SitesBLAST
Comparing AO356_26350 FitnessBrowser__pseudo5_N2C3_1:AO356_26350 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
62% identity, 98% coverage: 6:394/395 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, 100% coverage: 1:394/395 of query aligns to 2:397/397 of 6aqpA
- active site: C93 (= C90), H353 (= H350), C383 (= C380), G385 (= G382)
- binding coenzyme a: C93 (= C90), L153 (= L150), Y188 (≠ T186), N226 (≠ K224), N228 (≠ R226), K231 (= K229), A248 (= A245), P249 (≠ A246), S252 (= S249), A323 (= A320), F324 (= F321), H353 (= H350)
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, 100% coverage: 1:394/395 of query aligns to 1:398/398 of Q4WCL5
- Y187 (≠ T186) binding K(+)
- N229 (≠ R226) binding CoA
- K232 (= K229) binding CoA
- A249 (= A245) binding K(+)
- P250 (≠ A246) binding K(+)
- S252 (= S248) binding K(+)
- S253 (= S249) binding CoA
- V350 (≠ C346) binding K(+)
- N385 (≠ I381) binding chloride
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
52% identity, 100% coverage: 1:394/395 of query aligns to 2:399/399 of 6aqpC
- active site: C93 (= C90), H355 (= H350), C385 (= C380), G387 (= G382)
- binding acetyl coenzyme *a: C93 (= C90), L153 (= L150), M162 (= M160), Y188 (≠ T186), N230 (≠ R226), K233 (= K229), L234 (≠ I230), I237 (≠ L233), A250 (= A245), P251 (≠ A246), S254 (= S249), F295 (= F290), A325 (= A320), F326 (= F321), H355 (= H350)
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)
48% identity, 98% coverage: 6:392/395 of query aligns to 4:390/392 of P45359
- V77 (≠ K79) 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 (≠ I98) binding acetate
- N153 (≠ D155) 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 281:282) binding acetate
- A286 (≠ S288) 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 (= C380) modified: Disulfide link with 88, In inhibited form
- A386 (= A388) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
48% identity, 98% coverage: 6:392/395 of query aligns to 4:390/392 of 4xl4A
- active site: C88 (= C90), H348 (= H350), S378 (≠ C380), G380 (= G382)
- binding coenzyme a: L148 (= L150), H156 (≠ R158), R220 (≠ P223), L231 (= L233), A243 (= A245), S247 (= S249), F319 (= F321), H348 (= H350)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
48% identity, 98% coverage: 7:393/395 of query aligns to 4:391/394 of 7cw5B
- active site: C87 (= C90), H348 (= H350), C378 (= C380), G380 (= G382)
- binding coenzyme a: L147 (= L150), H155 (≠ L159), M156 (= M160), R220 (≠ P223), T223 (≠ A225), A243 (= A245), P247 (≠ S249), L249 (≠ I251), H348 (= H350)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
47% identity, 98% coverage: 6:394/395 of query aligns to 4:392/393 of 6bn2A
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, 98% coverage: 6:392/395 of query aligns to 5:396/398 of P41338
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 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)
48% identity, 98% coverage: 6:392/395 of query aligns to 4:391/393 of P14611
- C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ R158) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ Q221) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ P223) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S249) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H350) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C380) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
48% identity, 98% coverage: 6:392/395 of query aligns to 4:391/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H350), C379 (= C380), G381 (= G382)
- binding coenzyme a: S88 (≠ C90), L148 (= L150), R221 (≠ P223), F236 (= F237), A244 (= A245), S248 (= S249), L250 (≠ I251), A319 (= A320), F320 (= F321), H349 (= H350)
P24752 Acetyl-CoA acetyltransferase, mitochondrial; Acetoacetyl-CoA thiolase; T2; EC 2.3.1.9 from Homo sapiens (Human) (see 6 papers)
47% identity, 98% coverage: 6:394/395 of query aligns to 42:427/427 of P24752