SitesBLAST
Comparing Ac3H11_3920 FitnessBrowser__acidovorax_3H11:Ac3H11_3920 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)
66% identity, 100% coverage: 3:403/403 of query aligns to 3:403/403 of 6pccA
- active site: C93 (= C93), A359 (≠ H359), C389 (= C389), G391 (= G391)
- binding coenzyme a: C93 (= C93), I148 (= I148), R229 (= R230), T232 (= T232), A252 (= A252), S256 (= S256), N325 (= N325), F328 (= F328)
- binding hexanal: N61 (= N61), T146 (= T146), I148 (= I148), G149 (= G149), R151 (= R151), L361 (= L361)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
66% identity, 100% coverage: 3:403/403 of query aligns to 3:403/403 of 6pcbA
- active site: C93 (= C93), A359 (≠ H359), C389 (= C389), G391 (= G391)
- binding coenzyme a: C93 (= C93), I148 (= I148), R229 (= R230), A252 (= A252), S256 (= S256), G257 (= G257), N325 (= N325), F328 (= F328)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
65% identity, 100% coverage: 3:403/403 of query aligns to 4:401/401 of 6pcdA
- active site: S94 (≠ C93), A357 (≠ H359), C387 (= C389), G389 (= G391)
- binding coenzyme a: I149 (= I148), M167 (= M166), R227 (= R230), T230 (= T232), A250 (= A252), S254 (= S256), G255 (= G257), A325 (= A327), A357 (≠ H359)
- binding octanal: N62 (= N61), T147 (= T146), T148 (= T147), I149 (= I148), G150 (= G149), R152 (= R151), L359 (= L361)
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)
45% identity, 99% coverage: 5:402/403 of query aligns to 2:391/392 of P45359
- V77 (≠ I82) 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 (= C93) modified: Disulfide link with 378, In inhibited form
- S96 (≠ G101) binding
- N153 (≠ G162) 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 288:289) binding
- A286 (≠ R295) 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 (= C389) modified: Disulfide link with 88, In inhibited form
- A386 (= A397) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
45% identity, 99% coverage: 5:402/403 of query aligns to 2:391/392 of 4xl4A
- active site: C88 (= C93), H348 (= H359), S378 (≠ C389), G380 (= G391)
- binding coenzyme a: L148 (vs. gap), H156 (≠ S165), R220 (= R230), L231 (= L240), A243 (= A252), S247 (= S256), F319 (= F328), H348 (= H359)
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
44% identity, 99% coverage: 5:403/403 of query aligns to 1:398/400 of 5bz4K
- active site: C87 (= C93), H354 (= H359), C384 (= C389), G386 (= G391)
- binding coenzyme a: C87 (= C93), R146 (vs. gap), M160 (= M166), R220 (= R230), A246 (= A252), G247 (= G253), S250 (= S256), Q252 (≠ V258), M291 (= M297), A321 (= A327), F322 (= F328), H354 (= H359)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
46% identity, 100% coverage: 2:402/403 of query aligns to 1:394/394 of 5f38D
- active site: C90 (= C93), A348 (= A356), A378 (≠ C386), L380 (≠ M388)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C93), L151 (= L156), A246 (= A252), S250 (= S256), I252 (≠ V258), A321 (= A327), F322 (= F328), H351 (= H359)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
46% identity, 99% coverage: 5:403/403 of query aligns to 2:391/391 of 5f38B
- active site: C88 (= C93), H347 (= H359), C377 (= C389), G379 (= G391)
- binding coenzyme a: C88 (= C93), L149 (= L156), K219 (≠ R230), F234 (≠ V244), A242 (= A252), S246 (= S256), A317 (= A327), F318 (= F328), H347 (= H359)
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: 9:402/403 of query aligns to 6:392/393 of P14611
- C88 (= C93) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ S165) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ H228) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R230) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S256) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H359) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C389) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
44% identity, 98% coverage: 9:402/403 of query aligns to 6:392/393 of 4o9cC
- active site: S88 (≠ C93), H349 (= H359), C379 (= C389), G381 (= G391)
- binding coenzyme a: S88 (≠ C93), L148 (= L156), R221 (= R230), F236 (≠ V244), A244 (= A252), S248 (= S256), L250 (≠ V258), A319 (= A327), F320 (= F328), H349 (= H359)
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)
42% identity, 100% coverage: 1:401/403 of query aligns to 1:394/397 of P42765
- C92 (= C93) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R230) binding
- T227 (= T232) binding
- S251 (= S256) binding
- C382 (= C389) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
41% identity, 100% coverage: 1:401/403 of query aligns to 4:393/395 of 4c2jD