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)
38% identity, 89% coverage: 3:92/101 of query aligns to 2:90/101 of Q51507

query
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Q51507

K

K

T

T

P

P

A

E

E

D

C

C

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T

T

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D

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Y

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A

A

A

A

S

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K

R
x
A

P

S

L

-

N

-

L

-

K

E

A

A

D

A

I

I

P

P

A

A

-

P

-

E

R

R

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A

A

E

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E

P

N

E

A

R

R

A

R

R

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A

A

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E

A

E

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N

G

G

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L

E

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A

D

P

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F

Y

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E

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Q

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Q

R14 (= R15) binding substrate
R31 (= R32) binding substrate
A37 (≠ R38) 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 (= K43) 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 (≠ R44) 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 (= I89) 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 (≠ E92) binding substrate

2h9dA Pyruvate-bound structure of the isochorismate-pyruvate lyase from pseudomonas aerugionsa (see paper)
34% identity, 89% coverage: 3:92/101 of query aligns to 2:80/84 of 2h9dA

query
sites
2h9dA

K

K

T

T

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C

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T

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M

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E

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binding pyruvic acid: R31 (= R32), M47 (≠ D51)

2h9cA Native crystal structure of the isochorismate-pyruvate lyase from pseudomonas aeruginosa (see paper)
36% identity, 89% coverage: 3:92/101 of query aligns to 2:82/88 of 2h9cA

query
sites
2h9cA

K

K

T

T

P

P

A

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E

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C

T

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T

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A

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Y

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E

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binding nitrate ion: Q26 (≠ A27), R30 (≠ E31), R31 (= R32), K36 (≠ R38), A37 (= A39), R40 (≠ I42), R45 (≠ N47), M49 (≠ D51), I75 (= I85), Y78 (≠ A88)

Query Sequence

>WP_012706774.1 NCBI__GCF_000018545.1:WP_012706774.1
MPKTPAECTTMADVRAEIDRLDRALMALFAERWGYIDRAAEIKRPLNLKADIPARVAEVR
ENARRHAVAFGLEPDFYEELWAQLIDHAIAHERTLLGEDQE

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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