SitesBLAST
Comparing H281DRAFT_01504 FitnessBrowser__Burk376:H281DRAFT_01504 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)
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
71% 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), R229 (= R227), T232 (= T229), A252 (= A249), S256 (= S253), N325 (= N322), F328 (= F325)
- binding hexanal: N61 (= N58), T146 (= T143), I148 (= I145), G149 (= G146), R151 (= R148), L361 (= L358)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
71% 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), R229 (= R227), A252 (= A249), S256 (= S253), G257 (= G254), N325 (= N322), F328 (= F325)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
70% 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 (= R227), T230 (= T229), A250 (= A249), S254 (= S253), G255 (= G254), A325 (= A324), A357 (≠ H356)
- binding octanal: N62 (= N58), T147 (= T143), T148 (= T144), I149 (= I145), G150 (= G146), R152 (= R148), L359 (= L358)
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, 100% coverage: 1:399/400 of query aligns to 1:391/392 of P45359
- V77 (≠ K79) 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 acetate
- N153 (= N151) 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 (≠ AT 285:286) binding acetate
- 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 acetate
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, 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 (≠ H225) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R227) 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.
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
43% 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 (≠ M157), R220 (= R227), L231 (= L237), A243 (= A249), S247 (= S253), F319 (= F325), H348 (= H356)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
44% identity, 100% coverage: 1:399/400 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H356), C379 (= C386), G381 (= G388)
- binding coenzyme a: S88 (≠ C90), L148 (= L153), R221 (= R227), F236 (≠ V241), A244 (= A249), S248 (= S253), L250 (≠ V255), A319 (= A324), F320 (= F325), H349 (= H356)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
47% identity, 100% coverage: 1:399/400 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C90), A348 (= A353), A378 (≠ C383), L380 (≠ M385)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C90), L151 (= L153), A246 (= A249), S250 (= S253), I252 (≠ V255), A321 (= A324), F322 (= F325), H351 (= H356)
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
43% identity, 100% coverage: 3:400/400 of query aligns to 2:398/400 of 5bz4K
- active site: C87 (= C90), H354 (= H356), C384 (= C386), G386 (= G388)
- binding coenzyme a: C87 (= C90), R146 (vs. gap), M160 (= M157), R220 (= R227), A246 (= A249), G247 (= G250), S250 (= S253), Q252 (≠ V255), M291 (= M294), A321 (= A324), F322 (= F325), H354 (= H356)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
47% identity, 100% coverage: 1:400/400 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C90), H347 (= H356), C377 (= C386), G379 (= G388)
- binding coenzyme a: C88 (= C90), L149 (= L153), K219 (≠ R227), F234 (≠ V241), A242 (= A249), S246 (= S253), A317 (= A324), F318 (= F325), H347 (= H356)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
43% identity, 100% coverage: 2:400/400 of query aligns to 3:392/392 of P07097
- Q64 (≠ R65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C386) mutation to G: Loss of activity.
8jg2A Crystal structure of a biosynthetic thiolase from megasphaera hexanoica soaked with hexanoyl-coa
42% identity, 100% coverage: 1:398/400 of query aligns to 2:390/393 of 8jg2A