SitesBLAST
Comparing PP_3280 FitnessBrowser__Putida:PP_3280 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)
68% identity, 98% coverage: 8:406/406 of query aligns to 6:403/403 of 6pccA
- active site: C93 (= C95), A359 (≠ H362), C389 (= C392), G391 (= G394)
- binding coenzyme a: C93 (= C95), I148 (= I150), R229 (= R232), T232 (= T235), A252 (= A255), S256 (= S259), N325 (= N328), F328 (= F331)
- binding hexanal: N61 (= N63), T146 (= T148), I148 (= I150), G149 (= G151), R151 (= R153), L361 (= L364)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
68% identity, 98% coverage: 8:406/406 of query aligns to 6:403/403 of 6pcbA
- active site: C93 (= C95), A359 (≠ H362), C389 (= C392), G391 (= G394)
- binding coenzyme a: C93 (= C95), I148 (= I150), R229 (= R232), A252 (= A255), S256 (= S259), G257 (= G260), N325 (= N328), F328 (= F331)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
67% identity, 98% coverage: 8:406/406 of query aligns to 7:401/401 of 6pcdA
- active site: S94 (≠ C95), A357 (≠ H362), C387 (= C392), G389 (= G394)
- binding coenzyme a: I149 (= I150), M167 (= M168), R227 (= R232), T230 (= T235), A250 (= A255), S254 (= S259), G255 (= G260), A325 (= A330), A357 (≠ H362)
- binding octanal: N62 (= N63), T147 (= T148), T148 (= T149), I149 (= I150), G150 (= G151), R152 (= R153), L359 (= L364)
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, 98% coverage: 8:405/406 of query aligns to 3:391/392 of P45359
- V77 (≠ L84) 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 (≠ G103) binding acetate
- N153 (≠ G164) 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 291:292) binding acetate
- A286 (≠ R298) 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 (= C392) modified: Disulfide link with 88, In inhibited form
- A386 (= A400) binding acetate
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
48% identity, 98% coverage: 8:405/406 of query aligns to 5:394/394 of 5f38D
- active site: C90 (= C95), A348 (= A359), A378 (≠ C389), L380 (≠ M391)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C95), L151 (= L158), A246 (= A255), S250 (= S259), I252 (≠ V261), A321 (= A330), F322 (= F331), H351 (= H362)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
47% identity, 98% coverage: 8:406/406 of query aligns to 3:391/391 of 5f38B
- active site: C88 (= C95), H347 (= H362), C377 (= C392), G379 (= G394)
- binding coenzyme a: C88 (= C95), L149 (= L158), K219 (≠ R232), F234 (= F247), A242 (= A255), S246 (= S259), A317 (= A330), F318 (= F331), H347 (= H362)
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
43% identity, 98% coverage: 8:405/406 of query aligns to 3:391/392 of 4xl4A
- active site: C88 (= C95), H348 (= H362), S378 (≠ C392), G380 (= G394)
- binding coenzyme a: L148 (vs. gap), H156 (≠ S167), R220 (= R232), L231 (= L243), A243 (= A255), S247 (= S259), F319 (= F331), H348 (= H362)
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
42% identity, 98% coverage: 8:406/406 of query aligns to 6:390/390 of 2d3tC
- active site: C94 (= C95), H346 (= H362), C376 (= C392), G378 (= G394)
- binding acetyl coenzyme *a: C94 (= C95), R214 (= R232), L222 (= L240), L225 (= L243), A238 (= A255), G239 (= G256), S242 (= S259), I244 (≠ V261), A313 (= A330), F314 (= F331), H346 (= H362), C376 (= C392)
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)
45% identity, 98% coverage: 8:405/406 of query aligns to 3:392/393 of P14611
- C88 (= C95) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ S167) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ H230) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R232) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S259) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H362) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C392) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
44% identity, 98% coverage: 9:406/406 of query aligns to 5:392/392 of P07097
- Q64 (≠ R70) mutation to A: Slightly lower activity.
- C89 (= C95) mutation to A: Loss of activity.
- C378 (= C392) mutation to G: Loss of activity.
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
45% identity, 98% coverage: 10:406/406 of query aligns to 6:392/392 of 1ou6A
- active site: C89 (= C95), H348 (= H362), C378 (= C392), G380 (= G394)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L158), H156 (≠ S167), M157 (= M168), F235 (= F247), A243 (= A255), S247 (= S259), A318 (= A330), F319 (= F331), H348 (= H362)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
45% identity, 98% coverage: 10:406/406 of query aligns to 3:389/389 of 2vu2A