SitesBLAST
Comparing WP_028314019.1 NCBI__GCF_000429905.1:WP_028314019.1 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)
49% identity, 100% coverage: 1:428/428 of query aligns to 1:391/392 of P45359
- V77 (≠ K112) 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 (= C123) modified: Disulfide link with 378, In inhibited form
- S96 (≠ A131) binding acetate
- N153 (≠ Y191) 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 (≠ AS 316:317) binding acetate
- A286 (= A323) 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 (= C415) modified: Disulfide link with 88, In inhibited form
- A386 (= A423) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
49% identity, 100% coverage: 1:428/428 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C123), H348 (= H385), S378 (≠ C415), G380 (= G417)
- binding coenzyme a: L148 (= L186), H156 (= H194), R220 (vs. gap), L231 (= L268), A243 (= A280), S247 (= S284), F319 (= F356), H348 (= H385)
8jg2A Crystal structure of a biosynthetic thiolase from megasphaera hexanoica soaked with hexanoyl-coa
49% identity, 100% coverage: 1:427/428 of query aligns to 2:390/393 of 8jg2A
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)
47% identity, 100% coverage: 1:428/428 of query aligns to 1:392/393 of P14611
- C88 (= C123) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (= H194) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ R256) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ P257) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S284) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H385) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C415) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
48% identity, 100% coverage: 1:428/428 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C123), A348 (≠ S382), A378 (≠ I412), L380 (≠ M414)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C123), L151 (= L186), A246 (= A280), S250 (= S284), I252 (= I286), A321 (= A355), F322 (= F356), H351 (= H385)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
47% identity, 100% coverage: 1:428/428 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C123), H349 (= H385), C379 (= C415), G381 (= G417)
- binding coenzyme a: S88 (≠ C123), L148 (= L186), R221 (≠ P257), F236 (= F272), A244 (= A280), S248 (= S284), L250 (≠ I286), A319 (= A355), F320 (= F356), H349 (= H385)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
47% identity, 99% coverage: 5:427/428 of query aligns to 6:390/392 of 1ou6A
- active site: C89 (= C123), H348 (= H385), C378 (= C415), G380 (= G417)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L186), H156 (= H194), M157 (= M195), F235 (= F272), A243 (= A280), S247 (= S284), A318 (= A355), F319 (= F356), H348 (= H385)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
47% identity, 99% coverage: 5:427/428 of query aligns to 5:389/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
47% identity, 99% coverage: 5:427/428 of query aligns to 3:387/389 of 2vu2A
- active site: C86 (= C123), H345 (= H385), C375 (= C415), G377 (= G417)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (= H194), M154 (= M195), F232 (= F272), S244 (= S284), G245 (= G285), F316 (= F356), H345 (= H385)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
47% identity, 99% coverage: 5:427/428 of query aligns to 3:387/389 of 1dm3A
- active site: C86 (= C123), H345 (= H385), C375 (= C415), G377 (= G417)
- binding acetyl coenzyme *a: C86 (= C123), L145 (= L186), H153 (= H194), M154 (= M195), R217 (≠ P257), S224 (≠ K264), M225 (= M265), A240 (= A280), S244 (= S284), M285 (= M325), A315 (= A355), F316 (= F356), H345 (= H385), C375 (= C415)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
47% identity, 99% coverage: 5:427/428 of query aligns to 3:387/389 of 1dlvA
- active site: C86 (= C123), H345 (= H385), C375 (= C415), G377 (= G417)
- binding coenzyme a: C86 (= C123), L145 (= L186), H153 (= H194), M154 (= M195), R217 (≠ P257), L228 (= L268), A240 (= A280), S244 (= S284), H345 (= H385)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
46% identity, 99% coverage: 4:427/428 of query aligns to 5:390/392 of P07097
- Q64 (= Q98) mutation to A: Slightly lower activity.
- C89 (= C123) mutation to A: Loss of activity.
- C378 (= C415) mutation to G: Loss of activity.
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
47% identity, 99% coverage: 5:427/428 of query aligns to 3:387/389 of 2wkuA
- active site: C86 (= C123), H345 (= H385), C375 (= C415), G377 (= G417)
- binding D-mannose: S6 (= S8), A7 (≠ G9), R38 (= R40), K182 (≠ R223), D194 (= D235), V280 (≠ M320), D281 (= D321), T287 (≠ L327), P331 (≠ T371), S332 (≠ E372), V334 (≠ P374), V336 (≠ E376), F360 (≠ H400)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
48% identity, 100% coverage: 1:428/428 of query aligns to 1:390/391 of 5f38B
- active site: C88 (= C123), H347 (= H385), C377 (= C415), G379 (= G417)
- binding coenzyme a: C88 (= C123), L149 (= L186), K219 (vs. gap), F234 (= F272), A242 (= A280), S246 (= S284), A317 (= A355), F318 (= F356), H347 (= H385)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
47% identity, 99% coverage: 5:427/428 of query aligns to 4:388/390 of 1m1oA
- active site: A87 (≠ C123), H346 (= H385), C376 (= C415), G378 (= G417)
- binding acetoacetyl-coenzyme a: L86 (≠ V122), A87 (≠ C123), L146 (= L186), H154 (= H194), M155 (= M195), R218 (≠ P257), S225 (≠ K264), M226 (= M265), A241 (= A280), G242 (= G281), S245 (= S284), A316 (= A355), F317 (= F356), H346 (= H385), I377 (= I416), G378 (= G417)
Q9BWD1 Acetyl-CoA acetyltransferase, cytosolic; Acetyl-CoA transferase-like protein; Cytosolic acetoacetyl-CoA thiolase; EC 2.3.1.9 from Homo sapiens (Human) (see 2 papers)
44% identity, 99% coverage: 5:428/428 of query aligns to 9:396/397 of Q9BWD1
- K211 (≠ R246) to R: in dbSNP:rs25683
- R223 (≠ M258) binding CoA
- S226 (≠ T260) binding CoA
- S252 (= S284) binding CoA
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
44% identity, 99% coverage: 5:428/428 of query aligns to 6:393/394 of 1wl4A
- active site: C89 (= C123), H350 (= H385), C380 (= C415), G382 (= G417)
- binding coenzyme a: L148 (= L186), M157 (= M195), R220 (≠ M258), Y234 (≠ A271), P245 (≠ A280), A246 (≠ G281), S249 (= S284), A320 (= A355), F321 (= F356), H350 (= H385)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
44% identity, 99% coverage: 3:427/428 of query aligns to 2:390/394 of 7cw5B
- active site: C87 (= C123), H348 (= H385), C378 (= C415), G380 (= G417)
- binding coenzyme a: L147 (= L186), H155 (= H194), M156 (= M195), R220 (≠ M258), T223 (= T260), A243 (= A280), P247 (≠ S284), L249 (≠ I286), H348 (= H385)
8gqnA X-ray structure of thiolase with coa
43% identity, 99% coverage: 5:427/428 of query aligns to 4:388/390 of 8gqnA
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
39% identity, 100% coverage: 1:428/428 of query aligns to 1:391/393 of 6bn2A
Query Sequence
>WP_028314019.1 NCBI__GCF_000429905.1:WP_028314019.1
MKEAVIVSGARTAIGSFGGVLKSVPVIQLGSTVMKETLKRVNLRPVVSEAMLSAAPDALK
DQGVIELEEKGMDWDDSAQPVAIDEVIMGNVLTSGQGQNPARQAMVQAGICKETPAFTVN
KVCASGLKAIALGAASIMTGQADVILAGGQESMSNVPMALPLARWGYRMAISGKGEIDDL
MVLDGLYEIFYGYHMGVTAENIASKYGITREEQDALGVLSHNRARKAITEGLFKDEIVPV
SFMERRKEVVVDTDERPMDTSMEKMAKLRPAFIKDGTVTAGNASGINDGAASVLLMSAEK
AQELGLEPLAKIKAFASAGMDPAYMGLGPIPAVRKVLKATGMSIDDLQMLEVNEAFASQA
IACLRELGIDTEKPNELGSGISLGHPIGCTGARQMVTAIHHMERKGYNTGLITMCIGGGM
GMAMIIEK
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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