SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 3609007 FitnessBrowser__Dino:3609007 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)

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)
59% identity, 100% coverage: 1:340/340 of query aligns to 1:338/338 of C1DFH7

query
sites
C1DFH7

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D190 (= D191) binding
E226 (= E227) binding
E230 (= E231) binding

7rduA Crystal structure of campylobacter jejuni keto said reductoisomerase in complex with magnesium and oxidixized and reduced NADPH
61% identity, 97% coverage: 1:330/340 of query aligns to 2:329/329 of 7rduA

query
sites
7rduA

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binding nadp nicotinamide-adenine-dinucleotide phosphate: G24 (= G23), G26 (= G25), S27 (= S26), Q28 (= Q27), R48 (= R48), S51 (= S51), S53 (= S53), A81 (≠ M81), P82 (= P82), D83 (= D83), I89 (≠ T89), A107 (= A107), H108 (= H108), P130 (= P130), K131 (= K131), A132 (≠ G132)
binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G24 (= G23), F25 (≠ Y24), G26 (= G25), S27 (= S26), Q28 (= Q27), S51 (= S51), S53 (= S53), L80 (≠ T80), P82 (= P82), D83 (= D83), I89 (≠ T89), A107 (= A107), H108 (= H108)

7latA Campylobacter jejuni keto-acid reductoisomerase in complex with mg2+
61% identity, 97% coverage: 1:330/340 of query aligns to 2:329/329 of 7latA

query
sites
7latA

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

4xiyA Crystal structure of ketol-acid reductoisomerase from azotobacter (see paper)
59% identity, 97% coverage: 1:330/340 of query aligns to 1:328/328 of 4xiyA

query
sites
4xiyA

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T

S

K

R

A

Q

R

A

M

M

K

R

A

N

I

A

L

L

T

K

D

R

I

I

Q

Q

T

D

G

G

K

E

F

Y

V

A

R

K

D

M

F

F

M

I

Q

T

E

E

N

G

T

A

V

A

G

N

Q

Y

P

P

F

S

F

M

K

T

G

A

T

Y

R

R

L

N

N

N

D

A

E

A

H

H

Q

Q

I

I

E

E

A

V

V

V

G

G

K

E

E

K

L

L

R

R

G

T

M

M

P

P

W

W

I

I

S

A

active site: K130 (= K131), D190 (= D191), E194 (= E195)
binding fe (iii) ion: D190 (= D191), E194 (= E195)
binding magnesium ion: E226 (= E227), E230 (= E231)

8cy8A Apo form cryo-em structure of campylobacter jejune ketol-acid reductoisommerase crosslinked by glutaraldehyde
58% identity, 97% coverage: 1:330/340 of query aligns to 1:312/312 of 8cy8A

query
sites
8cy8A

M

I

R

T

V

V

Y

Y

D

D

R

K

D

D

C

C

D

D

V

L

N

N

L

L

I

I

K

K

D

S

K

K

V

V

A

A

I

I

L

I

G

G

Y

F

G

G

S

S

Q

Q

G

G

H

H

A

A

H

H

A

A

L

M

N

N

L

L

R

R

D

D

S

N

G

G

A

V

K

-

N

N

L

V

V

T

V

I

A

G

L

L

R

R

E

N

G

A

S

-

A

-

S

-

A

-

K

-

A

-

E

-

A

-

E

-

G

G

L

F

Q

E

V

V

M

M

G

S

I

V

A

S

E

E

A

A

A

S

A

K

W

I

C

A

D

D

L

V

I

I

M

M

F

I

T

L

M

A

P

P

D

D

E

E

L

I

Q

Q

A

A

E

D

T

I

Y

F

K

N

K

V

Y

E

V

I

H

K

D

P

N

N

I

L

R

S

E

E

G

G

A

K

A

A

I

I

A

A

F

F

A

A

H

H

G

G

L

F

N

N

V

I

H

H

F

Y

G

G

L

Q

I

I

E

V

P

V

K

P

A

K

G

G

V

V

D

D

V

V

I

I

M

M

M

I

A

A

P

P

K

K

G

A

P

P

G

G

H

H

T

T

V

V

R

R

G

N

E

E

Y

-

T

-

K

-

G

-

V

T

P

P

C

C

L

L

V

I

A

A

V

I

D

H

T

Q

D

D

A

E

T

S

G

K

R

N

A

A

L

K

E

N

I

L

G

A

L

L

S

S

Y

Y

C

A

S

S

A

A

I

I

G

G

R

R

S

T

G

G

I

I

E

E

T

T

N

T

F

F

R

K

E

A

E

E

C

T

E

E

T

T

D
|
D

L

L

F

F

G

G

E
|
E

Q

Q

A

A

V

V

L
|
L

C

C

G

G

L

L

V

S

E

A

L

L

I

I

R

Q

M

A

G

G

F

F

E

E

T

T

L

L

V

V

E

E

A

A

G

G

Y

Y

A

E

P

P

E

E

M

M

A

A

Y

Y

F

F

E

E

C

C

L

L

H

H

E

E

V

M

K

K

L

L

I

I

V

V

D

D

L

L

I

I

Y

Y

E

Q

G

G

I

I

A

A

N

D

M

M

N

R

Y

Y

S

S

I

I

S

S

N

N

T

T

A

A

E

E

Y

Y

G

G

E

D

Y

Y

V

I

S

T

G

G

P

P

R

K

V

I

L

I

P

T

Y

-

D

E

E

E

T

T

K

K

A

K

R

A

M

M

K

K

A

G

I

V

L

L

T

K

D

D

I

I

Q

Q

T

N

G

G

K

V

F

F

V

A

R

K

D

D

F

F

M

I

Q

L

E

E

N

R

T

R

V

A

G

G

Q

F

P

A

F

R

F

M

K

H

G

A

T

E

R

R

R

K

L

N

N

M

D

N

E

D

H

S

Q

L

I

I

E

E

A

K

V

T

G

G

K

R

E

N

L

L

R

R

G

A

M

M

P

P

W

W

I

I

S

S

binding pentanedial: D174 (= D191), E178 (= E195), L182 (= L199)

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)
56% identity, 99% coverage: 2:336/340 of query aligns to 3:334/344 of C8WR67

query
sites
C8WR67

R

K

V

I

Y

Y

D

D

R

A

D

D

C

I

D

S

V

I

N

Q

L

P

I

L

K

A

D

D

K

K

K

R

V

I

A

A

I

V

L

I

G

G

Y
|
Y

G
|
G

S
|
S

Q
|
Q

G

G

H

H

A

A

H

H

A

A

L

Q

N

N

L

L

R

R

D

D

S

S

G

G

A

F

K

-

N

D

L

V

V

V

V

I

A

G

L

L

R
|
R

E

P

G

G

S

S

A
x
S

S

W

A

A

K

K

K

-

A

A

E

E

A

A

E

D

G

G

L

F

Q

R

V

V

M

M

G

A

I

V

A

G

E

E

A

A

A

V

A

E

W

E

C

S

D

D

L

V

I

I

M

M

F

I

T

L

M

L

P

P

D
|
D

E
|
E

L
x
R

Q
|
Q

A

P

E

A

T

V

Y

Y

K

E

K

R

Y

E

V

I

H

R

D

P

N

Y

I

L

R

T

E

A

G

G

A

K

A

A

I

L

A

A

F

F

A

A

H

H

G

G

L

F

N

N

V

I

H

H

F

F

G

S

L

Q

I

I

E

Q

P

P

K

P

A

K

G

D

V

V

D

D

V

V

I

F

M

M

M

V

A

A

P

P

K

K

G

G

P

P

G
|
G

H

H

T

L

V

V

R

R

G

R

E

V

Y

Y

T

E

K

A

G

G

V

V

P

P

C

A

L

L

V

I

A

A

V

V

D

H

T

Q

D

D

A

A

T

S

G

G

R

Q

A

A

L

K

E

D

I

L

G

A

L

L

S

A

Y

Y

C

A

S

R

A

G

I

I

G

G

G

A

G

G

R

R

S

A

G

G

I

I

I

L

E

T

T

T

N

T

F

F

R

R

E

E

C

T

E

E

T

T

D
|
D

L

L

F

F

G

G

E
|
E

Q

Q

A

A

V

V

L

L

C

C

G

G

L

L

V

S

E

A

L

L

I

I

R

K

M

A

G

G

F

F

E

E

T

T

L

L

V

V

E

E

A

A

G

G

Y

Y

A

Q

P

P

E

E

M

I

A

A

Y

Y

F

F

E
|
E

C

C

L

L

H

H

E

E

V

M

K

K

L

L

I

I

V

V

D

D

L

L

I

I

Y

Y

E

E

G

G

I

L

A

E

N

Y

M

M

N

R

Y

Y

S

S

I

I

S

S

N

D

T

T

A

A

E

Q

Y

W

G

G

E

D

Y

F

V

T

S

S

G

G

P

P

R

R

V

I

L

I

P

-

Y

N

D

E

E

E

T

T

K

K

A

K

R

E

M

M

K

R

A

R

I

I

L

L

T

A

D

D

I

I

Q

Q

T

S

G

G

K

A

F

F

V

A

R

K

D

S

F

W

M

I

Q

L

E

E

N

N

T

Q

V

A

G

N

Q

R

P

P

F

M

F

F

K

N

G

A

T

I

R

N

R

R

L

R

N

E

D

L

E

E

H

H

Q

P

I

I

E

E

A

V

V

V

G

G

K

R

E

K

L

L

R

R

G

S

M

M

P

P

W

F

I

I

S

K

A

A

G

K

K

R

L

P

V

G

D

D

YGSQ 25:28 (= YGSQ 24:27) binding
R48 (= R48) binding ; mutation to P: Inversion of the cofactor specificity from NADPH to NADH.
S52 (≠ A52) binding ; mutation to D: Inversion of the cofactor specificity from NADPH to NADH.
DERQ 82:85 (≠ DELQ 83:86) binding
G133 (= G134) binding
D190 (= D191) binding
E194 (= E195) binding
E226 (= E227) binding

4tskA Ketol-acid reductoisomerase from alicyclobacillus acidocaldarius (see paper)
56% identity, 99% coverage: 2:336/340 of query aligns to 2:333/333 of 4tskA

query
sites
4tskA

R

K

V

I

Y

Y

D

D

R

A

D

D

C

I

D

S

V

I

N

Q

L

P

I

L

K

A

D

D

K

K

K

R

V

I

A

A

I

V

L

I

G

G

Y
|
Y

G
|
G

S
|
S

Q
|
Q

G

G

H

H

A

A

H

H

A

A

L

Q

N

N

L

L

R

R

D

D

S

S

G

G

A

F

K

-

N

D

L

V

V

V

V

I

A

G

L
|
L

R
|
R

E

P

G

G

S

S

A
x
S

S

W

A

A

K

K

K

-

A

A

E

E

A

A

E

D

G

G

L

F

Q

R

V

V

M

M

G

A

I

V

A

G

E

E

A

A

A

V

A

E

W

E

C

S

D

D

L

V

I

I

M

M

F

I

T
x
L

M
x
L

P
|
P

D
|
D

E

E

L

R

Q

Q

A

P

E

A

T

V

Y

Y

K

E

K

R

Y

E

V

I

H

R

D

P

N

Y

I

L

R

T

E

A

G

G

A

K

A

A

I

L

A

A

F

F

A

A

H
|
H

G

G

L

F

N

N

V

I

H

H

F

F

G

S

L

Q

I

I

E

Q

P

P

K

P

A

K

G

D

V

V

D

D

V

V

I

F

M

M

M

V

A

A

P

P

K
|
K

G

G

P
|
P

G

G

H

H

T

L

V

V

R

R

G

R

E

V

Y

Y

T

E

K

A

G

G

V

V

P

P

C

A

L

L

V

I

A

A

V

V

D

H

T

Q

D

D

A

A

T

S

G

G

R

Q

A

A

L

K

E

D

I

L

G

A

L

L

S

A

Y

Y

C

A

S

R

A

G

I

I

G

G

G

A

G

G

R

R

S

A

G

G

I

I

I

L

E

T

T

T

N

T

F

F

R

R

E

E

C

T

E

E

T

T

D
|
D

L

L

F

F

G

G

E
|
E

Q

Q

A

A

V

V

L

L

C

C

G

G

L

L

V

S

E

A

L

L

I

I

R

K

M

A

G

G

F

F

E

E

T

T

L

L

V

V

E

E

A

A

G

G

Y

Y

A

Q

P

P

E

E

M

I

A

A

Y

Y

F

F

E

E

C

C

L

L

H

H

E

E

V

M

K

K

L

L

I

I

V

V

D

D

L

L

I

I

Y

Y

E

E

G

G

I

L

A

E

N

Y

M

M

N
x
R

Y
|
Y

S

S

I
|
I

S

S

N
x
D

T

T

A

A

E
x
Q

Y

W

G

G

E

D

Y

F

V

T

S

S

G

G

P

P

R

R

V

I

L

I

P

-

Y

N

D

E

E

E

T

T

K

K

A

K

R

E

M

M

K

R

A

R

I

I

L

L

T

A

D

D

I

I

Q

Q

T

S

G

G

K

A

F

F

V

A

R

K

D

S

F

W

M

I

Q

L

E

E

N

N

T

Q

V

A

G

N

Q

R

P

P

F

M

F

F

K

N

G

A

T

I

R

N

R

R

L

R

N

E

D

L

E

E

H

H

Q

P

I

I

E

E

A

V

V

V

G

G

K

R

E

K

L

L

R

R

G

S

M

M

P

P

W

F

I

I

S

K

A

A

G

K

K

R

L

P

V

G

D

D

active site: K129 (= K131), D189 (= D191), E193 (= E195)
binding magnesium ion: D189 (= D191), D189 (= D191), E193 (= E195), E193 (= E195), R246 (≠ N248), Y247 (= Y249), I249 (= I251), D251 (≠ N253), Q254 (≠ E256)
binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y24), G25 (= G25), S26 (= S26), Q27 (= Q27), L46 (= L47), R47 (= R48), S51 (≠ A52), L78 (≠ T80), L79 (≠ M81), P80 (= P82), D81 (= D83), H106 (= H108), P131 (= P133)

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)
54% identity, 97% coverage: 1:329/340 of query aligns to 3:329/337 of P9WKJ7

query
sites
P9WKJ7

M

L

R

E

V

M

Y

F

Y

Y

D

D

R

D

D

D

C

A

D

D

V

L

N

S

L

I

I

I

K

Q

D

G

K

R

K

K

V

V

A

G

I

V

L

I

G

G

Y

Y

G

G

S

S

Q

Q

G

G

H

H

A

A

H

H

A

S

L

L

N

S

L

L

R

R

D

D

S

S

G

G

A

V

K

Q

N

-

L

V

V

R

V

V

A

G

L

L

R

K

E

Q

G

G

S

S

A

R

S

S

A

R

K

P

K

K

A

V

E

E

A

E

E

Q

G

G

L

L

Q

D

V

V

M

D

G

T

I

P

A

A

E

E

A

V

A

A

A

K

W

W

C

A

D

D

L

V

I

V

M

M

F

V

T

L

M

A

P

P

D

D

E

T

L

A

Q

Q

A

A

E

E

T

I

Y

F

K

A

K

G

Y

D

V

I

H

E

D

P

N

N

I

L

R

K

E

P

G

G

A

D

A

A

I

L

A

F

F

F

A

G

H

H

G

G

L

L

N

N

V

V

H

H

F

F

G

G

L

L

I

I

E

K

P

P

K

P

A

A

G

D

V

V

D

A

V

V

I

A

M

M

M

V

A

A

P

P

K

K

G

G

P

P

G

G

H

H

T

L

V

V

R

R

G

R

E

Q

Y

F

T

V

K

D

G

G

G

K

G

G

V

V

P

P

C

C

L

L

V

V

A

A

V

V

D

E

T

Q

D

D

A

P

T

R

G

G

R

D

A

G

L

L

E

A

I

L

G

A

L

L

S

S

Y

Y

C

A

S

K

A

A

I

I

G

G

G

T

R

R

S

A

G

G

I

V

I

I

E

K

T

T

N

T

F

F

R

K

E

D

E

E

C

T

E

E

T

T

D
|
D

L

L

F

F

G

G

E
|
E

Q

Q

A

T

V

V

L

L

C

C

G

G

L

T

V

E

E

E

L

L

I

V

R

K

M

A

G

G

F

F

E

E

T

V

L

M

V

V

E

E

A

A

G

G

Y

Y

A

P

P

A

E

E

M

L

A

A

Y

Y

F

F

E
|
E

C

V

L

L

H

H

E
|
E

V

L

K

K

L

L

I

I

V

V

D

D

L

L

I

M

Y

Y

E

E

G

G

I

L

A

A

N

R

M

M

N

Y

Y

Y

S

S

I

V

S

S

N

D

T

T

A

A

E

E

Y

F

G

G

E

G

Y

Y

V

L

S

S

G

G

P

P

R

R

V

V

L

I

P

D

Y

A

D

G

E

-

T

T

K

K

A

E

R

R

M

M

K

R

A

D

I

I

L

L

T

R

D

E

I

I

Q

Q

T

D

G

G

K

S

F

F

V

V

R

H

D

K

F

L

M

V

Q

A

E

D

N

V

T

E

V

G

G

G

Q

N

P

K

F

Q

F

L

K

E

G

E

T

L

R

R

L

Q

N

N

D

A

E

E

H

H

Q

P

I

I

E

E

A

V

V

V

G

G

K

K

E

K

L

L

R

R

G

D

M

L

M

M

P

S

W

W

I

V

D192 (= D191) binding ; binding
E196 (= E195) binding
E228 (= E227) binding
E232 (= E231) 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)
54% identity, 96% coverage: 3:329/340 of query aligns to 1:325/325 of 4ypoA

query
sites
4ypoA

V

M

Y

F

Y

Y

D

D

R

D

D

D

C

A

D

D

V

L

N

S

L

I

I

I

K

Q

D

G

K

R

K

K

V

V

A

G

I

V

L

I

G

G

Y

Y

G

G

S

S

Q

Q

G

G

H

H

A

A

H

H

A

S

L

L

N

S

L

L

R

R

D

D

S

S

G

G

A

V

K

Q

N

-

L

V

V

R

V

V

A

G

L

L

R

K

E

Q

G

G

S

S

A

R

S

S

A

R

K

P

K

K

A

V

E

E

A

E

E

Q

G

G

L

L

Q

D

V

V

M

D

G

T

I

P

A

A

E

E

A

V

A

A

A

K

W

W

C

A

D

D

L

V

I

V

M

M

F

V

T

L

M

A

P

P

D

D

E

T

L

A

Q

Q

A

A

E

E

T

I

Y

F

K

A

K

G

Y

D

V

I

H

E

D

P

N

N

I

L

R

K

E

P

G

G

A

D

A

A

I

L

A

F

F

F

A

G

H

H

G

G

L

L

N

N

V

V

H

H

F

F

G

G

L

L

I

I

E

K

P

P

K

P

A

A

G

D

V

V

D

A

V

V

I

A

M

M

M

V

A

A

P

P

K
|
K

G

G

P

P

G

G

H

H

T

L

V

V

R

R

G

R

E

Q

Y

F

T

V

K

D

G

G

G

K

G

G

V

V

P

P

C

C

L

L

V

V

A

A

V

V

D

E

T

Q

D

D

A

P

T

R

G

G

R

D

A

G

L

L

E

A

I

L

G

A

L

L

S

S

Y

Y

C

A

S

K

A

A

I

I

G

G

G

T

R

R

S

A

G

G

I

V

I

I

E

K

T

T

N

T

F

F

R

K

E

D

E

E

C

T

E

E

T

T

D
|
D

L

L

F

F

G

G

E
|
E

Q

Q

A

T

V

V

L

L

C

C

G

G

L

T

V

E

E

E

L

L

I

V

R

K

M

A

G

G

F

F

E

E

T

V

L

M

V

V

E

E

A

A

G

G

Y

Y

A

P

P

A

E

E

M

L

A

A

Y

Y

F

F

E
|
E

C

V

L

L

H

H

E
|
E

V

L

K

K

L

L

I

I

V

V

D

D

L

L

I

M

Y

Y

E

E

G

G

I

L

A

A

N

R

M

M

N

Y

Y

Y

S

S

I

V

S

S

N

D

T

T

A

A

E

E

Y

F

G

G

E

G

Y

Y

V

L

S

S

G

G

P

P

R

R

V

V

L

I

P

D

Y

A

D

G

E

-

T

T

K

K

A

E

R

R

M

M

K

R

A

D

I

I

L

L

T

R

D

E

I

I

Q

Q

T

D

G

G

K

S

F

F

V

V

R

H

D

K

F

L

M

V

Q

A

E

D

N

V

T

E

V

G

G

G

Q

N

P

K

F

Q

F

L

K

E

G

E

T

L

R

R

L

Q

N

N

D

A

E

E

H

H

Q

P

I

I

E

E

A

V

V

V

G

G

K

K

E

K

L

L

R

R

G

D

M

L

M

M

P

S

W

W

I

V

active site: K128 (= K131), D188 (= D191), E192 (= E195)
binding magnesium ion: D188 (= D191), E192 (= E195), E224 (= E227), E228 (= E231)

6jx2B Crystal structure of ketol-acid reductoisomerase from corynebacterium glutamicum (see paper)
56% identity, 97% coverage: 1:329/340 of query aligns to 1:327/327 of 6jx2B

query
sites
6jx2B

M

I

R

E

V

L

Y

L

Y

Y

D

D

R

A

D

D

C

A

D

D

V

L

N

S

L

L

I

I

K

Q

D

G

K

R

K

K

V

V

A

A

I

I

L

V

G

G

Y

Y

G

G

S

S

Q

Q

G

G

H

H

A

A

H

H

A

S

L

Q

N

N

L

L

R

R

D

D

S

S

G

G

A

V

K

E

N

-

L

V

V

V

V

I

A

G

L

L

R

R

E

E

G

G

S

S

A

K

S

S

A

A

K

E

K

K

A

A

E

K

A

E

E

A

G

G

L

F

Q

E

V

V

M

K

G

T

I

T

A

A

E

E

A

A

W

W

C
x
A

D

D

L

V

I

I

M

M

F

L

T

L

M

A

P

P

D

D

E

T

L

S

Q

Q

A

A

E

E

T

I

Y

F

K

T

K

N

Y

D

V

I

H

E

D

P

N

N

I

L

R
x
N

E

A

G

G

A
x
D

A

A

I

L

A

L

F

F

A

G

H

H

G

G

L

L

N

N

V

I

H

H

F

F

G

D

L

L

I

I

E

K

P

P

K

A

A

D

G

D

V

I

D

I

V

V

I

G

M

M

M

V

A

A

P

P

K

K

G

G

P

P

G

G

H

H

T

L

V

V

R

R

G

R

E

Q

Y

F

T

V

K

D

G

G

G

K

G

G

V

V

P

P

C

C

L

L

V

I

A

A

V

V

D

D

T

Q

D

D

A

P

T

T

G

G

R

T

A

A

L

Q

E

A

I

L

G

T

L

L

S

S

Y

Y

C

A

S

A

A

A

I

I

G

G

G

A

R

R

S

A

G

G

I

V

I

I

E

P

T

T

N

T

F

F

R

E

E

A

E

E

C

T

E

V

T

T

D
|
D

L

L

F

F

G

G

E
|
E

Q

Q

A

A

V

V

L

L

C

C

G

G

L

T

V

E

E

E

L

L

I

V

R

K

M

V

G

G

F

F

E

E

T

V

L

L

V

T

E

E

A

A

G

G

Y

Y

A

E

P

P

E

E

M

M

A

A

Y

Y

F

F

E
|
E

C

V

L

L

H

H

E
|
E

V

L

K

K

L

L

I

I

V

V

D

D

L

L

I

M

Y

F

E

E

G

G

I

I

A

S

N

N

M

M

N

N

Y

Y

S

S

I

V

S

S

N

D

T

T

A

A

E

E

Y

F

G

G

E

G

Y

Y

V

L

S

S

G

G

P

P

R

R

V

V

L

I

P

D

Y

A

D

D

E

-

T

T

K

K

A

S

R

R

M

M

K

K

A

D

I

I

L

L

T

T

D

D

I

I

Q

Q

T

D

G

G

K

T

F

F

V

T

R

K

D

R

F

L

M

I

Q

A

E

N

N

V

T

E

V

N

G

G

Q

N

P

T

F

E

F

L

K

E

G

G

T

L

R

R

R

A

L

S

N

Y

D

N

E

N

H

H

Q

P

I

I

E

E

A

E

V

T

G

G

K

A

E

K

L

L

R

R

G

D

M

L

M

M

P

S

W

W

I

V

binding magnesium ion: A73 (≠ C74), N98 (≠ R99), D101 (≠ A102), D190 (= D191), D190 (= D191), E194 (= E195), E194 (= E195), E226 (= E227), E230 (= E231)

8ep7C Crystal structure of the ketol-acid reductoisomerase from bacillus anthracis in complex with NADP
54% identity, 97% coverage: 1:331/340 of query aligns to 1:328/328 of 8ep7C

query
sites
8ep7C

M

M

R

K

V

T

Y

Y

D

E

R

Q

D

D

C

A

D

N

V

V

N

G

L

L

I

L

K

Q

D

G

K

K

K

T

V

V

A

A

I

V

L

I

G

G

Y
|
Y

G
|
G

S
|
S

Q
|
Q

G

G

H

H

A

A

H

Q

A

A

L

Q

N

N

L

L

R

R

D

D

S

S

G

G

A

V

K

E

N

-

L

V

V

V

A

G

L

V

R
|
R

E

P

G

G

S

K

A

-

S
|
S

A

F

K

E

K

V

A

A

E

K

A

A

E

D

G

G

L

F

Q

E

V

V

M

M

G

S

I

V

A

S

E

E

A

A

A

V

A

R

W

T

C

A

D

Q

L

V

I

V

M

Q

F

M

T
x
L

M
x
L

P
|
P

D
|
D

E

E

L
x
Q

Q

Q

A

A

E

H

T
x
V

Y

Y

K

K

K

A

Y

E

V

V

H

E

D

E

N

N

I

L

R

R

E

E

G

G

A

Q

A

M

I

L

A

L

F

F

A

S

H
|
H

G

G

L

F

N

N

V

I

H

H

F

F

G

G

L

Q

I

I

E

N

P

P

K

P

A

S

G

Y

V

V

D

D

V

V

I

A

M

M

M

V

A

A

P

P

K

K

G

S

P

P

G

G

H

H

T

L

V

V

R

R

G

R

E

V

Y

F

T

Q

K

E

G

G

G

N

G

G

V

V

P

P

C

A

L

L

V

V

A

A

V

V

D

H

T

Q

D

D

A

A

T

T

G

G

R

T

A

A

L

L

E

H

I

V

G

A

L

L

S

A

Y

Y

C

A

S

K

A

G

I

V

G

G

G

C

G

T

R

R

S

A

G

G

I

V

I

I

E

E

T

T

N

T

F

F

R

Q

E

E

C

T

E

E

T

T

D

D

L

L

F

F

G

G

E

E

Q

Q

A

A

V

V

L

L

C

C

G

G

L

V

V

T

E

A

L

L

I

V

R

K

M

A

G

G

F

F

E

E

T

T

L

L

V

T

E

E

A

G

G

G

Y

Y

A

R

P

P

E

E

M

I

A

A

Y

Y

F

F

E

E

C

C

L

L

H

H

E

E

V

L

K

K

L

L

I

I

V

V

D

D

L

L

I

M

Y

Y

E

E

G

G

I

L

A

T

N

N

M

M

N

R

Y

H

S

S

I

I

S

S

N

D

T

T

A

A

E

E

Y

F

G

G

E

D

Y

Y

V

V

S

T

G

G

P

S

R

R

V

I

L

V

P

T

Y

-

D

D

E

E

T

T

K

K

A

K

R

E

M

M

K

K

A

R

I

V

L

L

T

T

D

E

I

I

Q

Q

T

Q

G

G

K

E

F

F

V

A

R

K

D

K

F

W

M

I

Q

L

E

E

N

N

T

Q

V

A

G

G

Q

R

P

P

F

T

F

Y

K

N

G

A

T

M

R

K

L

A

N

E

D

Q

E

N

H

H

Q

Q

I

L

E

E

A

K

V

V

G

G

K

E

E

E

L

L

R

R

G

E

M

M

P

S

W

W

I

I

S

H

A

A

binding nadp nicotinamide-adenine-dinucleotide phosphate: Y24 (= Y24), G25 (= G25), S26 (= S26), Q27 (= Q27), R47 (= R48), S51 (= S53), L78 (≠ T80), L79 (≠ M81), P80 (= P82), D81 (= D83), Q83 (≠ L85), V87 (≠ T89), H106 (= H108)

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)
54% identity, 97% coverage: 1:329/340 of query aligns to 12:338/342 of D0WGK0

query
sites
D0WGK0

M

V

R

T

V

I

Y

L

Y

Y

D

E

R

Q

D

D

C

V

D

D

V

P

N

K

L

V

I

I

K

Q

D

G

K

L

K

K

V

V

A

G

I

I

L

I

G

G

Y
|
Y

G
|
G

S
|
S

Q
|
Q

G

G

H

H

A

A

H

H

A

A

L

L

N

N

L

L

R

M

D

D

S

S

G

G

A

V

K

-

N

D

L

V

V

R

V

V

A

G

L

L

R
|
R

E

E

G

G

S
|
S

A

S

S
|
S

A

W

K

K

K

T

A

A

E

E

A

E

E

A

G

G

L

L

Q

K

V

V

M

T

G

D

I

M

A

D

E

T

A

A

A

E

W

E

C

A

D

D

L

V

I

I

M

M

F

V

T

L

M

V

P

P

D
|
D

E
|
E

L
x
I

Q
|
Q

A

P

E

K

T

V

Y

Y

K

Q

K

E

Y

H

V

I

H

A

D

A

N

H

I

L

R

K

E

A

G

G

A

N

A

T

I

L

A

A

F

F

A

A

H

H

G

G

L

F

N

N

V

I

H

H

F

Y

G

G

L

Y

I

I

E

V

P

P

K

P

A

E

G

D

V

V

D

N

V

V

I

I

M

M

M

C

A

A

P

P

K

K

G

G

P

P

G
|
G

H

H

T

I

V

V

R

R

G

R

E

Q

Y

F

T

T

K

E

G

G

G

S

G

G

V

V

P

P

C

D

L

L

V

A

A

C

V

V

D

Q

T

Q

D

D

A

A

T

T

G

G

R

N

A

A

L

W

E

D

I

I

G

V

L

L

S

S

Y

Y

C

C

S

W

A

G

I

V

G

G

G

A

R

R

S

S

G

G

I

I

E

K

T

A

N

T

F

F

R

A

E

E

C

T

E

E

T

E

D
|
D

L

L

F

F

G

G

E
|
E

Q

Q

A

A

V

V

L

L

C

C

G

G

L

L

V

V

E

E

L

L

I

V

R

K

M

A

G

G

F

F

E

E

T

T

L

L

V

T

E

E

A

A

G

G

Y

Y

A

P

P

P

E

E

M

L

A

A

Y

Y

F

F

E

E

C

C

L

Y

H

H

E

E

V

M

K

K

L

M

I

I

V

V

D

D

L

L

I

M

Y

Y

E

E

G

S

G

G

I

I

A

H

N

F

M

M

N

N

Y

Y

S

S

I

I

S
|
S

N

N

T

T

A

A

E

E

Y

Y

G

G

E

E

Y

Y

V

Y

S

A

G

G

P

P

R

K

V

V

L

I

P

N

Y

-

D

E

E

Q

T

S

K

R

A

E

R

A

M

M

K

K

A

E

I

I

L

L

T

K

D

R

I

I

Q

Q

T

D

G

G

K

S

F

F

V

A

R

Q

D

E

F

F

M

V

Q

D

E

D

N

C

T

N

V

N

G

G

Q

H

P

K

F

R

F

L

K

L

G

E

T

Q

R

R

R

E

L

A

N

I

D

N

E

T

H

H

Q

P

I

I

E

E

A

T

V

T

G

G

K

A

E

Q

L

I

R

R

G

S

M

M

M

F

P

S

W

W

I

I

YGSQ 35:38 (= YGSQ 24:27) binding
R58 (= R48) binding
S61 (= S51) 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 (= S53) 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 (≠ DELQ 83:86) binding
G144 (= G134) binding
D201 (= D191) binding
E205 (= E195) binding
S262 (= S252) binding

4kqwA The structure of the slackia exigua kari in complex with NADP (see paper)
54% identity, 96% coverage: 3:329/340 of query aligns to 2:326/326 of 4kqwA

query
sites
4kqwA

V

I

Y

L

Y

Y

D

E

R

Q

D

D

C

V

D

D

V

P

N

K

L

V

I

I

K

Q

D

G

K

L

K

K

V

V

A

G

I

I

L

I

G

G

Y
|
Y

G
|
G

S
|
S

Q
|
Q

G

G

H

H

A

A

H

H

A

A

L

L

N

N

L

L

R

M

D

D

S

S

G

G

A

V

K

-

N

D

L

V

V

R

V

V

A

G

L

L

R
|
R

E

E

G

G

S
|
S

A

S

S
|
S

A

W

K

K

K

T

A

A

E

E

A

E

E

A

G

G

L

L

Q

K

V

V

M

T

G

D

I

M

A

D

E

T

A

A

A

E

W

E

C

A

D

D

L

V

I

I

M

M

F

V

T
x
L

M
x
V

P
|
P

D
|
D

E

E

L
x
I

Q
|
Q

A

P

E

K

T

V

Y

Y

K

Q

K

E

Y

H

V

I

H

A

D

A

N

H

I

L

R

K

E

A

G

G

A

N

A

T

I

L

A

A

F

F

A

A

H
|
H

G

G

L

F

N

N

V

I

H

H

F

Y

G

G

L

Y

I

I

E

V

P

P

K

P

A

E

G

D

V

V

D

N

V

V

I

I

M

M

M

C

A

A

P

P

K
|
K

G

G

P
|
P

G

G

H

H

T

I

V

V

R

R

G

R

E

Q

Y

F

T

T

K

E

G

G

G

S

G

G

V

V

P

P

C

D

L

L

V

A

A

C

V

V

D

Q

T

Q

D

D

A

A

T

T

G

G

R

N

A

A

L

W

E

D

I

I

G

V

L

L

S

S

Y

Y

C

C

S

W

A

G

I

V

G

G

G

A

R

R

S

S

G

G

I

I

E

K

T

A

N

T

F

F

R

A

E

E

C

T

E

E

T

E

D
|
D

L

L

F

F

G

G

E
|
E

Q

Q

A

A

V

V

L

L

C

C

G

G

L

L

V

V

E

E

L

L

I

V

R

K

M

A

G

G

F

F

E

E

T

T

L

L

V

T

E

E

A

A

G

G

Y

Y

A

P

P

P

E

E

M

L

A

A

Y

Y

F

F

E

E

C

C

L

Y

H

H

E

E

V

M

K

K

L

M

I

I

V

V

D

D

L

L

I

M

Y

Y

E

E

G

S

G

G

I

I

A

H

N

F

M

M

N

N

Y

Y

S

S

I
|
I

S
|
S

N

N

T

T

A

A

E

E

Y

Y

G

G

E

E

Y

Y

V

Y

S

A

G

G

P

P

R

K

V

V

L

I

P

N

Y

-

D

E

E

Q

T

S

K

R

A

E

R

A

M

M

K

K

A

E

I

I

L

L

T

K

D

R

I

I

Q

Q

T

D

G

G

K

S

F

F

V

A

R

Q

D

E

F

F

M

V

Q

D

E

D

N

C

T

N

V

N

G

G

Q

H

P

K

F

R

F

L

K

L

G

E

T

Q

R

R

R

E

L

A

N

I

D

N

E

T

H

H

Q

P

I

I

E

E

A

T

V

T

G

G

K

A

E

Q

L

I

R

R

G

S

M

M

M

F

P

S

W

W

I

I

active site: K129 (= K131), D189 (= D191), E193 (= E195)
binding magnesium ion: D189 (= D191), E193 (= E195)
binding nadp nicotinamide-adenine-dinucleotide phosphate: Y23 (= Y24), G24 (= G25), S25 (= S26), Q26 (= Q27), R46 (= R48), S49 (= S51), S51 (= S53), L78 (≠ T80), V79 (≠ M81), P80 (= P82), D81 (= D83), I83 (≠ L85), Q84 (= Q86), H106 (= H108), P131 (= P133), I249 (= I251), S250 (= S252)

6jx2A Crystal structure of ketol-acid reductoisomerase from corynebacterium glutamicum (see paper)
56% identity, 96% coverage: 1:326/340 of query aligns to 1:324/325 of 6jx2A

query
sites
6jx2A

M

I

R

E

V

L

Y

L

Y

Y

D

D

R

A

D

D

C

A

D

D

V

L

N

S

L

L

I

I

K

Q

D

G

K

R

K

K

V

V

A

A

I

I

L

V

G
|
G

Y
|
Y

G
|
G

S

S

Q

Q

G

G

H

H

A

A

H

H

A

S

L

Q

N

N

L

L

R

R

D

D

S

S

G

G

A

V

K

E

N

-

L

V

V

V

V

I

A

G

L

L

R
|
R

E

E

G

G

S
|
S

A
x
K

S
|
S

A

A

K

E

K

K

A

A

E

K

A

E

E

A

G

G

L

F

Q

E

V

V

M

K

G

T

I

T

A

A

E

E

A

A

W

W

C

A

D

D

L

V

I

I

M

M

F

L

T

L

M
x
A

P
|
P

D

D

E

T

L

S

Q

Q

A

A

E

E

T
x
I

Y

F

K

T

K

N

Y

D

V

I

H

E

D

P

N

N

I

L

R
x
N

E

A

G

G

A
x
D

A

A

I

L

A

L

F

F

A

G

H

H

G

G

L

L

N

N

V

I

H

H

F

F

G

D

L

L

I

I

E

K

P

P

K

A

A

D

G

D

V

I

D

I

V

V

I

G

M

M

M

V

A

A

P

P

K

K

G

G

P

P

G

G

H

H

T

L

V

V

R

R

G

R

E

Q

Y

F

T

V

K

D

G

G

G

K

G

G

V

V

P

P

C

C

L

L

V

I

A

A

V

V

D

D

T

Q