SitesBLAST
Comparing WP_085770214.1 NCBI__GCF_002117405.1:WP_085770214.1 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)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
74% identity, 99% coverage: 2:390/391 of query aligns to 2:390/392 of 1ou6A
- active site: C89 (= C89), H348 (= H348), C378 (= C378), G380 (= G380)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L148), H156 (= H156), M157 (= M157), F235 (= F235), A243 (= A243), S247 (= S247), A318 (= A318), F319 (= F319), H348 (= H348)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
74% identity, 99% coverage: 2:390/391 of query aligns to 1:389/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
74% identity, 99% coverage: 5:390/391 of query aligns to 2:387/389 of 2vu2A
- active site: C86 (= C89), 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 (= M157), F232 (= F235), S244 (= S247), G245 (= G248), F316 (= F319), H345 (= H348)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
74% identity, 99% coverage: 5:390/391 of query aligns to 2:387/389 of 1dm3A
- active site: C86 (= C89), H345 (= H348), C375 (= C378), G377 (= G380)
- binding acetyl coenzyme *a: C86 (= C89), L145 (= L148), H153 (= H156), M154 (= M157), R217 (≠ K220), S224 (= S227), M225 (≠ V228), 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)
74% identity, 99% coverage: 5:390/391 of query aligns to 2:387/389 of 1dlvA
- active site: C86 (= C89), H345 (= H348), C375 (= C378), G377 (= G380)
- binding coenzyme a: C86 (= C89), L145 (= L148), H153 (= H156), M154 (= M157), R217 (≠ K220), L228 (= L231), A240 (= A243), S244 (= S247), H345 (= H348)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
74% identity, 99% coverage: 5:390/391 of query aligns to 2:387/389 of 2wkuA
- active site: C86 (= C89), H345 (= H348), C375 (= C378), G377 (= G380)
- binding D-mannose: S6 (= S9), A7 (= A10), R38 (= R41), K182 (= K185), D194 (= D197), V280 (= V283), D281 (= D284), T287 (≠ S290), P331 (= P334), S332 (≠ A335), V334 (= V337), V336 (= V339), F360 (≠ Y363)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
74% identity, 99% coverage: 5:390/391 of query aligns to 3:388/390 of 1m1oA
- active site: A87 (≠ C89), H346 (= H348), C376 (= C378), G378 (= G380)
- binding acetoacetyl-coenzyme a: L86 (≠ V88), A87 (≠ C89), L146 (= L148), H154 (= H156), M155 (= M157), R218 (≠ K220), S225 (= S227), M226 (≠ V228), A241 (= A243), G242 (≠ A244), S245 (= S247), A316 (= A318), F317 (= F319), H346 (= H348), I377 (= I379), G378 (= G380)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
72% identity, 100% coverage: 1:390/391 of query aligns to 1:390/392 of P07097
- Q64 (= Q64) mutation to A: Slightly lower activity.
- C89 (= C89) mutation to A: Loss of activity.
- C378 (= C378) mutation to G: Loss of activity.
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)
66% identity, 99% coverage: 3:391/391 of query aligns to 2:392/393 of P14611
- C88 (= C89) 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 (≠ Y218) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ K220) 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)
66% identity, 99% coverage: 3:391/391 of query aligns to 2:392/393 of 4o9cC
- active site: S88 (≠ C89), H349 (= H348), C379 (= C378), G381 (= G380)
- binding coenzyme a: S88 (≠ C89), L148 (= L148), R221 (≠ K220), F236 (= F235), A244 (= A243), S248 (= S247), L250 (= L249), A319 (= A318), F320 (= F319), H349 (= H348)
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)
60% identity, 99% coverage: 4:391/391 of query aligns to 3:391/392 of P45359
- V77 (≠ D78) 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 (= C89) modified: Disulfide link with 378, In inhibited form
- S96 (≠ A97) 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 (≠ AT 279:280) binding acetate
- A286 (≠ S286) 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
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
58% identity, 99% coverage: 5:391/391 of query aligns to 5:393/394 of 1wl4A