SitesBLAST
Comparing GFF3267 PGA1_c33180 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)
49% identity, 100% coverage: 1:389/390 of query aligns to 1:391/392 of P45359
- V77 (≠ E75) 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 (= C86) modified: Disulfide link with 378, In inhibited form
- S96 (≠ M94) binding
- N153 (≠ D151) 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 (≠ AS 277:278) binding
- A286 (≠ G284) 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 (= C376) modified: Disulfide link with 88, In inhibited form
- A386 (= A384) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
48% identity, 100% coverage: 1:389/390 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C86), H348 (= H346), S378 (≠ C376), G380 (= G378)
- binding coenzyme a: L148 (= L146), H156 (≠ R154), R220 (≠ K219), L231 (= L229), A243 (= A241), S247 (= S245), F319 (= F317), H348 (= H346)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
48% identity, 100% coverage: 1:390/390 of query aligns to 1:392/393 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)
50% identity, 100% coverage: 1:389/390 of query aligns to 1:392/393 of P14611
- C88 (= C86) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ R154) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ Q217) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ K219) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S245) 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 (= C376) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
50% identity, 100% coverage: 1:389/390 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C86), H349 (= H346), C379 (= C376), G381 (= G378)
- binding coenzyme a: S88 (≠ C86), L148 (= L146), R221 (≠ K219), F236 (= F233), A244 (= A241), S248 (= S245), L250 (≠ I247), A319 (= A316), F320 (= F317), H349 (= H346)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
52% identity, 100% coverage: 1:389/390 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C86), A348 (= A343), A378 (= A373), L380 (≠ I375)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C86), L151 (= L146), A246 (= A241), S250 (= S245), I252 (= I247), A321 (= A316), F322 (= F317), H351 (= H346)
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
46% identity, 100% coverage: 1:390/390 of query aligns to 5:397/397 of 6aqpA
- active site: C93 (= C86), H353 (= H346), C383 (= C376), G385 (= G378)
- binding coenzyme a: C93 (= C86), L153 (= L146), Y188 (≠ L182), N226 (≠ S220), N228 (≠ R222), K231 (= K225), A248 (= A241), P249 (≠ A242), S252 (= S245), A323 (= A316), F324 (= F317), H353 (= H346)
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)
47% identity, 100% coverage: 1:390/390 of query aligns to 4:398/398 of Q4WCL5
- Y187 (≠ L182) binding
- N229 (≠ R222) binding
- K232 (= K225) binding
- A249 (= A241) binding
- P250 (≠ A242) binding
- S252 (≠ A244) binding
- S253 (= S245) binding
- V350 (≠ C342) binding
- N385 (≠ I377) binding
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
47% identity, 100% coverage: 1:390/390 of query aligns to 5:399/399 of 6aqpC
- active site: C93 (= C86), H355 (= H346), C385 (= C376), G387 (= G378)
- binding acetyl coenzyme *a: C93 (= C86), L153 (= L146), M162 (= M156), Y188 (≠ L182), N230 (≠ R222), K233 (= K225), L234 (≠ I226), I237 (≠ L229), A250 (= A241), P251 (≠ A242), S254 (= S245), F295 (= F286), A325 (= A316), F326 (= F317), H355 (= H346)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
51% identity, 100% coverage: 1:390/390 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C86), H347 (= H346), C377 (= C376), G379 (= G378)
- binding coenzyme a: C88 (= C86), L149 (= L146), K219 (= K219), F234 (= F233), A242 (= A241), S246 (= S245), A317 (= A316), F318 (= F317), H347 (= H346)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
46% identity, 99% coverage: 3:390/390 of query aligns to 1:389/389 of 2vu2A
- active site: C86 (= C86), H345 (= H346), C375 (= C376), G377 (= G378)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ L155), M154 (= M156), F232 (= F233), S244 (= S245), G245 (≠ S246), F316 (= F317), H345 (= H346)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
46% identity, 99% coverage: 3:390/390 of query aligns to 1:389/389 of 1dm3A
- active site: C86 (= C86), H345 (= H346), C375 (= C376), G377 (= G378)
- binding acetyl coenzyme *a: C86 (= C86), L145 (= L146), H153 (≠ L155), M154 (= M156), R217 (≠ K219), S224 (≠ K225), M225 (≠ I226), A240 (= A241), S244 (= S245), M285 (≠ F286), A315 (= A316), F316 (= F317), H345 (= H346), C375 (= C376)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
46% identity, 99% coverage: 3:390/390 of query aligns to 1:389/389 of 1dlvA
- active site: C86 (= C86), H345 (= H346), C375 (= C376), G377 (= G378)
- binding coenzyme a: C86 (= C86), L145 (= L146), H153 (≠ L155), M154 (= M156), R217 (≠ K219), L228 (= L229), A240 (= A241), S244 (= S245), H345 (= H346)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
46% identity, 99% coverage: 3:390/390 of query aligns to 4:392/392 of 1ou6A
- active site: C89 (= C86), H348 (= H346), C378 (= C376), G380 (= G378)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L146), H156 (≠ L155), M157 (= M156), F235 (= F233), A243 (= A241), S247 (= S245), A318 (= A316), F319 (= F317), H348 (= H346)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
46% identity, 99% coverage: 3:390/390 of query aligns to 3:391/391 of 2vu1A
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
46% identity, 99% coverage: 3:390/390 of query aligns to 1:389/389 of 2wkuA
- active site: C86 (= C86), H345 (= H346), C375 (= C376), G377 (= G378)
- binding D-mannose: S6 (≠ G8), A7 (= A9), R38 (vs. gap), K182 (≠ N184), D194 (≠ A196), V280 (≠ Q281), D281 (≠ A282), T287 (= T288), P331 (≠ R332), S332 (≠ D333), V334 (= V335), V336 (= V337), F360 (≠ N361)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
46% identity, 99% coverage: 3:390/390 of query aligns to 2:390/390 of 1m1oA
- active site: A87 (≠ C86), H346 (= H346), C376 (= C376), G378 (= G378)
- binding acetoacetyl-coenzyme a: L86 (≠ M85), A87 (≠ C86), L146 (= L146), H154 (≠ L155), M155 (= M156), R218 (≠ K219), S225 (≠ K225), M226 (≠ I226), A241 (= A241), G242 (≠ A242), S245 (= S245), A316 (= A316), F317 (= F317), H346 (= H346), I377 (= I377), G378 (= G378)
7feaB Py14 in complex with col-d (see paper)
46% identity, 99% coverage: 4:390/390 of query aligns to 5:393/396 of 7feaB
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
46% identity, 99% coverage: 3:390/390 of query aligns to 5:392/392 of P07097
- Q64 (= Q61) mutation to A: Slightly lower activity.
- C89 (= C86) mutation to A: Loss of activity.
- C378 (= C376) mutation to G: Loss of activity.
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
47% identity, 99% coverage: 2:388/390 of query aligns to 2:390/394 of 7cw5B
- active site: C87 (= C86), H348 (= H346), C378 (= C376), G380 (= G378)
- binding coenzyme a: L147 (= L146), H155 (≠ L155), M156 (= M156), R220 (≠ K219), T223 (≠ A221), A243 (= A241), P247 (≠ S245), L249 (≠ I247), H348 (= H346)
Query Sequence
>GFF3267 PGA1_c33180 acetyl-CoA acetyltransferase
MKTVVIAGAARTPMGGFQGMYDGVAAAELGGSAIRAALAGAGATTVDEILMGCVLPAGQG
QAPARQAGFAAGLGEEVPATTLNKMCGSGMKAAMMAYDQIALGQADTMIAGGMESMTNAP
YLLPKMRNGARLGHGQVVDHMFLDGLEDAYDKGRLMGTFAEDCAETYQFTREAQDEYALT
SLSNALAAQESGAFDAEIAPVTVKTRKGETVTNADEQPKSARPDKIPTLKPAFRKDGTVT
AANASSISDGAAALVLASEDAAEAQGLTVRARIMGHASHAQAPGLFTTAPVPAAKKLMAQ
LGWTVSDVDLWEVNEAFAVVPMAFMHEMGLPRDKVNVNGGACALGHPIGASGARIMVTLL
NALEKRNLKRGIAAICIGGGEGTAIAIERM
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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