SitesBLAST
Comparing WP_050654572.1 NCBI__GCF_002893965.1:WP_050654572.1 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)
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
66% identity, 99% coverage: 3:402/403 of query aligns to 2:398/400 of 5bz4K
- active site: C87 (= C88), H354 (= H358), C384 (= C388), G386 (= G390)
- binding coenzyme a: C87 (= C88), R146 (= R147), M160 (= M161), R220 (= R225), A246 (= A251), G247 (= G252), S250 (= S255), Q252 (= Q257), M291 (= M296), A321 (= A326), F322 (= F327), H354 (= H358)
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)
44% identity, 100% coverage: 1:401/403 of query aligns to 1:391/392 of P45359
- V77 (≠ I77) 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 (≠ I96) binding acetate
- N153 (≠ V157) 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 (≠ SV 287:288) binding acetate
- A286 (≠ R294) 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 (= C388) modified: Disulfide link with 88, In inhibited form
- A386 (= A396) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
43% identity, 100% coverage: 1:401/403 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C88), H348 (= H358), S378 (≠ C388), G380 (= G390)
- binding coenzyme a: L148 (≠ G152), H156 (≠ G160), R220 (= R225), L231 (= L236), A243 (= A251), S247 (= S255), F319 (= F327), H348 (= H358)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
44% identity, 100% coverage: 2:402/403 of query aligns to 3:392/392 of 1ou6A
- active site: C89 (= C88), H348 (= H358), C378 (= C388), G380 (= G390)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ V148), H156 (≠ P156), M157 (= M161), F235 (≠ I243), A243 (= A251), S247 (= S255), A318 (= A326), F319 (= F327), H348 (= H358)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
44% identity, 100% coverage: 2:402/403 of query aligns to 2:391/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
44% identity, 99% coverage: 4:402/403 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C88), H345 (= H358), C375 (= C388), G377 (= G390)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ P156), M154 (= M161), F232 (≠ I243), S244 (= S255), G245 (= G256), F316 (= F327), H345 (= H358)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
44% identity, 99% coverage: 4:402/403 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C88), H345 (= H358), C375 (= C388), G377 (= G390)
- binding acetyl coenzyme *a: C86 (= C88), L145 (≠ V148), H153 (≠ P156), M154 (= M161), R217 (= R225), S224 (= S232), M225 (≠ L233), A240 (= A251), S244 (= S255), M285 (= M296), A315 (= A326), F316 (= F327), H345 (= H358), C375 (= C388)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
44% identity, 99% coverage: 4:402/403 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C88), H345 (= H358), C375 (= C388), G377 (= G390)
- binding coenzyme a: C86 (= C88), L145 (≠ V148), H153 (≠ P156), M154 (= M161), R217 (= R225), L228 (= L236), A240 (= A251), S244 (= S255), H345 (= H358)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
44% identity, 100% coverage: 2:402/403 of query aligns to 1:390/390 of 1m1oA
- active site: A87 (≠ C88), H346 (= H358), C376 (= C388), G378 (= G390)
- binding acetoacetyl-coenzyme a: L86 (≠ R87), A87 (≠ C88), L146 (≠ V148), H154 (≠ P156), M155 (= M161), R218 (= R225), S225 (= S232), M226 (≠ L233), A241 (= A251), G242 (= G252), S245 (= S255), A316 (= A326), F317 (= F327), H346 (= H358), I377 (= I389), G378 (= G390)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
44% identity, 99% coverage: 4:402/403 of query aligns to 2:389/389 of 2wkuA
- active site: C86 (= C88), H345 (= H358), C375 (= C388), G377 (= G390)
- binding D-mannose: S6 (≠ E8), A7 (≠ P9), R38 (= R40), K182 (≠ R189), D194 (≠ E201), V280 (= V291), D281 (≠ P292), T287 (≠ I298), P331 (≠ D344), S332 (≠ P345), V334 (≠ I347), V336 (≠ P349), F360 (≠ R373)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
44% identity, 100% coverage: 2:402/403 of query aligns to 4:392/392 of P07097
- Q64 (≠ P63) mutation to A: Slightly lower activity.
- C89 (= C88) mutation to A: Loss of activity.
- C378 (= C388) 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)
45% identity, 100% coverage: 1:401/403 of query aligns to 1:392/393 of P14611