SitesBLAST

84 binding
85 binding
136 binding
232 modified: Phosphohistidine; by HPr; H→A: Loss of phosphorylation, no effect on activity.; H→E: Loss of phosphorylation, 2.5-fold reduced activity.; H→R: Loss of phosphorylation, 3.4-fold increased activity.
246 binding
247 binding

P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
27% identity, 23% coverage: 407:537/566 of query aligns to 349:477/496 of P18157

query
sites
P18157

G

G

R

L

R

G

T

T

P

P

D

Y

A

W

N

D

Q

S

E

D

L

V

K

R

G

G

A

S

I

V

T

F

G

G

L

L

G

T

L

R

G

G

T

T

D

T

A

K

P

E

R

H

F

F

F

I

R

R

A

A

L

T

A

L

A

E

A

S

T

L

C

A

F

Y

G

Q

A

T

K

K

A

D

I

V

V

L

D

D

R

A

F

M

K

E

E

A

Q

D

G

S

V

N

P

I

V

S

K

L

G

K

I

T

I

L

G

R

I

V

G

D

G

G

V

G

A

A

K

V

K

K

S

N

A

N

Y

F

I

L

M

M

Q

Q

M

F

M

Q

A

G

D

D

V

L

L

L

E

N

M

V

P

P

I

V

R

E

I

R

H

P

R

E

F

I

E

N

H

E

T

T

C

T

A

A

L

L

G

G

A

A

M

Y

F

L

A

A

A

G

V

I

A

A

A

V

G

G

I

F

Y

W

P

K

D

D

I

-

E

-

T

R

A

S

M

E

A

I

A

A

M

N

G

Q

T

W

G

N

F

L

E

D

K

K

E

R

Y

F

K

E

P

P

N

E

I

L

K

E

Q

E

K

K

Sites not aligning to the query:

230 H→R: Increased activity.
232 F→S: Increased activity.

2w40A Crystal structure of plasmodium falciparum glycerol kinase with bound glycerol (see paper)
20% identity, 26% coverage: 377:521/566 of query aligns to 320:467/501 of 2w40A

query
sites
2w40A

L

L

E

K

G

N

K

K

I

L

I

I

A

D

N

D

L

P

S

S

K

E

Q

A

A

S

D

D

A

I

L

M

P

E

N

K

E

C

D

E

Y

N

A

T

E

T

-

G

-

V

L

I

A

F

I

V

D

P

W

A

L

F

N

S

G

G

R

L

R

Y

T

A

P

P

D

R

A

W

N

R

Q

S

E

D

L

A

K

R

G

A

A

S

I

I

T

Y

G

G

L

M

G

T

L

F

G

N

T

T

D

E

A

R

P

S

R

H

F

I

F

V

R

R

A

A

L

L

A

L

A

E

A

G

T

I

C

A

F

F

G

Q

A

L

K

N

A

E

I

I

V

V

D

D

R

S

F

L

-

T

K

S

E

D

Q

M

G

G

V

I

P

E

V

M

K

L

G

H

I

V

I

L

G

R

I

C

G

D

G

G

V

G

A

M

K

T

K

K

S

N

A

K

Y

P

I

F

M

M

Q

Q

M

F

M

N

A

S

D

D

V

I

L

I

E

N

M

T

P

K

I

I

R

E

I

V

H

S

R

K

F

Y

E

K

H

E

T

V

C

T

A

S

L

L

G

G

A

A

M

V

F

L

A

A

A

G

V

L

A

E

A

V

G

K

I

I

Y

W

P

D

D

S

I

L

E

D

T

S

A

V

M

K

A

S

A

L

M

L

Sites not aligning to the query:

binding glycerol: 83, 84, 103, 114, 117, 135, 246, 271

2w41B Crystal structure of plasmodium falciparum glycerol kinase with adp (see paper)
20% identity, 26% coverage: 377:521/566 of query aligns to 326:473/507 of 2w41B

query
sites
2w41B

L

L

E

K

G

N

K

K

I

L

I

I

A

D

N

D

L
x
P

S

S

K

E

Q
x
A

A

S

D

D

A

I

L

M

P

E

N

K

E

C

D

E

Y

N

A

T

E

T

-

G

-

V

L

I

A

F

I

V

D

P

W

A

L

F

N

S

G

G

R

L

R

Y

T

A

P

P

D

R

A

W

N

R

Q

S

E

D

L

A

K

R

G

A

A

S

I

I

T

Y

G

G

L

M

G

T

L

F

G

N

T

T

D

E

A

R

P

S

R

H

F

I

F

V

R

R

A

A

L

L

A

L

A

E

A

G

T

I

C

A

F

F

G

Q

A

L

K

N

A

E

I

I

V

V

D

D

R

S

F

L

-

T

K

S

E

D

Q

M

G

G

V

I

P

E

V

M

K

L

G

H

I

V

I

L

G

R

I

C

G

D

G

G

V
x
G

A
x
M

K

T

K

K

S
x
N

A

K

Y

P

I

F

M

M

Q

Q

M

F

M

N

A

S

D

D

V

I

L

I

E

N

M

T

P

K

I

I

R

E

I

V

H

S

R

K

F

Y

E

K

H

E

T

V

C

T

A

S

L

L

G

G

A

A

M

V

F

L

A

A

A

G

V

L

A

E

A

V

G

K

I

I

Y

W

P

D

D

S

I

L

E

D

T

S

A

V

M

K

A

S

A

L

M

L

binding adenosine-5'-diphosphate: P334 (≠ L385), A337 (≠ Q388), G420 (≠ V468), M421 (≠ A469), N424 (≠ S472)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 273, 274, 319, 322

1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
25% identity, 22% coverage: 418:540/566 of query aligns to 351:472/489 of 1gldG

query
sites
1gldG

K

R

G

G

A

A

I

I

T

F

G

G

L

L

G

T

L

R

G

G

T

V

D

N

A

A

P

N

R

H

F

I

R

R

A

A

L

T

A

L

A

E

A

S

T

I

C

A

F

Y

G

Q

A

T

K

R

A

D

I

V

V

L

D

E

R

A

F

M

K

Q

-

A

E

D

Q

S

G

G

V

I

P

R

V

L

K

H

G

A

I

L

I

R

G

V

I

D

G

G

G
|
G

V

-

A
|
A

K

V

K

A

S
x
N

A

N

Y

F

I

L

M

M

Q

Q

M

F

M

Q

A

S

D

D

V

I

L

L

E

G

M

T

P

R

I

V

R

E

I

R

H

P

R

E

F

V

E

R

H

E

T

V

C

T

A

A

L

L

G

G

A

A

M

Y

F

L

A

A

A

G

V

L

A

A

A

V

G

G

I

F

Y

W

P

Q

D

N

I

L

E

D

T

E

A

L

M

Q

A

E

A

K

M

-

G

-

T

A

G

V

F

I

E

E

K

R

E

E

Y

F

K

R

P

P

N

G

I

I

K

E

-

T

K

T

Q

E

K

R

L

N

Y

Y

R

R

binding adenosine-5'-diphosphate: G401 (= G467), A402 (= A469), N405 (≠ S472)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 14, 256, 257, 300, 316
binding glyceraldehyde-3-phosphate: 10, 80, 81, 132, 235, 260
binding manganese (ii) ion: 7, 14

1glcG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
25% identity, 22% coverage: 418:540/566 of query aligns to 351:472/489 of 1glcG

query
sites
1glcG

K

R

G

G

A

A

I

I

T

F

G

G

L

L

G

T

L

R

G

G

T

V

D

N

A

A

P

N

R

H

F

I

R

R

A

A

L

T

A

L

A

E

A

S

T

I

C

A

F

Y

G

Q

A

T

K

R

A

D

I

V

V

L

D

E

R

A

F

M

K

Q

-

A

E

D

Q

S

G

G

V

I

P

R

V

L

K

H

G

A

I

L

I

R

G

V

I

D

G

G

G
|
G

V

-

A
|
A

K

V

K

A

S
x
N

A

N

Y

F

I

L

M

M

Q

Q

M

F

M

Q

A

S

D

D

V

I

L

L

E

G

M

T

P

R

I

V

R

E

I

R

H

P

R

E

F

V

E

R

H

E

T

V

C

T

A

A

L

L

G

G

A

A

M

Y

F

L

A

A

A

G

V

L

A

A

A

V

G

G

I

F

Y

W

P

Q

D

N

I

L

E

D

T

E

A

L

M

Q

A

E

A

K

M

-

G

-

T

A

G

V

F

I

E

E

K

R

E

E

Y

F

K

R

P

P

N

G

I

I

K

E

-

T

K

T

Q

E

K

R

L

N

Y

Y

R

R

binding adenosine-5'-diphosphate: G401 (= G467), A402 (= A469), N405 (≠ S472)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 256, 257, 300, 316
binding glyceraldehyde-3-phosphate: 10, 80, 81, 100, 132, 235, 260

1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
25% identity, 22% coverage: 418:540/566 of query aligns to 351:472/489 of 1glbG

query
sites
1glbG

K

R

G

G

A

A

I

I

T

F

G

G

L

L

G

T

L

R

G

G

T

V

D

N

A

A

P

N

R

H

F

I

R

R

A

A

L

T

A

L

A

E

A

S

T

I

C

A

F

Y

G

Q

A

T

K

R

A

D

I

V

V

L

D

E

R

A

F

M

K

Q

-

A

E

D

Q

S

G

G

V

I

P

R

V

L

K

H

G

A

I

L

I

R

G

V

I

D

G

G

G
|
G

V

-

A
|
A

K

V

K

A

S
x
N

A

N

Y

F

I

L

M

M

Q

Q

M

F

M

Q

A

S

D

D

V

I

L

L

E

G

M

T

P

R

I

V

R

E

I

R

H

P

R

E

F

V

E

R

H

E

T

V

C

T

A

A

L

L

G

G

A

A

M

Y

F

L

A

A

A

G

V

L

A

A

A

V

G

G

I

F

Y

W

P

Q

D

N

I

L

E

D

T

E

A

L

M

Q

A

E

A

K

M

-

G

-

T

A

G

V

F

I

E

E

K

R

E

E

Y

F

K

R

P

P

N

G

I

I

K

E

-

T

K

T

Q

E

K

R

L

N

Y

Y

R

R

binding adenosine-5'-diphosphate: G401 (= G467), A402 (= A469), N405 (≠ S472)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 14, 256, 257, 300, 303, 316
binding glycerol: 80, 81, 100, 132, 235, 260

1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
25% identity, 22% coverage: 418:540/566 of query aligns to 356:477/494 of 1gllO

query
sites
1gllO

K

R

G

G

A

A

I

I

T

F

G

G

L

L

G

T

L

R

G

G

T

V

D

N

A

A

P

N

R

H

F

I

R

R

A

A

L

T

A

L

A

E

A

S

T

I

C

A

F

Y

G

Q

A

T

K

R

A

D

I

V

V

L

D

E

R

A

F

M

K

Q

-

A

E

D

Q

S

G

G

V

I

P

R

V

L

K

H

G

A

I

L

I

R

G

V

I

D

G

G

G
|
G

V

-

A

A

K

V

K

A

S
x
N

A

N

Y

F

I

L

M

M

Q

Q

M

F

M

Q

A

S

D

D

V

I

L

L

E

G

M

T

P

R

I

V

R

E

I

R

H

P

R

E

F

V

E

R

H

E

T

V

C

T

A

A

L

L

G

G

A

A

M

Y

F

L

A

A

A

G

V

L

A

A

A

V

G

G

I

F

Y

W

P

Q

D

N

I

L

E

D

T

E

A

L

M

Q

A

E

A

K

M

-

G

-

T

A

G

V

F

I

E

E

K

R

E

E

Y

F

K

R

P

P

N

G

I

I

K

E

-

T

K

T

Q

E

K

R

L

N

Y

Y

R

R

binding phosphomethylphosphonic acid adenylate ester: G406 (= G467), N410 (≠ S472)

Sites not aligning to the query:

binding phosphomethylphosphonic acid adenylate ester: 12, 13, 261, 262, 305, 308, 309, 321
binding glycerol: 82, 83, 134, 240, 241, 265

1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
25% identity, 22% coverage: 418:540/566 of query aligns to 356:477/494 of 1gljO

query
sites
1gljO

K

R

G

G

A

A

I

I

T

F

G

G

L

L

G

T

L

R

G

G

T

V

D

N

A

A

P

N

R

H

F

I

R

R

A

A

L

T

A

L

A

E

A

S

T

I

C

A

F

Y

G

Q

A

T

K

R

A

D

I

V

V

L

D

E

R

A

F

M

K

Q

-

A

E

D

Q

S

G

G

V

I

P

R

V

L

K

H

G

A

I

L

I

R

G

V

I

D

G

G

G
|
G

V

-

A
|
A

K

V

K

A

S

N

A

N

Y

F

I

L

M

M

Q

Q

M

F

M

Q

A

S

D

D

V

I

L

L

E

G

M

T

P

R

I

V

R

E

I

R

H

P

R

E

F

V

E

R

H

E

T

V

C

T

A

A

L

L

G

G

A

A

M

Y

F

L

A

A

A

G

V

L

A

A

A

V

G

G

I

F

Y

W

P

Q

D

N

I

L

E

D

T

E

A

L

M

Q

A

E

A

K

M

-

G

-

T

A

G

V

F

I

E

E

K

R

E

E

Y

F

K

R

P

P

N

G

I

I

K

E

-

T

K

T

Q

E

K

R

L

N

Y

Y

R

R

binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: G406 (= G467), A407 (= A469)

Sites not aligning to the query:

binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: 12, 13, 261, 262, 305, 309, 321
binding glycerol: 82, 83, 102, 134, 240, 265

1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
25% identity, 22% coverage: 418:540/566 of query aligns to 356:477/494 of 1bwfO

query
sites
1bwfO

K

R

G

G

A

A

I

I

T

F

G

G

L

L

G

T

L

R

G

G

T

V

D

N

A

A

P

N

R

H

F

I

R

R

A

A

L

T

A

L

A

E

A

S

T

I

C

A

F

Y

G

Q

A

T

K

R

A

D

I

V

V

L

D

E

R

A

F

M

K

Q

-

A

E

D

Q

S

G

G

V

I

P

R

V

L

K

H

G

A

I

L

I

R

G

V

I

D

G

G

G
|
G

V

-

A

A

K

V

K

A

S
x
N

A

N

Y

F

I

L

M

M

Q

Q

M

F

M

Q

A

S

D

D

V

I

L

L

E

G

M

T

P

R

I

V

R

E

I

R

H

P

R

E

F

V

E

R

H

E

T

V

C

T

A

A

L

L

G

G

A

A

M

Y

F

L

A

A

A

G

V

L

A

A

A

V

G

G

I

F

Y

W

P

Q

D

N

I

L

E

D

T

E

A

L

M

Q

A

E

A

K

M

-

G

-

T

A

G

V

F

I

E

E

K

R

E

E

Y

F

K

R

P

P

N

G

I

I

K

E

-

T

K

T

Q

E

K

R

L

N

Y

Y

R

R

binding phosphodifluoromethylphosphonic acid-adenylate ester: G406 (= G467), N410 (≠ S472)

Sites not aligning to the query:

binding phosphodifluoromethylphosphonic acid-adenylate ester: 12, 13, 262, 305, 308, 309, 321
binding glycerol: 82, 83, 102, 134, 240, 241, 265

1bu6Y Crystal structures of escherichia coli glycerol kinase and the mutant a65t in an inactive tetramer: conformational changes and implications for allosteric regulation (see paper)
25% identity, 22% coverage: 418:540/566 of query aligns to 360:481/499 of 1bu6Y

query
sites
1bu6Y

K

R

G

G

A

A

I

I

T

F

G

G

L

L

G

T

L

R

G

G

T

V

D

N

A

A

P

N

R

H

F

I

R

R

A

A

L

T

A

L

A

E

A

S

T

I

C

A

F

Y

G

Q

A

T

K

R

A

D

I

V

V

L

D

E

R

A

F

M

K

Q

-

A

E

D

Q

S

G

G

V

I

P

R

V

L

K

H

G

A

I

L

I

R

G

V

I

D

G

G

V

-

A

A

K

V

K

A

S

N

A

N

Y

F

I

L

M

M

Q

Q

M

F

M

Q

A

S

D

D

V

I

L

L

E

G

M

T

P

R

I

V

R

E

I

R

H

P

R

E

F

V

E

R

H

E

T

V

C

T

A

A

L

L

G

G

A

A

M

Y

F

L

A

A

A

G

V

L

A

A

A

V

G

G

I

F

Y

W

P

Q

D

N

I

L

E

D

T

E

A

L

M

Q

A

E

A

K

M

-

G

-

T

A

G

V

F

I

E

E

K

R

E

E

Y

F

K

R

P

P

N

G

I

I

K

E

-

T

K

T

Q

E

K

R

L

N

Y

Y

R

R

Sites not aligning to the query:

binding glycerol: 81, 82, 83, 102, 134, 244

P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
25% identity, 22% coverage: 418:540/566 of query aligns to 362:483/502 of P0A6F3

query
sites
P0A6F3

K

R

G

G

A

A

I

I

T

F

G

G

L

L

G

T

L

R

G

G

T

V

D

N

A

A

P

N

R

H

F

I

R

R

A

A

L

T

A

L

A

E

A

S

T

I

C

A

F

Y

G

Q

A

T

K

R

A

D

I

V

V

L

D

E

R

A

F

M

K

Q

-

A

E

D

Q

S

G

G

V

I

P

R

V

L

K

H

G

A

I

L

I

R

G

V

I

D

G

G

G
|
G

V

-

A

A

K

V

K

A

S
x
N

A

N

Y

F

I

L

M

M

Q

Q

M

F

M

Q

A

S

D

D

V

I

L

L

E

G

M

T

P

R

I

V

R

E

I

R

H

P

R

E

F

V

E

R

H

E

T

V

C

T

A

A

L

L

G

G

A

A

M

Y

F

L

A

A

A

G

V

L

A

A

A

V

G

G

I

F

Y

W

P

Q

D

N

I

L

E

D

T

E

A

L

M

Q

A

E

A

K

M

-

G

-

T

A

G

V

F

I

E

E

K

R

E

E

Y

F

K

R

P

P

N

G

I
|
I

K

E

-

T

K

T

Q
x
E

K
x
R

L

N

Y

Y

R

R

G412 (= G467) binding
N416 (≠ S472) binding
I475 (= I533) mutation to D: It decreases Vmax to about 10% of the wild-type value and the affinity for substrate is increased about two- to fourfold. This mutation decreases the catalytic activity in a manner that is analogous to that obtained upon EIIA-Glc binding. It increases the affinity for FBP about fivefold.
E479 (≠ Q536) binding
R480 (≠ K537) mutation to D: It decreases Vmax to about 10% of the wild-type value and the affinity for substrate is increased about two- to fourfold. This mutation decreases the catalytic activity in a manner that is analogous to that obtained upon EIIA-Glc binding. Regulation by FBP is not affected by this substitution. No inhibition by EIIA-Glc is observed, which is consistent with a decrease in affinity for EIIA-Glc of about 250-fold.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
14 binding ; binding
18 binding
59 S→W: Abolishes inhibition of GK by FBP via disruption of the dimer-tetramer assembly reaction. Inhibition by EIIA-Glc is unchanged compared to wild type. The activity of this mutant is significantly higher than wild-type, and the Michaelis constants are increased slightly compared to wild-type.
66 A→T: Although it completely abolishes FBP regulation and disrupts dimer-tetramer equilibrium, the crystal structure is essentially identical to the symmetric tetramer found in the FBP-bound form of the enzyme.
84 binding ; binding
85 binding ; binding
136 binding ; binding
231 G→D: Displays an increased enzymatic activity and a decreased allosteric regulation by FBP compared to wild-type. It displays a dimer form and is resistant to tetramer formation in the presence of FBP, whereas wild-type dimers are converted into inactive tetramers in the presence of FBP.
233 modified: N6-malonyllysine
235 binding
237 binding ; R→A: Drastically reduces inhibition of GK by FBP and lowers, but did not eliminate, the ability of FBP to promote tetramer association.
246 binding ; binding
247 binding
268 binding
305 G→S: In glpK22; abolishes glucose control of glycerol utilization.
311 binding

1glfO Crystal structures of escherichia coli glycerol kinase and the mutant a65t in an inactive tetramer: conformational changes and implications for allosteric regulation (see paper)
25% identity, 22% coverage: 418:540/566 of query aligns to 360:481/498 of 1glfO

query
sites
1glfO

K

R

G

G

A

A

I

I

T

F

G

G

L

L

G

T

L

R

G

G

T

V

D

N

A

A

P

N

R

H

F

I

R

R

A

A

L

T

A

L

A

E

A

S

T

I

C

A

F

Y

G

Q

A

T

K

R

A

D

I

V

V

L

D

E

R

A

F

M

K

Q

-

A

E

D

Q

S

G

G

V

I

P

R

V

L

K

H

G

A

I

L

I

R

G

V

I

D

G

G

G
|
G

V

-

A
|
A

K

V

K

A

S

N

A

N

Y

F

I

L

M

M

Q

Q

M

F

M

Q

A

S

D

D

V

I

L

L

E

G

M

T

P

R

I

V

R

E

I

R

H

P

R

E

F

V

E

R

H

E

T

V

C

T

A

A

L

L

G

G

A

A

M

Y

F

L

A

A

A

G

V

L

A

A

A

V

G

G

I

F

Y

W

P

Q

D

N

I

L

E

D

T

E

A

L

M

Q

A

E

A

K

M

-

G

-

T

A

G

V

F

I

E

E

K

R

E

E

Y

F

K

R

P

P

N

G

I

I

K

E

-

T

K

T

Q

E

K

R

L

N

Y

Y

R

R

binding adenosine-5'-diphosphate: G410 (= G467), A411 (= A469)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 16, 265, 266, 309
binding glycerol: 82, 83, 134, 244
binding phosphate ion: 232, 233, 235

1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
25% identity, 22% coverage: 418:540/566 of query aligns to 360:481/498 of 1bo5O

query
sites
1bo5O

K

R

G

G

A

A

I

I

T

F

G

G

L

L

G

T

L

R

G

G

T

V

D

N

A

A

P

N

R

H

F

I

R

R

A

A

L

T

A

L

A

E

A

S

T

I

C

A

F

Y

G

Q

A

T

K

R

A

D

I

V

V

L

D

E

R

A

F

M

K

Q

-

A

E

D

Q

S

G

G

V

I

P

R

V

L

K

H

G

A

I

L

I

R

G

V

I

D

G

G

V

-

A

A

K

V

K

A

S

N

A

N

Y

F

I

L

M

M

Q

Q

M

F

M

Q

A

S

D

D

V

I

L

L

E

G

M

T

P

R

I

V

R

E

I

R

H

P

R

E

F

V

E

R

H

E

T

V

C

T

A

A

L

L

G

G

A

A

M

Y

F

L

A

A

A

G

V

L

A

A

A

V

G

G

I

F

Y

W

P

Q

D

N

I

L

E

D

T

E

A

L

M

Q

A

E

A

K

M

-

G

-

T

A

G

V

F

I

E

E

K

R

E

E

Y

F

K

R

P

P

N

G

I

I

K

E

-

T

K

T

Q

E

K

R

L

N

Y

Y

R

R

Sites not aligning to the query:

binding 1,6-di-O-phosphono-beta-D-fructofuranose: 232, 233, 235
binding glycerol: 82, 83, 102, 134, 244, 245, 269

Query Sequence

>CA265_RS08625 FitnessBrowser__Pedo557:CA265_RS08625
MSTANYVIGVDYGTDSVRSVLVDTANGKEIASSVFLYPRWQKGLYCKPAVNQFRQHPLDY
IEGLTHTIKDCLAKAGGAEIAHLVKGISVDTTGSSPVAVDATGTPLALTKDFEENPNAMF
VLWKDHTSVKEAAEINEHATKFDTNYLKYVGGIYSSEWFWSKLLHILRVDLTIKKGAASW
VEHCDWIPFLLCGGNDISTMKRSRCAAGHKALWAEEFNGLPPEDFFSSLDPLLAGFRAKL
FTDTYTSDVSAGTLSEEWANKLGLNTDVVVGVGAFDAHMGAVGGQIEPYYLSKVMGTSTC
DILVAPNQDLHGKLINGICGQVNGSVIPGMAGLEAGQSAFGDVYAWFKNLISWPLNHLLT
ESEVIDEATATALKAELEGKIIANLSKQADALPNEDYAELAIDWLNGRRTPDANQELKGA
ITGLGLGTDAPRFFRALAAATCFGAKAIVDRFKEQGVPVKGIIGIGGVAKKSAYIMQMMA
DVLEMPIRIHRFEHTCALGAAMFAAVAAGIYPDIETAMAAMGTGFEKEYKPNIKKQKLYR
QHYQQYLGLGRYLEKYNKKDVKPYLS

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