SitesBLAST
Comparing 6937205 FitnessBrowser__SB2B:6937205 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
49% identity, 99% coverage: 3:391/392 of query aligns to 1:390/392 of P45359
- V77 (≠ L79) 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 (≠ M98) binding
- N153 (≠ T155) 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 (≠ TT 280:281) binding
- A286 (= A287) 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 (= C379) modified: Disulfide link with 88, In inhibited form
- A386 (= A387) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
49% identity, 99% coverage: 3:391/392 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C90), H348 (= H349), S378 (≠ C379), G380 (= G381)
- binding coenzyme a: L148 (= L150), H156 (≠ A158), R220 (≠ G222), L231 (= L232), A243 (= A244), S247 (= S248), F319 (= F320), H348 (= H349)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
48% identity, 99% coverage: 3:391/392 of query aligns to 1:390/393 of 6bn2A
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)
51% identity, 99% coverage: 3:391/392 of query aligns to 1:391/393 of P14611
- C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ A158) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (vs. gap) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ Q220) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S248) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H349) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C379) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
50% identity, 99% coverage: 3:391/392 of query aligns to 1:391/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H349), C379 (= C379), G381 (= G381)
- binding coenzyme a: S88 (≠ C90), L148 (= L150), R221 (≠ Q220), F236 (= F236), A244 (= A244), S248 (= S248), L250 (≠ I250), A319 (= A319), F320 (= F320), H349 (= H349)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
52% identity, 99% coverage: 2:391/392 of query aligns to 2:393/394 of 5f38D
- active site: C90 (= C90), A348 (= A346), A378 (= A376), L380 (= L378)
- 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 (= A244), S250 (= S248), I252 (= I250), A321 (= A319), F322 (= F320), H351 (= H349)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
47% identity, 99% coverage: 4:392/392 of query aligns to 1:391/394 of 7cw5B
- active site: C87 (= C90), H348 (= H349), C378 (= C379), G380 (= G381)
- binding coenzyme a: L147 (= L150), H155 (≠ A158), M156 (= M159), R220 (vs. gap), T223 (≠ A224), A243 (= A244), P247 (≠ S248), L249 (≠ I250), H348 (= H349)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
51% identity, 99% coverage: 3:391/392 of query aligns to 1:389/391 of 5f38B
- active site: C88 (= C90), H347 (= H349), C377 (= C379), G379 (= G381)
- binding coenzyme a: C88 (= C90), L149 (= L150), K219 (vs. gap), F234 (= F236), A242 (= A244), S246 (= S248), A317 (= A319), F318 (= F320), H347 (= H349)
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, 99% coverage: 4:391/392 of query aligns to 3:396/398 of P41338
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
46% identity, 99% coverage: 2:391/392 of query aligns to 1:390/392 of 1ou6A
- active site: C89 (= C90), H348 (= H349), C378 (= C379), G380 (= G381)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L150), H156 (≠ A158), M157 (= M159), F235 (= F236), A243 (= A244), S247 (= S248), A318 (= A319), F319 (= F320), H348 (= H349)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
47% identity, 98% coverage: 6:391/392 of query aligns to 2:387/389 of 2vu2A
- active site: C86 (= C90), H345 (= H349), C375 (= C379), G377 (= G381)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ A158), M154 (= M159), F232 (= F236), S244 (= S248), G245 (≠ S249), F316 (= F320), H345 (= H349)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
47% identity, 98% coverage: 6:391/392 of query aligns to 2:387/389 of 1dm3A
- active site: C86 (= C90), H345 (= H349), C375 (= C379), G377 (= G381)
- binding acetyl coenzyme *a: C86 (= C90), L145 (= L150), H153 (≠ A158), M154 (= M159), R217 (≠ G222), S224 (≠ K228), M225 (≠ I229), A240 (= A244), S244 (= S248), M285 (≠ F289), A315 (= A319), F316 (= F320), H345 (= H349), C375 (= C379)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
47% identity, 98% coverage: 6:391/392 of query aligns to 2:387/389 of 1dlvA
- active site: C86 (= C90), H345 (= H349), C375 (= C379), G377 (= G381)
- binding coenzyme a: C86 (= C90), L145 (= L150), H153 (≠ A158), M154 (= M159), R217 (≠ G222), L228 (= L232), A240 (= A244), S244 (= S248), H345 (= H349)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
47% identity, 98% coverage: 6:391/392 of query aligns to 4:389/391 of 2vu1A
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
46% identity, 100% coverage: 2:392/392 of query aligns to 4:396/397 of 6aqpA
- active site: C93 (= C90), H353 (= H349), C383 (= C379), G385 (= G381)
- binding coenzyme a: C93 (= C90), L153 (= L150), Y188 (≠ L185), N226 (= N223), N228 (≠ R225), K231 (= K228), A248 (= A244), P249 (≠ A245), S252 (= S248), A323 (= A319), F324 (= F320), H353 (= H349)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
46% identity, 98% coverage: 6:391/392 of query aligns to 2:387/389 of 2wkuA
- active site: C86 (= C90), H345 (= H349), C375 (= C379), G377 (= G381)
- binding D-mannose: S6 (≠ A10), A7 (= A11), R38 (≠ D42), K182 (= K187), D194 (≠ A199), V280 (≠ Q284), D281 (≠ E285), T287 (= T291), P331 (≠ A335), S332 (≠ A336), V334 (= V338), V336 (= V340), F360 (≠ H364)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
46% identity, 100% coverage: 1:391/392 of query aligns to 1:390/392 of P07097
- Q64 (= Q65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C379) mutation to G: Loss of activity.
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
46% identity, 98% coverage: 6:391/392 of query aligns to 3:388/390 of 1m1oA
- active site: A87 (≠ C90), H346 (= H349), C376 (= C379), G378 (= G381)
- binding acetoacetyl-coenzyme a: L86 (≠ V89), A87 (≠ C90), L146 (= L150), H154 (≠ A158), M155 (= M159), R218 (≠ G222), S225 (≠ K228), M226 (≠ I229), A241 (= A244), G242 (≠ A245), S245 (= S248), A316 (= A319), F317 (= F320), H346 (= H349), I377 (= I380), G378 (= G381)
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)
46% identity, 100% coverage: 2:392/392 of query aligns to 3:397/398 of Q4WCL5
- Y187 (≠ L185) binding
- N229 (≠ R225) binding
- K232 (= K228) binding
- A249 (= A244) binding
- P250 (≠ A245) binding
- S252 (= S247) binding
- S253 (= S248) binding
- V350 (≠ C345) binding
- N385 (≠ I380) binding
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
46% identity, 100% coverage: 2:392/392 of query aligns to 4:398/399 of 6aqpC
- active site: C93 (= C90), H355 (= H349), C385 (= C379), G387 (= G381)
- binding acetyl coenzyme *a: C93 (= C90), L153 (= L150), M162 (= M159), Y188 (≠ L185), N230 (≠ R225), K233 (= K228), L234 (≠ I229), I237 (≠ L232), A250 (= A244), P251 (≠ A245), S254 (= S248), F295 (= F289), A325 (= A319), F326 (= F320), H355 (= H349)
Query Sequence
>6937205 FitnessBrowser__SB2B:6937205
MSVSDIVIVAAKRTAMGGFQGSLSEVPSPKLAATAVKALLDDTGLDGARVDELLMGCVLP
AGLGQAPARQAALGAGLPLSVGATTVNKVCGSGMKTVMLAHDLIKAGSAKVVIAGGMESM
SQAPYLLDKARGGMRMGHGKVLDHMFLDGLEDAYTGGAMGTFAQKTADDYGLTRESMDAF
ALSSLEKANAAINSGAFEAEIVPVTVSSRKGDVEVKVDEQPGNARPEKIPTLRPAFAKDG
TITAANSSSISDGAAALMLMSRDQADALGLKVLATIKGHTTHAQEPAMFTTAPVGAMTKL
LSNVGWSKDEVDLFEINEAFAMVTMLAISELKLDAARVNVNGGACALGHPIGCSGARVLV
TLIHALKARGLKRGVASLCIGGGEATAMAIEV
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