SitesBLAST
Comparing PP_1377 FitnessBrowser__Putida:PP_1377 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)
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
100% identity, 100% coverage: 1:400/400 of query aligns to 4:403/403 of 6pccA
- active site: C93 (= C90), A359 (≠ H356), C389 (= C386), G391 (= G388)
- binding coenzyme a: C93 (= C90), I148 (= I145), M166 (= M163), R229 (= R226), T232 (= T229), L240 (= L237), A252 (= A249), G253 (= G250), S256 (= S253), G257 (= G254), V258 (= V255), N325 (= N322), A327 (= A324), F328 (= F325), L361 (= L358)
- binding hexanal: N61 (= N58), L92 (= L89), T146 (= T143), T147 (= T144), I148 (= I145), G149 (= G146), R151 (= R148), M166 (= M163), L361 (= L358), G391 (= G388)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
100% identity, 100% coverage: 1:400/400 of query aligns to 4:403/403 of 6pcbA
- active site: C93 (= C90), A359 (≠ H356), C389 (= C386), G391 (= G388)
- binding coenzyme a: C93 (= C90), I148 (= I145), M166 (= M163), R229 (= R226), T232 (= T229), L237 (= L234), L240 (= L237), A252 (= A249), G253 (= G250), S256 (= S253), G257 (= G254), V258 (= V255), N325 (= N322), A327 (= A324), F328 (= F325), L361 (= L358)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
99% identity, 100% coverage: 1:400/400 of query aligns to 5:401/401 of 6pcdA
- active site: S94 (≠ C90), A357 (≠ H356), C387 (= C386), G389 (= G388)
- binding coenzyme a: I149 (= I145), M167 (= M163), R227 (= R226), T230 (= T229), L238 (= L237), A250 (= A249), G251 (= G250), S254 (= S253), G255 (= G254), V256 (= V255), N323 (= N322), A325 (= A324), F326 (= F325), A357 (≠ H356), L359 (= L358)
- binding octanal: A61 (= A57), N62 (= N58), L93 (= L89), E122 (= E118), T147 (= T143), T148 (= T144), I149 (= I145), G150 (= G146), R152 (= R148), M167 (= M163), L359 (= L358), G389 (= G388)
P45359 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; CaTHL; EC 2.3.1.9 from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) (see paper)
44% identity, 100% coverage: 1:399/400 of query aligns to 1:391/392 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 (≠ G98) binding
- N153 (≠ M154) 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 (≠ AS 285:286) binding
- A286 (≠ R292) 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 (= C386) modified: Disulfide link with 88, In inhibited form
- A386 (= A394) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
44% identity, 100% coverage: 1:399/400 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C90), H348 (= H356), S378 (≠ C386), G380 (= G388)
- binding coenzyme a: L148 (≠ F149), H156 (≠ Q157), M157 (≠ Y158), R220 (= R226), L228 (= L234), L231 (= L237), F235 (≠ N241), A243 (= A249), G244 (= G250), S247 (= S253), G248 (= G254), L249 (≠ V255), A318 (= A324), F319 (= F325), H348 (= H356)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
45% identity, 99% coverage: 4:400/400 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C90), H345 (= H356), C375 (= C386), G377 (= G388)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: C86 (= C90), L145 (= L153), H153 (≠ S162), M154 (= M163), F232 (≠ N241), A240 (= A249), S244 (= S253), G245 (= G254), L246 (≠ V255), A315 (= A324), F316 (= F325), H345 (= H356)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
45% identity, 99% coverage: 4:400/400 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C90), H345 (= H356), C375 (= C386), G377 (= G388)
- binding acetyl coenzyme *a: C86 (= C90), L145 (= L153), H153 (≠ S162), M154 (= M163), R217 (= R226), S224 (≠ A233), M225 (≠ L234), L228 (= L237), F232 (≠ N241), A240 (= A249), G241 (= G250), A243 (= A252), S244 (= S253), G245 (= G254), L246 (≠ V255), M285 (= M294), A315 (= A324), F316 (= F325), H345 (= H356), C375 (= C386), I376 (≠ V387)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
45% identity, 99% coverage: 4:400/400 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C90), H345 (= H356), C375 (= C386), G377 (= G388)
- binding coenzyme a: C86 (= C90), L145 (= L153), H153 (≠ S162), M154 (= M163), R217 (= R226), S224 (≠ A233), M225 (≠ L234), L228 (= L237), F232 (≠ N241), A240 (= A249), G241 (= G250), S244 (= S253), G245 (= G254), L246 (≠ V255), F316 (= F325), H345 (= H356)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
45% identity, 99% coverage: 4:400/400 of query aligns to 5:392/392 of 1ou6A
- active site: C89 (= C90), H348 (= H356), C378 (= C386), G380 (= G388)
- binding pantothenyl-aminoethanol-acetate pivalic acid: I144 (= I145), L148 (= L153), H156 (≠ S162), M157 (= M163), A234 (≠ V240), F235 (≠ N241), A243 (= A249), S247 (= S253), G248 (= G254), L249 (≠ V255), A318 (= A324), F319 (= F325), H348 (= H356)
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)
47% identity, 100% coverage: 1:399/400 of query aligns to 1:392/393 of P14611
- C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ S162) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ H224) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R226) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S253) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H356) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C386) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
45% identity, 99% coverage: 4:400/400 of query aligns to 4:391/391 of 2vu1A