SitesBLAST
Comparing AO353_27530 FitnessBrowser__pseudo3_N2E3:AO353_27530 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)
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, 99% coverage: 4:393/394 of query aligns to 2:391/392 of P45359
- V77 (≠ K80) 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 (= C91) modified: Disulfide link with 378, In inhibited form
- S96 (≠ V99) binding
- N153 (≠ A155) 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 (≠ AH 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, 99% coverage: 4:393/394 of query aligns to 2:391/392 of 4xl4A
- active site: C88 (= C91), H348 (= H350), S378 (≠ C380), G380 (= G382)
- binding coenzyme a: L148 (= L150), H156 (= H158), R220 (= R222), L231 (≠ M233), A243 (= A245), S247 (= S249), F319 (= F321), H348 (= H350)
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)
47% identity, 99% coverage: 4:393/394 of query aligns to 2:392/393 of P14611
- C88 (= C91) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (= H158) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ H220) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R222) 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)
47% identity, 99% coverage: 4:393/394 of query aligns to 2:392/393 of 4o9cC
- active site: S88 (≠ C91), H349 (= H350), C379 (= C380), G381 (= G382)
- binding coenzyme a: S88 (≠ C91), L148 (= L150), R221 (= R222), F236 (= F237), A244 (= A245), S248 (= S249), L250 (= L251), A319 (= A320), F320 (= F321), H349 (= H350)
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)
44% identity, 98% coverage: 6:392/394 of query aligns to 7:394/397 of P42765
- C92 (= C91) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R222) binding
- T227 (≠ V225) binding
- S251 (= S249) binding
- C382 (= C380) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
48% identity, 99% coverage: 5:393/394 of query aligns to 5:394/394 of 5f38D
- active site: C90 (= C91), A348 (≠ S347), A378 (= A377), L380 (≠ M379)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C91), L151 (= L150), A246 (= A245), S250 (= S249), I252 (≠ L251), A321 (= A320), F322 (= F321), H351 (= H350)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
45% identity, 99% coverage: 6:394/394 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C91), 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 (= H158), M154 (= M159), F232 (= F237), S244 (= S249), G245 (= G250), F316 (= F321), H345 (= H350)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
45% identity, 99% coverage: 6:394/394 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C91), H345 (= H350), C375 (= C380), G377 (= G382)
- binding acetyl coenzyme *a: C86 (= C91), L145 (= L150), H153 (= H158), M154 (= M159), R217 (= R222), S224 (≠ Q229), M225 (≠ L230), A240 (= A245), S244 (= S249), M285 (= M290), A315 (= A320), F316 (= F321), H345 (= H350), C375 (= C380)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
45% identity, 99% coverage: 6:394/394 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C91), H345 (= H350), C375 (= C380), G377 (= G382)
- binding coenzyme a: C86 (= C91), L145 (= L150), H153 (= H158), M154 (= M159), R217 (= R222), L228 (≠ M233), A240 (= A245), S244 (= S249), H345 (= H350)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
45% identity, 100% coverage: 2:394/394 of query aligns to 1:391/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
45% identity, 100% coverage: 2:394/394 of query aligns to 2:392/392 of 1ou6A
- active site: C89 (= C91), H348 (= H350), C378 (= C380), G380 (= G382)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L150), H156 (= H158), M157 (= M159), F235 (= F237), A243 (= A245), S247 (= S249), A318 (= A320), F319 (= F321), H348 (= H350)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
44% identity, 99% coverage: 6:394/394 of query aligns to 2:389/389 of 2wkuA
- active site: C86 (= C91), H345 (= H350), C375 (= C380), G377 (= G382)
- binding D-mannose: S6 (= S10), A7 (= A11), R38 (= R42), K182 (≠ R187), D194 (≠ G199), V280 (= V285), D281 (≠ E286), T287 (≠ L292), P331 (= P336), S332 (≠ E337), V334 (= V339), V336 (≠ P341), F360 (≠ H365)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
44% identity, 98% coverage: 7:394/394 of query aligns to 6:392/392 of P07097
- Q64 (≠ R64) mutation to A: Slightly lower activity.
- C89 (= C91) mutation to A: Loss of activity.
- C378 (= C380) mutation to G: Loss of activity.
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
44% identity, 99% coverage: 6:394/394 of query aligns to 3:390/390 of 1m1oA
- active site: A87 (≠ C91), H346 (= H350), C376 (= C380), G378 (= G382)
- binding acetoacetyl-coenzyme a: L86 (= L90), A87 (≠ C91), L146 (= L150), H154 (= H158), M155 (= M159), R218 (= R222), S225 (≠ Q229), M226 (≠ L230), A241 (= A245), G242 (= G246), S245 (= S249), A316 (= A320), F317 (= F321), H346 (= H350), I377 (= I381), G378 (= G382)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
48% identity, 99% coverage: 5:394/394 of query aligns to 3:391/391 of 5f38B
- active site: C88 (= C91), H347 (= H350), C377 (= C380), G379 (= G382)
- binding coenzyme a: C88 (= C91), L149 (= L150), K219 (≠ R222), F234 (= F237), A242 (= A245), S246 (= S249), A317 (= A320), F318 (= F321), H347 (= H350)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
44% identity, 98% coverage: 6:392/394 of query aligns to 10:393/395 of 4c2jD
7feaB Py14 in complex with col-d (see paper)
46% identity, 99% coverage: 4:394/394 of query aligns to 3:393/396 of 7feaB
7ei4A Crystal structure of masl in complex with a novel covalent inhibitor, collimonin c (see paper)
45% identity, 99% coverage: 4:394/394 of query aligns to 2:390/392 of 7ei4A
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)
42% identity, 98% coverage: 6:393/394 of query aligns to 8:396/397 of Q9BWD1
- K211 (= K210) to R: in dbSNP:rs25683
- R223 (= R222) binding
- S226 (≠ V225) binding
- S252 (= S249) binding
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
42% identity, 98% coverage: 6:393/394 of query aligns to 5:393/394 of 1wl4A
- active site: C89 (= C91), H350 (= H350), C380 (= C380), G382 (= G382)
- binding coenzyme a: L148 (= L150), M157 (= M159), R220 (= R222), Y234 (≠ A236), P245 (≠ A245), A246 (≠ G246), S249 (= S249), A320 (= A320), F321 (= F321), H350 (= H350)
Query Sequence
>AO353_27530 FitnessBrowser__pseudo3_N2E3:AO353_27530
MNPSDIFVVSAVRSAIGSFGGSLKDVPPIQLATDVCRAAIERSGLAPEHIGHAVMGHVIP
TEARDAYISRAVAMNAGLPKETPAFNVNRLCGSGLQAIVSAAQSLMLGDTGAALAGGVES
MSRGAYLLPQARWGARMGDIQGIDYMLGVLQDPFAGFHMGITAENIAEHYGISRQTQDQL
ALLSQQRAARAIAEGRFTGQIVPIEVASRKGTVSFATDEHVRAEVSFEQLSGMKPAFKKD
GSVTAGNASGLNDGAGALIMATGQVVQEQGLKPMARLVGYAHAGVEPSMMGLGPIPATRL
VLKRAGLTVADLDVIESNEAFAAQACAVAQELGFDPEKVNPNGSGISLGHPVGATGAIIA
TKAIHELHRIQGRYALATMCIGGGQGIAVLFERV
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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