SitesBLAST
Comparing PfGW456L13_2430 Acetyl-CoA acetyltransferase (EC 2.3.1.9) @ Beta-ketoadipyl CoA thiolase (EC 2.3.1.-) 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)
67% identity, 100% coverage: 1:401/403 of query aligns to 4:403/403 of 6pccA
- active site: C93 (= C90), A359 (≠ H357), C389 (= C387), G391 (= G389)
- binding coenzyme a: C93 (= C90), I148 (= I145), R229 (= R227), T232 (= T230), A252 (= A250), S256 (= S254), N325 (= N323), F328 (= F326)
- binding hexanal: N61 (= N58), T146 (= T143), I148 (= I145), G149 (= G146), R151 (= R148), L361 (= L359)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
67% identity, 100% coverage: 1:401/403 of query aligns to 4:403/403 of 6pcbA
- active site: C93 (= C90), A359 (≠ H357), C389 (= C387), G391 (= G389)
- binding coenzyme a: C93 (= C90), I148 (= I145), R229 (= R227), A252 (= A250), S256 (= S254), G257 (= G255), N325 (= N323), F328 (= F326)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
66% identity, 100% coverage: 1:401/403 of query aligns to 5:401/401 of 6pcdA
- active site: S94 (≠ C90), A357 (≠ H357), C387 (= C387), G389 (= G389)
- binding coenzyme a: I149 (= I145), M167 (= M163), R227 (= R227), T230 (= T230), A250 (= A250), S254 (= S254), G255 (= G255), A325 (= A325), A357 (≠ H357)
- binding octanal: N62 (= N58), T147 (= T143), T148 (= T144), I149 (= I145), G150 (= G146), R152 (= R148), L359 (= L359)
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)
44% identity, 99% coverage: 1:400/403 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 (≠ M154) 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 286:287) binding
- A286 (≠ R293) 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 (= C387) modified: Disulfide link with 88, In inhibited form
- A386 (= A395) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
44% identity, 99% coverage: 1:400/403 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C90), H348 (= H357), S378 (≠ C387), G380 (= G389)
- binding coenzyme a: L148 (≠ F149), H156 (≠ T157), R220 (= R227), L231 (= L238), A243 (= A250), S247 (= S254), F319 (= F326), H348 (= H357)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
46% identity, 99% coverage: 1:400/403 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C90), A348 (= A354), A378 (≠ C384), L380 (≠ M386)
- 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 (= L153), A246 (= A250), S250 (= S254), I252 (≠ V256), A321 (= A325), F322 (= F326), H351 (= H357)
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
43% identity, 99% coverage: 3:401/403 of query aligns to 6:390/390 of 2d3tC
- active site: C94 (= C90), H346 (= H357), C376 (= C387), G378 (= G389)
- binding acetyl coenzyme *a: C94 (= C90), R214 (= R227), L222 (= L235), L225 (= L238), A238 (= A250), G239 (= G251), S242 (= S254), I244 (≠ V256), A313 (= A325), F314 (= F326), H346 (= H357), C376 (= C387)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
45% identity, 100% coverage: 1:401/403 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C90), H347 (= H357), C377 (= C387), G379 (= G389)
- binding coenzyme a: C88 (= C90), L149 (= L153), K219 (≠ R227), F234 (= F242), A242 (= A250), S246 (= S254), A317 (= A325), F318 (= F326), H347 (= H357)
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, 99% coverage: 1:400/403 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 (≠ 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 (= S254) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H357) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C387) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
45% identity, 99% coverage: 3:401/403 of query aligns to 2:398/400 of 5bz4K
- active site: C87 (= C90), H354 (= H357), C384 (= C387), G386 (= G389)
- binding coenzyme a: C87 (= C90), R146 (vs. gap), M160 (= M163), R220 (= R227), A246 (= A250), G247 (= G251), S250 (= S254), Q252 (≠ V256), M291 (= M295), A321 (= A325), F322 (= F326), H354 (= H357)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
44% identity, 99% coverage: 4:401/403 of query aligns to 5:392/392 of P07097
- Q64 (≠ R65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C387) mutation to G: Loss of activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
44% identity, 99% coverage: 1:400/403 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H357), C379 (= C387), G381 (= G389)
- binding coenzyme a: S88 (≠ C90), L148 (= L153), R221 (= R227), F236 (= F242), A244 (= A250), S248 (= S254), L250 (≠ V256), A319 (= A325), F320 (= F326), H349 (= H357)
8oqoC Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-49
43% identity, 99% coverage: 3:401/403 of query aligns to 3:398/398 of 8oqoC
8oqmD Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-10
43% identity, 99% coverage: 3:401/403 of query aligns to 4:399/399 of 8oqmD
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
44% identity, 99% coverage: 5:401/403 of query aligns to 6:392/392 of 1ou6A
- active site: C89 (= C90), H348 (= H357), C378 (= C387), G380 (= G389)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L153), H156 (≠ S162), M157 (= M163), F235 (= F242), A243 (= A250), S247 (= S254), A318 (= A325), F319 (= F326), H348 (= H357)
8oqlC Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-1
43% identity, 99% coverage: 3:401/403 of query aligns to 3:397/397 of 8oqlC
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
44% identity, 99% coverage: 5:401/403 of query aligns to 3:389/389 of 2vu2A
- active site: C86 (= C90), H345 (= H357), C375 (= C387), G377 (= G389)
- 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 (= F242), S244 (= S254), G245 (= G255), F316 (= F326), H345 (= H357)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
44% identity, 99% coverage: 5:401/403 of query aligns to 3:389/389 of 1dm3A
- active site: C86 (= C90), H345 (= H357), C375 (= C387), G377 (= G389)
- binding acetyl coenzyme *a: C86 (= C90), L145 (= L153), H153 (≠ S162), M154 (= M163), R217 (= R227), S224 (≠ Q234), M225 (≠ L235), A240 (= A250), S244 (= S254), M285 (= M295), A315 (= A325), F316 (= F326), H345 (= H357), C375 (= C387)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
44% identity, 99% coverage: 5:401/403 of query aligns to 3:389/389 of 1dlvA
- active site: C86 (= C90), H345 (= H357), C375 (= C387), G377 (= G389)
- binding coenzyme a: C86 (= C90), L145 (= L153), H153 (≠ S162), M154 (= M163), R217 (= R227), L228 (= L238), A240 (= A250), S244 (= S254), H345 (= H357)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
44% identity, 99% coverage: 5:401/403 of query aligns to 5:391/391 of 2vu1A
Query Sequence
>PfGW456L13_2430 Acetyl-CoA acetyltransferase (EC 2.3.1.9) @ Beta-ketoadipyl CoA thiolase (EC 2.3.1.-)
MNDALIIDAVRTPIGRYAGVLSSVRADDLGAVPLRELLRRHPQVDWNTVDDVIYGCANQA
GEDNRNVARMSALLAGLPVSVPGTTLNRLCGSGLDAIGTAARAIRSGETGLMLVGGVESM
SRAPLVMGKAEQAFSRTAEVFDTTIGWRFVNPLMKKTYGIDSMPETAENVAEQFNISRAD
QDAFALRSQQRAAAAQASGRLAKEIVAVEIPQRKGPAKVVEHDEHPRGDTTLEQLAKLGT
PFREGGSITAGNASGVNDGACALLLASPEVAKRQGLTARGRVVAMATAGVEPRIMGIGPV
PATRKVLEVANLSLADMDVIELNEAFAAQGLAVLRELGLSDTDPRVNPNGGAIALGHPLG
MSGARLVTTALHELEERNGRYALCTMCIGVGQGIALIIERLSH
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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