SitesBLAST
Comparing 7025620 Shewana3_2771 acetyl-CoA acetyltransferases (RefSeq) 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)
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)
49% identity, 98% coverage: 8:395/396 of query aligns to 2:390/392 of P45359
- V77 (≠ L83) 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 (= C94) modified: Disulfide link with 378, In inhibited form
- S96 (≠ M102) binding
- N153 (≠ T159) 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 (≠ TT 284:285) binding
- A286 (≠ S291) 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 (= C383) modified: Disulfide link with 88, In inhibited form
- A386 (= A391) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
49% identity, 98% coverage: 8:395/396 of query aligns to 2:390/392 of 4xl4A
- active site: C88 (= C94), H348 (= H353), S378 (≠ C383), G380 (= G385)
- binding coenzyme a: L148 (= L154), H156 (≠ A162), R220 (≠ G226), L231 (= L236), A243 (= A248), S247 (= S252), F319 (= F324), H348 (= H353)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
49% identity, 98% coverage: 8:395/396 of query aligns to 2:390/393 of 6bn2A
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)
51% identity, 98% coverage: 9:395/396 of query aligns to 3:391/393 of P14611
- C88 (= C94) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ A162) 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 (≠ Q224) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S252) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H353) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C383) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
51% identity, 98% coverage: 9:395/396 of query aligns to 3:391/393 of 4o9cC
- active site: S88 (≠ C94), H349 (= H353), C379 (= C383), G381 (= G385)
- binding coenzyme a: S88 (≠ C94), L148 (= L154), R221 (≠ Q224), F236 (= F240), A244 (= A248), S248 (= S252), L250 (≠ I254), A319 (= A323), F320 (= F324), H349 (= H353)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
53% identity, 98% coverage: 8:395/396 of query aligns to 4:393/394 of 5f38D
- active site: C90 (= C94), A348 (= A350), A378 (= A380), L380 (= L382)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C94), L151 (= L154), A246 (= A248), S250 (= S252), I252 (= I254), A321 (= A323), F322 (= F324), H351 (= H353)
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
48% identity, 98% coverage: 10:396/396 of query aligns to 8:396/397 of 6aqpA
- active site: C93 (= C94), H353 (= H353), C383 (= C383), G385 (= G385)
- binding coenzyme a: C93 (= C94), L153 (= L154), Y188 (≠ L189), N226 (= N227), N228 (≠ R229), K231 (= K232), A248 (= A248), P249 (≠ A249), S252 (= S252), A323 (= A323), F324 (= F324), H353 (= H353)
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
48% identity, 98% coverage: 10:396/396 of query aligns to 8:398/399 of 6aqpC
- active site: C93 (= C94), H355 (= H353), C385 (= C383), G387 (= G385)
- binding acetyl coenzyme *a: C93 (= C94), L153 (= L154), M162 (= M163), Y188 (≠ L189), N230 (≠ R229), K233 (= K232), L234 (≠ I233), I237 (≠ L236), A250 (= A248), P251 (≠ A249), S254 (= S252), F295 (= F293), A325 (= A323), F326 (= F324), H355 (= H353)
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, 98% coverage: 10:396/396 of query aligns to 7:397/398 of Q4WCL5
- Y187 (≠ L189) binding
- N229 (≠ R229) binding
- K232 (= K232) binding
- A249 (= A248) binding
- P250 (≠ A249) binding
- S252 (= S251) binding
- S253 (= S252) binding
- V350 (≠ C349) binding
- N385 (≠ I384) binding
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
48% identity, 97% coverage: 11:396/396 of query aligns to 4:391/394 of 7cw5B
- active site: C87 (= C94), H348 (= H353), C378 (= C383), G380 (= G385)
- binding coenzyme a: L147 (= L154), H155 (≠ A162), M156 (= M163), R220 (vs. gap), T223 (≠ A228), A243 (= A248), P247 (≠ S252), L249 (≠ I254), H348 (= H353)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
52% identity, 98% coverage: 8:395/396 of query aligns to 2:389/391 of 5f38B
- active site: C88 (= C94), H347 (= H353), C377 (= C383), G379 (= G385)
- binding coenzyme a: C88 (= C94), L149 (= L154), K219 (vs. gap), F234 (= F240), A242 (= A248), S246 (= S252), A317 (= A323), F318 (= F324), H347 (= H353)
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)
47% identity, 98% coverage: 7:395/396 of query aligns to 2:396/398 of P41338
- S2 (≠ N7) modified: N-acetylserine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
47% identity, 97% coverage: 10:395/396 of query aligns to 2:387/389 of 2vu2A
- active site: C86 (= C94), H345 (= H353), C375 (= C383), G377 (= G385)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ A162), M154 (= M163), F232 (= F240), S244 (= S252), G245 (≠ S253), F316 (= F324), H345 (= H353)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
47% identity, 97% coverage: 10:395/396 of query aligns to 2:387/389 of 1dm3A
- active site: C86 (= C94), H345 (= H353), C375 (= C383), G377 (= G385)
- binding acetyl coenzyme *a: C86 (= C94), L145 (= L154), H153 (≠ A162), M154 (= M163), R217 (≠ G226), S224 (≠ K232), M225 (≠ I233), A240 (= A248), S244 (= S252), M285 (≠ F293), A315 (= A323), F316 (= F324), H345 (= H353), C375 (= C383)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
47% identity, 97% coverage: 10:395/396 of query aligns to 2:387/389 of 1dlvA
- active site: C86 (= C94), H345 (= H353), C375 (= C383), G377 (= G385)
- binding coenzyme a: C86 (= C94), L145 (= L154), H153 (≠ A162), M154 (= M163), R217 (≠ G226), L228 (= L236), A240 (= A248), S244 (= S252), H345 (= H353)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
47% identity, 97% coverage: 10:395/396 of query aligns to 4:389/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
47% identity, 97% coverage: 10:395/396 of query aligns to 5:390/392 of 1ou6A
- active site: C89 (= C94), H348 (= H353), C378 (= C383), G380 (= G385)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L154), H156 (≠ A162), M157 (= M163), F235 (= F240), A243 (= A248), S247 (= S252), A318 (= A323), F319 (= F324), H348 (= H353)
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)
46% identity, 97% coverage: 10:395/396 of query aligns to 8:395/397 of Q9BWD1
- K211 (≠ R214) to R: in dbSNP:rs25683
- R223 (≠ G226) binding
- S226 (≠ A228) binding
- S252 (= S252) binding
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
46% identity, 97% coverage: 10:395/396 of query aligns to 5:392/394 of 1wl4A
- active site: C89 (= C94), H350 (= H353), C380 (= C383), G382 (= G385)
- binding coenzyme a: L148 (= L154), M157 (= M163), R220 (≠ G226), Y234 (≠ A239), P245 (≠ A248), A246 (= A249), S249 (= S252), A320 (= A323), F321 (= F324), H350 (= H353)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
47% identity, 97% coverage: 10:395/396 of query aligns to 2:387/389 of 2wkuA
- active site: C86 (= C94), H345 (= H353), C375 (= C383), G377 (= G385)
- binding D-mannose: S6 (≠ A14), A7 (= A15), R38 (≠ D46), K182 (= K191), D194 (≠ A203), V280 (≠ Q288), D281 (≠ E289), T287 (= T295), P331 (≠ M339), S332 (≠ A340), V334 (= V342), V336 (= V344), F360 (≠ H368)
Query Sequence
>7025620 Shewana3_2771 acetyl-CoA acetyltransferases (RefSeq)
MSTEQFNQEIVIVAAKRTPMGGFQGSLSGVMSPSLAATAIKALLADTQVAPDKVDEVLMG
CVLPAGLGQAPARQATLGAGLPLSVGATTVNKVCGSGMKTVMLAHDLLKAGSAKLVVAGG
MESMSQAPYLLDKARAGMRMGHGKVLDHMFLDGLEDAYTGGAMGTFAQKTADEYGLTREQ
MDAFALSSLEKANAAINSGAFKAEIVPVTVSDRRGDVTVDTDEQPGNARPEKIPALRPAF
AKDGTITAANSSSISDGAAALMLTTRANAEQLGLTVLATIKGHTTHAQEPSLFTTAPVGA
MAKLLSNVGWSKDEVDLFEINEAFAMVTMLAVSELGLDMAKVNVNGGACALGHPIGCSGA
RLLVTLIHALKARGLKRGVASLCIGGGEATAMAIEV
Or try a new SitesBLAST search
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