SitesBLAST
Comparing N515DRAFT_2688 N515DRAFT_2688 acetyl-CoA acyltransferase 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)
47% identity, 98% coverage: 7:399/401 of query aligns to 37:420/424 of P09110
- V387 (≠ A367) 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.
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)
44% identity, 99% coverage: 5:399/401 of query aligns to 1:390/392 of P45359
- V77 (≠ D84) 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 (= C95) modified: Disulfide link with 378, In inhibited form
- S96 (≠ A103) binding
- N153 (vs. gap) 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 288:289) binding
- A286 (≠ D295) 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 (= C387) modified: Disulfide link with 88, In inhibited form
- A386 (= A395) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
44% identity, 99% coverage: 5:399/401 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C95), H348 (= H357), S378 (≠ C387), G380 (= G389)
- binding coenzyme a: L148 (≠ I149), H156 (≠ G152), R220 (= R226), L231 (= L237), A243 (= A252), S247 (= S256), F319 (= F328), H348 (= H357)
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
44% identity, 98% coverage: 6:399/401 of query aligns to 5:388/390 of 2d3tC
- active site: C94 (= C95), H346 (= H357), C376 (= C387), G378 (= G389)
- binding acetyl coenzyme *a: C94 (= C95), R214 (= R226), L222 (= L234), L225 (= L237), A238 (= A252), G239 (= G253), S242 (= S256), I244 (≠ T258), A313 (= A327), F314 (= F328), H346 (= H357), C376 (= C387)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
43% identity, 98% coverage: 10:401/401 of query aligns to 7:392/392 of P07097
- Q64 (≠ M70) mutation to A: Slightly lower activity.
- C89 (= C95) mutation to A: Loss of activity.
- C378 (= C387) mutation to G: Loss of activity.
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
44% identity, 98% coverage: 10:401/401 of query aligns to 7:392/392 of 1ou6A
- active site: C89 (= C95), H348 (= H357), C378 (= C387), G380 (= G389)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ I141), H156 (≠ G152), M157 (= M153), F235 (= F241), A243 (= A252), S247 (= S256), A318 (= A327), F319 (= F328), H348 (= H357)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
44% identity, 98% coverage: 10:401/401 of query aligns to 6:391/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
44% identity, 98% coverage: 10:401/401 of query aligns to 4:389/389 of 2vu2A
- active site: C86 (= C95), H345 (= H357), C375 (= C387), G377 (= G389)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ G152), M154 (= M153), F232 (= F241), S244 (= S256), G245 (≠ Q257), F316 (= F328), H345 (= H357)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
44% identity, 98% coverage: 10:401/401 of query aligns to 4:389/389 of 1dm3A
- active site: C86 (= C95), H345 (= H357), C375 (= C387), G377 (= G389)
- binding acetyl coenzyme *a: C86 (= C95), L145 (≠ I141), H153 (≠ G152), M154 (= M153), R217 (= R226), S224 (≠ V233), M225 (≠ L234), A240 (= A252), S244 (= S256), M285 (= M297), A315 (= A327), F316 (= F328), H345 (= H357), C375 (= C387)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
44% identity, 98% coverage: 10:401/401 of query aligns to 4:389/389 of 1dlvA
- active site: C86 (= C95), H345 (= H357), C375 (= C387), G377 (= G389)
- binding coenzyme a: C86 (= C95), L145 (≠ I141), H153 (≠ G152), M154 (= M153), R217 (= R226), L228 (= L237), A240 (= A252), S244 (= S256), H345 (= H357)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
43% identity, 98% coverage: 10:401/401 of query aligns to 4:389/389 of 2wkuA
- active site: C86 (= C95), H345 (= H357), C375 (= C387), G377 (= G389)
- binding D-mannose: S6 (≠ A12), A7 (= A13), R38 (≠ Q45), K182 (≠ R181), D194 (= D193), V280 (= V292), D281 (≠ R293), T287 (≠ I299), P331 (= P343), S332 (= S344), V334 (≠ I346), V336 (≠ P348), F360 (≠ H372)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
43% identity, 98% coverage: 10:401/401 of query aligns to 5:390/390 of 1m1oA
- active site: A87 (≠ C95), H346 (= H357), C376 (= C387), G378 (= G389)
- binding acetoacetyl-coenzyme a: L86 (≠ F94), A87 (≠ C95), L146 (≠ I141), H154 (≠ G152), M155 (= M153), R218 (= R226), S225 (≠ V233), M226 (≠ L234), A241 (= A252), G242 (= G253), S245 (= S256), A316 (= A327), F317 (= F328), H346 (= H357), I377 (= I388), G378 (= G389)
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)
40% identity, 98% coverage: 9:400/401 of query aligns to 8:395/397 of P42765
- C92 (= C95) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R226) binding
- T227 (≠ S229) binding
- S251 (= S256) binding
- C382 (= C387) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
40% identity, 98% coverage: 9:400/401 of query aligns to 11:394/395 of 4c2jD
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
42% identity, 99% coverage: 5:401/401 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C95), H347 (= H357), C377 (= C387), G379 (= G389)
- binding coenzyme a: C88 (= C95), L149 (≠ I141), K219 (≠ R226), F234 (= F241), A242 (= A252), S246 (= S256), A317 (= A327), F318 (= F328), H347 (= H357)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
42% identity, 99% coverage: 5:399/401 of query aligns to 3:393/394 of 5f38D
- active site: C90 (= C95), A348 (= A354), A378 (≠ V384), L380 (≠ M386)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C95), L151 (≠ I141), A246 (= A252), S250 (= S256), I252 (≠ T258), A321 (= A327), F322 (= F328), H351 (= H357)
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)
43% identity, 97% coverage: 7:395/401 of query aligns to 3:387/393 of P14611
- C88 (= C95) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ G152) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ G224) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R226) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S256) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H357) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C387) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
40% identity, 99% coverage: 6:401/401 of query aligns to 1:398/400 of 5bz4K
- active site: C87 (= C95), H354 (= H357), C384 (= C387), G386 (= G389)
- binding coenzyme a: C87 (= C95), R146 (vs. gap), M160 (= M153), R220 (= R226), A246 (= A252), G247 (= G253), S250 (= S256), Q252 (≠ T258), M291 (= M297), A321 (= A327), F322 (= F328), H354 (= H357)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
43% identity, 97% coverage: 7:395/401 of query aligns to 3:387/393 of 4o9cC
- active site: S88 (≠ C95), H349 (= H357), C379 (= C387), G381 (= G389)
- binding coenzyme a: S88 (≠ C95), L148 (vs. gap), R221 (= R226), F236 (= F241), A244 (= A252), S248 (= S256), L250 (≠ T258), A319 (= A327), F320 (= F328), H349 (= H357)
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
42% identity, 98% coverage: 5:395/401 of query aligns to 4:397/403 of 6pccA
- active site: C93 (= C95), A359 (≠ H357), C389 (= C387), G391 (= G389)
- binding coenzyme a: C93 (= C95), I148 (vs. gap), R229 (= R226), T232 (≠ S229), A252 (= A252), S256 (= S256), N325 (= N325), F328 (= F328)
- binding hexanal: N61 (≠ M63), T146 (vs. gap), I148 (vs. gap), G149 (vs. gap), R151 (vs. gap), L361 (= L359)
Query Sequence
>N515DRAFT_2688 N515DRAFT_2688 acetyl-CoA acyltransferase
MSKQVQDAYIVAATRTPVGKAPRGVFRNTRPDDMLAHVIRAVMAQAPGIDAHRIGDVIVG
CAMPEAEQGMNVARIGLLLAGLPDTVPGVTVNRFCSSGVQAIAQAADRIRLGEADLMIAA
GTESMSMVPMMGHKVAMNPGIFDNEHIGIAYGMGITAENVAKQWKISREEQDTFAAASHE
RALAAIKAGEFKDEITPFKLDDHYPDLATRSIKTDSRLIDTDEGPRPGSTVEVLGKLKPV
FRNGQFGGSVTAGNSSQTSDGAGAVLLASEAAIKEYGLTPIARFVSYSVAGVRPDIMGIG
PKEAIPKALKQAGMTQDQLDWIELNEAFAAQSLAVIKDLGLDPSKINPLGGAIALGHPLG
ATGAIRAATLVHGMRRRKQKYGMVTMCIGTGMGAAGIFESL
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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