SitesBLAST

P9WQI3 Trehalose import ATP-binding protein SugC; MtbSugC; Nucleotide-binding domain of SugABC transporter; NBD of SugABC transporter; SugABC transporter ATPase SugC; EC 7.5.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
41% identity, 64% coverage: 2:240/373 of query aligns to 4:237/393 of P9WQI3

query
sites
P9WQI3

I

I

R

V

L

L

D

D

A

H

A

V

T

N

K

K

V

S

F

Y

P

P

G

D

S

G

D

-

Q

H

P

T

A

A

V

V

D

R

Q

D

L

L

S

N

L

L

A

T

I

I

P

A

E

D

G

G

E

E

L

F

V

L

V

I

F

L

V

V

G

G

P

P

S

S

G

G

C

C

G

G

K

K

T

T

L

L

K

N

M

M

I

I

N

A

R

G

I

L

V

E

E

D

P

I

T

S

S

S

G

G

T

E

I

L

T

R

I

I

G

A

G

G

E

E

D

R

V

V

L

N

S

E

R

K

P

A

A

P

H

K

L

-

V

-

R

D

R

R

D

D

I

I

G

A

Y

M

V

V

I

F

Q

Q

Q

S

I

Y

G

A

L

L

F

Y

P

P

H

H

R

M

T

T

I

V

E

R

R

Q

N

N

V

I

A

A

T

F

V

P

P

L

R

T

L

L

L

A

G

K

W

M

D

R

E

K

D

A

R

D

T

I

A

A

A

Q

R

K

V

V

D

S

E

E

L

T

L

A

E

K

L

I

M

L

D

D

L

L

D

T

P

N

A

L

M

L

K

D

T

-

R

R

Y

K

P

P

G

S

E

Q

L

L

S

S

G

G

Q

Q

R

R

Q

Q

R

R

V

V

G

A

V

M

A

G

R

R

A

A

L

I

A

V

A

R

D

H

P

P

P

K

V

A

L

F

L

L

M

M

D

D

E

E

P

P

Y

L

G

S

A

N

V

L

D

D

P

A

V

K

V

L

R

R

G

V

R

Q

L

M

Q

R

D

G

Q

E

L

I

L

A

E

Q

L

L

Q

Q

R

R

D

R

L

L

H

G

K

T

T

T

I

T

V

V

F

Y

V

V

T

T

H
|
H

D

D

I

Q

D

T

E

E

A

A

I

M

R

T

L

L

G

G

D

D

R

R

I

V

A

V

I

V

L

M

N

-

I

Y

G

G

K

I

L

A

E

Q

Q

Q

F

I

D

G

T

T

P

P

E

E

T

E

I

L

L

Y

R

E

D

R

P

P

A

A

N

N

G

L

F

F

V

V

E

A

D

G

F

F

L

I

G

G

G

S

H193 (= H195) mutation to A: Decreased hydrolysis of ATP. No change in KM, but 2-fold reduction in Vmax compared to wild-type.

1g291 Malk (see paper)
42% identity, 64% coverage: 2:239/373 of query aligns to 4:241/372 of 1g291

query
sites
1g291

I

V

R

R

L

L

D

V

A

D

A

V

T

W

K

K

V

V

F

F

P

-

G

-

S

G

D

E

Q

V

P

T

A

A

V

V

D

R

Q

E

L

M

S

S

L

L

A

E

I

V

P

K

E

D

G

G

E

E

L

F

V

M

V

I

F

L

V

L

G

G

P

P

S
|
S

G
|
G

C
|
C

G
|
G

K
|
K

T
|
T

T

T

L

L

K

R

M

M

I

I

N

A

R

G

I

L

V

E

E

E

P

P

T

S

S

R

G

G

T

Q

I

I

T

Y

I

I

G

G

G

-

E

D

D

K

V

L

L

V

S

A

R
x
D

P

P

A
x
E

H
x
K

L

G

V

I

R

F

-

V

-

P

-
x
K

-
x
D

R

R

D

D

I

I

G

A

Y

M

V

V

I

F

Q

Q

Q

S

I

Y

G

A

L

L

F

Y

P

P

H

H

R

M

T

T

I

V

E

Y

R

D

N

N

V

I

A

A

T

F

V

P

P

L

R

K

L

L

L

R

G

K

W

V

D

P

E

R

D

Q

R

E

T

I

A

D

A

Q

R

R

V

V

D

R

E

E

L

V

L

A

E

E

L

L

M

L

D

G

L

L

D

T

P

E

A

L

M

L

K

-

T

N

R

R

Y

K

P

P

G

R

E

E

L

L

S

S

G

G

Q

Q

R

R

Q

Q

R

R

V

V

G

A

V

L

A

G

R

R

A

A

L

I

A

V

A

R

D

K

P

P

P

Q

V

V

L

F

L

L

M

M

D

D

E

E

P

P

Y

L

G

S

A

N

V

L

D

D

P

A

V

K

V

L

R

R

G

V

R

R

L

M

Q

R

D

A

Q

E

L

L

L

K

E

K

L

L

Q

Q

R

R

D

Q

L

L

H

G

K

V

T

T

I

T

V

I

F

Y

V

V

T

T

H

H

D

D

I

Q

D

V

E

E

A

A

I

M

R

T

L

M

G

G

D

D

R

R

I

I

A

A

I

V

L

M

N

N

I

-

G

R

G

G

K

V

L

L

E

Q

Q

Q

F

V

D

G

T

S

P

P

E

D

T

E

I

V

L

Y

R

D

D

K

P

P

A

A

N

N

G

T

F

F

V

V

E

A

D

G

F

F

L

I

G

G

binding magnesium ion: D69 (≠ R70), E71 (≠ A72), K72 (≠ H73), K79 (vs. gap), D80 (vs. gap)
binding pyrophosphate 2-: S38 (= S38), G39 (= G39), C40 (= C40), G41 (= G41), K42 (= K42), T43 (= T43), T44 (= T44)

Sites not aligning to the query:

binding magnesium ion: 292, 293, 359

2d62A Crystal structure of multiple sugar binding transport atp- binding protein
43% identity, 61% coverage: 15:240/373 of query aligns to 18:245/375 of 2d62A

query
sites
2d62A

D

D

Q

V

P

T

A

A

V

V

D

K

Q

D

L

L

S

S

L

L

A

E

I

I

P

K

E

D

G

G

E

E

L

F

V

L

V

V

F

L

V

L

G

G

P

P

S

S

G
|
G

C
|
C

G
|
G

K
|
K

T
|
T

T

T

L

L

K

R

M

M

I

I

N

A

R

G

I

L

V

E

E

E

P

P

T

T

S

R

G

G

T

Q

I

I

T

Y

I

I

G

E

G

-

E

D

D

N

V

L

L

V

S

A

R

D

P

P

A

E

H

K

L

G

V

V

-

F

-

V

-

P

-

K

R

E

R

R

D

D

I

V

G

A

Y

M

V

V

I

F

Q

Q

Q

S

I

Y

G

A

L

L

F

Y

P

P

H

H

R

M

T

T

I

V

E

Y

R

D

N

N

V

I

A

A

T

F

V

P

P

L

R

K

L

L

L

R

G

K

W

V

D

P

E

K

D

Q

R

E

T

I

A

D

A

K

R

R

V

V

D

R

E

E

L

V

L

A

E

E

L

M

M

L

D

G

L

L

D

T

P

E

A

L

M

L

K

-

T

N

R

R

Y

K

P

P

G

R

E

E

L

L

S

S

G

G

Q

Q

R

R

Q

Q

R

R

V

V

G

A

V

L

A

G

R

R

A

A

L

I

A

I

A

R

D

R

P

P

P

K

V

V

L

F

L

L

M

M

D

D

E

E

P

P

Y

L

G

S

A

N

V

L

D

D

P

A

V

K

V

L

R

R

G

V

R

K

L

M

Q

R

D

A

Q

E

L

L

L

K

E

K

L

L

Q

Q

R

R

D

Q

L

L

H

G

K

V

T

T

I

T

V

I

F

Y

V

V

T

T

H

H

D

D

I

Q

D

V

E

E

A

A

I

M

R

T

L

M

G

G

D

D

R

R

I

I

A

A

I

V

L

M

N

N

I

-

G

K

G

G

K

E

L

L

E

Q

Q

Q

F

V

D

G

T

T

P

P

E

D

T

E

I

V

L

Y

R

Y

D

K

P

P

A

V

N

N

G

T

F

F

V

V

E

A

D

G

F

F

L

I

G

G

G

S

binding pyrophosphate 2-: G42 (= G39), C43 (= C40), G44 (= G41), K45 (= K42), T46 (= T43), T47 (= T44)

P69874 Spermidine/putrescine import ATP-binding protein PotA; EC 7.6.2.11 from Escherichia coli (strain K12) (see 3 papers)
35% identity, 93% coverage: 1:348/373 of query aligns to 17:349/378 of P69874

query
sites
P69874

M

L

I

V

R

Q

L

L

D

A

A

G

A

I

T

R

K

K

V
x
C

F
|
F

P

D

G

G

S

K

D

E

Q

-

P

-

A

V

V

I

D

P

Q

Q

L

L

S

D

L

L

A

T

I

I

P

N

E

N

G

G

E

E

L
x
F

V

L

V

T

F

L

V

L

G

G

P

P

S

S

G

G

C
|
C

G

G

K

K

T

T

T

V

L
|
L

K

R

M

L

I

I

N

A

R

G

I

L

V

E

E

T

P

V

T

D

S

S

G

G

T

R

I

I

T

M

I
x
L

G

D

G

N

E

E

D

D

V

I

L

T

S

H

R

V

P

P

A

A

H

E

L

-

V

-

R

N

R

R

D

Y

I

V

G

N

Y

T

V

V

I

F

Q

Q

Q

S

I

Y

G

A

L

L

F

F

P

P

H

H

R

M

T

T

I

V

E

F

R

E

N

N

V

V

A

A

T

F

V

G

P

L

R

R

L

M

L

Q

G

K

W

T

D

P

E

A

D

A

R

E

T

I

A

T

A

P

R

R

V

V

D

M

E

E

L

A

L

L

E

R

L

M

M
x
V

D

Q

L

L

D

E

P

-

A

T

M

F

K

A

T

Q

R

R

Y

K

P

P

G

H

E

Q

L

L

S

S

G

G

Q

Q

R

Q

Q

Q

R

R

V

V

G

A

V

I

A

A

R

R

A

A

L

V

A

V

A

N

D

K

P

P

P

R

V

L

L

L

M

L

D
|
D

E

E

P

S

Y

L

G

S

A

A

V

L

D

D

P

Y

V

K

V

L

R

R

G

K

R

Q

L

M

Q

Q

D

N

Q

E

L

L

L

K

E

A

L

L

Q

Q

R

R

D

K

L

L

H

G

K

I

T

T

I

F

V

V

F

F

V

V

T

T

H

H

D

D

I

Q

D

E

E

E

A

A

I

L

R

T

L

M

G

S

D

D

R

R

I

I

A

V

I

V

L

M

N

R

I

-

G

D

G

G

K

R

L

I

E

E

Q

Q

F

D

D

G

T

T

P

P

E

R

T

E

I

I

L

Y

R

E

D

E

P

P

A

K

N

N

G

L

F

F

V

V

E

A

D

G

F

F

L

I

G

G

G

-

E

-

R

-

G

E

L

I

K

N

R

M

L

F

A

N

L

A

R

T

C

V

V

I

G

E

D

R

L

L

G

D

E

E

L

Q

P

R

R

V

G

R

A

A

T

N

V

V

T

E

A

G

D

R

D

E

T
x
C

G

N

D

I

H

Y

A

-

V

V

A

N

V

F

A

A

E

V

A

E

Y

P

G

G

V

Q

D

K

W

L

C

H

G

V

I

L

L

L

D

R

G

P

E
|
E

D

D

L

L

R

R

G

V

W

E

A

E

W

I

L

N

D

D

L

N

R

H

G

A

V

E

P

G

R

L

A

I

G

G

E

Y

V

V

E

R

T

E

R

R

R

N

F

Y

R

K

V

G

A

M

T

T

T

-

R

-

D

-

S

-

T

-

L

-

R

-

E

-

A

-

L

L

D

E

A

S

M

V

V

V

R

E

S

L

S

E

T

N

G

G

-

K

-

M

-

V

-

M

V

V

S

S

A

E

V

F

F

F

D

N

E

E

A

D

D

D

C26 (≠ V10) mutation to A: Lower ATPase activity and transport efficiency.
F27 (= F11) mutation to L: Lower ATPase activity and transport efficiency.
F45 (≠ L31) mutation to L: Lower ATPase activity and transport efficiency.
C54 (= C40) mutation to T: Loss of ATPase activity and transport.
L60 (= L46) mutation to F: Lower ATPase activity and transport efficiency.
L76 (≠ I62) mutation to P: Lower ATPase activity and transport efficiency.
V135 (≠ M123) mutation to M: Loss of ATPase activity and transport.
D172 (= D161) mutation to N: Loss of ATPase activity and transport.
C276 (≠ T269) mutation to A: Lower ATPase activity and transport efficiency.
E297 (= E291) mutation E->K,D: Lower ATPase activity and transport efficiency.; mutation to Q: Loss of ATPase activity and transport.

1vciA Crystal structure of the atp-binding cassette of multisugar transporter from pyrococcus horikoshii ot3 complexed with atp (see paper)
42% identity, 64% coverage: 2:240/373 of query aligns to 7:231/353 of 1vciA

query
sites
1vciA

I

V

R

K

L

L

D

E

A

N

A

L

T

T

K

K

V

R

F
|
F

P

-

G

-

S

G

D

N

Q
x
F

P

T

A

A

V

V

D

N

Q

K

L

L

S

N

L

L

A

T

I

I

P

K

E

D

G

G

E

E

L

F

V

L

V

V

F

L

V

L

G

G

P

P

S
|
S

G
|
G

C

C

G
|
G

K
|
K

T
|
T

T

T

L

L

K

R

M

M

I

I

N

A

R

G

I

L

V

E

E

E

P

P

T

T

S

E

G

G

T

R

I

I

T

Y

I

F

G

G

G

D

E

R

D

D

V

V

L

T

S

Y

R

L

P

P

A

P

H

K

L

-

V

-

R

D

R

R

D

N

I

I

G

S

Y

M

V

V

I

F

Q

Q

Q

-

I

-

G

-

L

-

F

-

P

-

H

H

R

M

T

T

I

V

E

Y

R

E

N

N

V

I

A

A

T

-

V

F

P

P

R

-

L

L

L

K

G

K

W

F

D

P

E

K

D

D

R

E

T

I

A

D

A

K

R

R

V

V

D

R

E

W

L

A

E

E

L

L

M

L

D

Q

L

I

D

E

P

E

A

L

M

L

K

-

T

N

R

R

Y

Y

P

P

G

A

E

Q

L

L

S

S

G

G

Q

Q

R

R

Q

Q

R

R

V

V

G

A

V

V

A

A

R

R

A

A

L

I

A

V

D

E

P

P

P

D

V

V

L

L

M

M

D

D

E

E

P

P

Y

L

G

S

A

N

V

L

D

D

P

A

V

K

V

L

R

R

G

V

R

A

L

M

Q

R

D

A

Q

E

L

I

L

K

E

K

L

L

Q

Q

R

Q

D

K

L

L

H

K

K

V

T

T

I

T

V

I

F

Y

V

V

T

T

H

H

D

D

I

Q

D

V

E

E

A

A

I

M

R

T

L

M

G

G

D

D

R

R

I

I

A

A

I

V

L

M

N

N

I

-

G

R

G

G

K

Q

L

L

E

L

Q

Q

F

I

D

G

T

S

P

P

E

T

T

E

I

V

L

Y

R

L

D

R

P

P

A

N

N

S

G

V

F

F

V

V

E

A

D

T

F

F

L

I

G

G

G

A

binding adenosine-5'-triphosphate: F16 (= F11), F19 (≠ Q16), S41 (= S38), G42 (= G39), G44 (= G41), K45 (= K42), T46 (= T43), T47 (= T44)

2awnB Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
36% identity, 66% coverage: 22:268/373 of query aligns to 21:251/374 of 2awnB

query
sites
2awnB

L

I

S

N

L

L

A

D

I

I

P

H

E

E

G

G

E

E

L

F

V

V

F

F

V

V

G

G

P

P

S
|
S

G
|
G

C

C

G
|
G

K
|
K

T
x
S

T
|
T

T

L

L

L

K

R

M

M

I

I

N

A

R

G

I

L

V

E

E

T

P

I

T

T

S

S

G

G

T

D

I

L

T

F

I

I

G

G

G

E

E

K

D

R

V

M

L

N

S

D

R

T

P

P

A

P

H

-

L

-

V

A

R

E

R

R

D

G

I

V

G

G

Y

M

V

V

I

F

Q

Q

Q

S

I

Y

G

A

L

L

F

Y

P

P

H

H

R

L

T

S

I

V

E

A

R

E

N

N

V

M

A

S

T

F

V

G

P

L

R

K

L

L

L

A

G

G

W

A

D

K

E

K

D

E

R

V

T

I

A

N

A

Q

R

R

V

V

D

N

E

Q

L

V

L

A

E

E

L

V

M

L

D

Q

L

L

D

A

P

H

A

L

M

L

K

D

T

-

R

R

Y

K

P

P

G

K

E

A

L

L

S

S

G

G

Q

Q

R

R

Q

Q

R

R

V

V

G

A

V

I

A

G

R

R

A

T

L

L

A

V

A

A

D

E

P

P

P

S

V

V

L

F

L

L

M

L

D

D

E

E

P

P

Y

L

G

S

A

N

V

L

D

D

P

A

V

A

V

L

R

R

G

V

R

Q

L

M

Q

R

D

I

Q

E

L

I

L

S

E

R

L

L

Q

H

R

K

D

R

L

L

H

G

K

R

T

T

I

M

V

I

F

Y

V

V

T

T

H

H

D

D

I

Q

D

V

E

E

A

A

I

M

R

T

L

L

G

A

D

D

R

K

I

I

A

V

I

V

L

L

N

D

I

-

G

A

G

G

K

R

L

V

E

A

Q

Q

F

V

D

G

T

K

P

P

E

L

T

E

I

L

L

Y

R

H

D

Y

P

P

A

A

N

D

G

R

F

F

V

V

E

A

D

G

F

F

L

I

G

G

G

S

E

P

R

K

G

-

L

-

K

-

R

-

L

-

A

-

L

-

R

-

C

-

V

-

G

-

D

-

L

M

G

N

E

F

L

L

P

P

R

V

G

K

A

V

T

T

V

A

T

T

A

A

D

I

D

D

binding adenosine-5'-diphosphate: S37 (= S38), G38 (= G39), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 12, 17

P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 5 papers)
36% identity, 66% coverage: 22:268/373 of query aligns to 22:252/371 of P68187

query
sites
P68187

L

I

S

N

L

L

A

D

I

I

P

H

E

E

G

G

E

E

L

F

V

V

F

F

V

V

G

G

P

P

S

S

G

G

C

C

G

G

K

K

T

S

T

T

T

L

L

L

K

R

M

M

I

I

N

A

R

G

I

L

V

E

E

T

P

I

T

T

S

S

G

G

T

D

I

L

T

F

I

I

G

G

G

E

E

K

D

R

V

M

L

N

S

D

R

T

P

P

A

P

H

-

L

-

V

A

R

E

R

R

D

G

I

V

G

G

Y

M

V

V

I

F

Q

Q

Q

S

I

Y

G
x
A

L

L

F

Y

P

P

H

H

R

L

T

S

I

V

E

A

R

E

N

N

V

M

A

S

T

F

V

G

P

L

R

K

L

L

L

A

G

G

W

A

D
x
K

E

K

D

E

R

V

T

I

A

N

A

Q

R

R

V
|
V

D

N

E

Q

L
x
V

L

A

E
|
E

L

V

M

L

D

Q

L

L

D
x
A

P

H

A

L

M

L

K

D

T

-

R

R

Y

K

P

P

G

K

E

A

L

L

S

S

G

G

G
|
G

Q

Q

R

R

Q

Q

R

R

V

V

G

A

V

I

A

G

R

R

A

T

L

L

A

V

A

A

D

E

P

P

P

S

V

V

L

F

L

L

M

L

D
|
D

E

E

P

P

Y

L

G

S

A

N

V

L

D

D

P

A

V

A

V

L

R

R

G

V

R

Q

L

M

Q

R

D

I

Q

E

L

I

L

S

E

R

L

L

Q

H

R

K

D

R

L

L

H

G

K

R

T

T

I

M

V

I

F

Y

V

V

T

T

H

H

D

D

I

Q

D

V

E

E

A

A

I

M

R

T

L

L

G

A

D

D

R

K

I

I

A

V

I

V

L

L

N

D

I

-

G

A

G

G

K

R

L

V

E

A

Q

Q

F

V

D

G

T

K

P

P

E

L

T

E

I

L

L

Y

R

H

D

Y

P

P

A

A

N

D

G
x
R

F

F

V

V

E

A

D

G

F

F

L

I

G

G

G

S

E

P

R

K

G

-

L

-

K

-

R

-

L

-

A

-

L

-

R

-

C

-

V

-

G

-

D

-

L

M

G

N

E
x
F

L

L

P

P

R

V

G

K

A

V

T

T

V

A

T

T

A

A

D

I

D

D

A85 (≠ G87) mutation to M: Suppressor of EAA loop mutations in MalFG.
K106 (≠ D108) mutation to C: Suppressor of EAA loop mutations in MalFG.
V114 (= V116) mutation to C: Suppressor of EAA loop mutations in MalFG.
V117 (≠ L119) mutation to M: Suppressor of EAA loop mutations in MalFG.
E119 (= E121) mutation to K: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
A124 (≠ D126) mutation to T: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
G137 (= G140) mutation to A: Loss of maltose transport. Has greater ability to decrease mal gene expression than wild-type MalK.
D158 (= D161) mutation to N: Loss of maltose transport but retains ability to repress mal genes.
R228 (≠ G232) mutation to C: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
F241 (≠ E257) mutation to I: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.

Sites not aligning to the query:

267 W→G: Normal maltose transport but constitutive mal gene expression.
278 G→P: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
282 S→L: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
284 G→S: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
302 G→D: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
308 E→Q: Maltose transport is affected but retains ability to interact with MalT.
322 S→F: Resistant to inhibitory effects of alpha-methylglucoside but retains transport capacity.
340 G→A: Maltose transport is affected but retains ability to interact with MalT.
346 G→S: Normal maltose transport but constitutive mal gene expression.
355 F→Y: Maltose transport is affected but retains ability to interact with MalT.

3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state (see paper)
36% identity, 66% coverage: 22:268/373 of query aligns to 21:251/371 of 3puyA

query
sites
3puyA

L

I

S

N

L

L

A

D

I

I

P

H

E

E

G

G

E

E

L

F

V

V

F

F

V

V

G

G

P

P

S
|
S

G
|
G

C
|
C

G
|
G

K
|
K

T
x
S

T
|
T

T

L

L

L

K

R

M

M

I

I

N

A

R

G

I

L

V

E

E

T

P

I

T

T

S

S

G

G

T

D

I

L

T

F

I

I

G

G

G

E

E

K

D

R

V

M

L

N

S

D

R

T

P

P

A

P

H

-

L

-

V

A

R

E

R

R

D

G

I

V

G

G

Y

M

V

V

I

F

Q
|
Q

Q

S

I

Y

G

A

L

L

F

Y

P

P

H

H

R

L

T

S

I

V

E

A

R

E

N

N

V

M

A

S

T

F

V

G

P

L

R

K

L

L

L

A

G

G

W

A

D

K

E

K

D

E

R

V

T

I

A

N

A

Q

R

R

V

V

D

N

E

Q

L

V

L

A

E

E

L

V

M

L

D

Q

L

L

D

A

P

H

A

L

M

L

K

D

T

-

R
|
R

Y

K

P

P

G

K

E
x
A

L

L

S
|
S

G

G

G
|
G

Q
|
Q

R

R

Q

Q

R

R

V

V

G

A

V

I

A

G

R

R

A

T

L

L

A

V

A

A

D

E

P

P

P

S

V

V

L

F

L

L

M

L

D

D

E
|
E

P

P

Y

L

G

S

A

N

V

L

D

D

P

A

V

A

V

L

R

R

G

V

R

Q

L

M

Q

R

D

I

Q

E

L

I

L

S

E

R

L

L

Q

H

R

K

D

R

L

L

H

G

K

R

T

T

I

M

V

I

F

Y

V

V

T

T

H
|
H

D

D

I

Q

D

V

E

E

A

A

I

M

R

T

L

L

G

A

D

D

R

K

I

I

A

V

I

V

L

L

N

D

I

-

G

A

G

G

K

R

L

V

E

A

Q

Q

F

V

D

G

T

K

P

P

E

L

T

E

I

L

L

Y

R

H

D

Y

P

P

A

A

N

D

G

R

F

F

V

V

E

A

D

G

F

F

L

I

G

G

G

S

E

P

R

K

G

-

L

-

K

-

R

-

L

-

A

-

L

-

R

-

C

-

V

-

G

-

D

-

L

M

G

N

E

F

L

L

P

P

R

V

G

K

A

V

T

T

V

A

T

T

A

A

D

I

D

D

binding phosphoaminophosphonic acid-adenylate ester: S37 (= S38), G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), Q81 (= Q84), R128 (= R132), A132 (≠ E136), S134 (= S138), G136 (= G140), Q137 (= Q141), E158 (= E162), H191 (= H195)
binding magnesium ion: S42 (≠ T43), Q81 (= Q84)

Sites not aligning to the query:

binding phosphoaminophosphonic acid-adenylate ester: 12

3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3 (see paper)
36% identity, 66% coverage: 22:268/373 of query aligns to 21:251/371 of 3puxA

query
sites
3puxA

L

I

S

N

L

L

A

D

I

I

P

H

E

E

G

G

E

E

L

F

V

V

F

F

V

V

G

G

P

P

S
|
S

G
|
G

C
|
C

G
|
G

K
|
K

T
x
S

T
|
T

T

L

L

L

K

R

M

M

I

I

N

A

R

G

I

L

V

E

E

T

P

I

T

T

S

S

G

G

T

D

I

L

T

F

I

I

G

G

G

E

E

K

D

R

V

M

L

N

S

D

R

T

P

P

A

P

H

-

L

-

V

A

R

E

R

R

D

G

I

V

G

G

Y

M

V

V

I

F

Q
|
Q

Q

S

I

Y

G

A

L

L

F

Y

P

P

H

H

R

L

T

S

I

V

E

A

R

E

N

N

V

M

A

S

T

F

V

G

P

L

R

K

L

L

L

A

G

G

W

A

D

K

E

K

D

E

R

V

T

I

A

N

A

Q

R

R

V

V

D

N

E

Q

L

V

L

A

E

E

L

V

M

L

D

Q

L

L

D

A

P

H

A

L

M

L

K

D

T

-

R
|
R

Y

K

P

P

G

K

E

A

L

L

S
|
S

G

G

G
|
G

Q
|
Q

R

R

Q

Q

R

R

V

V

G

A

V

I

A

G

R

R

A

T

L

L

A

V

A

A

D

E

P

P

P

S

V

V

L

F

L

L

M

L

D

D

E

E

P

P

Y

L

G

S

A

N

V

L

D

D

P

A

V

A

V

L

R

R

G

V

R

Q

L

M

Q

R

D

I

Q

E

L

I

L

S

E

R

L

L

Q

H

R

K

D

R

L

L

H

G

K

R

T

T

I

M

V

I

F

Y

V

V

T

T

H
|
H

D

D

I

Q

D

V

E

E

A

A

I

M

R

T

L

L

G

A

D

D

R

K

I

I

A

V

I

V

L

L

N

D

I

-

G

A

G

G

K

R

L

V

E

A

Q

Q

F

V

D

G

T

K

P

P

E

L

T

E

I

L

L

Y

R

H

D

Y

P

P

A

A

N

D

G

R

F

F

V

V

E

A

D

G

F

F

L

I

G

G

G

S

E

P

R

K

G

-

L

-

K

-

R

-

L

-

A

-

L

-

R

-

C

-

V

-

G

-

D

-

L

M

G

N

E

F

L

L

P

P

R

V

G

K

A

V

T

T

V

A

T

T

A

A

D

I

D

D

binding adenosine-5'-diphosphate: G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (= R132), S134 (= S138), Q137 (= Q141)
binding beryllium trifluoride ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q84), S134 (= S138), G136 (= G140), H191 (= H195)
binding magnesium ion: S42 (≠ T43), Q81 (= Q84)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 12

3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4 (see paper)
36% identity, 66% coverage: 22:268/373 of query aligns to 21:251/371 of 3puwA

query
sites
3puwA

L

I

S

N

L

L

A

D

I

I

P

H

E

E

G

G

E

E

L

F

V

V

F

F

V

V

G

G

P

P

S
|
S

G
|
G

C
|
C

G
|
G

K
|
K

T
x
S

T
|
T

T

L

L

L

K

R

M

M

I

I

N

A

R

G

I

L

V

E

E

T

P

I

T

T

S

S

G

G

T

D

I

L

T

F

I

I

G

G

G

E

E

K

D

R

V

M

L

N

S

D

R

T

P

P

A

P

H

-

L

-

V

A

R

E

R

R

D

G

I

V

G

G

Y

M

V

V

I

F

Q
|
Q

Q

S

I

Y

G

A

L

L

F

Y

P

P

H

H

R

L

T

S

I

V

E

A

R

E

N

N

V

M

A

S

T

F

V

G

P

L

R

K

L

L

L

A

G

G

W

A

D

K

E

K

D

E

R

V

T

I

A

N

A

Q

R

R

V

V

D

N

E

Q

L

V

L

A

E

E

L

V

M

L

D

Q

L

L

D

A

P

H

A

L

M

L

K

D

T

-

R
|
R

Y

K

P

P

G

K

E
x
A

L

L

S
|
S

G
|
G

Q
|
Q

R

R

Q

Q

R

R

V

V

G

A

V

I

A

G

R

R

A

T

L

L

A

V

A

A

D

E

P

P

P

S

V

V

L

F

L

L

M

L

D

D

E
|
E

P

P

Y

L

G

S

A

N

V

L

D

D

P

A

V

A

V

L

R

R

G

V

R

Q

L

M

Q

R

D

I

Q

E

L

I

L

S

E

R

L

L

Q

H

R

K

D

R

L

L

H

G

K

R

T

T

I

M

V

I

F

Y

V

V

T

T

H
|
H

D

D

I

Q

D

V

E

E

A

A

I

M

R

T

L

L

G

A

D

D

R

K

I

I

A

V

I

V

L

L

N

D

I

-

G

A

G

G

K

R

L

V

E

A

Q

Q

F

V

D

G

T

K

P

P

E

L

T

E

I

L

L

Y

R

H

D

Y

P

P

A

A

N

D

G

R

F

F

V

V

E

A

D

G

F

F

L

I

G

G

G

S

E

P

R

K

G

-

L

-

K

-

R

-

L

-

A

-

L

-

R

-

C

-

V

-

G

-

D

-

L

M

G

N

E

F

L

L

P

P

R

V

G

K

A

V

T

T

V

A

T

T

A

A

D

I

D

D

binding adenosine-5'-diphosphate: G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (= R132), A132 (≠ E136), S134 (= S138), Q137 (= Q141)
binding tetrafluoroaluminate ion: S37 (= S38), G38 (= G39), K41 (= K42), Q81 (= Q84), S134 (= S138), G135 (= G139), G136 (= G140), E158 (= E162), H191 (= H195)
binding magnesium ion: S42 (≠ T43), Q81 (= Q84)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 12, 17

3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4 (see paper)
36% identity, 66% coverage: 22:268/373 of query aligns to 21:251/371 of 3puvA

query
sites
3puvA

L

I

S

N

L

L

A

D

I

I

P

H

E

E

G

G

E

E

L

F

V

V

F

F

V

V

G

G

P

P

S

S

G
|
G

C
|
C

G
|
G

K
|
K

T
x
S

T
|
T

T

L

L

L

K

R

M

M

I

I

N

A

R

G

I

L

V

E

E

T

P

I

T

T

S

S

G

G

T

D

I

L

T

F

I

I

G

G

G

E

E

K

D

R

V

M

L

N

S

D

R

T

P

P

A

P

H

-

L

-

V

A

R

E

R

R

D

G

I

V

G

G

Y

M

V

V

I

F

Q
|
Q

Q

S

I

Y

G

A

L

L

F

Y

P

P

H

H

R

L

T

S

I

V

E

A

R

E

N

N

V

M

A

S

T

F

V

G

P

L

R

K

L

L

L

A

G

G

W

A

D

K

E

K

D

E

R

V

T

I

A

N

A

Q

R

R

V

V

D

N

E

Q

L

V

L

A

E

E

L

V

M

L

D

Q

L

L

D

A

P

H

A

L

M

L

K

D

T

-

R
|
R

Y

K

P

P

G

K

E
x
A

L

L

S
|
S

G

G

Q
|
Q

R

R

Q

Q

R

R

V

V

G

A

V

I

A

G

R

R

A

T

L

L

A

V

A

A

D

E

P

P

P

S

V

V

L

F

L

L

M

L

D

D

E

E

P

P

Y

L

G

S

A

N

V

L

D

D

P

A

V

A

V

L

R

R

G

V

R

Q

L

M

Q

R

D

I

Q

E

L

I

L

S

E

R

L

L

Q

H

R

K

D

R

L

L

H

G

K

R

T

T

I

M

V

I

F

Y

V

V

T

T

H

H

D

D

I

Q

D

V

E

E

A

A

I

M

R

T

L

L

G

A

D

D

R

K

I

I

A

V

I

V

L

L

N

D

I

-

G

A

G

G

K

R

L

V

E

A

Q

Q

F

V

D

G

T

K

P

P

E

L

T

E

I

L

L

Y

R

H

D

Y

P

P

A

A

N

D

G

R

F

F

V

V

E

A

D

G

F

F

L

I

G

G

G

S

E

P

R

K

G

-

L

-

K

-

R

-

L

-

A

-

L

-

R

-

C

-

V

-

G

-

D

-

L

M

G

N

E

F

L

L

P

P

R

V

G

K

A

V

T

T

V

A

T

T

A

A

D

I

D

D

binding adenosine-5'-diphosphate: G38 (= G39), C39 (= C40), G40 (= G41), K41 (= K42), S42 (≠ T43), T43 (= T44), R128 (= R132), A132 (≠ E136), S134 (= S138), Q137 (= Q141)
binding magnesium ion: S42 (≠ T43), Q81 (= Q84)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 12, 17

1q12A Crystal structure of the atp-bound e. Coli malk (see paper)
36% identity, 66% coverage: 22:268/373 of query aligns to 19:249/367 of 1q12A

query
sites
1q12A

L

I

S

N

L

L

A

D

I

I

P

H

E

E

G

G

E

E

L

F

V

V

F

F

V

V

G

G

P

P

S
|
S

G
|
G

C
|
C

G
|
G

K
|
K

T
x
S

T
|
T

T

L

L

L

K

R

M

M

I

I

N

A

R

G

I

L

V

E

E

T

P

I

T

T

S

S

G

G

T

D

I

L

T

F

I

I

G

G

G

E

E

K

D

R

V

M

L

N

S

D

R

T

P

P

A

P

H

-

L

-

V

A

R

E

R

R

D

G

I

V

G

G

Y

M

V

V

I

F

Q

Q

Q

S

I

Y

G

A

L

L

F

Y

P

P

H

H

R

L

T

S

I

V

E

A

R

E

N

N

V

M

A

S

T

F

V

G

P

L

R

K

L

L

L

A

G

G

W

A

D

K

E

K

D

E

R

V

T

I

A

N

A

Q

R

R

V

V

D

N

E

Q

L

V

L

A

E

E

L

V

M

L

D

Q

L

L

D

A

P

H

A

L

M

L

K

D

T

-

R
|
R

Y

K

P

P

G

K

E
x
A

L

L

S
|
S

G

G

G
|
G

Q
|
Q

R

R

Q

Q

R

R

V

V

G

A

V

I

A

G

R

R

A

T

L

L

A

V

A

A

D

E

P

P

P

S

V

V

L

F

L

L

M

L

D

D

E

E

P

P

Y

L

G

S

A

N

V

L

D

D

P

A

V

A

V

L

R

R

G

V

R

Q

L

M

Q

R

D

I

Q

E

L

I

L

S

E

R

L

L

Q

H

R

K

D

R

L

L

H

G

K

R

T

T

I

M

V

I

F

Y

V

V

T

T

H

H

D

D

I

Q

D

V

E

E

A

A

I

M

R

T

L

L

G

A

D

D

R

K

I

I

A

V

I

V

L

L

N

D

I

-

G

A

G

G

K

R

L

V

E

A

Q

Q

F

V

D

G

T

K

P

P

E

L

T

E

I

L

L

Y

R

H

D

Y

P

P

A

A

N

D

G

R

F

F

V

V

E

A

D

G

F

F

L

I

G

G

G

S

E

P

R

K

G

-

L

-

K

-

R

-

L

-

A

-

L

-

R

-

C

-

V

-

G

-

D

-

L

M

G

N

E

F

L

L

P

P

R

V

G

K

A

V

T

T

V

A

T

T

A

A

D

I

D

D

binding adenosine-5'-triphosphate: S35 (= S38), G36 (= G39), C37 (= C40), G38 (= G41), K39 (= K42), S40 (≠ T43), T41 (= T44), R126 (= R132), A130 (≠ E136), S132 (= S138), G134 (= G140), Q135 (= Q141)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 10

P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
38% identity, 59% coverage: 22:242/373 of query aligns to 22:238/369 of P19566

query
sites
P19566

L

I

S

N

L

L

A

D

I

I

P

H

E

D

G

G

E

E

L

F

V

V

F

F

V

V

G

G

P

P

S

S

G

G

C

C

G

G

K

K

T

S

T

T

T

L

L

L

K

R

M

M

I

I

N

A

R

G

I

L

V

E

E

T

P

I

T

T

S

S

G

G

T

D

I

L

T

F

I

I

G

G

G

E

E

T

D

R

V

M

L

N

S

D

R

I

P

P

A

P

H

-

L

-

V

A

R

E

R

R

D

G

I

V

G

G

Y

M

V

V

I

F

Q

Q

Q

S

I

Y

G

A

L
|
L

F

Y

P

P

H

H

R

L

T

S

I

V

E

A

R

E

N

N

V

M

A

S

T

F

V

G

P

L

R

K

L

L

L

A

G

G

W

A

D

K

E

K

D

E

R

V

T

M

A

N

A

Q

R

R

V

V

D

N

E

Q

L

V

L

A

E

E

L

V

M

L

D

Q

L

L

D

A

P

H

A

L

M

L

K

E

T

-

R

R

Y

K

P

P

G

K

E

A

L

L

S

S

G

G

Q

Q

R

R

Q

Q

R

R

V

V

G

A

V

I

A

G

R

R

A

T

L

L

A

V

A

A

D

E

P

P

P

R

V

V

L

F

L

L

M

L

D

D

E

E

P
|
P

Y

L

G

S

A

N

V

L

D
|
D

P

A

V

A

V

L

R

R

G

V

R

Q

L

M

Q

R

D

I

Q

E

L

I

L

S

E

R

L

L

Q

H

R

K

D

R

L

L

H

G

K

R

T

T

I

M

V

I

F

Y

V

V

T

T

H

H

D

D

I

Q

D

V

E

E

A

A

I

M

R

T

L

L

G

A

D

D

R

K

I

I

A

V

I

V

L

L

N

D

I

-

G

A

G

G

K

R

L

V

E

A

Q

Q

F

V

D

G

T

K

P

P

E

L

T

E

I

L

L

Y

R

H

D

Y

P

P

A

A

N

D

G

R

F

F

V

V

E

A

D

G

F

F

L

I

G

G

G

S

E

P

R

K

L86 (= L88) mutation to F: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
P160 (= P163) mutation to L: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.
D165 (= D168) mutation to N: Loss of transport. No effect on ATP-binding activity but decrease in ATP hydrolysis. Retains repressor activity.

Sites not aligning to the query:

306 E→K: Loss of transport. No effect on ATP-binding and ATP hydrolysis. Retains repressor activity.

P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
35% identity, 64% coverage: 1:238/373 of query aligns to 1:241/343 of P30750

query
sites
P30750

M

M

I

I

R

K

L

L

D

S

A

N

A

I

T

T

K

K

V

V

F

F

P

H

G

Q

S

G

D

T

Q

R

P

T

-

I

-

Q

A

A

V

L

D

N

Q

N

L

V

S

S

L

L

A

H

I

V

P

P

E

A

G

G

E

Q

L

I

V

Y

V

G

F

V

V

I

G

G

P

A

S
|
S

G
|
G

C
x
A

G
|
G

K
|
K

T
x
S

T
|
T

T

L

L

I

K

R

M

C

I

V

N

N

R

L

I

L

V

E

E

R

P

P

T

T

S

E

G

G

T

S

I

V

T

L

I

V

G

D

G

G

E

Q

D

E

V

L

L

T

S

T

R

L

P

S

A

E

H

S

L

E

V

L

-

T

-

K

-

A

R

R

D

Q

I

I

G

G

Y

M

V

I

I

F

Q

Q

Q

H

I

F

G

N

L

L

F

L

P

S

H

S

R

R

T

T

I

V

E

F

R

G

N

N

V

V

A

A

T

L

V

P

P

L

R

E

L

L

L

D

G

N

W

T

D

P

E

K

D

D

R

E

T

V

A

K

A

R

R

R

V

V

D

T

E

E

L

L

E

S

L

L

M

V

D

G

L

L

D

G

P

D

A

K

M

H

K

D

T

S

R

-

Y

Y

P

P

G

S

E

N

L

L

S

S

G

G

Q

Q

R

K

Q

Q

R

R

V

V

G

A

V

I

A

A

R

R

A

A

L

L

A

A

A

S

D

N

P

P

P

K

V

V

L

L

M

C

D

D

E
|
E

P

A

Y

T

G

S

A

A

V

L

D

D

P

P

V

A

V

T

R

T

G

R

R

S

L

I

Q

L

D

E

Q

L

L

L

L

K

E

D

L

I

Q

N

R

R

D

R

L

L

H

G

K

L

T

T

I

I

V

L

F

L

V

I

T

T

H

H

D

E

I

M

D

D

E

V

A

V

I

K

R

R

L

I

G

C

D

D

R

C

I

V

A

A

I

V

L

I

N

S

I

N

G

G

G

E

K

L

L

I

E

E

Q

Q

F

-

D

D

T

T

P

V

E

S

T

E

I

V

L

F

R

S

D

H

P

P

A

K

N

T

G

P

F

L

V

A

E

Q

D

K

F

F

L

I

40:46 (vs. 38:44, 71% identical) binding ATP
E166 (= E162) mutation to Q: Exhibits little ATPase activity.

Sites not aligning to the query:

278:283 binding L-methionine
295 N→A: Reduces the binding of L-methionine to undetectable levels.
295:296 binding L-methionine

Query Sequence

>WP_052669764.1 NCBI__GCF_000969705.1:WP_052669764.1
MIRLDAATKVFPGSDQPAVDQLSLAIPEGELVVFVGPSGCGKTTTLKMINRIVEPTSGTI
TIGGEDVLSRPAHLVRRDIGYVIQQIGLFPHRTIERNVATVPRLLGWDEDRTAARVDELL
ELMDLDPAMKTRYPGELSGGQRQRVGVARALAADPPVLLMDEPYGAVDPVVRGRLQDQLL
ELQRDLHKTIVFVTHDIDEAIRLGDRIAILNIGGKLEQFDTPETILRDPANGFVEDFLGG
ERGLKRLALRCVGDLGELPRGATVTADDTGDHAVAVAEAYGVDWCGILDGEDLRGWAWLD
DLRGVPRAGEVETRRFRVATTRDSTLREALDAMVRSSTGVSAVFDEADRYLGMLQLSDLT
AEITGSSGTPAAA

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