SitesBLAST
Comparing AZOBR_RS28180 AZOBR_RS28180 acetyl-CoA acetyltransferase 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)
45% identity, 98% coverage: 5:395/397 of query aligns to 1:391/392 of P45359
- V77 (≠ D81) 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 (= C92) modified: Disulfide link with 378, In inhibited form
- S96 (≠ M100) binding
- N153 (≠ E157) 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 283:284) binding
- A286 (= A290) 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 (= C382) modified: Disulfide link with 88, In inhibited form
- A386 (= A390) binding
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
50% identity, 99% coverage: 2:394/397 of query aligns to 2:395/397 of 6aqpA
- active site: C93 (= C92), H353 (= H352), C383 (= C382), G385 (= G384)
- binding coenzyme a: C93 (= C92), L153 (= L152), Y188 (≠ L188), N226 (≠ K226), N228 (≠ A228), K231 (= K231), A248 (= A247), P249 (≠ A248), S252 (= S251), A323 (= A322), F324 (= F323), H353 (= H352)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
45% identity, 98% coverage: 5:395/397 of query aligns to 1:391/393 of 6bn2A
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)
50% identity, 99% coverage: 2:394/397 of query aligns to 1:396/398 of Q4WCL5
- Y187 (≠ L188) binding
- N229 (≠ A228) binding
- K232 (= K231) binding
- A249 (= A247) binding
- P250 (≠ A248) binding
- S252 (= S250) binding
- S253 (= S251) binding
- V350 (≠ C348) binding
- N385 (≠ I383) binding
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
50% identity, 99% coverage: 2:394/397 of query aligns to 2:397/399 of 6aqpC
- active site: C93 (= C92), H355 (= H352), C385 (= C382), G387 (= G384)
- binding acetyl coenzyme *a: C93 (= C92), L153 (= L152), M162 (= M162), Y188 (≠ L188), N230 (≠ A228), K233 (= K231), L234 (≠ I232), I237 (≠ L235), A250 (= A247), P251 (≠ A248), S254 (= S251), F295 (= F292), A325 (= A322), F326 (= F323), H355 (= H352)
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
45% identity, 98% coverage: 5:395/397 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C92), H348 (= H352), S378 (≠ C382), G380 (= G384)
- binding coenzyme a: L148 (= L152), H156 (≠ P161), R220 (vs. gap), L231 (= L235), A243 (= A247), S247 (= S251), F319 (= F323), H348 (= H352)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
48% identity, 97% coverage: 9:394/397 of query aligns to 4:390/394 of 7cw5B
- active site: C87 (= C92), H348 (= H352), C378 (= C382), G380 (= G384)
- binding coenzyme a: L147 (= L152), H155 (≠ R160), M156 (= M162), R220 (≠ L225), T223 (≠ V227), A243 (= A247), P247 (≠ S251), L249 (≠ N253), H348 (= H352)
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: 8:395/397 of query aligns to 4:392/393 of P14611
- C88 (= C92) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ R160) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ P224) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ K226) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S251) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H352) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C382) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
48% identity, 97% coverage: 8:394/397 of query aligns to 2:387/389 of 2vu2A
- active site: C86 (= C92), H345 (= H352), C375 (= C382), G377 (= G384)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ P161), M154 (= M162), F232 (= F239), S244 (= S251), G245 (≠ A252), F316 (= F323), H345 (= H352)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
48% identity, 97% coverage: 8:394/397 of query aligns to 2:387/389 of 1dm3A
- active site: C86 (= C92), H345 (= H352), C375 (= C382), G377 (= G384)
- binding acetyl coenzyme *a: C86 (= C92), L145 (= L152), H153 (≠ P161), M154 (= M162), R217 (≠ L225), S224 (≠ K231), M225 (≠ I232), A240 (= A247), S244 (= S251), M285 (≠ F292), A315 (= A322), F316 (= F323), H345 (= H352), C375 (= C382)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
48% identity, 97% coverage: 8:394/397 of query aligns to 2:387/389 of 1dlvA
- active site: C86 (= C92), H345 (= H352), C375 (= C382), G377 (= G384)
- binding coenzyme a: C86 (= C92), L145 (= L152), H153 (≠ P161), M154 (= M162), R217 (≠ L225), L228 (= L235), A240 (= A247), S244 (= S251), H345 (= H352)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
48% identity, 97% coverage: 8:394/397 of query aligns to 4:389/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
48% identity, 97% coverage: 8:394/397 of query aligns to 5:390/392 of 1ou6A
- active site: C89 (= C92), H348 (= H352), C378 (= C382), G380 (= G384)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L152), H156 (≠ P161), M157 (= M162), F235 (= F239), A243 (= A247), S247 (= S251), A318 (= A322), F319 (= F323), H348 (= H352)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
48% identity, 98% coverage: 8:395/397 of query aligns to 4:392/393 of 4o9cC
- active site: S88 (≠ C92), H349 (= H352), C379 (= C382), G381 (= G384)
- binding coenzyme a: S88 (≠ C92), L148 (= L152), R221 (≠ K226), F236 (= F239), A244 (= A247), S248 (= S251), L250 (≠ N253), A319 (= A322), F320 (= F323), H349 (= H352)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
48% identity, 97% coverage: 8:394/397 of query aligns to 2:387/389 of 2wkuA
- active site: C86 (= C92), H345 (= H352), C375 (= C382), G377 (= G384)
- binding D-mannose: S6 (= S12), A7 (= A13), R38 (= R44), K182 (≠ R190), D194 (≠ A202), V280 (≠ Q287), D281 (= D288), T287 (= T294), P331 (≠ R338), S332 (≠ D339), V334 (≠ L341), V336 (= V343), F360 (≠ H367)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
47% identity, 98% coverage: 7:394/397 of query aligns to 4:390/392 of P07097
- Q64 (= Q67) mutation to A: Slightly lower activity.
- C89 (= C92) mutation to A: Loss of activity.
- C378 (= C382) mutation to G: Loss of activity.
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
48% identity, 97% coverage: 8:394/397 of query aligns to 3:388/390 of 1m1oA
- active site: A87 (≠ C92), H346 (= H352), C376 (= C382), G378 (= G384)
- binding acetoacetyl-coenzyme a: L86 (≠ V91), A87 (≠ C92), L146 (= L152), H154 (≠ P161), M155 (= M162), R218 (≠ L225), S225 (≠ K231), M226 (≠ I232), A241 (= A247), G242 (≠ A248), S245 (= S251), A316 (= A322), F317 (= F323), H346 (= H352), I377 (= I383), G378 (= G384)
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, 98% coverage: 6:395/397 of query aligns to 6:396/397 of Q9BWD1
- K211 (≠ G213) to R: in dbSNP:rs25683
- R223 (≠ L225) binding
- S226 (≠ A228) binding
- S252 (= S251) binding
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
46% identity, 98% coverage: 6:395/397 of query aligns to 3:393/394 of 1wl4A
- active site: C89 (= C92), H350 (= H352), C380 (= C382), G382 (= G384)
- binding coenzyme a: L148 (= L152), M157 (= M162), R220 (≠ L225), Y234 (≠ A238), P245 (≠ A247), A246 (= A248), S249 (= S251), A320 (= A322), F321 (= F323), H350 (= H352)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
48% identity, 99% coverage: 4:395/397 of query aligns to 2:394/394 of 5f38D
- active site: C90 (= C92), A348 (= A349), A378 (= A379), L380 (= L381)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C92), L151 (= L152), A246 (= A247), S250 (= S251), I252 (≠ N253), A321 (= A322), F322 (= F323), H351 (= H352)
Query Sequence
>AZOBR_RS28180 AZOBR_RS28180 acetyl-CoA acetyltransferase
IMDTLDPVVIVSAARTPLGRFQGELSALPAHALGAHAVRAALSRAGLAPERVDEVLLGCV
LPAGQGQAPARQAARGAGLPDATGATTVNKVCGSGMKATMLAHDLIRAGSADLVVAGGME
SMSNAPYLLAKARGGYRIGHDRILDHLMLDGLEDAYEGGRPMGDFGEATADLYGFTRAEQ
DAYAVETLTRARAAIASGAFTAEIAPVTLAVKGGERTVADDENPLKVAPEKIPALKPAFR
RDGTITAASSSANADGAAALLLTRRSLAEREGLPVLATILGHATHSQDPAWFTTAPIPAI
RKLLDRVGWGIGDVDLFEINEAFAVVAMAAQRDLGIPRDALNVNGGACALGHPIGATGAR
LIVTLLHALAARGLRRGVASLCIGGGEATAIAVERPA
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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