SitesBLAST
Comparing WP_110804635.1 NCBI__GCF_003217355.1:WP_110804635.1 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)
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)
50% identity, 100% coverage: 1:390/391 of query aligns to 1:391/392 of P45359
- V77 (= V78) 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 (= C89) modified: Disulfide link with 378, In inhibited form
- S96 (≠ V97) binding acetate
- N153 (≠ G153) 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 (≠ AI 278:279) binding acetate
- A286 (≠ E285) 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 (= C377) modified: Disulfide link with 88, In inhibited form
- A386 (= A385) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
49% identity, 100% coverage: 1:390/391 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C89), H348 (= H347), S378 (≠ C377), G380 (= G379)
- binding coenzyme a: L148 (= L148), H156 (= H156), R220 (≠ K220), L231 (= L230), A243 (= A242), S247 (= S246), F319 (= F318), H348 (= H347)
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)
51% identity, 100% coverage: 1:390/391 of query aligns to 1:392/393 of P14611
- C88 (= C89) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (= H156) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ H218) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ K220) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S246) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H347) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C377) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
50% identity, 100% coverage: 1:390/391 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C89), H349 (= H347), C379 (= C377), G381 (= G379)
- binding coenzyme a: S88 (≠ C89), L148 (= L148), R221 (≠ K220), F236 (= F234), A244 (= A242), S248 (= S246), L250 (≠ I248), A319 (= A317), F320 (= F318), H349 (= H347)
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)
46% identity, 99% coverage: 1:389/391 of query aligns to 4:394/397 of P42765
- C92 (= C89) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (≠ K220) binding CoA
- T227 (= T222) binding CoA
- S251 (= S246) binding CoA
- C382 (= C377) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
51% identity, 100% coverage: 1:390/391 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C89), A348 (= A344), A378 (≠ I374), L380 (≠ M376)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C89), L151 (= L148), A246 (= A242), S250 (= S246), I252 (= I248), A321 (= A317), F322 (= F318), H351 (= H347)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
46% identity, 99% coverage: 1:389/391 of query aligns to 7:393/395 of 4c2jD
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
50% identity, 100% coverage: 1:391/391 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C89), H347 (= H347), C377 (= C377), G379 (= G379)
- binding coenzyme a: C88 (= C89), L149 (= L148), K219 (= K220), F234 (= F234), A242 (= A242), S246 (= S246), A317 (= A317), F318 (= F318), H347 (= H347)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
48% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C89), H345 (= H347), C375 (= C377), G377 (= G379)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (= H156), M154 (= M157), F232 (= F234), S244 (= S246), G245 (= G247), F316 (= F318), H345 (= H347)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
48% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C89), H345 (= H347), C375 (= C377), G377 (= G379)
- binding acetyl coenzyme *a: C86 (= C89), L145 (= L148), H153 (= H156), M154 (= M157), R217 (≠ K220), S224 (≠ K226), M225 (≠ L227), A240 (= A242), S244 (= S246), M285 (= M287), A315 (= A317), F316 (= F318), H345 (= H347), C375 (= C377)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
48% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C89), H345 (= H347), C375 (= C377), G377 (= G379)
- binding coenzyme a: C86 (= C89), L145 (= L148), H153 (= H156), M154 (= M157), R217 (≠ K220), L228 (= L230), A240 (= A242), S244 (= S246), H345 (= H347)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
48% identity, 99% coverage: 4:391/391 of query aligns to 4:391/391 of 2vu1A