SitesBLAST
Comparing WP_110806646.1 NCBI__GCF_003217355.1:WP_110806646.1 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)
8gqnA X-ray structure of thiolase with coa
63% identity, 98% coverage: 6:391/395 of query aligns to 3:388/390 of 8gqnA
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
48% identity, 98% coverage: 6:391/395 of query aligns to 8:395/397 of 6aqpA
- active site: C93 (= C90), H353 (= H349), C383 (= C379), G385 (= G381)
- binding coenzyme a: C93 (= C90), L153 (= L150), Y188 (≠ L186), N226 (≠ K223), N228 (≠ R225), K231 (= K228), A248 (= A244), P249 (≠ A245), S252 (= S248), A323 (= A319), F324 (= F320), H353 (= H349)
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)
48% identity, 98% coverage: 6:391/395 of query aligns to 7:396/398 of Q4WCL5
- Y187 (≠ L186) binding K(+)
- N229 (≠ R225) binding CoA
- K232 (= K228) binding CoA
- A249 (= A244) binding K(+)
- P250 (≠ A245) binding K(+)
- S252 (= S247) binding K(+)
- S253 (= S248) binding CoA
- V350 (≠ C345) binding K(+)
- N385 (≠ I380) binding chloride
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
48% identity, 98% coverage: 6:391/395 of query aligns to 8:397/399 of 6aqpC
- active site: C93 (= C90), H355 (= H349), C385 (= C379), G387 (= G381)
- binding acetyl coenzyme *a: C93 (= C90), L153 (= L150), M162 (= M160), Y188 (≠ L186), N230 (≠ R225), K233 (= K228), L234 (≠ I229), I237 (≠ L232), A250 (= A244), P251 (≠ A245), S254 (= S248), F295 (= F289), A325 (= A319), F326 (= F320), H355 (= H349)
P45359 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; CaTHL; EC 2.3.1.9 from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W) (see paper)
47% identity, 98% coverage: 6:392/395 of query aligns to 4:391/392 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 acetate
- N153 (≠ D155) 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 280:281) binding acetate
- A286 (≠ N287) 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 acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
46% identity, 98% coverage: 6:392/395 of query aligns to 4:391/392 of 4xl4A
- active site: C88 (= C90), H348 (= H349), S378 (≠ C379), G380 (= G381)
- binding coenzyme a: L148 (= L150), H156 (≠ R158), R220 (≠ G222), L231 (= L232), A243 (= A244), S247 (= S248), F319 (= F320), H348 (= H349)
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)
48% identity, 99% coverage: 2:392/395 of query aligns to 1:392/393 of P14611
- C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ R158) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ Q220) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ G222) 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.
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
47% identity, 99% coverage: 2:393/395 of query aligns to 1:392/392 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.
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)
46% identity, 99% coverage: 2:393/395 of query aligns to 1:398/398 of P41338
- M1 (= M2) modified: Initiator methionine, Removed
- S2 (≠ T3) modified: N-acetylserine
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
48% identity, 99% coverage: 3:393/395 of query aligns to 2:392/392 of 1ou6A
- active site: C89 (= C90), H348 (= H349), C378 (= C379), G380 (= G381)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L150), H156 (≠ L159), M157 (= M160), F235 (= F236), A243 (= A244), S247 (= S248), A318 (= A319), F319 (= F320), H348 (= H349)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
48% identity, 99% coverage: 3:393/395 of query aligns to 1:391/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
48% identity, 98% coverage: 6:393/395 of query aligns to 2:389/389 of 2vu2A