SitesBLAST
Comparing GFF329 FitnessBrowser__Phaeo:GFF329 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)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
74% identity, 99% coverage: 3:389/391 of query aligns to 1:387/389 of 2vu2A
- active site: C86 (= C88), H345 (= H347), C375 (= C377), G377 (= G379)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: C86 (= C88), L145 (= L147), H153 (= H155), M154 (= M156), F232 (= F234), A240 (= A242), S244 (= S246), G245 (= G247), L246 (= L248), A315 (= A317), F316 (= F318), H345 (= H347)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
74% identity, 99% coverage: 3:389/391 of query aligns to 1:387/389 of 1dm3A
- active site: C86 (= C88), H345 (= H347), C375 (= C377), G377 (= G379)
- binding acetyl coenzyme *a: C86 (= C88), L145 (= L147), H153 (= H155), M154 (= M156), R217 (= R219), S224 (≠ A226), M225 (= M227), L228 (= L230), F232 (= F234), A240 (= A242), G241 (≠ A243), A243 (= A245), S244 (= S246), G245 (= G247), L246 (= L248), M285 (= M287), A315 (= A317), F316 (= F318), H345 (= H347), C375 (= C377), I376 (= I378)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
74% identity, 99% coverage: 3:389/391 of query aligns to 1:387/389 of 1dlvA
- active site: C86 (= C88), H345 (= H347), C375 (= C377), G377 (= G379)
- binding coenzyme a: C86 (= C88), L145 (= L147), H153 (= H155), M154 (= M156), R217 (= R219), S224 (≠ A226), M225 (= M227), L228 (= L230), F232 (= F234), A240 (= A242), G241 (≠ A243), S244 (= S246), G245 (= G247), L246 (= L248), F316 (= F318), H345 (= H347)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
74% identity, 99% coverage: 3:389/391 of query aligns to 4:390/392 of 1ou6A
- active site: C89 (= C88), H348 (= H347), C378 (= C377), G380 (= G379)
- binding pantothenyl-aminoethanol-acetate pivalic acid: I144 (= I143), L148 (= L147), H156 (= H155), M157 (= M156), A234 (= A233), F235 (= F234), A243 (= A242), S247 (= S246), G248 (= G247), L249 (= L248), A318 (= A317), F319 (= F318), H348 (= H347)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
74% identity, 99% coverage: 3:389/391 of query aligns to 3:389/391 of 2vu1A
- active site: C88 (= C88), H347 (= H347), C377 (= C377), G379 (= G379)
- binding pantothenyl-aminoethanol-11-pivalic acid: L147 (= L147), H155 (= H155), F234 (= F234), A242 (= A242), S246 (= S246), G247 (= G247), L248 (= L248), A317 (= A317), F318 (= F318), H347 (= H347)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
74% identity, 99% coverage: 3:389/391 of query aligns to 1:387/389 of 2wkuA
- active site: C86 (= C88), H345 (= H347), C375 (= C377), G377 (= G379)
- binding D-mannose: A5 (= A7), S6 (= S8), A7 (= A9), R38 (= R40), K182 (= K184), D194 (= D196), L269 (= L271), V280 (≠ L282), D281 (= D283), V284 (≠ I286), T287 (≠ V289), P331 (= P333), S332 (≠ A334), V334 (= V336), N335 (= N337), V336 (= V338), F360 (= F362), R365 (= R367)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
74% identity, 99% coverage: 3:389/391 of query aligns to 2:388/390 of 1m1oA
- active site: A87 (≠ C88), H346 (= H347), C376 (= C377), G378 (= G379)
- binding acetoacetyl-coenzyme a: L86 (≠ V87), A87 (≠ C88), L146 (= L147), H154 (= H155), M155 (= M156), R218 (= R219), S225 (≠ A226), M226 (= M227), L229 (= L230), F233 (= F234), A241 (= A242), G242 (≠ A243), S245 (= S246), G246 (= G247), L247 (= L248), A316 (= A317), F317 (= F318), H346 (= H347), C376 (= C377), I377 (= I378), G378 (= G379)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
73% identity, 99% coverage: 3:389/391 of query aligns to 5:390/392 of P07097
- Q64 (= Q63) mutation to A: Slightly lower activity.
- C89 (= C88) mutation to A: Loss of activity.
- C378 (= C377) mutation to G: Loss of activity.
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)
65% identity, 100% coverage: 1:390/391 of query aligns to 1:392/393 of P14611
- C88 (= C88) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (= H155) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ Y217) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R219) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S246) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H347) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C377) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
65% identity, 100% coverage: 1:390/391 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C88), H349 (= H347), C379 (= C377), G381 (= G379)
- binding coenzyme a: S88 (≠ C88), L148 (= L147), H156 (= H155), R221 (= R219), S228 (≠ A226), L232 (= L230), F236 (= F234), A244 (= A242), A247 (= A245), S248 (= S246), G249 (= G247), L250 (= L248), A319 (= A317), F320 (= F318), H349 (= H347), I351 (= I349), C379 (= C377)
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)
61% identity, 100% coverage: 1:390/391 of query aligns to 1:391/392 of P45359
- V77 (≠ Q77) 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 (= C88) modified: Disulfide link with 378, In inhibited form
- S96 (≠ A96) binding
- N153 (= N152) 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 (≠ AT 278:279) binding
- A286 (≠ S285) 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 (= C377) modified: Disulfide link with 88, In inhibited form
- A386 (= A385) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
61% identity, 100% coverage: 1:390/391 of query aligns to 1:391/392 of 4xl4A