SitesBLAST
Comparing Dsui_0317 Dsui_0317 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)
P09110 3-ketoacyl-CoA thiolase, peroxisomal; Acetyl-CoA C-myristoyltransferase; Acetyl-CoA acyltransferase; Beta-ketothiolase; Peroxisomal 3-oxoacyl-CoA thiolase; EC 2.3.1.16; EC 2.3.1.155; EC 2.3.1.9 from Homo sapiens (Human) (see 3 papers)
46% identity, 98% coverage: 7:397/399 of query aligns to 37:420/424 of P09110
- V387 (≠ T365) to A: in dbSNP:rs2229528
Sites not aligning to the query:
- 1:26 PTS2-type peroxisomal targeting signal
- 5 mutation Q->D,K,L: Does not affect localization to peroxisomes.
- 6 V→D: Abolished localization to peroxisomes.; V→K: Does not affect localization to peroxisomes.
- 7 mutation V->D,K: Abolished localization to peroxisomes.
- 8 mutation L->D,K: Does not affect localization to peroxisomes.
- 9 mutation G->D,R,L: Does not affect localization to peroxisomes.
- 10 H→E: In S3E mutant; Abolished localization to peroxisomes.
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
45% identity, 98% coverage: 6:397/399 of query aligns to 5:388/390 of 2d3tC
- active site: C94 (= C94), H346 (= H355), C376 (= C385), G378 (= G387)
- binding acetyl coenzyme *a: C94 (= C94), R214 (= R227), L222 (= L235), L225 (= L238), A238 (= A250), G239 (= G251), S242 (= S254), I244 (≠ M256), A313 (= A325), F314 (= F326), H346 (= H355), C376 (= C385)
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)
41% identity, 98% coverage: 5:397/399 of query aligns to 1:390/392 of P45359
- V77 (≠ D83) 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 (= C94) modified: Disulfide link with 378, In inhibited form
- S96 (≠ A102) binding
- N153 (≠ I150) 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 (≠ SV 286:287) binding
- A286 (≠ E293) 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 (= C385) modified: Disulfide link with 88, In inhibited form
- A386 (= A393) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
41% identity, 98% coverage: 5:397/399 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C94), H348 (= H355), S378 (≠ C385), G380 (= G387)
- binding coenzyme a: L148 (≠ D145), H156 (≠ G153), R220 (= R227), L231 (= L238), A243 (= A250), S247 (= S254), F319 (= F326), H348 (= H355)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
41% identity, 98% coverage: 10:399/399 of query aligns to 7:392/392 of P07097
- Q64 (≠ M69) mutation to A: Slightly lower activity.
- C89 (= C94) mutation to A: Loss of activity.
- C378 (= C385) mutation to G: Loss of activity.
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
41% identity, 98% coverage: 10:399/399 of query aligns to 4:389/389 of 2vu2A
- active site: C86 (= C94), H345 (= H355), C375 (= C385), G377 (= G387)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ G153), M154 (= M154), F232 (= F242), S244 (= S254), G245 (≠ Q255), F316 (= F326), H345 (= H355)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
41% identity, 98% coverage: 10:399/399 of query aligns to 4:389/389 of 1dm3A
- active site: C86 (= C94), H345 (= H355), C375 (= C385), G377 (= G387)
- binding acetyl coenzyme *a: C86 (= C94), L145 (≠ D145), H153 (≠ G153), M154 (= M154), R217 (= R227), S224 (≠ G234), M225 (≠ L235), A240 (= A250), S244 (= S254), M285 (= M295), A315 (= A325), F316 (= F326), H345 (= H355), C375 (= C385)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
41% identity, 98% coverage: 10:399/399 of query aligns to 4:389/389 of 1dlvA
- active site: C86 (= C94), H345 (= H355), C375 (= C385), G377 (= G387)
- binding coenzyme a: C86 (= C94), L145 (≠ D145), H153 (≠ G153), M154 (= M154), R217 (= R227), L228 (= L238), A240 (= A250), S244 (= S254), H345 (= H355)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
41% identity, 98% coverage: 10:399/399 of query aligns to 6:391/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
41% identity, 98% coverage: 10:399/399 of query aligns to 7:392/392 of 1ou6A
- active site: C89 (= C94), H348 (= H355), C378 (= C385), G380 (= G387)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ D145), H156 (≠ G153), M157 (= M154), F235 (= F242), A243 (= A250), S247 (= S254), A318 (= A325), F319 (= F326), H348 (= H355)
P42765 3-ketoacyl-CoA thiolase, mitochondrial; Acetyl-CoA acetyltransferase; Acetyl-CoA acyltransferase; Acyl-CoA hydrolase, mitochondrial; Beta-ketothiolase; Mitochondrial 3-oxoacyl-CoA thiolase; T1; EC 2.3.1.16; EC 2.3.1.9; EC 3.1.2.-; EC 3.1.2.1; EC 3.1.2.2 from Homo sapiens (Human) (see paper)
39% identity, 99% coverage: 5:398/399 of query aligns to 4:395/397 of P42765
- C92 (= C94) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R227) binding
- T227 (≠ S230) binding
- S251 (= S254) binding
- C382 (= C385) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
41% identity, 98% coverage: 10:399/399 of query aligns to 4:389/389 of 2wkuA
- active site: C86 (= C94), H345 (= H355), C375 (= C385), G377 (= G387)
- binding D-mannose: S6 (≠ A12), A7 (= A13), R38 (≠ Q44), K182 (= K182), D194 (= D194), V280 (= V290), D281 (≠ P291), T287 (≠ I297), P331 (= P341), S332 (≠ A342), V334 (≠ I344), V336 (≠ P346), F360 (≠ H370)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
38% identity, 99% coverage: 5:398/399 of query aligns to 7:394/395 of 4c2jD
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
41% identity, 98% coverage: 10:399/399 of query aligns to 5:390/390 of 1m1oA
- active site: A87 (≠ C94), H346 (= H355), C376 (= C385), G378 (= G387)
- binding acetoacetyl-coenzyme a: L86 (≠ F93), A87 (≠ C94), L146 (≠ D145), H154 (≠ G153), M155 (= M154), R218 (= R227), S225 (≠ G234), M226 (≠ L235), A241 (= A250), G242 (= G251), S245 (= S254), A316 (= A325), F317 (= F326), H346 (= H355), I377 (= I386), G378 (= G387)
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
43% identity, 97% coverage: 5:393/399 of query aligns to 4:397/403 of 6pccA
- active site: C93 (= C94), A359 (≠ H355), C389 (= C385), G391 (= G387)
- binding coenzyme a: C93 (= C94), I148 (= I150), R229 (= R227), T232 (≠ S230), A252 (= A250), S256 (= S254), N325 (= N323), F328 (= F326)
- binding hexanal: N61 (≠ M62), T146 (≠ V148), I148 (= I150), G149 (≠ A151), R151 (vs. gap), L361 (= L357)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
43% identity, 97% coverage: 5:393/399 of query aligns to 4:397/403 of 6pcbA
- active site: C93 (= C94), A359 (≠ H355), C389 (= C385), G391 (= G387)
- binding coenzyme a: C93 (= C94), I148 (= I150), R229 (= R227), A252 (= A250), S256 (= S254), G257 (≠ Q255), N325 (= N323), F328 (= F326)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
42% identity, 97% coverage: 5:393/399 of query aligns to 5:395/401 of 6pcdA
- active site: S94 (≠ C94), A357 (≠ H355), C387 (= C385), G389 (= G387)
- binding coenzyme a: I149 (= I150), M167 (= M154), R227 (= R227), T230 (≠ S230), A250 (= A250), S254 (= S254), G255 (≠ Q255), A325 (= A325), A357 (≠ H355)
- binding octanal: N62 (≠ M62), T147 (≠ V148), T148 (≠ A149), I149 (= I150), G150 (≠ A151), R152 (vs. gap), L359 (= L357)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
40% identity, 99% coverage: 5:399/399 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C94), H347 (= H355), C377 (= C385), G379 (= G387)
- binding coenzyme a: C88 (= C94), L149 (≠ E146), K219 (≠ R227), F234 (= F242), A242 (= A250), S246 (= S254), A317 (= A325), F318 (= F326), H347 (= H355)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
39% identity, 98% coverage: 5:397/399 of query aligns to 3:393/394 of 5f38D
- active site: C90 (= C94), A348 (= A352), A378 (≠ V382), L380 (≠ M384)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C94), L151 (vs. gap), A246 (= A250), S250 (= S254), I252 (≠ M256), A321 (= A325), F322 (= F326), H351 (= H355)
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)
40% identity, 97% coverage: 5:393/399 of query aligns to 1:387/393 of P14611
- C88 (= C94) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ G153) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ G225) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R227) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S254) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H355) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C385) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
Query Sequence
>Dsui_0317 Dsui_0317 acetyl-CoA acetyltransferase
MTKQIQDAYIVAATRLPVAKRNGMFKTTRPDDMLAHALKSVMAQVPQLDPALVEDVIVGC
AMPEAEQGMNVARIGLLLAGLPDTVPGLTINRFCSSGVQAVADAAARIRLGEADVMLAAG
TETMSLMSQMMGNKVSLNPAIFEKDENVAIAYGMGLTAEKVAQKWGISRDDQDAFAVASH
QKAVAAIAAGKFKDEISPYTVRAHLPDLKSGTVRIVEKVCDTDEGPRPDSSLQGLAKLKP
VFNARGSVTAGNSSQMSDGAGAVLLVSEKILKQFNLQPLARFAGFSVAGVPPEIMGIGPI
AAIPKVLAQAGIKQDDLDWIELNEAFAAQALAVTRELGLDPAKINPQGGAIALGHPLGAT
GAIRTATLVHGMRRENKKWGMVTMCIGTGMGAAGLFEAL
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