SitesBLAST
Comparing WP_091371536.1 NCBI__GCF_900105165.1:WP_091371536.1 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
64% identity, 100% coverage: 1:392/392 of query aligns to 1:393/393 of 6bn2A
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: 1:391/392 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 (= N119) to D: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs148639841
- G183 (= G146) to R: in 3KTD; no activity; dbSNP:rs120074141
- Y219 (= Y182) binding CoA; binding K(+)
- RVD 258:260 (≠ AVK 221:223) binding CoA
- K263 (= K226) binding CoA
- A280 (= A242) binding K(+)
- A281 (= A243) binding K(+)
- A283 (= A245) binding K(+)
- S284 (= S246) binding CoA
- T297 (≠ S259) to M: in 3KTD; decreased protein abundance; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs886041122
- A301 (= A263) to P: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs1420321267
- I312 (≠ V274) to T: in 3KTD; decreased protein stability; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074146
- A333 (≠ I295) to P: in 3KTD; loss of protein solubility; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs120074147
- A380 (= A342) to T: in 3KTD; decreased protein stability; dbSNP:rs120074140
- V381 (= V343) binding K(+)
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: 1:391/392 of query aligns to 5:393/393 of 2ib8D
2f2sA Human mitochondrial acetoacetyl-coa thiolase
55% identity, 99% coverage: 3:391/392 of query aligns to 10:389/389 of 2f2sA
- active site: C95 (= C87), H347 (= H347), C375 (= C377), G377 (= G379)
- binding coenzyme a: C95 (= C87), L153 (= L147), H161 (= H155), M162 (= M156), Y188 (= Y182), R220 (≠ A221), V221 (= V222), D222 (≠ K223), K225 (= K226), L229 (= L230), F233 (= F234), A242 (= A242), S246 (= S246), A317 (= A317), F318 (= F318), H347 (= H347)
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
55% identity, 100% coverage: 1:391/392 of query aligns to 5:397/397 of 6aqpA
- active site: C93 (= C87), H353 (= H347), C383 (= C377), G385 (= G379)
- binding coenzyme a: C93 (= C87), L153 (= L147), Y188 (= Y182), N226 (≠ A221), N228 (≠ K223), K231 (= K226), A248 (= A242), P249 (≠ A243), S252 (= S246), A323 (= A317), F324 (= F318), H353 (= H347)
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
55% identity, 100% coverage: 1:391/392 of query aligns to 5:399/399 of 6aqpC
- active site: C93 (= C87), H355 (= H347), C385 (= C377), G387 (= G379)
- binding acetyl coenzyme *a: C93 (= C87), L153 (= L147), M162 (= M156), Y188 (= Y182), N230 (≠ K223), K233 (= K226), L234 (≠ I227), I237 (≠ L230), A250 (= A242), P251 (≠ A243), S254 (= S246), F295 (= F287), A325 (= A317), F326 (= F318), H355 (= H347)
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: 1:391/392 of query aligns to 4:398/398 of Q4WCL5
- Y187 (= Y182) binding K(+)
- N229 (≠ K223) binding CoA
- K232 (= K226) binding CoA
- A249 (= A242) binding K(+)
- P250 (≠ A243) binding K(+)
- S252 (≠ A245) binding K(+)
- S253 (= S246) binding CoA
- V350 (= V343) binding K(+)
- N385 (= N378) binding chloride
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, 99% coverage: 2:391/392 of query aligns to 3:398/398 of P41338
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
P45359 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; CaTHL; EC 2.3.1.9 from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W) (see paper)
50% identity, 99% coverage: 1:389/392 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 (= C87) modified: Disulfide link with 378, In inhibited form
- S96 (≠ M95) binding acetate
- N153 (= N152) 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 278:279) binding acetate
- A286 (≠ E285) 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 (= C377) modified: Disulfide link with 88, In inhibited form
- A386 (= A385) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
49% identity, 99% coverage: 1:389/392 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C87), H348 (= H347), S378 (≠ C377), G380 (= G379)
- binding coenzyme a: L148 (= L147), H156 (= H155), R220 (≠ P219), L231 (= L230), A243 (= A242), S247 (= S246), F319 (= F318), H348 (= H347)
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: 1:391/392 of query aligns to 37:429/433 of B0XMC1
- N229 (≠ G192) binding CoA
6l2cA Crystal structure of aspergillus fumigatus mitochondrial acetyl-coa acetyltransferase in complex with coa (see paper)
52% identity, 100% coverage: 1:391/392 of query aligns to 6:398/402 of 6l2cA