SitesBLAST
Comparing WP_043527088.1 NCBI__GCF_000759345.1:WP_043527088.1 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
67% identity, 99% coverage: 5:393/394 of query aligns to 2:390/390 of 8gqnA
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
47% identity, 98% coverage: 7:392/394 of query aligns to 4:391/394 of 7cw5B
- active site: C87 (= C90), H348 (= H349), C378 (= C379), G380 (= G381)
- binding coenzyme a: L147 (= L150), H155 (≠ L158), M156 (= M159), R220 (≠ F222), T223 (≠ A224), A243 (= A244), P247 (≠ S248), L249 (≠ I250), H348 (= H349)
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
45% identity, 98% coverage: 6:393/394 of query aligns to 8:397/397 of 6aqpA
- active site: C93 (= C90), H353 (= H349), C383 (= C379), G385 (= G381)
- binding coenzyme a: C93 (= C90), L153 (= L150), Y188 (≠ L185), N226 (≠ Q223), N228 (≠ K225), 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)
45% identity, 98% coverage: 6:393/394 of query aligns to 7:398/398 of Q4WCL5
- Y187 (≠ L185) binding K(+)
- N229 (≠ K225) binding CoA
- K232 (= K228) binding CoA
- A249 (= A244) binding K(+)
- P250 (≠ A245) binding K(+)
- S252 (≠ A247) 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
45% identity, 98% coverage: 6:393/394 of query aligns to 8:399/399 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 (≠ K225), 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)
42% identity, 98% coverage: 5:391/394 of query aligns to 3:390/392 of P45359
- V77 (≠ D79) 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 (≠ 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 (≠ AT 280:281) binding acetate
- A286 (≠ S287) 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)
42% identity, 98% coverage: 5:391/394 of query aligns to 3:390/392 of 4xl4A
- active site: C88 (= C90), H348 (= H349), S378 (≠ C379), G380 (= G381)
- binding coenzyme a: L148 (= L150), H156 (≠ L158), R220 (vs. gap), L231 (= L232), A243 (= A244), S247 (= S248), F319 (= F320), H348 (= H349)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
44% identity, 98% coverage: 5:391/394 of query aligns to 3:390/393 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)
46% identity, 98% coverage: 5:391/394 of query aligns to 3:391/393 of P14611
- C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ L158) 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 (≠ F222) 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)
46% identity, 98% coverage: 5:391/394 of query aligns to 3:391/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H349), C379 (= C379), G381 (= G381)
- binding coenzyme a: S88 (≠ C90), L148 (= L150), R221 (≠ F222), 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)
45% identity, 99% coverage: 2:391/394 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)
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)
43% identity, 99% coverage: 5:393/394 of query aligns to 4:398/398 of P41338