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)
55% identity, 91% coverage: 4:100/107 of query aligns to 1:97/101 of Q51507

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Q51507

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R14 (= R17) binding
R31 (= R34) binding
A37 (= A40) 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 (= A46) 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.
Q90 (= Q93) binding

2h9cA Native crystal structure of the isochorismate-pyruvate lyase from pseudomonas aeruginosa (see paper)
48% identity, 90% coverage: 4:99/107 of query aligns to 1:88/88 of 2h9cA

query
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2h9cA

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binding nitrate ion: Q26 (≠ E29), R30 (≠ L33), R31 (= R34), K36 (= K39), A37 (= A40), R40 (≠ Q43), R45 (= R56), M49 (= M60), I75 (= I86), Y78 (≠ N89)

2h9dA Pyruvate-bound structure of the isochorismate-pyruvate lyase from pseudomonas aerugionsa (see paper)
47% identity, 88% coverage: 4:97/107 of query aligns to 1:84/84 of 2h9dA

query
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2h9dA

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binding pyruvic acid: R31 (= R34), M47 (= M60)

Query Sequence

>AO353_23985 FitnessBrowser__pseudo3_N2E3:AO353_23985
MSPLKTPEACENLNDIRAGIDFYDRQILESLKLRLGYVKAAAQFKANERAIPAPERVAAM
LEDRREWAVAAGFEVAFVEKLYKHIIHWNIQQQILHWQETYSDRNTA

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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