SitesBLAST
Comparing WP_011939882.1 NCBI__GCF_000016745.1:WP_011939882.1 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 (≠ D77) 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 (= C88) modified: Disulfide link with 378, In inhibited form
- S96 (≠ M96) binding acetate
- N153 (≠ S153) 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 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 (= C88), H348 (= H347), S378 (≠ C377), G380 (= G379)
- binding coenzyme a: L148 (= L148), H156 (= H156), R220 (vs. gap), L231 (= L230), A243 (= A242), S247 (= S246), F319 (= F318), H348 (= H347)
8gqnA X-ray structure of thiolase with coa
49% identity, 99% coverage: 3:389/391 of query aligns to 2:388/390 of 8gqnA
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 (= C88) 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 (= F220) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ V222) 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 (≠ C88), H349 (= H347), C379 (= C377), G381 (= G379)
- binding coenzyme a: S88 (≠ C88), L148 (= L148), R221 (vs. gap), F236 (= F234), A244 (= A242), S248 (= S246), L250 (≠ I248), A319 (= A317), F320 (= F318), H349 (= 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 (= C88), 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 (≠ S247), 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 (= C88), H345 (= H347), C375 (= C377), G377 (= G379)
- binding acetyl coenzyme *a: C86 (= C88), L145 (= L148), H153 (= H156), M154 (= M157), R217 (≠ P219), S224 (≠ K226), M225 (≠ L227), A240 (= A242), S244 (= S246), M285 (≠ Y287), 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 (= C88), H345 (= H347), C375 (= C377), G377 (= G379)
- binding coenzyme a: C86 (= C88), L145 (= L148), H153 (= H156), M154 (= M157), R217 (≠ P219), L228 (= L230), A240 (= A242), S244 (= S246), H345 (= H347)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
49% identity, 99% coverage: 5:391/391 of query aligns to 6:392/392 of P07097
- Q64 (= Q63) mutation to A: Slightly lower activity.
- C89 (= C88) mutation to A: Loss of activity.
- C378 (= C377) mutation to G: Loss of activity.
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
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
48% identity, 99% coverage: 4:391/391 of query aligns to 5:392/392 of 1ou6A
- active site: C89 (= C88), H348 (= H347), C378 (= C377), G380 (= G379)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L148), H156 (= H156), M157 (= M157), F235 (= F234), A243 (= A242), S247 (= S246), A318 (= A317), F319 (= F318), H348 (= H347)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
48% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 2wkuA
- active site: C86 (= C88), H345 (= H347), C375 (= C377), G377 (= G379)
- binding D-mannose: S6 (≠ E8), A7 (≠ S9), R38 (= R40), K182 (≠ L185), D194 (= D197), V280 (≠ M282), D281 (≠ H283), T287 (≠ D289), P331 (= P333), S332 (≠ A334), V334 (= V336), V336 (= V338), F360 (≠ R362)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
48% identity, 99% coverage: 4:391/391 of query aligns to 3:390/390 of 1m1oA
- active site: A87 (≠ C88), H346 (= H347), C376 (= C377), G378 (= G379)
- binding acetoacetyl-coenzyme a: L86 (≠ V87), A87 (≠ C88), L146 (= L148), H154 (= H156), M155 (= M157), R218 (≠ P219), S225 (≠ K226), M226 (≠ L227), A241 (= A242), G242 (= G243), S245 (= S246), A316 (= A317), F317 (= F318), H346 (= H347), I377 (= I378), G378 (= G379)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
45% identity, 100% coverage: 1:391/391 of query aligns to 1:392/393 of 6bn2A
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
47% identity, 99% coverage: 4:389/391 of query aligns to 3:390/394 of 7cw5B
- active site: C87 (= C88), H348 (= H347), C378 (= C377), G380 (= G379)
- binding coenzyme a: L147 (= L148), H155 (= H156), M156 (= M157), R220 (≠ F220), T223 (≠ V222), A243 (= A242), P247 (≠ S246), L249 (≠ I248), H348 (= H347)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
49% identity, 100% coverage: 1:390/391 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C88), A348 (= A344), A378 (= A374), L380 (= L376)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C88), L151 (= L148), A246 (= A242), S250 (= S246), I252 (= I248), A321 (= A317), F322 (= F318), H351 (= H347)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
49% identity, 100% coverage: 1:391/391 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C88), H347 (= H347), C377 (= C377), G379 (= G379)
- binding coenzyme a: C88 (= C88), L149 (= L148), K219 (≠ F220), F234 (= F234), A242 (= A242), S246 (= S246), A317 (= A317), F318 (= F318), H347 (= H347)
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
46% identity, 99% coverage: 4:389/391 of query aligns to 8:395/397 of 6aqpA
- active site: C93 (= C88), H353 (= H347), C383 (= C377), G385 (= G379)
- binding coenzyme a: C93 (= C88), L153 (= L148), Y188 (= Y183), N226 (≠ K221), N228 (≠ D223), K231 (= K226), A248 (= A242), P249 (≠ G243), S252 (= S246), A323 (= A317), F324 (= F318), H353 (= H347)
Q4WCL5 Acetyl-CoA acetyltransferase erg10B, cytosolic; Acetoacetyl-CoA thiolase erg10B; ACAT; Cytosolic thiolase erg10B; CT; Ergosterol biosynthesis protein 10B; EC 2.3.1.9 from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
46% identity, 99% coverage: 4:389/391 of query aligns to 7:396/398 of Q4WCL5
- Y187 (= Y183) binding K(+)
- N229 (≠ D223) binding CoA
- K232 (= K226) binding CoA
- A249 (= A242) binding K(+)
- P250 (≠ G243) binding K(+)
- S252 (≠ A245) binding K(+)
- S253 (= S246) binding CoA
- V350 (≠ C343) binding K(+)
- N385 (≠ I378) binding chloride
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
46% identity, 99% coverage: 4:389/391 of query aligns to 8:397/399 of 6aqpC
- active site: C93 (= C88), H355 (= H347), C385 (= C377), G387 (= G379)
- binding acetyl coenzyme *a: C93 (= C88), L153 (= L148), M162 (= M157), Y188 (= Y183), N230 (≠ D223), K233 (= K226), L234 (= L227), I237 (≠ L230), A250 (= A242), P251 (≠ G243), S254 (= S246), F295 (≠ Y287), A325 (= A317), F326 (= F318), H355 (= H347)
Query Sequence
>WP_011939882.1 NCBI__GCF_000016745.1:WP_011939882.1
MKDVFVVESLRTPFGSFGGVLSDVEAPKLAATVIGAALERTGLDPAAVSEVILGQVLSGG
AGQAPARQAMRLAGIPDGVHAMTINKVCGSGLKSIMLGAGSIMLGDSNLVVAGGMENMSL
TPFILKKARYGYRMGHGELLDLMIYDGLQDPYSGKHMGDIAEAAVAKHGFSREEQDEFAV
RSYRLAQEAVKGGVFKDEIVPVVKNGKKGDEVVADDEDPFKVDFAKLTQLRPAFKKDGAI
TAGNASSISDGAAVTLLADEGALKKHNLKPRARLVAYATYSMHPELYTDAPVGAIQAACA
RAGLKVADIDLFEINEAFAAVTMIAIKQLGLDPAKVNVNGGACAIGHPIGASGARLAATV
IRELHRRQSRYGLATLCIGGGEAVAVIFERV
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory