SitesBLAST
Comparing WP_028311754.1 NCBI__GCF_000482785.1:WP_028311754.1 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)
68% 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), R229 (= R227), T232 (= T230), A252 (= A250), S256 (= S254), N325 (= N323), F328 (= F326)
- binding hexanal: N61 (= N58), T146 (= T143), I148 (= I145), G149 (= G146), R151 (= R148), L361 (= L359)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
68% 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), R229 (= R227), A252 (= A250), S256 (= S254), G257 (= G255), N325 (= N323), F328 (= F326)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
67% 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), A250 (= A250), S254 (= S254), G255 (= G255), A325 (= A325), A357 (≠ H357)
- binding octanal: N62 (= N58), T147 (= T143), T148 (= T144), I149 (= I145), G150 (= G146), R152 (= R148), L359 (= L359)
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: 1:400/401 of query aligns to 1:391/392 of P45359
- V77 (≠ P79) 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 (≠ A98) binding acetate
- N153 (≠ H158) 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 286:287) binding acetate
- A286 (≠ R293) 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 acetate
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, 99% coverage: 5:399/401 of query aligns to 8:394/397 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 CoA
- T227 (= T230) binding CoA
- S251 (= S254) binding CoA
- C382 (= C387) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
43% 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 (= L153), H156 (≠ S162), R220 (= R227), L231 (= L238), A243 (= A250), S247 (= S254), F319 (= F326), H348 (= H357)
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, 100% coverage: 1:400/401 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 (= S254) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H357) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C387) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
45% identity, 99% coverage: 4:401/401 of query aligns to 3:398/400 of 5bz4K
- active site: C87 (= C90), H354 (= H357), C384 (= C387), G386 (= G389)
- binding coenzyme a: C87 (= C90), R146 (vs. gap), M160 (= M157), R220 (= R227), A246 (= A250), G247 (= G251), S250 (= S254), Q252 (≠ V256), M291 (= M295), A321 (= A325), F322 (= F326), H354 (= H357)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
42% identity, 99% coverage: 5:399/401 of query aligns to 11:393/395 of 4c2jD
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
45% identity, 100% coverage: 1:400/401 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H357), C379 (= C387), G381 (= G389)
- binding coenzyme a: S88 (≠ C90), L148 (vs. gap), R221 (= R227), F236 (≠ V242), A244 (= A250), S248 (= S254), L250 (≠ V256), A319 (= A325), F320 (= F326), H349 (= H357)
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
- Q64 (≠ R65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C387) mutation to G: Loss of activity.
8jg2A Crystal structure of a biosynthetic thiolase from megasphaera hexanoica soaked with hexanoyl-coa
44% identity, 100% coverage: 1:399/401 of query aligns to 2:390/393 of 8jg2A