SitesBLAST
Comparing RR42_RS07610 RR42_RS07610 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)
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)
92% identity, 100% coverage: 1:393/393 of query aligns to 1:393/393 of P14611
- C88 (= C88) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (= H156) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (= F219) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R221) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S248) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H349) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C379) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
92% identity, 100% coverage: 1:393/393 of query aligns to 1:393/393 of 4o9cC
- active site: S88 (≠ C88), H349 (= H349), C379 (= C379), G381 (= G381)
- binding coenzyme a: S88 (≠ C88), L148 (= L148), R221 (= R221), F236 (= F236), A244 (= A244), S248 (= S248), L250 (= L250), A319 (= A319), F320 (= F320), H349 (= H349)
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)
63% identity, 100% coverage: 1:392/393 of query aligns to 1:391/392 of P45359
- V77 (= V77) 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 (= N153) 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 (≠ GT 280:281) binding
- A286 (≠ K287) 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 (= C379) modified: Disulfide link with 88, In inhibited form
- A386 (= A387) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
63% identity, 100% coverage: 1:392/393 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C88), H348 (= H349), S378 (≠ C379), G380 (= G381)
- binding coenzyme a: L148 (= L148), H156 (= H156), R220 (= R221), L231 (= L232), A243 (= A244), S247 (= S248), F319 (= F320), H348 (= H349)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
64% identity, 99% coverage: 4:391/393 of query aligns to 5:390/392 of 1ou6A
- active site: C89 (= C88), H348 (= H349), C378 (= C379), G380 (= G381)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L148), H156 (= H156), M157 (= M157), F235 (= F236), A243 (= A244), S247 (= S248), A318 (= A319), F319 (= F320), H348 (= H349)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
64% identity, 99% coverage: 4:391/393 of query aligns to 4:389/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
64% identity, 99% coverage: 4:391/393 of query aligns to 2:387/389 of 2vu2A
- active site: C86 (= C88), H345 (= H349), C375 (= C379), G377 (= G381)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (= H156), M154 (= M157), F232 (= F236), S244 (= S248), G245 (= G249), F316 (= F320), H345 (= H349)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
64% identity, 99% coverage: 4:391/393 of query aligns to 2:387/389 of 1dm3A
- active site: C86 (= C88), H345 (= H349), C375 (= C379), G377 (= G381)
- binding acetyl coenzyme *a: C86 (= C88), L145 (= L148), H153 (= H156), M154 (= M157), R217 (= R221), S224 (≠ A228), M225 (≠ L229), A240 (= A244), S244 (= S248), M285 (= M289), A315 (= A319), F316 (= F320), H345 (= H349), C375 (= C379)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
64% identity, 99% coverage: 4:391/393 of query aligns to 2:387/389 of 1dlvA
- active site: C86 (= C88), H345 (= H349), C375 (= C379), G377 (= G381)
- binding coenzyme a: C86 (= C88), L145 (= L148), H153 (= H156), M154 (= M157), R217 (= R221), L228 (= L232), A240 (= A244), S244 (= S248), H345 (= H349)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
64% identity, 99% coverage: 4:391/393 of query aligns to 2:387/389 of 2wkuA
- active site: C86 (= C88), H345 (= H349), C375 (= C379), G377 (= G381)
- binding D-mannose: S6 (= S8), A7 (= A9), R38 (= R40), K182 (= K185), D194 (≠ E197), V280 (= V284), D281 (= D285), T287 (≠ M291), P331 (≠ T335), S332 (= S336), V334 (= V338), V336 (= V340), F360 (≠ H364)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
64% identity, 99% coverage: 4:391/393 of query aligns to 3:388/390 of 1m1oA
- active site: A87 (≠ C88), H346 (= H349), C376 (= C379), G378 (= G381)
- binding acetoacetyl-coenzyme a: L86 (≠ V87), A87 (≠ C88), L146 (= L148), H154 (= H156), M155 (= M157), R218 (= R221), S225 (≠ A228), M226 (≠ L229), A241 (= A244), G242 (≠ A245), S245 (= S248), A316 (= A319), F317 (= F320), H346 (= H349), I377 (= I380), G378 (= G381)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
63% identity, 99% coverage: 2:391/393 of query aligns to 3:390/392 of P07097
- Q64 (= Q63) mutation to A: Slightly lower activity.
- C89 (= C88) mutation to A: Loss of activity.
- C378 (= C379) mutation to G: Loss of activity.
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
57% identity, 99% coverage: 4:393/393 of query aligns to 5:394/394 of 1wl4A
- active site: C89 (= C88), H350 (= H349), C380 (= C379), G382 (= G381)
- binding coenzyme a: L148 (= L148), M157 (= M157), R220 (= R221), Y234 (≠ A235), P245 (≠ A244), A246 (= A245), S249 (= S248), A320 (= A319), F321 (= F320), H350 (= H349)
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)
57% identity, 99% coverage: 4:393/393 of query aligns to 8:397/397 of Q9BWD1
- K211 (= K208) to R: in dbSNP:rs25683
- R223 (= R221) binding
- S226 (≠ V224) binding
- S252 (= S248) binding
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
60% identity, 100% coverage: 1:392/393 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C88), A348 (= A346), A378 (= A376), L380 (= L378)
- 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 (= A244), S250 (= S248), I252 (≠ L250), A321 (= A319), F322 (= F320), H351 (= H349)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
60% identity, 100% coverage: 1:392/393 of query aligns to 1:390/391 of 5f38B
- active site: C88 (= C88), H347 (= H349), C377 (= C379), G379 (= G381)
- binding coenzyme a: C88 (= C88), L149 (= L148), K219 (≠ R221), F234 (= F236), A242 (= A244), S246 (= S248), A317 (= A319), F318 (= F320), H347 (= H349)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
54% identity, 98% coverage: 5:391/393 of query aligns to 4:390/394 of 7cw5B
- active site: C87 (= C88), H348 (= H349), C378 (= C379), G380 (= G381)
- binding coenzyme a: L147 (= L148), H155 (= H156), M156 (= M157), R220 (= R221), T223 (≠ V224), A243 (= A244), P247 (≠ S248), L249 (= L250), H348 (= H349)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
51% identity, 100% coverage: 1:392/393 of query aligns to 1:391/393 of 6bn2A
A0R1Y7 Probable acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; EC 2.3.1.9 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
54% identity, 99% coverage: 5:392/393 of query aligns to 1:388/388 of A0R1Y7
- K187 (= K191) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7feaB Py14 in complex with col-d (see paper)
51% identity, 99% coverage: 3:392/393 of query aligns to 4:392/396 of 7feaB
Query Sequence
>RR42_RS07610 RR42_RS07610 acetyl-CoA acetyltransferase
MTDIVIVSAARTAVGKFGGSLAKIPAPELGAIVIKAALERAGVKPEQVSEVIMGQVLTAG
SGQNPARQAALKAGLPVMVPAMTINKVCGSGLKAVMLAANAIAAGDAEIVVAGGQENMSA
APHVLPGSRDGFRMGDAKLIDSMIVDGLWDVYNQYHMGVTAENVAKEYGITREAQDAFAA
GSQNKAEAAQKAGKFDEEIVPVPIPQRKGDPVMFATDEFVRHGVTQDALAGLKPAFDKAG
SVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIRAYGTAGVDPKVMGMGPVPASKRC
LSRAGWSVEELDLMEINEAFAAQALAVHKQMGWDTSKVNVNGGAIAIGHPIGASGCRILV
TLLHEMKRRDAHKGLASLCIGGGMGVALAVERK
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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