SitesBLAST
Comparing WP_101588980.1 NCBI__GCF_900169175.1:WP_101588980.1 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)
64% identity, 98% coverage: 10:412/413 of query aligns to 2:399/400 of 5bz4K
- active site: C87 (= C95), H354 (= H367), C384 (= C397), G386 (= G399)
- binding coenzyme a: C87 (= C95), R146 (= R154), M160 (= M168), R220 (= R233), A246 (= A259), G247 (= G260), S250 (= S263), Q252 (= Q265), M291 (= M304), A321 (= A334), F322 (= F335), H354 (= H367)
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)
43% identity, 97% coverage: 10:410/413 of query aligns to 3:391/392 of P45359
- V77 (= V84) 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 (= C95) modified: Disulfide link with 378, In inhibited form
- S96 (≠ L103) binding acetate
- N153 (≠ K160) 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 (≠ GV 295:296) binding acetate
- A286 (≠ R302) 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 (= C397) modified: Disulfide link with 88, In inhibited form
- A386 (= A405) binding acetate
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
44% identity, 97% coverage: 11:411/413 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C95), H345 (= H367), C375 (= C397), G377 (= G399)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ P163), M154 (= M168), F232 (≠ L251), S244 (= S263), G245 (= G264), F316 (= F335), H345 (= H367)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
44% identity, 97% coverage: 11:411/413 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C95), H345 (= H367), C375 (= C397), G377 (= G399)
- binding acetyl coenzyme *a: C86 (= C95), L145 (= L155), H153 (≠ P163), M154 (= M168), R217 (= R233), S224 (= S240), M225 (≠ L241), A240 (= A259), S244 (= S263), M285 (= M304), A315 (= A334), F316 (= F335), H345 (= H367), C375 (= C397)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
44% identity, 97% coverage: 11:411/413 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C95), H345 (= H367), C375 (= C397), G377 (= G399)
- binding coenzyme a: C86 (= C95), L145 (= L155), H153 (≠ P163), M154 (= M168), R217 (= R233), L228 (= L244), A240 (= A259), S244 (= S263), H345 (= H367)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
44% identity, 98% coverage: 7:411/413 of query aligns to 1:392/392 of 1ou6A
- active site: C89 (= C95), H348 (= H367), C378 (= C397), G380 (= G399)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L155), H156 (≠ P163), M157 (= M168), F235 (≠ L251), A243 (= A259), S247 (= S263), A318 (= A334), F319 (= F335), H348 (= H367)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
44% identity, 97% coverage: 11:411/413 of query aligns to 4:391/391 of 2vu1A
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
42% identity, 97% coverage: 10:410/413 of query aligns to 3:391/392 of 4xl4A
- active site: C88 (= C95), H348 (= H367), S378 (≠ C397), G380 (= G399)
- binding coenzyme a: L148 (= L155), H156 (≠ P163), R220 (= R233), L231 (= L244), A243 (= A259), S247 (= S263), F319 (= F335), H348 (= H367)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
44% identity, 97% coverage: 11:411/413 of query aligns to 2:389/389 of 2wkuA
- active site: C86 (= C95), H345 (= H367), C375 (= C397), G377 (= G399)
- binding D-mannose: S6 (≠ E15), A7 (≠ P16), R38 (≠ K47), K182 (≠ R196), D194 (≠ E208), V280 (= V299), D281 (≠ P300), T287 (≠ I306), P331 (≠ F353), S332 (≠ E354), V334 (≠ T356), V336 (= V358), F360 (≠ R382)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
44% identity, 97% coverage: 11:411/413 of query aligns to 3:390/390 of 1m1oA
- active site: A87 (≠ C95), H346 (= H367), C376 (= C397), G378 (= G399)
- binding acetoacetyl-coenzyme a: L86 (≠ R94), A87 (≠ C95), L146 (= L155), H154 (≠ P163), M155 (= M168), R218 (= R233), S225 (= S240), M226 (≠ L241), A241 (= A259), G242 (= G260), S245 (= S263), A316 (= A334), F317 (= F335), H346 (= H367), I377 (= I398), G378 (= G399)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
44% identity, 97% coverage: 12:411/413 of query aligns to 6:392/392 of P07097
- Q64 (≠ P70) mutation to A: Slightly lower activity.
- C89 (= C95) mutation to A: Loss of activity.
- C378 (= C397) mutation to G: Loss of activity.
8jg2A Crystal structure of a biosynthetic thiolase from megasphaera hexanoica soaked with hexanoyl-coa
44% identity, 96% coverage: 9:405/413 of query aligns to 3:386/393 of 8jg2A