SitesBLAST
Comparing AO353_25685 FitnessBrowser__pseudo3_N2E3:AO353_25685 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)
8gqnA X-ray structure of thiolase with coa
63% identity, 98% coverage: 8:396/397 of query aligns to 3:390/390 of 8gqnA
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
52% identity, 99% coverage: 3:396/397 of query aligns to 2:397/397 of 6aqpA
- active site: C93 (= C92), H353 (= H352), C383 (= C382), G385 (= G384)
- binding coenzyme a: C93 (= C92), L153 (= L152), Y188 (≠ T188), N226 (≠ K226), N228 (≠ K228), K231 (= K231), A248 (= A247), P249 (≠ A248), S252 (= S251), A323 (= A322), F324 (= F323), H353 (= H352)
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)
52% identity, 99% coverage: 3:396/397 of query aligns to 1:398/398 of Q4WCL5
- Y187 (≠ T188) binding K(+)
- N229 (≠ K228) binding CoA
- K232 (= K231) binding CoA
- A249 (= A247) binding K(+)
- P250 (≠ A248) binding K(+)
- S252 (= S250) binding K(+)
- S253 (= S251) binding CoA
- V350 (≠ C348) binding K(+)
- N385 (≠ I383) binding chloride
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
52% identity, 99% coverage: 3:396/397 of query aligns to 2:399/399 of 6aqpC
- active site: C93 (= C92), H355 (= H352), C385 (= C382), G387 (= G384)
- binding acetyl coenzyme *a: C93 (= C92), L153 (= L152), M162 (= M162), Y188 (≠ T188), N230 (≠ K228), K233 (= K231), L234 (≠ I232), I237 (≠ L235), A250 (= A247), P251 (≠ A248), S254 (= S251), F295 (= F292), A325 (= A322), F326 (= F323), H355 (= H352)
P45359 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; CaTHL; EC 2.3.1.9 from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W) (see paper)
49% identity, 97% coverage: 8:394/397 of query aligns to 4:390/392 of P45359
- V77 (≠ K81) 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 (≠ I100) binding acetate
- N153 (≠ D157) 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 (≠ AA 283:284) binding acetate
- A286 (≠ G290) 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 acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
48% identity, 97% coverage: 8:394/397 of query aligns to 4:390/392 of 4xl4A
- active site: C88 (= C92), H348 (= H352), S378 (≠ C382), G380 (= G384)
- binding coenzyme a: L148 (= L152), H156 (≠ R160), R220 (≠ K226), L231 (= L235), A243 (= A247), S247 (= S251), F319 (= F323), H348 (= H352)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
48% identity, 97% coverage: 9:395/397 of query aligns to 4:391/394 of 7cw5B
- active site: C87 (= C92), H348 (= H352), C378 (= C382), G380 (= G384)
- binding coenzyme a: L147 (= L152), H155 (≠ L161), M156 (= M162), R220 (≠ K226), T223 (≠ A227), A243 (= A247), P247 (≠ S251), L249 (≠ I253), H348 (= H352)
P41338 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Ergosterol biosynthesis protein 10; EC 2.3.1.9 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
48% identity, 99% coverage: 3:394/397 of query aligns to 1:396/398 of P41338
- M1 (= M3) modified: Initiator methionine, Removed
- S2 (= S4) modified: N-acetylserine
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)
49% identity, 97% coverage: 8:394/397 of query aligns to 4:391/393 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 (≠ E222) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ P224) 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.
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
46% identity, 98% coverage: 8:396/397 of query aligns to 4:392/393 of 6bn2A
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
48% identity, 97% coverage: 8:394/397 of query aligns to 4:391/393 of 4o9cC
- active site: S88 (≠ C92), H349 (= H352), C379 (= C382), G381 (= G384)
- binding coenzyme a: S88 (≠ C92), L148 (= L152), R221 (≠ P224), F236 (= F239), A244 (= A247), S248 (= S251), L250 (≠ I253), A319 (= A322), F320 (= F323), H349 (= H352)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
50% identity, 97% coverage: 9:394/397 of query aligns to 7:393/394 of 5f38D