SitesBLAST

Comparing WP_013419231.1 NCBI__GCF_000166055.1:WP_013419231.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 2 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)
29% identity, 86% coverage: 1:90/105 of query aligns to 1:87/101 of Q51507

query
sites
Q51507

M

M

T

K

T

T

P

P

R

E

K

-

A

-

D

D

C

C

E

T

N

G

M

L

D

A

Q

D

V

I

R
|
R

V

E

E

A

I

I

D

D

R

R

V

I

D

D

D

L

A

D

I

I

L

V

D

Q

L

A

V

L

A

G

E

R

R
|
R

F

M

S

D

Y

Y

V

V

D

K

R
x
A

A

A

W

S

Q

R

L

F

K
|
K

K
x
A

N

S

T

E

H

A

E

A

A

I

T

P

V

A

P

P

W

E

R

R

I

V

R

A

Q

A

V

M

I

L

D

P

R

E

V

R

E

A

A

R

R

W

A

A

K

E

E

E

R

N

D

G

L

L

P

D

P

A

E

P

L

F

A

V

V

E

A

G

L

L

W

F

R

A

Q

Q

M

I

I

I

G

H

W

W

F

Y

I
|
I

R14 (= R17) binding substrate

R31 (= R34) binding substrate

A37 (≠ R40) 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 (= K45) 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 (≠ K46) 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 (= I90) 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.

Sites not aligning to the query:

90 binding substrate

query
sites
2h9dD

M

M

T

K

T

T

P

P

R

E

K

-

A

-

D

D

C

C

E

T

N

G

M

L

D

A

Q

D

V

I

R

R

V
x
E

E

A

I

I

D
|
D

R

R

V

I

D

D

D

L

A

D

I

I

L

V

D

Q

L

A

V

L

A

G

E

R

R
|
R

F

M

S

D

Y

Y

V

V

D

K

R

A

A

A

W

S

Q

R

L

F

K
|
K

K

A

N

S

T

E

H

A

E

A

A

I

T

P

V

A

P

P

W

E

R

R

I

V

R

A

Q

A

V
x
M

I

L

D

P

R

E

V

R

E

A

A

R

R

W

A

A

K

E

E

E

R

N

D

G

L

L

P

D

P

A

E

P

L

F

A

V

V

E

A

G

L

L

W

F

R

A

Q

Q

M

I

I

I

G

H

W

W

F

Y

I

I

Sites not aligning to the query:

Query Sequence

>WP_013419231.1 NCBI__GCF_000166055.1:WP_013419231.1
MTTPRKAADCENMDQVRVEIDRVDDAILDLVAERFSYVDRAWQLKKNTHEATVPWRIRQV
IDRVEARAKERDLPPELAVALWRQMIGWFIQYEEEKLAKRGEPKD

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

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