SitesBLAST

C145 (= C106) mutation to S: No significant effect on transport activity; when associated with S-237, S-241, S-245, S-263, S-335, S-399, S-434, S-455, S-474, S-510 and S-519.
F160 (≠ I121) mutation to C: Reduces phosphate binding, transport and signaling activities.
R168 (= R131) mutation to A: Reduces transport activity. No significant effects on affinity for inorganic phosphate. No significant effects on growth rates.; mutation to C: Abolishes transport and signaling activities.; mutation to E: Reduces transport activity. Moderately reduces affinity for inorganic phosphate. No significant effects on growth rates.; mutation to Q: Reduces transport activity. Moderately reduces affinity for inorganic phosphate. Moderately reduces growth rates under low phosphate conditions. No significant effects on growth rates under high phosphate conditions.
G172 (= G135) mutation to C: Abolishes transport and signaling activities.
G174 (≠ A137) mutation to C: Abolishes transport and signaling activities.
G176 (= G139) mutation to C: Abolishes transport and signaling activities.
D178 (≠ E141) mutation D->E,N: Reduces transport activity. No significant effects on affinity for inorganic phosphate. No significant effects on signaling activities. No significant effects on growth rates.
Y179 (= Y142) mutation to A: Significantly reduces transport activity. Causes pronounced increase in secreted phosphatase activity under high phosphate conditions. Reduces growth rates under low phosphate conditions. Slightly reduces signaling activity.; mutation to G: Abolishes transport activity. Causes pronounced increase in secreted phosphatase activity under high phosphate conditions. Reduces growth rates under low phosphate conditions. Abolishes signaling activity.; mutation Y->S,F: No significant effects on transport activity. No significant effects on growth rates under low phosphate conditions. Does not affect patterns of secreted phosphatase activities under low and high phosphate conditions. No significant effects on signaling activity.
C237 (vs. gap) mutation to S: No significant effect on transport activity; when associated with S-145, S-241, S-245, S-263, S-335, S-399, S-434, S-455, S-474, S-510 and S-519.
C241 (≠ T189) mutation to S: No significant effect on transport activity; when associated with S-145, S-237, S-245, S-263, S-335, S-399, S-434, S-455, S-474, S-510 and S-519.
C245 (≠ S193) mutation to S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-263, S-335, S-399, S-434, S-455, S-474, S-510 and S-519.
C263 (≠ V211) mutation to S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-335, S-399, S-434, S-455, S-474, S-510 and S-519.
K298 (= K236) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); mutation to A: No significant effect on membrane localization under low phosphate conditions and internalization after phosphate addition. Strongly affects vacuolar sorting of the protein after internalization.

Sites not aligning to the query:

6 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
304:327 mutation Missing: Increases transport activity. Has no significant effect on membrane localization under low phosphate conditions. Results in severely delayed internalization after phosphate addition.
335 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-399, S-434, S-455, S-474, S-510 and S-519.
358 D→E: Abolishes transport activity. Causes pronounced increase in secreted phosphatase activity under high phosphate conditions. Moderately decreases signaling activities. Significantly reduces growth rates under low phosphate conditions. No significant effects on growth rates under high phosphate conditions.; D→N: Significantly reduces transport activity. No significant effects on affinity for inorganic phosphate. Causes pronounced increase in secreted phosphatase activity under high phosphate conditions. No significant effects on signaling activities. Significantly reduces growth rates under low phosphate conditions. No significant effects on growth rates under high phosphate conditions.
392 V→C: Reduces transport and signaling activities.
399 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-434, S-455, S-474, S-510 and S-519.
408 V→C: Reduces signaling activity and enhances transport activity.
434 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-399, S-455, S-474, S-510 and S-519.
455 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-399, S-434, S-474, S-510 and S-519.
473 E→K: No significant effects on transport activity. No significant effects on affinity for inorganic phosphate. No significant effects on growth rates.; E→Q: No significant effects on transport activity. Reduces affinity for inorganic phosphate. No significant effects on growth rates.
474 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-399, S-434, S-455, S-510 and S-519.
492 mutation K->A,Q: No significant effects on transport activity. Reduces affinity for inorganic phosphate. No significant effects on growth rates.; K→E: Reduces transport activity. Reduces affinity for inorganic phosphate. Significantly reduces growth rates under low phosphate conditions. No significant effects on growth rates under high phosphate conditions.
510 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-399, S-434, S-455, S-474 and S-519.
519 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-399, S-434, S-455, S-474 and S-510.

Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
27% identity, 55% coverage: 37:280/445 of query aligns to 56:282/444 of Q8NLB7

query
sites
Q8NLB7

Y

Y

D
|
D

V

L

Y

I

V

V

Y

Y

S

G

V

T

F

V

A

Q

K

S

Y

A

F

L

E

A

S

K

Q

E

F

W

F

-

S

-

A

-

D

-

K

N

N

L

S

S

T

S

M

A

Y

T

I

L

W

G

G

T

I

I

F

G

A

S

A

T

T

A

F

F

L

F

M

G

R

M

P

A

I

I

G

G

A

A

W

V

Y

F

F

I

G

G

R

R

F

L

A

S

D

D

R
|
R

Y

V

G

G

R

R

R

K

L

A

A

A

L

V

T

I

V

G

S

S

V

V

S

L

V

I

M

L

A

S

A

V

C

F

S

T

F

M

L

L

I

C

A

A

I

F

A

A

P

P

T

N

A

P

A

W

S

V

I

F

G

G

I

A

W

F

A

-

V

-

I

-

L

-

F

-

A

-

R

R

L

F

L

I

Q

A

G

G

F

L

A

G

T

L

G

G

E

L

Y

V

G

-

A

P

S

S

A

V

T

N

Y

A

M

M

S

T

E

S

A

D

A

L

V

V

P

P

G

-

W

-

R

R

G

K

F

T

L

M

S

S

S

A

F

W

H

A

Y

T

V

V

T

M

L

M

-

S

-

G

-

V

-

P

V

I

G

G

H

S

V

I

L

A

A

A

Q

V

A

L

V

A

L

L

L

V

V

V

M

V

L

P

L

S

S

S

W

-

D

-

T

-

S

-

H

-

V

-

S

E

E

E

W

W

G

G

W

W

R

R

V

F

A

M

F

F

G

L

I

I

G

A

G

L

I

I

G

P

A

-

L

-

V

L

V

V

F

V

W

G

L

L

R

P

R

I

T

A

M

M

D

K

E

V

S

I

L

P

S

S

A

D

E

K

S

A

I

I

E

K

A

A

A

D

K

H

D

D

-

I

-

R

-

E

G

G

K

H

A

D

K

E

A

P

S

A

G

G

S

-

M

F

R

K

E

D

L

L

F

L

V

V

N

D

Q

R

W

Y

R

R

P

W

L

I

L

S

L

I

C

W

F

F

-

A

L

L

I

A

T

T

A

F

G

V

G

T

T

L

V

L

A

A

F

W

Y

Y

T

G

Y

L

T

G

I

T

N

W

G

L

P

P

K

R

M

L

I

M

Q

E

T

T

A

A

D57 (= D38) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
R103 (= R89) mutation to A: Loss of transport activity.

Sites not aligning to the query:

54 D→A: Loss of transport activity.; D→E: Retains 50% of its transport activity.
309 W→V: Loss of transport activity.
312 D→A: Loss of transport activity.
313 R→A: Loss of transport activity.
317 mutation I->H,Y: Loss of transport activity.
386 R→A: Loss of transport activity.

Q9Y7Q9 Probable metabolite transporter C2H8.02 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 39% coverage: 70:241/445 of query aligns to 90:265/583 of Q9Y7Q9

query
sites
Q9Y7Q9

A

A

T

T

F

N

L

I

M

G

R

N

P

I

I

M

G

G

A

Q

W

L

Y

L

F

F

G

G

R

F

F

L

A

G

D

D

R

F

Y

F

G

G

R

R

R

K

L

F

A

V

L

Y

T

G

V

K

S

E

V

M

S

M

V

V

M

V

A

I

C

A

S

T

F

I

L

L

I

I

A

I

I

C

A

L

P

P

T

D

A

R

A

I

S

P

I

T

G

P

I

T

W

-

A

A

A

K

V

M

I

M

L

W

L

L

F

F

A

A

-

F

R

R

L

V

L

M

Q

L

G

G

F

I

A

G

T

I

G

G

E

D

Y

Y

G

P

A

M

S

S

A

A

T

S

Y

I

M

T

S

S

E

E

A

Q

A

S

V

L

P

I

G

N

W

R

R

R

G

G

F

A

L

L

S

L

S

A

F

W

H

I

Y

F

V

S

T

N

L

Q

V

-

G

G

G

W

H

G

V

T

L

L

A

A

Q

G

A

C

V

V

L

A

L

T

V

L

M

I

L

I

L

L

S

A

W

C

D

F

T

E

S

K

H

P

V

L

S

N

E

D

W

R

G

G

-

E

-

Y

-

T

-

K

-

L

-

N

-

G

-

V

W

W

R

R

V

I

A

Q

F

F

G

G

I

I

G

A

G

L

I

F

G

P

A

A

L

V

V

I

V

V

F

L

W

I

L

P

R

R

R

L

T

R

M

M

D

Q

E

E

S

S

L

-

S

-

A

-

E

E

S

Q

I

F

E

K

A

N

A

S

K

K

D

N

G

M

K

K

A

S

K

P

A

G

S

E

G

G

S

D

M

L

Sites not aligning to the query:

267 modified: Phosphoserine
269 modified: Phosphoserine
289 modified: Phosphoserine
290 modified: Phosphoserine
292 modified: Phosphoserine
330 modified: Phosphoserine

6m2lA Crystal structure of plasmodium falciparum hexose transporter pfht1 bound with c3361 (see paper)
25% identity, 72% coverage: 60:378/445 of query aligns to 41:378/447 of 6m2lA

query
sites
6m2lA

N

N

S

N

T

T

M

I

Y

Q

I

S

W

S

G

F

I

L

F

L

A

A

A

S

T

V

F
|
F

L

I

M

G

R

A

P

V

I

L

G

G

A

C

W

G

Y

F

F

S

G

G

R

Y

F

L

A

V

D

-

R

Q

Y

F

G

G

R

R

L

L

A

S

L

L

T

L

V

I

S

I

V

Y

S

N

V

F

M

F

A

F

A

L

C

V

S

S

F

I

L

L

I

T

A

S

I

I

A

T

P

H

T

H

A

F

A

H

S

T

I

I

G

-

I

-

W

-

A

-

V

-

I

-

L

-

L

L

F

F

A

A

R

R

L

L

Q

S

G

G

F

F

A

G

T

I

G

G

G

L

E

V

Y

T

G

V

A

S

S

V

A

P

T

M

Y

Y

M

I

S

S

E

E

A

M

A

T

V

H

P

K

G

D

W

K

R

K

G

G

F

A

L

Y

S

G

S

V

F

M

H

H

Y
x
Q

V

L

T

F

L

I

V

T

G

F

G

G

H

I

V

F

L

V

A

A

Q

-

A

-

V

-

L

-

V

V

M

M

L

L

L

-

S

-

W

-

D

G

T

L

S

S

H

F

V

A

S

K

E

L

W

W

G

-

W

W

R

R

V

L

A

M

F

F

-

L

-

F

-

P

-

S

-

V

-

I

G

S

I

L

G

I

G

G

I

I

G

L

A

A

L

L

V

V

F

F

W

F

L

K

R

E

T

T

-

P

-

Y

-

F

-

L

-

F

-

E

-

K

-

G

-

R

-

I

-

E

-

S

-

K

-

N

-

I

-

L

-

K

-

I

-

Y

-

E

-

T

-

D

-

N

M

V

D

D

E

E

S

P

L

L

S

N

A

A

-

I

-

K

E

E

S

A

I

V

E

E

A

Q

A

N

K

E

D

S

G

A

K

K

A

K

K

N

A

S

S

L

G

S

S

L

M

L

R

S

E

A

L

L

F

K

V

I

N

P

Q

S

W

Y

R

R

P

Y

L

V

L

I

-

L

-

G

C

C

F

L

L

L

I

-

T

-

A

-

G

S

G

G

T

L

V

Q

A

Q

F

F

-

T

-

G

Y

I

T
x
N

Y

V

T

L

I

V

N
x
S

G

N

P

S

K

N

M

E

I

L

Q

Y

T

K

A

E

F

F

A

L

G

D

D

S

D

H

V

L

I

I

T

T

G

I

T

L

W

S

I

V

N

V

L

M

G

T

V

A

L

V

T

N

F

F

L

L

M

M

L

T

L

F

Q

P

P

A

L

I

G

-

L

Y

L

I

S

V

D

E

R

K

I

L

G

G

R

R

K

K

S

T

L

L

V

L

F

-

F

W

G

G

V

C

G

V

G

G

V

V

L

L

Y

V

T

A

W

-

Y

Y

L

L

V

P

T

T

A

A

L

I

P

A

Q

N

Q

E

T

I

S

N

A

R

L

N

S

S

A

N

F

F

L

V

-

K

-

I

-

L

-

S

I

I

L

V

A

A

T

T

G

F

F

V

V

M

I

I

L

I

T

S

G

F

Y

A

T

V

S

S

I

Y

N

G

A

P

V

V

V

L

-
x
W

-

I

-

Y

K

L

A

H

E

E

L

M

F

F

P

P

A

S

H

E

I

I

R

K

binding (2S,3R,4S,5R,6R)-6-(hydroxymethyl)-4-undec-10-enoxy-oxane-2,3,5-triol: F54 (= F73), Q138 (≠ Y166), N265 (≠ T268), S269 (≠ N272), W366 (vs. gap)

Sites not aligning to the query:

binding (2S,3R,4S,5R,6R)-6-(hydroxymethyl)-4-undec-10-enoxy-oxane-2,3,5-triol: 25

6m20B Crystal structure of plasmodium falciparum hexose transporter pfht1 bound with glucose (see paper)
24% identity, 72% coverage: 57:378/445 of query aligns to 48:403/478 of 6m20B

query
sites
6m20B

D

N

D

C

K

S

N

N

S

N

T

T

M

I

Y

Q

I

S

W

S

G

F

I

L

F

L

A

A

A

S

T

V

F

F

L

I

M

G

R

A

P

V

I

L

G

G

A

C

W

G

Y

F

F

S

G

G

R

Y

F

L

A

V

D

-

R

Q

Y

F

G

G

R

R

L

L

A

S

L

L

T

L

V

I

S

I

V

Y

S

N

V

F

M

F

A

F

A

L

C

V

S

S

F

I

L

L

I

T

A

S

I

I

A

T

P

H

T

H

A

F

A

H

S

T

I

I

G

-

I

-

W

-

A

-

V

-

I

-

L

-

L

L

F

F

A

A

R

R

L

L

Q

S

G

G

F

F

A

G

T

I

G

G

G

L

E

V

Y

T

G

V

A

S

S

V

A

P

T

M

Y

Y

M

I

S

S

E

E

A

M

A

T

V

H

P

K

G

D

W

K

R

K

G

G

F

A

L

Y

S

G

S

V

F

M

H

H

Y
x
Q

V

L

T

F

L

I

V

T

G

F

G

G

H

I

V

F

L

V

A

A

Q

V

A

M

V

L

L

G

L

L

V

A

M

M

-

G

-

E

-

G

-

P

-

K

-

A

-

D

L

S

L

T

S

E

W

P

D

L

T

T

S

S

H

F

V

A

S

K

E

L

W

W

G

-

W

W

R

R

V

L

A

M

F

F

-

L

-

F

-

P

-

S

-

V

-

I

G

S

I

L

G

I

G

G

I

I

G

L

A

A

L

L

V

V

F

F

W

F

L

K

R

E

T

T

-

P

-

Y

-

F

-

L

-

F

-

E

-

K

-

G

-

R

-

I

-

E

-

S

-

K

-

N

-

I

-

L

-

K

-

I

-

Y

-

E

-

T

-

D

-

N

M

V

D

D

E

E

S

P

L

L

S

N

A

A

-

I

-

K

E

E

S

A

I

V

E

E

A

Q

A

N

K

E

D

S

G

A

K

K

A

K

K

N

A

S

S

L

G

S

S

L

M

L

R

S

E

A

L

L

F

K

V

I

N

P

Q

S

W

Y

R

R

P

Y

L

V

L

I

-

L

-

G

C

C

F

L

L

L

I

-

T

-

A

-

G

S

G

G

T

L

V
x
Q

A

Q

F

F

-

T

-

G

Y

I

T
x
N

Y

V

T

L

I

V

N

S

G

N

P

S

K

N

M

E

I

L

Q

Y

T

K

A

E

F

F

A

L

G

D

D

S

D

H

V

L

I

I

T

T

G

I

T

L

W

S

I

V

N

V

L

M

G

T

V

A

L

V

T

N

F

F

L

L

M

M

L

T

L

F

Q

P

P

A

L

I

G

-

L

Y

L

I

S

V

D

E

R

K

I

L

G

G

R

R

K

K

S

T

L

L

V

L

F

-

F

W

G

G

V

C

G

V

G

G

V

V

L

L

Y

V

T

A

W

-

Y

Y

L

L

V

P

T

T

A

A

L

I

P

A

Q

N

Q

E

T

I

S

N

A

R

L

N

S

S

A

N

F

F

L

V

-

K

-

I

-

L

-

S

I

I

L

V

A

A

T

T

G

F

F

V

V

M

I

I

L

I

T

S

G

F

Y

A

T

V

S

S

I

Y

N
x
G

A

P

V

V

V

L

-
x
W

-

I

-

Y

K

L

A

H

E

E

L

M

F

F

P

P

A

S

H

E

I

I

R

K

binding beta-D-glucopyranose: Q148 (≠ Y166), Q284 (≠ V264), N290 (≠ T268), G387 (≠ N365), W391 (vs. gap)

O42885 Putative inorganic phosphate transporter C8E4.01c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
24% identity, 49% coverage: 19:236/445 of query aligns to 42:273/572 of O42885

query
sites
O42885

K

K

R

R

S

E

V

F

S

K

N

L

T

M

L

M

K

L

G

A

S

G

A

V

G

G

N

F

L

F

V

L

E

D

W

S

Y

Y

D

D

V

L

Y

F

V

I

Y

I

S

N

V

L

F

V

A

T

K

P

Y

I

F

F

E

E

S

Y

Q

L

F

Y

F

W

S

G

A

G

D

I

D

E

K

K

N

G

S

P

T

T

-

G

-

K

-

G

M

H

Y

Y

I

P

W

S

G

G

I

I

-

R

-

G

-

L

-

V

F

N

A

A

A

S

T

A

F

N

L

I

M

G

R

N

P

I

I

F

G

G

A

Q

W

L

Y

L

F

F

G

G

R

F

F

M

A

G

D

D

R

F

Y

F

G

G

R

R

R

K

L

F

A

V

L

Y

T

G

V

K

S

E

V

M

S

V

V

I

M

V

A

I

C

A

S

T

F

V

L

L

I

V

A

I

I

A

A

M

P

P

T

K

A

S

A

I

S

H

I

S

G

P

I

L

W

S

A

K

A

M

V

M

I

W

L

V

L

F

F

C

A

W

R

R

L

W

L

L

Q

L

G

G

F

V

A

G

T

I

G

G

E

D

Y

Y

G

P

A

M

S

S

A

A

T

A

Y

I

M

T

S

S

E

E

A

R

A

S

V

K

P

I

G

K

W

R

R

R

G

G

F

T

L

L

S

I

S

S

F

L

H

I

Y

F

V

-

T

A

L

F

V

Q

G

G

G

F

H

G

V

T

L

L

A

A

Q

G

A

A

V

I

L

V

L

T

V

I

M

I

L

L

S

G

W

C

D

F

T

E

S

H

H

P

V

L

S

N

E

R

W

E

G

G

-

H

-

Y

-

H

-

K

-

L

-

E

-

G

-

V

W

W

R

R

V

L

A

Q

F

F

G

G

I

L

G

A

G

L

I

V

G

P

A

A

L

I

V

G

V

V

F

L

W

I

L

P

R

R

R

L

T

I

M

M

D

K

E

E

S

S

L

K

S

S

A

Y

E

E

S

N

I

S

E

K

A

A

A

L

K

N

D

S

G

A

K

E

A

G

K

K

Sites not aligning to the query:

12 modified: Phosphoserine
14 modified: Phosphoserine
292 modified: Phosphoserine
296 modified: Phosphoserine

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, 41% coverage: 68:248/445 of query aligns to 55:212/403 of P77589

query
sites
P77589

I

I

F

F

A

S

A

A

T

G

F

I

L

L

M

G

R

L

P

L

I

P

G

G

A

A

W

L

Y

V

F

G

G

G

R

M

F

L

A

A

D
|
D

R

R

Y

Y

G

G

R

R

R

K

L

R

A

I

L

L

T

I

V

G

S

S

V

V

S

A

V

L

M

F

A

G

A

L

C

F

S

S

F

L

L

A

I

T

A

A

I

I

A

A

P

-

T

-

A

-

S

-

I

-

G

-

I

-

W

W

A

D

A

F

V

P

I

S

L

L

L

V

F

F

A

A

R

R

L

L

L

M

Q

T

G

G

F

V

A

G

T

L

G

G

G

A

E

A

Y

L

G

P

A

N

S

L

A

I

T

A

Y

L

M

T

S

S

E

E

A

A

V

G

P

P

G

R

W

F

R

R

G

G

F

T

L

A

S

V

S

S

F

L

H

M

Y

Y

V

C

T

G

L

V

V

P

G

I

G

G

H

A

V

A

L

L

A

A

Q

A

A

T

V

-

L

-

V

-

M

-

L

-

L

L

S

G

W

F

D

A

T

G

S

A

H

N

V

L

S

A

E

-

W

-

G

-

W

W

R

Q

V

T

A

V

F

F

G

W

I

V

G

G

I

V

G

V

A

P

L

L

V

I

-

L

V

V

F

P

W

L

L

L

R

M

R

R

T

W

M

L

D

P

E

E

S

S

L

-

S

-

A

-

E

-

S

-

I

-

E

-

A

A

A

V

K

F

D

A

G

G

K

E

A

K

K

Q

A

S

S

A

G

P

S

P

M

L

R

R

E

A

L

L

F

F

V

A

N

P

Q

E

D75 (= D88) mutation D->A,E: Lack of 3HPP transport activity.

Sites not aligning to the query:

27 E→A: Lack of 3HPP transport activity.; E→D: Slight decrease in 3HPP transport activity.
272 A→H: 30% increase in 3HPP transport activity.
276 K→D: Lack of 3HPP transport activity.

Q09852 Putative inorganic phosphate transporter C23D3.12 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 45% coverage: 30:229/445 of query aligns to 51:261/559 of Q09852

query
sites
Q09852

A

A

G

G

N

F

L

F

V

L

E

D

W

S

Y

Y

D

D

V

L

Y

F

V

I

Y

I

S

N

V

L

F

V

A

S

K

P

Y

I

F

Y

E

E

S

Y

Q

L

F

Y

F

W

S

G

A

G

D

L

D

E

K

G

N

K

S

K

T

P

M

H

Y

Y

I

P

W

S

G

G

I

I

F

H

-

G

-

L

-

V

-

N

A

A

T

A

F

N

L

I

M

G

R

N

P

V

I

F

G

G

A

Q

W

I

Y

L

F

F

G

G

R

F

F

M

A

G

D

D

R

F

Y

F

G

G

R

R

R

K

L

F

A

V

L

Y

T

G

V

K

S

E

V

M

S

I

V

V

M

V

A

I

C

A

S

T

F

V

L

L

I

V

A

I

I

A

A

L

P

P

T

K

A

S

A

I

S

P

I

T

G

P

I

L

W

G

A

K

A

M

V

M

I

W

L

I

L

F

F

A

A

W

R

R

L

W

L

L

Q

L

G

G

F

L

A

G

T

I

G

G

E

D

Y

Y

G

P

A

M

S

S

A

A

T

T

Y

I

M

T

S

S

E

E

A

R

A

S

V

L

P

L

G

S

W

R

R

R

G

G

F

T

L

L

S

L

S

S

F

I

H

V

Y

F

V

-

T

S

L

F

V

Q

G

G

G

F

H

G

V

T

L

L

A

A

Q

G

A

A

V

I

L

V

L

T

V

I

M

I

L

L

S

A

W

C

D

F

T

E

S

K

H

P

V

L

S

N

E

Q

W

R

G

G

-

E

-

Y

-

T

-

K

-

L

-

E

-

G

-

V

W

W

R

R

V

L

A

Q

F

M

G

G

I

L

G

A

G

L

I

V

G

P

A

A

L

L

V

L

V

V

F

L

W

I

L

P

R

R

R

L

T

T

M

M

D

K

E

E

S

S

L

K

S

S

A

Y

E

E

S

Q

I

S

E

K

A

A

Sites not aligning to the query:

297 modified: Phosphoserine
299 modified: Phosphoserine

Q9LT15 Sugar transport protein 10; AtSTP10; D-glucose-H(+) symport protein STP10; D-glucose-proton symporter STP10; Hexose transporter 10 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
23% identity, 53% coverage: 89:325/445 of query aligns to 108:357/514 of Q9LT15

query
sites
Q9LT15

R

K

Y

H

G

G

R

R

R

K

L

V

A

S

L

M

T

F

V

I

S

-

V

-

S

-

V

-

M

-

A

G

C

L

S

A

F

F

L

L

I

I

A

G

I

A

A

L

P

F

T

N

A

A

A

F

S

A

I

V

G

N

I

V

W

-

A

-

V

S

I

M

L

L

L

I

F

I

A

G

R

R

L

L

Q

L

G

G

F

V

A

G

T

V

G

G

G

F

E

A

Y

N

G

Q

A

S

S

T

A

P

T

V

Y

Y

M

L

S

S

E
|
E

A

M

A

A

V

P

P

A

G

K

W

I

R

R

G

G

F

A

L

L

S

N

-

I

S

G

F

F

H
x
Q

Y

M

V

A

T

I

L

T

V

I

G

G

G

-

H

-

V

-

L

-

A

-

Q

-

A

-

V
x
I

L

L

L

V

V

A

M

N

L

L

L

I

S

N

W

Y

D

G

T

T

S

S

H

K

V

M

S

A

E

Q

W

H

G

G

W

W

R

R

V

V

A

S

F

L

G

G

I

L

G

A

I

V

G

P

A

A

L

V

V

V

V

M

-

V

-

I

-

G

-

S

F

F

W

I

L

L

R

P

R

D

T

T

M

P

D

N

E

S

S

M

L

L

S

E

A

R

E

G

S

K

I

N

E

E

A

E

A

A

K

K

-

Q

-

M

-

L

-

K

-

I

-

R

-

G

-

A

-

D

-

N

-

V

-

D

-

H

-

E

-

F

-

Q

-

D

-

L

-

I

-

D

-

A

-

V

D

E

G

A

K

A

A

K

K

K

A

V

S

E

G

N

S

P

M

W

R

K

E

N

L

I

F

M

V

E

N

S

Q

K

W

Y

R

R

P

P

-

A

L

L

L

I

L

F

C

C

-

S

-

A

-

I

-

P

F

F

L

F

-
x
Q

I

I

T

T

A

G

G

I

G
x
N

T

V

V

I

A

M

F

F

Y

Y

T

-

Y

-

T

-

I

-

N

-

G

A

P

P

K

V

M

L

I

F

Q

K

T

T

A

L

F

G

A

F

G

G

D

D

V

A

I

A

T

L

G

M

T

S

W

A

I

V

N

I

L

T

G

G

V

V

L

V

T
x
N

F

M

L

L

M

S

L

T

L

F

Q

V

P

S

L

I

G

Y

G

A

L

V

L

-

S

-

D
|
D

R

R

I

Y

G

G

R

R

K

R

S

L

L

L

L

F

V

L

F

E

F

G

G

G

V

I

E162 (= E151) mutation to Q: Abolishes glucose transport activity; when associated with N-344.
Q177 (≠ H165) binding ; mutation to A: Reduces affinity for glucose 37-fold.
I184 (≠ V179) mutation to A: Reduces affinity for glucose 3-fold.
Q295 (vs. gap) binding
Q296 (vs. gap) binding
N301 (≠ G262) binding
N332 (≠ T298) binding
D344 (= D312) mutation to N: Abolishes glucose transport activity; when associated with Q-162.

Sites not aligning to the query:

39 F→A: Reduces affinity for glucose 8-fold.
43 L→A: Reduces affinity for glucose 150-fold and turns STP10 into a low affinity transporter.
77 modified: Disulfide link with 449; C→A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
410 binding
449 modified: Disulfide link with 77; C→A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).

7aaqA Sugar/h+ symporter stp10 in outward occluded conformation (see paper)
23% identity, 53% coverage: 89:325/445 of query aligns to 88:337/487 of 7aaqA

query
sites
7aaqA

R

K

Y

H

G

G

R

R

R

K

L

V

A

S

L

M

T

F

V

I

S

-

V

-

S

-

V

-

M

-

A

G

C

L

S

A

F

F

L

L

I

I

A

G

I

A

A

L

P

F

T

N

A

A

A

F

S

A

I

V

G

N

I

V

W

-

A

-

V

S

I

M

L

L

L

I

F

I

A

G

R

R

L

L

Q

L

G

G

F

V

A

G

T

V

G

G

G

F

E

A

Y

N

G

Q

A

S

S

T

A

P

T

V

Y

Y

M

L

S

S

E

E

A

M

A

A

V

P

P

A

G

K

W

I

R

R

G

G

F

A

L

L

S

N

-

I

S

G

F

F

H
x
Q

Y

M

V

A

T

I

L

T

V

I

G

G

G

-

H

-

V

-

L

-

A

-

Q

-

A

-

V
x
I

L

L

L

V

V

A

M

N

L

L

L

I

S

N

W

Y

D

G

T

T

S

S

H

K

V

M

S

A

E

Q

W

H

G

G

W

W

R

R

V

V

A

S

F

L

G

G

I

L

G

A

I

V

G

P

A

A

L

V

V

V

V

M

-

V

-

I

-

G

-

S

F

F

W

I

L

L

R

P

R

D

T

T

M

P

D

N

E

S

S

M

L

L

S

E

A

R

E

G

S

K

I

N

E

E

A

E

A

A

K

K

-

Q

-

M

-

L

-

K

-

I

-

R

-

G

-

A

-

D

-

N

-

V

-

D

-

H

-

E

-

F

-

Q

-

D

-

L

-

I

-

D

-

A

-

V

D

E

G

A

K

A

A

K

K

K

A

V

S

E

G

N

S

P

M

W

R

K

E

N

L

I

F

M

V

E

N

S

Q

K

W

Y

R

R

P

P

-

A

L

L

L

I

L

F

C

C

-

S

-

A

-

I

-

P

F

F

L

F

-
x
Q

-

Q

I

I

T

T

A

G

G

I

G
x
N

T

V

V

I

A

M

F

F

Y

Y

T

-

Y

-

T

-

I

-

N

-

G

A

P

P

K

V

M

L

I

F

Q

K

T

T

A

L

F

G

A

F

G

G

D

D

V

A

I

A

T

L

G

M

T

S

W

A

I

V

N

I

L

T

G

G

V

V

L

V

T
x
N

F

M

L

L

M

S

L

T

L

F

Q

V

P

S

L

I

G

Y

G

A

L

V

L

-

S

-

D

D

R

R

I

Y

G

G

R

R

K

R

S

L

L

L

L

F

V

L

F

E

F

G

G

G

V

I

binding beta-D-glucopyranose: Q157 (≠ H165), I164 (≠ V179), Q275 (vs. gap), N281 (≠ G262), N312 (≠ T298)

Sites not aligning to the query:

binding beta-D-glucopyranose: 386, 390

P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
25% identity, 85% coverage: 23:400/445 of query aligns to 12:429/491 of P0AGF4

query
sites
P0AGF4

S

S

N

I

T

T

L

L

K

V

G

A

S

T

A

L

G

G

N

G

L

L

V

L

E
x
F

W

G

Y

Y

D

D

V

T

Y

A

V

V

Y

I

S

S

V

G

F

T

A

V

K

E

Y

S

F

L

E

N

S

T

Q

V

F

F

F

V

S

A

A

P

D

Q

D

N

-

L

-

S

K

E

N

S

S

A

T

A

M

N

Y

S

I

L

W

L

G

G

I

F

F

C

A

V

A

A

T

S

F

A

L

L

M

I

R

G

P

C

I

I

-

I

G

G

A

G

W

A

Y

L

F

G

G

G

R

Y

F

C

A

S

D

N

R

R

Y

F

G
|
G

R

R

L

D

A

S

L

L

T

K

V

I

S

-

V

-

S

-

V

-

M

-

A

A

C

V

S

L

F

F

L

F

I

I

A

S

-

G

-

V

-

G

-

S

-

A

-

W

-

P

-

E

-

L

-

G

-

F

-

T

-

S

I

I

A

N

P

P

T

D

A

N

A

T

S

V

I

P

G

V

I

Y

W

L

A

A

A

G

V

Y

I

V

L

P

L

E

F

F

A

V

-

I

-

Y

R
|
R

L

I

Q

G

G

G

F

I

A

G

T

V

G

G

G

L

E

A

Y

S

G

M

A

L

S

S

A

P

T

M

Y

Y

M

I

S

A

E
|
E

A

L

A

A

V

P

P

A

G

H

W

I

R
|
R

G

G

F

K

L

L

S

V

S

S

F

F

H

N

Y
x
Q

V

F

T

A

L

I

V

I

G

F

G

G

H

Q

V

L

L

L

A

V

Q

Y

A

C

V

V

L

N

L

Y

V

F

M

I

L

A

L

R

S

S

W

G

D

D

T

A

S

S

H

W

V

L

S

N

E

T

W

D

G

G

W

W

R

R

V

Y

A

M

F

F

G

A

I

S

G

E

G

C

I

I

G

P

A

A

L

L

V

L

V

F

F

L

W

M

L

L

R

L

R

Y

T

T

M

V

D

P

E

E

S

S

L

P

-

R

-

W

-

L

-

M

-

S

-

R

-

G

-

K

-

Q

-

E

S

Q

A

A

E

E

S

G

I

I

E

L

A

R

A

K

K

I

D

M

G

G

K

N

A

T

K

L

A

A

S

T

G

Q

S

A

M

V

R

Q

E

E

L

I

-

K

-

H

F

S

V

L

N

D

Q

H

W

G

R

R

P

K

L

T

-

G

-

R

L

L

C

M

F

F

-

G

-

V

-

G

L

V

I

I

T

V

A

I

G

G

G

V

T

M

V

L

A

S

F

I

Y

F

T
x
Q

Y
x
Q

T

F

I

V

N

G

-

I

-
x
N

-

V

-

L

-
x
Y

-

Y

G

A

P

P

K

E

M

V

I

F

Q

K

T

T

A

L

F

G

A

A

G

S

D

T

D

D

V

I

I

A

T

L

G

L

T

Q

W

T

I

I

N

I

L

V

G

G

V

V

L

I

T
x
N

F

L

L

T

M

F

L

T

L

V

Q

-

P

-

L

L

G

A

G

I

L

M

L

T

S

V

D

D

R

K

I

F

G
|
G

R
|
R

K

K

S

P

L

L

L

Q

V

I

F

I

F

G

G

A

V

L

G

G

G

M

V

A

L

I

Y

G

T

M

W

F

Y

S

L

L

V

G

T

T

A

A

L

F

P

Y

Q

T

Q

Q

T

A

S

P

-

G

-

I

-

V

A

A

L

L

S

L

A

S

F

M

L

L

I

F

L

Y

A

V

T

A

G

A

F

F

V

A

I

M

L

S

T

W

G

G

Y

-

T

-

S

P

I

V

N

C

A
x
W

V

V

V

L

K

L

A

S

E
|
E

L

I

F

F

P

P

A

N

H

A

I

I

R
|
R

A

G

L

K

G

A

V

L

G

A

L

I

G

A

Y

V

A

A

-

A

-
x
Q

-
x
W

L

L

A

A

N

N

S

Y

L

F

F

V

G

S

G

W

T

T

A

F

P

P

L

M

F24 (≠ E35) mutation to A: Decreases xylose transport.
G83 (= G91) mutation to A: Abolishes xylose transport.
R133 (= R131) mutation R->C,H,L: Abolishes xylose transport.
E153 (= E151) mutation to A: Abolishes xylose transport.
R160 (= R158) mutation to A: Abolishes xylose transport.
Q168 (≠ Y166) binding ; mutation to A: Abolishes xylose transport.
Q288 (≠ T268) mutation to A: Abolishes xylose transport.
QQ 288:289 (≠ TY 268:269) binding
Q289 (≠ Y269) mutation to A: Strongly decreases xylose transport.
N294 (vs. gap) binding ; mutation to A: Abolishes xylose transport.
Y298 (vs. gap) mutation to A: Abolishes xylose transport.
N325 (≠ T298) mutation to A: No effect on xylose transport.
G340 (= G315) mutation to A: Abolishes xylose transport.
R341 (= R316) mutation R->A,W: Abolishes xylose transport.
W392 (≠ A366) binding ; mutation to A: Abolishes xylose transport.
E397 (= E371) mutation to A: Abolishes xylose transport.
R404 (= R378) mutation to A: Strongly decreases xylose transport.
Q415 (vs. gap) binding
W416 (vs. gap) mutation to A: Strongly decreases xylose transport.

4gc0A The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to 6-bromo-6-deoxy-d-glucose (see paper)
25% identity, 85% coverage: 23:400/445 of query aligns to 8:425/475 of 4gc0A

query
sites
4gc0A

S

S

N

I

T

T

L

L

K

V

G

A

S

T

A

L

G

G

N

G

L

L

V

L

E

F

W

G

Y

Y

D

D

V

T

Y

A

V

V

Y

I

S

S

V

G

F

T

A

V

K

E

Y

S

F

L

E

N

S

T

Q

V

F

F

F

V

S

A

A

P

D

Q

D

N

-

L

-

S

K

E

N

S

S

A

T

A

M

N

Y

S

I

L

W

L

G

G

I

F

F

C

A

V

A

A

T

S

F

A

L

L

M

I

R

G

P

C

I

I

-

I

G

G

A

G

W

A

Y

L

F

G

G

G

R

Y

F

C

A

S

D

N

R

R

Y

F

G

G

R

R

L

D

A

S

L

L

T

K

V

I

S

-

V

-

S

-

V

-

M

-

A

A

C

V

S

L

F

F

L

F

I

I

A

S

-

G

-

V

-

G

-

S

-

A

-

W

-

P

-

E

-

L

-

G

-

F

-

T

-

S

I

I

A

N

P

P

T

D

A

N

A

T

S

V

I

P

G

V

I

Y

W

L

A

A

A

G

V

Y

I

V

L

P

L

E

F

F

A

V

-

I

-

Y

R

R

L

I

Q

G

G

G

F

I

A

G

T

V

G

G

G

L

E

A

Y

S

G

M

A

L

S

S

A

P

T

M

Y

Y

M

I

S

A

E

E

A

L

A

A

V

P

P

A

G

H

W

I

R

R

G

G

F

K

L

L

S

V

S

S

F

F

H

N

Y
x
Q

V

F

T

A

L

I

V

I

G

F

G

G

H

Q

V

L

L

L

A

V

Q

Y

A

C

V

V

L

N

L

Y

V

F

M

I

L

A

L

R

S

S

W

G

D

D

T

A

S

S

H

W

V

L

S

N

E

T

W

D

G

G

W

W

R

R

V

Y

A

M

F

F

G

A

I

S

G

E

G

C

I

I

G

P

A

A

L

L

V

L

V

F

F

L

W

M

L

L

R

L

R

Y

T

T

M

V

D

P

E

E

S

S

L

P

-

R

-

W

-

L

-

M

-

S

-

R

-

G

-

K

-

Q

-

E

S

Q

A

A

E

E

S

G

I

I

E

L

A

R

A

K

K

I

D

M

G

G

K

N

A

T

K

L

A

A

S

T

G

Q

S

A

M

V

R

Q

E

E

L

I

-

K

-

H

F

S

V

L

N

D

Q

H

W

G

R

R

P

K

L

T

-

G

-

R

L

L

C

M

F

F

-

G

-

V

-

G

L

V

I

I

T

V

A

I

G

G

G

V

T

M

V

L

A

S

F

I

Y

F

T
x
Q

Y

Q

T

F

I

V

N

G

-

I

-
x
N

-

V

-
x
L

-

Y

G

A

P

P

K

E

M

V

I

F

Q

K

T

T

A

L

F

G

A

A

G

S

D

T

D

D

V

I

I

A

T

L

G

L

T

Q

W

T

I

I

N

I

L

V

G

G

V

V

L

I

T

N

F

-

L

-

M

L

L

T

L

F

Q

T

P

V

L

L

G

A

G

I

L

M

L

T

S

V

D

D

R

K

I

F

G

G

R

R

K

K

S

P

L

L

L

Q

V

I

F

I

F

G

G

A

V

L

G

G

G

M

V

A

L

I

Y

G

T

M

W

F

Y

S

L

L

V

G

T

T

A

A

L

F

P

Y

Q

T

Q

Q

T

A

S

P

-

G

-

I

-

V

A

A

L

L

S

L

A

S

F

M

L

L

I

F

L

Y

A

V

T

A

G

A

F

F

V

A

I

M

L

S

T

W

G

G

Y

-

T

-

S

P

I

V

N

C

A
x
W

V

V

V

L

K

L

A

S

E

E

L

I

F

F

P

P

A

N

H

A

I

I

R

R

A

G

L

K

G

A

V

L

G

A

L

I

G

A

Y

V

A

A

-

A

-

Q

-

W

L

L

A

A

N

N

S

Y

L

F

F

V

G

S

G

W

T

T

A

F

P

P

L

M

binding 6-bromo-6-deoxy-beta-D-glucopyranose: Q164 (≠ Y166), Q284 (≠ T268), N290 (vs. gap), L293 (vs. gap), W388 (≠ A366)

4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
25% identity, 85% coverage: 23:400/445 of query aligns to 8:425/475 of 4gbzA

query
sites
4gbzA

S

S

N

I

T

T

L

L

K

V

G

A

S

T

A

L

G

G

N

G

L

L

V

L

E

F

W

G

Y

Y

D

D

V

T

Y

A

V

V

Y

I

S

S

V

G

F

T

A

V

K

E

Y

S

F

L

E

N

S

T

Q

V

F

F

F

V

S

A

A

P

D

Q

D

N

-

L

-

S

K

E

N

S

S

A

T

A

M

N

Y

S

I

L

W

L

G

G

I

F

F

C

A

V

A

A

T

S

F

A

L

L

M

I

R

G

P

C

I

I

-

I

G

G

A

G

W

A

Y

L

F

G

G

G

R

Y

F

C

A

S

D

N

R

R

Y

F

G

G

R

R

L

D

A

S

L

L

T

K

V

I

S

-

V

-

S

-

V

-

M

-

A

A

C

V

S

L

F

F

L

F

I

I

A

S

-

G

-

V

-

G

-

S

-

A

-

W

-

P

-

E

-

L

-

G

-

F

-

T

-

S

I

I

A

N

P

P

T

D

A

N

A

T

S

V

I

P

G

V

I

Y

W

L

A

A

A

G

V

Y

I

V

L

P

L

E

F

F

A

V

-

I

-

Y

R

R

L

I

Q

G

G

G

F

I

A

G

T

V

G

G

G

L

E

A

Y

S

G

M

A

L

S

S

A

P

T

M

Y

Y

M

I

S

A

E

E

A

L

A

A

V

P

P

A

G

H

W

I

R

R

G

G

F

K

L

L

S

V

S

S

F

F

H

N

Y
x
Q

V

F

T

A

L

I

V

I

G

F

G

G

H

Q

V

L

L

L

A

V

Q

Y

A

C

V

V

L

N

L

Y

V

F

M

I

L

A

L

R

S

S

W

G

D

D

T

A

S

S

H

W

V

L

S

N

E

T

W

D

G

G

W

W

R

R

V

Y

A

M

F

F

G

A

I

S

G

E

G

C

I

I

G

P

A

A

L

L

V

L

V

F

F

L

W

M

L

L

R

L

R

Y

T

T

M

V

D

P

E

E

S

S

L

P

-

R

-

W

-

L

-

M

-

S

-

R

-

G

-

K

-

Q

-

E

S

Q

A

A

E

E

S

G

I

I

E

L

A

R

A

K

K

I

D

M

G

G

K

N

A

T

K

L

A

A

S

T

G

Q

S

A

M

V

R

Q

E

E

L

I

-

K

-

H

F

S

V

L

N

D

Q

H

W

G

R

R

P

K

L

T

-

G

-

R

L

L

C

M

F

F

-

G

-

V

-

G

L

V

I

I

T

V

A

I

G

G

G

V

T

M

V

L

A

S

F

I

Y

F

T
x
Q

Y

Q

T

F

I

V

N

G

-

I

-
x
N

-

V

-

L

-

Y

G

A

P

P

K

E

M

V

I

F

Q

K

T

T

A

L

F

G

A

A

G

S

D

T

D

D

V

I

I

A

T

L

G

L

T

Q

W

T

I

I

N

I

L

V

G

G

V

V

L

I

T

N

F

-

L

-

M

L

L

T

L

F

Q

T

P

V

L

L

G

A

G

I

L

M

L

T

S

V

D

D

R

K

I

F

G

G

R

R

K

K

S

P

L

L

L

Q

V

I

F

I

F

G

G

A

V

L

G

G

G

M

V

A

L

I

Y

G

T

M

W

F

Y

S

L

L

V

G

T

T

A

A

L

F

P

Y

Q

T

Q

Q

T

A

S

P

-

G

-

I

-

V

A

A

L

L

S

L

A

S

F

M

L

L

I

F

L

Y

A

V

T

A

G

A

F

F

V

A

I

M

L

S

T

W

G

G

Y

-

T

-

S

P

I

V

N

C

A
x
W

V

V

V

L

K

L

A

S

E

E

L

I

F

F

P

P

A

N

H

A

I

I

R

R

A

G

L

K

G

A

V

L

G

A

L

I

G

A

Y

V

A

A

-

A

-

Q

-

W

L

L

A

A

N

N

S

Y

L

F

F

V

G

S

G

W

T

T

A

F

P

P

L

M

binding beta-D-glucopyranose: Q164 (≠ Y166), Q284 (≠ T268), N290 (vs. gap), W388 (≠ A366)

4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
25% identity, 85% coverage: 23:400/445 of query aligns to 8:425/475 of 4gbyA

query
sites
4gbyA

S

S

N

I

T

T

L

L

K

V

G

A

S

T

A

L

G

G

N

G

L

L

V

L

E

F

W

G

Y

Y

D

D

V

T

Y

A

V

V

Y

I

S

S

V

G

F

T

A

V

K

E

Y

S

F

L

E

N

S

T

Q

V

F

F

F

V

S

A

A

P

D

Q

D

N

-

L

-

S

K

E

N

S

S

A

T

A

M

N

Y

S

I

L

W

L

G

G

I

F

F

C

A

V

A

A

T

S

F

A

L

L

M

I

R

G

P

C

I

I

-

I

G

G

A

G

W

A

Y

L

F

G

G

G

R

Y

F

C

A

S

D

N

R

R

Y

F

G

G

R

R

L

D

A

S

L

L

T

K

V

I

S

-

V

-

S

-

V

-

M

-

A

A

C

V

S

L

F

F

L

F

I

I

A

S

-

G

-

V

-

G

-

S

-

A

-

W

-

P

-

E

-

L

-

G

-

F

-

T

-

S

I

I

A

N

P

P

T

D

A

N

A

T

S

V

I

P

G

V

I

Y

W

L

A

A

A

G

V

Y

I

V

L

P

L

E

F

F

A

V

-

I

-

Y

R

R

L

I

Q

G

G

G

F

I

A

G

T

V

G

G

G

L

E

A

Y

S

G

M

A

L

S

S

A

P

T

M

Y

Y

M

I

S

A

E

E

A

L

A

A

V

P

P

A

G

H

W

I

R

R

G

G

F

K

L

L

S

V

S

S

F

F

H

N

Y
x
Q

V

F

T

A

L

I

V

I

G

F

G

G

H

Q

V

L

L

L

A

V

Q

Y

A

C

V

V

L

N

L

Y

V

F

M

I

L

A

L

R

S

S

W

G

D

D

T

A

S

S

H

W

V

L

S

N

E

T

W

D

G

G

W

W

R

R

V

Y

A

M

F

F

G

A

I

S

G

E

G

C

I

I

G

P

A

A

L

L

V

L

V

F

F

L

W

M

L

L

R

L

R

Y

T

T

M

V

D

P

E

E

S

S

L

P

-

R

-

W

-

L

-

M

-

S

-

R

-

G

-

K

-

Q

-

E

S

Q

A

A

E

E

S

G

I

I

E

L

A

R

A

K

K

I

D

M

G

G

K

N

A

T

K

L

A

A

S

T

G

Q

S

A

M

V

R

Q

E

E

L

I

-

K

-

H

F

S

V

L

N

D

Q

H

W

G

R

R

P

K

L

T

-

G

-

R

L

L

C

M

F

F

-

G

-

V

-

G

L

V

I

I

T

V

A

I

G

G

G

V

T

M

V

L

A

S

F

I

Y

F

T
x
Q

Y

Q

T

F

I

V

N

G

-

I

-
x
N

-

V

-

L

-

Y

G

A

P

P

K

E

M

V

I

F

Q

K

T

T

A

L

F

G

A

A

G

S

D

T

D

D

V

I

I

A

T

L

G

L

T

Q

W

T

I

I

N

I

L

V

G

G

V

V

L

I

T

N

F

-

L

-

M

L

L

T

L

F

Q

T

P

V

L

L

G

A

G

I

L

M

L

T

S

V

D

D

R

K

I

F

G

G

R

R

K

K

S

P

L

L

L

Q

V

I

F

I

F

G

G

A

V

L

G

G

G

M

V

A

L

I

Y

G

T

M

W

F

Y

S

L

L

V

G

T

T

A

A

L

F

P

Y

Q

T

Q

Q

T

A

S

P

-

G

-

I

-

V

A

A

L

L

S

L

A

S

F

M

L

L

I

F

L

Y

A

V

T

A

G

A

F

F

V

A

I

M

L

S

T

W

G

G

Y

-

T

-

S

P

I

V

N

C

A
x
W

V

V

V

L

K

L

A

S

E

E

L

I

F

F

P

P

A

N

H

A

I

I

R

R

A

G

L

K

G

A

V

L

G

A

L

I

G

A

Y

V

A

A

-

A

-

Q

-

W

L

L

A

A

N

N

S

Y

L

F

F

V

G

S

G

W

T

T

A

F

P

P

L

M

binding beta-D-xylopyranose: Q164 (≠ Y166), Q284 (≠ T268), N290 (vs. gap), W388 (≠ A366)

7aarA Sugar/h+ symporter stp10 in inward open conformation (see paper)
25% identity, 34% coverage: 89:240/445 of query aligns to 93:234/485 of 7aarA

query
sites
7aarA

R

K

Y
x
H

G

G

R

R

R

K

L
x
V

A

S

L

M

T
x
F

V

I

S

-

V

-

S

-

V

-

M

-

A

G

C

L

S

A

F

F

L

L

I

I

A

G

I

A

A

L

P

F

T

N

A

A

A

F

S

A

I

V

G

N

I

V

W

-

A

-

V

S

I

M

L

L

L

I

F

I

A

G

R

R

L

L

Q

L

G

G

F

V

A

G

T

V

G

G

G

F

E

A

Y
x
N

G

Q

A

S

S

T

A
x
P

T

V

Y

Y

M

L

S

S

E

Q

A

M

A

A

V

P

P

A

G

K

W

I

R

R

G

G

F

A

L

L

S
x
N

-

I

S

G

F
|
F

H
x
Q

Y

M

V

A

T
x
I

L

T

V

I

G

G

G

-

H

-

V

-

L

-

A

-

Q

-

A

-

V

I

L

L

L

V

V

A

M

N

L

L

L

I

S

N

W

Y

D

G

T

T

S

S

H

K

V

M

S

A

E

Q

W

H

G

G

W

W

R

R

V

V

A

S

F

L

G

G

I

L

G

A

I

V

G

P

A

A

L

V

V

V

V

M

-

V

-

I

-

G

-

S

F

F

W

I

L

L

R

P

R
x
D

T

T

M

P

D

N

E

S

S

M

L

L

S

E

A

R

E

G

S

K

I

N

E

E

A

E

A

A

K

K

D

Q

G

M

K

L

A

K

K

K

A

I

S

R

G

G

S

A

binding Octyl Glucose Neopentyl Glycol : H94 (≠ Y90), V98 (≠ L94), F101 (≠ T97), N138 (≠ Y142), P142 (≠ A146), N158 (≠ S162), F161 (= F164), Q162 (≠ H165), I165 (≠ T168), D210 (≠ R216)

Sites not aligning to the query:

binding Octyl Glucose Neopentyl Glycol : 28, 90, 391, 392, 395, 419
binding beta-D-glucopyranose: 280, 286, 289, 391, 395

O23492 Inositol transporter 4; Myo-inositol-proton symporter INT4; Protein INOSITOL TRANSPORTER 4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
26% identity, 30% coverage: 88:221/445 of query aligns to 92:210/582 of O23492

query
sites
O23492

D

D

R

K

Y

F

G

G

R

R

L

M

A

S

L

I

T

L

V

I

S

A

V

D

S

V

V

L

M

F

A

L

A

I

C

G

S

A

F

I

L

V

I

M

A

A

I

F

A

A

P

P

T

-

A

-

S

-

I

-

G

-

I

-

W

-

A

A

A

P

V

W

I

V

L

I

F

V

A

G

R

R

L

I

L

F

Q

V

G

G

F

F

A

G

T

V

G

G

G

M

E

A

Y

S

G

M

A

T

S

S

A

P

T

L

Y

Y

M

I

S

S

E

E

A

A

A

S

V

P

P

A

G

R

W

I

R

R

G

G

F

A

L

L

S

V

S

S

F

T

H

N

Y

G

V

L

T

L

L

I

V

T

G

G

H

Q

V

F

L

F

A

S

Q

Y

A

L

V

I

L

N

L

L

V

A

M

F

L

V

L

H

S

T

W

P

D

G

T

T

S

-

H

-

V

-

S

-

E

-

W

-

G

-

W

W

R

R

V

W

A

M

F

L

G

G

I

V

G

A

G

G

I

V

G

P

A

A

L

I

V

V

V

Q

F

F

W

V

L

L

R

M

R

L

T

S

M

L

D

P

E

E

S

S

Sites not aligning to the query:

559:561 LLE→AAA: No effect on targeting.
559:582 mutation Missing: No effect on targeting.
564:565 FK→AA: No effect on targeting.
570:575 RRREKK→AAAAAA: No effect on targeting.

A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
25% identity, 42% coverage: 60:244/445 of query aligns to 40:220/446 of A0A0H2VG78

query
sites
A0A0H2VG78

N

N

S

S

T

T

M

T

Y

E

I

-

W

-

G

G

I

I

F

V

A

V

A

S

T

S

F

M

L

L

M

I

R

G

P

A

I

I

-

V

G

G

A

A

W

G

Y

S

F

S

G

G

R

P

F

L

A

A

D

D

R

K

Y

L

G

G

R

R

L

-

A

-

L

-

T

-

V

-

S

R

V

L

S

V

V

M

M

L

A

I

A

A

C

I

S

V

F

F

L

I

I

I

A

G

I

A

A

L

P

I

T

L

A

A

S

S

I

T

G

N

I

L

W

-

A

-

V

A

I

L

L

L

L

I

F

I

A

G

R
|
R

L

L

L

I

Q
x
I

G

G

F

L

A

A

T

V

G

G

E

S

Y

M

G

S

A

T

S

V

A

P

T

V

Y

Y

M

L

S

S

E
|
E

A

M

A

A

V

P

P

T

G

E

W

Y

R

R

G

G

F

S

L

L

S

G

S

S

F

L

H

N

Y
x
Q

V

L

T

M

L

I

V

T

G

I

G

G

H

-

V

-

L

-

A

-

Q

-

A

-

V

I

L

L

L

A

V

A

M

Y

L

L

L

V

S

N

W

Y

D

A

T

F

S

A

H

D

V

I

S

E

E

-

W

-

G

G

W

W

R

R

V

W

A

M

F

L

G

G

I

L

G

A

G

V

I

V

G

P

A

S

L

V

V

I

V

L

F

L

-

V

-

G

-

I

-

Y

-

F

-

M

-

P

-

E

-

S

-

P

-

R

W

W

L

L

R

L

R

E

T

N

M

R

D

N

E

E

S

E

L

A

S

A

A

R

E

Q

S

V

I

M

E

K

A

I

A

T

K

Y

D

D

G

D

K

S

A

E

-

I

-

D

K

K

A

E

S

L

G

K

S

E

M

M

R

K

E

E

L

I

R102 (= R131) mutation to A: Loss of transport activity.
I105 (≠ Q134) mutation to S: Affects symport activity. May function as an uniporter.
E122 (= E151) mutation to A: Loss of transport activity.
Q137 (≠ Y166) mutation to A: Loss of transport activity.

Sites not aligning to the query:

22 D→N: Affects symport activity. May function as an uniporter.
250 Q→A: Loss of transport activity.
251 Q→A: Loss of transport activity.
256 N→A: Loss of transport activity.
357 W→A: Loss of transport activity.

Query Sequence

>WP_057507967.1 NCBI__GCF_001431535.1:WP_057507967.1
MSISQSTAASPVSERAALKRSVSNTLKGSAGNLVEWYDVYVYSVFAKYFESQFFSADDKN
STMYIWGIFAATFLMRPIGAWYFGRFADRYGRRLALTVSVSVMAACSFLIAIAPTAASIG
IWAAVILLFARLLQGFATGGEYGASATYMSEAAVPGWRGFLSSFHYVTLVGGHVLAQAVL
LVMLLSWDTSHVSEWGWRVAFGIGGIGALVVFWLRRTMDESLSAESIEAAKDGKAKASGS
MRELFVNQWRPLLLCFLITAGGTVAFYTYTINGPKMIQTAFAGDDVITGTWINLGVLTFL
MLLQPLGGLLSDRIGRKSLLVFFGVGGVLYTWYLVTALPQQTSALSAFLILATGFVILTG
YTSINAVVKAELFPAHIRALGVGLGYALANSLFGGTAPLLYQGALKAGRVDEFVIYITAV
IAVSLVVYIFFLKNKGPNWLDGTRK

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