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)
33% identity, 93% coverage: 7:100/101 of query aligns to 4:96/101 of Q51507

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Q51507

P

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E

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D

C

C

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Y

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A

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E

N

-

W

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A

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I

I

P

P

A

A

-

P

-

E

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R

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G

G

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R14 (= R17) binding
R31 (= R34) binding
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 ; 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 (≠ T46) 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 (= I91) 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 (≠ E94) binding

2h9cA Native crystal structure of the isochorismate-pyruvate lyase from pseudomonas aeruginosa (see paper)
31% identity, 93% coverage: 7:100/101 of query aligns to 4:88/88 of 2h9cA

query
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2h9cA

P

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binding nitrate ion: Q26 (≠ A29), R30 (≠ E33), R31 (= R34), K36 (= K45), A37 (≠ T46), R40 (≠ N49), R45 (= R57), M49 (≠ V61), I75 (≠ V87), Y78 (≠ S90)

2h9dA Pyruvate-bound structure of the isochorismate-pyruvate lyase from pseudomonas aerugionsa (see paper)
29% identity, 89% coverage: 7:96/101 of query aligns to 4:82/84 of 2h9dA

query
sites
2h9dA

P

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binding pyruvic acid: R31 (= R34), M47 (≠ V61)

Query Sequence

>GFF586 FitnessBrowser__Phaeo:GFF586
MTDRHPPQDCADMPALRQQIDRLDRDLIALLVERAGYIDRAIALKTANNWPARIPARVEE
VVANARTTASAAGLDPDLVESLWRQLVEWSIAREARVIREE

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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