SitesBLAST
Comparing WP_012645344.1 NCBI__GCF_000022265.1:WP_012645344.1 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)
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)
52% identity, 100% coverage: 1:391/391 of query aligns to 1:392/392 of P45359
- V77 (≠ D77) 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 (≠ M96) binding acetate
- N153 (≠ S153) 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 acetate
- A286 (≠ D285) 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 acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
52% identity, 100% coverage: 1:391/391 of query aligns to 1:392/392 of 4xl4A
- active site: C88 (= C88), H348 (= H347), S378 (≠ C377), G380 (= G379)
- binding coenzyme a: L148 (= L148), H156 (= H156), R220 (≠ L220), L231 (= L230), A243 (= A242), S247 (= S246), F319 (= F318), H348 (= H347)
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)
52% 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 (= H156) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ P219) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ K221) 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)
52% 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 (= L148), R221 (≠ K221), F236 (= F234), A244 (= A242), S248 (= S246), L250 (≠ I248), A319 (= A317), F320 (= F318), H349 (= H347)
8gqnA X-ray structure of thiolase with coa
49% identity, 99% coverage: 2:389/391 of query aligns to 1:388/390 of 8gqnA
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
50% identity, 99% coverage: 4:391/391 of query aligns to 5:392/392 of 1ou6A
- active site: C89 (= C88), H348 (= H347), C378 (= C377), G380 (= G379)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L148), H156 (= H156), M157 (= M157), F235 (= F234), A243 (= A242), S247 (= S246), A318 (= A317), F319 (= F318), H348 (= H347)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
48% identity, 100% coverage: 1:391/391 of query aligns to 1:392/393 of 6bn2A
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
50% identity, 99% coverage: 4:391/391 of query aligns to 4:391/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
50% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 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: H153 (= H156), M154 (= M157), F232 (= F234), S244 (= S246), G245 (≠ T247), F316 (= F318), H345 (= H347)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
50% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C88), H345 (= H347), C375 (= C377), G377 (= G379)
- binding acetyl coenzyme *a: C86 (= C88), L145 (= L148), H153 (= H156), M154 (= M157), R217 (≠ L220), S224 (≠ K226), M225 (≠ L227), A240 (= A242), S244 (= S246), M285 (≠ F287), A315 (= A317), F316 (= F318), H345 (= H347), C375 (= C377)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
50% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C88), H345 (= H347), C375 (= C377), G377 (= G379)
- binding coenzyme a: C86 (= C88), L145 (= L148), H153 (= H156), M154 (= M157), R217 (≠ L220), L228 (= L230), A240 (= A242), S244 (= S246), H345 (= H347)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
50% identity, 99% coverage: 5:391/391 of query aligns to 6:392/392 of P07097