SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing BPHYT_RS24200 FitnessBrowser__BFirm:BPHYT_RS24200 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 3 hits to proteins with known functional sites (download)

P70994 2-hydroxymuconate tautomerase; (2Z,4E)-2-hydroxyhexa-2,4-dienedioate keto-enol isomerase; 4-oxalocrotonate tautomerase; 4-OT; EC 5.3.2.6 from Bacillus subtilis (strain 168) (see paper)
33% identity, 98% coverage: 1:60/61 of query aligns to 1:60/62 of P70994

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P70994

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P2 (= P2) active site, Proton acceptor; via imino nitrogen; mutation to A: Absence of tautomerase activity using 2-hydroxymuconate. For 2-hydroxy-2,4-pentadienoate and phenylenolpyruvate, a strong decrease of catalytic efficiency and a 2-fold decrease of affinity is observed.
R12 (= R12) mutation to A: Absence of tautomerase activity using 2-hydroxymuconate. For 2-hydroxy-2,4-pentadienoate and phenylenolpyruvate, a strong decrease of catalytic efficiency and a 2-fold decrease of affinity is observed.

2opaA Ywhb binary complex with 2-fluoro-p-hydroxycinnamate
32% identity, 97% coverage: 2:60/61 of query aligns to 1:59/61 of 2opaA

query
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2opaA

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active site: V39 (≠ D40), Y50 (≠ W51)
binding 2-fluoro-3-(4-hydroxyphenyl)-2e-propeneoate: M7 (≠ L8), R11 (= R12), Y50 (≠ W51)

Sites not aligning to the query:

active site: 61

Q01468 2-hydroxymuconate tautomerase; 4-oxalocrotonate tautomerase; 4-OT; EC 5.3.2.6 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
34% identity, 97% coverage: 1:59/61 of query aligns to 1:59/63 of Q01468

query
sites
Q01468

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M1 (= M1) modified: Initiator methionine, Removed
P2 (= P2) active site, Proton acceptor; via imino nitrogen

Query Sequence

>BPHYT_RS24200 FitnessBrowser__BFirm:BPHYT_RS24200
MPTFRIELFEGRSVEQKRQFVEAITKATCESLGVEPNSVDIILTDVKRENWATAGRLWSD
A

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