SitesBLAST
Comparing SMc00966 SMc00966 acetyl-COA acyltransferase 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)
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
38% identity, 96% coverage: 9:391/397 of query aligns to 2:392/392 of 4xl4A
- active site: C88 (= C93), H348 (= H346), S378 (≠ G377), G380 (= G379)
- binding coenzyme a: L148 (vs. gap), H156 (≠ D157), M157 (= M158), R220 (= R217), L228 (= L225), L231 (= L228), F235 (= F232), A243 (= A240), G244 (= G241), S247 (≠ C244), G248 (≠ P245), L249 (≠ V246), A318 (= A316), F319 (= F317), H348 (= H346)
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)
41% identity, 94% coverage: 12:385/397 of query aligns to 5:387/393 of P14611
- C88 (= C93) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ D157) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ C215) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R217) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (≠ C244) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H346) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (≠ G377) 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)
38% identity, 96% coverage: 9:391/397 of query aligns to 2:392/392 of P45359
- V77 (= V82) 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 (= C93) modified: Disulfide link with 378, In inhibited form
- S96 (≠ V101) binding
- N153 (≠ G154) 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 276:277) binding
- A286 (≠ K283) 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 (≠ G377) modified: Disulfide link with 88, In inhibited form
- A386 (= A385) binding
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
43% identity, 95% coverage: 9:385/397 of query aligns to 2:385/391 of 5f38B
- active site: C88 (= C93), H347 (= H346), C377 (≠ G377), G379 (= G379)
- binding coenzyme a: C88 (= C93), L149 (≠ M148), H157 (≠ D157), M158 (= M158), K219 (≠ R217), S222 (≠ A220), L227 (= L225), L230 (= L228), F234 (= F232), A242 (= A240), G243 (= G241), S246 (≠ C244), G247 (≠ P245), I248 (≠ V246), M287 (≠ L285), A317 (= A316), F318 (= F317), H347 (= H346)
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)
38% identity, 97% coverage: 1:385/397 of query aligns to 1:391/397 of Q9BWD1
- K211 (≠ E207) to R: in dbSNP:rs25683
- R223 (= R217) binding
- S226 (≠ A220) binding
- S252 (≠ C244) binding
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
42% identity, 95% coverage: 9:385/397 of query aligns to 4:389/394 of 5f38D
- active site: C90 (= C93), A348 (= A343), A378 (= A374), L380 (≠ M376)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C93), L151 (≠ M148), H159 (≠ D157), M160 (= M158), F238 (= F232), A246 (= A240), S250 (≠ C244), G251 (≠ P245), I252 (≠ V246), M291 (≠ L285), A321 (= A316), F322 (= F317), H351 (= H346)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
41% identity, 94% coverage: 12:385/397 of query aligns to 5:387/393 of 4o9cC
- active site: S88 (≠ C93), H349 (= H346), C379 (≠ G377), G381 (= G379)
- binding coenzyme a: S88 (≠ C93), L148 (≠ I153), H156 (≠ D157), R221 (= R217), S228 (≠ T224), L232 (= L228), F236 (= F232), A244 (= A240), A247 (= A243), S248 (≠ C244), G249 (≠ P245), L250 (≠ V246), A319 (= A316), F320 (= F317), H349 (= H346), I351 (≠ Y348), C379 (≠ G377)
7ei4A Crystal structure of masl in complex with a novel covalent inhibitor, collimonin c (see paper)
41% identity, 94% coverage: 12:385/397 of query aligns to 5:384/392 of 7ei4A
- binding (6S,7R,9E)-6,7-bis(oxidanyl)hexadeca-9,15-dien-11,13-diynoic acid: F17 (≠ V24), V87 (≠ Q92), C88 (= C93), L148 (vs. gap), H156 (≠ D157), S157 (≠ M158), F233 (= F232), P245 (≠ C244), L247 (≠ V246), A316 (= A316), F317 (= F317), H346 (= H346), I377 (= I378), G378 (= G379)
7feaB Py14 in complex with col-d (see paper)
40% identity, 94% coverage: 12:385/397 of query aligns to 6:387/396 of 7feaB
- binding (6~{R},7~{R},9~{E})-6,7-bis(oxidanyl)hexadeca-9,15-dien-11,13-diynoic acid: F18 (≠ V24), C89 (= C93), L149 (vs. gap), H157 (≠ D157), F236 (= F232), P248 (≠ C244), L250 (≠ V246), F289 (≠ L285), F320 (= F317), G381 (= G379)
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
38% identity, 96% coverage: 5:385/397 of query aligns to 2:388/394 of 1wl4A
- active site: C89 (= C93), H350 (= H346), C380 (≠ G377), G382 (= G379)
- binding coenzyme a: C89 (= C93), L148 (vs. gap), H156 (≠ D157), M157 (= M158), R220 (= R217), S223 (≠ A220), M228 (≠ L225), L231 (= L228), Y234 (≠ V231), F235 (= F232), P245 (≠ A240), A246 (≠ G241), S249 (≠ C244), G250 (≠ P245), I251 (≠ V246), A320 (= A316), F321 (= F317), H350 (= H346), L352 (≠ Y348)
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
37% identity, 96% coverage: 9:388/397 of query aligns to 1:395/400 of 5bz4K
- active site: C87 (= C93), H354 (= H346), C384 (≠ G377), G386 (= G379)
- binding coenzyme a: C87 (= C93), R146 (≠ Q141), M160 (= M158), L161 (≠ G159), R220 (= R217), L228 (= L225), L231 (= L228), A246 (= A240), G247 (= G241), S250 (≠ C244), Q252 (≠ V246), M291 (≠ L285), A321 (= A316), F322 (= F317), H354 (= H346)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
40% identity, 96% coverage: 10:390/397 of query aligns to 3:391/392 of P07097