SitesBLAST
Comparing 202206 SO3089 fatty oxidation complex, beta subunit (NCBI ptt file) 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)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
35% identity, 96% coverage: 15:434/436 of query aligns to 2:387/389 of 2wkuA
- active site: C86 (= C99), H345 (= H392), C375 (= C422), G377 (≠ A424)
- binding D-mannose: S6 (≠ A19), A7 (≠ G20), R38 (= R51), K182 (≠ L212), D194 (= D224), V280 (≠ I309), D281 (= D310), T287 (≠ M317), P331 (≠ M378), S332 (= S379), V334 (≠ F381), V336 (= V383), F360 (≠ R407)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
35% identity, 96% coverage: 17:434/436 of query aligns to 7:390/392 of P07097
- Q64 (≠ P74) mutation to A: Slightly lower activity.
- C89 (= C99) mutation to A: Loss of activity.
- C378 (= C422) mutation to G: Loss of activity.
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
35% identity, 96% coverage: 15:434/436 of query aligns to 4:389/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
35% identity, 96% coverage: 15:434/436 of query aligns to 2:387/389 of 2vu2A
- active site: C86 (= C99), H345 (= H392), C375 (= C422), G377 (≠ A424)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ S183), M154 (= M184), F232 (= F260), S244 (≠ T273), G245 (≠ P274), F316 (= F346), H345 (= H392)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
35% identity, 96% coverage: 15:434/436 of query aligns to 2:387/389 of 1dm3A
- active site: C86 (= C99), H345 (= H392), C375 (= C422), G377 (≠ A424)
- binding acetyl coenzyme *a: C86 (= C99), L145 (= L169), H153 (≠ S183), M154 (= M184), R217 (= R245), S224 (= S252), M225 (≠ Y253), A240 (= A269), S244 (≠ T273), M285 (= M315), A315 (= A345), F316 (= F346), H345 (= H392), C375 (= C422)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
35% identity, 96% coverage: 15:434/436 of query aligns to 2:387/389 of 1dlvA
- active site: C86 (= C99), H345 (= H392), C375 (= C422), G377 (≠ A424)
- binding coenzyme a: C86 (= C99), L145 (= L169), H153 (≠ S183), M154 (= M184), R217 (= R245), L228 (= L256), A240 (= A269), S244 (≠ T273), H345 (= H392)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
35% identity, 96% coverage: 15:434/436 of query aligns to 5:390/392 of 1ou6A
- active site: C89 (= C99), H348 (= H392), C378 (= C422), G380 (≠ A424)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L169), H156 (≠ S183), M157 (= M184), F235 (= F260), A243 (= A269), S247 (≠ T273), A318 (= A345), F319 (= F346), H348 (= H392)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
35% identity, 96% coverage: 15:434/436 of query aligns to 3:388/390 of 1m1oA
- active site: A87 (≠ C99), H346 (= H392), C376 (= C422), G378 (≠ A424)
- binding acetoacetyl-coenzyme a: L86 (≠ A98), A87 (≠ C99), L146 (= L169), H154 (≠ S183), M155 (= M184), R218 (= R245), S225 (= S252), M226 (≠ Y253), A241 (= A269), G242 (≠ A270), S245 (≠ T273), A316 (= A345), F317 (= F346), H346 (= H392), I377 (≠ A423), G378 (≠ A424)
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
34% identity, 96% coverage: 15:434/436 of query aligns to 7:388/390 of 2d3tC
- active site: C94 (= C99), H346 (= H392), C376 (= C422), G378 (≠ A424)
- binding acetyl coenzyme *a: C94 (= C99), R214 (= R245), L222 (≠ Y253), L225 (= L256), A238 (= A269), G239 (≠ A270), S242 (≠ T273), I244 (≠ L275), A313 (= A345), F314 (= F346), H346 (= H392), C376 (= C422)
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)
32% identity, 97% coverage: 13:434/436 of query aligns to 2:390/392 of P45359
- V77 (= V88) 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 (= C99) modified: Disulfide link with 378, In inhibited form
- S96 (≠ V107) binding
- N153 (≠ A176) 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 (≠ AF 305:306) binding
- A286 (≠ Q313) 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 (= C422) modified: Disulfide link with 88, In inhibited form
- A386 (= A430) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
32% identity, 97% coverage: 13:434/436 of query aligns to 2:390/392 of 4xl4A
- active site: C88 (= C99), H348 (= H392), S378 (≠ C422), G380 (≠ A424)
- binding coenzyme a: L148 (= L169), H156 (≠ S179), R220 (= R245), L231 (= L256), A243 (= A269), S247 (≠ T273), F319 (= F346), H348 (= H392)
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)
33% identity, 96% coverage: 15:434/436 of query aligns to 4:391/393 of P14611
- C88 (= C99) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ S183) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ N243) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R245) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (≠ T273) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H392) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C422) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
30% identity, 97% coverage: 13:434/436 of query aligns to 2:390/393 of 6bn2A
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
32% identity, 96% coverage: 15:434/436 of query aligns to 10:393/395 of 4c2jD
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)
32% identity, 96% coverage: 15:434/436 of query aligns to 7:394/397 of P42765
- C92 (= C99) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R245) binding
- T227 (≠ S248) binding
- S251 (≠ T273) binding
- C382 (= C422) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
33% identity, 96% coverage: 15:434/436 of query aligns to 4:391/393 of 4o9cC
- active site: S88 (≠ C99), H349 (= H392), C379 (= C422), G381 (≠ A424)
- binding coenzyme a: S88 (≠ C99), L148 (= L168), R221 (= R245), F236 (= F260), A244 (= A269), S248 (≠ T273), L250 (= L275), A319 (= A345), F320 (= F346), H349 (= H392)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
30% identity, 97% coverage: 14:435/436 of query aligns to 2:391/394 of 7cw5B
- active site: C87 (= C99), H348 (= H392), C378 (= C422), G380 (≠ A424)
- binding coenzyme a: L147 (≠ V175), H155 (≠ S183), M156 (= M184), R220 (= R245), T223 (≠ S248), A243 (= A269), P247 (≠ T273), L249 (= L275), H348 (= H392)
2f2sA Human mitochondrial acetoacetyl-coa thiolase
28% identity, 97% coverage: 11:434/436 of query aligns to 7:387/389 of 2f2sA
- active site: C95 (= C99), H347 (= H392), C375 (= C422), G377 (≠ A424)
- binding coenzyme a: C95 (= C99), L153 (≠ V175), H161 (≠ S183), M162 (= M184), Y188 (≠ H210), R220 (≠ N247), V221 (≠ S248), D222 (= D249), K225 (≠ S252), L229 (= L256), F233 (= F260), A242 (= A269), S246 (≠ T273), A317 (= A345), F318 (= F346), H347 (= H392)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
33% identity, 96% coverage: 17:434/436 of query aligns to 6:389/391 of 5f38B
- active site: C88 (= C99), H347 (= H392), C377 (= C422), G379 (≠ A424)
- binding coenzyme a: C88 (= C99), L149 (= L169), K219 (≠ R245), F234 (= F260), A242 (= A269), S246 (≠ T273), A317 (= A345), F318 (= F346), H347 (= H392)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
34% identity, 96% coverage: 17:434/436 of query aligns to 8:393/394 of 5f38D
- active site: C90 (= C99), A348 (= A389), A378 (= A419), L380 (≠ A421)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C99), L151 (= L169), A246 (= A269), S250 (≠ T273), I252 (≠ L275), A321 (= A345), F322 (= F346), H351 (= H392)
Query Sequence
>202206 SO3089 fatty oxidation complex, beta subunit (NCBI ptt file)
MSDRQQVTNARGERIAIVAGLRTPFAKQATAFHGISALDMGKMVVNELLVRSELDPKLIE
QLVYGQVVQMPAAPNIAREIVLGTGMDVSTDAYSVTRACATSFQSAVNVAESIMTGNIEI
GIAGGADSSSVLPIGVSKKLAHALVDLNKARTFGQKLQIFRRLGIKDLLPVPPAVAEYST
GLSMGQTAEQMAKTYNISRADQDALAHRSHTLANETWASGHLRDEVMVAHVPPYKQFIER
DNNIRENSDLASYAKLRPAFDKKHGSVTAANSTPLTDGASAIILMSEGRAKALGYQPIGY
IKSYAFTAIDVWQDMLMGPSYATPLALKRAGMELEDLTLIEMHEAFAAQTLANMQMFASK
KFAEEKLGRNRAIGDIDMSKFNVLGGSLAYGHPFAATGTRLITQVCRELKRRGGGTGLAT
ACAAGGLGAAMIVEVE
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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