SitesBLAST
Comparing H281DRAFT_05559 FitnessBrowser__Burk376:H281DRAFT_05559 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
49% identity, 99% coverage: 3:394/394 of query aligns to 2:392/392 of P45359
- V77 (≠ E79) 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 (= C90) modified: Disulfide link with 378, In inhibited form
- S96 (≠ I98) binding acetate
- N153 (≠ H154) 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 (≠ AH 281:282) binding acetate
- A286 (≠ K288) 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 (= C380) modified: Disulfide link with 88, In inhibited form
- A386 (= A388) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
49% identity, 99% coverage: 3:394/394 of query aligns to 2:392/392 of 4xl4A
- active site: C88 (= C90), H348 (= H350), S378 (≠ C380), G380 (= G382)
- binding coenzyme a: L148 (= L149), H156 (= H157), R220 (= R221), L231 (= L232), A243 (= A245), S247 (= S249), F319 (= F321), H348 (= H350)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
48% identity, 99% coverage: 1:392/394 of query aligns to 1:390/392 of P07097
- Q64 (≠ M65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C380) mutation to G: Loss of activity.
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
48% identity, 98% coverage: 5:392/394 of query aligns to 5:390/392 of 1ou6A
- active site: C89 (= C90), H348 (= H350), C378 (= C380), G380 (= G382)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L149), H156 (= H157), M157 (= M158), F235 (= F236), A243 (= A245), S247 (= S249), A318 (= A320), F319 (= F321), H348 (= H350)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
48% identity, 98% coverage: 5:392/394 of query aligns to 4:389/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
48% identity, 98% coverage: 5:392/394 of query aligns to 2:387/389 of 2vu2A
- active site: C86 (= C90), H345 (= H350), C375 (= C380), G377 (= G382)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (= H157), M154 (= M158), F232 (= F236), S244 (= S249), G245 (= G250), F316 (= F321), H345 (= H350)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
48% identity, 98% coverage: 5:392/394 of query aligns to 2:387/389 of 1dm3A
- active site: C86 (= C90), H345 (= H350), C375 (= C380), G377 (= G382)
- binding acetyl coenzyme *a: C86 (= C90), L145 (= L149), H153 (= H157), M154 (= M158), R217 (= R221), S224 (≠ D228), M225 (≠ F229), A240 (= A245), S244 (= S249), M285 (= M290), A315 (= A320), F316 (= F321), H345 (= H350), C375 (= C380)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
48% identity, 98% coverage: 5:392/394 of query aligns to 2:387/389 of 1dlvA
- active site: C86 (= C90), H345 (= H350), C375 (= C380), G377 (= G382)
- binding coenzyme a: C86 (= C90), L145 (= L149), H153 (= H157), M154 (= M158), R217 (= R221), L228 (= L232), A240 (= A245), S244 (= S249), H345 (= H350)
P42765 3-ketoacyl-CoA thiolase, mitochondrial; Acetyl-CoA acetyltransferase; Acetyl-CoA acyltransferase; Acyl-CoA hydrolase, mitochondrial; Beta-ketothiolase; Mitochondrial 3-oxoacyl-CoA thiolase; T1; EC 2.3.1.16; EC 2.3.1.9; EC 3.1.2.-; EC 3.1.2.1; EC 3.1.2.2 from Homo sapiens (Human) (see paper)
47% identity, 99% coverage: 1:392/394 of query aligns to 3:394/397 of P42765
- C92 (= C90) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R221) binding CoA
- T227 (≠ A224) binding CoA
- S251 (= S249) binding CoA
- C382 (= C380) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
48% identity, 98% coverage: 5:392/394 of query aligns to 2:387/389 of 2wkuA
- active site: C86 (= C90), H345 (= H350), C375 (= C380), G377 (= G382)
- binding D-mannose: S6 (= S9), A7 (≠ G10), R38 (= R41), K182 (≠ R186), D194 (≠ E198), V280 (= V285), D281 (= D286), T287 (≠ I292), P331 (= P336), S332 (≠ H337), V334 (= V339), V336 (≠ P341), F360 (≠ Y365)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
48% identity, 98% coverage: 5:392/394 of query aligns to 3:388/390 of 1m1oA
- active site: A87 (≠ C90), H346 (= H350), C376 (= C380), G378 (= G382)
- binding acetoacetyl-coenzyme a: L86 (= L89), A87 (≠ C90), L146 (= L149), H154 (= H157), M155 (= M158), R218 (= R221), S225 (≠ D228), M226 (≠ F229), A241 (= A245), G242 (= G246), S245 (= S249), A316 (= A320), F317 (= F321), H346 (= H350), I377 (= I381), G378 (= G382)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
46% identity, 99% coverage: 1:392/394 of query aligns to 6:393/395 of 4c2jD