SitesBLAST

Comparing WP_011951983.1 NCBI__GCF_000016765.1:WP_011951983.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 3 hits to proteins with known functional sites (download)

Q51507 Isochorismate pyruvate lyase; IPL; Chorismate mutase; CM; Salicylate biosynthesis protein; EC 4.2.99.21; EC 5.4.99.5 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 5 papers)
28% identity, 82% coverage: 14:102/108 of query aligns to 6:94/101 of Q51507

query
sites
Q51507

E

D

C

C

T

T

D

G

M

L

A

A

Q

D

V

I

R
|
R

A

E

A

A

I

I

D

D

G

R

L

I

D

D

T

L

L

D

I

I

V

V

S

Q

L

A

L

L

A

G

E

R

R
|
R

M

M

R

D

Y

Y

I

V

E

K

A
|
A

A

A

A

S

R

R

I

F

K
|
K

P
x
A

A

S

R

E

D

A

T

A

V

I

R

P

D

A

E

P

V

E

R

R

K

V

A

A

E

A

V

M

V

L

A

P

H

E

A

R

V

A

K

R

V

W

A

A

N

E

D

E

R

N

G

G

F

L

P

D

P

A

K

P

L

F

A

V

Y

E

R

G

L

L

Y

F

D

A

M

Q

L

I

V

I

E

H

G

W

S

Y

I
|
I

A

A

H

E

E
x
Q

F

I

D

K

V

Y

F

W

R14 (= R22) binding substrate

R31 (= R39) binding substrate

A37 (= A45) mutation to I: Increases the rate constant for the mutase activity by a factor of 1000, and also increases the lyase catalytic efficiency by a factor of 6.

K42 (= K50) binding substrate; mutation to A: Active across the entire pH range from 4 to 9. 11-fold reduction of the affinity for isochorismate and 7-fold reduction of the catalytic efficiency for lyase activity. 6-fold reduction of the affinity for chorismate and 15-fold reduction of the catalytic efficiency for mutase activity.; mutation to E: Loss of both lyase and mutase activity at any pH tested.; mutation to H: At pH 5, 15-fold reduction of the affinity for isochorismate, but only a slight reduction of the catalytic efficiency for lyase activity. At pH 7.5, 13-fold reduction of the affinity for isochorismate and 4-fold reduction of the catalytic efficiency for lyase activity. At pH 5, strong reduction of the affinity for chorismate, but only a 2-fold reduction of the catalytic efficiency for mutase activity. At pH 7.5, strong reduction of the affinity for chorismate, but only a slight reduction of the catalytic efficiency for mutase activity.; mutation to Q: Loss of mutase activity. 15-fold reduction of the affinity for isochorismate and 3-fold reduction of the catalytic efficiency for isochorismate-pyruvate lyase activity.

A43 (≠ P51) mutation to P: Slight reduction of the affinity for isochorismate and of the catalytic efficiency for isochorismate-pyruvate lyase activity. Slight reduction of the affinity for chorismate and of the catalytic efficiency for mutase activity.

I87 (= I95) mutation to T: 4-fold reduction of the affinity for isochorismate and 3-fold reduction of the catalytic efficiency for isochorismate-pyruvate lyase activity. 4-fold reduction of the affinity for chorismate and 15-fold reduction of the catalytic efficiency for mutase activity.

Q90 (≠ E98) binding substrate

query
sites
2h9dD

E

D

C

C

T

T

D

G

M

L

A

A

Q

D

V

I

R

R

A
x
E

A

A

I

I

D
|
D

G

R

L

I

D

D

T

L

L

D

I

I

V

V

S

Q

L

A

L

L

A

G

E

R

R
|
R

M

M

R

D

Y

Y

I

V

E

K

A

A

A

S

R

R

I

F

K
|
K

P

A

A

S

R

E

D

A

T

A

V

I

R

P

D

A

E

P

V

E

R

R

K

V

A

A

E

A

V
x
M

V

L

A

P

H

E

A

R

V

A

K

R

V

W

A

A

N

E

D

E

R

N

G

G

F

L

P

D

P

A

K

P

L

F

A

V

Y

E

R

G

L

L

Y

F

D

A

M

Q

L

I

V

I

E

H

G

W

S

Y

I

I

A

A

H

E

E
x
Q

F

I

D

K

V

Y

F

W

query
sites
2h9cA

E

D

C

C

T

T

D

G

M

L

A

A

Q

D

V

I

R

R

A

E

A

A

I

I

D

D

G

R

L

I

D

D

T

L

L

D

I

I

V

V

S
x
Q

L

A

L

L

A

G

E
x
R

R
|
R

M

M

R

D

Y

Y

I

V

E
x
K

A
|
A

A

A

A

S

R
|
R

I

F

K

A

P

P

A

E

R

-

D

-

T

-

V

-

R

-

D

-

E

-

V

-

R
|
R

K

V

A

A

E

A

V
x
M

V

L

A

P

H

E

A

R

V

A

K

R

V

W

A

A

N

E

D

E

R

N

G

G

F

L

P

D

P

A

K

P

L

F

A

V

Y

E

R

G

L

L

Y

F

D

A

M

Q

L

I

V
x
I

E

H

G

W

S
x
Y

I

I

A

A

H

E

E

Q

F

I

D

K

V

Y

F

W

Query Sequence

>WP_011951983.1 NCBI__GCF_000016765.1:WP_011951983.1
MTDITASKAVPAAECTDMAQVRAAIDGLDTLIVSLLAERMRYIEAAARIKPARDTVRDEV
RKAEVVAHAVKVANDRGFPPKLAYRLYDMLVEGSIAHEFDVFDARDPS

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

SitesBLAST – Find functional sites

SitesBLAST

Query Sequence

SitesBLAST's Database