SitesBLAST
Comparing Echvi_3705 Echvi_3705 acetyl-CoA acetyltransferases 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)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
60% identity, 100% coverage: 1:393/393 of query aligns to 1:393/393 of 6bn2A
Q4WCL5 Acetyl-CoA acetyltransferase erg10B, cytosolic; Acetoacetyl-CoA thiolase erg10B; ACAT; Cytosolic thiolase erg10B; CT; Ergosterol biosynthesis protein 10B; EC 2.3.1.9 from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
55% identity, 100% coverage: 1:392/393 of query aligns to 4:398/398 of Q4WCL5
- Y187 (= Y183) binding
- N229 (≠ L224) binding
- K232 (= K227) binding
- A249 (= A243) binding
- P250 (≠ A244) binding
- S252 (≠ A246) binding
- S253 (= S247) binding
- V350 (= V344) binding
- N385 (= N379) binding
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
55% identity, 100% coverage: 1:392/393 of query aligns to 5:399/399 of 6aqpC
- active site: C93 (= C88), H355 (= H348), C385 (= C378), G387 (= G380)
- binding acetyl coenzyme *a: C93 (= C88), L153 (= L148), M162 (= M157), Y188 (= Y183), N230 (≠ L224), K233 (= K227), L234 (≠ I228), I237 (≠ L231), A250 (= A243), P251 (≠ A244), S254 (= S247), F295 (= F288), A325 (= A318), F326 (= F319), H355 (= H348)
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
56% identity, 100% coverage: 1:392/393 of query aligns to 5:397/397 of 6aqpA
- active site: C93 (= C88), H353 (= H348), C383 (= C378), G385 (= G380)
- binding coenzyme a: C93 (= C88), L153 (= L148), Y188 (= Y183), N226 (= N222), N228 (≠ L224), K231 (= K227), A248 (= A243), P249 (≠ A244), S252 (= S247), A323 (= A318), F324 (= F319), H353 (= H348)
P24752 Acetyl-CoA acetyltransferase, mitochondrial; Acetoacetyl-CoA thiolase; T2; EC 2.3.1.9 from Homo sapiens (Human) (see 6 papers)
55% identity, 100% coverage: 1:392/393 of query aligns to 39:427/427 of P24752
- N93 (= N55) to S: in 3KTD; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074145
- N158 (= N120) to D: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs148639841
- G183 (= G147) to R: in 3KTD; no activity; dbSNP:rs120074141
- Y219 (= Y183) binding ; binding
- RVD 258:260 (≠ NVL 222:224) binding
- K263 (= K227) binding
- A280 (= A243) binding
- A281 (= A244) binding
- A283 (= A246) binding
- S284 (= S247) binding
- T297 (≠ S260) to M: in 3KTD; decreased protein abundance; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs886041122
- A301 (= A264) to P: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs1420321267
- I312 (= I275) to T: in 3KTD; decreased protein stability; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074146
- A333 (≠ I296) to P: in 3KTD; loss of protein solubility; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs120074147
- A380 (= A343) to T: in 3KTD; decreased protein stability; dbSNP:rs120074140
- V381 (= V344) binding
Sites not aligning to the query:
- 5 A → P: in dbSNP:rs3741056
2ib8D Crystallographic and kinetic studies of human mitochondrial acetoacetyl-coa thiolase (t2): the importance of potassium and chloride for its structure and function (see paper)
55% identity, 100% coverage: 1:392/393 of query aligns to 5:393/393 of 2ib8D
P41338 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Ergosterol biosynthesis protein 10; EC 2.3.1.9 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
54% identity, 99% coverage: 2:392/393 of query aligns to 3:398/398 of P41338
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
2f2sA Human mitochondrial acetoacetyl-coa thiolase
55% identity, 99% coverage: 3:392/393 of query aligns to 10:389/389 of 2f2sA
- active site: C95 (= C88), H347 (= H348), C375 (= C378), G377 (= G380)
- binding coenzyme a: C95 (= C88), L153 (= L148), H161 (≠ P156), M162 (= M157), Y188 (= Y183), R220 (≠ N222), V221 (= V223), D222 (≠ L224), K225 (= K227), L229 (= L231), F233 (= F235), A242 (= A243), S246 (= S247), A317 (= A318), F318 (= F319), H347 (= H348)
Q22100 Acetyl-CoA acetyltransferase homolog, mitochondrial; 3-ketoacyl-CoA thiolase; EC 2.3.1.- from Caenorhabditis elegans (see 2 papers)
52% identity, 99% coverage: 2:392/393 of query aligns to 22:407/407 of Q22100
- A119 (= A99) mutation to P: In mg368; increased uptake of the lipophilic dye Nile Red and the synthetic fatty acid analog C1-BODIPY-C12.
B0XMC1 Acetyl-CoA acetyltransferase erg10A, mitochondrial; Acetoacetyl-CoA thiolase erg10A; Ergosterol biosynthesis protein 10A; EC 2.3.1.9 from Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya fumigata) (see paper)
52% identity, 100% coverage: 1:392/393 of query aligns to 37:429/433 of B0XMC1
6l2cA Crystal structure of aspergillus fumigatus mitochondrial acetyl-coa acetyltransferase in complex with coa (see paper)
52% identity, 100% coverage: 1:392/393 of query aligns to 6:398/402 of 6l2cA
- active site: C93 (= C88), H356 (= H348), C384 (= C378), G386 (= G380)
- binding coenzyme a: C93 (= C88), Y188 (= Y183), N226 (= N222), R228 (≠ L224), M232 (≠ I228), L235 (= L231), F239 (= F235), A249 (= A243), S253 (= S247), F327 (= F319)
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)
49% identity, 99% coverage: 1:390/393 of query aligns to 1:390/392 of P45359
- V77 (≠ Y77) 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 (= C88) modified: Disulfide link with 378, In inhibited form
- S96 (≠ M96) binding
- N153 (≠ Y153) 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 (≠ AD 279:280) binding
- A286 (≠ I286) 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 (= C378) modified: Disulfide link with 88, In inhibited form
- A386 (= A386) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
48% identity, 99% coverage: 1:390/393 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C88), H348 (= H348), S378 (≠ C378), G380 (= G380)
- binding coenzyme a: L148 (= L148), H156 (≠ P156), R220 (≠ Q221), L231 (= L231), A243 (= A243), S247 (= S247), F319 (= F319), H348 (= H348)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
50% identity, 99% coverage: 3:390/393 of query aligns to 2:390/394 of 7cw5B
- active site: C87 (= C88), H348 (= H348), C378 (= C378), G380 (= G380)
- binding coenzyme a: L147 (= L148), H155 (≠ P156), M156 (= M157), R220 (≠ Y220), T223 (≠ V223), A243 (= A243), P247 (≠ S247), L249 (≠ M249), H348 (= H348)
6bjbA Crystal structure of acat2-c91s thiolase from ascaris suum in complex with propionyl-coa and nitrate (see paper)
49% identity, 100% coverage: 1:392/393 of query aligns to 3:384/384 of 6bjbA
- active site: S90 (≠ C88), H342 (= H348), C370 (= C378), G372 (= G380)
- binding propionyl Coenzyme A: S90 (≠ C88), L148 (= L148), M157 (= M157), Y183 (= Y183), N218 (≠ L224), K221 (= K227), I222 (= I228), L225 (= L231), A237 (= A243), A238 (= A244), S241 (= S247), F282 (= F288), A312 (= A318), F313 (= F319), H342 (= H348), C370 (= C378), N371 (= N379), G372 (= G380)
6bjaA Crystal structure of acat5 thiolase from ascaris suum in complex with coenzyme a (see paper)
49% identity, 99% coverage: 2:392/393 of query aligns to 1:382/382 of 6bjaA
- active site: C87 (= C88), H340 (= H348), C368 (= C378), G370 (= G380)
- binding coenzyme a: Y180 (= Y183), L213 (≠ V223), I214 (≠ L224), K217 (= K227), L221 (= L231), A235 (= A243), A236 (= A244), S239 (= S247), H340 (= H348)
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)
49% identity, 99% coverage: 1:391/393 of query aligns to 1:392/393 of P14611
- C88 (= C88) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ P156) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (vs. gap) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ Y220) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S247) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H348) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C378) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
48% identity, 99% coverage: 1:391/393 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C88), H349 (= H348), C379 (= C378), G381 (= G380)
- binding coenzyme a: S88 (≠ C88), L148 (= L148), R221 (≠ Y220), F236 (= F235), A244 (= A243), S248 (= S247), L250 (≠ M249), A319 (= A318), F320 (= F319), H349 (= H348)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
48% identity, 99% coverage: 1:390/393 of query aligns to 3:393/394 of 5f38D
- active site: C90 (= C88), A348 (≠ S345), A378 (= A375), L380 (≠ I377)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C88), L151 (= L148), A246 (= A243), S250 (= S247), I252 (≠ M249), A321 (= A318), F322 (= F319), H351 (= H348)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
48% identity, 100% coverage: 1:392/393 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C88), H347 (= H348), C377 (= C378), G379 (= G380)
- binding coenzyme a: C88 (= C88), L149 (= L148), K219 (≠ Y220), F234 (= F235), A242 (= A243), S246 (= S247), A317 (= A318), F318 (= F319), H347 (= H348)
Query Sequence
>Echvi_3705 Echvi_3705 acetyl-CoA acetyltransferases
MKEVYIISAVRTPLGSFGGKLSGLTAVELGAQAIKGALGRAQVTPEQVDEVIMGNVLSAN
LGQAPARQAAIGAGIGYHVPCTTVNKVCASGMKSVMFAAQSIMTGQSDIIVAGGMESMSN
VPYYIPKARFGYKFGNGEFVDGLAKDGLHEVYYNFPMGNCADNTAKEKNISREAQDEYAI
QSYRRAAEAWKAQAFQDEVIPVTFKSRKGESITVDEDEEYQNVLFEKIPSLRPVFDKEGT
VTAANASTMNDGAAALVLMSKEKAEALGLQPVAKILGFADAATDPIWFTTAPALAIPKAL
KNAGIQAEAVDYYEINEAFSAVALANQQELNIPNDRLNVFGGAVSLGHPLGASGARIMAT
LHSVLRQKGGKIGVAGICNGGGGASAMVIENLR
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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