SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing SMc02253 FitnessBrowser__Smeli:SMc02253 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 4 hits to proteins with known functional sites (download)

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, 91% coverage: 3:94/101 of query aligns to 2:92/101 of Q51507

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Q51507

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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

2h9dD Pyruvate-bound structure of the isochorismate-pyruvate lyase from pseudomonas aerugionsa (see paper)
38% identity, 91% coverage: 3:94/101 of query aligns to 2:92/100 of 2h9dD

query
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2h9dD

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binding calcium ion: E15 (≠ V16), D18 (= D19)
binding pyruvic acid: R31 (= R32), K42 (= K43), M57 (≠ V59), Q90 (≠ E92)

2h9cA Native crystal structure of the isochorismate-pyruvate lyase from pseudomonas aeruginosa (see paper)
35% identity, 91% coverage: 3:94/101 of query aligns to 2:84/88 of 2h9cA

query
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2h9cA

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binding nitrate ion: Q26 (≠ T27), R30 (≠ E31), R31 (= R32), K36 (≠ E37), A37 (≠ R38), R40 (≠ E41), R45 (= R55), M49 (≠ V59), I75 (≠ V85), Y78 (≠ A88)

2h9dA Pyruvate-bound structure of the isochorismate-pyruvate lyase from pseudomonas aerugionsa (see paper)
34% identity, 91% coverage: 3:94/101 of query aligns to 2:82/84 of 2h9dA

query
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2h9dA

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

Query Sequence

>SMc02253 FitnessBrowser__Smeli:SMc02253
MQKTPAECTTMADIRVEIDRLDRALMTLFAERWGYIERAAEIKRPLNLKADIPARVAEVK
ENARRNAVELGLDPDFYERFWGQLVERAIAHERKLLGEDDA

Or try a new SitesBLAST search

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