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), R220 (= R217), L231 (= L228), A243 (= A240), S247 (≠ C244), 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), K219 (≠ R217), F234 (= F232), A242 (= A240), S246 (≠ C244), 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), A246 (= A240), S250 (≠ C244), I252 (≠ V246), 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), R221 (= R217), F236 (= F232), A244 (= A240), S248 (≠ C244), L250 (≠ V246), A319 (= A316), F320 (= F317), H349 (= H346)
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
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
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: L148 (vs. gap), M157 (= M158), R220 (= R217), Y234 (≠ V231), P245 (≠ A240), A246 (≠ G241), S249 (≠ C244), A320 (= A316), F321 (= F317), H350 (= H346)
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), R220 (= R217), 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
- Q64 (≠ G68) mutation to A: Slightly lower activity.
- C89 (= C93) mutation to A: Loss of activity.
- C378 (≠ G377) mutation to G: Loss of activity.
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
39% identity, 95% coverage: 12:390/397 of query aligns to 3:388/389 of 2vu2A
- active site: C86 (= C93), H345 (= H346), C375 (≠ G377), G377 (= G379)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ D157), M154 (= M158), F232 (= F232), S244 (≠ C244), G245 (≠ P245), F316 (= F317), H345 (= H346)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
39% identity, 95% coverage: 12:390/397 of query aligns to 3:388/389 of 1dm3A
- active site: C86 (= C93), H345 (= H346), C375 (≠ G377), G377 (= G379)
- binding acetyl coenzyme *a: C86 (= C93), L145 (≠ I153), H153 (≠ D157), M154 (= M158), R217 (= R217), S224 (≠ T224), M225 (≠ L225), A240 (= A240), S244 (≠ C244), M285 (≠ L285), A315 (= A316), F316 (= F317), H345 (= H346), C375 (≠ G377)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
39% identity, 95% coverage: 12:390/397 of query aligns to 3:388/389 of 1dlvA
- active site: C86 (= C93), H345 (= H346), C375 (≠ G377), G377 (= G379)
- binding coenzyme a: C86 (= C93), L145 (≠ I153), H153 (≠ D157), M154 (= M158), R217 (= R217), L228 (= L228), A240 (= A240), S244 (≠ C244), H345 (= H346)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
39% identity, 95% coverage: 12:390/397 of query aligns to 6:391/392 of 1ou6A
- active site: C89 (= C93), H348 (= H346), C378 (≠ G377), G380 (= G379)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ I153), H156 (≠ D157), M157 (= M158), F235 (= F232), A243 (= A240), S247 (≠ C244), A318 (= A316), F319 (= F317), H348 (= H346)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
39% identity, 95% coverage: 12:390/397 of query aligns to 5:390/391 of 2vu1A
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
39% identity, 95% coverage: 12:390/397 of query aligns to 3:388/389 of 2wkuA
- active site: C86 (= C93), H345 (= H346), C375 (≠ G377), G377 (= G379)
- binding D-mannose: S6 (≠ A15), A7 (= A16), R38 (≠ D47), K182 (≠ R186), D194 (≠ R198), V280 (= V280), D281 (≠ E281), T287 (≠ L287), P331 (= P332), S332 (≠ E333), V334 (= V335), V336 (≠ R337), F360 (≠ S361)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
39% identity, 95% coverage: 12:390/397 of query aligns to 4:389/390 of 1m1oA
- active site: A87 (≠ C93), H346 (= H346), C376 (≠ G377), G378 (= G379)
- binding acetoacetyl-coenzyme a: L86 (≠ Q92), A87 (≠ C93), L146 (≠ I153), H154 (≠ D157), M155 (= M158), R218 (= R217), S225 (≠ T224), M226 (≠ L225), A241 (= A240), G242 (= G241), S245 (≠ C244), A316 (= A316), F317 (= F317), H346 (= H346), I377 (= I378), G378 (= G379)
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
37% identity, 96% coverage: 9:388/397 of query aligns to 5:387/390 of 2d3tC
- active site: C94 (= C93), H346 (= H346), C376 (≠ G377), G378 (= G379)
- binding acetyl coenzyme *a: C94 (= C93), R214 (= R217), L222 (= L225), L225 (= L228), A238 (= A240), G239 (= G241), S242 (≠ C244), I244 (≠ V246), A313 (= A316), F314 (= F317), H346 (= H346), C376 (≠ G377)
Query Sequence
>SMc00966 SMc00966 acetyl-COA acyltransferase
MNASSDPARTPVVIAALRTPVGRVNGSLAAVEPARLAALLIERIIADTGIDRAEIDDVLV
GNAANSAGNLARLAALEAGLPVAIPGVTVDRQCGSGLEAIVLAARQIQAGAGRFYLAGGT
ESASRAHIRLRPPLTRGEEPQPVKRARMAPDSIGDPDMGVAAENVATACGISRERQDRFA
LESHRRAVAAEAEGRFSREIVPVPTPEGPIARDECPRANASAETLSRLRPVFVAGGTVTA
GNACPVNDGAAMVLMTNLAEARKLGTRFGLAFTDAATAGVEPKLLGLGPVPAMAKLRARN
PALDVARVDFIEFNEAFASQVLGSLDQLDIAPERVNRDGGAIALGHPYGASGAILVVRLF
SQMLAASSPAEGLAMMGIGGGMGIAAHFSSCRPDQAA
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory