SitesBLAST
Comparing WP_100845789.1 NCBI__GCF_003031005.1:WP_100845789.1 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)
66% identity, 100% coverage: 1:392/393 of query aligns to 1:391/392 of P45359
- V77 (≠ H77) 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 (≠ H96) binding acetate
- N153 (= N153) 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 (≠ AN 280:281) binding acetate
- A286 (= A287) 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
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)
68% identity, 100% coverage: 1:392/393 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 (≠ Q219) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R221) 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.
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
65% identity, 100% coverage: 1:392/393 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C88), H348 (= H349), S378 (≠ C379), G380 (= G381)
- binding coenzyme a: L148 (= L148), H156 (= H156), R220 (= R221), L231 (= L232), A243 (= A244), S247 (= S248), F319 (= F320), H348 (= H349)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
67% identity, 100% coverage: 1:392/393 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C88), H349 (= H349), C379 (= C379), G381 (= G381)
- binding coenzyme a: S88 (≠ C88), L148 (= L148), R221 (= R221), F236 (= F236), A244 (= A244), S248 (= S248), L250 (= L250), A319 (= A319), F320 (= F320), H349 (= H349)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
57% identity, 99% coverage: 4:391/393 of query aligns to 2:387/389 of 2vu2A
- active site: C86 (= C88), H345 (= H349), C375 (= C379), G377 (= G381)
- 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 (= F236), S244 (= S248), G245 (≠ S249), F316 (= F320), H345 (= H349)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
57% identity, 99% coverage: 4:391/393 of query aligns to 2:387/389 of 1dm3A
- active site: C86 (= C88), H345 (= H349), C375 (= C379), G377 (= G381)
- binding acetyl coenzyme *a: C86 (= C88), L145 (= L148), H153 (= H156), M154 (= M157), R217 (= R221), S224 (= S228), M225 (≠ L229), A240 (= A244), S244 (= S248), M285 (= M289), A315 (= A319), F316 (= F320), H345 (= H349), C375 (= C379)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
57% identity, 99% coverage: 4:391/393 of query aligns to 2:387/389 of 1dlvA
- active site: C86 (= C88), H345 (= H349), C375 (= C379), G377 (= G381)
- binding coenzyme a: C86 (= C88), L145 (= L148), H153 (= H156), M154 (= M157), R217 (= R221), L228 (= L232), A240 (= A244), S244 (= S248), H345 (= H349)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
57% identity, 99% coverage: 4:391/393 of query aligns to 4:389/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
57% identity, 99% coverage: 4:391/393 of query aligns to 5:390/392 of 1ou6A
- active site: C89 (= C88), H348 (= H349), C378 (= C379), G380 (= G381)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L148), H156 (= H156), M157 (= M157), F235 (= F236), A243 (= A244), S247 (= S248), A318 (= A319), F319 (= F320), H348 (= H349)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
57% identity, 99% coverage: 4:391/393 of query aligns to 2:387/389 of 2wkuA
- active site: C86 (= C88), H345 (= H349), C375 (= C379), G377 (= G381)
- binding D-mannose: S6 (≠ A8), A7 (= A9), R38 (≠ Q40), K182 (= K185), D194 (≠ E197), V280 (= V284), D281 (= D285), T287 (≠ I291), P331 (≠ L335), S332 (≠ D336), V334 (= V338), V336 (= V340), F360 (≠ H364)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
57% identity, 98% coverage: 5:391/393 of query aligns to 6:390/392 of P07097
- Q64 (= Q63) mutation to A: Slightly lower activity.
- C89 (= C88) mutation to A: Loss of activity.
- C378 (= C379) mutation to G: Loss of activity.
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
57% identity, 99% coverage: 4:391/393 of query aligns to 3:388/390 of 1m1oA