SitesBLAST
Comparing WP_011950736.1 NCBI__GCF_000016765.1:WP_011950736.1 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)
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
62% identity, 100% coverage: 1:399/400 of query aligns to 4:402/403 of 6pccA
- active site: C93 (= C90), A359 (≠ H356), C389 (= C386), G391 (= G388)
- binding coenzyme a: C93 (= C90), I148 (≠ L145), R229 (= R227), T232 (= T229), A252 (= A249), S256 (= S253), N325 (= N322), F328 (= F325)
- binding hexanal: N61 (= N58), T146 (= T143), I148 (≠ L145), G149 (= G146), R151 (= R148), L361 (= L358)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
62% identity, 100% coverage: 1:399/400 of query aligns to 4:402/403 of 6pcbA
- active site: C93 (= C90), A359 (≠ H356), C389 (= C386), G391 (= G388)
- binding coenzyme a: C93 (= C90), I148 (≠ L145), R229 (= R227), A252 (= A249), S256 (= S253), G257 (= G254), N325 (= N322), F328 (= F325)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
61% identity, 100% coverage: 1:399/400 of query aligns to 5:400/401 of 6pcdA
- active site: S94 (≠ C90), A357 (≠ H356), C387 (= C386), G389 (= G388)
- binding coenzyme a: I149 (≠ L145), M167 (= M163), R227 (= R227), T230 (= T229), A250 (= A249), S254 (= S253), G255 (= G254), A325 (= A324), A357 (≠ H356)
- binding octanal: N62 (= N58), T147 (= T143), T148 (= T144), I149 (≠ L145), G150 (= G146), R152 (= R148), L359 (= L358)
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, 100% coverage: 1:399/400 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 (≠ T162) 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 (= S253) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H356) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C386) 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, 100% coverage: 1:399/400 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H356), C379 (= C386), G381 (= G388)
- binding coenzyme a: S88 (≠ C90), L148 (≠ M154), R221 (= R227), F236 (≠ T241), A244 (= A249), S248 (= S253), L250 (= L255), A319 (= A324), F320 (= F325), H349 (= H356)
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)
42% identity, 100% coverage: 1:399/400 of query aligns to 1:391/392 of P45359
- V77 (≠ E79) 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 acetate
- 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 (≠ AA 285:286) binding acetate
- A286 (≠ R292) 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 (= C386) modified: Disulfide link with 88, In inhibited form
- A386 (= A394) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
42% identity, 100% coverage: 1:399/400 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C90), H348 (= H356), S378 (≠ C386), G380 (= G388)
- binding coenzyme a: L148 (≠ M154), H156 (≠ T162), R220 (= R227), L231 (= L237), A243 (= A249), S247 (= S253), F319 (= F325), H348 (= H356)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
44% identity, 97% coverage: 11:398/400 of query aligns to 12:390/392 of P07097
- Q64 (≠ R65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C386) mutation to G: Loss of activity.
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
44% identity, 98% coverage: 6:398/400 of query aligns to 7:390/392 of 1ou6A
- active site: C89 (= C90), H348 (= H356), C378 (= C386), G380 (= G388)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ M154), H156 (≠ T162), M157 (= M163), F235 (≠ T241), A243 (= A249), S247 (= S253), A318 (= A324), F319 (= F325), H348 (= H356)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
44% identity, 98% coverage: 6:398/400 of query aligns to 4:387/389 of 2vu2A
- active site: C86 (= C90), H345 (= H356), C375 (= C386), G377 (= G388)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ T162), M154 (= M163), F232 (≠ T241), S244 (= S253), G245 (= G254), F316 (= F325), H345 (= H356)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
44% identity, 98% coverage: 6:398/400 of query aligns to 4:387/389 of 1dm3A
- active site: C86 (= C90), H345 (= H356), C375 (= C386), G377 (= G388)
- binding acetyl coenzyme *a: C86 (= C90), L145 (≠ M154), H153 (≠ T162), M154 (= M163), R217 (= R227), S224 (≠ I233), M225 (≠ L234), A240 (= A249), S244 (= S253), M285 (= M294), A315 (= A324), F316 (= F325), H345 (= H356), C375 (= C386)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
44% identity, 98% coverage: 6:398/400 of query aligns to 4:387/389 of 1dlvA
- active site: C86 (= C90), H345 (= H356), C375 (= C386), G377 (= G388)
- binding coenzyme a: C86 (= C90), L145 (≠ M154), H153 (≠ T162), M154 (= M163), R217 (= R227), L228 (= L237), A240 (= A249), S244 (= S253), H345 (= H356)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
44% identity, 98% coverage: 6:398/400 of query aligns to 6:389/391 of 2vu1A
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
44% identity, 98% coverage: 6:398/400 of query aligns to 4:387/389 of 2wkuA
- active site: C86 (= C90), H345 (= H356), C375 (= C386), G377 (= G388)
- binding D-mannose: S6 (≠ D8), A7 (= A9), R38 (= R40), K182 (= K191), D194 (≠ A203), V280 (≠ I289), D281 (≠ A290), T287 (≠ A296), P331 (= P340), S332 (≠ P343), V334 (= V345), V336 (≠ P347), F360 (≠ E371)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
43% identity, 98% coverage: 6:398/400 of query aligns to 5:388/390 of 1m1oA
- active site: A87 (≠ C90), H346 (= H356), C376 (= C386), G378 (= G388)
- binding acetoacetyl-coenzyme a: L86 (= L89), A87 (≠ C90), L146 (≠ M154), H154 (≠ T162), M155 (= M163), R218 (= R227), S225 (≠ I233), M226 (≠ L234), A241 (= A249), G242 (= G250), S245 (= S253), A316 (= A324), F317 (= F325), H346 (= H356), I377 (≠ V387), G378 (= G388)
8opxC Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with trehalose (fragment-b-tre) (see paper)
42% identity, 99% coverage: 3:399/400 of query aligns to 3:397/398 of 8opxC
8oqmD Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-10 (see paper)
42% identity, 99% coverage: 3:399/400 of query aligns to 4:398/399 of 8oqmD
8oqoC Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-49 (see paper)
42% identity, 99% coverage: 3:399/400 of query aligns to 3:397/398 of 8oqoC
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
45% identity, 100% coverage: 1:399/400 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C90), A348 (= A353), A378 (= A383), L380 (≠ M385)
- 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 (≠ A153), A246 (= A249), S250 (= S253), I252 (≠ L255), A321 (= A324), F322 (= F325), H351 (= H356)
8oqlC Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-1 (see paper)
42% identity, 99% coverage: 3:399/400 of query aligns to 3:396/397 of 8oqlC
Query Sequence
>WP_011950736.1 NCBI__GCF_000016765.1:WP_011950736.1
MAQAFICDAIRTPIGKLNGSLATVRADDLAALPIKALMDRNPDTDWSTLDDVILGCANQA
GEDNRNVARMAVLLAGLPECVPGVTVNRLCSSGLNALGIASQAIRSGDADFMIAGGVESM
TRAPYVLGKAGSAFGRDQKIEDTTLGWRFVNPAMQAAYGVDTMPQTGENVAQEWGVSREA
QDRFALASQEKAARAQAGGRFAAEIIPVSVPQHRGDHVLFEADEHLRATSLDILAKLKPV
TGPGGTVTAGNASGLNDGAAAMLVATEATAAAQGLVTRARVVGMAASGIAPRIMGAGPIE
AARRVMARHSITTDALDVIELNEAFASQAIATLSSLGIDPLDPRVNPNGGAIALGHPLGM
SGARIALSAVEELHRVQGRYALAFMCVGVGQGVAVLLERA
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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