SitesBLAST
Comparing HSERO_RS04635 FitnessBrowser__HerbieS:HSERO_RS04635 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
48% identity, 100% coverage: 1:399/400 of query aligns to 2:396/397 of 6aqpA
- active site: C93 (= C93), H353 (= H356), C383 (= C386), G385 (= G388)
- binding coenzyme a: C93 (= C93), L153 (= L153), Y188 (≠ T192), N226 (≠ A230), N228 (= N232), K231 (≠ R235), A248 (= A251), P249 (≠ A252), S252 (= S255), A323 (= A326), F324 (= F327), H353 (= H356)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
49% identity, 98% coverage: 6:398/400 of query aligns to 4:390/393 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)
48% identity, 100% coverage: 1:399/400 of query aligns to 1:397/398 of Q4WCL5
- Y187 (≠ T192) binding
- N229 (= N232) binding
- K232 (≠ R235) binding
- A249 (= A251) binding
- P250 (≠ A252) binding
- S252 (= S254) binding
- S253 (= S255) binding
- V350 (≠ C352) binding
- N385 (≠ I387) binding
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
48% identity, 100% coverage: 1:399/400 of query aligns to 2:398/399 of 6aqpC
- active site: C93 (= C93), H355 (= H356), C385 (= C386), G387 (= G388)
- binding acetyl coenzyme *a: C93 (= C93), L153 (= L153), M162 (= M166), Y188 (≠ T192), N230 (= N232), K233 (≠ R235), L234 (≠ I236), I237 (≠ L239), A250 (= A251), P251 (≠ A252), S254 (= S255), F295 (= F296), A325 (= A326), F326 (= F327), H355 (= H356)
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)
47% identity, 98% coverage: 6:398/400 of query aligns to 4:390/392 of P45359
- V77 (≠ Q82) 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 (= C93) modified: Disulfide link with 378, In inhibited form
- S96 (≠ M101) binding
- N153 (≠ S158) 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 (≠ AS 287:288) binding
- A286 (≠ E294) 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 (= C386) modified: Disulfide link with 88, In inhibited form
- A386 (= A394) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
47% identity, 98% coverage: 6:398/400 of query aligns to 4:390/392 of 4xl4A
- active site: C88 (= C93), H348 (= H356), S378 (≠ C386), G380 (= G388)
- binding coenzyme a: L148 (= L153), H156 (≠ Y161), R220 (vs. gap), L231 (= L239), A243 (= A251), S247 (= S255), F319 (= F327), H348 (= H356)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
52% identity, 98% coverage: 7:398/400 of query aligns to 7:393/394 of 5f38D
- active site: C90 (= C93), A348 (= A353), A378 (= A383), L380 (= L385)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C93), L151 (= L153), A246 (= A251), S250 (= S255), I252 (= I257), A321 (= A326), F322 (= F327), H351 (= H356)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
48% identity, 98% coverage: 7:399/400 of query aligns to 4:391/394 of 7cw5B
- active site: C87 (= C93), H348 (= H356), C378 (= C386), G380 (= G388)
- binding coenzyme a: L147 (= L153), H155 (≠ L165), M156 (= M166), R220 (≠ M229), T223 (≠ V231), A243 (= A251), P247 (≠ S255), L249 (≠ I257), H348 (= H356)
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)
50% identity, 98% coverage: 6:398/400 of query aligns to 4:391/393 of P14611
- C88 (= C93) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ R162) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ G227) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ P228) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S255) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H356) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C386) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
52% identity, 98% coverage: 7:398/400 of query aligns to 5:389/391 of 5f38B
- active site: C88 (= C93), H347 (= H356), C377 (= C386), G379 (= G388)
- binding coenzyme a: C88 (= C93), L149 (= L153), K219 (≠ M229), F234 (= F243), A242 (= A251), S246 (= S255), A317 (= A326), F318 (= F327), H347 (= H356)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
49% identity, 98% coverage: 6:398/400 of query aligns to 4:391/393 of 4o9cC
- active site: S88 (≠ C93), H349 (= H356), C379 (= C386), G381 (= G388)
- binding coenzyme a: S88 (≠ C93), L148 (= L153), R221 (≠ P228), F236 (= F243), A244 (= A251), S248 (= S255), L250 (≠ I257), A319 (= A326), F320 (= F327), H349 (= H356)
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)
46% identity, 100% coverage: 1:398/400 of query aligns to 1:396/398 of P41338
- M1 (= M1) modified: Initiator methionine, Removed
- S2 (= S2) modified: N-acetylserine
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
47% identity, 98% coverage: 6:398/400 of query aligns to 2:387/389 of 2vu2A
- active site: C86 (= C93), H345 (= H356), C375 (= C386), G377 (= G388)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ L165), M154 (= M166), F232 (= F243), S244 (= S255), G245 (≠ S256), F316 (= F327), H345 (= H356)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
47% identity, 98% coverage: 6:398/400 of query aligns to 2:387/389 of 1dm3A
- active site: C86 (= C93), H345 (= H356), C375 (= C386), G377 (= G388)
- binding acetyl coenzyme *a: C86 (= C93), L145 (= L153), H153 (≠ L165), M154 (= M166), R217 (≠ P228), S224 (≠ R235), M225 (≠ I236), A240 (= A251), S244 (= S255), M285 (≠ F296), A315 (= A326), F316 (= F327), H345 (= H356), C375 (= C386)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
47% identity, 98% coverage: 6:398/400 of query aligns to 2:387/389 of 1dlvA
- active site: C86 (= C93), H345 (= H356), C375 (= C386), G377 (= G388)
- binding coenzyme a: C86 (= C93), L145 (= L153), H153 (≠ L165), M154 (= M166), R217 (≠ P228), L228 (= L239), A240 (= A251), S244 (= S255), H345 (= H356)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
46% identity, 99% coverage: 2:398/400 of query aligns to 1:390/392 of 1ou6A
- active site: C89 (= C93), H348 (= H356), C378 (= C386), G380 (= G388)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L153), H156 (≠ L165), M157 (= M166), F235 (= F243), A243 (= A251), S247 (= S255), A318 (= A326), F319 (= F327), H348 (= H356)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
47% identity, 98% coverage: 6:398/400 of query aligns to 4:389/391 of 2vu1A
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
46% identity, 98% coverage: 6:398/400 of query aligns to 2:387/389 of 2wkuA
- active site: C86 (= C93), H345 (= H356), C375 (= C386), G377 (= G388)
- binding D-mannose: S6 (= S10), A7 (= A11), R38 (= R42), K182 (≠ R194), D194 (≠ W206), V280 (≠ G291), D281 (≠ A292), T287 (= T298), P331 (≠ M342), S332 (≠ E343), V334 (≠ I345), V336 (= V347), F360 (≠ G371)
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: 5:398/400 of query aligns to 4:390/392 of P07097
- Q64 (= Q68) mutation to A: Slightly lower activity.
- C89 (= C93) mutation to A: Loss of activity.
- C378 (= C386) mutation to G: Loss of activity.
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
46% identity, 98% coverage: 6:398/400 of query aligns to 3:388/390 of 1m1oA
- active site: A87 (≠ C93), H346 (= H356), C376 (= C386), G378 (= G388)
- binding acetoacetyl-coenzyme a: L86 (≠ V92), A87 (≠ C93), L146 (= L153), H154 (≠ L165), M155 (= M166), R218 (≠ P228), S225 (≠ R235), M226 (≠ I236), A241 (= A251), G242 (≠ A252), S245 (= S255), A316 (= A326), F317 (= F327), H346 (= H356), I377 (= I387), G378 (= G388)
Query Sequence
>HSERO_RS04635 FitnessBrowser__HerbieS:HSERO_RS04635
MSEDPVVIVSAARTAMGSFQGALADLPAPHLGAVAISAALQRAQLSAAQIAQIEQVWMGC
VLQAGLGQAPARQAALRAGLPQTVACATLNKVCGSAMQAVMLGHDSILAGSASMVVAGGM
ESMSNAPYLLPKARRGYRLGHDRLLDHMFLDGLEDAYSDQYRGRLMGTFAEDCASEFGFT
RAQQDAFAVQSTLRARQAISGGGFDWEVVPVDVAGKKGSVVISQDEGPMAVNLERIATLK
PAFSVDGTVTAANSSSISDGAAALLLMRESAALKQGLTPLARILGHASYAGAPEKFPTAP
IGVLRKIFAKTGLDAASTDLFEINEAFAVVPMAASRELDIDMEKINVHGGACALGHPIGA
SGARIIVSLLGALKARGLKTGIASLCIGGGEATAIALELS
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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