SitesBLAST
Comparing SMa1450 FitnessBrowser__Smeli:SMa1450 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: 7:394/396 of query aligns to 3:389/390 of 8gqnA
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: 7:393/396 of query aligns to 4:390/392 of P45359
- V77 (≠ P80) 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 (= C91) modified: Disulfide link with 378, In inhibited form
- S96 (≠ M99) binding acetate
- N153 (≠ D156) 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 282:283) binding acetate
- A286 (≠ S289) 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 (= C381) modified: Disulfide link with 88, In inhibited form
- A386 (= A389) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
48% identity, 98% coverage: 7:393/396 of query aligns to 4:390/392 of 4xl4A
- active site: C88 (= C91), H348 (= H351), S378 (≠ C381), G380 (= G383)
- binding coenzyme a: L148 (= L151), H156 (≠ R159), R220 (≠ Q224), L231 (= L234), A243 (= A246), S247 (= S250), F319 (= F322), H348 (= H351)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
48% identity, 98% coverage: 7:393/396 of query aligns to 4:390/393 of 6bn2A
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
49% identity, 98% coverage: 7:394/396 of query aligns to 3:391/394 of 7cw5B
- active site: C87 (= C91), H348 (= H351), C378 (= C381), G380 (= G383)
- binding coenzyme a: L147 (= L151), H155 (≠ L160), M156 (= M161), R220 (≠ Q224), T223 (≠ A226), A243 (= A246), P247 (≠ S250), L249 (≠ I252), H348 (= H351)
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
49% identity, 99% coverage: 1:394/396 of query aligns to 2:396/397 of 6aqpA
- active site: C93 (= C91), H353 (= H351), C383 (= C381), G385 (= G383)
- binding coenzyme a: C93 (= C91), L153 (= L151), Y188 (≠ L187), N226 (≠ K225), N228 (≠ R227), K231 (= K230), A248 (= A246), P249 (≠ A247), S252 (= S250), A323 (= A321), F324 (= F322), H353 (= H351)
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
48% identity, 98% coverage: 5:393/396 of query aligns to 3:392/394 of 1wl4A
- active site: C89 (= C91), H350 (= H351), C380 (= C381), G382 (= G383)
- binding coenzyme a: L148 (= L151), M157 (= M161), R220 (≠ Q224), Y234 (≠ A237), P245 (≠ A246), A246 (= A247), S249 (= S250), A320 (= A321), F321 (= F322), H350 (= H351)
Q9BWD1 Acetyl-CoA acetyltransferase, cytosolic; Acetyl-CoA transferase-like protein; Cytosolic acetoacetyl-CoA thiolase; EC 2.3.1.9 from Homo sapiens (Human) (see 2 papers)
48% identity, 98% coverage: 5:393/396 of query aligns to 6:395/397 of Q9BWD1
- K211 (= K212) to R: in dbSNP:rs25683
- R223 (≠ Q224) binding CoA
- S226 (≠ A226) binding CoA
- S252 (= S250) binding CoA
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)
50% identity, 98% coverage: 7:393/396 of query aligns to 4:391/393 of P14611
- C88 (= C91) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ R159) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (vs. gap) 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 (= S250) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H351) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C381) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
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)
48% identity, 99% coverage: 1:394/396 of query aligns to 1:397/398 of Q4WCL5
- Y187 (≠ L187) binding K(+)
- N229 (≠ R227) binding CoA
- K232 (= K230) binding CoA
- A249 (= A246) binding K(+)
- P250 (≠ A247) binding K(+)
- S252 (≠ A249) binding K(+)
- S253 (= S250) binding CoA
- V350 (≠ C347) binding K(+)
- N385 (≠ I382) binding chloride
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
48% identity, 99% coverage: 1:394/396 of query aligns to 2:398/399 of 6aqpC
- active site: C93 (= C91), H355 (= H351), C385 (= C381), G387 (= G383)
- binding acetyl coenzyme *a: C93 (= C91), L153 (= L151), M162 (= M161), Y188 (≠ L187), N230 (≠ R227), K233 (= K230), L234 (≠ I231), I237 (≠ L234), A250 (= A246), P251 (≠ A247), S254 (= S250), F295 (= F291), A325 (= A321), F326 (= F322), H355 (= H351)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
50% identity, 98% coverage: 7:393/396 of query aligns to 4:391/393 of 4o9cC