SitesBLAST
Comparing 3606642 Dshi_0074 acetyl-CoA acetyltransferase (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)
47% identity, 100% coverage: 1:391/392 of query aligns to 1:391/392 of P45359
- V77 (≠ D77) 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 (= C88) modified: Disulfide link with 378, In inhibited form
- S96 (≠ M96) binding
- N153 (≠ D153) 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 279:280) binding
- A286 (= A286) 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 (= C378) modified: Disulfide link with 88, In inhibited form
- A386 (= A386) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
47% identity, 100% coverage: 1:391/392 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C88), H348 (= H348), S378 (≠ C378), G380 (= G380)
- binding coenzyme a: L148 (= L148), H156 (≠ R156), R220 (≠ A221), L231 (= L231), A243 (= A243), S247 (= S247), F319 (= F319), H348 (= H348)
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, 100% coverage: 1:391/392 of query aligns to 1:392/393 of P14611
- C88 (= C88) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ R156) 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 (≠ P220) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S247) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H348) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C378) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
45% identity, 100% coverage: 1:391/392 of query aligns to 1:391/393 of 6bn2A
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
47% identity, 100% coverage: 1:391/392 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C88), H349 (= H348), C379 (= C378), G381 (= G380)
- binding coenzyme a: S88 (≠ C88), L148 (= L148), R221 (≠ P220), F236 (= F235), A244 (= A243), S248 (= S247), L250 (≠ I249), A319 (= A318), F320 (= F319), H349 (= H348)
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
46% identity, 99% coverage: 4:390/392 of query aligns to 8:395/397 of 6aqpA
- active site: C93 (= C88), H353 (= H348), C383 (= C378), G385 (= G380)
- binding coenzyme a: C93 (= C88), L153 (= L148), Y188 (≠ L184), N226 (≠ A222), N228 (≠ R224), K231 (= K227), A248 (= A243), P249 (≠ A244), S252 (= S247), A323 (= A318), F324 (= F319), H353 (= H348)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
45% identity, 99% coverage: 3:390/392 of query aligns to 4:390/392 of 1ou6A
- active site: C89 (= C88), H348 (= H348), C378 (= C378), G380 (= G380)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L148), H156 (≠ L157), M157 (= M158), F235 (= F235), A243 (= A243), S247 (= S247), A318 (= A318), F319 (= F319), H348 (= H348)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
45% identity, 99% coverage: 3:390/392 of query aligns to 3:389/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
45% identity, 99% coverage: 3:390/392 of query aligns to 1:387/389 of 2vu2A
- active site: C86 (= C88), H345 (= H348), C375 (= C378), G377 (= G380)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ L157), M154 (= M158), F232 (= F235), S244 (= S247), G245 (≠ S248), F316 (= F319), H345 (= H348)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
45% identity, 99% coverage: 3:390/392 of query aligns to 1:387/389 of 1dm3A
- active site: C86 (= C88), H345 (= H348), C375 (= C378), G377 (= G380)
- binding acetyl coenzyme *a: C86 (= C88), L145 (= L148), H153 (≠ L157), M154 (= M158), R217 (≠ P220), S224 (≠ K227), M225 (≠ I228), A240 (= A243), S244 (= S247), M285 (≠ F288), A315 (= A318), F316 (= F319), H345 (= H348), C375 (= C378)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
45% identity, 99% coverage: 3:390/392 of query aligns to 1:387/389 of 1dlvA
- active site: C86 (= C88), H345 (= H348), C375 (= C378), G377 (= G380)
- binding coenzyme a: C86 (= C88), L145 (= L148), H153 (≠ L157), M154 (= M158), R217 (≠ P220), L228 (= L231), A240 (= A243), S244 (= S247), H345 (= H348)
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)
46% identity, 99% coverage: 4:390/392 of query aligns to 7:396/398 of Q4WCL5
- Y187 (≠ L184) binding
- N229 (≠ R224) binding
- K232 (= K227) binding
- A249 (= A243) binding
- P250 (≠ A244) binding
- S252 (= S246) binding
- S253 (= S247) binding
- V350 (≠ C344) binding
- N385 (≠ I379) binding
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
46% identity, 99% coverage: 4:390/392 of query aligns to 8:397/399 of 6aqpC
- active site: C93 (= C88), H355 (= H348), C385 (= C378), G387 (= G380)
- binding acetyl coenzyme *a: C93 (= C88), L153 (= L148), M162 (= M158), Y188 (≠ L184), N230 (≠ R224), K233 (= K227), L234 (≠ I228), I237 (≠ L231), A250 (= A243), P251 (≠ A244), S254 (= S247), F295 (= F288), A325 (= A318), F326 (= F319), H355 (= H348)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
50% identity, 100% coverage: 1:391/392 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C88), A348 (= A345), A378 (= A375), L380 (≠ I377)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C88), L151 (= L148), A246 (= A243), S250 (= S247), I252 (= I249), A321 (= A318), F322 (= F319), H351 (= H348)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
45% identity, 99% coverage: 3:390/392 of query aligns to 1:387/389 of 2wkuA
- active site: C86 (= C88), H345 (= H348), C375 (= C378), G377 (= G380)
- binding D-mannose: S6 (≠ G8), A7 (= A9), R38 (≠ D40), K182 (≠ N186), D194 (≠ M198), V280 (≠ Q283), D281 (≠ K284), T287 (= T290), P331 (≠ R334), S332 (≠ E335), V334 (≠ M337), V336 (= V339), F360 (≠ N363)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
45% identity, 99% coverage: 3:390/392 of query aligns to 2:388/390 of 1m1oA
- active site: A87 (≠ C88), H346 (= H348), C376 (= C378), G378 (= G380)
- binding acetoacetyl-coenzyme a: L86 (≠ M87), A87 (≠ C88), L146 (= L148), H154 (≠ L157), M155 (= M158), R218 (≠ P220), S225 (≠ K227), M226 (≠ I228), A241 (= A243), G242 (≠ A244), S245 (= S247), A316 (= A318), F317 (= F319), H346 (= H348), I377 (= I379), G378 (= G380)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
45% identity, 98% coverage: 6:390/392 of query aligns to 5:390/394 of 7cw5B
- active site: C87 (= C88), H348 (= H348), C378 (= C378), G380 (= G380)
- binding coenzyme a: L147 (= L148), H155 (≠ L157), M156 (= M158), R220 (≠ A221), T223 (≠ A223), A243 (= A243), P247 (≠ S247), L249 (≠ I249), H348 (= H348)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
45% identity, 98% coverage: 6:390/392 of query aligns to 7:390/392 of P07097
- Q64 (= Q63) mutation to A: Slightly lower activity.
- C89 (= C88) mutation to A: Loss of activity.
- C378 (= C378) mutation to G: Loss of activity.
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
49% identity, 100% coverage: 1:391/392 of query aligns to 1:390/391 of 5f38B
- active site: C88 (= C88), H347 (= H348), C377 (= C378), G379 (= G380)
- binding coenzyme a: C88 (= C88), L149 (= L148), K219 (≠ A221), F234 (= F235), A242 (= A243), S246 (= S247), A317 (= A318), F318 (= F319), H347 (= H348)
7feaB Py14 in complex with col-d (see paper)
44% identity, 99% coverage: 4:391/392 of query aligns to 5:392/396 of 7feaB
Query Sequence
>3606642 Dshi_0074 acetyl-CoA acetyltransferase (RefSeq)
MRTVAICGAARTPMGGFQGVFSDVSAAQLGGAAIAGALADAGVAPAQVNELLMGCVLPAG
QGQAPARQAGYAAGLGDAVPATTLNKMCGSGMKAAMIACDQIALGQSDLVVAGGMESMTN
APYLLDKMRGGARIGHGQVIDHMFLDGLEDAYDKGRLMGTFAEDCAEAFQFTRAAQDTYA
LGSLENALAAEASEAFAMELVPVTVSGRKGETVVIRDEQPAAARPEKIPHLKPAFRKDGT
VTAANSSSISDGAAALVLADAGQAEAHGLPVRARVLGHASHAQKPALFPTAPVPAARKLL
DRLGWCVADVDLWEVNEAFAVVPMAFMHEMGVPREKMNVNGGACALGHPIGASGARILVT
LLNAMEARDLKRGVAAICIGGGEGTAIALERD
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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