SitesBLAST
Comparing AO356_26350 AO356_26350 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)
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
52% identity, 100% coverage: 1:394/395 of query aligns to 2:397/397 of 6aqpA
- active site: C93 (= C90), H353 (= H350), C383 (= C380), G385 (= G382)
- binding coenzyme a: C93 (= C90), L153 (= L150), Y188 (≠ T186), N226 (≠ K224), N228 (≠ R226), K231 (= K229), A248 (= A245), P249 (≠ A246), S252 (= S249), A323 (= A320), F324 (= F321), H353 (= H350)
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)
52% identity, 100% coverage: 1:394/395 of query aligns to 1:398/398 of Q4WCL5
- Y187 (≠ T186) binding
- N229 (≠ R226) binding
- K232 (= K229) binding
- A249 (= A245) binding
- P250 (≠ A246) binding
- S252 (= S248) binding
- S253 (= S249) binding
- V350 (≠ C346) binding
- N385 (≠ I381) binding
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
52% identity, 100% coverage: 1:394/395 of query aligns to 2:399/399 of 6aqpC
- active site: C93 (= C90), H355 (= H350), C385 (= C380), G387 (= G382)
- binding acetyl coenzyme *a: C93 (= C90), L153 (= L150), M162 (= M160), Y188 (≠ T186), N230 (≠ R226), K233 (= K229), L234 (≠ I230), I237 (≠ L233), A250 (= A245), P251 (≠ A246), S254 (= S249), F295 (= F290), A325 (= A320), F326 (= F321), H355 (= H350)
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)
48% identity, 98% coverage: 6:392/395 of query aligns to 4:390/392 of P45359
- V77 (≠ K79) 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 (= C90) modified: Disulfide link with 378, In inhibited form
- S96 (≠ I98) binding
- N153 (≠ D155) 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 (≠ AA 281:282) binding
- A286 (≠ S288) 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 (= C380) modified: Disulfide link with 88, In inhibited form
- A386 (= A388) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
48% identity, 98% coverage: 6:392/395 of query aligns to 4:390/392 of 4xl4A
- active site: C88 (= C90), H348 (= H350), S378 (≠ C380), G380 (= G382)
- binding coenzyme a: L148 (= L150), H156 (≠ R158), R220 (≠ P223), L231 (= L233), A243 (= A245), S247 (= S249), F319 (= F321), H348 (= H350)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
48% identity, 98% coverage: 7:393/395 of query aligns to 4:391/394 of 7cw5B
- active site: C87 (= C90), H348 (= H350), C378 (= C380), G380 (= G382)
- binding coenzyme a: L147 (= L150), H155 (≠ L159), M156 (= M160), R220 (≠ P223), T223 (≠ A225), A243 (= A245), P247 (≠ S249), L249 (≠ I251), H348 (= H350)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
47% identity, 98% coverage: 6:394/395 of query aligns to 4:392/393 of 6bn2A
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)
48% identity, 98% coverage: 6:392/395 of query aligns to 5:396/398 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)
48% identity, 98% coverage: 6:392/395 of query aligns to 4:391/393 of P14611
- C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ R158) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ Q221) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ P223) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S249) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H350) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C380) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
48% identity, 98% coverage: 6:392/395 of query aligns to 4:391/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H350), C379 (= C380), G381 (= G382)
- binding coenzyme a: S88 (≠ C90), L148 (= L150), R221 (≠ P223), F236 (= F237), A244 (= A245), S248 (= S249), L250 (≠ I251), A319 (= A320), F320 (= F321), H349 (= H350)
P24752 Acetyl-CoA acetyltransferase, mitochondrial; Acetoacetyl-CoA thiolase; T2; EC 2.3.1.9 from Homo sapiens (Human) (see 6 papers)
47% identity, 98% coverage: 6:394/395 of query aligns to 42:427/427 of P24752
- N93 (≠ C57) to S: in 3KTD; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074145
- N158 (= N122) to D: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs148639841
- G183 (= G149) to R: in 3KTD; no activity; dbSNP:rs120074141
- Y219 (≠ T186) binding ; binding
- RVD 258:260 (≠ KAR 224:226) binding
- K263 (= K229) binding
- A280 (= A245) binding
- A281 (= A246) binding
- A283 (≠ S248) binding
- S284 (= S249) binding
- T297 (≠ R262) to M: in 3KTD; decreased protein abundance; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs886041122
- A301 (= A266) to P: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs1420321267
- I312 (= I277) to T: in 3KTD; decreased protein stability; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074146
- A333 (≠ V298) to P: in 3KTD; loss of protein solubility; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs120074147
- A380 (= A345) to T: in 3KTD; decreased protein stability; dbSNP:rs120074140
- V381 (≠ C346) binding
Sites not aligning to the query:
- 5 A → P: in dbSNP:rs3741056
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)
47% identity, 98% coverage: 6:394/395 of query aligns to 8:393/393 of 2ib8D
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
50% identity, 98% coverage: 7:392/395 of query aligns to 7:393/394 of 5f38D
- active site: C90 (= C90), A348 (= A347), A378 (= A377), L380 (≠ I379)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C90), L151 (= L150), A246 (= A245), S250 (= S249), I252 (= I251), A321 (= A320), F322 (= F321), H351 (= H350)
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)
47% identity, 99% coverage: 3:392/395 of query aligns to 5:395/397 of Q9BWD1
- K211 (= K211) to R: in dbSNP:rs25683
- R223 (≠ P223) binding
- S226 (≠ A225) binding
- S252 (= S249) binding
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
47% identity, 99% coverage: 3:392/395 of query aligns to 2:392/394 of 1wl4A
- active site: C89 (= C90), H350 (= H350), C380 (= C380), G382 (= G382)
- binding coenzyme a: L148 (= L150), M157 (= M160), R220 (≠ P223), Y234 (≠ A236), P245 (≠ A245), A246 (= A246), S249 (= S249), A320 (= A320), F321 (= F321), H350 (= H350)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
46% identity, 99% coverage: 2:394/395 of query aligns to 1:392/392 of 1ou6A
- active site: C89 (= C90), H348 (= H350), C378 (= C380), G380 (= G382)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L150), H156 (≠ L159), M157 (= M160), F235 (= F237), A243 (= A245), S247 (= S249), A318 (= A320), F319 (= F321), H348 (= H350)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
46% identity, 98% coverage: 6:394/395 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C90), H345 (= H350), C375 (= C380), G377 (= G382)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ L159), M154 (= M160), F232 (= F237), S244 (= S249), G245 (≠ S250), F316 (= F321), H345 (= H350)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
46% identity, 98% coverage: 6:394/395 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C90), H345 (= H350), C375 (= C380), G377 (= G382)
- binding acetyl coenzyme *a: C86 (= C90), L145 (= L150), H153 (≠ L159), M154 (= M160), R217 (≠ P223), S224 (≠ K229), M225 (≠ I230), A240 (= A245), S244 (= S249), M285 (≠ F290), A315 (= A320), F316 (= F321), H345 (= H350), C375 (= C380)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
46% identity, 98% coverage: 6:394/395 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C90), H345 (= H350), C375 (= C380), G377 (= G382)
- binding coenzyme a: C86 (= C90), L145 (= L150), H153 (≠ L159), M154 (= M160), R217 (≠ P223), L228 (= L233), A240 (= A245), S244 (= S249), H345 (= H350)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
46% identity, 98% coverage: 6:394/395 of query aligns to 4:391/391 of 2vu1A
Query Sequence
>AO356_26350 AO356_26350 acetyl-CoA acetyltransferase
MSNDPIVIVSAVRTPMGGFQGELKSLTAPQLGAAAIKAAVERAGIAPGAVEEVLFGCVLA
AGQGQAPARQAALGAGLDKSTRCTTLNKMCGSGMEAAILAHDMLIAGSAEVVVAGGMESM
SNAPYLLDRARGGYRMGHGRVLDHMFLDGLEDAYDKGRLMGTFAEDCAEANGLGREAQDA
FAIASTTRAQQAIEDGSFDAEIVPLQVMVGKEQVTIRHDEQPPKARIDKIASLKPAFREG
GTVTAANSSSISDGAAALVLMRQSQAVQRGLKPLAVIHGHAAFADTPSLFPTAPIGAVKK
LMQKTGWTLDQVDLFEVNEAFAVVGLVTMDKLEIAHDKVNVHGGACALGHPIGASGARIL
VTLLSALRQKGLKRGVAAICIGGGEATAMAVECLY
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