SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 14452 FitnessBrowser__Keio:14452 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 9 hits to proteins with known functional sites (download)

P54582 Glycine betaine transporter BetP; Glycine betaine permease from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see 6 papers)
35% identity, 75% coverage: 33:541/677 of query aligns to 78:594/595 of P54582

query
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P54582

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W101 (= W56) 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 (= E90) mutation to A: Strongly decreased betaine transport.
G149 (= G104) mutation to A: Decreases betaine transport. No effect on activation by increased osmolality.
M150 (≠ I105) mutation to F: No effect on activation by increased osmolality; when associated with A-152.
G151 (= G106) mutation to A: Nearly abolishes betaine transport.
I152 (= I107) mutation to A: No effect on activation by increased osmolality; when associated with F-150.
IG 152:153 (≠ ID 107:108) binding
G153 (≠ D108) 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 (= F111) mutation to A: Decreases betaine transport, but has no major effect on affinity for glycine betaine.
W189 (≠ Y146) mutation to C: Mildly decreased betaine transport.
W194 (= W151) mutation to L: Strongly decreased betaine transport.
Y197 (= Y154) mutation to L: Nearly abolishes betaine transport.
R210 (= R167) mutation to A: Nearly abolishes betaine transport.
S253 (≠ T209) binding
G301 (= G256) mutation to L: Strongly decreased betaine transport.
N309 (= N264) mutation to A: Decreases affinity for sodium ions.
T351 (≠ S306) 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 (= W315) mutation to C: Strongly decreased betaine transport.
W366 (= W319) mutation to C: No effect on betaine transport.
F369 (= F322) mutation to G: Decreases affinity for glycine betaine. Decreases betaine transport.
W371 (= W324) mutation to L: No effect on betaine transport.
W373 (= W326) mutation to A: Strongly decreases affinity for glycine betaine and betaine transport.
WWISW 373:377 (≠ WWVAW 326:330) binding
W374 (= W327) 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 (= W330) mutation to A: Abolishes betaine transport.; mutation to L: Nearly abolishes betaine transport.
F380 (= F333) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
F384 (= F337) mutation to A: Decreases betaine transport, but has no effect on affinity for glycine betaine.
R387 (= R340) mutation to A: Mildly decreased betaine transport.
R392 (= R345) mutation to K: Moderately decreased betaine transport.

4llhA Substrate bound outward-open state of the symporter betp (see paper)
36% identity, 70% coverage: 33:508/677 of query aligns to 22:497/524 of 4llhA

query
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binding 2-(trimethyl-lambda~5~-arsanyl)ethanol: M94 (≠ I105), G95 (= G106), D97 (= D108), W314 (= W326), W315 (= W327), W318 (= W330)
binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: R495 (= R506)
binding sodium ion: A91 (= A102), M94 (≠ I105), G95 (= G106), F405 (= F420), T408 (= T423), S409 (= S424)

Sites not aligning to the query:

binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: 499

3p03C Crystal structure of betp-g153d with choline bound (see paper)
36% identity, 70% coverage: 33:508/677 of query aligns to 22:496/508 of 3p03C

query
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G

A

Y

Y

F

S

S

T

Y

F

R

R

Y

V

N

G

L

R

P

K

L

Q

T

L

I

L

R

S

S

S

A

A

L

F

Y

V

P

P

I

L

F

I

G

G

K

E

R

K

-

G

I

A

N

E

G

G

P

W

I

L

G

G

H

K

S

L

V

I

D

D

I

I

A

L

A

A

V

I

I

I

G

A

T

T

I

V

F

F

G

G

I

T

A

A

T

C

T

S

L

L

G

G

I

L

G

G

V

A

V

L

Q

Q

L

I

N

G

Y

A

G

G

L

L

S

S

V

A

L

A

F

N

D

I

I

I

P

D

D

W

S

T

M

I

A

V

A

G

K

I

A

V

A

S

L

V

I

L

A

T

L

L

S

A

V

F

I

I

I

F

A

S

T

A

I

I

S

S

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-

T

-

S

-

G

G

V

V

D

G

K

K

G

G

I

I

R

Q

V

Y

L

L

S

S

E

N

L

A

N

N

V

M

A

V

L

L

A

A

L

A

G

L

L

L

I

A

L

I

F

F

V

V

L

F

F

V

M

V

G

G

D

P

T

T

S

V

F

S

L

I

L

L

N

N

A

L

L

L

V

P

L

G

N

S

V

I

G

G

D

N

Y

Y

V

L

N

S

R

N

F

F

M

F

G

Q

M

M

T

A

L

G

N

R

S

T

F

A

-

M

-

S

A

A

F

D

D

G

R

T

P

A

V

G

E

E

W

W

M

L

N

G

N

S

W

W

T

T

L

I

F

F

F

Y

W

W

A

A

W

W

V

I

A

S

W

W

S

S

P

P

F
|
F

V

V

G

G

L

M

F

F

L

L

A

A

R

R

I

I

S

S

R

R

G

G

R

R

T

S

I

I

R

R

Q

E

F

F

V

I

L

L

G

G

T

V

L

L

I

L

I

V

P

P

F

A

T

G

F

V

T

S

L

T

L

V

W

W

L

F

S

S

V

I

F

F

G

G

N

G

S

T

A

A

L

I

Y

V

E

F

I

E

I

Q

H

N

G

G

G

E

A

S

A

I

F

W

A

G

E

D

E

G

A

A

M

-

V

-

H

-

P

A

E

E

R

E

G

Q

F

L

Y

F

S

G

L

L

A

H

Q

A

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L

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P

A

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F

G

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F

I

S

M

A

G

S

I

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I

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M

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L

L

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F

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D

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A

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V

L

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G

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F

M

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S

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Q

H

L

G

K

Q

D

-

I

-

N

-

S

L

D

E

A

A

P

N

G

K

W

W

L

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R

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V

A

F

A

W

W

S

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V

A

A

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T

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A

L

A

L

I

T

G

L

L

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M

L

L

L

M

L

T

S

-

G

-

D

N

N

G

A

I

L

S

S

A

N

L

L

Q

Q

N

N

T

V

T

T

V

I

I

V

M

A

G

A

L

T

P

P

F

F

S

L

F

F

V

V

I

V

F

I

F

G

V

L

M

M

A

F

G

A

L

L

Y

V

K

K

S

D

L

L

K

S

V

N

E

D

-

V

-

I

-

Y

-

L

D

E

Y

Y

R

R

R

E

E

Q

binding choline ion: A92 (= A103), M94 (≠ I105), D97 (= D108), F320 (= F333)

2wswA Crystal structure of carnitine transporter from proteus mirabilis (see paper)
27% identity, 74% coverage: 5:503/677 of query aligns to 5:506/508 of 2wswA

query
sites
2wswA

S

S

H

H

S

M

R

K

E

D

K

N

D

K

K

K

-

A

-

G

I

I

N

E

P

P

V

K

V

V

F

F

Y

F

T

P

S

P

A

L

G

I

L

I

I

V

L

G

L

I

F

L

S

C

L

W

T

L

T

T

I

V

L

R

F

D

R

L

D

D

F

A

S

S

A

N

L

E

W

V

I

I

G

N

R

A

T

V

L

F

D

S

W

Y

V

V

S

T

K

N

T

V

F

W

G

G

W

W

Y

A

Y

F

-

E

-

W

-

Y

-

M

-

V

-

I

L

M

L

F

A

G

T

W

L
x
F

Y

W

I

L

V

V

F
|
F

V

-

C

-

I

-

A

-

C

-

S

G

R
|
R

F

Y

G

A

S

K

V

K

K

R

L

L

G

G

P

D

E

E

Q

-

S

-

K

K

P

P

E

E

F

F

S

S

L

T

L

A

S

S

W

W

A

I

A

F

M

M

L

M

F

F

A

A

A

S

G

C

I

T

G

S

I

A

D

A

L

V

M

L

F

F

F

W

S

G

V

S

A

I

E

E

P

I

V

Y

T

Y

Q

Y

Y

I

M

S

Q

S

P

P

E

F

G

G

-

M

A

E

G

G

Q

Y

T

S

I

A

E

P

A

A

A

K

R

E

Q

I

A

G

M

L

V

A

W

Y

T

S

L

L

F

F

H

H

Y

W

G

G

L

P

T

L

G

P

W

W

S

A

M

T

Y

Y

A

S

L

F

M

L

G

S

M

V

A

A

L

F

G

A

Y

Y

F

F

S

F

Y

F

R

V

Y

R

N

K

L

M

P

E

L

V

T

-

I

I

R

R

-

P

-

S

S

S

A

T

L

L

Y

V

P

P

I

L

F

V

G

G

-

E

K

K

R

H

I

V

N

N

G

G

P

L

I

F

G

G

H

T

S

V

V

V

D

D

I

N

A

F

A

Y

V

L

I

V

G

A

T

L

I

I

F

L

G

A

I

M

A

G

T

T

T

S

L

L

G

G

I

L

G

A

V

T

V

P

Q

L

L

V

N

T

Y

E

G

C

L

I

S

Q

V

Y

L

L

F

F

D

G

I

I

P

P

D

H

S

T

M

L

A

Q

A

L

K

D

A

A

A

I

L

I

I

I

A

S

L

C

S

W

V

I

I

L

A

N

T

A

I

I

S

C

V

V

T

A

S

F

G

G

V

L

D

Q

K

K

G

G

I

V

R

K

V

I

L

A

S

S

E

D

L

V

N

R

V

T

A

Y

L

L

A

S

L

F

G

L

L

M

I

L

L

G

F

W

V

V

L

F

F

I

M

V

G

G

D

G

T

A

S

S

F

F

L

I

L

V

N

N

A

Y

L

F

V

T

L

D

N

S

V

V

G

G

D

T

-

L

-

M

Y

Y

V

M

N

P

R

R

F

M

M

L

G

F

M

Y

T

T

-

D

-

P

L

I

N

G

S

K

F

G

A

G

F

F

D

P

R

Q

P

-

V

-

E

-

W

-

M

-

N

-

N

A

W

W

T

T

L

V

F

F

F

Y

W

W

A

A

W

W

V

V

A

I

W

Y

S

A

P

I

F

Q

V

M

G

S

L

I

F

F

L

L

A

A

R

R

I

I

S

S

R

K

G

G

R

R

T

T

I

V

R

R

Q

E

F

L

V

C

L

L

G

G

T

M

L

V

I

S

I

G

P

L

F

T

T

A

F

G

T

T

L

W

L

L

W

I

L

W

S

T

V

I

F

L

G

G

N

G

S

N

A

T

L

L

Y

Q

E

L

I

I

-

D

-

Q

-

N

I

I

H

L

G

N

G

I

A

P

A

Q

F

L

A

I

E

D

E

Q

A

Y

M

G

V

V

H

-

P

-

E

P

R

R

G

A

F

I

Y

I

S

E

L

T

L

W

A

A

Q

A

Y

L

P

P

A

L

F

S

T

T

F

A

S

T

A

M

S

W

V

G

A

F

T

F

I

I

T

L

G

C

L

F

L

I

F

A

Y

T

V

V

T

T

S

L

A

I

D

N

S

A

G

C

A

S

L

Y

V

T

L

L

G

A

N

M

F

S

T

T

S

C

Q

R

L

S

K

M

D

K

I

E

N

G

S

A

D

D

A

P

P

P

G

L

W

L

L

V

R

R

V

I

F

G

W

W

S

S

V

V

A

L

I

V

G

G

L

I

T

G

L

I

G

I

M

L

L

L

M

A

T

L

N

G

G

G

I

L

S

K

A

P

L

I

Q

Q

N

T

T

A

T

I

V

I

I

A

M

G

G

G

L

C

P

P

F

L

S

F

F

F

V

V

I

N

F

I

F

M

V

V

M

T

A

L

G

S

L

F

Y

I

K

K

S

D

L

A

K

K

V

V

E

H

binding 5-cyclohexyl-1-pentyl-beta-d-maltoside: F72 (≠ L64), F76 (= F68), R78 (= R76)

B4EY22 L-carnitine/gamma-butyrobetaine antiporter from Proteus mirabilis (strain HI4320) (see 2 papers)
27% identity, 74% coverage: 4:503/677 of query aligns to 1:501/514 of B4EY22

query
sites
B4EY22

L

M

S

S

H

K

S

D

R

N

E

K

K

K

D

A

K

G

I

I

N

E

P

P

V

K

V

V

F

F

Y

F

T

P

S

P

A

L

G

I

L

I

I

V

L

G

L

I

F

L

S

C

L

W

T

L

T

T

I

V

L

R

F

D

R

L

D

D

F

A

S

S

A

N

L

E

W

V

I

I

G

N

R

A

T

V

L

F

D

S

W

Y

V

V

S

T

K

N

T

V

F

W

G

G

W

W

Y

A

Y

F

-

E

-

W

-

Y

-

M

-

V

-

I

L

M

L

F

A

G

T

W

L

F

Y

W

I

L

V

V

F

F

V

-

C

-

I

-

A

-

C

-

S

G

R

R

F

Y

G

A

S

K

V

K

K

R

L

L

G

G

P

D

E

E

Q

-

S

-

K

K

P

P

E

E

F

F

S

S

L

T

L

A

S

S

W

W

A

I

A

F

M

M

L

M

F

F

A

A

A

S

G

C

I

T

G

S

I

A

D

A

L

V

M

L

F

F

F

W

S

G

V

S

A

I

E
|
E

P

I

V

Y

T

Y

Q

Y

Y

I

M

S

Q

S

P

P

E

F

G

G

-

M

A

E

G

G

Q

Y

T

S

I

A

E

P

A

A

A

K

R

E

Q

I

A

G

M

L

V

A

W

Y

T

S

L

L

F

F

H

H

Y

W

G

G

L

P

T

L

G

P

W

W

S

A

M

T

Y

Y

A

S

L

F

M

L

G

S

M

V

A

A

L

F

G

A

Y

Y

F

F

S

F

Y

F

R

V

Y

R

N

K

L

M

P

E

L

V

T

-

I

I

R

R

-

P

-

S

S

S

A

T

L

L

Y

T

P

P

I

L

F

V

G

G

-

E

K

K

R

H

I

V

N

N

G

G

P

L

I

F

G

G

H

T

S

V

V

V

D

D

I

N

A

F

A

Y

V

L

I

V

G

A

T

L

I

I

F

L

G

A

I

M

A

G

T

T

T

S

L

L

G

G

I

L

G

A

V

T

V

P

Q

L

L

V

N

T

Y

E

G

C

L

I

S

Q

V

Y

L

L

F

F

D

G

I

I

P

P

D

H

S

T

M

L

A

Q

A

L

K

D

A

A

A

I

L

I

I

I

A

S

L

C

S

W

V

I

I

L

A

N

T

A

I

I

S

C

V

V

T

A

S

F

G

G

V

L

D

Q

K

K

G

G

I

V

R

K

V

I

L

A

S

S

E

D

L

V

N
x
R

V

T

A

Y

L

L

A

S

L

F

G

L

L

M

I

L

L

G

F

W

V

V

L

F

F

I

M

V

G

G

D

G

T

A

S

S

F

F

L

I

L

V

N

N

A

Y

L

F

V

T

L

D

N

S

V

V

G

G

D

T

-

L

-

M

Y

Y

V

M

N

P

R

R

F

M

M

L

G

F

M

Y

T

T

-

D

-

P

L

I

N

G

S

K

F

G

A

G

F

F

D

P

R

Q

P

-

V

-

E

-

W

-

M

-

N

-

N

A

W
|
W

T

T

L

V

F

F

F

Y

W

W

A

A

W

W

V

V

A

I

W

Y

S

A

P

I

F

Q

V
x
M

G

S

L

I

F

F

L

L

A

A

R

R

I

I

S

S

R

K

G

G

R

R

T

T

I

V

R

R

Q

E

F

L

V

C

L

L

G

G

T

M

L

V

I

S

I

G

P

L

F

T

T

A

F

G

T

T

L

W

L

L

W

I

L

W

S

T

V

I

F

L

G

G

N

G

S

N

A

T

L

L

Y

Q

E

L

I

I

-

D

-

Q

-

N

I

I

H

L

G

N

G

I

A

P

A

Q

F

L

A

I

E

D

E

Q

A

Y

M

G

V

V

H

-

P

-

E

P

R

R

G

A

F

I

Y

I

S

E

L

T

L

W

A

A

Q

A

Y

L

P

P

A

L

F

S

T

T

F

A

S

T

A

M

S

W

V

G

A

F

T

F

I

I

T

L

G

C

L

F

L

I

F

A

Y

T

V

V

T

T

S

L

A

I

D

N

S

A

G

C

A

S

L

Y

V

T

L

L

G

A

N

M

F

S

T

T

S

C

Q

R

L

S

K

M

D

K

I

E

N

G

S

A

D

E

A

P

P

P

G

L

W

L

L

V

R

R

V

I

F

G

W

W

S

S

V

V

A

L

I

V

G

G

L

I

T

G

L

I

G

I

M

L

L

L

M

A

T

L

N

G

G

G

I

L

S

K

A

P

L

I

Q

Q

N

T

T

A

T

I

V

I

I

A

M

G

G

G

L

C

P

P

F

L

S

F

F

F

V

V

I

N

F

I

F

M

V

V

M

T

A

L

G

S

L

F

Y

I

K

K

S

D

L

A

K

K

V

V

E

H

E111 (= E116) mutation to A: Abolishes transport activity.
R262 (≠ N264) mutation R->A,E: Strong decrease in L-carnitine transport. Mutant is Na(+)-dependent for substrate binding and transport.
W316 (= W319) mutation to A: 2.5-fold decrease in Vmax.
M331 (≠ V334) mutation to V: 10-fold decrease in Vmax.

4m8jA Crystal structure of cait r262e bound to gamma-butyrobetaine (see paper)
27% identity, 73% coverage: 13:503/677 of query aligns to 2:493/495 of 4m8jA

query
sites
4m8jA

I

I

N

E

P

P

V

K

V

V

F

F

Y

F

T

P

S

P

A

L

G

I

L

I

I

V

L

G

L

I

F

L

S

C

L

W

T

L

T

T

I

V

L

R

F

D

R

L

D

D

F

A

S

S

A

N

L

E

W

V

I

I

G

N

R

A

T

V

L

F

D

S

W

Y

V

V

S

T

K

N

T

V

F

W

G

G

W

W

Y

A

Y

F

-

E

-

W

-

Y

-

M

-

V

-

I

L

M

L

F

A

G

T

W

L

F

Y

W

I

L

V

V

F

F

V

-

C

-

I

-

A

-

C

-

S

G

R

R

F

Y

G

A

S

K

V

K

K

R

L

L

G

G

P

D

E

E

Q

-

S

-

K

K

P

P

E

E

F

F

S

S

L

T

L

A

S

S

W

W

A

I

A

F

M

M

L

M

F

F

A

A

A

S

G

C

I

T

G

S

I

A

D

A

L

V

M

L

F

F

F

W

S

G

V

S

A

I

E

E

P

I

V

Y

T

Y

Q

Y

Y

I

M

S

Q

S

P

P

E

F

G

G

-

M

A

E

G

G

Q

Y

T

S

I

A

E

P

A

A

A

K

R

E

Q

I

A

G

M

L

V

A

W

Y

T

S

L

L

F

F

H

H

Y

W

G

G

L

P

T

L

G

P

W
|
W

S

A

M

T

Y

Y

A

S

L

F

M

L

G

S

M

V

A

A

L

F

G

A

Y

Y

F

F

S

F

Y

F

R

V

Y

R

N

K

L

M

P

E

L

V

T

-

I

I

R

R

-

P

-

S

S

S

A

T

L

L

Y

V

P

P

I

L

F

V

G

G

-

E

K

K

R

H

I

V

N

N

G

G

P

L

I

F

G

G

H

T

S

V

V

V

D

D

I

N

A

F

A

Y

V

L

I

V

G

A

T

L

I

I

F

L

G

A

I

M

A

G

T

T

T

S

L

L

G

G

I

L

G

A

V

T

V

P

Q

L

L

V

N

T

Y

E

G

C

L

I

S

Q

V

Y

L

L

F

F

D

G

I

I

P

P

D

H

S

T

M

L

A

Q

A

L

K

D

A

A

A

I

L

I

I

I

A

S

L

C

S

W

V

I

I

L

A

N

T

A

I

I

S

C

V

V

T

A

S

F

G

G

V

L

D

Q

K

K

G

G

I

V

R

K

V

I

L

A

S

S

E

D

L

V

N

E

V

T

A

Y

L

L

A

S

L

F

G

L

L

M

I

L

L

G

F

W

V

V

L

F

F

I

M

V

G

G

D

G

T

A

S

S

F

F

L

I

L

V

N

N

A

Y

L

F

V

T

L

D

N

S

V

V

G

G

D

T

-

L

-

M

Y

Y

V

M

N

P

R

R

F

M

M

L

G

F

M

Y

T

T

-

D

-

P

L

I

N

G

S

K

F

G

A

G

F

F

D

P

R

Q

P

-

V

-

E

-

W

-

M

-

N

-

N

A

W

W

T

T

L

V

F

F

F

Y

W

W

A

A

W
|
W

V

V

A

I

W

Y

S

A

P

I

F

Q

V

M

G

S

L

I

F

F

L

L

A

A

R

R

I

I

S

S

R

K

G

G

R

R

T

T

I

V

R

R

Q

E

F

L

V

C

L

L

G

G

T

M

L

V

I

S

I

G

P

L

F

T

T

A

F

G

T

T

L

W

L

L

W

I

L

W

S

T

V

I

F

L

G

G

N

G

S

N

A

T

L

L

Y

Q

E

L

I

I

-

D

-

Q

-

N

I

I

H

L

G

N

G

I

A

P

A

Q

F

L

A

I

E

D

E

Q

A

Y

M

G

V

V

H

-

P

-

E

P

R

R

G

A

F

I

Y

I

S

E

L

T

L

W

A

A

Q

A

Y

L

P

P

A

L

F

S

T

T

F

A

S

T

A

M

S

W

V

G

A

F

T

F

I

I

T

L

G

C

L

F

L

I

F

A

Y

T

V

V

T

T

S

L

A

I

D

N

S

A

G

C

A

S

L

Y

V

T

L

L

G

A

N

M

F

S

T

T

S

C

Q

R

L

S

K

M

D

K

I

E

N

G

S

A

D

D

A

P

P

P

G

L

W

L

L

V

R

R

V

I

F

G

W

W

S

S

V

V

A

L

I

V

G

G

L

I

T

G

L

I

G

I

M

L

L

L

M

A

T

L

N

G

G

G

I

L

S

K

A

P

L

I

Q

Q

N

T

T

A

T

I

V

I

I

A

M

G

G

G

L

C

P

P

F

L

S

F

F

F

V

V

I

N

F

I

F

M

V

V

M

T

A

L

G

S

L

F

Y

I

K

K

S

D

L

A

K

K

V

V

E

H

binding 3-carboxy-n,n,n-trimethylpropan-1-aminium: W139 (= W151), W315 (= W326), W316 (= W327)

P31553 L-carnitine/gamma-butyrobetaine antiporter from Escherichia coli (strain K12) (see 3 papers)
26% identity, 74% coverage: 4:501/677 of query aligns to 1:499/504 of P31553

query
sites
P31553

L

M

S

K

H

N

S

E

R

K

E

R

K

K

D

T

K

G

I

I

N

E

P

P

V

K

V

V

F

F

Y

F

T

P

S

P

A

L

G

I

L

I

I

V

L

G

L

I

F

L

S

C

L

W

T

L

T

T

I

V

L

R

F

D

R

L

D

D

F

A

S

A

A

N

L

V

W

V

I

I

G

N

R

A

T

V

L

F

D

S

W

Y

V

V

S

T

K

N

T

V

F

W

G

G

W

W

Y

A

Y

F

-

E

-

W

-

Y

-

M

-

V

L

M

L

L

A

F

A

G

T

W

L

F

Y

W

I

L

V

V

F

F

V

-

C

-

I

-

A

-

C

-

S

G

R

P

F

Y

G

A

S

K

V

K

K

R

L

L

G

G

P

N

E

E

Q

-

S

-

K

P

P

P

E

E

F

F

S

S

L

T

L

A

S

S

W

W

A

I

A

F

M

M

L

M

F

F

A

A

A

S

G

C

I

T

G

S

I

A

D

A

L

V

M

L

F

F

F

W

S

G

V

S

A

I

E

E

P

I

V

Y

T
x
Y

Q

Y

Y

I

M

S

Q

T

P

P

E

F

G

G

A

L

G

E

Q

P

T

N

I

S

E

T

A

G

A

A

R

K

Q

E

-

L

A

G

M

L

V

A

W

Y

T

S

L

L

F

F

H

H

Y
x
W

G

G

L

P

T

L

G

P

W

W

S

A

M

T

Y

Y

A

S

L

F

M

L

G

S

M

V

A

A

L

F

G

A

Y

Y

F

F

S

F

Y

F

R

V

Y

R

N

K

L

M

P

E

L

V

T

-

I

I

R

R

-

P

-

S

S

S

A

T

L

L

Y

V

P

P

I

L

F

V

G

G

-

E

K

K

R

H

I

A

N

K

G

G

P

L

I

F

G

G

H

T

S

I

V

V

D

D

I

N

A

F

A

Y

V

L

I

V

G

A

T

L

I

I

F

F

G

A

I

M

A

G

T

T

T

S

L

L

G

G

I

L

G

A

V

T

V

P

Q

L

L

V

N

T

Y

E

G

C

L

M

S

Q

V

W

L

L

F

F

D

G

I

I

P

P

D

H

S

T

M

L

A

Q

A

L

K

D

A

A

A

I

L

I

I

I

A

T

L

C

S

W

V

I

I

I

I

L

A

N

T

A

I

I

S

C

V

V

T

A

S

C

G

G

V

L

D

Q

K

K

G

G

I

V

R

R

V

I

L

A

S

S

E

D

L

V

N

R

V

S

A

Y

L

L

A

S

L

F

G

L

L

M

I

L

L

G

F

W

V

V

L

F

F

I

M

V

G

S

D

G

T

A

S

S

F

F

L

I

L

M

N

N

A

Y

L

F

V

T

L
x
D

N

S

V

V

G

G

D

M

-

L

-
x
M

Y

Y

V

L

N

P

R
|
R

F

M

M

L

G

F

M

Y

T
|
T

L

D

N

P

S

I

F

A

A

K

F

G

D

G

R

F

P

P

V

-

E

-

W

-

M

-

N

Q

N
x
G

W
|
W

T

T

L

V

F

F

F

Y

W

W

A

A

W
|
W

V

V

A

I

W
x
Y

S
x
A

P
x
I

F
x
Q

V
x
M

G

S

L

I

F

F

L

L

A

A

R

R

I

I

S

S

R

R

G

G

R

R

T

T

I

V

R

R

Q

E

F

L

V

C

L

F

G

G

T

M

L

V

I

L

I

G

P

L

F

T

T

A

F

S

T

T

L

W

L

I

W

L

L

W

S

T

V

V

F

L

G

G

N

S

S

N

A

T

L

L

Y

L

E

L

I

I

-

D

-

K

-

N

I

I

H

I

G

N

G

I

A

P

A

N

F

L

A

I

E

E

E

Q

A

Y

M

G

V

V

H

-

P

-

E

A

R

R

G

A

F

I

Y

I

S

E

L

T

L

W

A

A

Q

A

Y

L

P

P

A

L

F

S

T

T

F

A

S

T

A

M

S

W

V

G

A

F

T

F

I

I

T

L

G

C

L

F

L

I

F

A

Y

T

V

V

T

T

S

L

A

V

D

N

S

A

G

C

A

S

L

Y

V

T

L

L

G

A

N

M

F

S

T

T

S

C

Q

R

L

E

K

V

D

R

I

D

N

G

S

E

D

E

A

P

P

P

G

L

W

L

L

V

R

R

V

I

F

G

W

W

S

S

V

I

A

L

I

V

G

G

L

I

T

G

L

I

G

V

M

L

L

L

M

A

T

L

N

G

G

G

I

L

S

K

A

P

L

I

Q

Q

N

T

T

A

T

I

V

I

I

A

M

G

G

G

L

C

P

P

F

L

S

F

F

F

V

V

I

N

F

I

F

M

V

V

M

T

A

L

G

S

L

F

Y

I

K

K

S

D

L

A

K

K

Y114 (≠ T119) binding ; mutation to L: Small decrease in transport activity.
W142 (≠ Y146) binding
D288 (≠ L290) 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 (vs. gap) mutation to E: Does not affect transport activity. Forms mostly monomers. Can also form small amounts of homodimers and homotrimers.
R299 (= R298) 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 (= T303) mutation to A: Does not affect transport activity. Forms mostly monomers. Shows a high tendency to aggregate.
GW 315:316 (≠ NW 318:319) binding
W316 (= W319) mutation to L: Decrease in transport activity.
W323 (= W326) binding ; mutation to L: Abolishes transport activity.
WW 323:324 (= WW 326:327) binding
W324 (= W327) mutation to L: Abolishes transport activity.
Y327 (≠ W330) mutation to L: Strong decrease in transport activity.
YAIQ 327:330 (≠ WSPF 330:333) binding
Q330 (≠ F333) mutation to L: Decrease in transport activity.
M331 (≠ V334) binding

2wsxA Crystal structure of carnitine transporter from escherichia coli (see paper)
26% identity, 72% coverage: 13:501/677 of query aligns to 3:492/496 of 2wsxA

query
sites
2wsxA

I

I

N

E

P

P

V

K

V

V

F

F

Y

F

T

P

S

P

A

L

G

I

L

I

I

V

L

G

L

I

F

L

S

C

L

W

T

L

T

T

I

V

L

R

F

D

R

L

D

D

F

A

S

A

A

N

L

V

W

V

I

I

G

N

R

A

T

V

L

F

D

S

W

Y

V

V

S

T

K

N

T

V

F

W

G

G

W

W

Y

A

Y

F

-

E

-

W

-

Y

-

M

-

V

L

M

L

L

A

F

A

G

T

W

L

F

Y

W

I

L

V

V

F

F

V

-

C

-

I

-

A

-

C

-

S

G

R

P

F

Y

G

A

S

K

V

K

K

R

L

L

G

G

P

E

E

E

Q

-

S

-

K

P

P

P

E

E

F

F

S

S

L

T

L

A

S

S

W

W

A

I

A

F

M

M

L

M

F

F

A

A

A

S

G

C

I

T

G

S

I

A

D

A

L

V

M

L

F

F

F

W

S

G

V

S

A

I

E

E

P

I

V

Y

T

Y

Q

Y

Y

I

M

S

Q

T

P

P

E

F

G

G

A

L

G

E

Q

P

T

N

I

S

E

T

A

G

A

A

R

K

Q

E

-

L

A

G

M

L

V

A

W

Y

T

S

L

L

F

F

H

H

Y
x
W

G

G

L

P

T

L

G

P

W

W

S

A

M

T

Y

Y

A

S

L

F

M

L

G

S

M

V

A

A

L

F

G

A

Y

Y

F

F

S

F

Y

F

R

V

Y

R

N

K

L

M

P

E

L

V

T

-

I

I

R

R

-

P

-

S

S

S

A

T

L

L

Y

V

P

P

I

L

F

V

G

G

-

E

K

K

R

H

I

A

N

K

G

G

P

L

I

F

G

G

H

T

S

I

V

V

D

D

I

N

A

F

A

Y

V

L

I

V

G

A

T

L

I

I

F

F

G

A

I

M

A

G

T

T

T

S

L

L

G

G

I

L

G

A

V

T

V

P

Q

L

L

V

N

T

Y

E

G

C

L

M

S

Q

V

W

L

L

F

F

D

G

I

I

P

P

D

H

S

T

M

L

A

Q

A

L

K

D

A

A

A

I

L

I

I

I

A

T

L

C

S

W

V

I

I

I

I

L

A

N

T

A

I

I

S

C

V

V

T

A

S

C

G

G

V

L

D

Q

K

K

G

A

I

V

R

R

V

I

L

A

S

S

E

D

L

V

N

R

V

S

A

Y

L

L

A

S

L

F

G

L

L

M

I

L

L

G

F

W

V

V

L

F

F

I

M

V

G

S

D

G

T

A

S

S

F

F

L

I

L

M

N

N

A

Y

L

F

V

T

L

D

N

S

V

V

G

G

D

M

-

L

-

M

Y

Y

V

L

N

P

R

R

F

M

M

L

G

F

M

Y

T

T

L

D

N

P

S

I

F

A

A

K

F

G

D
x
G

R

F

P

P

V

-

E

-

W

-

M

-

N

Q

N
x
G

W

W

T

T

L

V

F

F

F

Y

W

W

A

A

W
|
W

W

W

V

V

A

I

W
x
Y

S

A

P

I

F

Q

V
x
M

G

S

L

I

F

F

L

L

A

A

R

R

I

I

S

S

R

R

G

G

R

R

T

T

I

V

R

R

Q

E

F

L

V

C

L

F

G

G

T

M

L

V

I

L

I

G

P

L

F

T

T

A

F

S

T

T

L

W

L

I

W

L

L

W

S

T

V

V

F

L

G

G

N

S

S

N

A

T

L

L

Y

L

E

L

I

I

-

D

-

K

-

N

I

I

H

L

G

N

G

I

A

P

A

N

F

L

A

I

E

E

E

Q

A

Y

M

G

V

V

H

-

P

-

E

A

R

R

G

A

F

I

Y

I

S

E

L

T

L

W

A

A

Q

A

Y

L

P

P

A

L

F

S

T

T

F

A

S

T

A

M

S

W

V

G

A

F

T

F

I

I

T

L

G

C

L

F

L

I

F

A

Y

T

V

V

T

T

S

L

A

V

D

N

S

A

G

C

A

S

L

Y

V

T

L

L

G

A

N

M

F

S

T

T

S

C

Q

R

L

E

K

V

D

R

I

D

N

G

S

E

D

D

A

P

P

P

G

L

W

L

L

V

R

R

V

I

F

G

W

W

S

S

V

I

A

L

I

V

G

G

L

I

T

G

L

I

G

V

M

L

L

L

M

A

T

L

N

G

G

G

I

L

S

K

A

P

L

I

Q
|
Q

N

T

T

A

T

I

V

I

I

A

M

G

G

G

L

C

P

P

F

L

S

F

F

F

V

V

I

N

F

I

F

M

V

V

M

T

A

L

G

S

L

F

Y

I

K

K

S

D

L

A

K

K

binding 3-carboxy-n,n,n-trimethylpropan-1-aminium: W135 (≠ Y146), G304 (≠ D310), G308 (≠ N318), W316 (= W326), Y320 (≠ W330), M324 (≠ V334), Q466 (= Q475)

3hfxA Crystal structure of carnitine transporter (see paper)
26% identity, 72% coverage: 15:501/677 of query aligns to 1:488/493 of 3hfxA

query
sites
3hfxA

P

P

V

K

V

V

F

F

Y

F

T

P

S

P

A

L

G

I

L

I

I

V

L

G

L

I

F

L

S

C

L

W

T

L

T

T

I

V

L

R

F

D

R

L

D

D

F

A

S

A

A

N

L

V

W

V

I

I

G

N

R

A

T

V

L

F

D

S

W

Y

V

V

S

T

K

N

T

V

F

W

G

G

W

W

Y

A

Y

F

-

E

-

W

-

Y

-

M

-

V

L

M

L

L

A

F

A

G

T

W

L

F

Y

W

I

L

V

V

F

F

V

-

C

-

I

-

A

-

C

-

S

G

R

P

F

Y

G

A

S

K

V

K

K

R

L

L

G

G

P

N

E

E

Q

-

S

-

K

P

P

P

E

E

F

F

S

S

L

T

L

A

S

S

W

W

A

I

A

F

M

M

L

M

F

F

A

A

A

S

G

C

I

T

G

S

I

A

D

A

L

V

M

L

F

F

F

W

S

G

V

S

A

I

E

E

P

I

V

Y

T
x
Y

Q

Y

Y

I

M

S

Q

T

P

P

E

F

G

G

A

L

G

E

Q

P

T

N

I

S

E

T

A

G

A

A

R

K

Q

E

-

L

A

G

M

L

V

A

W

Y

T

S

L

L

F

F

H

H

Y
x
W

G

G

L

P

T

L

G

P

W

W

S

A

M

T

Y

Y

A

S

L

F

M

L

G

S

M

V

A

A

L

F

G

A

Y

Y

F

F

S

F

Y

F

R

V

Y

R

N

K

L

M

P

E

L

V

T

-

I

I

R

R

-

P

-

S

S

S

A

T

L

L

Y

V

P

P

I

L

F

V

G

G

-

E

K

K

R

H

I

A

N

K

G

G

P

L

I

F

G

G

H

T

S

I

V

V

D

D

I

N

A

F

A

Y

V

L

I

V

G

A

T

L

I

I

F

F

G

A

I

M

A

G

T

T

T

S

L

L

G

G

I

L

G

A

V

T

V

P

Q

L

L

V

N

T

Y

E

G

C

L

M

S

Q

V

W

L

L

F

F

D

G

I

I

P

P

D

H

S

T

M

L

A

Q

A

L

K

D

A

A

A

I

L

I

I

I

A

T

L

C

S

W

V

I

I

I

I

L

A

N

T

A

I

I

S

C

V

V

T

A

S

C

G

G

V

L

D

Q

K

K

G

G

I

V

R

R

V

I

L

A

S

S

E

D

L

V

N

R

V

S

A

Y

L

L

A

S

L

F

G

L

L

M

I

L

L

G

F

W

V

V

L

F

F

I

M

V

G

S

D

G

T

A

S

S

F

F

L

I

L

M

N

N

A

Y

L

F

V

T

L

D

N

S

V

V

G

G

D

M

-

L

-

M

Y

Y

V

L

N

P

R

R

F

M

M

L

G

F

M

Y

T

T

L

D

N

P

S

I

F

A

A

K

F

G

D

G

R

F

P

P

V

-

E

-

W

-

M

-

N

Q

N

G

W
|
W

T

T

L

V

F

F

F

Y

W

W

A

A

W
|
W

V

V

A

I

W
x
Y

S

A

P

I

F
x
Q

V

M

G

S

L

I

F
|
F

L

L

A

A

R

R

I

I

S

S

R

R

G

G

R

R

T

T

I

V

R

R

Q

E

F

L

V

C

L

F

G

G

T

M

L

V

I

L

I

G

P

L

F

T

T

A

F

S

T

T

L

W

L

I

W

L

L

W

S

T

V

V

F

L

G

G

N

S

S

N

A

T

L

L

Y

L

E

L

I

I

-

D

-

K

-

N

I

I

H

I

G

N

G

I

A

P

A

N

F

L

A

I

E

E

E

Q

A

Y

M

G

V

V

H

-

P

-

E

A

R

R

G

A

F

I

Y

I

S

E

L

T

L

W

A

A

Q

A

Y

L

P

P

A

L

F

S

T

T

F

A

S

T

A

M

S

W

V

G

A

F

T

F

I

I

T

L

G

C

L

F

L

I

F

A

Y

T

V

V

T

T

S

L

A

V

D

N

S

A

G

C

A

S

L

Y

V

T

L

L

G

A

N

M

F

S

T

T

S

C

Q

R

L

E

K

V

D

R

I

D

N

G

S

E

D

E

A

P

P

P

G

L

W

L

L

V

R

R

V

I

F

G

W

W

S

S

V

I

A

L

I

V

G

G

L

I

T

G

L

I

G

V

M

L

L

L

M

A

T

L

N

G

G

G

I

L

S

K

A

P

L

I

Q

Q

N

T

T

A

T

I

V

I

I

A

M

G

G

G

L

C

P

P

F

L

S

F

F

F

V

V

I

N

F

I

F

M

V

V

M

T

A

L

G

S

L

F

Y

I

K

K

S

D

L

A

K

K

binding carnitine: Y103 (≠ T119), W131 (≠ Y146), W305 (= W319), W312 (= W326), W313 (= W327), Y316 (≠ W330), Y316 (≠ W330), Q319 (≠ F333), F323 (= F337)

Query Sequence

>14452 FitnessBrowser__Keio:14452
MTDLSHSREKDKINPVVFYTSAGLILLFSLTTILFRDFSALWIGRTLDWVSKTFGWYYLL
AATLYIVFVVCIACSRFGSVKLGPEQSKPEFSLLSWAAMLFAAGIGIDLMFFSVAEPVTQ
YMQPPEGAGQTIEAARQAMVWTLFHYGLTGWSMYALMGMALGYFSYRYNLPLTIRSALYP
IFGKRINGPIGHSVDIAAVIGTIFGIATTLGIGVVQLNYGLSVLFDIPDSMAAKAALIAL
SVIIATISVTSGVDKGIRVLSELNVALALGLILFVLFMGDTSFLLNALVLNVGDYVNRFM
GMTLNSFAFDRPVEWMNNWTLFFWAWWVAWSPFVGLFLARISRGRTIRQFVLGTLIIPFT
FTLLWLSVFGNSALYEIIHGGAAFAEEAMVHPERGFYSLLAQYPAFTFSASVATITGLLF
YVTSADSGALVLGNFTSQLKDINSDAPGWLRVFWSVAIGLLTLGMLMTNGISALQNTTVI
MGLPFSFVIFFVMAGLYKSLKVEDYRRESANRDTAPRPLGLQDRLSWKKRLSRLMNYPGT
RYTKQMMETVCYPAMEEVAQELRLRGAYVELKSLPPEEGQQLGHLDLLVHMGEEQNFVYQ
IWPQQYSVPGFTYRARSGKSTYYRLETFLLEGSQGNDLMDYSKEQVITDILDQYERHLNF
IHLHREAPGHSVMFPDA

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