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)
34% identity, 37% coverage: 135:220/232 of query aligns to 7:92/101 of Q51507

query
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Q51507

C

C

T

T

S

G

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L

D

A

E

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V

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R
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R

Q

E

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D

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Y

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Q
x
A

A

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G

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F

F

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K

K
x
A

T

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T

E

D

A

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R

P

A

A

P

P

A

E

R

R

V

V

E

A

Q

A

V

M

I

L

K

P

K

E

A

R

R

A

E

R

M

W

A

A

D

E

E

E

T

N

G

G

A

L

S

D

A

A

E

P

V

F

V

V

E

E

Q

G

V

L

Y

F

R

A

A

Q

M

I

I

I

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A

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F

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I
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I

A

A

E

E

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Q

L

I

N

K

R14 (= R142) binding
R31 (= R159) binding
A37 (≠ Q165) 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 (= K170) binding ; 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 (≠ K171) 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 (= I215) 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 (≠ E218) binding

2h9cA Native crystal structure of the isochorismate-pyruvate lyase from pseudomonas aeruginosa (see paper)
33% identity, 37% coverage: 135:220/232 of query aligns to 7:84/88 of 2h9cA

query
sites
2h9cA

C

C

T

T

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L

D

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D

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E

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I

I

D

D

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I

D

D

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D

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R
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R

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A

A

A

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R

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F

K

-

T

-

D

-

V

-

R

-

A

A

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P

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R

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M

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P

K

E

A

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R

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W

A

A

D

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E

E

T

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I

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Y

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binding nitrate ion: Q26 (≠ S154), R30 (≠ K158), R31 (= R159), K36 (≠ T164), A37 (≠ Q165), R40 (≠ G168), R45 (= R181), M49 (≠ V185), I75 (= I211), Y78 (≠ F214)

2h9dA Pyruvate-bound structure of the isochorismate-pyruvate lyase from pseudomonas aerugionsa (see paper)
31% identity, 37% coverage: 135:219/232 of query aligns to 7:81/84 of 2h9dA

query
sites
2h9dA

C

C

T

T

S

G

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L

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A

E

D

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E

R

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D

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D

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L

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R
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R

G

M

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Y

V

V

T

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Q

A

A

A

A

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G

R

F

F

K

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K

-

T

-

D

-

V

-

R

-

A

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P

-

A

-

R

R

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M

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P

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A

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R

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A

A

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E

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I

binding pyruvic acid: R31 (= R159), M47 (≠ V185)

Query Sequence

>PP_2170 FitnessBrowser__Putida:PP_2170
MATIRARKKADSTVSYTVQIRLKKKGVLVYQRSQTFARQQAAQAWATDGWRGGSAFSRSA
PRRCEQVIRNGLGILRVSRVSGHRDGHSLRRYTPSVEREADLAQKLHCTPRSPTTACSNQ
SQAHEKEVMQMDVPCTSLDEVRQRIDEIDRSLVSLLAKRGRLVTQAAGFKKTTDDVRAPA
RVEQVIKKAREMADETGASAEVVEQVYRAMISAFIAEELNTHAKLADEASAS

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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