SitesBLAST
Comparing Echvi_3705 Echvi_3705 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)
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), N228 (= N222), L229 (≠ V223), N230 (≠ L224), K233 (= K227), L234 (≠ I228), I237 (≠ L231), F241 (= F235), A250 (= A243), P251 (≠ A244), S254 (= S247), P255 (≠ T248), L256 (≠ M249), 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), M162 (= M157), Y188 (= Y183), N226 (= N222), L227 (≠ V223), N228 (≠ L224), K231 (= K227), L232 (≠ I228), I235 (≠ L231), F239 (= F235), A248 (= A243), P249 (≠ A244), S252 (= S247), P253 (≠ T248), L254 (≠ M249), F293 (= F288), A323 (= A318), F324 (= F319), H353 (= H348), I355 (≠ L350)
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), V226 (≠ I228), L229 (= L231), V232 (= V234), F233 (= F235), A242 (= A243), A243 (= A244), S246 (= S247), A317 (= A318), F318 (= F319), H347 (= H348), I349 (≠ L350)
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), L153 (= L148), H161 (≠ P156), Y188 (= Y183), N226 (= N222), L227 (≠ V223), R228 (≠ L224), M232 (≠ I228), L235 (= L231), F239 (= F235), A249 (= A243), G250 (≠ A244), S253 (= S247), T254 (= T248), A326 (= A318), F327 (= F319), H356 (= H348)
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