SitesBLAST
Comparing WP_083780269.1 NCBI__GCF_000092905.1:WP_083780269.1 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)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
59% identity, 90% coverage: 45:437/437 of query aligns to 2:391/394 of 7cw5B
- active site: C87 (= C130), H348 (= H394), C378 (= C424), G380 (= G426)
- binding coenzyme a: L147 (= L190), H155 (= H198), M156 (= M199), R220 (= R262), T223 (= T265), A243 (= A285), P247 (= P289), L249 (≠ V291), H348 (= H394)
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)
49% identity, 90% coverage: 44:436/437 of query aligns to 2:390/392 of P45359
- V77 (≠ W119) 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 (= C130) modified: Disulfide link with 378, In inhibited form
- S96 (≠ T138) binding acetate
- N153 (≠ H195) 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 (≠ AE 321:322) binding acetate
- A286 (= A328) 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 (= C424) modified: Disulfide link with 88, In inhibited form
- A386 (= A432) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
49% identity, 90% coverage: 44:436/437 of query aligns to 2:390/392 of 4xl4A
- active site: C88 (= C130), H348 (= H394), S378 (≠ C424), G380 (= G426)
- binding coenzyme a: L148 (= L190), H156 (= H198), R220 (= R262), L231 (= L273), A243 (= A285), S247 (≠ P289), F319 (= F361), H348 (= H394)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
49% identity, 90% coverage: 44:436/437 of query aligns to 4:393/394 of 5f38D
- active site: C90 (= C130), A348 (= A391), A378 (= A421), L380 (≠ I423)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C130), L151 (= L190), A246 (= A285), S250 (≠ P289), I252 (≠ V291), A321 (= A360), F322 (= F361), H351 (= H394)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
49% identity, 90% coverage: 44:436/437 of query aligns to 2:389/391 of 5f38B
- active site: C88 (= C130), H347 (= H394), C377 (= C424), G379 (= G426)
- binding coenzyme a: C88 (= C130), L149 (= L190), K219 (≠ R262), F234 (= F277), A242 (= A285), S246 (≠ P289), A317 (= A360), F318 (= F361), H347 (= H394)
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)
48% identity, 89% coverage: 48:436/437 of query aligns to 6:391/393 of P14611
- C88 (= C130) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (= H198) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ A260) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R262) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (≠ P289) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H394) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C424) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
43% identity, 90% coverage: 44:436/437 of query aligns to 2:390/393 of 6bn2A
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
48% identity, 89% coverage: 48:436/437 of query aligns to 6:391/393 of 4o9cC
- active site: S88 (≠ C130), H349 (= H394), C379 (= C424), G381 (= G426)
- binding coenzyme a: S88 (≠ C130), L148 (= L190), R221 (= R262), F236 (= F277), A244 (= A285), S248 (≠ P289), L250 (≠ V291), A319 (= A360), F320 (= F361), H349 (= H394)
8jg2A Crystal structure of a biosynthetic thiolase from megasphaera hexanoica soaked with hexanoyl-coa
45% identity, 90% coverage: 44:437/437 of query aligns to 3:391/393 of 8jg2A
A0R1Y7 Probable acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; EC 2.3.1.9 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
46% identity, 89% coverage: 48:435/437 of query aligns to 2:386/388 of A0R1Y7
- K187 (≠ D233) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
47% identity, 89% coverage: 48:436/437 of query aligns to 4:387/389 of 2vu2A
- active site: C86 (= C130), H345 (= H394), C375 (= C424), G377 (= G426)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (= H198), M154 (= M199), F232 (= F277), S244 (≠ P289), G245 (= G290), F316 (= F361), H345 (= H394)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
47% identity, 89% coverage: 48:436/437 of query aligns to 4:387/389 of 1dm3A
- active site: C86 (= C130), H345 (= H394), C375 (= C424), G377 (= G426)
- binding acetyl coenzyme *a: C86 (= C130), L145 (= L190), H153 (= H198), M154 (= M199), R217 (= R262), S224 (≠ Q269), M225 (≠ L270), A240 (= A285), S244 (≠ P289), M285 (≠ I330), A315 (= A360), F316 (= F361), H345 (= H394), C375 (= C424)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
47% identity, 89% coverage: 48:436/437 of query aligns to 4:387/389 of 1dlvA
- active site: C86 (= C130), H345 (= H394), C375 (= C424), G377 (= G426)
- binding coenzyme a: C86 (= C130), L145 (= L190), H153 (= H198), M154 (= M199), R217 (= R262), L228 (= L273), A240 (= A285), S244 (≠ P289), H345 (= H394)
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)
45% identity, 89% coverage: 48:436/437 of query aligns to 10:395/397 of Q9BWD1
- K211 (≠ R250) to R: in dbSNP:rs25683
- R223 (= R262) binding CoA
- S226 (≠ T265) binding CoA
- S252 (≠ P289) binding CoA
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
47% identity, 89% coverage: 48:436/437 of query aligns to 7:390/392 of 1ou6A
- active site: C89 (= C130), H348 (= H394), C378 (= C424), G380 (= G426)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L190), H156 (= H198), M157 (= M199), F235 (= F277), A243 (= A285), S247 (≠ P289), A318 (= A360), F319 (= F361), H348 (= H394)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
47% identity, 89% coverage: 48:436/437 of query aligns to 6:389/391 of 2vu1A
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
45% identity, 89% coverage: 48:436/437 of query aligns to 7:392/394 of 1wl4A
- active site: C89 (= C130), H350 (= H394), C380 (= C424), G382 (= G426)
- binding coenzyme a: L148 (= L190), M157 (= M199), R220 (= R262), Y234 (≠ V276), P245 (≠ A285), A246 (≠ G286), S249 (≠ P289), A320 (= A360), F321 (= F361), H350 (= H394)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
47% identity, 89% coverage: 48:436/437 of query aligns to 7:390/392 of P07097
- Q64 (= Q105) mutation to A: Slightly lower activity.
- C89 (= C130) mutation to A: Loss of activity.
- C378 (= C424) mutation to G: Loss of activity.
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
47% identity, 89% coverage: 48:436/437 of query aligns to 4:387/389 of 2wkuA
- active site: C86 (= C130), H345 (= H394), C375 (= C424), G377 (= G426)
- binding D-mannose: S6 (≠ G50), A7 (= A51), R38 (= R82), K182 (≠ R227), D194 (≠ E239), V280 (≠ A325), D281 (≠ E326), T287 (= T332), P331 (= P376), S332 (≠ D377), V334 (= V383), V336 (= V385), F360 (≠ Y409)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
47% identity, 89% coverage: 48:436/437 of query aligns to 5:388/390 of 1m1oA
- active site: A87 (≠ C130), H346 (= H394), C376 (= C424), G378 (= G426)
- binding acetoacetyl-coenzyme a: L86 (≠ V129), A87 (≠ C130), L146 (= L190), H154 (= H198), M155 (= M199), R218 (= R262), S225 (≠ Q269), M226 (≠ L270), A241 (= A285), G242 (= G286), S245 (≠ P289), A316 (= A360), F317 (= F361), H346 (= H394), I377 (≠ S425), G378 (= G426)
Query Sequence
>WP_083780269.1 NCBI__GCF_000092905.1:WP_083780269.1
MWWRCWTSRSTVNLKNARRFPGGRTSRPARVRLRFGGGRWRVARRTAVVGAARTPFGKLG
GALAAKKAVELGAAAIRGAMDRAGVGPDEVDELIMGMVLQGGAGQIPSRQAARLAGLPWE
LPTETINKVCASGLRAVTLGDQIIRAGDARAVVAGGMESMSQAPYAVFGAREGLRMGHGR
MVDLMIYDGLWCAFHDVHMAALGSRVAGEYGISREDQDLWALRSHRRAVAAMDAGRLGEE
IVPVEVQEKRGVRRVEQDEAPRRNTSLEQLAVLPPVFTKDGTVTAGNAPGVNDGAGALVL
MDEETARSEGKEVLAVIHGHAEVGAEAAYIATTPALAIQKLLKKAGRRLEDIRLFEINEA
FAAVVLTSAKLLEMSPDVLEEKVNVNGGAVALGHPIGASGARILMTLIYELRRRGGGLGV
AAICSGAAQGDAILIEV
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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