SitesBLAST
Comparing WP_101589711.1 NCBI__GCF_900169175.1:WP_101589711.1 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)
A0R1Y7 Probable acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; EC 2.3.1.9 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
63% identity, 98% coverage: 5:393/398 of query aligns to 1:386/388 of A0R1Y7
- K187 (≠ D195) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
48% identity, 99% coverage: 1:393/398 of query aligns to 1:389/392 of P45359
- V77 (≠ M77) 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 (≠ T96) binding acetate
- N153 (≠ T153) 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.
- G-S 279:280 (≠ AWT 283:285) binding acetate
- A286 (≠ S291) 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 (= C382) modified: Disulfide link with 88, In inhibited form
- A386 (= A390) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
48% identity, 99% coverage: 1:393/398 of query aligns to 1:389/392 of 4xl4A
- active site: C88 (= C88), H348 (= H352), S378 (≠ C382), G380 (= G384)
- binding coenzyme a: L148 (= L148), H156 (≠ A156), R220 (= R224), L231 (= L235), A243 (= A247), S247 (= S251), F319 (= F323), H348 (= H352)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
48% identity, 99% coverage: 2:395/398 of query aligns to 1:391/394 of 7cw5B
- active site: C87 (= C88), H348 (= H352), C378 (= C382), G380 (= G384)
- binding coenzyme a: L147 (= L148), H155 (≠ A156), M156 (= M157), R220 (= R224), T223 (≠ S227), A243 (= A247), P247 (≠ S251), L249 (≠ I253), H348 (= H352)
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)
51% identity, 99% coverage: 1:393/398 of query aligns to 1:390/393 of P14611
- C88 (= C88) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ A156) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ G222) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R224) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S251) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H352) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C382) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
51% identity, 99% coverage: 1:393/398 of query aligns to 1:390/393 of 4o9cC
- active site: S88 (≠ C88), H349 (= H352), C379 (= C382), G381 (= G384)
- binding coenzyme a: S88 (≠ C88), L148 (= L148), R221 (= R224), F236 (= F239), A244 (= A247), S248 (= S251), L250 (≠ I253), A319 (= A322), F320 (= F323), H349 (= H352)
8gqnA X-ray structure of thiolase with coa
49% identity, 99% coverage: 2:395/398 of query aligns to 1:389/390 of 8gqnA
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
47% identity, 98% coverage: 2:393/398 of query aligns to 3:389/392 of P07097
- Q64 (= Q63) mutation to A: Slightly lower activity.
- C89 (= C88) mutation to A: Loss of activity.
- C378 (= C382) mutation to G: Loss of activity.
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
47% identity, 98% coverage: 5:393/398 of query aligns to 3:386/389 of 2vu2A
- active site: C86 (= C88), H345 (= H352), C375 (= C382), G377 (= G384)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ A156), M154 (= M157), F232 (= F239), S244 (= S251), G245 (≠ Q252), F316 (= F323), H345 (= H352)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
47% identity, 98% coverage: 5:393/398 of query aligns to 3:386/389 of 1dm3A
- active site: C86 (= C88), H345 (= H352), C375 (= C382), G377 (= G384)
- binding acetyl coenzyme *a: C86 (= C88), L145 (= L148), H153 (≠ A156), M154 (= M157), R217 (= R224), S224 (= S231), M225 (= M232), A240 (= A247), S244 (= S251), M285 (≠ Q293), A315 (= A322), F316 (= F323), H345 (= H352), C375 (= C382)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
47% identity, 98% coverage: 5:393/398 of query aligns to 3:386/389 of 1dlvA
- active site: C86 (= C88), H345 (= H352), C375 (= C382), G377 (= G384)
- binding coenzyme a: C86 (= C88), L145 (= L148), H153 (≠ A156), M154 (= M157), R217 (= R224), L228 (= L235), A240 (= A247), S244 (= S251), H345 (= H352)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
47% identity, 98% coverage: 5:393/398 of query aligns to 6:389/392 of 1ou6A