SitesBLAST
Comparing AZOBR_RS28180 AZOBR_RS28180 acetyl-CoA acetyltransferase 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)
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)
45% identity, 98% coverage: 5:395/397 of query aligns to 1:391/392 of P45359
- V77 (≠ D81) 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 (= C92) modified: Disulfide link with 378, In inhibited form
- S96 (≠ M100) binding
- N153 (≠ E157) 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 283:284) binding
- A286 (= A290) 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 (= C382) modified: Disulfide link with 88, In inhibited form
- A386 (= A390) binding
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
50% identity, 99% coverage: 2:394/397 of query aligns to 2:395/397 of 6aqpA
- active site: C93 (= C92), H353 (= H352), C383 (= C382), G385 (= G384)
- binding coenzyme a: C93 (= C92), L153 (= L152), M162 (= M162), Y188 (≠ L188), N226 (≠ K226), L227 (≠ V227), N228 (≠ A228), K231 (= K231), L232 (≠ I232), I235 (≠ L235), F239 (= F239), A248 (= A247), P249 (≠ A248), S252 (= S251), P253 (≠ A252), L254 (≠ N253), F293 (= F292), A323 (= A322), F324 (= F323), H353 (= H352), I355 (= I354)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
45% identity, 98% coverage: 5:395/397 of query aligns to 1:391/393 of 6bn2A
Q4WCL5 Acetyl-CoA acetyltransferase erg10B, cytosolic; Acetoacetyl-CoA thiolase erg10B; ACAT; Cytosolic thiolase erg10B; CT; Ergosterol biosynthesis protein 10B; EC 2.3.1.9 from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
50% identity, 99% coverage: 2:394/397 of query aligns to 1:396/398 of Q4WCL5
- Y187 (≠ L188) binding
- N229 (≠ A228) binding
- K232 (= K231) binding
- A249 (= A247) binding
- P250 (≠ A248) binding
- S252 (= S250) binding
- S253 (= S251) binding
- V350 (≠ C348) binding
- N385 (≠ I383) binding
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
50% identity, 99% coverage: 2:394/397 of query aligns to 2:397/399 of 6aqpC
- active site: C93 (= C92), H355 (= H352), C385 (= C382), G387 (= G384)
- binding acetyl coenzyme *a: C93 (= C92), L153 (= L152), M162 (= M162), Y188 (≠ L188), N228 (≠ K226), L229 (≠ V227), N230 (≠ A228), K233 (= K231), L234 (≠ I232), I237 (≠ L235), F241 (= F239), A250 (= A247), P251 (≠ A248), S254 (= S251), P255 (≠ A252), L256 (≠ N253), F295 (= F292), A325 (= A322), F326 (= F323), H355 (= H352)
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
45% identity, 98% coverage: 5:395/397 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C92), H348 (= H352), S378 (≠ C382), G380 (= G384)
- binding coenzyme a: L148 (= L152), H156 (≠ P161), M157 (= M162), R220 (vs. gap), L228 (≠ I232), L231 (= L235), F235 (= F239), A243 (= A247), G244 (≠ A248), S247 (= S251), G248 (≠ A252), L249 (≠ N253), A318 (= A322), F319 (= F323), H348 (= H352)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
48% identity, 97% coverage: 9:394/397 of query aligns to 4:390/394 of 7cw5B
- active site: C87 (= C92), H348 (= H352), C378 (= C382), G380 (= G384)
- binding coenzyme a: C87 (= C92), G146 (= G151), L147 (= L152), H155 (≠ R160), M156 (= M162), H182 (≠ L188), R220 (≠ L225), T223 (≠ V227), L228 (≠ I232), L231 (= L235), F235 (= F239), A243 (= A247), G244 (≠ A248), P247 (≠ S251), G248 (≠ A252), L249 (≠ N253), H348 (= H352), G380 (= G384)
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)
48% identity, 98% coverage: 8:395/397 of query aligns to 4:392/393 of P14611
- C88 (= C92) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ R160) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ P224) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ K226) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S251) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H352) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C382) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
48% identity, 97% coverage: 8:394/397 of query aligns to 2:387/389 of 2vu2A
- active site: C86 (= C92), H345 (= H352), C375 (= C382), G377 (= G384)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: C86 (= C92), L145 (= L152), H153 (≠ P161), M154 (= M162), F232 (= F239), A240 (= A247), S244 (= S251), G245 (≠ A252), L246 (≠ N253), A315 (= A322), F316 (= F323), H345 (= H352)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
48% identity, 97% coverage: 8:394/397 of query aligns to 2:387/389 of 1dm3A
- active site: C86 (= C92), H345 (= H352), C375 (= C382), G377 (= G384)
- binding acetyl coenzyme *a: C86 (= C92), L145 (= L152), H153 (≠ P161), M154 (= M162), R217 (≠ L225), S224 (≠ K231), M225 (≠ I232), L228 (= L235), F232 (= F239), A240 (= A247), G241 (≠ A248), A243 (≠ S250), S244 (= S251), G245 (≠ A252), L246 (≠ N253), M285 (≠ F292), A315 (= A322), F316 (= F323), H345 (= H352), C375 (= C382), I376 (= I383)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
48% identity, 97% coverage: 8:394/397 of query aligns to 2:387/389 of 1dlvA
- active site: C86 (= C92), H345 (= H352), C375 (= C382), G377 (= G384)
- binding coenzyme a: C86 (= C92), L145 (= L152), H153 (≠ P161), M154 (= M162), R217 (≠ L225), S224 (≠ K231), M225 (≠ I232), L228 (= L235), F232 (= F239), A240 (= A247), G241 (≠ A248), S244 (= S251), G245 (≠ A252), L246 (≠ N253), F316 (= F323), H345 (= H352)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
48% identity, 97% coverage: 8:394/397 of query aligns to 4:389/391 of 2vu1A