SitesBLAST
Comparing WP_095511582.1 NCBI__GCF_002283365.1:WP_095511582.1 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)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
53% identity, 99% coverage: 5:389/390 of query aligns to 6:391/393 of 6bn2A
8gqnA X-ray structure of thiolase with coa
55% identity, 99% coverage: 4:388/390 of query aligns to 4:388/390 of 8gqnA
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)
51% identity, 99% coverage: 4:389/390 of query aligns to 5:391/392 of P45359
- V77 (≠ Q76) 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 (= C87) modified: Disulfide link with 378, In inhibited form
- S96 (≠ M95) binding acetate
- N153 (≠ D152) 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 (≠ SQ 277:278) binding acetate
- A286 (≠ M284) 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 (= C376) modified: Disulfide link with 88, In inhibited form
- A386 (= A384) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
51% identity, 99% coverage: 4:389/390 of query aligns to 5:391/392 of 4xl4A
- active site: C88 (= C87), H348 (= H346), S378 (≠ C376), G380 (= G378)
- binding coenzyme a: L148 (= L147), H156 (≠ A155), R220 (≠ A219), L231 (= L229), A243 (= A241), S247 (= S245), F319 (= F317), H348 (= H346)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
51% identity, 99% coverage: 3:388/390 of query aligns to 3:390/394 of 7cw5B
- active site: C87 (= C87), H348 (= H346), C378 (= C376), G380 (= G378)
- binding coenzyme a: L147 (= L147), H155 (≠ A155), M156 (= M156), R220 (= R220), T223 (= T221), A243 (= A241), P247 (≠ S245), L249 (≠ I247), H348 (= H346)
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
52% identity, 99% coverage: 2:388/390 of query aligns to 7:395/397 of 6aqpA
- active site: C93 (= C87), H353 (= H346), C383 (= C376), G385 (= G378)
- binding coenzyme a: C93 (= C87), L153 (= L147), Y188 (= Y182), N226 (≠ R220), N228 (= N222), K231 (= K225), A248 (= A241), P249 (≠ A242), S252 (= S245), A323 (= A316), F324 (= F317), H353 (= H346)
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)
52% identity, 99% coverage: 2:388/390 of query aligns to 6:396/398 of Q4WCL5
- Y187 (= Y182) binding K(+)
- N229 (= N222) binding CoA
- K232 (= K225) binding CoA
- A249 (= A241) binding K(+)
- P250 (≠ A242) binding K(+)
- S252 (≠ A244) binding K(+)
- S253 (= S245) binding CoA
- V350 (= V342) binding K(+)
- N385 (≠ I377) binding chloride
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
52% identity, 99% coverage: 2:388/390 of query aligns to 7:397/399 of 6aqpC
- active site: C93 (= C87), H355 (= H346), C385 (= C376), G387 (= G378)
- binding acetyl coenzyme *a: C93 (= C87), L153 (= L147), M162 (= M156), Y188 (= Y182), N230 (= N222), K233 (= K225), L234 (≠ I226), I237 (≠ L229), A250 (= A241), P251 (≠ A242), S254 (= S245), F295 (= F286), A325 (= A316), F326 (= F317), H355 (= H346)
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)
53% identity, 99% coverage: 4:389/390 of query aligns to 5:392/393 of P14611
- C88 (= C87) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ A155) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ P218) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R220) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S245) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H346) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C376) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase 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)
51% identity, 99% coverage: 5:389/390 of query aligns to 7:397/398 of P41338
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
53% identity, 99% coverage: 4:389/390 of query aligns to 5:392/393 of 4o9cC
- active site: S88 (≠ C87), H349 (= H346), C379 (= C376), G381 (= G378)
- binding coenzyme a: S88 (≠ C87), L148 (= L147), R221 (= R220), F236 (= F233), A244 (= A241), S248 (= S245), L250 (≠ I247), A319 (= A316), F320 (= F317), H349 (= H346)
P24752 Acetyl-CoA acetyltransferase, mitochondrial; Acetoacetyl-CoA thiolase; T2; EC 2.3.1.9 from Homo sapiens (Human) (see 6 papers)
49% identity, 99% coverage: 4:389/390 of query aligns to 43:426/427 of P24752