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

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)
23% identity, 25% coverage: 393:530/557 of query aligns to 339:474/499 of 1bu6Y

query
sites
1bu6Y

N

N

G

G

A

V

S

Y

A

V

L

V

D

P

W

A

I

F

N

T

G

G

R

L

R

G

S

A

P

P

F

Y

A

W

K

D

E

P

T

Y

L

A

K

R

G

G

A

A

F

I

L

F

N

G

L

L

H

T

M

R

G

G

T

V

Q

N

A

A

S

N

H

H

M

I

F

I

R

R

A

A

M

T

V

L

E

E

A

S

L

I

C

A

F

Y

G

Q

S

T

K

R

K

D

I

V

I

L

D

E

H

A

L

M

E

Q

G

A

K

D

G

S

L

G

T

I

V

R

E

L

E

H

I

A

I

L

A

R

I

V

G

D

G

G

V

G

A

A

N

V

K

A

S

N

P

N

L

F

V

L

M

M

Q

Q

T

F

M

Q

A

S

D

D

I

I

I

L

G

G

K

T

P

R

I

V

K

E

I

R

A

P

A

E

S

V

K

R

E

E

A

V

P

T

A

A

L

L

G

G

A

A

I

Y

H

L

A

A

A

G

V

L

A

A

S

V

K

G

V

F

Y

W

P

Q

S

N

M

L

D

D

Q

E

A

L

V

Q

A

E

K

K

M

A

V

V

P

-

A

-

F

I

K

E

K

R

V

E

Y

F

S

R

P

P

D

G

L

I

Q

E

Sites not aligning to the query:

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

1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
23% identity, 25% coverage: 393:530/557 of query aligns to 335:470/494 of 1gllO

query
sites
1gllO

N

N

G

G

A

V

S

Y

A

V

L

V

D

P

W

A

I

F

N

T

G

G

R

L

R

G

S

A

P

P

F

Y

A

W

K

D

E

P

T

Y

L

A

K

R

G

G

A

A

F

I

L

F

N

G

L

L

H

T

M

R

G

G

T

V

Q

N

A

A

S

N

H

H

M

I

F

I

R

R

A

A

M

T

V

L

E

E

A

S

L

I

C

A

F

Y

G

Q

S

T

K

R

K

D

I

V

I

L

D

E

H

A

L

M

E

Q

G

A

K

D

G

S

L

G

T

I

V

R

E

L

E

H

I

A

I

L

A

R

I

V

G

D

G

G

V
x
G

A

A

N

V

K

A

S
x
N

P

N

L

F

V

L

M

M

Q

Q

T

F

M

Q

A

S

D

D

I

I

I

L

G

G

K

T

P

R

I

V

K

E

I

R

A

P

A

E

S

V

K

R

E

E

A

V

P

T

A

A

L

L

G

G

A

A

I

Y

H

L

A

A

A

G

V

L

A

A

S

V

K

G

V

F

Y

W

P

Q

S

N

M

L

D

D

Q

E

A

L

V

Q

A

E

K

K

M

A

V

V

P

-

A

-

F

I

K

E

K

R

V

E

Y

F

S

R

P

P

D

G

L

I

Q

E

binding phosphomethylphosphonic acid adenylate ester: G406 (≠ V464), N410 (≠ S468)

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)
23% identity, 25% coverage: 393:530/557 of query aligns to 335:470/494 of 1gljO

query
sites
1gljO

N

N

G

G

A

V

S

Y

A

V

L

V

D

P

W

A

I

F

N

T

G

G

R

L

R

G

S

A

P

P

F

Y

A

W

K

D

E

P

T

Y

L

A

K

R

G

G

A

A

F

I

L

F

N

G

L

L

H

T

M

R

G

G

T

V

Q

N

A

A

S

N

H

H

M

I

F

I

R

R

A

A

M

T

V

L

E

E

A

S

L

I

C

A

F

Y

G

Q

S

T

K

R

K

D

I

V

I

L

D

E

H

A

L

M

E

Q

G

A

K

D

G

S

L

G

T

I

V

R

E

L

E

H

I

A

I

L

A

R

I

V

G

D

G

G

V
x
G

A
|
A

N

V

K

A

S

N

P

N

L

F

V

L

M

M

Q

Q

T

F

M

Q

A

S

D

D

I

I

I

L

G

G

K

T

P

R

I

V

K

E

I

R

A

P

A

E

S

V

K

R

E

E

A

V

P

T

A

A

L

L

G

G

A

A

I

Y

H

L

A

A

A

G

V

L

A

A

S

V

K

G

V

F

Y

W

P

Q

S

N

M

L

D

D

Q

E

A

L

V

Q

A

E

K

K

M

A

V

V

P

-

A

-

F

I

K

E

K

R

V

E

Y

F

S

R

P

P

D

G

L

I

Q

E

binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: G406 (≠ V464), A407 (= A465)

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

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)
23% identity, 25% coverage: 393:530/557 of query aligns to 339:474/498 of 1glfO

query
sites
1glfO

N

N

G

G

A

V

S

Y

A

V

L

V

D

P

W

A

I

F

N

T

G

G

R

L

R

G

S

A

P

P

F

Y

A

W

K

D

E

P

T

Y

L

A

K

R

G

G

A

A

F

I

L

F

N

G

L

L

H

T

M

R

G

G

T

V

Q

N

A

A

S

N

H

H

M

I

F

I

R

R

A

A

M

T

V

L

E

E

A

S

L

I

C

A

F

Y

G

Q

S

T

K

R

K

D

I

V

I

L

D

E

H

A

L

M

E

Q

G

A

K

D

G

S

L

G

T

I

V

R

E

L

E

H

I

A

I

L

A

R

I

V

G

D

G

G

V
x
G

A
|
A

N

V

K

A

S

N

P

N

L

F

V

L

M

M

Q

Q

T

F

M

Q

A

S

D

D

I

I

I

L

G

G

K

T

P

R

I

V

K

E

I

R

A

P

A

E

S

V

K

R

E

E

A

V

P

T

A

A

L

L

G

G

A

A

I

Y

H

L

A

A

A

G

V

L

A

A

S

V

K

G

V

F

Y

W

P

Q

S

N

M

L

D

D

Q

E

A

L

V

Q

A

E

K

K

M

A

V

V

P

-

A

-

F

I

K

E

K

R

V

E

Y

F

S

R

P

P

D

G

L

I

Q

E

binding adenosine-5'-diphosphate: G410 (≠ V464), A411 (= A465)

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

1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
23% identity, 25% coverage: 393:530/557 of query aligns to 335:470/494 of 1bwfO

query
sites
1bwfO

N

N

G

G

A

V

S

Y

A

V

L

V

D

P

W

A

I

F

N

T

G

G

R

L

R

G

S

A

P

P

F

Y

A

W

K

D

E

P

T

Y

L

A

K

R

G

G

A

A

F

I

L

F

N

G

L

L

H

T

M

R

G

G

T

V

Q

N

A

A

S

N

H

H

M

I

F

I

R

R

A

A

M

T

V

L

E

E

A

S

L

I

C

A

F

Y

G

Q

S

T

K

R

K

D

I

V

I

L

D

E

H

A

L

M

E

Q

G

A

K

D

G

S

L

G

T

I

V

R

E

L

E

H

I

A

I

L

A

R

I

V

G

D

G

G

V
x
G

A

A

N

V

K

A

S
x
N

P

N

L

F

V

L

M

M

Q

Q

T

F

M

Q

A

S

D

D

I

I

I

L

G

G

K

T

P

R

I

V

K

E

I

R

A

P

A

E

S

V

K

R

E

E

A

V

P

T

A

A

L

L

G

G

A

A

I

Y

H

L

A

A

A

G

V

L

A

A

S

V

K

G

V

F

Y

W

P

Q

S

N

M

L

D

D

Q

E

A

L

V

Q

A

E

K

K

M

A

V

V

P

-

A

-

F

I

K

E

K

R

V

E

Y

F

S

R

P

P

D

G

L

I

Q

E

binding phosphodifluoromethylphosphonic acid-adenylate ester: G406 (≠ V464), N410 (≠ S468)

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

1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
23% identity, 25% coverage: 393:530/557 of query aligns to 339:474/498 of 1bo5O

query
sites
1bo5O

N

N

G

G

A

V

S

Y

A

V

L

V

D

P

W

A

I

F

N

T

G

G

R

L

R

G

S

A

P

P

F

Y

A

W

K

D

E

P

T

Y

L

A

K

R

G

G

A

A

F

I

L

F

N

G

L

L

H

T

M

R

G

G

T

V

Q

N

A

A

S

N

H

H

M

I

F

I

R

R

A

A

M

T

V

L

E

E

A

S

L

I

C

A

F

Y

G

Q

S

T

K

R

K

D

I

V

I

L

D

E

H

A

L

M

E

Q

G

A

K

D

G

S

L

G

T

I

V

R

E

L

E

H

I

A

I

L

A

R

I

V

G

D

G

G

V

G

A

A

N

V

K

A

S

N

P

N

L

F

V

L

M

M

Q

Q

T

F

M

Q

A

S

D

D

I

I

I

L

G

G

K

T

P

R

I

V

K

E

I

R

A

P

A

E

S

V

K

R

E

E

A

V

P

T

A

A

L

L

G

G

A

A

I

Y

H

L

A

A

A

G

V

L

A

A

S

V

K

G

V

F

Y

W

P

Q

S

N

M

L

D

D

Q

E

A

L

V

Q

A

E

K

K

M

A

V

V

P

-

A

-

F

I

K

E

K

R

V

E

Y

F

S

R

P

P

D

G

L

I

Q

E

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

P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
23% identity, 25% coverage: 393:530/557 of query aligns to 341:476/502 of P0A6F3

query
sites
P0A6F3

N

N

G

G

A

V

S

Y

A

V

L

V

D

P

W

A

I

F

N

T

G

G

R

L

R

G

S

A

P

P

F

Y

A

W

K

D

E

P

T

Y

L

A

K

R

G

G

A

A

F

I

L

F

N

G

L

L

H

T

M

R

G

G

T

V

Q

N

A

A

S

N

H

H

M

I

F

I

R

R

A

A

M

T

V

L

E

E

A

S

L

I

C

A

F

Y

G

Q

S

T

K

R

K

D

I

V

I

L

D

E

H

A

L

M

E

Q

G

A

K

D

G

S

L

G

T

I

V

R

E

L

E

H

I

A

I

L

A

R

I

V

G

D

G

G

V
x
G

A

A

N

V

K

A

S
x
N

P

N

L

F

V

L

M

M

Q

Q

T

F

M

Q

A

S

D

D

I

I

I

L

G

G

K

T

P

R

I

V

K

E

I

R

A

P

A

E

S

V

K

R

E

E

A

V

P

T

A

A

L

L

G

G

A

A

I

Y

H

L

A

A

A

G

V

L

A

A

S

V

K

G

V

F

Y

W

P

Q

S

N

M

L

D

D

Q

E

A

L

V

Q

A

E

K

K

M

A

V

V

P

-

A

-

F

I

K

E

K

R

V

E

Y

F

S

R

P

P

D

G

L
x
I

Q

E

G412 (≠ V464) binding
N416 (≠ S468) binding
I475 (≠ L529) 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.

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
479 binding
480 R→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.

1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
23% identity, 25% coverage: 393:530/557 of query aligns to 330:465/489 of 1gldG

query
sites
1gldG

N

N

G

G

A

V

S

Y

A

V

L

V

D

P

W

A

I

F

N

T

G

G

R

L

R

G

S

A

P

P

F

Y

A

W

K

D

E

P

T

Y

L

A

K

R

G

G

A

A

F

I

L

F

N

G

L

L

H

T

M

R

G

G

T

V

Q

N

A

A

S

N

H

H

M

I

F

I

R

R

A

A

M

T

V

L

E

E

A

S

L

I

C

A

F

Y

G

Q

S

T

K

R

K

D

I

V

I

L

D

E

H

A

L

M

E

Q

G

A

K

D

G

S

L

G

T

I

V

R

E

L

E

H

I

A

I

L

A

R

I

V

G

D

G

G

V
x
G

A
|
A

N

V

K

A

S
x
N

P

N

L

F

V

L

M

M

Q

Q

T

F

M

Q

A

S

D

D

I

I

I

L

G

G

K

T

P

R

I

V

K

E

I

R

A

P

A

E

S

V

K

R

E

E

A

V

P

T

A

A

L

L

G

G

A

A

I

Y

H

L

A

A

A

G

V

L

A

A

S

V

K

G

V

F

Y

W

P

Q

S

N

M

L

D

D

Q

E

A

L

V

Q

A

E

K

K

M

A

V

V

P

-

A

-

F

I

K

E

K

R

V

E

Y

F

S

R

P

P

D

G

L

I

Q

E

binding adenosine-5'-diphosphate: G401 (≠ V464), A402 (= A465), N405 (≠ S468)

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

Query Sequence

>Echvi_4514 FitnessBrowser__Cola:Echvi_4514
MSKNFVIGVDFGTDSVRSILVDTLDGKIVKSAVYRYPRWSKKLYCDAGSHQFRQHPLDHL
EGLEHTVSAIIRDSGIDPDSVKGIGVATTGSSPIPVDENGDALSMSSRFSNNPNAMVVLW
KDHTAVAEAEEITKAAKNGEVDYTAFSGGSYSSEWFWAKILSVYKKDPGVARNTCTWMEH
CDFIVGQLTGERPLNLKRSRTAAGHKAMWNKKWSGLPPASFWGGISPELGSLRETLYEQT
FHGSEKAGHLCSKWAEKLGLSADTAVAVGTLDAHAGAVGAGISPNTLVKVVGTSTCDILV
GSPTDPELDPIEGICGQVEDAVLPGTIGLEAGQAGFGDVLAWFAEVVLGPSRQIIHRSTQ
LDAVIKETIIEELEHSILDELSREALELAPCLNGASALDWINGRRSPFAKETLKGAFLNL
HMGTQASHMFRAMVEALCFGSKKIIDHLEGKGLTVEEIIAIGGVANKSPLVMQTMADIIG
KPIKIAASKEAPALGAAIHAAVASKVYPSMDQAVAKMVPAFKKVYSPDLQHQQVYVEKYK
MYEREGEVVENLKLTTQ

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