SitesBLAST
Comparing WP_110206770.1 NCBI__GCF_003194585.1:WP_110206770.1 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)
62% identity, 99% coverage: 7:408/408 of query aligns to 2:399/400 of 5bz4K
- active site: C87 (= C92), H354 (= H363), C384 (= C393), G386 (= G395)
- binding coenzyme a: C87 (= C92), R146 (= R151), M160 (= M165), R220 (= R230), A246 (= A256), G247 (= G257), S250 (= S260), Q252 (= Q262), M291 (= M301), A321 (= A331), F322 (= F332), H354 (= H363)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
46% identity, 98% coverage: 7:407/408 of query aligns to 1:389/389 of 2vu2A
- active site: C86 (= C92), H345 (= H363), C375 (= C393), G377 (= G395)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ P160), M154 (= M165), F232 (≠ V248), S244 (= S260), G245 (= G261), F316 (= F332), H345 (= H363)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
46% identity, 98% coverage: 7:407/408 of query aligns to 1:389/389 of 1dm3A
- active site: C86 (= C92), H345 (= H363), C375 (= C393), G377 (= G395)
- binding acetyl coenzyme *a: C86 (= C92), L145 (≠ V152), H153 (≠ P160), M154 (= M165), R217 (= R230), S224 (≠ A237), M225 (≠ L238), A240 (= A256), S244 (= S260), M285 (= M301), A315 (= A331), F316 (= F332), H345 (= H363), C375 (= C393)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
46% identity, 98% coverage: 7:407/408 of query aligns to 1:389/389 of 1dlvA
- active site: C86 (= C92), H345 (= H363), C375 (= C393), G377 (= G395)
- binding coenzyme a: C86 (= C92), L145 (≠ V152), H153 (≠ P160), M154 (= M165), R217 (= R230), L228 (= L241), A240 (= A256), S244 (= S260), H345 (= H363)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
46% identity, 98% coverage: 7:407/408 of query aligns to 3:391/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
46% identity, 98% coverage: 7:407/408 of query aligns to 4:392/392 of 1ou6A
- active site: C89 (= C92), H348 (= H363), C378 (= C393), G380 (= G395)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ V152), H156 (≠ P160), M157 (= M165), F235 (≠ V248), A243 (= A256), S247 (= S260), A318 (= A331), F319 (= F332), H348 (= H363)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
45% identity, 98% coverage: 7:407/408 of query aligns to 1:389/389 of 2wkuA
- active site: C86 (= C92), H345 (= H363), C375 (= C393), G377 (= G395)
- binding D-mannose: S6 (≠ E12), A7 (≠ P13), R38 (= R44), K182 (≠ R193), D194 (= D205), V280 (= V296), D281 (≠ P297), T287 (≠ I303), P331 (≠ D349), S332 (≠ A350), V334 (= V352), V336 (= V354), F360 (≠ R378)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
45% identity, 98% coverage: 7:407/408 of query aligns to 2:390/390 of 1m1oA
- active site: A87 (≠ C92), H346 (= H363), C376 (= C393), G378 (= G395)
- binding acetoacetyl-coenzyme a: L86 (≠ R91), A87 (≠ C92), L146 (≠ V152), H154 (≠ P160), M155 (= M165), R218 (= R230), S225 (≠ A237), M226 (≠ L238), A241 (= A256), G242 (= G257), S245 (= S260), A316 (= A331), F317 (= F332), H346 (= H363), I377 (= I394), G378 (= G395)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
45% identity, 99% coverage: 5:407/408 of query aligns to 2:392/392 of P07097
- Q64 (≠ P67) mutation to A: Slightly lower activity.
- C89 (= C92) mutation to A: Loss of activity.
- C378 (= C393) mutation to G: Loss of activity.
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, 98% coverage: 7:405/408 of query aligns to 3:390/392 of P45359
- V77 (= V81) 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 (= C92) modified: Disulfide link with 378, In inhibited form
- S96 (≠ L100) binding acetate
- N153 (≠ V161) 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 (≠ AV 292:293) binding acetate
- A286 (= A299) 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 (= C393) modified: Disulfide link with 88, In inhibited form
- A386 (= A401) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
43% identity, 98% coverage: 7:405/408 of query aligns to 3:390/392 of 4xl4A
- active site: C88 (= C92), H348 (= H363), S378 (≠ C393), G380 (= G395)
- binding coenzyme a: L148 (≠ G156), H156 (≠ G164), R220 (= R230), L231 (= L241), A243 (= A256), S247 (= S260), F319 (= F332), H348 (= H363)
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)
44% identity, 98% coverage: 6:405/408 of query aligns to 2:391/393 of P14611