SitesBLAST

H10 (= H9) mutation to C: Loss of phosphotransferase activity. Unable to dimerize.; mutation to E: Results in the formation of a single complex corresponding to the productive phosphoryl transfer complex.
W12 (≠ H11) mutation to F: Slight phosphotransferase activity. Unable to dimerize.
K48 (= K47) mutation to C: Retains more than 50% of phosphotransferase activity.
K55 (≠ E54) modified: N6-acetyllysine
S72 (= S71) mutation to C: Slight phosphotransferase activity. Unable to dimerize.
H86 (≠ K85) mutation to N: Loss of phosphotransferase activity.
S110 (≠ N112) mutation to C: Retains more than 50% of phosphotransferase activity.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
175 H→C: Loss of phosphotransferase activity.
219 H→Q: Slight phosphotransferase activity.
234 modified: N6-acetyllysine

1vrcB Complex of enzyme iiamannose and the histidine-containing phosphocarrier protein hpr from escherichia coli nmr, restrained regularized mean structure (see paper)
43% identity, 70% coverage: 2:104/147 of query aligns to 2:104/129 of 1vrcB

query
sites
1vrcB

L

I

G

A

I

I

I

V

V

I

G

G

T

T

H
|
H

G

G

H

W

L

A

A

A

E

E

E

Q

L

L

V

L

N

K

T

T

C

A

A

E

M

M

I

L

C

L

G

G

Q

E

P

Q

D

E

N

N

L

V

T

G

T

W

V

I

T

D

L
x
F

V

V

P

P

G

G

E

E

G

N

P

A

E

E

D

T

L

L

M

I

A

E

K

K

Y

Y

N

N

K

A

A

Q

M

L

E

A

E

K

M

L

D

D

T

T

N

K

G

G

V

V

I

L

I

F

L

L

N

V

D

D

L

T

F

W

G

G

G
|
G

S
|
S

P

P

Y

F

N

N

A

A

C

S

R

R

V

I

A

V

M

V

E

D

N

K

D

E

K

H

C

Y

G

E

I

V

V

I

T

A

G

G

V

V

S

N

L

I

P

P

M

M

L

L

V

V

E

E

V

T

I

L

N

M

Y

A

R

R

binding phosphite ion: H9 (= H9), F35 (≠ L35), G70 (= G70), S71 (= S71)

P26379 PTS system fructose-specific EIIA component; EIIA-Fru; Fructose-specific phosphotransferase enzyme IIA component; lev-PTS; p16 from Bacillus subtilis (strain 168) (see paper)
37% identity, 71% coverage: 1:104/147 of query aligns to 1:104/146 of P26379

query
sites
P26379

M

M

L

I

G

S

I

V

I

I

V

I

G

S

T

G

H
|
H

G

G

H

D

L

F

A

P

E

I

E

A

L

L

V

K

N

E

T

S

C

S

A

G

M

M

I

I

C

F

G

G

Q

E

P

E

D

N

N

N

L

L

T

I

T

A

V

V

T

P

L

F

V

F

P

K

G

G

E

E

G

G

P

I

E

Q

D

T

L

L

M

Q

A

E

K

K

Y

Y

N

H

K

Q

A

A

M

L

E

K

E

D

M

I

D

P

T

E

N

H

G

E

V

V

I

L

I

F

L

L

N

V

D

D

L

I

F

F

G

G

S

T

P

P

Y

Y

N

N

A

A

C

A

R

S

V

F

A

I

M

A

E

E

N

D

D

Q

K

R

C

M

G

D

I

M

V

A

T

A

G

G

V

V

S

N

L

L

P

P

M

I

L

L

V

L

E

E

V

V

I

L

N

S

Y

L

R

R

H9 (= H9) active site, Tele-phosphohistidine intermediate; modified: Phosphohistidine; by HPr; mutation to A: Phosphorylation is only slightly increased.

Query Sequence

>WP_008538999.1 NCBI__GCF_000245775.1:WP_008538999.1
MLGIIVGTHGHLAEELVNTCAMICGQPDNLTTVTLVPGEGPEDLMAKYNKAMEEMDTTNG
VIILNDLFGGSPYNAACRVAMENDKCGIVTGVSLPMLVEVINYRLCNGENANVQDAMEKA
VEASVAGAQKFHKSQVESETDDEGDDL

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