SitesBLAST

C204 (≠ L217) mutation to S: Destabilizes the protein structure; when associated with S-326.
C326 (≠ T339) mutation to S: Destabilizes the protein structure; when associated with S-204.
D419 (= D435) mutation to A: Still allows binding to Mlc.
C421 (= C437) modified: Phosphocysteine; mutation to D: Still allows binding to Mlc. Derepression of Mlc targets becomes constitutive, i.e. independent of PTS phosphorylation.; mutation to S: Unable to be phosphorylated and to catalyze the phosphoryl exchange between glucose and glucose 6-phosphate at equilibrium. Remains susceptible to CdiA toxin from E.coli strain 3006. Still allows binding to Mlc. Derepression of Mlc targets becomes constitutive, i.e. independent of PTS phosphorylation.
I422 (= I438) mutation to A: Still allows binding to Mlc.
T423 (= T439) mutation to A: Decreases Mlc binding.
R424 (= R440) mutation R->A,H: Cannot bind Mlc. Destroys the ability of Cys-421 to be phosphorylated in vitro.; mutation to K: Cannot bind Mlc. Cys-421 can be phosphorylated in vitro.
R426 (= R442) mutation to A: Still allows binding to Mlc. Cys-421 is weakly phosphorylated in vitro.
V449 (≠ M464) mutation to Q: Interaction with Mlc is hardly detectable.
A451 (= A466) mutation to F: The complex with Mlc shows much weaker association than the wild-type.
Q456 (= Q471) mutation to A: Decreases Mlc binding. Interaction with Mlc is hardly detectable.
I458 (≠ V473) mutation to A: Still allows binding to Mlc.

8qsrA Cryo-em structure of the glucose-specific pts transporter iicb from e. Coli in the inward-facing conformation (see paper)
42% identity, 59% coverage: 6:399/667 of query aligns to 3:383/383 of 8qsrA

query
sites
8qsrA

F

F

S

A

V

N

L

L

Q

Q

K

K

I

V

G

G

K

K

S

S

L

L

M

M

L

L

P

P

V

V

S

S

V

V

L

L

P

P

A

I

A

A

G

G

I

I

L

L

R

G

L

V

G

G

Q

S

P

A

D

N

L

F

L

S

N

W

M

L

P

P

Y

A

I

V

E

V

A

S

-

H

-

V

-

M

-

A

-

E

A

A

G

G

N

G

A

S

I

V

F

F

T

A

N

N

L

M

P

P

M

L

I

I

F

F

A

A

V

I

G

G

V

V

A

A

I

L

G

G

F

F

S

T

G

N

E

D

A

G

V

V

A

S

A

A

L

L

A

A

V

V

G

-

E

-

L

-

I

-

L

-

E

-

N

-

I

-

E

-

K

-

L

-

A

-

S

-

N

-

A

A

A

Y

T

G

A

I

L

M

A

V

Q

K

T

T

T

M

A

A

A

V

S

V

H

A

H

P

M

L

T

V

L

L

K

H

A

L

F

P

M

A

E

E

T

-

Q

-

V

-

Y

-

Q

-

N

E

I

I

V

A

T

S

K

K

T

H

T

L

I

A

N

D

M

T

G

G

V

V

F

L

G

G

I

I

I

S

G

G

I

A

V

I

A

A

L

Y

L

M

Y

F

N

N

R

R

F

F

H

Y

S

R

I

I

K

K

L

L

P

P

Q

E

V

Y

L

L

G

G

F

F

G

A

G

G

K

K

R

R

F

F

V

V

P

P

I

I

V

I

T

S

S

G

A

L

A

A

L

I

I

F

I

T

G

G

A

V

I

V

G

L

V

S

S

F

I

I

W

W

V

P

P

P

V

I

Q

G

G

S

W

A

I

I

D

Q

T

T

M

F

A

S

N

Q

L

W

A

A

S

A

-

Y

-

Q

N

N

S

P

A

V

L

V

G

A

P

F

A

G

F

I

Y

Y

A

G

A

F

G

I

K

E

R
|
R

L

C

L

L

I

V

P

P

V

F

G

G

L

L

H

H

I

I

Y

W

Y

N

P

V

V

P

F

F

L

Q

Y

M

Q

Q

F

I

G

G

H

E

F

Y

I

T

-

N

S

A

N

A

G

G

I

Q

T

V

Y

F

I

H

G

G

D

D

S

I

P

P

R

R

Y

Y

F

M

H

A

G

G

D

D

P

P

T

T

A

A

G

G

I

K

F

-

M

L

A

S

S

G

E

G

F

F

P

L

I

F

L
x
K

M

M

F

Y

G

G

L

L

P

P

G

A

A

A

L

I

A

A

M

I

I

W

A

H

A

S

A

A

K

K

K

P

S

E

K

N

R

R

K

A

Q

K

M

V

A

G

G

G

M

I

M

M

I

I

S

S

S

A

A

A

F

L

V

T

A

S

F

F

V

L

T

T

G

G

I

I

T
|
T

E
|
E

P

P

I

I

E

E

F

F

S

S

F

F

I

M

F

F

V

V

A

A

P

P

I

I

L

L

F

Y

V

I

F

I

H

H

V

A

L

I

V

L

A

A

F

G

C

L

S

A

G

F

L

P

V

I

T

C

S

I

F

L

L

L

H

G

I

M

R

R

L

D

G

G

Y

T

T

S

F
|
F

S

S

A

H

S

G

F

L

I

I

D

D

Y

F

I

I

L

V

G

L

F

S

R

G

Y

N

A

S

E

S

H

K

P

L

W

W

L

L

I

F

W

P

P

I

V

V

G

G

V

I

A

G

F

Y

F

A

L

I

L

V

Y

Y

F

Y

V

T

V

I

F

F

Y

R

F

V

L

L

I

I

R

K

A

A

M

L

N

D

L

L

K

K

T

T

P

P

G

G

R

R

binding beta-D-glucopyranose: R200 (= R216), K254 (≠ L270), T294 (= T310), E295 (= E311), F334 (= F350)

6bvgA Crystal structure of bcmalt t280c-e54c crosslinked by divalent mercury (see paper)
29% identity, 59% coverage: 6:399/667 of query aligns to 2:442/447 of 6bvgA

query
sites
6bvgA

F

F

S

D

V

F

L

W

Q

Q

K

K

I

F

G

G

K

K

S

A

L

L

M

L

L

V

P

V

V

V

S

A

V

V

L

M

P

P

A

A

G

G

I

L

L

M

L

I

R

S

L

I

G

G

Q

K

P

L

D

I

L

G

L

M

N

S

M

A

P

G

Y

D

I

I

E

N

A

A

A

V

-

H

-

T

-

I

-

A

-

R

-

V

-

M

-

C

-

D

-

I

G

G

N

W

A

A

I

I

F

I

T

T

N

N

L

L

P

H

M

I

I

L

F

F

A

A

V

V

G

A

V

I

A

G

I

G

G

S

F

W

S

A

G

K

G

D

E

R

A

A

V

G

A

G

A

A

L

F

A

A

V

L

G

A

E

F

L

V

I

L

L

T

E

N

N

R

I

I

E

T

K

G

L

A

A

I

S

F

S

G

N

V

A

N

A

A

T

E

A

M

L

L

A

A

Q

D

T

S

T

K

A

A

A

K

S

V

H

S

M

V

T

L

L

A

K

G

A

D

F

L

M

I

E

V

T

K

Q

D

V

Y

Y

F

Q

T

N

S

I

V

V

L

T

G

K

A

T

P

T

A

I

L

N

N

M

M

G

G

V

V

F

F

G

V

G

G

I

I

I

T

G

G

I

F

V

L

A

G

A

A

L

T

L

L

Y

Y

N

N

R

K

F

Y

H

Y

S

N

I

Y

-

N

K

K

L

L

P

P

Q

Q

V

A

L

L

G

A

F

F

G

N

G

G

K

K

R

R

F

F

V

V

P

P

I

F

V

V

T

V

S

I

A

V

A

W

A

S

L

T

I

V

I

T

G

A

A

I

I

V

G

L

V

S

S

L

I

L

W

W

V

P

P

F

V

I

Q

Q

G

S

-

G

-

L

-

N

-

E

-

F

-

G

-

R

W

W

I

I

D

A

T

-

M

-

A

A

N

S

L

K

A

D

S

S

N

A

S

P

A

I

L

V

G

A

P

P

A

F

F

V

Y

Y

A

G

A

T

G

L

K
x
E

R
|
R

L

L

I

L

P

P

V

F

G

G

L

L

H
|
H

I

M

Y

L

-
x
T

Y

I

P

P

V

M

F

N

L
x
Y

Y

T

Q

E

F

L

G

G

H

G

F

T

I

Y

S

T

N

M

-

L

-

T

-

G

-

S

-

K

-

V

G

G

I

Q

T

V

Y

V

I

A

G

G

D

Q

S

D

P

P

R

L

Y

W

F

L

-

A

-

W

-

I

-

C

-

D

-

L

-

N

-

L

-

A

H

N

G

G

D

D

P

T

T

K

A

A

-

Y

-

N

-

D

-

L

-

N

-

V

-

P

G

A

I

R

F

F

M
x
K

A

A

S

G

E

Q

F

V

P

I

I

G

L

S

M

T

F

A

G

A

L

L

P

M

G

G

A

I

A

A

L

F

A

A

M

M

I

F

A

R

A

N

A

V

K

D

K

K

S

E

K

K

R

R

K

A

Q

K

M

Y

A

K

G

P

M

M

M

F

I

L

S

S

S

A

A

A

F

L

V

A

A

V

F

F

V

L

T

T

G

G

I

V

T
|
T

E
|
E

P

P

I

I

E

E

F

F

S

M

F

F

I

M

F

F

V

I

A

A

P

P

I

V

L

L

F

Y

V

V

F

V

H

Y

V

A

L

I

V

T

A

T

F

G

C

L

S

A

G

F

L

A

V

L

T

A

S

D

F

L

L

I

H

N

I

L

R

R

L

V

G

-

Y

-

T

-

F

H

S

A

A
x
F

S

G

F

F

I

I

D

E

Y

L

I

I

L

-

G

-

F

-

R

-

Y

-

A

T

E

R

H

T

P

P

W

M

L

M

I

V

W

N

P

A

-

G

-

L

-

T

-

R

-

D

-

L

-

I

-

N

-

F

-

V

-

I

V

V

G

S

V

L

A

V

F

F

L

G

L

L

Y

N

F

F

V

T

V

L

F

F

Y

N

F

F

L

L

I

I

R

K

A

K

M

F

N

N

L

L

K

P

T

T

P

P

G

G

R

R

binding alpha-D-glucopyranose: E227 (≠ K215), R228 (= R216), H236 (= H224), H237 (= H225), H237 (= H225), T240 (vs. gap), Y245 (≠ L232), K303 (≠ M263), T350 (= T310), E351 (= E311), F389 (≠ A352)

P69783 PTS system glucose-specific EIIA component; EIIA-Glc; EIII-Glc; Glucose-specific phosphotransferase enzyme IIA component from Escherichia coli (strain K12) (see 6 papers)
45% identity, 20% coverage: 510:643/667 of query aligns to 12:145/169 of P69783

query
sites
P69783

S

S

E

D

S

D

K

K

A

K

V

D

S

T

G

G

V

T

N

I

L

E

L

I

S

A

P

P

A

L

D

S

G

G

E

E

I

I

V

V

T

N

L

I

E

E

E

D

V

V

P

P

D

D

P

V

T

V

F

F

S

A

E

E

K

K

L

I

L

V

G

G

D

D

G

G

F

I

A

A

V

I

I

K

P

P

S

T

G

G

D

N

N

K

I

M

Y

V

A

A

P

P

A

V

D

D

G

G

E

T

I

I

T

G

V

K

L

I

F

F

P

E

T

T

K

N

H
|
H

A

A

F

F

A

S

I

I

T

E

T

S

A

D

Q

S

G

G

L

V

E

E

L

L

L

F

I

V

H
|
H

I

F

G

G

I

I

D

D

T

T

V

V

A

E

L

L

N

K

G

G

E

E

G

G

F

F

T

K

A

R

H

I

V

A

K

E

Q

E

G

G

D

Q

K

R

V

V

K

K

K

V

G

G

D

D

L

T

I

V

L

I

N

E

L

F

D

D

S

L

K

P

F

L

I

L

K

E

S

E

K

K

G

A

K

K

N

S

M

T

I

L

T

T

P

P

V

V

I

V

V

I

T

S

N

N

M

M

D

D

H76 (= H574) Important for phospho-donor activity; binding Zn(2+); mutation to Q: Unable to transfer phosphoryl group.
H91 (= H589) active site, Tele-phosphohistidine intermediate; for EIIA activity; binding Zn(2+); modified: Phosphohistidine; by HPr; mutation to Q: Unable to be phosphorylated by Hpr.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
4 F→W: Same activity as the wild-type.

1glcF Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
46% identity, 18% coverage: 521:643/667 of query aligns to 15:137/161 of 1glcF

query
sites
1glcF

L

I

S

A

P

P

A

L

D

S

G

G

E

E

I

I

V

V

T

N

L

I

E

E

E

D

V

V

P

P

D

D

P

V

T

V

F

F

S

A

E

E

K

K

L

I

L

V

G

G

D

D

G

G

F

I

A

A

V

I

I

K

P

P

S

T

G

G

D

N

N

K

I

M

Y

V

A

A

P

P

A

V

D

D

G

G

E

T

I

I

T

G

V

K

L

I

F

F

P

E

T

T

K

N

H
|
H

A

A

F

F

A

S

I

I

T

E

T

S

A

D

Q

S

G

G

L

V

E

E

L

L

L

F

I

V

H
|
H

I

F

G

G

I

I

D

D

T

T

V

V

A

E

L

L

N

K

G

G

E

E

G

G

F

F

T

K

A

R

H

I

V

A

K

E

Q

E

G

G

D

Q

K

R

V

V

K

K

K

V

G

G

D

D

L

T

I

V

L

I

N

E

L

F

D

D

S

L

K

P

F

L

I

L

K

E

S

E

K

K

G

A

K

K

N

S

M

T

I

L

T

T

P

P

V

V

I

V

V

I

T

S

N

N

M

M

D

D

binding zinc ion: H68 (= H574), H83 (= H589)

1o2fA Complex of enzyme iiaglc and iibglc phosphocarrier protein hpr from escherichia coli nmr, restrained regularized mean structure (see paper)
46% identity, 18% coverage: 521:643/667 of query aligns to 4:126/150 of 1o2fA

query
sites
1o2fA

L

I

S

A

P

P

A

L

D

S

G

G

E

E

I

I

V

V

T

N

L

I

E

E

E

D

V

V

P

P

D

D

P

V

T

V

F

F

S

A

E

E

K

K

L

I

L

V

G

G

D

D

G

G

F

I

A

A

V

I

I

K

P

P

S

T

G

G

D

N

N

K

I

M

Y

V

A

A

P

P

A

V

D

D

G

G

E

T

I

I

T

G

V

K

L

I

F

F

P

E

T
|
T

K

N

H
|
H

A

A

F

F

A

S

I

I

T

E

T

S

A

D

Q

S

G

G

L

V

E

E

L

L

L

F

I

V

H
|
H

I

F

G

G

I

I

D
|
D

T

T

V

V

A

E

L

L

N

K

G

G

E

E

G

G

F

F

T

K

A

R

H

I

V

A

K

E

Q

E

G

G

D

Q

K

R

V

V

K

K

K

V

G

G

D

D

L

T

I

V

L

I

N

E

L

F

D

D

S

L

K

P

F

L

I

L

K

E

S

E

K

K

G

A

K

K

N

S

M

T

I

L

T

T

P

P

V

V

I

V

V

I

T

S

N

N

M

M

D

D

active site: T55 (= T572), H57 (= H574), H72 (= H589)
binding phosphite ion: H72 (= H589), D76 (= D593)

1o2fB Complex of enzyme iiaglc and iibglc phosphocarrier protein hpr from escherichia coli nmr, restrained regularized mean structure (see paper)
48% identity, 11% coverage: 418:491/667 of query aligns to 3:77/77 of 1o2fB

query
sites
1o2fB

A

A

K

A

V

L

L

V

E

A

A

A

I

F

G

G

K

K

D

E

N

N

I

I

K

T

V

N

L

L

D

D

A

A

C
|
C

I
|
I

T
|
T

R

R

L

L

R

R

L

V

T

S

L

V

N

A

D

D

-

V

P

S

A

K

V

V

D

D

E

Q

K

A

T

G

L

L

R

K

A

K

L

L

G

G

A

A

G

G

I

V

M

V

K

V

A

A

G

G

N

S

S

G

V

V

Q

Q

V

A

V

I

F

F

G

G

T

T

E

K

A

S

E

D

R

N

I

L

K

K

D

T

D

E

I

M

K

D

A

E

I

Y

I

I

A

R

N

N

binding phosphite ion: C22 (= C437), I23 (= I438), T24 (= T439)

Query Sequence

>WP_039653499.1 NCBI__GCF_000816635.1:WP_039653499.1
MKKKIFSVLQKIGKSLMLPVSVLPAAGILLRLGQPDLLNMPYIEAAGNAIFTNLPMIFAV
GVAIGFSGGEAVAALAAVVGELILENIEKLASSNAATALAQTTAASHHMTLKAFMETQVY
QNIVTKTTINMGVFGGIIIGIVAALLYNRFHSIKLPQVLGFFGGKRFVPIVTSAAALIIG
AIGVSIWVPVQGWIDTMANLASNSALGPAFYAAGKRLLIPVGLHHIYYPVFLYQFGHFIS
NGITYIGDSPRYFHGDPTAGIFMASEFPILMFGLPGAALAMIAAAKKSKRKQMAGMMISS
AFVAFVTGITEPIEFSFIFVAPILFVFHVLVAFCSGLVTSFLHIRLGYTFSASFIDYILG
FRYAEHPWLIWPVGVAFFLLYFVVFYFLIRAMNLKTPGREDEDGEEIVHINVKGSAKAAK
VLEAIGGKDNIKVLDACITRLRLTLNDPAVDEKTLRALGAAGIMKAGNSVQVVFGTEAER
IKDDIKAIIANGGVVEESETQQGEDTSGGSESKAVSGVNLLLSPADGEIVTLEEVPDPTF
SEKLLGDGFAVIPSGDNIYAPADGEITVLFPTKHAFAITTAQGLELLIHIGIDTVALNGE
GFTAHVKQGDKVKKGDLILNLDSKFIKSKGKNMITPVIVTNMDIVDNIDIKKGKVDHAKT
AAEILIK

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