SitesBLAST

P54582 Glycine betaine transporter BetP; Glycine betaine permease from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see 6 papers)
33% identity, 74% coverage: 26:561/725 of query aligns to 52:582/595 of P54582

query
sites
P54582

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W101 (= W75) mutation to A: Mainly monomeric, shows a decrease in activity and cannot be activated in response to increased osmolality; when associated with A-351.
E135 (≠ K109) mutation to A: Strongly decreased betaine transport.
G149 (= G123) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
M150 (≠ I124) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
G151 (= G125) mutation to A: Nearly abolishes betaine transport.
I152 (≠ V126) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
IG 152:153 (≠ VD 126:127) binding glycine betaine
G153 (≠ D127) mutation to A: Decreases betaine transport and alters activation at higher osmolality.; mutation to D: Changes substrate specificity, giving rise to proton-coupled choline transport. Decreases sodium-dependent betaine transport.
F156 (= F130) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
W189 (≠ Y165) mutation to C: Mildly decreased betaine transport.
W194 (= W170) mutation to L: Strongly decreased betaine transport.
Y197 (= Y173) mutation to L: Nearly abolishes betaine transport.
R210 (= R186) mutation to A: Nearly abolishes betaine transport.
S253 (= S228) binding glycine betaine
G301 (= G275) mutation to L: Strongly decreased betaine transport.
N309 (= N283) mutation to A: Decreases affinity for sodium ions.
T351 (= T325) mutation to A: Mainly trimeric, but shows reduced activity at high osmolalities. Mainly monomeric, shows a decrease in activity and cannot be activated in response to increased osmolality; when associated with A-101.
W362 (= W340) mutation to C: Strongly decreased betaine transport.
W366 (= W344) mutation to C: No effect on betaine transport.
F369 (= F347) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
W371 (= W349) mutation to L: No effect on betaine transport.
W373 (= W351) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
WWISW 373:377 (≠ WWIAW 351:355) binding glycine betaine
W374 (= W352) mutation to A: Strongly decreases betaine transport, but has no major effect on affinity for glycine betaine.; mutation to L: No effect on betaine transport.
W377 (= W355) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
F380 (= F358) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
F384 (= F362) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
R387 (= R365) mutation to A: Mildly decreased betaine transport.
R392 (= R370) mutation to K: Moderately decreased betaine transport.

4llhA Substrate bound outward-open state of the symporter betp (see paper)
33% identity, 73% coverage: 31:561/725 of query aligns to 1:523/524 of 4llhA

query
sites
4llhA

A

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A

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-

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x
R

P

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N

L

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L

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R

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K

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L

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A

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K

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binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (≠ I124), G95 (= G125), D97 (= D127), W314 (= W351), W315 (= W352), W318 (= W355)
binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: R495 (= R533), R499 (≠ L537)
binding sodium ion: A91 (= A121), M94 (≠ I124), G95 (= G125), F405 (= F443), T408 (= T446), S409 (= S447)

3p03C Crystal structure of betp-g153d with choline bound (see paper)
35% identity, 70% coverage: 31:534/725 of query aligns to 1:495/508 of 3p03C

query
sites
3p03C

A

S

V

L

N

N

W

W

P

S

V

V

F

I

A

V

G

P

T

A

S

L

V

V

I

I

I

V

V

L

A

A

F

T

V

V

L

V

W

W

A

G

A

I

I

G

W

F

P

K

D

D

A

S

A

F

S

T

T

N

A

F

I

A

F

S

G

S

A

A

M

L

D

S

W

A

V

V

A

V

T

D

N

N

F

L

G

G

W

W

Y

A

Y

F

I

I

L

L

T

F

A

G

T

T

I

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V

F

V

V

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F

F

F

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I

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V

V

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A

A

F

A

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S

R

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G

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T

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L

G

G

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I

H

D

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E

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A

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P

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E

F

F

N

R

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T

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W

W

A

I

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M

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|
A

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x
M

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|
D

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M

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F

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binding choline ion: A92 (= A122), M94 (≠ I124), D97 (= D127), F320 (= F358)

2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
26% identity, 67% coverage: 42:526/725 of query aligns to 24:506/508 of 2wswA

query
sites
2wswA

V

L

I

I

V

V

A

G

F

I

V

L

L

C

W

W

A

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|
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|
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binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: F72 (≠ I89), F76 (= F93), R78 (= R95)

B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
26% identity, 67% coverage: 42:526/725 of query aligns to 19:501/514 of B4EY22

query
sites
B4EY22

V

L

I

I

V

V

A

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F

I

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L

L

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W

W

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-

C

-

F

-

I

-

A

-

T

V

V

T

T

S

L

A

I

D

N

S

A

G

C

S

S

L

Y

V

T

M

L

A

A

N

M

M

S

T

T

S

C

K

R

P

S

T

M

M

K

N

E

D

G

S

A

D

E

G

P

P

P

P

L

W

L

L

V

R

R

I

I

V

G

W

W

A

S

V

V

I

L

T

V

G

G

A

I

L

I

T

G

L

I

V

I

M

L

L

L

F

A

I

L

D

G

G

G

V

L

Y

K

T

P

L

I

Q

Q

A

T

A

A

T

I

V

I

M

A

V

G

G

G

L

C

P

P

L

L

S

F

I

F

L

V

I

N

Y

I

L

M

V

V

M

T

F

L

S

S

L

F

W

I

K

K

V

D

L

A

K

K

T

V

E

H

E111 (≠ P136) mutation to A: Abolishes transport activity.
R262 (≠ N283) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
W316 (= W344) mutation to A: 2.5-fold decrease in Vmax.
M331 (≠ V359) mutation to V: 10-fold decrease in Vmax.

4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
26% identity, 67% coverage: 42:526/725 of query aligns to 11:493/495 of 4m8jA

query
sites
4m8jA

V

L

I

I

V

V

A

G

F

I

V

L

L

C

W

W

A

L

A

T

I

V

W

R

P

D

-

L

D

D

A

A

A

S

S

N

T

E

A

V

I

I

F

N

G

A

A

V

M

F

D

S

W

Y

V

V

A

T

T

N

N

V

F

W

G

G

W

W

Y

A

Y

F

I

E

L

W

T

Y

A

M

T

V

I

I

V

M

V

F

V

G

F

G

V

W

I

F

V

W

V

L

A

V

F

F

S

G

R

R

V

Y

G

A

R

K

T

K

K

R

M

L

G

G

P

D

D

E

H

-

S

-

R

K

P

P

K

E

F

F

N

S

L

T

F

A

T

S

W

W

A

I

A

F

M

M

L

M

F

F

A

A

A

S

G

C

I

T

G

S

V

A

D

A

L

V

M

L

F

F

F

W

G

G

I

-

S

S

G

I

P

E

A

I

T

Y

N

Y

Y

Y

L

I

T

S

P

S

P

P

D

P

V

F

G

G

-

M

-

E

A

G

M

Y

S

S

D

A

E

P

A

A

A

K

R

E

M

I

A

G

P

L

I

A

W

Y

T

S

I

L

F

F

H

H

Y

W

G

G

I

P

P

L

G

P

W
|
W

A

A

M

T

Y

Y

A

S

L

F

M

L

G

S

M

V

A

A

F

F

G

A

L

Y

F

F

A

F

Y

F

R

V

Y

R

H

K

L

M

P

E

L

V

S

-

I

I

R

R

-

P

-

S

S

S

A

T

L

L

A

V

P

P

I

L

F

V

G

G

-

E

K

K

R

H

I

V

H

N

G

G

A

L

A

F

G

G

H

T

T

V

V

V

E

D

I

N

A

F

A

Y

T

L

I

V

G

A

T

L

I

I

F

L

G

A

I

M

S

G

V

T

S

S

L

L

G

G

I

L

G

A

V

T

V

P

F

L

L

V

N

T

Y

E

G

C

L

I

S

Q

E

Y

L

L

F

F

G

G

V

I

P

P

N

H

S

T

L

L

S

Q

V

L

Q

D

I

A

A

I

L

I

M

I

A

S

L

C

A

W

V

I

F

L

I

L

T

N

I

A

A

I

S

C

T

V

V

A

S

F

G

G

V

L

D

Q

K

K

G

G

I

V

R

K

R

I

L

A

S

S

E

D

L

V

N

E

V

T

I

Y

L

L

A

S

I

F

V

L

L

M

A

L

L

G

W

W

V

V

L

F

F

I

S

V

G

G

Q

G

T

A

A

S

H

F

M

I

L

V

D

N

A

Y

L

F

V

T

Q

D

N

S

I

V

G

G

D

T

F

L

S

M

R

Y

F

M

P

P

S

R

M

M

M

L

M

F

N

Y

T

T

F

-

A

-

Y

D

S

P

T

I

G

G

T

K

A

G

D

G

Y

F

P

P

A

Q

E

A

Q

-

W

-

K

-

A

-

D

-

W

W

T

T

L

V

F

F

F

Y

W

W

A

A

W
|
W

I

V

A

I

W

Y

A

A

P

I

F

Q

V

M

S

S

L

I

F

F

L

L

A

A

R

R

I

I

S

S

R

K

G

G

R

R

T

T

L

V

R

R

Q

E

F

L

V

C

I

L

G

G

V

M

L

V

L

S

-

G

I

L

P

T

F

A

S

G

F

T

I

W

L

L

M

I

W

W

V

-

S

T

I

I

F

L

G

G

N

G

A

N

A

T

L

L

S

Q

F

L

F

I

D

-

D

D

Q

Q

E

N

F

I

L

L

N

N

Q

I

A

P

V

Q

E

L

L

I

P

D

E

Q

S

Y

G

G

F

V

-

P

F

R

T

A

L

I

E

E

Q

T

Y

W

P

-

G

-

S

A

T

A

F

L

T

P

I

L

S

S

I

T

A

A

V

T

L

M

T

W

G

G

M

F

F

F

F

I

Y

L

-

C

-

F

-

I

-

A

-

T

V

V

T

T

S

L

A

I

D

N

S

A

G

C

S

S

L

Y

V

T

M

L

A

A

N

M

M

S

T

T

S

C

K

R

P

S

T

M

M

K

N

E

D

G

S

A

D

D

G

P

P

P

P

L

W

L

L

V

R

R

I

I

V

G

W

W

A

S

V

V

I

L

T

V

G

G

A

I

L

I

T

G

L

I

V

I

M

L

L

L

F

A

I

L

D

G

G

G

V

L

Y

K

T

P

L

I

Q

Q

A

T

A

A

T

I

V

I

M

A

V

G

G

G

L

C

P

P

L

L

S

F

I

F

L

V

I

N

Y

I

L

M

V

V

M

T

F

L

S

S

L

F

W

I

K

K

V

D

L

A

K

K

T

V

E

H

binding 3-carboxy-n,n,n-trimethylpropan-1-aminium: W139 (= W170), W315 (= W351), W316 (= W352)

P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
25% identity, 66% coverage: 42:521/725 of query aligns to 19:496/504 of P31553

query
sites
P31553

V

L

I

I

V

V

A

G

F

I

V

L

L

C

W

W

A

L

A

T

I

V

W

R

P

D

-

L

D

D

A

A

S

N

T

V

A

V

I

I

F

N

G

A

A

V

M

F

D

S

W

Y

V

V

A

T

T

N

N

V

F

W

G

G

W

W

Y

A

Y

F

I

E

L

W

T

Y

A

M

T

V

I

V

V

M

V

L

V

F

F

G

V

W

I

F

V

W

V

L

A

V

F

F

S

G

R

P

V

Y

G

A

R

K

T

K

K

R

M

L

G

G

P

-

D

-

H

N

S

E

R

P

P

P

K

E

F

F

N

S

L

T

F

A

T

S

W

W

A

I

A

F

M

M

L

M

F

F

A

A

A

S

G

C

I

T

G

S

V

A

D

A

L

V

M

L

F

F

F

W

G

G

I

-

S

S

G

I

P

E

A

I

T

Y

N
x
Y

Y

Y

L

I

T

S

P

T

P

P

D

P

V

F

G

G

-

L

-

E

A

P

M

N

S

S

D

T

E

G

A

A

A

K

R

E

M

L

A

G

P

L

I

A

W

Y

T

S

I

L

F

F

H

H

Y
x
W

G

G

I

P

P

L

G

P

W

W

A

A

M

T

Y

Y

A

S

L

F

M

L

G

S

M

V

A

A

F

F

G

A

L

Y

F

F

A

F

Y

F

R

V

Y

R

H

K

L

M

P

E

L

V

S

-

I

I

R

R

-

P

-

S

S

S

A

T

L

L

A

V

P

P

I

L

F

V

G

G

-

E

K

K

R

H

I

A

H

K

G

G

A

L

A

F

G

G

H

T

T

I

V

V

E

D

I

N

A

F

A

Y

T

L

I

V

G

A

T

L

I

I

F

F

G

A

I

M

S

G

V

T

S

S

L

L

G

G

I

L

G

A

V

T

V

P

F

L

L

V

N

T

Y

E

G

C

L

M

S

Q

E

W

L

L

F

F

G

G

V

I

P

P

N

H

S

T

L

L

S

Q

V

L

Q

D

I

A

A

I

L

I

M

I

A

T

L

C

A

W

V

I

F

I

I

L

T

N

I

A

A

I

S

C

T

V

V

A

S

C

G

G

V

L

D

Q

K

K

G

G

I

V

R

R

R

I

L

A

S

S

E

D

L

V

N

R

V

S

I

Y

L

L

A

S

I

F

V

L

L

M

A

L

L

G

W

W

V

V

L

F

F

I

S

V

G

S

Q

G

T

A

A

S

H

F

M

I

L

M

D

N

A

Y

L

F

V

T

Q
x
D

N

S

I

V

G

G

D

M

F

L

S
x
M

R

Y

F

L

P

P

S
x
R

M

M

M

L

M

F

N

Y

T
|
T

F

D

A

P

Y

I

S

A

T

K

G

G

T

-

A

-

D

G

Y

F

P

P

A

Q

E

-

Q

-

W

-

K

-

A

-

D
x
G

W
|
W

T

T

L

V

F

F

F

Y

W

W

A

A

W
|
W

I

V

A

I

W
x
Y

A
|
A

P
x
I

F
x
Q

V
x
M

S

S

L

I

F

F

L

L

A

A

R

R

I

I

S

S

R

R

G

G

R

R

T

T

L

V

R

R

Q

E

F

L

V

C

I

F

G

G

V

M

L

V

L

L

-

G

I

L

P

T

F

A

S

S

F

T

I

W

L

I

M

L

W

W

V

-

S

T

I

V

F

L

G

G

N

S

A

N

A

T

L

L

S

L

F

L

F

I

D

D

D

-

Q

-

E

-

F

-

L

-

N

K

Q

N

A

I

V

I

E

N

L

I

P

P

E

N

S

-

G

-

F

-

T

-

L

L

L

I

E

E

Q

Q

Y

Y

-

G

-

V

-

A

-

R

-

A

-

I

-

E

P

T

G

W

S

A

T

A

F

L

T

P

I

L

S

S

I

T

A

A

V

T

L

M

T

W

G

G

M

F

F

F

F

I

Y

L

-

C

-

F

-

I

-

A

-

T

V

V

T

T

S

L

A

V

D

N

S

A

G

C

S

S

L

Y

V

T

M

L

A

A

N

M

M

S

T

T

S

C

K

R

P

E

T

V

M

R

N

D

D

G

S

E

D

E

G

P

P

P

P

L

W

L

L

V

R

R

I

I

V

G

W

W

A

S

V

I

I

L

T

V

G

G

A

I

L

I

T

G

L

I

V

V

M

L

L

L

F

A

I

L

D

G

G

G

V

L

Y

K

T

P

L

I

Q

Q

A

T

A

A

T

I

V

I

M

A

V

G

G

G

L

C

P

P

L

L

S

F

I

F

L

V

I

N

Y

I

L

M

V

V

M

T

F

L

S

S

L

F

W

I

K

K

Y114 (≠ N139) binding 4-(trimethylamino)butanoate; mutation to L: Small decrease in transport activity.
W142 (≠ Y165) binding (R)-carnitine
D288 (≠ Q309) mutation to A: Retains 70% of transport activity. Forms mostly monomers.; mutation to R: Abolishes transport activity. Forms mostly monomers.; mutation to W: Retains 4% of transport activity. Forms mostly monomers.
M295 (≠ S316) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
R299 (≠ S320) mutation to A: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers. Shows a high tendency to aggregate.
T304 (= T325) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
GW 315:316 (≠ DW 343:344) binding 4-(trimethylamino)butanoate
W316 (= W344) mutation to L: Decrease in transport activity.
W323 (= W351) binding 4-(trimethylamino)butanoate; mutation to L: Abolishes transport activity.
WW 323:324 (= WW 351:352) binding (R)-carnitine
W324 (= W352) mutation to L: Abolishes transport activity.
Y327 (≠ W355) mutation to L: Strong decrease in transport activity.
YAIQ 327:330 (≠ WAPF 355:358) binding (R)-carnitine
Q330 (≠ F358) mutation to L: Decrease in transport activity.
M331 (≠ V359) binding 4-(trimethylamino)butanoate

3hfxA Crystal structure of carnitine transporter (see paper)
25% identity, 66% coverage: 42:521/725 of query aligns to 8:485/493 of 3hfxA

query
sites
3hfxA

V

L

I

I

V

V

A

G

F

I

V

L

L

C

W

W

A

L

A

T

I

V

W

R

P

D

-

L

D

D

A

A

S

N

T

V

A

V

I

I

F

N

G

A

A

V

M

F

D

S

W

Y

V

V

A

T

T

N

N

V

F

W

G

G

W

W

Y

A

Y

F

I

E

L

W

T

Y

A

M

T

V

I

V

V

M

V

L

V

F

F

G

V

W

I

F

V

W

V

L

A

V

F

F

S

G

R

P

V

Y

G

A

R

K

T

K

K

R

M

L

G

G

P

-

D

-

H

N

S

E

R

P

P

P

K

E

F

F

N

S

L

T

F

A

T

S

W

W

A

I

A

F

M

M

L

M

F

F

A

A

A

S

G

C

I

T

G

S

V

A

D

A

L

V

M

L

F

F

F

W

G

G

I

-

S

S

G

I

P

E

A

I

T

Y

N
x
Y

Y

Y

L

I

T

S

P

T

P

P

D

P

V

F

G

G

-

L

-

E

A

P

M

N

S

S

D

T

E

G

A

A

A

K

R

E

M

L

A

G

P

L

I

A

W

Y

T

S

I

L

F

F

H

H

Y
x
W

G

G

I

P

P

L

G

P

W

W

A

A

M

T

Y

Y

A

S

L

F

M

L

G

S

M

V

A

A

F

F

G

A

L

Y

F

F

A

F

Y

F

R

V

Y

R

H

K

L

M

P

E

L

V

S

-

I

I

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binding carnitine: Y103 (≠ N139), W131 (≠ Y165), W305 (= W344), W312 (= W351), W313 (= W352), Y316 (≠ W355), Y316 (≠ W355), Q319 (≠ F358), F323 (= F362)

2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
26% identity, 66% coverage: 42:521/725 of query aligns to 12:489/496 of 2wsxA

query
sites
2wsxA

V

L

I

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binding 3-carboxy-n,n,n-trimethylpropan-1-aminium: W135 (≠ Y165), G304 (≠ D334), G308 (≠ D343), W316 (= W351), Y320 (≠ W355), M324 (≠ V359), Q466 (= Q498)

Query Sequence

>WP_075844956.1 NCBI__GCF_001659785.1:WP_075844956.1
MADSAEFAAPESNDTTDGRPDTATTQATHSAVNWPVFAGTSVIIVAFVLWAAIWPDAAST
AIFGAMDWVATNFGWYYILTATIVVVFVIVVAFSRVGRTKMGPDHSRPKFNLFTWAAMLF
AAGIGVDLMFFGISGPATNYLTPPDVGAMSDEAARMAPIWTIFHYGIPGWAMYALMGMAF
GLFAYRYHLPLSIRSALAPIFGKRIHGAAGHTVEIAATIGTIFGISVSLGIGVVFLNYGL
SELFGVPNSLSVQIALMALAVFITIASTVSGVDKGIRRLSELNVILAIVLALWVLFSGQT
AHMLDALVQNIGDFFSRFPSMMMNTFAYSTGTADYPAEQWKADWTLFFWAWWIAWAPFVS
LFLARISRGRTLRQFVIGVLLIPFSFILMWVSIFGNAALSFFDDQEFLNQAVELPESGFF
TLLEQYPGSTFTISIAVLTGMFFYVTSADSGSLVMANMTSKPTMNDSDGPPWLRIVWAVI
TGALTLVMLFIDGVYTLQAATVMVGLPLSILIYLVMFSLWKVLKTEQLGIDSRQATLPTL
LTSRVRDQGERGNWRQRLKHRMSYASETEAADFVSNVASPAIEEVAAEIKSMGFEVSCHR
GSHPDSNIPYIDLVVSFPNSEDFKYQAYPVAYSVPSFATNLAAVRDTYYRVEIFSIHGSR
GRDIMGYTQDQVITDVLDAYDAHIAYLNLSGDGSLATGDVAANVPEEWIDSDRIDPSTTS
EEEHS

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