SitesBLAST
Comparing CCNA_02490 CCNA_02490 3-ketoacyl-CoA thiolase 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)
72% identity, 100% coverage: 1:399/399 of query aligns to 4:403/403 of 6pccA
- active site: C93 (= C90), A359 (≠ H355), C389 (= C385), G391 (= G387)
- binding coenzyme a: C93 (= C90), I148 (= I145), R229 (= R226), T232 (= T228), A252 (= A248), S256 (= S252), N325 (= N321), F328 (= F324)
- binding hexanal: N61 (= N58), T146 (= T143), I148 (= I145), G149 (= G146), R151 (= R148), L361 (= L357)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
72% identity, 100% coverage: 1:399/399 of query aligns to 4:403/403 of 6pcbA
- active site: C93 (= C90), A359 (≠ H355), C389 (= C385), G391 (= G387)
- binding coenzyme a: C93 (= C90), I148 (= I145), R229 (= R226), A252 (= A248), S256 (= S252), G257 (= G253), N325 (= N321), F328 (= F324)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
71% identity, 100% coverage: 1:399/399 of query aligns to 5:401/401 of 6pcdA
- active site: S94 (≠ C90), A357 (≠ H355), C387 (= C385), G389 (= G387)
- binding coenzyme a: I149 (= I145), M167 (= M163), R227 (= R226), T230 (= T228), A250 (= A248), S254 (= S252), G255 (= G253), A325 (= A323), A357 (≠ H355)
- binding octanal: N62 (= N58), T147 (= T143), T148 (= T144), I149 (= I145), G150 (= G146), R152 (= R148), L359 (= L357)
P45359 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; CaTHL; EC 2.3.1.9 from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) (see paper)
45% identity, 100% coverage: 1:398/399 of query aligns to 1:391/392 of P45359
- V77 (= V79) 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
- 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 (≠ AS 284:285) binding
- A286 (≠ R291) 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 (= C385) modified: Disulfide link with 88, In inhibited form
- A386 (= A393) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
44% identity, 100% coverage: 1:398/399 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C90), H348 (= H355), S378 (≠ C385), G380 (= G387)
- binding coenzyme a: L148 (≠ M154), H156 (≠ S162), R220 (= R226), L231 (= L236), A243 (= A248), S247 (= S252), F319 (= F324), H348 (= H355)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
47% identity, 100% coverage: 1:398/399 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C90), A348 (= A352), A378 (= A382), L380 (= L384)
- 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 (= A248), S250 (= S252), I252 (≠ V254), A321 (= A323), F322 (= F324), H351 (= H355)
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: 1:398/399 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 (≠ H224) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R226) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S252) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H355) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C385) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
47% identity, 100% coverage: 1:399/399 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C90), H347 (= H355), C377 (= C385), G379 (= G387)
- binding coenzyme a: C88 (= C90), L149 (≠ A153), K219 (≠ R226), F234 (≠ V240), A242 (= A248), S246 (= S252), A317 (= A323), F318 (= F324), H347 (= H355)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
45% identity, 100% coverage: 1:398/399 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H355), C379 (= C385), G381 (= G387)
- binding coenzyme a: S88 (≠ C90), L148 (≠ M154), R221 (= R226), F236 (≠ V240), A244 (= A248), S248 (= S252), L250 (≠ V254), A319 (= A323), F320 (= F324), H349 (= H355)
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)
42% identity, 97% coverage: 11:397/399 of query aligns to 14:394/397 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 (= R226) binding
- T227 (= T228) binding
- S251 (= S252) binding
- C382 (= C385) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
43% identity, 97% coverage: 11:399/399 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 (= C385) mutation to G: Loss of activity.
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
44% identity, 99% coverage: 4:399/399 of query aligns to 3:398/400 of 5bz4K
- active site: C87 (= C90), H354 (= H355), C384 (= C385), G386 (= G387)
- binding coenzyme a: C87 (= C90), R146 (vs. gap), M160 (= M163), R220 (= R226), A246 (= A248), G247 (= G249), S250 (= S252), Q252 (≠ V254), M291 (= M293), A321 (= A323), F322 (= F324), H354 (= H355)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
43% identity, 99% coverage: 6:399/399 of query aligns to 4:389/389 of 2vu2A
- active site: C86 (= C90), H345 (= H355), C375 (= C385), G377 (= G387)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ S162), M154 (= M163), F232 (≠ V240), S244 (= S252), G245 (= G253), F316 (= F324), H345 (= H355)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
43% identity, 99% coverage: 6:399/399 of query aligns to 4:389/389 of 1dm3A
- active site: C86 (= C90), H345 (= H355), C375 (= C385), G377 (= G387)
- binding acetyl coenzyme *a: C86 (= C90), L145 (≠ F149), H153 (≠ S162), M154 (= M163), R217 (= R226), S224 (≠ A232), M225 (≠ L233), A240 (= A248), S244 (= S252), M285 (= M293), A315 (= A323), F316 (= F324), H345 (= H355), C375 (= C385)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
43% identity, 99% coverage: 6:399/399 of query aligns to 4:389/389 of 1dlvA
- active site: C86 (= C90), H345 (= H355), C375 (= C385), G377 (= G387)
- binding coenzyme a: C86 (= C90), L145 (≠ F149), H153 (≠ S162), M154 (= M163), R217 (= R226), L228 (= L236), A240 (= A248), S244 (= S252), H345 (= H355)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
43% identity, 99% coverage: 6:399/399 of query aligns to 6:391/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
43% identity, 99% coverage: 6:399/399 of query aligns to 7:392/392 of 1ou6A
- active site: C89 (= C90), H348 (= H355), C378 (= C385), G380 (= G387)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ F149), H156 (≠ S162), M157 (= M163), F235 (≠ V240), A243 (= A248), S247 (= S252), A318 (= A323), F319 (= F324), H348 (= H355)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
41% identity, 97% coverage: 11:397/399 of query aligns to 17:393/395 of 4c2jD
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
42% identity, 99% coverage: 6:399/399 of query aligns to 4:389/389 of 2wkuA
- active site: C86 (= C90), H345 (= H355), C375 (= C385), G377 (= G387)
- binding D-mannose: S6 (≠ D8), A7 (≠ G9), R38 (= R40), K182 (≠ R191), D194 (≠ G203), V280 (= V288), D281 (≠ E289), T287 (≠ I295), P331 (≠ G341), S332 (≠ A342), V334 (= V344), V336 (≠ A346), F360 (≠ R370)
8oqoC Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-49
43% identity, 99% coverage: 4:399/399 of query aligns to 4:398/398 of 8oqoC
Query Sequence
>CCNA_02490 CCNA_02490 3-ketoacyl-CoA thiolase
MTAAYICDGIRTPIGRYGGSLSKVRADDLAAIPLKALVARNPSLDLAAIDEIVLGSANQA
GEDNRNVARMALLLAGYPVSVPGVTVNRLCASGLEAVGYAARAIASGHNDLVIAGGVESM
SRAPFVMGKADSAFSRSAEIFDTTIGWRFVNPAMRKLYGVDSMPETAENVATDYGVNRED
QDAFALRSQARTAAAQANGFLAGEITPVEIPGKAGPTIVDRDEHPRETTMEALAKLKPIV
REGGTVTAGNASGVNDGAVALVIASEDAVKRHGLTPRARITGYASAGVEPRVMGIGPVPA
VRKLMAKTGLAIGDFDVVELNEAFAAQGLAVLRQLGLPDDGAHVNANGGAIALGHPLGAS
GARLVLTALRQLEASGGQRGLATLCIGVGQGAALAFERV
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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