SitesBLAST
Comparing 16925 FitnessBrowser__Keio:16925 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)
57% identity, 99% coverage: 1:391/393 of query aligns to 1:391/392 of P45359
- V77 (≠ N77) 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 (≠ AS 279:280) binding acetate
- A286 (= A286) 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 (= C378) modified: Disulfide link with 88, In inhibited form
- A386 (= A386) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
57% identity, 99% coverage: 1:391/393 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C88), H348 (= H348), S378 (≠ C378), G380 (= G380)
- binding coenzyme a: L148 (= L148), H156 (= H156), R220 (= R220), L231 (= L231), A243 (= A243), S247 (= S247), F319 (= F319), H348 (= H348)
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)
60% identity, 99% coverage: 1:391/393 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 (≠ Q218) 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 (= S247) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H348) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C378) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
59% identity, 99% coverage: 1:391/393 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C88), H349 (= H348), C379 (= C378), G381 (= G380)
- binding coenzyme a: S88 (≠ C88), L148 (= L148), R221 (= R220), F236 (= F235), A244 (= A243), S248 (= S247), L250 (≠ I249), A319 (= A318), F320 (= F319), H349 (= H348)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
58% identity, 99% coverage: 1:391/393 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C88), A348 (= A345), A378 (= A375), L380 (= L377)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C88), L151 (= L148), A246 (= A243), S250 (= S247), I252 (= I249), A321 (= A318), F322 (= F319), H351 (= H348)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
55% identity, 98% coverage: 4:390/393 of query aligns to 5:390/392 of 1ou6A
- active site: C89 (= C88), H348 (= H348), C378 (= C378), G380 (= G380)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L148), H156 (= H156), M157 (≠ I157), F235 (= F235), A243 (= A243), S247 (= S247), A318 (= A318), F319 (= F319), H348 (= H348)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
58% identity, 99% coverage: 1:391/393 of query aligns to 1:390/391 of 5f38B
- active site: C88 (= C88), H347 (= H348), C377 (= C378), G379 (= G380)
- binding coenzyme a: C88 (= C88), L149 (= L148), K219 (≠ R220), F234 (= F235), A242 (= A243), S246 (= S247), A317 (= A318), F318 (= F319), H347 (= H348)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
55% identity, 98% coverage: 4:390/393 of query aligns to 2:387/389 of 2vu2A
- active site: C86 (= C88), H345 (= H348), C375 (= C378), G377 (= G380)
- 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 (≠ I157), F232 (= F235), S244 (= S247), G245 (≠ S248), F316 (= F319), H345 (= H348)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
55% identity, 98% coverage: 4:390/393 of query aligns to 2:387/389 of 1dm3A
- active site: C86 (= C88), H345 (= H348), C375 (= C378), G377 (= G380)
- binding acetyl coenzyme *a: C86 (= C88), L145 (= L148), H153 (= H156), M154 (≠ I157), R217 (= R220), S224 (≠ G227), M225 (≠ L228), A240 (= A243), S244 (= S247), M285 (= M288), A315 (= A318), F316 (= F319), H345 (= H348), C375 (= C378)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
55% identity, 98% coverage: 4:390/393 of query aligns to 2:387/389 of 1dlvA
- active site: C86 (= C88), H345 (= H348), C375 (= C378), G377 (= G380)
- binding coenzyme a: C86 (= C88), L145 (= L148), H153 (= H156), M154 (≠ I157), R217 (= R220), L228 (= L231), A240 (= A243), S244 (= S247), H345 (= H348)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
55% identity, 98% coverage: 4:390/393 of query aligns to 4:389/391 of 2vu1A
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
55% identity, 98% coverage: 4:390/393 of query aligns to 2:387/389 of 2wkuA