SitesBLAST

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, 99% coverage: 1:99/100 of query aligns to 1:99/101 of Q51507

query
sites
Q51507

M

M

S

K

E

T

V

P

K

E

K

D

C

C

N

T

S

G

L

L

L

A

E

D

I

I

R
|
R

N

E

E

A

I

I

D

D

K

R

I

I

D

D

D

L

L

D

I

I

V

V

E

Q

L

A

I

L

S

G

K

R

R
|
R

S

M

H

D

L

Y

V

V

R

K

Q
x
A

A

A

A

S

S

R

F

F

K
|
K

N
x
A

S

S

I

E

E

A

V

I

K

P

A

A

D

P

D

E

R

R

V

V

D

A

Y

A

I

M

L

L

Q

P

K

E

V

R

R

A

H

R

S

W

A

A

I

E

K

E

A

N

D

G

V

L

S

D

P

A

N

P

M

F

I

V

S

E

D

G

L

L

F

F

K

A

I

Q

M

I

I

I

N

H

E

W

M

Y

V
x
I

E

A

T

E

E
x
Q

I

I

S

K

E

Y

F

W

R

R

N

Q

T

T

Q

R

T

G

R14 (= R14) binding substrate

R31 (= R31) binding substrate

A37 (≠ Q37) 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 (= K42) 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 (≠ N43) 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 (≠ V87) 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 (≠ E90) binding substrate

Query Sequence

>WP_011371944.1 NCBI__GCF_000012965.1:WP_011371944.1
MSEVKKCNSLLEIRNEIDKIDDLIVELISKRSHLVRQAASFKNSIEEVKADDRVDYILQK
VRHSAIKADVSPNMISDLFKIMINEMVETEISEFRNTQTF

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

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Query Sequence

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