SitesBLAST
Comparing Echvi_1071 Echvi_1071 acetyl-CoA acetyltransferases to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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 / LMG 5710 / VKM B-1787) (see paper)
44% identity, 98% coverage: 5:388/391 of query aligns to 6:390/392 of P45359
- V77 (≠ K78) 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 (= C89) modified: Disulfide link with 378, In inhibited form
- S96 (≠ A97) binding
- N153 (≠ P140) 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 (≠ SV 277:278) binding
- A286 (≠ R284) 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 (= C376) modified: Disulfide link with 88, In inhibited form
- A386 (= A384) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
43% identity, 98% coverage: 5:388/391 of query aligns to 6:390/392 of 4xl4A
- active site: C88 (= C89), H348 (= H346), S378 (≠ C376), G380 (= G378)
- binding coenzyme a: L148 (vs. gap), H156 (≠ Y143), R220 (= R218), L231 (= L229), A243 (= A241), S247 (= S245), F319 (= F317), H348 (= H346)
P09110 3-ketoacyl-CoA thiolase, peroxisomal; Acetyl-CoA C-myristoyltransferase; Acetyl-CoA acyltransferase; Beta-ketothiolase; Peroxisomal 3-oxoacyl-CoA thiolase; EC 2.3.1.16; EC 2.3.1.155; EC 2.3.1.9 from Homo sapiens (Human) (see 3 papers)
42% identity, 99% coverage: 2:388/391 of query aligns to 37:420/424 of P09110
- V387 (≠ T356) to A: in dbSNP:rs2229528
Sites not aligning to the query:
- 1:26 PTS2-type peroxisomal targeting signal
- 5 mutation Q->D,K,L: Does not affect localization to peroxisomes.
- 6 V→D: Abolished localization to peroxisomes.; V→K: Does not affect localization to peroxisomes.
- 7 mutation V->D,K: Abolished localization to peroxisomes.
- 8 mutation L->D,K: Does not affect localization to peroxisomes.
- 9 mutation G->D,R,L: Does not affect localization to peroxisomes.
- 10 H→E: In S3E mutant; Abolished localization to peroxisomes.
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
42% identity, 99% coverage: 2:388/391 of query aligns to 6:388/390 of 2d3tC
- active site: C94 (= C89), H346 (= H346), C376 (= C376), G378 (= G378)
- binding acetyl coenzyme *a: C94 (= C89), R214 (= R218), L222 (= L226), L225 (= L229), A238 (= A241), G239 (= G242), S242 (= S245), I244 (≠ T247), A313 (= A316), F314 (= F317), H346 (= H346), C376 (= C376)
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)
39% identity, 98% coverage: 4:388/391 of query aligns to 8:394/397 of P42765
- C92 (= C89) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R218) binding
- T227 (= T221) binding
- S251 (= S245) binding
- C382 (= C376) 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)
41% identity, 99% coverage: 5:390/391 of query aligns to 7:392/392 of P07097
- Q64 (≠ M65) mutation to A: Slightly lower activity.
- C89 (= C89) mutation to A: Loss of activity.
- C378 (= C376) mutation to G: Loss of activity.
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
39% identity, 98% coverage: 4:388/391 of query aligns to 11:393/395 of 4c2jD
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
41% identity, 99% coverage: 5:390/391 of query aligns to 4:389/389 of 2vu2A
- active site: C86 (= C89), H345 (= H346), C375 (= C376), G377 (= G378)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ S145), M154 (= M146), F232 (= F233), S244 (= S245), G245 (≠ Q246), F316 (= F317), H345 (= H346)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
41% identity, 99% coverage: 5:390/391 of query aligns to 4:389/389 of 1dm3A
- active site: C86 (= C89), H345 (= H346), C375 (= C376), G377 (= G378)
- binding acetyl coenzyme *a: C86 (= C89), L145 (≠ H139), H153 (≠ S145), M154 (= M146), R217 (= R218), S224 (≠ V225), M225 (≠ L226), A240 (= A241), S244 (= S245), M285 (= M286), A315 (= A316), F316 (= F317), H345 (= H346), C375 (= C376)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
41% identity, 99% coverage: 5:390/391 of query aligns to 4:389/389 of 1dlvA
- active site: C86 (= C89), H345 (= H346), C375 (= C376), G377 (= G378)
- binding coenzyme a: C86 (= C89), L145 (≠ H139), H153 (≠ S145), M154 (= M146), R217 (= R218), L228 (= L229), A240 (= A241), S244 (= S245), H345 (= H346)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
41% identity, 99% coverage: 5:390/391 of query aligns to 6:391/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
41% identity, 99% coverage: 5:390/391 of query aligns to 7:392/392 of 1ou6A
- active site: C89 (= C89), H348 (= H346), C378 (= C376), G380 (= G378)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ H139), H156 (≠ S145), M157 (= M146), F235 (= F233), A243 (= A241), S247 (= S245), A318 (= A316), F319 (= F317), H348 (= H346)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
41% identity, 99% coverage: 5:390/391 of query aligns to 4:389/389 of 2wkuA
- active site: C86 (= C89), H345 (= H346), C375 (= C376), G377 (= G378)
- binding D-mannose: S6 (≠ K7), A7 (≠ G8), R38 (≠ T41), K182 (≠ R174), D194 (≠ E186), V280 (= V281), D281 (= D282), T287 (≠ I288), P331 (= P332), S332 (≠ N333), V334 (= V335), V336 (= V337), F360 (≠ N361)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
41% identity, 99% coverage: 5:390/391 of query aligns to 5:390/390 of 1m1oA
- active site: A87 (≠ C89), H346 (= H346), C376 (= C376), G378 (= G378)
- binding acetoacetyl-coenzyme a: L86 (≠ Y88), A87 (≠ C89), L146 (≠ H139), H154 (≠ S145), M155 (= M146), R218 (= R218), S225 (≠ V225), M226 (≠ L226), A241 (= A241), G242 (= G242), S245 (= S245), A316 (= A316), F317 (= F317), H346 (= H346), I377 (≠ V377), G378 (= G378)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
40% identity, 99% coverage: 2:390/391 of query aligns to 3:391/391 of 5f38B
- active site: C88 (= C89), H347 (= H346), C377 (= C376), G379 (= G378)
- binding coenzyme a: C88 (= C89), L149 (≠ I135), K219 (≠ R218), F234 (= F233), A242 (= A241), S246 (= S245), A317 (= A316), F318 (= F317), H347 (= H346)
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
41% identity, 100% coverage: 2:391/391 of query aligns to 2:399/400 of 5bz4K
- active site: C87 (= C89), H354 (= H346), C384 (= C376), G386 (= G378)
- binding coenzyme a: C87 (= C89), R146 (vs. gap), M160 (= M146), R220 (= R218), A246 (= A241), G247 (= G242), S250 (= S245), Q252 (≠ T247), M291 (= M286), A321 (= A316), F322 (= F317), H354 (= H346)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
40% identity, 99% coverage: 2:388/391 of query aligns to 5:393/394 of 5f38D
- active site: C90 (= C89), A348 (= A343), A378 (≠ V373), L380 (≠ A375)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C89), L151 (≠ I135), A246 (= A241), S250 (= S245), I252 (≠ T247), A321 (= A316), F322 (= F317), H351 (= H346)
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)
42% identity, 99% coverage: 2:388/391 of query aligns to 3:391/393 of P14611
- C88 (= C89) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ S145) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ G216) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R218) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S245) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H346) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C376) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
42% identity, 99% coverage: 2:388/391 of query aligns to 3:391/393 of 4o9cC
- active site: S88 (≠ C89), H349 (= H346), C379 (= C376), G381 (= G378)
- binding coenzyme a: S88 (≠ C89), L148 (≠ H139), R221 (= R218), F236 (= F233), A244 (= A241), S248 (= S245), L250 (≠ T247), A319 (= A316), F320 (= F317), H349 (= H346)
8oqoC Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-49
37% identity, 99% coverage: 2:388/391 of query aligns to 3:396/398 of 8oqoC
Query Sequence
>Echvi_1071 Echvi_1071 acetyl-CoA acetyltransferases
MDAYIIKGYRTAVGKAKKGGFRFYRPDDLAVDVIKKLIADTPGLEAERVDDLIVGNAVPE
AEQGMQMGRMISLMALGKVVPGFIINRYCGSGLEAIALATAKIKSGMADCIIAGGTESMS
MVPMMGYKTALNWKIASEHPDYYLSMGLTAEELAKDYDISREDSDQFAVTSHERAISAIK
EGRFKEEIVPIEVEETFVDASGKRQTRTFTVDTDEGPRPGTNMDVLGGLKPAFKQGGQVT
AGNSSQTSDGAAFTVVMSERMVKELNLEPVARLVSYSVAGVDPRIMGIGPKEAVPKALKQ
AGMKMSDISLVELNEAFAAQALAVIRALDMDPNTVNVNGGAVALGHPLGCTGAKLTVQMI
NELRRRNQKYGMVTACVGGGQGVAGVVELLK
Or try a new SitesBLAST search
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