SitesBLAST
Comparing BPHYT_RS29385 FitnessBrowser__BFirm:BPHYT_RS29385 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
71% identity, 100% coverage: 1:400/400 of query aligns to 4:403/403 of 6pccA
- active site: C93 (= C90), A359 (≠ H356), C389 (= C386), G391 (= G388)
- binding coenzyme a: C93 (= C90), I148 (= I145), M166 (= M163), R229 (= R227), T232 (= T229), L240 (= L237), A252 (= A249), G253 (= G250), S256 (= S253), G257 (= G254), V258 (= V255), N325 (= N322), A327 (= A324), F328 (= F325), L361 (= L358)
- binding hexanal: N61 (= N58), L92 (= L89), T146 (= T143), T147 (= T144), I148 (= I145), G149 (= G146), R151 (= R148), M166 (= M163), L361 (= L358), G391 (= G388)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
71% identity, 100% coverage: 1:400/400 of query aligns to 4:403/403 of 6pcbA
- active site: C93 (= C90), A359 (≠ H356), C389 (= C386), G391 (= G388)
- binding coenzyme a: C93 (= C90), I148 (= I145), M166 (= M163), R229 (= R227), T232 (= T229), L237 (= L234), L240 (= L237), A252 (= A249), G253 (= G250), S256 (= S253), G257 (= G254), V258 (= V255), N325 (= N322), A327 (= A324), F328 (= F325), L361 (= L358)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
70% identity, 100% coverage: 1:400/400 of query aligns to 5:401/401 of 6pcdA
- active site: S94 (≠ C90), A357 (≠ H356), C387 (= C386), G389 (= G388)
- binding coenzyme a: I149 (= I145), M167 (= M163), R227 (= R227), T230 (= T229), L238 (= L237), A250 (= A249), G251 (= G250), S254 (= S253), G255 (= G254), V256 (= V255), N323 (= N322), A325 (= A324), F326 (= F325), A357 (≠ H356), L359 (= L358)
- binding octanal: A61 (= A57), N62 (= N58), L93 (= L89), E122 (= E118), T147 (= T143), T148 (= T144), I149 (= I145), G150 (= G146), R152 (= R148), M167 (= M163), L359 (= L358), G389 (= G388)
P14611 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) (see paper)
44% identity, 100% coverage: 1:399/400 of query aligns to 1:392/393 of P14611
- C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ S162) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ H225) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R227) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S253) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H356) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C386) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
P45359 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; CaTHL; EC 2.3.1.9 from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) (see paper)
43% identity, 100% coverage: 1:399/400 of query aligns to 1:391/392 of P45359
- V77 (≠ Q79) mutation to Q: 3-fold increase in thiolase activity, prevents disulfide bond formation under oxidized condition and results in the loss of regulatory mechanism based on redox-switch modulation; when associated with Y-153 and K-286.
- C88 (= C90) modified: Disulfide link with 378, In inhibited form
- S96 (≠ G98) binding
- N153 (= N151) mutation to Y: 3-fold increase in thiolase activity, prevents disulfide bond formation under oxidized condition and results in the loss of regulatory mechanism based on redox-switch modulation; when associated with Q-77 and K-286.
- GS 279:280 (≠ AT 285:286) binding
- A286 (≠ R292) mutation to K: 3-fold increase in thiolase activity, prevents disulfide bond formation under oxidized condition and results in the loss of regulatory mechanism based on redox-switch modulation; when associated with Q-77 and Y-153.
- C378 (= C386) modified: Disulfide link with 88, In inhibited form
- A386 (= A394) binding
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
44% identity, 100% coverage: 3:400/400 of query aligns to 2:398/400 of 5bz4K
- active site: C87 (= C90), H354 (= H356), C384 (= C386), G386 (= G388)
- binding coenzyme a: C87 (= C90), R146 (vs. gap), M160 (= M163), L161 (≠ P164), R220 (= R227), L228 (= L234), L231 (= L237), A246 (= A249), G247 (= G250), S250 (= S253), Q252 (≠ V255), M291 (= M294), A321 (= A324), F322 (= F325), H354 (= H356)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
44% identity, 100% coverage: 1:399/400 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H356), C379 (= C386), G381 (= G388)
- binding coenzyme a: S88 (≠ C90), L148 (= L153), H156 (≠ S162), R221 (= R227), S228 (≠ T233), L232 (= L237), F236 (≠ V241), A244 (= A249), A247 (= A252), S248 (= S253), G249 (= G254), L250 (≠ V255), A319 (= A324), F320 (= F325), H349 (= H356), I351 (≠ L358), C379 (= C386)
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
42% identity, 100% coverage: 1:399/400 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C90), H348 (= H356), S378 (≠ C386), G380 (= G388)
- binding coenzyme a: L148 (vs. gap), H156 (≠ S162), M157 (= M163), R220 (= R227), L228 (= L234), L231 (= L237), F235 (≠ V241), A243 (= A249), G244 (= G250), S247 (= S253), G248 (= G254), L249 (≠ V255), A318 (= A324), F319 (= F325), H348 (= H356)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
44% identity, 100% coverage: 2:400/400 of query aligns to 3:392/392 of P07097
- Q64 (≠ R65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C386) mutation to G: Loss of activity.
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
46% identity, 100% coverage: 1:399/400 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C90), A348 (= A353), A378 (≠ C383), L380 (≠ M385)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C90), L151 (= L153), H159 (≠ D161), M160 (= M163), F238 (≠ V241), A246 (= A249), S250 (= S253), G251 (= G254), I252 (≠ V255), M291 (= M294), A321 (= A324), F322 (= F325), H351 (= H356)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
44% identity, 99% coverage: 6:400/400 of query aligns to 4:389/389 of 2vu2A