

Q

H

G

A

L

L

N

N

L

L

R

M

D

D

S

S

G

G

L

V

D

D

V

V

S

R

Y

V

T

G

L

L

R
|
R

K

-

E

-

A

-

I

-

E

E

G

G

K

D

R

S

D

D

S

-

W

W

K

K

N

T

A

A

T

E

E

E

N

A

N

G

F

L

T

K

V

V

G

T

T

D

Y

M

E

D

E

T

L

A

I
x
A

P
x
E

N

E

A
|
A

D

D

V

V

V

I

I

M

N

V

L
|
L

T
x
V

P
|
P

D
|
D

K

E

Q

V

H

Q

T

P

A

K

V
|
V

V

Y

N

Q

A

E

-

H

I

I

M

A

P

A

L

H

M

L

K

K

E

A

G

G

A
x
N

T

T

L

L

L

A

Y

F

S

A

H
|
H

G

G

F

F

N

N

I

I

V

H

E

Y

E

G

G

Y

M

I

Q

V

I

P

R

P

K

E

D

D

L

V

T

N

V

V

I

I

M

M

V

C

A

A

P

P

K
|
K

C

G

P
|
P

G

G

S

H

E

I

V

V

R

R

A

R

E

Q

Y

F

V

T

R

E

G

G

F

S

G

G

V

V

P

P

T

D

L

L

I

A

A

C

V

V

H

-

P

-

E

Q

N

Q

D

D

P

A

Q

T

G

G

K

N

G

A

L

W

A

D

Q

I

A

V

K

L

A

S

Y

Y

C

C

A

W

G

G

T

V

G

G

H

A

R

R

A

S

G

G

V

I

L

I

K

K

S

A

S

T

F

F

V

A

A

E

E

E

V

T

K

E

S

E

D
|
D

L

L

M

F

G

G

E
|
E

Q

Q

T

A

I

V

L

L

C

C

G

G

L

G

L

L

Q

V

T

E

G

L

S

V

I

K

L

A

S

G

F

F

D

E

K

T

M

L

V

T

E

E

K

A

G

G

I

Y

D

P

A

P

G

E

Y

L

A

A

S

Y

K

F

L

E

V

C

Q

Y

Y

H

G
x
E

V

M

E

K

V

M

I

I

T

V

E

D

A

L

L

M

K

Y

Q

E

G

S

G

G

I

I

T

H

A

F

M

M

M
x
N

D

Y

R
x
S

L
x
I

S
|
S

N
|
N

V

T

A
|
A

K
x
E

I

Y

K

G

A

E

F

Y

E

Y

-

A

-

G

-

P

-

K

-

V

I

I

S

N

E

E

E

Q

L

S

K

R

D

E

I

A

M

M

R

K

P

E

L

I

F

L

Q

K

K

R

H

I

Q

Q

D

D

D

-

I

-

M

-

S

-

G

G

E

S

F

F

S

A

R

Q

T

E

M

F

M

V

E

D

D

D

W

C

A

N

N

N

G

G

D

H

K

K

N

R

L

L

K

E

W

Q

R

R

A

E

E

A

T

I

G

N

E

T

T

H

A

P

F

I

E

E

K

T

T

T

P

G

A

A

active site: K132 (= K155), D192 (= D217), E196 (= E221)
binding n-hydroxy-n-isopropyloxamic acid: P134 (= P157), D192 (= D217), E196 (= E221), E232 (≠ G257), I252 (≠ L277), S253 (= S278), A256 (= A281)
binding magnesium ion: G27 (= G46), Q29 (= Q48), G30 (= G49), A72 (≠ I96), E73 (≠ P97), A75 (= A99), L81 (= L105), N103 (≠ A126), D192 (= D217), E196 (= E221), N249 (≠ M274), S251 (≠ R276), I252 (≠ L277), I252 (≠ L277), S253 (= S278), N254 (= N279), E257 (≠ K282)
binding nicotinamide-adenine-dinucleotide: Y26 (≠ C45), G27 (= G46), S28 (≠ A47), Q29 (= Q48), R49 (= R68), L81 (= L105), V82 (≠ T106), P83 (= P107), D84 (= D108), V90 (= V114), H109 (= H132), P134 (= P157), S251 (≠ R276), I252 (≠ L277), S253 (= S278)

Sites not aligning to the query:

binding histidine: 333, 334, 335

D0WGK0 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 Slackia exigua (strain ATCC 700122 / DSM 15923 / CIP 105133 / JCM 11022 / KCTC 5966 / S-7) (see paper)
34% identity, 63% coverage: 35:344/493 of query aligns to 25:329/342 of D0WGK0

query
sites
D0WGK0

L

I

K

Q

G

G

K

L

K

K

L

V

V

G

I

I

V

I

G

G

C
x
Y

G
|
G

A
x
S

Q
|
Q

G

G

L

H

N

A

Q

H

G

A

L

L

N

N

L

L

R

M

D

D

S

S

G

G

L

V

D

D

V

V

S

R

Y

V

T

G

L

L

R
|
R

K

-

E

-

A

-

I

-

E

E

G

G

K
x
S

R

-

D

S

S
|
S

W

W

K

K

N

T

A

A

T

E

E

E

N

A

N

G

F

L

T

K

V

V

G

T

T

D

Y

M

E

D

E

T

L

A

I

A

P

E

N

E

A

A

D

D

V

V

V

I

I

M

N

V

L

L

T

V

P

P

D
|
D

K
x
E

Q
x
I

H
x
Q

T

P

A

K

V

V

V

Y

N

Q

A

E

-

H

I

I

M

A

P

A

L

H

M

L

K

K

E

A

G

G

A

N

T

T

L

L

L

A

Y

F

S

A

H

H

G

G

F

F

N

N

I

I

V

H

E

Y

E

G

G

Y

M

I

Q

V

I

P

R

P

K

E

D

D

L

V

T

N

V

V

I

I

M

M

V

C

A

A

P

P

K

K

C

G

P

P

G
|
G

S

H

E

I

V

V

R

R

A

R

E

Q

Y

F

V

T

R

E

G

G

F

S

G

G

V

V

P

P

T

D

L

L

I

A

A

C

V

V

H

-

P

-

E

Q

N

Q

D

D

P

A

Q

T

G

G

K

N

G

A

L

W

A

D

Q

I

A

V

K

L

A

S

Y

Y

C

C

A

W

G

G

T

V

G

G

H

A

R

R

A

S

G

G

V

I

L

I

K

K

S

A

S

T

F

F

V

A

A

E

E

E

V

T

K

E

S

E

D
|
D

L

L

M

F

G

G

E
|
E

Q

Q

T

A

I

V

L

L

C

C

G

G

L

G

L

L

Q

V

T

E

G

L

S

V

I

K

L

A

S

G

F

F

D

E

K

T

M

L

V

T

E

E

K

A

G

G

I

Y

D

P

A

P

G

E

Y

L

A

A

S

Y

K

F

L

E

V

C

Q

Y

Y

H

G

E

V

M

E

K

V

M

I

I

T

V

E

D

A

L

L

M

K

Y

Q

E

G

S

G

G

I

I

T

H

A

F

M

M

M

N

D

Y

R

S

L

I

S
|
S

N

N

V

T

A

A

K

E

I

Y

K

G

A

E

F

Y

E

Y

-

A

-

G

-

P

-

K

-

V

I

I

S

N

E

E

E

Q

L

S

K

R

D

E

I

A

M

M

R

K

P

E

L

I

F

L

Q

K

K

R

H

I

Q

Q

D

D

D

-

I

-

M

-

S

-

G

G

E

S

F

F

S

A

R

Q

T

E

M

F

M

V

E

D

D

D

W

C

A

N

N

N

G

G

D

H

K

K

N

R

L

L

K

E

W

Q

R

R

A

E

E

A

T

I

G

N

E

T

T

H

A

P

F

I

E

E

K

T

T

T

P

G

A

A

YGSQ 35:38 (≠ CGAQ 45:48) binding
R58 (= R68) binding
S61 (≠ K75) binding ; mutation to D: Inversion of cofactor specificity from NADPH to NADH. Strong decrease of the affinity for NADPH and 2.5-fold decrease of the affinity for NADH. 8-fold decrease of the catalytic efficiency for NADPH and 2-fold increase of the catalytic efficiency for NADH; when associated with D-63.
S63 (= S78) binding ; mutation to D: Inversion of cofactor specificity from NADPH to NADH. Strong decrease of the affinity for NADPH and 2.5-fold decrease of the affinity for NADH. 8-fold decrease of the catalytic efficiency for NADPH and 2-fold increase of the catalytic efficiency for NADH; when associated with D-61.
DEIQ 93:96 (≠ DKQH 108:111) binding
G144 (= G158) binding
D201 (= D217) binding
E205 (= E221) binding
S262 (= S278) binding

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)
37% identity, 59% coverage: 32:322/493 of query aligns to 12:297/344 of C8WR67

query
sites
C8WR67

V

I

N

Q

A

P

L

L

K

A

G

D

K

K

K

R

L

I

V

A

I

V

V

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

L

L

R

R

D

D

S

S

G

G

L

F

D

D

V

V

S

V

Y

I

T

G

L

L

R
|
R

K

P

E

G

A

S

I

-

E

-

G

-

K

-

R

-

D

-

S
|
S

W

W

K

A

N

K

A

A

T

E

E

A

N

D

N

G

F

F

T

R

V

V

G

M

T

A

Y

V

E

G

E

E

L

A

I

V

P

E

N

E

A

S

D

D

V

V

V

I

I

M

N

I

L

L

T

L

P

P

D
|
D

K
x
E

Q
x
R

H
x
Q

T

P

A

A

V

V

V

Y

-

E

N

R

A

E

I

I

M

R

P

P

L

Y

M

L

K

T

E

A

G

G

A

K

T

A

L

L

L

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

K

K

D

D

L

V

T

D

V

V

I

F

M

M

V

V

A

A

P

P

K

K

C

G

P

P

G
|
G

S

H

E

L

V

V

R

R

A

R

E

V

Y

Y

V

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

Q

E

D

N

A

D

S

P

G

Q

Q

G

A

K

K

G

D

L

L

A

A

Q

L

A

-

K

-

A

A

Y

Y

C

A

A

R

G

G

T

I

G

G

G

A

H

G

R

R

A

A

G

G

V

I

L

L

K

T

S

T

F

F

V

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

L

G

L

L

Q

S

T

A

G

L

S

I

I

K

L

A

S

G

F

F

D

E

K

T

M

L

V

V

E

E

K

A

G

G

I

Y

D

Q

A

P

G

E

Y

I

A

A

S

Y

K

F

L
x
E

V

C

Q

L

Y

H

G

E

V

M

E

K

V

L

I

I

T

V

E

D

A

L

L

I

K

Y

Q

E

G

G

I

L

T

E

A

Y

M

M

M

R

D

Y

R

S

L

I

S

S

N

D

V

T

A

A

K

Q

I

W

K

G

A

D

F

F

E

T

-

S

-

G

-

P

-

R

-

I

I

I

S

N

E

E

L

T

K

K

D

K

I

E

M

M

R

R

P

R

L

I

F

L

Q

A

K

-

H

-

Q

-

D

-

D

D

I

I

M

Q

S

S

G

G

E

A

F

F

S

A

R

K

T

S

-

W

M

I

M

L

E

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

4kqwA The structure of the slackia exigua kari in complex with NADP (see paper)
34% identity, 63% coverage: 35:344/493 of query aligns to 13:317/326 of 4kqwA

query
sites
4kqwA

L

I

K

Q

G

G

K

L

K

K

L

V

V

G

I

I

V

I

G

G

C
x
Y

G
|
G

A
x
S

Q
|
Q

G

G

L

H

N

A

Q

H

G

A

L

L

N

N

L

L

R

M

D

D

S

S

G

G

L

V

D

D

V

V

S

R

Y

V

T

G

L

L

R
|
R

K

-

E

-

A

-

I

-

E

E

G

G

K
x
S

R

-

D

S

S
|
S

W

W

K

K

N

T

A

A

T

E

E

E

N

A

N

G

F

L

T

K

V

V

G

T

T

D

Y

M

E

D

E

T

L

A

I

A

P

E

N

E

A

A

D

D

V

V

V

I

I

M

N

V

L
|
L

T
x
V

P
|
P

D
|
D

K

E

Q
x
I

H
x
Q

T

P

A

K

V

V

V

Y

N

Q

-

E

A

H

I

I

M

A

P

A

L

H

M

L

K

K

E

A

G

G

A

N

T

T

L

L

L

A

Y

F

S

A

H
|
H

G

G

F

F

N

N

I

I

V

H

E

Y

E

G

G

Y

M

I

Q

V

I

P

R

P

K

E

D

D

L

V

T

N

V

V

I

I

M

M

V

C

A

A

P

P

K
|
K

C

G

P
|
P

G

G

S

H

E

I

V

V

R

R

A

R

E

Q

Y

F

V

T

R

E

G

G

F

S

G

G

V

V

P

P

T

D

L

L

I

A

A

C

V

V

H

-

P

-

E

Q

N

Q

D

D

P

A

Q

T

G

G

K

N

G

A

L

W

A

D

Q

I

A

V

K

L

A

S

Y

Y

C

C

A

W

G

G

T

V

G

G

H

A

R

R

A

S

G

G

V

I

L

I

K

K

S

A

S

T

F

F

V

A

A

E

E

E

V

T

K

E

S

E

D
|
D

L

L

M

F

G

G

E
|
E

Q

Q

T

A

I

V

L

L

C

C

G

G

L

G

L

L

Q

V

T

E

G

L

S

V

I

K

L

A

S

G

F

F

D

E

K

T

M

L

V

T

E

E

K

A

G

G

I

Y

D

P

A

P

G

E

Y

L

A

A

S

Y

K

F

L

E

V

C

Q

Y

Y

H

G

E

V

M

E

K

V

M

I

I

T

V

E

D

A

L

L

M

K

Y

Q

E

G

S

G

G

I

I

T

H

A

F

M

M

M

N

D

Y

R

S

L
x
I

S
|
S

N

N

V

T

A

A

K

E

I

Y

K

G

A

E

F

Y

E

Y

-

A

-

G

-

P

-

K

-

V

I

I

S

N

E

E

E

Q

L

S

K

R

D

E

I

A

M

M

R

K

P

E

L

I

F

L

Q

K

K

R

H

I

Q

Q

D

D

D

-

I

-

M

-

S

-

G

G

E

S

F

F

S

A

R

Q

T

E

M

F

M

V

E

D

D

D

W

C

A

N

N

N

G

G

D

H

K

K

N

R

L

L

K

E

W

Q

R

R

A

E

E

A

T

I

G

N

E

T

T

H

A

P

F

I

E

E

K

T

T

T

P

G

A

A

active site: K129 (= K155), D189 (= D217), E193 (= E221)
binding magnesium ion: D189 (= D217), E193 (= E221)
binding nadp nicotinamide-adenine-dinucleotide phosphate: Y23 (≠ C45), G24 (= G46), S25 (≠ A47), Q26 (= Q48), R46 (= R68), S49 (≠ K75), S51 (= S78), L78 (= L105), V79 (≠ T106), P80 (= P107), D81 (= D108), I83 (≠ Q110), Q84 (≠ H111), H106 (= H132), P131 (= P157), I249 (≠ L277), S250 (= S278)

4tskA Ketol-acid reductoisomerase from alicyclobacillus acidocaldarius (see paper)
37% identity, 59% coverage: 32:322/493 of query aligns to 11:296/333 of 4tskA

query
sites
4tskA

V

I

N

Q

A

P

L

L

K

A

G

D

K

K

K

R

L

I

V

A

I

V

V

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

L

L

R

R

D

D

S

S

G

G

L

F

D

D

V

V

S

V

Y

I

T

G

L
|
L

R
|
R

K

P

E

G

A

S

I

-

E

-

G

-

K

-

R

-

D

-

S
|
S

W

W

K

A

N

K

A

A

T

E

E

A

N

D

N

G

F

F

T

R

V

V

G

M

T

A

Y

V

E

G

E

E

L

A

I

V

P

E

N

E

A

S

D

D

V

V

V

I

I

M

N

I

L
|
L

T
x
L

P
|
P

D
|
D

K

E

Q

R

H

Q

T

P

A

A

V

V

V

Y

-

E

N

R

A

E

I

I

M

R

P

P

L

Y

M

L

K

T

E

A

G

G

A

K

T

A

L

L

L

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

K

K

D

D

L

V

T

D

V

V

I

F

M

M

V

V

A

A

P

P

K
|
K

C

G

P
|
P

G

G

S

H

E

L

V

V

R

R

A

R

E

V

Y

Y

V

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

Q

E

D

N

A

D

S

P

G

Q

Q

G

A

K

K

G

D

L

L

A

A

Q

L

A

-

K

-

A

A

Y

Y

C

A

A

R

G

G

T

I

G

G

G

A

H

G

R

R

A

A

G

G

V

I

L

L

K

T

S

T

F

F

V

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

L

G

L

L

Q

S

T

A

G

L

S

I

I

K

L

A

S

G

F

F

D

E

K

T

M

L

V

V

E

E

K

A

G

G

I

Y

D

Q

A

P

G

E

Y

I

A

A

S

Y

K

F

L

E

V

C

Q

L

Y

H

G

E

V

M

E

K

V

L

I

I

T

V

E

D

A

L

L

I

K

Y

Q

E

G

G

I

L

T

E

A

Y

M

M

M
x
R

D
x
Y

R

S

L
x
I

S

S

N
x
D

V

T

A

A

K
x
Q

I

W

K

G

A

D

F

F

E

T

-

S

-

G

-

P

-

R

-

I

I

I

S

N

E

E

L

T

K

K

D

K

I

E

M

M

R

R

P

R

L

I

F

L

Q

A

K

-

H

-

Q

-

D

-

D

D

I

I

M

Q

S

S

G

G

E

A

F

F

S

A

R

K

T

S

-

W

M

I

M

L

E

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)

7q03A Ketol-acid reductoisomerase from methanothermococcus thermolithotrophicus in the close state with NADP and mg2+ (see paper)
35% identity, 61% coverage: 22:321/493 of query aligns to 4:291/328 of 7q03A

query
sites
7q03A

F

F

M

Y

D

D

S

S

S

D

E

T

F

T

L

F

D

D

G

-

V

-

N

-

A

A

L

V

K

K

G

D

K

K

K

T

L

I

V

A

I

V

V

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

L

M

R

K

D

D

S

S

G

G

L

L

D

K

V

V

S

V

Y

V

T

G

L

L

R
|
R

K

P

E

N

A

G

I

A

E

-

G

-

K

-

R

-

D

-

S
|
S

W

W

K

N

N

K

A

A

T

K

E

E

N

D

N

G

F

H

T

E

V

V

G

L

T

S

Y

I

E

E

L

A

I

A

P

E

N

K

A

A

D

D

V

I

I

H

N

I

L
|
L

T
x
I

P
|
P

D
|
D

K

E

Q
x
I

H

Q

T

G

A

D

V

V

V

Y

N

N

-

K

A

Q

I

I

M

K

P

P

L

Y

M

L

K

K

E

E

G

G

A

K

T

T

L

L

L

S

Y

F

S

S

H
|
H

G

G

F

Y

N

N

I

I

V

H

E

Y

E

G

G

Y

M

I

Q

V

I

P

R

P

K

E

D

G

L

V

T

N

V

V

I

V

M

M

V

V

A

A

P

P

K

K

C

S

P
|
P

G

G

S

A

E

M

V

V

R

R

A

R

E

T

Y

Y

V

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

Q

T

G

G

K

D

G

A

L

L

A

D

Q

I

A

A

K

L

A

G

Y

M

C

A

A

K

G

G

T

V

G

G

G

L

H

T

R

R

A

A

G

G

V

V

L

I

K

Q

S

T

F

F

V

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

L

G

L

V

Q

T

T

E

G

L

S

I

I

K

L

A

S

G

F

F

D

E

K

T

M

L

V

V

E

E

K

A

G

G

I

Y

D

S

A

P

G

E

Y

M

A

A

S

Y

K

F

L

E

V

T

Q

C

Y

H

G

E

V

L

E

K

V

L

I

I

T

I

E

D

A

L

L

I

K

Y

Q

Q

G

K

G

G

I

F

T

A

A

G

M

M

M

W

D

N

R

D

L

V

S

S

N

N

V

T

A

A

K

E

I

Y

-

G

-

L

-

T

-

R

K

R

A

S

F

R

E

V

I

I

S

N

E

E

E

Q

L

S

K

R

D

Q

I

E

M

M

R

R

P

K

L

I

F

L

Q

K

K

E

H

I

Q

Q

D

D

D

-

I

-

M

-

S

-

G

G

E

R

F

F

S

T

R

K

T

-

M

-

E

-

D

E

W

W

A

A

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)

6l2iA Ilvc, a ketol-acid reductoisomerase, from streptococcus pneumoniae_wt
34% identity, 63% coverage: 32:344/493 of query aligns to 11:317/324 of 6l2iA

query
sites
6l2iA

V

V

N

A

A

A

L

L

K

D

G

G

K

K

L

I

V

A

I

V

V

I

G

G

C

Y

G

G

A

S

Q

Q

G

G

L

H

N

A

Q

H

G

A

L

Q

N

N

L

L

R

R

D

D

S

S

G

G

L

R

D

D

V

V

S

I

Y

I

T

G

L

V

R

R

K

P

E

-

A

-

I

-

E

-

G

G

K

K

R

-

D

-

S

S

W

F

K

D

N

K

A

A

T

K

E

E

N

D

N

G

F

F

T

D

V

T

G

Y

T

T

Y

V

E

A

E

E

L

A

I

T

P

K

N

L

A

A

D

D

V

V

V

I

I

M

N

I

L

L

T

A

P

P

D

D

K

E

Q

I

H

Q

T

Q

A

E

V

L

V

Y

N

E

A

A

-

E

I

I

M

A

P

P

L

N

M

L

K

E

E

A

G

G

A

N

T

A

L

V

L

G

Y

F

S

A

H

H

G

G

F

F

N

N

I

I

V

H

E

F

E

E

G

F

M

I

Q

K

I

V

R

P

K

A

D

D

L

V

T

D

V

V

I

F

M

M

V

C

A

A

P

P

K

K

C

G

P

P

G

G

S

H

E

L

V

V

R

R

A

R

E

T

Y

Y

V

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

Q

T

G

G

K

N

G

A

L

K

A

N

Q

I

A

A

K

M

A

D

Y

W

C

C

A

K

G

G

T

V

G

G

G

A

H

A

R

R

A

V

G

G

V

L

L

L

K

E

S

T

F

Y

V

K

A

E

E

E

V

T

K

E

S

E

D

D

L

L

M

F

G

G

E

E

Q

Q

T

A

I

V

L

L

C

C

G

G

L

G

L

L

Q

T

T

A

G

L

S

I

I

E

L

A

S

G

F

F

D

E

K

V

M

L

V

T

E

E

K

-

G

-

I

-

D

-

A

A

G

G

Y

Y

A

A

S

P

K

E

L

L

V

A

Q

Y

Y

F

G

E

V

V

-

L

-

H

-

E

-

M

E

K

V

L

I

I

T

V

E

D

A

L

L

I

K

Y

Q

E

G

G

I

F

T

K

A

K

M

M

M

R

D

Q

R
x
S

L

I

S
|
S

N

N

V

T

A

A

K

E

I

Y

K

G

A

D

F

Y

-

V

-

S

-

G

-

P

-

R

E

V

I

I

S

T

E

E

E

Q

L

V

K

K

D

E

I

N

M

M

R

K

P

A

L

V

F

L

Q

A

K

-

H

-

Q

-

D

-

D

D

I

I

M

Q

S

N

G

G

E

K

F

F

S

A

R

N

T

D

M

F

M

V

E

N

D

D

W

Y

A

K

N

A

G

G

D

R

K

P

N

K

L

L

L

T

K

A

W

Y

R

R

A

E

E

Q

T

A

G

A

E

N

T

L

A

E

F

I

E

E

K

K

T

V

P

G

A

A

binding nadp nicotinamide-adenine-dinucleotide phosphate: S248 (≠ R276), S250 (= S278)

6l2iB Ilvc, a ketol-acid reductoisomerase, from streptococcus pneumoniae_wt
34% identity, 63% coverage: 32:344/493 of query aligns to 11:317/323 of 6l2iB

query
sites
6l2iB

V

V

N

A

A

A

L

L

K

D

G

G

K

K

L

I

V

A

I

V

V

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

L

L

R

R

D

D

S

S

G

G

L

R

D

D

V

V

S

I

Y

I

T

G

L
x
V

R
|
R

K

P

E

-

A

-

I

-

E

-

G

G

K

K

R

-

D

-

S
|
S

W

F

K

D

N

K

A

A

T

K

E

E

N

D

N

G

F

F

T

D

V

T

G

Y

T

T

Y

V

E

A

E

E

L

A

I

T

P

K

N

L

A

A

D

D

V

V

V

I

I

M

N

I

L

L

T

A

P
|
P

D
|
D

K

E

Q
x
I

H

Q

T

Q

A

E

V
x
L

V

Y

N

E

A

A

-

E

I

I

M

A

P

P

L

N

M

L

K

E

E

A

G

G

A

N

T

A

L

V

L

G

Y

F

S

A

H
|
H

G

G

F

F

N

N

I

I

V

H

E

F

E

E

G

F

M

I

Q

K

I

V

R

P

K

A

D

D

L

V

T

D

V

V

I

F

M

M

V

C

A

A

P

P

K

K

C

G

P
|
P

G

G

S

H

E

L

V

V

R

R

A

R

E

T

Y

Y

V

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

Q

T

G

G

K

N

G

A

L

K

A

N

Q

I

A

A

K

M

A

D

Y

W

C

C

A

K

G

G

T

V

G

G

G

A

H

A

R

R

A

V

G

G

V

L

L

L

K

E

S

T

F

Y

V

K

A

E

E

E

V

T

K

E

S

E

D
|
D

L

L

M

F

G

G

E
|
E

Q

Q

T

A

I

V

L

L

C

C

G

G

L

G

L

L

Q

T

T

A

G

L

S

I

I

E

L

A

S

G

F

F

D

E

K

V

M

L

V

T

E

E

K

-

G

-

I

-

D

-

A

A

G

G

Y

Y

A

A

S

P

K

E

L

L

V

A

Q

Y

Y

F

G

E

V

V

-

L

-

H

-

E

-

M

E

K

V

L

I

I

T

V

E

D

A

L

L

I

K

Y

Q

E

G

G

I

F

T

K

A

K

M

M

M

R

D

Q

R

S

L

I

S

S

N

N

V

T

A

A

K

E

I

Y

K

G

A

D

F

Y

-

V

-

S

-

G

-

P

-

R

E

V

I

I

S

T

E

E

E

Q

L

V

K

K

D

E

I

N

M

M

R

K

P

A

L

V

F

L

Q

A

K

-

H

-

Q

-

D

-

D

D

I

I

M

Q

S

N

G

G

E

K

F

F

S

A

R

N

T

D

M

F

M

V

E

N

D

D

W

Y

A

K

N

A

G

G

D

R

K

P

N

K

L

L

L

T

K

A

W

Y

R

R

A

E

E

Q

T

A

G

A

E

N

T

L

A

E

F

I

E

E

K

K

T

V

P

G

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)

5yeqB The structure of sac-kari protein (see paper)
32% identity, 63% coverage: 32:342/493 of query aligns to 11:316/329 of 5yeqB

query
sites
5yeqB

V

L

N

D

A

V

L

I

K

K

G

E

K

K

K

R

L

V

V

A

I

V

V

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

L

L

R

R

D

D

S

S

G

G

L

I

D

K

V

V

S

S

Y

V

T

G

L

L

R

E

K

R

E

E

A

G

I

-

E

-

G

-

K

-

R

-

D

N

S

S

W

W

K

K

N

Q

A

A

T

E

E

N

N

D

N

G

F

F

T

K

V

P

G

L

T

R

Y

T

E

E

L

A

I

V

P

R

N

N

A

S

D

D

V

I

I

I

N

F

L

L

T

L

P

P

D

D

K

M

-

I

Q

Q

H

R

T

T

A

V

V

Y

V

L

N

E

A

R

I

V

M

K

P

P

L

Y

M

L

K

K

E

E

G

G

A

M

T

D

L

L

L

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

K

S

D

N

L

V

T

D

V

V

I

Y

M

M

V

I

A

A

P

P

K

K

C

A

P

P

G

G

S

P

E

I

V

V

R

R

A

E

E

Y

Y

F

V

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

Q

S

G

G

K

K

G

A

L

L

A

Q

Q

K

A

A

K

L

A

A

Y

V

C

A

A

K

G

A

T

I

G

G

G

A

H

T

R

R

A

A

G

G

V

V

L

I

K

E

S

T

F

F

V

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

D

L

L

C

V

G

G

L

G

L

V

Q

M

T

Q

G

L

S

M

I

R

L

Y

S

A

F

F

D

Q

K

T

M

L

V

V

E

E

K

-

G

-

I

-

D

-

A

A

G

G

Y

Y

A

Q

S

P

K

E

L

V

V

A

Q

Y

Y

F

-
x
E

-

T

-

I

-

N

G
x
E

V

M

E

K

V

L

I

I

T

V

E

D

A

L

L

V

K

Y

Q

E

G

K

G

G

I

F

T

S

A

G

M

M

M

L

D

T

R

A

L

V

S

S

N

D

V

T

A

A

K

K

-

Y

-

G

-

M

-

T

I

V

K

G

A

K

F

M

E

V

I

I

S

D

E

E

E

S

L

V

K

K

D

E

I

R

M

M

R

K

P

-

L

-

F

-

Q

-

K

K

H

A

Q

L

D

D

D

N

I

I

M

R

S

S

G

G

E

K

F

F

S

A

R

E

T

K

M

W

M

V

E

E

D

E

W

Y

A

G

N

K

G

G

D

A

K

N

N

T

L

I

L

K

K

E

W

G

R

M

A

K

E

E

T

V

G

D

E

N

T

S

A

T

F

E

E

E

K

K

T

V

binding magnesium ion: E226 (vs. gap), E230 (≠ G257)

Query Sequence

>CA265_RS15825 FitnessBrowser__Pedo557:CA265_RS15825
MANYFNTLPLREKLNQLGVCDFMDSSEFLDGVNALKGKKLVIVGCGAQGLNQGLNLRDSG
LDVSYTLRKEAIEGKRDSWKNATENNFTVGTYEELIPNADVVINLTPDKQHTAVVNAIMP
LMKEGATLLYSHGFNIVEEGMQIRKDLTVIMVAPKCPGSEVRAEYVRGFGVPTLIAVHPE
NDPQGKGLAQAKAYCAGTGGHRAGVLKSSFVAEVKSDLMGEQTILCGLLQTGSILSFDKM
VEKGIDAGYASKLVQYGVEVITEALKQGGITAMMDRLSNVAKIKAFEISEELKDIMRPLF
QKHQDDIMSGEFSRTMMEDWANGDKNLLKWRAETGETAFEKTPAGDVKIGEQEYFDNYTL
MVAFVRAGVELAFETMVQAGIKPESAYYESLHETPLIANTIARKKLFEMNRVISDTAEYG
CYLFDQACKPLLGDFMKKVDTDLVGKNFNEGKDGAVDNRKLIDINEAIRSHEVEQIGATL
RKAMTAMKAIKTA

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