SitesBLAST
Comparing Dsui_0976 FitnessBrowser__PS:Dsui_0976 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)
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
54% identity, 99% coverage: 5:393/393 of query aligns to 8:397/397 of 6aqpA
- active site: C93 (= C89), H353 (= H349), C383 (= C379), G385 (= G381)
- binding coenzyme a: C93 (= C89), L153 (= L149), Y188 (≠ T185), N226 (≠ K223), N228 (≠ Q225), K231 (= K228), A248 (= A244), P249 (≠ A245), S252 (= S248), A323 (= A319), F324 (= F320), H353 (= H349)
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
54% identity, 99% coverage: 5:393/393 of query aligns to 8:399/399 of 6aqpC
- active site: C93 (= C89), H355 (= H349), C385 (= C379), G387 (= G381)
- binding acetyl coenzyme *a: C93 (= C89), L153 (= L149), M162 (= M159), Y188 (≠ T185), N230 (≠ Q225), K233 (= K228), L234 (≠ I229), I237 (≠ L232), A250 (= A244), P251 (≠ A245), S254 (= S248), F295 (= F289), A325 (= A319), F326 (= F320), H355 (= H349)
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)
54% identity, 99% coverage: 5:393/393 of query aligns to 7:398/398 of Q4WCL5
- Y187 (≠ T185) binding
- N229 (≠ Q225) binding
- K232 (= K228) binding
- A249 (= A244) binding
- P250 (≠ A245) binding
- S252 (= S247) binding
- S253 (= S248) binding
- V350 (≠ C345) binding
- N385 (≠ I380) binding
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)
52% identity, 98% coverage: 5:391/393 of query aligns to 4:390/392 of P45359
- V77 (≠ L78) 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 (≠ M97) binding
- N153 (≠ Q154) 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 (≠ TT 280:281) binding
- A286 (≠ N287) 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 (= C379) modified: Disulfide link with 88, In inhibited form
- A386 (= A387) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
52% identity, 98% coverage: 5:391/393 of query aligns to 4:390/392 of 4xl4A
- active site: C88 (= C89), H348 (= H349), S378 (≠ C379), G380 (= G381)
- binding coenzyme a: L148 (= L149), H156 (≠ R157), R220 (vs. gap), L231 (= L232), A243 (= A244), S247 (= S248), F319 (= F320), H348 (= H349)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
51% identity, 98% coverage: 6:392/393 of query aligns to 4:391/394 of 7cw5B
- active site: C87 (= C89), H348 (= H349), C378 (= C379), G380 (= G381)
- binding coenzyme a: L147 (= L149), H155 (≠ L158), M156 (= M159), R220 (≠ L222), T223 (≠ A224), A243 (= A244), P247 (≠ S248), L249 (≠ I250), H348 (= H349)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
50% identity, 98% coverage: 5:391/393 of query aligns to 4:390/393 of 6bn2A
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)
52% identity, 99% coverage: 1:391/393 of query aligns to 1:391/393 of P14611
- C88 (= C89) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ R157) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ P221) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ K223) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S248) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H349) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C379) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
52% identity, 99% coverage: 1:391/393 of query aligns to 1:391/393 of 4o9cC
- active site: S88 (≠ C89), H349 (= H349), C379 (= C379), G381 (= G381)
- binding coenzyme a: S88 (≠ C89), L148 (= L149), R221 (≠ K223), F236 (= F236), A244 (= A244), S248 (= S248), L250 (≠ I250), A319 (= A319), F320 (= F320), H349 (= H349)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
52% identity, 98% coverage: 6:391/393 of query aligns to 7:393/394 of 5f38D
- active site: C90 (= C89), A348 (= A346), A378 (= A376), L380 (= L378)
- 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 (= L149), A246 (= A244), S250 (= S248), I252 (= I250), A321 (= A319), F322 (= F320), H351 (= H349)
P24752 Acetyl-CoA acetyltransferase, mitochondrial; Acetoacetyl-CoA thiolase; T2; EC 2.3.1.9 from Homo sapiens (Human) (see 6 papers)
49% identity, 98% coverage: 5:391/393 of query aligns to 42:425/427 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 (= N121) to D: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs148639841
- G183 (= G148) to R: in 3KTD; no activity; dbSNP:rs120074141
- Y219 (≠ T185) binding ; binding
- RVD 258:260 (≠ KAQ 223:225) binding
- K263 (= K228) binding
- A280 (= A244) binding
- A281 (= A245) binding
- A283 (≠ S247) binding
- S284 (= S248) binding
- T297 (≠ K261) to M: in 3KTD; decreased protein abundance; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs886041122
- A301 (= A265) to P: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs1420321267
- I312 (= I276) to T: in 3KTD; decreased protein stability; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074146
- A333 (≠ M297) to P: in 3KTD; loss of protein solubility; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs120074147
- A380 (= A344) to T: in 3KTD; decreased protein stability; dbSNP:rs120074140
- V381 (≠ C345) binding
Sites not aligning to the query:
- 5 A → P: in dbSNP:rs3741056
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)
48% identity, 99% coverage: 1:391/393 of query aligns to 1:396/398 of P41338
- M1 (= M1) modified: Initiator methionine, Removed
- S2 (= S2) modified: N-acetylserine
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)
49% identity, 98% coverage: 5:391/393 of query aligns to 8:391/393 of 2ib8D
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
52% identity, 98% coverage: 6:391/393 of query aligns to 5:389/391 of 5f38B
- active site: C88 (= C89), H347 (= H349), C377 (= C379), G379 (= G381)
- binding coenzyme a: C88 (= C89), L149 (= L149), K219 (vs. gap), F234 (= F236), A242 (= A244), S246 (= S248), A317 (= A319), F318 (= F320), H347 (= H349)
2f2sA Human mitochondrial acetoacetyl-coa thiolase
48% identity, 98% coverage: 5:391/393 of query aligns to 11:387/389 of 2f2sA
- active site: C95 (= C89), H347 (= H349), C375 (= C379), G377 (= G381)
- binding coenzyme a: C95 (= C89), L153 (= L149), H161 (≠ R157), M162 (= M159), Y188 (≠ T185), R220 (≠ K223), V221 (≠ A224), D222 (≠ Q225), K225 (= K228), L229 (= L232), F233 (= F236), A242 (= A244), S246 (= S248), A317 (= A319), F318 (= F320), H347 (= H349)
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
47% identity, 99% coverage: 2:391/393 of query aligns to 2:392/394 of 1wl4A
- active site: C89 (= C89), H350 (= H349), C380 (= C379), G382 (= G381)
- binding coenzyme a: L148 (= L149), M157 (= M159), R220 (≠ L222), Y234 (≠ A235), P245 (≠ A244), A246 (= A245), S249 (= S248), A320 (= A319), F321 (= F320), H350 (= H349)
Q9BWD1 Acetyl-CoA acetyltransferase, cytosolic; Acetyl-CoA transferase-like protein; Cytosolic acetoacetyl-CoA thiolase; EC 2.3.1.9 from Homo sapiens (Human) (see 2 papers)
47% identity, 99% coverage: 2:391/393 of query aligns to 5:395/397 of Q9BWD1
- K211 (= K210) to R: in dbSNP:rs25683
- R223 (≠ L222) binding
- S226 (≠ A224) binding
- S252 (= S248) binding
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
46% identity, 99% coverage: 1:391/393 of query aligns to 1:390/392 of P07097
- Q64 (= Q64) mutation to A: Slightly lower activity.
- C89 (= C89) mutation to A: Loss of activity.
- C378 (= C379) mutation to G: Loss of activity.
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
47% identity, 98% coverage: 5:391/393 of query aligns to 5:390/392 of 1ou6A
- active site: C89 (= C89), H348 (= H349), C378 (= C379), G380 (= G381)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L149), H156 (≠ L158), M157 (= M159), F235 (= F236), A243 (= A244), S247 (= S248), A318 (= A319), F319 (= F320), H348 (= H349)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
47% identity, 98% coverage: 5:391/393 of query aligns to 2:387/389 of 2vu2A
- active site: C86 (= C89), H345 (= H349), C375 (= C379), G377 (= G381)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ L158), M154 (= M159), F232 (= F236), S244 (= S248), G245 (≠ S249), F316 (= F320), H345 (= H349)
Query Sequence
>Dsui_0976 FitnessBrowser__PS:Dsui_0976
MSDPIVIVSVARTPMGGFQGDFNSLTAPQLGATAIKAAVERAGIKPEQVEEVVFGNVLQA
GVGQAPARQAALGAGLPLSAGCTTIHKVCGSALKSVMMVHDSLLAGSYEIGVAGGQESMS
NAPYLLPKARGGYRLGHGQLLDHMFFDGLEDAYQKGRLMGTFAEECAESYGFTREAQDEW
AIQSTVRAQKAIKEGLFKWEIAPVTIAGKKGDVVVDQDEQPLKAQIEKIPALKPAFKKDG
TVTAANSSSISDGAAALVLMKESKAKVLGLAPIAKIVGHTTHAQEPNLFTTAPVFAMEKL
MQKTGWNVADVDLWEINEAFAVVTMAAIKDLKLDPAKVNVHGGACALGHPIGASGARILV
TLIGALKQYGKKKGVASLCIGGGEAVAVGVEMF
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