SitesBLAST
Comparing WP_055437058.1 NCBI__GCF_001418085.1:WP_055437058.1 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)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
67% identity, 99% coverage: 3:390/392 of query aligns to 2:390/393 of 6bn2A
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)
55% identity, 100% coverage: 1:391/392 of query aligns to 1:397/398 of P41338
- M1 (= M1) modified: Initiator methionine, Removed
- S2 (≠ N2) modified: N-acetylserine
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
55% identity, 98% coverage: 5:390/392 of query aligns to 8:397/399 of 6aqpC
- active site: C93 (= C89), H355 (= H348), C385 (= C378), G387 (= G380)
- binding acetyl coenzyme *a: C93 (= C89), L153 (= L148), M162 (= M157), Y188 (= Y183), N230 (≠ R224), K233 (= K227), L234 (≠ I228), I237 (≠ L231), A250 (= A243), P251 (≠ A244), S254 (= S247), F295 (= F288), A325 (= A318), F326 (= F319), H355 (= H348)
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, 98% coverage: 5:390/392 of query aligns to 7:396/398 of Q4WCL5
- Y187 (= Y183) binding K(+)
- N229 (≠ R224) binding CoA
- K232 (= K227) binding CoA
- A249 (= A243) binding K(+)
- P250 (≠ A244) binding K(+)
- S252 (≠ A246) binding K(+)
- S253 (= S247) binding CoA
- V350 (= V344) binding K(+)
- N385 (= N379) binding chloride
P24752 Acetyl-CoA acetyltransferase, mitochondrial; Acetoacetyl-CoA thiolase; T2; EC 2.3.1.9 from Homo sapiens (Human) (see 6 papers)
55% identity, 99% coverage: 3:391/392 of query aligns to 40:426/427 of P24752
- N93 (= N56) to S: in 3KTD; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074145
- N158 (≠ L121) 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 CoA; binding K(+)
- RVD 258:260 (≠ NVR 222:224) binding CoA
- K263 (= K227) binding CoA
- A280 (= A243) binding K(+)
- A281 (= A244) binding K(+)
- A283 (= A246) binding K(+)
- S284 (= S247) binding CoA
- 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 (≠ L296) 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 K(+)
Sites not aligning to the query:
- 5 A → P: in dbSNP:rs3741056
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
54% identity, 98% coverage: 5:390/392 of query aligns to 8:395/397 of 6aqpA
- active site: C93 (= C89), H353 (= H348), C383 (= C378), G385 (= G380)
- binding coenzyme a: C93 (= C89), L153 (= L148), Y188 (= Y183), N226 (= N222), N228 (≠ R224), K231 (= K227), A248 (= A243), P249 (≠ A244), S252 (= S247), A323 (= A318), F324 (= F319), H353 (= H348)
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, 99% coverage: 3:391/392 of query aligns to 6:392/393 of 2ib8D
2f2sA Human mitochondrial acetoacetyl-coa thiolase
55% identity, 99% coverage: 4:391/392 of query aligns to 10:388/389 of 2f2sA
- active site: C95 (= C89), H347 (= H348), C375 (= C378), G377 (= G380)
- binding coenzyme a: C95 (= C89), L153 (= L148), H161 (≠ A156), M162 (= M157), Y188 (= Y183), R220 (≠ N222), V221 (= V223), D222 (≠ R224), K225 (= K227), L229 (= L231), F233 (= F235), A242 (= A243), S246 (= S247), A317 (= A318), F318 (= F319), H347 (= H348)
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, 99% coverage: 3:391/392 of query aligns to 38:428/433 of B0XMC1
- N229 (≠ G193) binding CoA
6l2cA Crystal structure of aspergillus fumigatus mitochondrial acetyl-coa acetyltransferase in complex with coa (see paper)
52% identity, 99% coverage: 3:391/392 of query aligns to 7:397/402 of 6l2cA
- active site: C93 (= C89), H356 (= H348), C384 (= C378), G386 (= G380)
- binding coenzyme a: C93 (= C89), Y188 (= Y183), N226 (= N222), R228 (= R224), M232 (≠ I228), L235 (= L231), F239 (= F235), A249 (= A243), S253 (= S247), F327 (= F319)
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)
53% identity, 99% coverage: 4:391/392 of query aligns to 3:392/393 of P14611
- C88 (= C89) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ A156) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ E219) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ K221) 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.
Q22100 Acetyl-CoA acetyltransferase homolog, mitochondrial; 3-ketoacyl-CoA thiolase; EC 2.3.1.- from Caenorhabditis elegans (see 2 papers)
49% identity, 99% coverage: 2:391/392 of query aligns to 21:406/407 of Q22100