SitesBLAST
Comparing WP_093396488.1 NCBI__GCF_900114975.1:WP_093396488.1 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)
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
43% identity, 99% coverage: 4:411/414 of query aligns to 3:396/400 of 5bz4K
- active site: C87 (= C88), H354 (= H369), C384 (= C399), G386 (= G401)
- binding coenzyme a: C87 (= C88), R146 (= R161), M160 (= M176), R220 (= R240), A246 (= A261), G247 (= G262), S250 (= S265), Q252 (≠ E267), M291 (≠ T306), A321 (= A336), F322 (= F337), H354 (= H369)
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)
40% identity, 99% coverage: 1:411/414 of query aligns to 1:390/392 of P45359
- V77 (≠ D77) 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 (= C88) modified: Disulfide link with 378, In inhibited form
- S96 (≠ R96) binding acetate
- N153 (≠ Q158) 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 (≠ DV 297:298) binding acetate
- A286 (≠ R304) 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 (= C399) modified: Disulfide link with 88, In inhibited form
- A386 (= A407) binding acetate
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)
44% identity, 99% coverage: 1:411/414 of query aligns to 1:391/393 of P14611
- C88 (= C88) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ Q165) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ T238) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R240) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S265) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H369) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C399) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
40% identity, 99% coverage: 1:411/414 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C88), H348 (= H369), S378 (≠ C399), G380 (= G401)
- binding coenzyme a: L148 (= L153), H156 (≠ R161), R220 (= R240), L231 (= L251), A243 (= A261), S247 (= S265), F319 (= F337), H348 (= H369)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
39% identity, 99% coverage: 3:411/414 of query aligns to 2:390/394 of 7cw5B
- active site: C87 (= C88), H348 (= H369), C378 (= C399), G380 (= G401)
- binding coenzyme a: L147 (≠ I157), H155 (≠ Q165), M156 (= M176), R220 (= R240), T223 (= T243), A243 (= A261), P247 (≠ S265), L249 (≠ E267), H348 (= H369)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
43% identity, 99% coverage: 1:411/414 of query aligns to 1:391/393 of 4o9cC
- active site: S88 (≠ C88), H349 (= H369), C379 (= C399), G381 (= G401)
- binding coenzyme a: S88 (≠ C88), L148 (≠ I157), R221 (= R240), F236 (≠ L255), A244 (= A261), S248 (= S265), L250 (≠ E267), A319 (= A336), F320 (= F337), H349 (= H369)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
42% identity, 99% coverage: 1:411/414 of query aligns to 3:393/394 of 5f38D
- active site: C90 (= C88), A348 (≠ S366), A378 (≠ E396), L380 (≠ I398)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C88), L151 (≠ V162), A246 (= A261), S250 (= S265), I252 (≠ E267), A321 (= A336), F322 (= F337), H351 (= H369)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
42% identity, 99% coverage: 1:411/414 of query aligns to 1:389/391 of 5f38B
- active site: C88 (= C88), H347 (= H369), C377 (= C399), G379 (= G401)
- binding coenzyme a: C88 (= C88), L149 (≠ V162), K219 (≠ R240), F234 (≠ L255), A242 (= A261), S246 (= S265), A317 (= A336), F318 (= F337), H347 (= H369)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
36% identity, 99% coverage: 1:411/414 of query aligns to 1:390/393 of 6bn2A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
39% identity, 99% coverage: 5:412/414 of query aligns to 3:388/389 of 2vu2A
- active site: C86 (= C88), H345 (= H369), C375 (= C399), G377 (= G401)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ S175), M154 (= M176), F232 (≠ L255), S244 (= S265), G245 (≠ S266), F316 (= F337), H345 (= H369)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
39% identity, 99% coverage: 5:412/414 of query aligns to 3:388/389 of 1dm3A
- active site: C86 (= C88), H345 (= H369), C375 (= C399), G377 (= G401)
- binding acetyl coenzyme *a: C86 (= C88), L145 (≠ I157), H153 (≠ S175), M154 (= M176), R217 (= R240), S224 (≠ K247), M225 (≠ L248), A240 (= A261), S244 (= S265), M285 (≠ Y307), A315 (= A336), F316 (= F337), H345 (= H369), C375 (= C399)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
39% identity, 99% coverage: 5:412/414 of query aligns to 3:388/389 of 1dlvA
- active site: C86 (= C88), H345 (= H369), C375 (= C399), G377 (= G401)
- binding coenzyme a: C86 (= C88), L145 (≠ I157), H153 (≠ S175), M154 (= M176), R217 (= R240), L228 (= L251), A240 (= A261), S244 (= S265), H345 (= H369)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
39% identity, 99% coverage: 5:412/414 of query aligns to 3:388/389 of 2wkuA
- active site: C86 (= C88), H345 (= H369), C375 (= C399), G377 (= G401)
- binding D-mannose: S6 (= S8), A7 (= A9), R38 (= R40), K182 (≠ N204), D194 (≠ E216), V280 (≠ C301), D281 (= D302), T287 (≠ S309), P331 (≠ E352), S332 (≠ K353), V334 (≠ I358), V336 (= V360), F360 (≠ H384)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
39% identity, 99% coverage: 5:412/414 of query aligns to 5:390/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
39% identity, 99% coverage: 5:412/414 of query aligns to 6:391/392 of 1ou6A
- active site: C89 (= C88), H348 (= H369), C378 (= C399), G380 (= G401)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ I157), H156 (≠ S175), M157 (= M176), F235 (≠ L255), A243 (= A261), S247 (= S265), A318 (= A336), F319 (= F337), H348 (= H369)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
38% identity, 99% coverage: 4:412/414 of query aligns to 5:391/392 of P07097
- Q64 (≠ V63) mutation to A: Slightly lower activity.
- C89 (= C88) mutation to A: Loss of activity.
- C378 (= C399) mutation to G: Loss of activity.
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
39% identity, 99% coverage: 5:412/414 of query aligns to 4:389/390 of 1m1oA
- active site: A87 (≠ C88), H346 (= H369), C376 (= C399), G378 (= G401)
- binding acetoacetyl-coenzyme a: L86 (≠ R87), A87 (≠ C88), L146 (≠ I157), H154 (≠ S175), M155 (= M176), R218 (= R240), S225 (≠ K247), M226 (≠ L248), A241 (= A261), G242 (= G262), S245 (= S265), A316 (= A336), F317 (= F337), H346 (= H369), I377 (≠ G400), G378 (= G401)
8jg2A Crystal structure of a biosynthetic thiolase from megasphaera hexanoica soaked with hexanoyl-coa
37% identity, 99% coverage: 1:411/414 of query aligns to 2:390/393 of 8jg2A
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)
39% identity, 98% coverage: 6:411/414 of query aligns to 9:396/398 of Q4WCL5
- Y187 (≠ H202) binding K(+)
- N229 (≠ S244) binding CoA
- K232 (= K247) binding CoA
- A249 (= A261) binding K(+)
- P250 (≠ G262) binding K(+)
- S252 (= S264) binding K(+)
- S253 (= S265) binding CoA
- V350 (≠ I365) binding K(+)
- N385 (≠ G400) binding chloride
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
39% identity, 98% coverage: 6:411/414 of query aligns to 10:397/399 of 6aqpC
- active site: C93 (= C88), H355 (= H369), C385 (= C399), G387 (= G401)
- binding acetyl coenzyme *a: C93 (= C88), L153 (≠ I167), M162 (= M176), Y188 (≠ H202), N230 (≠ S244), K233 (= K247), L234 (= L248), I237 (≠ L251), A250 (= A261), P251 (≠ G262), S254 (= S265), F295 (≠ T306), A325 (= A336), F326 (= F337), H355 (= H369)
Query Sequence
>WP_093396488.1 NCBI__GCF_900114975.1:WP_093396488.1
MEKAVIVSAVRTPVGRYLGSLRSVEAYDLAALVLKEAVARAGLSPDQVDEVVMGQSYQNG
EYVNIARMALLKAGWPDSIPGITLDRRCCSGLEVVRYAASLIATGQAEVVVAGGVESMSN
AEFYLPGHIKWGIGGREGMPRGHGDLKIWGIPLYDRIQRARVMHQPIERYGVLQSMMTWA
ETAAREEGISREECDAWALRSHQNACRAWREGKFQEEVVPVPVRGSDGSDTLFERDETPR
EDTSLEKLSRLKPVLGGVCTAGNSSSENDGAAAVLVMSERKAREFGLRPMARFLACDVAA
CDPRKTYLSVPIAVKKVLSRTGLKLEDMGLIEIQEAFAAQVLADMKQMGLDEKDYDRINV
NGSGISLGHPIACTGTRVLVTLLHEMKRRGVKYGLECICGGGGLGIAAVMEAGE
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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