SitesBLAST
Comparing N515DRAFT_3009 FitnessBrowser__Dyella79:N515DRAFT_3009 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)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
33% identity, 99% coverage: 6:427/427 of query aligns to 4:394/394 of 5f38D
- active site: C90 (= C92), A348 (= A381), A378 (≠ I411), L380 (≠ I413)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C92), L151 (≠ V169), A246 (= A259), S250 (≠ T263), I252 (≠ L265), A321 (= A337), F322 (= F338), H351 (= H384)
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)
35% identity, 94% coverage: 28:427/427 of query aligns to 14:392/393 of P14611
- C88 (= C92) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ S177) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (= F231) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R233) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (≠ T263) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H384) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C414) 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)
33% identity, 99% coverage: 6:427/427 of query aligns to 2:390/391 of 5f38B
- active site: C88 (= C92), H347 (= H384), C377 (= C414), G379 (≠ A416)
- binding coenzyme a: C88 (= C92), L149 (≠ V169), K219 (≠ R233), F234 (= F248), A242 (= A259), S246 (≠ T263), A317 (= A337), F318 (= F338), H347 (= H384)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
35% identity, 94% coverage: 28:427/427 of query aligns to 14:392/393 of 4o9cC
- active site: S88 (≠ C92), H349 (= H384), C379 (= C414), G381 (≠ A416)
- binding coenzyme a: S88 (≠ C92), L148 (≠ V169), R221 (= R233), F236 (= F248), A244 (= A259), S248 (≠ T263), L250 (= L265), A319 (= A337), F320 (= F338), H349 (= H384)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
32% identity, 95% coverage: 22:426/427 of query aligns to 7:390/394 of 7cw5B
- active site: C87 (= C92), H348 (= H384), C378 (= C414), G380 (≠ A416)
- binding coenzyme a: L147 (≠ F153), H155 (≠ S177), M156 (= M178), R220 (= R233), T223 (≠ S236), A243 (= A259), P247 (≠ T263), L249 (= L265), H348 (= H384)
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
30% identity, 97% coverage: 14:427/427 of query aligns to 9:397/400 of 5bz4K
- active site: C87 (= C92), H354 (= H384), C384 (= C414), G386 (≠ A416)
- binding coenzyme a: C87 (= C92), R146 (≠ K163), M160 (= M178), R220 (= R233), A246 (= A259), G247 (= G260), S250 (≠ T263), Q252 (≠ L265), M291 (≠ V302), A321 (= A337), F322 (= F338), H354 (= H384)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
32% identity, 95% coverage: 22:426/427 of query aligns to 16:387/389 of 2wkuA
- active site: C86 (= C92), H345 (= H384), C375 (= C414), G377 (≠ A416)
- binding D-mannose: R38 (= R44), K182 (= K206), D194 (= D218), V280 (= V299), D281 (= D300), T287 (≠ E305), P331 (= P370), S332 (≠ A371), V334 (≠ L373), V336 (= V375), F360 (≠ K399)
Sites not aligning to the query:
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
31% identity, 98% coverage: 10:426/427 of query aligns to 7:390/392 of P07097
- Q64 (≠ W67) mutation to A: Slightly lower activity.
- C89 (= C92) mutation to A: Loss of activity.
- C378 (= C414) mutation to G: Loss of activity.
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
32% identity, 95% coverage: 22:426/427 of query aligns to 19:390/392 of 1ou6A
- active site: C89 (= C92), H348 (= H384), C378 (= C414), G380 (≠ A416)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ V169), H156 (≠ S177), M157 (= M178), F235 (= F248), A243 (= A259), S247 (≠ T263), A318 (= A337), F319 (= F338), H348 (= H384)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
32% identity, 95% coverage: 22:426/427 of query aligns to 18:389/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
32% identity, 95% coverage: 22:426/427 of query aligns to 16:387/389 of 2vu2A
- active site: C86 (= C92), H345 (= H384), C375 (= C414), G377 (≠ A416)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ S177), M154 (= M178), F232 (= F248), S244 (≠ T263), G245 (= G264), F316 (= F338), H345 (= H384)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
32% identity, 95% coverage: 22:426/427 of query aligns to 16:387/389 of 1dm3A
- active site: C86 (= C92), H345 (= H384), C375 (= C414), G377 (≠ A416)
- binding acetyl coenzyme *a: C86 (= C92), L145 (≠ V169), H153 (≠ S177), M154 (= M178), R217 (= R233), S224 (≠ K240), M225 (≠ L241), A240 (= A259), S244 (≠ T263), M285 (≠ H303), A315 (= A337), F316 (= F338), H345 (= H384), C375 (= C414)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
32% identity, 95% coverage: 22:426/427 of query aligns to 16:387/389 of 1dlvA
- active site: C86 (= C92), H345 (= H384), C375 (= C414), G377 (≠ A416)
- binding coenzyme a: C86 (= C92), L145 (≠ V169), H153 (≠ S177), M154 (= M178), R217 (= R233), L228 (= L244), A240 (= A259), S244 (≠ T263), H345 (= H384)
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)
31% identity, 94% coverage: 28:427/427 of query aligns to 14:391/392 of P45359
- V77 (≠ P81) 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 (= C92) modified: Disulfide link with 378, In inhibited form
- S96 (≠ I100) binding
- N153 (≠ T174) 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 (≠ EV 295:296) binding
- A286 (≠ F301) 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 (= C414) modified: Disulfide link with 88, In inhibited form
- A386 (≠ T422) binding
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
31% identity, 95% coverage: 22:426/427 of query aligns to 17:388/390 of 1m1oA
- active site: A87 (≠ C92), H346 (= H384), C376 (= C414), G378 (≠ A416)
- binding acetoacetyl-coenzyme a: L86 (≠ A91), A87 (≠ C92), L146 (≠ V169), H154 (≠ S177), M155 (= M178), R218 (= R233), S225 (≠ K240), M226 (≠ L241), A241 (= A259), G242 (= G260), S245 (≠ T263), A316 (= A337), F317 (= F338), H346 (= H384), I377 (≠ T415), G378 (≠ A416)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
31% identity, 98% coverage: 6:425/427 of query aligns to 2:388/393 of 6bn2A
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
30% identity, 99% coverage: 6:427/427 of query aligns to 2:391/392 of 4xl4A
- active site: C88 (= C92), H348 (= H384), S378 (≠ C414), G380 (≠ A416)
- binding coenzyme a: L148 (= L162), H156 (≠ S177), R220 (vs. gap), L231 (= L244), A243 (= A259), S247 (≠ T263), F319 (= F338), H348 (= H384)
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)
29% identity, 95% coverage: 22:427/427 of query aligns to 22:396/397 of Q9BWD1
- K211 (≠ R224) to R: in dbSNP:rs25683
- R223 (= R233) binding
- S226 (= S236) binding
- S252 (≠ T263) binding
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
29% identity, 95% coverage: 22:427/427 of query aligns to 19:393/394 of 1wl4A
- active site: C89 (= C92), H350 (= H384), C380 (= C414), G382 (≠ A416)
- binding coenzyme a: L148 (≠ V169), M157 (= M178), R220 (= R233), Y234 (≠ A247), P245 (≠ A259), A246 (≠ G260), S249 (≠ T263), A320 (= A337), F321 (= F338), H350 (= H384)
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
30% identity, 99% coverage: 4:427/427 of query aligns to 3:389/390 of 2d3tC
- active site: C94 (= C92), H346 (= H384), C376 (= C414), G378 (≠ A416)
- binding acetyl coenzyme *a: C94 (= C92), R214 (= R233), L222 (= L241), L225 (= L244), A238 (= A259), G239 (= G260), S242 (≠ T263), I244 (≠ L265), A313 (= A337), F314 (= F338), H346 (= H384), C376 (= C414)
Query Sequence
>N515DRAFT_3009 FitnessBrowser__Dyella79:N515DRAFT_3009
MDNTPKRVGVIGGIRIPFCRNNTAYADVGNFGMSVKVLGALVERFRLHGEELGEVAMGAV
IKHSSEWNLAREAVLSSGLAPTTPGITTARACGTSLDNAIIIANKIAAGQIEAGIAGGSD
TTSDVPIVLGERFRKRLLAINRAKGWQDKMAAFTRGFSLKELKPSFPGVAEPRTGMSMGD
HCERMAKEWHIGREAQDRLALESHQKLAAAYEAGFFEDLVVPFRGLKRDGFLRADSSMEK
LGTLKPAFDKISGHGTLTAGNSTGLSDGAAAVLLGSDEWAARRGLKVQAYFLDAEVAAVD
FVHGEGLLMAPTVAVPRMLARHGLTLQDFDFYEIHEAFAAQVLCTLRAWESETYCRNRLG
LEQPLGSIDPAKLNVHGSSLAAGHPFAATGARIVATLAKMLEEKGSGRGLISICTAGGMG
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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