SitesBLAST
Comparing BWI76_RS13135 FitnessBrowser__Koxy:BWI76_RS13135 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)
65% identity, 100% coverage: 1:401/401 of query aligns to 4:403/403 of 6pccA
- active site: C93 (= C90), A359 (≠ H357), C389 (= C387), G391 (= G389)
- binding coenzyme a: C93 (= C90), I148 (= I145), M166 (= M163), R229 (= R227), T232 (= T230), L240 (= L238), A252 (= A250), G253 (= G251), S256 (= S254), G257 (= G255), V258 (= V256), N325 (= N323), A327 (= A325), F328 (= F326), L361 (= L359)
- binding hexanal: N61 (= N58), L92 (= L89), T146 (= T143), T147 (= T144), I148 (= I145), G149 (= G146), R151 (= R148), M166 (= M163), L361 (= L359), G391 (= G389)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
65% identity, 100% coverage: 1:401/401 of query aligns to 4:403/403 of 6pcbA
- active site: C93 (= C90), A359 (≠ H357), C389 (= C387), G391 (= G389)
- binding coenzyme a: C93 (= C90), I148 (= I145), M166 (= M163), R229 (= R227), T232 (= T230), L237 (= L235), L240 (= L238), A252 (= A250), G253 (= G251), S256 (= S254), G257 (= G255), V258 (= V256), N325 (= N323), A327 (= A325), F328 (= F326), L361 (= L359)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
64% identity, 100% coverage: 1:401/401 of query aligns to 5:401/401 of 6pcdA
- active site: S94 (≠ C90), A357 (≠ H357), C387 (= C387), G389 (= G389)
- binding coenzyme a: I149 (= I145), M167 (= M163), R227 (= R227), T230 (= T230), L238 (= L238), A250 (= A250), G251 (= G251), S254 (= S254), G255 (= G255), V256 (= V256), N323 (= N323), A325 (= A325), F326 (= F326), A357 (≠ H357), L359 (= L359)
- binding octanal: A61 (= A57), N62 (= N58), L93 (= L89), E122 (= E118), T147 (= T143), T148 (= T144), I149 (= I145), G150 (= G146), R152 (= R148), M167 (= M163), L359 (= L359), G389 (= G389)
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, 100% coverage: 1:400/401 of query aligns to 1:391/392 of P45359
- V77 (≠ H79) 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 (≠ G159) 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 286:287) binding
- A286 (≠ K293) 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 (= C387) modified: Disulfide link with 88, In inhibited form
- A386 (= A395) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
44% identity, 100% coverage: 1:400/401 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C90), H348 (= H357), S378 (≠ C387), G380 (= G389)
- binding coenzyme a: L148 (≠ M154), H156 (≠ S162), M157 (= M163), R220 (= R227), L228 (= L235), L231 (= L238), F235 (= F242), A243 (= A250), G244 (= G251), S247 (= S254), G248 (= G255), L249 (≠ V256), A318 (= A325), F319 (= F326), H348 (= H357)
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
45% identity, 100% coverage: 2:401/401 of query aligns to 5:390/390 of 2d3tC
- active site: C94 (= C90), H346 (= H357), C376 (= C387), G378 (= G389)
- binding acetyl coenzyme *a: C94 (= C90), M129 (≠ F125), M150 (= M163), H176 (≠ Q189), R214 (= R227), L222 (= L235), L225 (= L238), A238 (= A250), G239 (= G251), S242 (= S254), I244 (≠ V256), M283 (= M295), A313 (= A325), F314 (= F326), H346 (= H357), C376 (= C387)
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
45% identity, 100% coverage: 2:401/401 of query aligns to 1:398/400 of 5bz4K
- active site: C87 (= C90), H354 (= H357), C384 (= C387), G386 (= G389)
- binding coenzyme a: C87 (= C90), R146 (vs. gap), M160 (= M163), L161 (≠ P164), R220 (= R227), L228 (= L235), L231 (= L238), A246 (= A250), G247 (= G251), S250 (= S254), Q252 (≠ V256), M291 (= M295), A321 (= A325), F322 (= F326), H354 (= H357)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
47% identity, 100% coverage: 1:400/401 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C90), A348 (= A354), A378 (≠ C384), L380 (≠ M386)
- 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), H159 (≠ D161), M160 (= M163), F238 (= F242), A246 (= A250), S250 (= S254), G251 (= G255), I252 (≠ V256), M291 (= M295), A321 (= A325), F322 (= F326), H351 (= H357)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
46% identity, 100% coverage: 1:401/401 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C90), H347 (= H357), C377 (= C387), G379 (= G389)
- binding coenzyme a: C88 (= C90), L149 (= L153), H157 (≠ D161), M158 (= M163), K219 (≠ R227), S222 (≠ T230), L227 (= L235), L230 (= L238), F234 (= F242), A242 (= A250), G243 (= G251), S246 (= S254), G247 (= G255), I248 (≠ V256), M287 (= M295), A317 (= A325), F318 (= F326), H347 (= H357)
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)
43% identity, 100% coverage: 1:399/401 of query aligns to 4:394/397 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 (= R227) binding
- T227 (= T230) binding
- S251 (= S254) binding
- C382 (= C387) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
45% identity, 98% coverage: 11:401/401 of query aligns to 12:392/392 of P07097