SitesBLAST
Comparing CA265_RS06590 CA265_RS06590 acetyl-CoA acetyltransferase to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
64% identity, 99% coverage: 1:388/391 of query aligns to 1:389/393 of 6bn2A
P24752 Acetyl-CoA acetyltransferase, mitochondrial; Acetoacetyl-CoA thiolase; T2; EC 2.3.1.9 from Homo sapiens (Human) (see 6 papers)
55% identity, 100% coverage: 1:391/391 of query aligns to 39:427/427 of P24752
- N93 (= N55) to S: in 3KTD; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074145
- N158 (= N119) to D: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs148639841
- G183 (= G146) to R: in 3KTD; no activity; dbSNP:rs120074141
- Y219 (= Y182) binding ; binding
- RVD 258:260 (≠ AVK 221:223) binding
- K263 (= K226) binding
- A280 (= A242) binding
- A281 (= A243) binding
- A283 (= A245) binding
- S284 (= S246) binding
- T297 (≠ S259) to M: in 3KTD; decreased protein abundance; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs886041122
- A301 (= A263) to P: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs1420321267
- I312 (= I274) to T: in 3KTD; decreased protein stability; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074146
- A333 (≠ I295) to P: in 3KTD; loss of protein solubility; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs120074147
- A380 (= A342) to T: in 3KTD; decreased protein stability; dbSNP:rs120074140
- V381 (= V343) binding
Sites not aligning to the query:
- 5 A → P: in dbSNP:rs3741056
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
55% identity, 99% coverage: 1:388/391 of query aligns to 5:394/397 of 6aqpA
- active site: C93 (= C87), H353 (= H347), C383 (= C377), G385 (= G379)
- binding coenzyme a: C93 (= C87), L153 (= L147), Y188 (= Y182), N226 (≠ A221), N228 (≠ K223), K231 (= K226), A248 (= A242), P249 (≠ A243), S252 (= S246), A323 (= A317), F324 (= F318), H353 (= H347)
2ib8D Crystallographic and kinetic studies of human mitochondrial acetoacetyl-coa thiolase (t2): the importance of potassium and chloride for its structure and function (see paper)
55% identity, 100% coverage: 1:391/391 of query aligns to 5:393/393 of 2ib8D
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)
55% identity, 99% coverage: 1:388/391 of query aligns to 4:395/398 of Q4WCL5
- Y187 (= Y182) binding
- N229 (≠ K223) binding
- K232 (= K226) binding
- A249 (= A242) binding
- P250 (≠ A243) binding
- S252 (≠ A245) binding
- S253 (= S246) binding
- V350 (= V343) binding
- N385 (= N378) binding
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
55% identity, 99% coverage: 1:388/391 of query aligns to 5:396/399 of 6aqpC
- active site: C93 (= C87), H355 (= H347), C385 (= C377), G387 (= G379)
- binding acetyl coenzyme *a: C93 (= C87), L153 (= L147), M162 (= M156), Y188 (= Y182), N230 (≠ K223), K233 (= K226), L234 (≠ I227), I237 (≠ L230), A250 (= A242), P251 (≠ A243), S254 (= S246), F295 (= F287), A325 (= A317), F326 (= F318), H355 (= H347)
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)
54% identity, 100% coverage: 1:390/391 of query aligns to 1:391/392 of P45359
- V77 (vs. gap) 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 (= C87) modified: Disulfide link with 378, In inhibited form
- S96 (≠ M95) binding
- N153 (= N152) 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 (≠ AD 278:279) binding
- A286 (≠ E285) 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 (= C377) modified: Disulfide link with 88, In inhibited form
- A386 (= A385) binding
2f2sA Human mitochondrial acetoacetyl-coa thiolase
55% identity, 99% coverage: 3:391/391 of query aligns to 10:389/389 of 2f2sA
- active site: C95 (= C87), H347 (= H347), C375 (= C377), G377 (= G379)
- binding coenzyme a: C95 (= C87), L153 (= L147), H161 (= H155), M162 (= M156), Y188 (= Y182), R220 (≠ A221), V221 (= V222), D222 (≠ K223), K225 (= K226), L229 (= L230), F233 (= F234), A242 (= A242), S246 (= S246), A317 (= A317), F318 (= F318), H347 (= H347)
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
53% identity, 100% coverage: 1:390/391 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C87), H348 (= H347), S378 (≠ C377), G380 (= G379)
- binding coenzyme a: L148 (= L147), H156 (= H155), R220 (≠ T220), L231 (= L230), A243 (= A242), S247 (= S246), F319 (= F318), H348 (= H347)
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)
54% identity, 100% coverage: 2:391/391 of query aligns to 3:398/398 of P41338
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
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)
54% identity, 99% coverage: 1:388/391 of query aligns to 1:390/393 of P14611
- C88 (= C87) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (= H155) 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 (≠ P219) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S246) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H347) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C377) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
54% identity, 99% coverage: 1:388/391 of query aligns to 1:390/393 of 4o9cC
- active site: S88 (≠ C87), H349 (= H347), C379 (= C377), G381 (= G379)
- binding coenzyme a: S88 (≠ C87), L148 (= L147), R221 (≠ P219), F236 (= F234), A244 (= A242), S248 (= S246), L250 (= L248), A319 (= A317), F320 (= F318), H349 (= H347)
B0XMC1 Acetyl-CoA acetyltransferase erg10A, mitochondrial; Acetoacetyl-CoA thiolase erg10A; Ergosterol biosynthesis protein 10A; EC 2.3.1.9 from Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) (see paper)
52% identity, 100% coverage: 1:391/391 of query aligns to 37:429/433 of B0XMC1
6l2cA Crystal structure of aspergillus fumigatus mitochondrial acetyl-coa acetyltransferase in complex with coa (see paper)
52% identity, 100% coverage: 1:391/391 of query aligns to 6:398/402 of 6l2cA
- active site: C93 (= C87), H356 (= H347), C384 (= C377), G386 (= G379)
- binding coenzyme a: C93 (= C87), Y188 (= Y182), N226 (≠ A221), R228 (≠ K223), M232 (≠ I227), L235 (= L230), F239 (= F234), A249 (= A242), S253 (= S246), F327 (= F318)
Q22100 Acetyl-CoA acetyltransferase homolog, mitochondrial; 3-ketoacyl-CoA thiolase; EC 2.3.1.- from Caenorhabditis elegans (see 2 papers)
51% identity, 100% coverage: 2:391/391 of query aligns to 22:407/407 of Q22100
- A119 (= A98) mutation to P: In mg368; increased uptake of the lipophilic dye Nile Red and the synthetic fatty acid analog C1-BODIPY-C12.
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
49% identity, 99% coverage: 3:388/391 of query aligns to 2:389/394 of 7cw5B
- active site: C87 (= C87), H348 (= H347), C378 (= C377), G380 (= G379)
- binding coenzyme a: L147 (= L147), H155 (= H155), M156 (= M156), R220 (≠ T220), T223 (≠ V222), A243 (= A242), P247 (≠ S246), L249 (= L248), H348 (= H347)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
51% identity, 100% coverage: 1:390/391 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C87), A348 (≠ S344), A378 (= A374), L380 (≠ I376)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C87), L151 (= L147), A246 (= A242), S250 (= S246), I252 (≠ L248), A321 (= A317), F322 (= F318), H351 (= H347)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
50% identity, 100% coverage: 1:391/391 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C87), H347 (= H347), C377 (= C377), G379 (= G379)
- binding coenzyme a: C88 (= C87), L149 (= L147), K219 (≠ T220), F234 (= F234), A242 (= A242), S246 (= S246), A317 (= A317), F318 (= F318), H347 (= H347)
6bjbA Crystal structure of acat2-c91s thiolase from ascaris suum in complex with propionyl-coa and nitrate (see paper)
49% identity, 100% coverage: 1:391/391 of query aligns to 3:384/384 of 6bjbA
- active site: S90 (≠ C87), H342 (= H347), C370 (= C377), G372 (= G379)
- binding propionyl Coenzyme A: S90 (≠ C87), L148 (= L147), M157 (= M156), Y183 (= Y182), N218 (≠ K223), K221 (= K226), I222 (= I227), L225 (= L230), A237 (= A242), A238 (= A243), S241 (= S246), F282 (= F287), A312 (= A317), F313 (= F318), H342 (= H347), C370 (= C377), N371 (= N378), G372 (= G379)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
46% identity, 99% coverage: 4:391/391 of query aligns to 5:392/392 of 1ou6A
- active site: C89 (= C87), H348 (= H347), C378 (= C377), G380 (= G379)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L147), H156 (= H155), M157 (= M156), F235 (= F234), A243 (= A242), S247 (= S246), A318 (= A317), F319 (= F318), H348 (= H347)
Query Sequence
>CA265_RS06590 CA265_RS06590 acetyl-CoA acetyltransferase
MKEVVIVSAVRTPIGSFGGSLAQFSATQLGGFAIKAAIEKAGLKPEQIQEVYMGNVLSAN
LGQAPATQAAKFAGLPDLPATTINKVCASGTKAIMLAAQSIANGDNEIIVAGGMESMSNV
PYYLDKARNGYRLGHGQITDGLVKDGLWDVYNDYHMGSAAELCATECNINREAQDNFAIS
SYKRAQAAQTSGKFANEIVAIEVKDRKGDITLVDTDDEPTAVKFDKIPSLKPVFKKDGTV
TAANASTLNDGAAALVLMSADKAKELGLTPLAKILGYADAQQAPEWFTTAPSKAIPLALH
KANVNINDVDFFEINEAFAVVSIANNQLLALNDNQVNVNGGAVSLGHPLGASGARIVVTL
LSVLAQNDGKIGVAGICNGGGGASALVIGKL
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