SitesBLAST

D41 (= D36) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
D44 (= D39) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
G85 (= G80) mutation to V: Abolishes 4-HBA transport and chemotaxis.
D89 (= D84) mutation to N: Abolishes 4-HBA transport and chemotaxis.
G92 (= G87) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to C: No change in 4-HBA transport and chemotaxis.; mutation G->L,V: Abolishes 4-HBA transport and chemotaxis.; mutation to Q: Decrease in 4-HBA transport and strong decrease in chemotaxis.
R124 (= R119) mutation to A: Abolishes 4-HBA transport.
E144 (= E139) mutation to A: Strong decrease in 4-HBA transport.
H183 (≠ R178) mutation to A: Decrease in 4-HBA transport and chemotaxis.
D323 (= D316) mutation to N: Abolishes 4-HBA transport and chemotaxis.
H328 (≠ N321) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to R: Decrease in 4-HBA transport and loss of chemotaxis.
R386 (= R379) mutation to A: Strong decrease in 4-HBA transport.
R398 (= R391) mutation to A: Abolishes 4-HBA transport.

Sites not aligning to the query:

444 H→A: No change in 4-HBA transport and chemotaxis.

Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
41% identity, 95% coverage: 4:431/452 of query aligns to 2:429/452 of Q5EXK5

query
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D82 (= D84) mutation to A: Loss of activity.
V311 (= V313) mutation to W: Loss of activity.
D314 (= D316) mutation to A: Loss of activity.

P77589 3-(3-hydroxy-phenyl)propionate transporter; 3HPP transporter; 3-(3-hydroxy-phenyl)propionate:H(+) symporter; 3HPP:H(+) symporter from Escherichia coli (strain K12) (see paper)
31% identity, 91% coverage: 28:439/452 of query aligns to 19:397/403 of P77589

query
sites
P77589

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E27 (≠ D36) mutation to A: Lack of 3HPP transport activity.; mutation to D: Slight decrease in 3HPP transport activity.
D75 (= D84) mutation D->A,E: Lack of 3HPP transport activity.
A272 (≠ V313) mutation to H: 30% increase in 3HPP transport activity.
K276 (≠ R317) mutation to D: Lack of 3HPP transport activity.

Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
29% identity, 81% coverage: 30:395/452 of query aligns to 48:390/444 of Q8NLB7

query
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Q8NLB7

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D54 (= D36) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
D57 (= D39) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
R103 (= R85) mutation to A: Loss of transport activity.
W309 (≠ V313) mutation to V: Loss of transport activity.
D312 (= D316) mutation to A: Loss of transport activity.
R313 (= R317) mutation to A: Loss of transport activity.
I317 (≠ N321) mutation I->H,Y: Loss of transport activity.
R386 (= R391) mutation to A: Loss of transport activity.

P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
24% identity, 65% coverage: 22:316/452 of query aligns to 14:301/430 of P0AA76

query
sites
P0AA76

Q

R

W

Y

L

L

V

T

F

L

F

V

M

M

C

I

F

F

I

I

I

T

V

V

L

V

L

I

D

C

G
x
Y

F

V

D
|
D

T
x
R

A

A

A

N

I

L

G

A

F

V

I

A

A

S

P

A

S

H

L

I

I

Q

A

E

E

E

W

F

G

G

I

I

T

T

R

K

P

A

A

E

L

M

A

G

P

Y

V

V

L

F

S

S

A

A

A

F

L

A

F

W

G

L

L
x
Y

A

T

C

L

G

C

A

Q

L

I

G

P

S

G

G

G

P

W

L

F

S

L

D

D

R

R

L

V

G

G

R

S

R

R

S

V

L

T

L

Y

L

F

G

I

S

A

V

I

L

F

L

G

F

W

G

S

V

V

A

A

C

T

L

L

G

F

S

Q

A

G

F

F

S

A

T

T

S

G

I

L

E

M

Q

S

L

L

T

I

T

G

L

L

R

R

F

A

I

I

T

T

G

G

V

I

G

F

L
x
E

G

A

A

P

A

A

M

F

P

P

N

T

A

N

V

N

T

R

M

M

M

V

G

T

E

S

Y

W

C

F

P

P

D

E

R

H

R

E

R

R

A

A

T

S

V

A

I

V

N

G

L

F

M

Y

F

T

C

S

G

G

F

Q

P

F

L

V

G

G

A

L

A

A

F

F

G

L

G

T

F

P

L

L

A

L

A

I

W

W

M

I

I

Q

P

E

H

M

F

L

G

S

W

W

R

H

S

W

V

V

L

F

L

I

L

V

-

T

G

G

I

I

T

G

P

I

L

I

L

W

L

S

L

L

I

I

V

W

L

F

A

K

I

V

K

Y

M

Q

P

P

E

P

S

R

V

L

R

T

Y

K

M

G

V

I

A

S

N

K

N

A

K

E

P

-

V

L

E

D

R

Y

I

I

R

R

A

D

A

G

L

G

A

G

R

L

I

V

S

D

S

G

E

D

A

A

A

P

Q

-

A

-

G

-

S

-

F

-

V

V

M

K

T

K

E

E

T

A

A

R

P

Q

Q

P

T

L

G

T

G

A

K

K

G

D

M

W

A

K

V

L

V

V

L

F

S

H

R

R

S

K

Y

-

I

L

I

I

G

G

S

-

V

-

M

-

L

V

W

Y

I

L

A

G

Y

Q

F

F

M

A

G

V

L

A

V

S

I

T

F

L

Y

W

A

F

S

F

I

L

N

T

W

W

M

F

P

P

-

N

I

Y

L

L

L

T

K

Q

D

E

A

K

G

G

L

I

T

T

P

A

Q

L

R

K

A

A

T

G

L

F

I

M

S

T

A

T

L

V

-

P

F

F

P

L

L

A

G

A

G

F

V

V

G

G

A

V

V

L

L

L

C

S

G

G

V

W

L

V

M

A

D

D

Y29 (≠ G37) binding
D31 (= D39) mutation to N: Loss of galactonate transport activity.
R32 (≠ T40) binding
Y64 (≠ L72) binding
E118 (≠ L126) mutation to Q: Loss of galactonate transport activity.

Sites not aligning to the query:

358 binding

6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
24% identity, 65% coverage: 22:316/452 of query aligns to 3:282/409 of 6e9nA

query
sites
6e9nA

Q

R

W

Y

L

L

V

T

F

L

F

V

M

M

C

I

F

F

I

I

I

T

V

V

L

V

L

I

D

C

G

Y

F

V

D

D

T

R

A

A

A

N

I

L

G

A

F

V

I

A

A

S

P

A

S

H

L

I

I

Q

A

E

E

E

W

F

G

G

I

I

T

T

R

K

P

A

A

E

L

M

A

G

P

Y

V

V

L

F

S

S

A

A

A

F

L

A

F

W

G

L

L

Y

A

T

C

L

G

C

A

Q

L

I

G

P

S

G

G

G

P

W

L

F

S

L

D

D

R

R

L

V

G

G

R

S

R

R

S

V

L

T

L

Y

L

F

G

I

S

A

V

I

L

F

L

G

F

W

G

S

V

V

A

A

C

T

L

L

G

F

S

Q

A

G

F

F

S

A

T

T

S

G

I

L

E

M

Q

S

L

L

T

I

T

G

L

L

R

R

F

A

I

I

T

T

G

G

V

I

G

F

L

E

G

A

A

P

A

A

M
x
F

P

P

N

T

A

N

V

N

T

R

M

M

M

V

G

T

E

S

Y

W

C

F

P

P

D

E

R

H

R

E

R

R

A

A

T

S

V

A

I

V

N

G

L

F

M

Y

F

T

C

S

G

G

F

Q

P

F

L

V

G

G

A

L

A

A

F

F

G

L

G

T

F

P

L

L

A

L

A

I

W

W

M

I

I

Q

P

E

H

M

F

L

G

S

W

W

R

H

S

W

V

V

L

F

L

I

L

V

-

T

G

G

I

I

T

G

P

I

L

I

L

W

L

S

L

L

I

I

V

W

L

F

A

K

I

V

K

Y

M

Q

P

P

E

-

S

-

V

-

R

-

Y

-

M

-

V

-

A

-

N

-

K

-

P

-

V

-

E

P

R

R

I

L

R

T

A

K

A

G

L

I

A

S

R

K

I

A

S

E

S

L

E

D

A

Y

A

I

Q

R

A

D

G

G

S

G

F

G

V

L

M

V

T

D

E

G

T

D

A

A

P

P

Q

L

T

T

G

-

G

A

K

K

G

D

M

W

A

K

V

L

V

V

L

F

S

H

R

R

S

K

Y

-

I

L

I

I

G

G

S

-

V

-

M

-

L

V

W

Y

I

L

A

G

Y

Q

F

F

M

A

G

V

L

A

V

S

I

T

F

L

Y

W

A

F

S

F

I

L

N

T

W

W

M

F

P

P

-

N

I

Y

L

L

L

T

K

Q

D

E

A

K

G

G

L

I

T

T

P

A

Q

L

R

K

A

A

T

G

L

F

I

M

S

T

A

T

L

V

-

P

F

F

P

L

L

A

G

A

G

F

V

V

G

G

A

V

V

L

L

L

C

S

G

G

V

W

L

V

M

A

D

D

binding D-gluconic acid: F111 (≠ M130)

Sites not aligning to the query:

binding D-gluconic acid: 359

Q02563 Synaptic vesicle glycoprotein 2A; Synaptic vesicle protein 2; Synaptic vesicle protein 2A from Rattus norvegicus (Rat) (see 2 papers)
25% identity, 46% coverage: 6:214/452 of query aligns to 149:369/742 of Q02563

query
sites
Q02563

A

A

V

Q

N

Q

V

Y

Q

E

T

T

F

I

I

L

N

R

E

E

H

C

P

G

F

H

S

G

P

R

F

F

Q

Q

W

W

L

T

V

L

F

Y

F

F

M

V

C

L

F

G

I

L

I

A

V

L

L

M

L

A

D

D

G

G

F

V

D

E

T

V

A

F

A

V

I

V

G

G

F

F

I

V

A

L

P

P

S

S

L

A

I

E

A

K

E
x
D

W
x
M

G
x
C

I
x
L

T
x
S

R

D

P

S

A

N

L

K

A

G

P

M

V

L

L

G

S

L

A

I

A

V

L

Y

F

L

G

G

L

M

A

M

C

V

G

G

A

A

L

F

G

L

S

W

G

G

P

G

L

L

S

A

D

D

R

R

L

L

G

G

R

R

S

Q

L

C

L

L

G

I

S

S

V

L

L

S

L

V

F

N

G

S

V

V

A

F

C

A

L

F

G

F

S

S

A

S

F

F

S

V

T

Q

S

G

I

Y

E

G

Q

T

L

F

T

L

T

F

L

C

R

R

F

L

I

L

T

S

G

G

V

V

G

G

L

I

G

G

A

G

A

S

M

I

P

P

N

I

A

V

V

F

T

S

M

Y

M

F

G

S

E

E

Y

F

C

L

P

A

D

Q

R

E

R

K

R

R

A

G

T

E

V

H

I

L

N

S

L

W

M

L

F

C

C

M

G

F

F

W

P

M

L

I

G

G

A

G

A

V

F

Y

G

A

F

A

L

M

A

A

A

W

W

A

M

I

I

I

P

P

H

H

F

Y

G

G

W

W

R
x
S

-
x
F

-
x
Q

-
x
M

-
x
G

-
x
S

-
x
A

-
x
Y

-
x
Q

-
x
F

-
x
H

-

S

-

W

S

R

V

V

L

F

L

V

L

L

G

V

G

C

I

A

T

F

P

P

L

S

L

V

L

F

L

A

I

I

V

G

L

A

A

L

I

T

K

T

M

Q

P

P

E

E

S

S

V

P

R

R

Y

F

M

F

V

L

A

E

N

N

N

G

K

K

P

H

V

D

E

E

DMCLS 196:200 (≠ EWGIT 53:57) mutation Missing: No change in uptake of C.botulinum neurotoxin type D (BoNT/D, botD) or C.botulinum neurotoxin type E (BoNT/E).
321:331 (vs. 178:178, 0% identical) mutation Missing: No change in uptake of BoNT/D or BoNT/E.

Sites not aligning to the query:

498 N→Q: No change in uptake of BoNT/E or C.botulinum neurotoxin type A (BoNT/A, botA) by mouse SV2A/SV2B knockout neurons; SV2A apparent molecular weight decreases. No change in uptake of BoNT/E; when associated with Q-548. No change in uptake of BoNT/D.
548 N→Q: No change in uptake of BoNT/E or BoNT/A by mouse SV2A/SV2B knockout neurons; SV2A apparent molecular weight decreases. No change in uptake of BoNT/E; when associated with Q-498. No change in uptake of BoNT/D.
570:573 RLVN→TLVQ: Restores apparent molecular weight to wild-type, does not restore uptake of BoNT/E.
573 N→Q: BoNT/E not taken up by mouse SV2A/SV2B knockout neurons, decreased uptake of BoNT/A; SV2A apparent molecular weight decreases. No change in uptake of BoNT/D.

6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
28% identity, 40% coverage: 22:200/452 of query aligns to 6:185/393 of 6e9oA

query
sites
6e9oA

Q

R

W

Y

L

L

V

T

F

L

F

V

M

M

C

I

F

F

I

I

I

T

V

V

L

V

L

I

D

C

G
x
Y

F

V

D

D

T

R

A

A

A

N

I

L

G

A

F

V

I

A

A

S

P

A

S

H

L

I

I

Q

A

E

E

E

W

F

G

G

I

I

T

T

R

K

P

A

A

E

L

M

A

G

P

Y

V

V

L

F

S

S

A

A

A

F

L

A

F

W

G

L

L

Y

A

T

C

L

G

C

A

Q

L

I

G

P

S

G

G

G

P

W

L

F

S

L

D

D

R

R

L

V

G

G

R

S

R

R

S

V

L

T

L

Y

L

F

G

I

S

A

V

I

L

F

L

G

F

W

G

S

V

V

A

A

C

T

L

L

G

F

S

Q

A

G

F

F

S

A

T

T

S

G

I

L

E

M

Q

S

L

L

T

I

T

G

L

L

R

R

F

A

I

I

T

T

G

G

V

I

G

F

L

Q

G

A

A

P

A

A

M
x
F

P

P

N

T

A

N

V

N

T

R

M

M

M

V

G

T

E

S

Y

W

C

F

P

P

D

E

R

H

R

E

R

R

A

A

T

S

V

A

I

V

N

G

L

F

M

Y

F

T

C

S

G

G

F
x
Q

P

F

L

V

G

G

A

L

A

A

F

F

G

L

G

T

F

P

L

L

A

L

A

I

W

W

M

I

I

Q

P

E

H

M

F

L

G

S

W

W

R

H

S

W

V

V

L

F

L

I

L

V

-

T

G

G

I

I

T

G

P

I

L

I

L

W

L

S

L

L

I

I

V

W

L

F

A

K

I

V

K

Y

M

Q

P

P

binding D-galactonic acid: Y21 (≠ G37), F114 (≠ M130), Q141 (≠ F157)

Sites not aligning to the query:

binding D-galactonic acid: 228, 320, 343

Q9NSA0 Solute carrier family 22 member 11; Organic anion transporter 4; OAT4; Organic anion:dicarboxylate exchanger OAT4 from Homo sapiens (Human) (see 3 papers)
28% identity, 39% coverage: 49:224/452 of query aligns to 127:303/550 of Q9NSA0

query
sites
Q9NSA0

S

T

L

I

I

V

A

A

E

K

W

W

G

D

I

L

-

V

-

C

T

S

R

S

P

Q

A

G

L

L

A

K

P

P

V

-

L

L

S

S

A

Q

A

S

L

I

F

F

-

M

-

S

G

G

L

I

A

L

C

V

G

G

A

S

L

F

G

I

S

W

G

G

P

L

L

L

S

S

D

Y

R

R

L

F

G

G

R

R

R

K

S

P

L

M

L

L

L

S

G

W

S

C

V

C

L

L

L

Q

F

L

G

A

V

V

A

A

C

G

L

T

G

S

S

T

A

I

F

F

S

A

T

P

S

T

I

F

E

V

Q

I

L

Y

T

C

T

G

L

L

R

R

F

F

I

V

T

A

G

A

V

F

G

G

L

M

G

A

A

G

A

I

M

F

P

L

N

S

A

S

V

L

T

T

M

L

M

M

G

V

E

E

Y

W

C

T

P

T

D

T

R

S

R

R

A

A

T

V

V

T

I

M

N

T

L

V

M

V

F

G

C

C

G

A

F

F

P

S

L

A

G
|
G

-

Q

A

A

F

L

G

G

F

L

L

A

A

F

A

A

W

L

M

R

I

-

P

-

H

-

F

-

G

D

W

W

R

R

S

T

V

L

L

Q

L

L

L

A

G

A

G

S

I

V

T

-

P

P

L

F

L

A

L

I

I

S

V

L

L

I

A

S

I

W

K

W

M

L

P

P

E

E

S

S

V

A

R

R

Y

W

M

L

V

I

A

I

N

K

N

G

K

K

P

P

V

D

E

Q

R

A

I

L

R

Q

A

E

-

L

-

R

A

K

L

V

A

A

R

R

I

I

S

N

G241 (= G160) mutation G->L,S,V: Strongly reduced cell surface expression and estrone 3-sulfate transport.

Sites not aligning to the query:

39 N→Q: No visible effect on N-glycosylation. Loss of N-glycosylation and of cell surface location; when associated with Q-56; Q-63 and Q-99.
47 H→A: Reduced cell surface expression and estrone 3-sulfate transport. Reduced cell surface expression and estrone 3-sulfate transport; when associated with A-52; A-83; A-305 and A-469.
52 H→A: Slightly reduced estrone 3-sulfate transport. Reduced cell surface expression and estrone 3-sulfate transport; when associated with A-47; A-83; A-305 and A-469.
56 N→Q: No visible effect on N-glycosylation. Loss of N-glycosylation and of cell surface expression; when associated with Q-39; Q-63 and Q-99.
63 N→Q: No visible effect on N-glycosylation. Loss of N-glycosylation and of cell surface expression; when associated with Q-39; Q-56 and Q-99.
83 H→A: Reduced cell surface expression and estrone 3-sulfate transport; when associated with A-47; A-52; A-305 and A-469.
99 N→Q: No visible effect on N-glycosylation. Loss of N-glycosylation and of cell surface expression; when associated with Q-39; Q-56 and Q-63.
305 H→A: Reduced cell surface expression and estrone 3-sulfate transport; when associated with A-47; A-52; A-83 and A-469.
400 mutation G->L,S,V: Strongly reduced cell surface expression and estrone 3-sulfate transport.
469 H→A: Slightly reduced estrone 3-sulfate transport. Reduced cell surface expression and estrone 3-sulfate transport; when associated with A-47; A-52; A-83 and A-305.

Q9Z2I6 Synaptic vesicle glycoprotein 2C; Synaptic vesicle protein 2C from Rattus norvegicus (Rat) (see 3 papers)
24% identity, 46% coverage: 6:214/452 of query aligns to 135:355/727 of Q9Z2I6

query
sites
Q9Z2I6

A

A

V

Q

N

Q

V

Y

Q

E

T

L

F

I

I

I

N

Q

E

E

H

C

P

G

F

H

S

G

P

R

F

F

Q

Q

W

W

L

A

V

L

F

F

M

V

C

L

F

G

I

M

I

A

V

L

L

M

L

A

D

D

G

G

F

V

D

E

T

V

A

F

A

V

I

V

G

G

F

F

I

V

A

L

P

P

S

S

L

A

I

E

A

T

E

D

W

L

G

C

I

I

T

P

R

N

P

S

A

G

L

S

A

G

P

W

V

L

L

G

S

S

A

I

A

V

L

Y

F

L

G

G

L

M

A

M

C

V

G

G

A

A

L

F

G

F

S

W

G

G

P

G

L

L

S

A

D

D

R

K

L

V

G

G

R

R

R

K

S

Q

L

S

L

L

G

I

S

C

V

M

L

S

L

V

F

N

G

G

V

F

A

F

C

A

L

F

G

L

S

S

A

S

F

F

S

V

T

Q

S

G

I

Y

E

G

Q

F

L

F

T

L

L

C

R

R

F

L

I

L

T

S

G

G

V

F

G

G

L

I

G

G

A

G

A

A

M

I

P

P

N

T

A

V

V

F

T

S

M

Y

M

F

G

A

E

E

Y

V

C

L

P

A

D

R

R

E

R

K

R

R

A

G

T

E

V

H

I

L

N

S

L

W

M

L

F

C

C

M

G

F

F

W

P

M

L

I

G

G

A

G

A

I

F

Y

G

A

G

S

F

A

L

M

A

A

A

W

W

A

M

I

I

I

P

P

H

H

F

Y

G

G

W

W

R

S

-

F

-

S

-

M

-

G

-

S

-

A

-

Y

-

Q

-

F

-

H

-

S

-

W

S

R

V

V

L

F

L

V

L

I

G

V

G

C

I

A

T

L

P

P

L

C

L

V

L

S

I

V

V

V

L

A

A

L

I

T

K

F

M

M

P

P

E

E

S

S

V

P

R

R

Y

F

M

L

V

L

A

E

N

V

N

G

K

K

P

H

V

D

E

E

Sites not aligning to the query:

1:57 Interaction with SYT1
529:566 (Microbial infection) C.botulinum neurotoxin type A-binding
559 N→A: Loss of one glycosylation site. No effect on C.botulinum neurotoxin type A (BoNT/A, botA) binding, but reduces the uptake of BoNT/A.

Q496J9 Synaptic vesicle glycoprotein 2C from Homo sapiens (Human) (see 4 papers)
24% identity, 46% coverage: 6:214/452 of query aligns to 135:355/727 of Q496J9

query
sites
Q496J9

A

A

V

Q

N

Q

V

Y

Q

E

T

L

F

I

I

I

N

Q

E

E

H

C

P

G

F

H

S

G

P

R

F

F

Q

Q

W

W

L

A

V

L

F

F

M

V

C

L

F

G

I

M

I

A

V

L

L

M

L

A

D

D

G

G

F

V

D

E

T

V

A

F

A

V

I

V

G

G

F

F

I

V

A

L

P

P

S

S

L

A

I

E

A

T

E

D

W

L

G

C

I

I

T

P

R

N

P

S

A

G

L

S

A

G

P

W

V

L

L

G

S

S

A

I

A

V

L

Y

F

L

G

G

L

M

A

M

C

V

G

G

A

A

L

F

G

F

S

W

G

G

P

G

L

L

S

A

D

D

R

K

L

V

G

G

R

R

R

K

S

Q

L

S

L

L

G

I

S

C

V

M

L

S

L

V

F

N

G

G

V

F

A

F

C

A

L

F

G

L

S

S

A

S

F

F

S

V

T

Q

S

G

I

Y

E

G

Q

F

L

F

T

L

T

F

L

C

R

R

F

L

I

L

T

S

G

G

V

F

G

G

L

I

G

G

A

G

A

A

M

I

P

P

N

T

A

V

V

F

T

S

M

Y

M

F

G

A

E

E

Y

V

C

L

P

A

D

R

R

E

R

K

R

R

A

G

T

E

V

H

I

L

N

S

L

W

M

L

F

C

C

M

G

F

F

W

P

M

L

I

G

G

A

G

A

I

F

Y

G

A

G

S

F

A

L

M

A

A

A

W

W

A

M

I

I

I

P

P

H

H

F

Y

G

G

W

W

R

S

-

F

-

S

-

M

-

G

-

S

-

A

-

Y

-

Q

-

F

-

H

-

S

-

W

S

R

V

V

L

F

L

V

L

I

G

V

G

C

I

A

T

L

P

P

L

C

L

V

L

S

I

V

V

V

L

A

A

L

I

T

K

F

M

M

P

P

E

E

S

S

V

P

R

R

Y

F

M

L

V

L

A

E

N

V

N

G

K

K

P

H

V

D

E

E

Sites not aligning to the query:

519:563 (Microbial infection) C.botulinum neurotoxin type A-binding
534 modified: carbohydrate, N-linked (GlcNAc...) asparagine
559 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: No change in interaction with C.botulinum neurotoxin type A heavy chain (botA, BoNT/A HC). Decreased molecular weight probably due to glycosylation loss, decreased interaction with BoNT/A HC.; N→Q: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC. Greater reduction in weight; when associated with Q-565.
561 S→A: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC.
563 F→A: No longer interacts with BoNT/A HC.
565 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Decreased molecular weight probably due to glycosylation loss, no change in binding to BoNT/A heavy chain. Greater reduction in weight; when associated with Q-559.

O57379 Solute carrier family 22 member 6; Organic anion transporter 1; Renal organic anion transporter 1; ROAT1; fROAT1 from Pseudopleuronectes americanus (Winter flounder) (Pleuronectes americanus) (see paper)
31% identity, 35% coverage: 71:230/452 of query aligns to 156:313/562 of O57379

query
sites
O57379

G

G

L

V

A

L

C

V

G

G

A

A

L

L

G

L

S

F

G

G

P

G

L

L

S

S

D

D

R

R

L

Y

G

G

R

R

S

I

L

L

G

I

S

S

V

N

L

L

F

M

G

A

V

V

A

S

C

G

L

T

G

C

S

A

A

A

F

F

S

S

T

S

S

S

I

F

E

S

Q

L

L

F

T

C

T

V

L

F

R

R

F

F

I

G

T

C

G

G

V

L

G

A

L

L

G

S

A

G

A

L

M

G

P

L

N

N

A

T

V

F

T

S

M

L

M

I

G

V

E

E

Y

W

C

I

P

P

D

T

R

R

R

I

R

R

A

T

T

A

V

V

I

G

N

T

L

T

M

T

F

G

C

Y

G

C

F

Y

P

T

L

L

G

G

A

Q

A

L

F

I

G

-

G

L

F

V

L

L

A

L

A

A

W

Y

M

F

I

I

P

R

H

D

F

W

G

R

W

W

R

-

S

-

V

-

L

L

L

T

L

L

G

A

G

V

I

S

T

L

P

P

L

F

L

Y

L

V

L

F

I

F

V

L

L

I

A

A

I

W

K

W

M

F

P

H

E

E

S

S

V

S

R

R

Y

W

M

L

V

A

A

L

N

S

N

N

K

R

P

T

V

E

E

H

R

A

I

L

R

K

-

N

-

L

A

K

A

S

L

V

A

A

R

R

I

F

S

N

S

G

E

R

A

H

A

E

Q

E

A

A

Sites not aligning to the query:

34 H→I: Reduced transport activity.
394 K→A: Reduced transport activity.
478 R→D: Reduced transport activity.

Q497L9 Solute carrier family 22 member 14 from Mus musculus (Mouse) (see paper)
24% identity, 78% coverage: 35:388/452 of query aligns to 148:509/629 of Q497L9

query
sites
Q497L9

L

L

D

N

G

Y

F

T

D

E

T

T

A

C

A

K

I

F

G

G

F

W

I

I

A

Y

P

P

-

F

-

A

-

H

-

T

-

R

S

S

L

L

I

I

A

N

E

E

W

F

G

D

I

L

-

V

-

C

-

G

T

N

R

E

P

P

A

N

L

K

A

E

P

N

V

G

L

L

S

T

A

V

A

F

L

L

F

S

G

G

L

V

A

L

C

T

G

G

A

S

L

L

G

L

S

F

G

G

P

F

L

L

S

S

D

D

R

K

L

L

G

G

R

R

R

Y

S

P

L

I

L

L

G

L

S

S

V

L

L

L

L

G

F

F

G

L

V

I

A

F

C

G

L

F

G

G

S

T

A

A

F

F

S

V

T

S

S

S

I

F

E

Y

Q

Q

L

Y

T

L

T

F

L

F

R

R

-

F

F

F

I

V

T

A

G

Q

V

A

G

S

L

V

G

G

A

Y

A

A

M

I

P

-

N

C

A

S

V

V

T

S

M

L

M

V

G

M

E

E

Y

W

C

L

P

V

D

G

R

E

R

H

R

R

A

A

T

Q

V

A

I

V

N

I

L

L

M

Q

F
x
H

C

S

G

F

F

L

P

T

L

I

G

G

A

V

A

I

F

L

G

L

G

T

F

G

L

L

A

-

A

A

W

Y

M

K

I

V

P

V

H

H

F

-

G

-

W

W

R

R

S

L

V

L

L

C

L

L

G

G

I

M

T

-

P

P

L

M

L

F

L

P

L

L

I

I

V

C

L

N

A

I

I

W

K

V

M

L

P

R

E

E

S

S

V

P

R

R

Y

W

M

L

V

M

A

V

N

R

N

G

K

K

P

-

V

V

E

E

R

E

I

A

R

K

A

K

A

V

L

L

A

C

R

-

I

Y

S

A

E

E

A

V

A

N

Q

K

A

K

G

T

S

I

F

P

V

L

M

N

T

L

E

L

T

N

A

E

P

L

Q

Q

T

I

G

S

G

G

K

K

G

K

M

V

A

A

V

K

V

A

L

S

S

I

R

L

S

D

Y

F

I

C

I

T

G

N

S

Q

V

H

M

L

L

F

W

K

I

V

A

V

Y

L

F

A

M

I

G

G

L

C

V

V

I

W

F

F

Y

T

A

V

S
|
S

I
x
Y

N
x
I

W
x
S

M

F

P

T

I

L

L

N

L

L

K

K

-

M

-

N

D

D

A

F

G

G

L

L

T

D

P

V

Q

Y

R

F

A

V

T

Q

L

M

I

V

S

R

A

S

L

I

F

V

P

-

L

-

G

-

G

A

V

V

G

P

A

A

V

R

L

L

C

C

G

C

V

I

L

I

M

L

D

L

R

E

F

Y

N

F

A

G

N

R

R

K

-

W

-

A

I

L

I

N

A

L

A

T

C

L

Y

F

A

L

L

V

T

T

A

S

V

M

S

C

V

L

Y

F

F

L

I

L

G

F

Q

L

A

P

V

Q

G

E

N

P

V

K

G

S

A

T

L

I

V

I

F

L

I

T

V

L

F

M

V

L

A

A

G

E

V

F

L

S

M

M

N

A

T

G

A

T

Q

L

S

S

S

I

M

F

P

F

A

I

L

Y

A

T

A

A

A

E

F

L

Y

L

P

P

T

T

E

V

G

L

R

R

G

S

T

T

G

G

-

L

-

G

-

M

-

V

-

S

V

L

A

A

W

W

M

V

L

A

G

G

H275 (≠ F154) mutation to A: Strongly reduced riboflavin transport; when associated with 391-A--A-394.
SYIS 391:394 (≠ SINW 276:279) mutation to AYIA: Strongly reduced riboflavin transport; when associated with A-275.

4zp0A Crystal structure of e. Coli multidrug transporter mdfa in complex with deoxycholate (see paper)
51% identity, 10% coverage: 80:126/452 of query aligns to 65:111/392 of 4zp0A

query
sites
4zp0A

G

G

P

P

L

L

S

S

D

D

R

R

L

I

G

G

R

R

S

P

L

V

L

M

L

L

G

A

S

G

V

V

L

V

L

W

F

F

G

I

V

V

A

T

C

C

L

L

G

A

S

I

A

L

F

L

S

A

T

Q

S

N

I

I

E

E

Q

Q

L

F

T

T

T

L

L

L

R

R

F

F

I

L

T

Q

G

G

V

I

G

S

L

L

Sites not aligning to the query:

binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: 26, 54, 146, 228, 350

4zowA Crystal structure of e. Coli multidrug transporter mdfa in complex with chloramphenicol (see paper)
51% identity, 10% coverage: 80:126/452 of query aligns to 64:110/391 of 4zowA

query
sites
4zowA

G

G

P

P

L

L

S

S

D

D

R

R

L

I

G

G

R

R

S

P

L

V

L

M

L

L

G

A

S

G

V

V

L

V

L

W

F

F

G

I

V

V

A

T

C

C

L

L

G

A

S

I

A

L

F

L

S

A

T

Q

S

N

I

I

E

E

Q

Q

L

F

T

T

T

L

L

L

R

R

F

F

I

L

T

Q

G

G

V

I

G

S

L
|
L

binding chloramphenicol: L110 (= L126)

Sites not aligning to the query:

binding chloramphenicol: 21, 24, 25, 141

6oopA Protein b (see paper)
51% identity, 10% coverage: 80:126/452 of query aligns to 65:111/392 of 6oopA

query
sites
6oopA

G

G

P

P

L

L

S

S

D

D

R

R

L

I

G

G

R

R

S

P

L

V

L

M

L

L

G

A

S

G

V

V

L

V

L

W

F

F

G

I

V

V

A

T

C

C

L

L

G

A

S

I

A

L

F

L

S

A

T

Q

S

N

I

I

E

E

Q

Q

L

F

T

T

T

L

L

L

R

R

F

F

I

L

T

Q

G

G

V

I

G

S

L

L

Sites not aligning to the query:

binding 1,1'-dimethyl-4,4'-bipyridin-1-ium: 22, 224

P0AEY8 Multidrug transporter MdfA; Chloramphenicol resistance pump Cmr from Escherichia coli (strain K12) (see paper)
51% identity, 10% coverage: 80:126/452 of query aligns to 73:119/410 of P0AEY8

query
sites
P0AEY8

G

G

P

P

L

L

S

S

D

D

R

R

L

I

G

G

R

R

S

P

L

V

L

M

L

L

G

A

S

G

V

V

L

V

L

W

F

F

G

I

V

V

A

T

C

C

L

L

G

A

S

I

A

L

F

L

S

A

T

Q

S

N

I

I

E

E

Q

Q

L

F

T

T

T

L

L

L

R

R

F

F

I

L

T

Q

G

G

V

I

G

S

L

L

Sites not aligning to the query:

26 E→A: Loss of ethidium bromide efflux activity.; E→D: No change in ethidium bromide efflux activity.; E→H: Almost no chloramphenicol efflux activity. Loss of ethidium bromide efflux activity.; mutation E->I,V: Slight decrease in chloramphenicol efflux activity. Exhibits low ethidium bromide efflux activity.; E→K: Decrease in TPP efflux activity. Exhibits low ethidium bromide efflux activity.; mutation E->L,N: Strong decrease in chloramphenicol efflux activity. Loss of ethidium bromide and TPP efflux activities.; E→Q: Slight decrease in chloramphenicol efflux activity. Loss of ethidium bromide efflux activity.; E→T: Strong decrease in chloramphenicol efflux activity. Loss of ethidium bromide efflux activity.

6zguA Crystal structure of a mfs transporter with bound 3-(2-methylphenyl) propanoic acid at 2.41 angstroem resolution
27% identity, 79% coverage: 45:400/452 of query aligns to 28:356/404 of 6zguA

query
sites
6zguA

F

F

I

I

A

K

P

P

S

-

L

L

I

N

A

A

E

E

W

F

G

G

I

W

T

S

R

R

P

A

-

E

-

I

A

A

L

M

A

A

P

F

V

A

L

I

S

C

A

C

A

L

L

I

F
|
F

G

G

L

L

A

M

C

-

G

-

A

T

L

F

G

P

S

A

G

G

P

R

L

L

S

S

D

D

R

K

L

M

G

G

-

P

R

R

R

K

S

V

L

V

L

M

L

T

G

G

S

G

V

V

L

L

F

-

G

A

V

I

A

G

C

F

L

I

G

L

S

S

A

G

F

F

S

I

T

Q

S

S

I

K

E

Y

Q

Q

L

L

-

Y

T

I

T

T

L

Y

R

G

F

V

I

I

T

A

G

G

V

F

G

G

L

G

G

G

A

M

A

I

M
x
Y

P

L

N

P

A

P

V

I

T

A

M

T

M

A

G

P

E

K

Y

W

C

W

P

P

D

D

R

-

R

R

A

A

T

L

V

A

I

T

N

G

L

F

M

A

F

V

C

V

G

G

F
x
L

P

G

L

L

G

G

A

S

A

F

F

L

G

M

G

G

F

P

L

L

A

A

A

T

W

Y

M

I

I

I

-

E

-

K

P

P

H

G

F

M

G

G

W

W

R

R

S

Y

V

V

L

F

L

W

L

Y

G

C

G

G

I

V

T

A

-

M

P

G

L

I

L

M

L

A

L

L

I

I

V

A

L

G

A

A

I

F

K

L

M

E

P

P

E

P

S

P

V

A

R

G

Y

W

M

K

V

P

A

A

N

G

N

Y

K

T

P

P

V

-

E

-

R

-

I

-

R

-

A

-

L

-

A

-

R

K

I

V

S

T

S

R

E

D

A

-

Q

-

A

-

G

-

S

-

F

-

V

-

M

-

T

-

E

W

T

T

A

Y

P

E

Q

E

T

A

G

K

G

G

K

D

G

T

M

K

A

F

V

W

V

L

L

L

S

Y

R

L

S

A

Y

Y

I

F

I

C

G

G

S

S

V

-

M

-

L

-

W

-

I

-

A

-

Y

-

F

F

M

A

G

G

L

L

V

M

I

V

F

-

Y

-

A

-

S

-

I

I

N

G

W

H

M

L

P

A

I

G

L

F

L

G

K

R

D

D

A

A

G

G

L

L

T

T

P

A

Q

M

R

A

A

A

T

A

-

G

L

A

I

V

S

S

A

S

L

L

F

A

P

F

L

S

G

N

G

A

V

A

G

T

A
x
R

V

I

L

L

C

S

G

G

V

W

L

F

M

V

D

D

R

K

F

I

N

G

A

I

N

R

R

V

I

Y

I

F

A

A

C

L

Y

F

A

A

L

L

T

Q

A

T

V

A

S

A

V

M

Y

I

F

A

I

I

G

F

Q

Q

A

L

V

G

G

G

N

S

V

V

G

V

A

G

L

L

V

S

F

I

I

V

V

A

F

I

V

V

A

I

G

G

V

W

L

N

M

Y

N

G

T

A

A

M

Q
x
F

S

T

S

L

M

F

P

P

A

A

L

T

A

C

A

L

A

Q

F

F

Y

Y

P

G

T

P

E

T

G

A

R

Q

G

G

T

S

G

N

V

Y

A

G

W

L

M

L

L

F

G

T

I

A

G
x
C

R

G

F

L

G

A

G

G

I

F

A

A

G

G

S

P

F

W

L

V

binding 3-(2-methylphenyl)propanoic acid: F54 (= F70), Y113 (≠ M130), L139 (≠ F157), R264 (≠ A308), F319 (≠ Q363), C346 (≠ G390)

6zgtA Crystal structure of a mfs transporter with bound 2-naphthoic acid at 2.39 angstroem resolution
27% identity, 79% coverage: 45:400/452 of query aligns to 28:356/404 of 6zgtA

query
sites
6zgtA

F

F

I

I

A

K

P

P

S

-

L

L

I

N

A

A

E

E

W

F

G

G

I

W

T

S

R

R

P

A

-

E

-

I

A

A

L

M

A

A

P

F

V

A

L

I

S

C

A
x
C

A

L

L

I

F
|
F

G

G

L

L

A

M

C

-

G

-

A

T

L

F

G

P

S

A

G

G

P

R

L

L

S

S

D

D

R

K

L

M

G

G

-

P

R

R

R

K

S

V

L

V

L

M

L

T

G

G

S

G

V

V

L

L

F

-

G

A

V

I

A

G

C

F

L

I

G

L

S

S

A

G

F

F

S

I

T

Q

S

S

I

K

E

Y

Q

Q

L

L

-

Y

T

I

T

T

L

Y

R

G

F

V

I

I

T

A

G

G

V

F

G

G

L

G

G

G

A

M

A

I

M
x
Y

P

L

N

P

A

P

V

I

T

A

M

T

M

A

G

P

E

K

Y

W

C

W

P

P

D

D

R

-

R

R

A

A

T

L

V

A

I

T

N

G

L

F

M

A

F

V

C

V

G

G

F
x
L

P

G

L

L

G

G

A

S

A

F

F

L

G

M

G

G

F

P

L

L

A

A

A

T

W

Y

M

I

I

I

-

E

-

K

P

P

H

G

F

M

G

G

W

W

R

R

S

Y

V

V

L

F

L

W

L

Y

G

C

G

G

I

V

T

A

-

M

P

G

L

I

L

M

L

A

L

L

I

I

V

A

L

G

A

A

I

F

K

L

M

E

P

P

E

P

S

P

V

A

R

G

Y

W

M

K

V

P

A

A

N

G

N

Y

K

T

P

P

V

-

E

-

R

-

I

-

R

-

A

-

L

-

A

-

R

K

I

V

S

T

S

R

E

D

A

-

Q

-

A

-

G

-

S

-

F

-

V

-

M

-

T

-

E

W

T

T

A

Y

P

E

Q

E

T

A

G

K

G

G

K

D

G

T

M

K

A

F

V

W

V

L

L

L

S

Y

R

L

S

A

Y

Y

I

F

I

C

G

G

S

S

V

-

M

-

L

-

W

-

I

-

A

-

Y

-

F

F

M

A

G

G

L

L

V

M

I

V

F

-

Y

-

A

-

S

-

I

I

N

G

W

H

M

L

P

A

I

G

L

F

L

G

K

R

D

D

A

A

G

G

L

L

T

T

P

A

Q

M

R

A

A

A

T

A

-

G

L

A

I

V

S

S

A

S

L

L

F

A

P

F

L

S

G

N

G

A

V

A

G

T

A
x
R

V

I

L

L

C

S

G

G

V

W

L

F

M

V

D

D

R

K

F

I

N

G

A

I

N

R

R

V

I

Y

I

F

A

A

C

L

Y

F

A

A

L

L

T

Q

A

T

V

A

S

A

V

M

Y

I

F

A

I

I

G

F

Q

Q

A

L

V

G

G

G

N

S

V

V

G

V

A

G

L

L

V

S

F

I

I

V

V

A

F

I

V

V

A

I

G

G

V

W

L

N

M

Y

N

G

T

A

A

M

Q
x
F

S

T

S

L

M

F

P

P

A

A

L

T

A

C

A

L

A

Q

F

F

Y

Y

P

G

T

P

E

T

G

A

R

Q

G

G

T

S

G

N

V

Y

A

G

W

L

M

L

L
x
F

G

T

I

A

G
x
C

R

G

F

L

G

A

G

G

I

F

A

A

G

G

S

P

F

W

L

V

binding naphthalene-2-carboxylic acid: C51 (≠ A67), F54 (= F70), Y113 (≠ M130), L139 (≠ F157), R264 (≠ A308), F319 (≠ Q363), F343 (≠ L387), C346 (≠ G390)

6zgsA Crystal structure of a mfs transporter with bound 3-phenylpropanoic acid at 2.39 angstroem resolution
27% identity, 79% coverage: 45:400/452 of query aligns to 28:356/404 of 6zgsA

query
sites
6zgsA

F

F

I

I

A

K

P

P

S

-

L

L

I

N

A

A

E

E

W

F

G

G

I

W

T

S

R

R

P

A

-

E

-

I

A

A

L

M

A

A

P

F

V

A

L

I

S

C

A

C

A

L

L

I

F
|
F

G

G

L

L

A

M

C

-

G

-

A

T

L

F

G

P

S

A

G

G

P

R

L

L

S

S

D

D

R

K

L

M

G

G

-

P

R

R

R

K

S

V

L

V

L

M

L

T

G

G

S

G

V

V

L

L

F

-

G

A

V

I

A

G

C

F

L

I

G

L

S

S

A

G

F

F

S

I

T

Q

S

S

I

K

E

Y

Q

Q

L

L

-

Y

T

I

T

T

L

Y

R

G

F

V

I

I

T

A

G

G

V

F

G

G

L

G

G

G

A

M

A

I

M
x
Y

P

L

N

P

A

P

V

I

T

A

M

T

M

A

G

P

E

K

Y

W

C

W

P

P

D

D

R

-

R

R

A

A

T

L

V

A

I

T

N

G

L

F

M

A

F

V

C

V

G

G

F
x
L

P

G

L

L

G

G

A

S

A

F

F

L

G

M

G

G

F

P

L

L

A

A

A

T

W

Y

M

I

I

I

-

E

-

K

P

P

H

G

F

M

G

G

W

W

R

R

S

Y

V

V

L

F

L

W

L

Y

G

C

G

G

I

V

T

A

-

M

P

G

L

I

L

M

L

A

L

L

I

I

V

A

L

G

A

A

I

F

K

L

M

E

P

P

E

P

S

P

V

A

R

G

Y

W

M

K

V

P

A

A

N

G

N

Y

K

T

P

P

V

-

E

-

R

-

I

-

R

-

A

-

L

-

A

-

R

K

I

V

S

T

S

R

E

D

A

-

Q

-

A

-

G

-

S

-

F

-

V

-

M

-

T

-

E

W

T

T

A

Y

P

E

Q

E

T

A

G

K

G

G

K

D

G

T

M

K

A

F

V

W

V

L

L

L

S

Y

R

L

S

A

Y

Y

I

F

I

C

G

G

S

S

V

-

M

-

L

-

W

-

I

-

A

-

Y

-

F

F

M

A

G

G

L

L

V

M

I

V

F

-

Y

-

A

-

S

-

I

I

N

G

W

H

M

L

P

A

I

G

L

F

L

G

K

R

D

D

A

A

G

G

L

L

T

T

P

A

Q

M

R

A

A

A

T

A

-

G

L

A

I

V

S

S

A

S

L

L

F

A

P

F

L

S

G

N

G

A

V

A

G

T

A
x
R

V

I

L

L

C

S

G

G

V

W

L

F

M

V

D

D

R

K

F

I

N

G

A

I

N

R

R

V

I

Y

I

F

A

A

C

L

Y

F

A

A

L

L

T

Q

A

T

V

A

S

A

V

M

Y

I

F

A

I

I

G

F

Q

Q

A

L

V

G

G

G

N

S

V

V

G

V

A

G

L

L

V

S

F

I

I

V

V

A

F

I

V

V

A

I

G

G

V

W

L

N

M

Y

N

G

T

A

A

M

Q
x
F

S

T

S

L

M

F

P

P

A

A

L

T

A

C

A

L

A

Q

F

F

Y

Y

P

G

T

P

E

T

G

A

R

Q

G

G

T

S

G

N

V

Y

A

G

W

L

M

L

L

F

G

T

I

A

G
x
C

R

G

F

L

G

A

G

G

I

F

A

A

G

G

S

P

F

W

L

V

binding hydrocinnamic acid: F54 (= F70), Y113 (≠ M130), L139 (≠ F157), R264 (≠ A308), F319 (≠ Q363), C346 (≠ G390)

Query Sequence

>BPHYT_RS30250 FitnessBrowser__BFirm:BPHYT_RS30250
MNRSTAVNVQTFINEHPFSPFQWLVFFMCFIIVLLDGFDTAAIGFIAPSLIAEWGITRPA
LAPVLSAALFGLACGALGSGPLSDRLGRRSLLLGSVLLFGVACLGSAFSTSIEQLTTLRF
ITGVGLGAAMPNAVTMMGEYCPDRRRATVINLMFCGFPLGAAFGGFLAAWMIPHFGWRSV
LLLGGITPLLLLIVLAIKMPESVRYMVANNKPVERIRAALARISSEAAQAGSFVMTETAP
QTGGKGMAVVLSRSYIIGSVMLWIAYFMGLVIFYASINWMPILLKDAGLTPQRATLISAL
FPLGGVGAVLCGVLMDRFNANRIIAACYALTAVSVYFIGQAVGNVGALVFIVFVAGVLMN
TAQSSMPALAAAFYPTEGRGTGVAWMLGIGRFGGIAGSFLVAELTRRHFSFAGIFAMVAV
AGLLACLALLIKQAARPHVANVGAPKAESFGH

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