SitesBLAST

E190 (= E466) mutation E->A,C,K,L: Reduction of transport rate.
A192 (= A468) mutation A->D,S,L: Loss of transport and MalK dissociation from the membrane.
G196 (= G472) mutation to A: No effect.; mutation to P: Loss of transport and MalK dissociation from the membrane.
P209 (= P485) mutation to A: No effect.

4ki0F Crystal structure of the maltose-binding protein/maltose transporter complex in an outward-facing conformation bound to maltohexaose (see paper)
32% identity, 23% coverage: 77:204/563 of query aligns to 279:408/490 of 4ki0F

query
sites
4ki0F

M

L

S

T

T

V

T

A

I

V

G

G

T

M

F

V

F

L

A

A

W

C

L

L

V

V

T

Q

R

W

T

E

D

A

L

L

P

R

F

G

K

K

A

A

A

V

M

Y

K

R

V

V

L

L

F

L

L

I

V

L

P

P

F
x
Y

M

A

L

V

P

P

S

S

F

F

I

I

G

S

A

I

L

L

A

I

W

F

K

K

M

G

L

L

L

F

S

N

P

Q

R

S

A

F

G

G

Y

E

I

I

N

N

R

M

L

M

F

L

M

S

D

A

T

L

F

F

G

G

F

V

S

K

G

P

P

A

V

W

F

F

D

S

I

D

Y

P

T

T

Y

T

H

A

G

R

I

T

M

M

-

L

-

I

A

I

V

V

E
x
N

T

T

M

W

Y

L

L
x
G

F

Y

P

P

F
x
Y

V

M

F

M

I

I

Q

L

V

C

C

M

G

G

A

L

L

L

E

K

R

A

M

I

D

P

P

D

T

D

L

L

E

Y

E

E

A

A

A

S

R

A

I

M

S

D

G

G

A

A

S

G

L

P

F

F

T

Q

I

N

T

F

R

F

K

K

I

I

T

T

I

L

P

P

L

L

V

L

M

I

binding alpha-D-glucopyranose: Y310 (≠ F108), N361 (≠ E157), G365 (≠ L161), Y368 (≠ F164)

Sites not aligning to the query:

binding alpha-D-glucopyranose: 418, 422

P02916 Maltose/maltodextrin transport system permease protein MalF from Escherichia coli (strain K12) (see 4 papers)
32% identity, 23% coverage: 77:204/563 of query aligns to 294:423/514 of P02916

query
sites
P02916

M

L

S

T

T

V

T

A

I

V

G

G

T

M

F

V

F

L

A

A

W

C

L

L

V

V

T

Q

R

W

T

E

D

A

L

L

P

R

F

G

K

K

A

A

A

V

M

Y

K

R

V

V

L

L

F

L

L

I

V

L

P

P

F

Y

M

A

L

V

P

P

S

S

F

F

I

I

G

S

A

I

L
|
L

A

I

W

F

K

K

M

G

L

L

L

F

S

N

P

Q

R

S

A

F

G

G

Y

E

I

I

N

N

R

M

L

M

F

L

M

S

D

A

T

L

F

F

G

G

F

V

S

K

G

P

P

A

V

W

F

F

D

S

I

D

Y

P

T

T

Y

T

H

A

G

R

I

T

M

M

-
x
L

-

I

A

I

V

V

E
x
N

T

T

M

W

Y

L

L
x
G

F

Y

P

P

F

Y

V

M

F

M

I

I

Q

L

V

C

C

M

G

G

A

L

L

L

E

K

R

A

M

I

D

P

P

D

T

D

L

L

E

Y

E
|
E

A

A

A
x
S

R

A

I

M

S

D

G
|
G

A

A

S

G

L

P

F

F

T

Q

I

N

T

F

R

F

K

K

I

I

T

T

I

L

P
|
P

L

L

V

L

M

I

L334 (= L117) mutation to W: Ability to transport lactose in a saturable manner.
L372 (vs. gap) mutation to W: Growth on maltose but not on media containing either maltoheptaose or maltoheptaose plus maltose.
N376 (≠ E157) mutation N->K,H: No growth on maltose.
G380 (≠ L161) mutation G->C,S: No growth on maltose.
E401 (= E182) mutation E->A,C,K,L: Reduction of transport rate.
S403 (≠ A184) mutation S->C,D,K,L: Reduction of transport rate.
G407 (= G188) mutation G->A,P: No effect.
P420 (= P201) mutation to A: No effect.

Query Sequence

>8500850 FitnessBrowser__Miya:8500850
MAALAKSRSFGVAEVILAISIAVLVIVVAVPVLLIFFNAFWVDGSPNFTDVVKILRQPDT
YEALLNSLFIASGVTVMSTTIGTFFAWLVTRTDLPFKAAMKVLFLVPFMLPSFIGALAWK
MLLSPRAGYINRLFMDTFGFSGPVFDIYTYHGIMAVETMYLFPFVFIQVCGALERMDPTL
EEAARISGASLFTITRKITIPLVMPSIVSGALLIMLYSMAHFGTVAVLGIEIGIFNIPTL
IYEKIHQSAGSFQSIRTGTVLASVLVVTAAAIIWLQNKVLERGRFQIIAGKSFRPMELKL
RGFRIPLLVLCIAYIAFTIVLPTATIFLVGGLKTYGLPLTMENLTLDNYKFILFDWQLTR
DAIWNSVSLGLAAALITMFAGVMISYVIVKMKVRGKGFLEFLGMLPFSVPGSVIALGVIL
AWSGKFGINIYNTVWIILVAYIARYMAFSLKANSAALEQVHDSLVEAARACGATMWQALR
DIVLPLVRPGMLAAFFLIFLPALRELTVSVLLYGPTTRTIGVAIYTLNEDGETVYSAALA
GIALIIIVTGQTLIKRFTGGNGR

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