SitesBLAST
Comparing GFF3052 FitnessBrowser__Marino:GFF3052 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)
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)
69% identity, 98% coverage: 7:398/398 of query aligns to 1:392/393 of P14611
- C88 (= C94) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (= H162) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ G225) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R227) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S254) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H355) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C385) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
69% identity, 98% coverage: 7:398/398 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C94), H349 (= H355), C379 (= C385), G381 (= G387)
- binding coenzyme a: S88 (≠ C94), L148 (= L154), R221 (= R227), F236 (= F242), A244 (= A250), S248 (= S254), L250 (= L256), A319 (= A325), F320 (= F326), H349 (= H355)
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)
60% identity, 98% coverage: 7:398/398 of query aligns to 1:391/392 of P45359
- V77 (≠ A83) 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 (= C94) modified: Disulfide link with 378, In inhibited form
- S96 (≠ H102) binding
- N153 (= N159) 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 (≠ AN 286:287) binding
- A286 (≠ T293) 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 (= C385) modified: Disulfide link with 88, In inhibited form
- A386 (= A393) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
60% identity, 98% coverage: 7:398/398 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C94), H348 (= H355), S378 (≠ C385), G380 (= G387)
- binding coenzyme a: L148 (= L154), H156 (= H162), R220 (= R227), L231 (= L238), A243 (= A250), S247 (= S254), F319 (= F326), H348 (= H355)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
59% identity, 97% coverage: 10:397/398 of query aligns to 2:387/389 of 2vu2A
- active site: C86 (= C94), H345 (= H355), C375 (= C385), G377 (= G387)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (= H162), M154 (= M163), F232 (= F242), S244 (= S254), G245 (≠ S255), F316 (= F326), H345 (= H355)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
59% identity, 97% coverage: 10:397/398 of query aligns to 2:387/389 of 1dm3A
- active site: C86 (= C94), H345 (= H355), C375 (= C385), G377 (= G387)
- binding acetyl coenzyme *a: C86 (= C94), L145 (= L154), H153 (= H162), M154 (= M163), R217 (= R227), S224 (≠ G234), M225 (≠ L235), A240 (= A250), S244 (= S254), M285 (= M295), A315 (= A325), F316 (= F326), H345 (= H355), C375 (= C385)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
59% identity, 97% coverage: 10:397/398 of query aligns to 2:387/389 of 1dlvA
- active site: C86 (= C94), H345 (= H355), C375 (= C385), G377 (= G387)
- binding coenzyme a: C86 (= C94), L145 (= L154), H153 (= H162), M154 (= M163), R217 (= R227), L228 (= L238), A240 (= A250), S244 (= S254), H345 (= H355)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
59% identity, 97% coverage: 10:397/398 of query aligns to 5:390/392 of 1ou6A
- active site: C89 (= C94), H348 (= H355), C378 (= C385), G380 (= G387)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L154), H156 (= H162), M157 (= M163), F235 (= F242), A243 (= A250), S247 (= S254), A318 (= A325), F319 (= F326), H348 (= H355)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
59% identity, 97% coverage: 10:397/398 of query aligns to 4:389/391 of 2vu1A
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
59% identity, 97% coverage: 10:397/398 of query aligns to 2:387/389 of 2wkuA
- active site: C86 (= C94), H345 (= H355), C375 (= C385), G377 (= G387)
- binding D-mannose: S6 (≠ A14), A7 (= A15), R38 (≠ E46), K182 (= K191), D194 (≠ G203), V280 (= V290), D281 (= D291), T287 (= T297), P331 (≠ T341), S332 (≠ G342), V334 (= V344), V336 (= V346), F360 (≠ H370)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
59% identity, 97% coverage: 10:397/398 of query aligns to 3:388/390 of 1m1oA
- active site: A87 (≠ C94), H346 (= H355), C376 (= C385), G378 (= G387)
- binding acetoacetyl-coenzyme a: L86 (≠ V93), A87 (≠ C94), L146 (= L154), H154 (= H162), M155 (= M163), R218 (= R227), S225 (≠ G234), M226 (≠ L235), A241 (= A250), G242 (= G251), S245 (= S254), A316 (= A325), F317 (= F326), H346 (= H355), I377 (= I386), G378 (= G387)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
58% identity, 97% coverage: 11:397/398 of query aligns to 6:390/392 of P07097
- Q64 (= Q69) mutation to A: Slightly lower activity.
- C89 (= C94) mutation to A: Loss of activity.
- C378 (= C385) mutation to G: Loss of activity.
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
55% identity, 98% coverage: 7:398/398 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C94), A348 (= A352), A378 (= A382), L380 (= L384)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C94), L151 (= L154), A246 (= A250), S250 (= S254), I252 (≠ L256), A321 (= A325), F322 (= F326), H351 (= H355)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
55% identity, 98% coverage: 7:398/398 of query aligns to 1:390/391 of 5f38B
- active site: C88 (= C94), H347 (= H355), C377 (= C385), G379 (= G387)
- binding coenzyme a: C88 (= C94), L149 (= L154), K219 (≠ R227), F234 (= F242), A242 (= A250), S246 (= S254), A317 (= A325), F318 (= F326), H347 (= H355)
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
51% identity, 98% coverage: 10:398/398 of query aligns to 5:393/394 of 1wl4A
- active site: C89 (= C94), H350 (= H355), C380 (= C385), G382 (= G387)
- binding coenzyme a: L148 (= L154), M157 (= M163), R220 (= R227), Y234 (≠ A241), P245 (≠ A250), A246 (≠ G251), S249 (= S254), A320 (= A325), F321 (= F326), H350 (= H355)
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)
51% identity, 98% coverage: 10:398/398 of query aligns to 8:396/397 of Q9BWD1
- K211 (= K214) to R: in dbSNP:rs25683
- R223 (= R227) binding
- S226 (≠ V230) binding
- S252 (= S254) binding
7feaB Py14 in complex with col-d (see paper)
50% identity, 98% coverage: 9:398/398 of query aligns to 4:392/396 of 7feaB
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)
51% identity, 97% coverage: 11:398/398 of query aligns to 1:388/388 of A0R1Y7
- K187 (≠ E197) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7ei4A Crystal structure of masl in complex with a novel covalent inhibitor, collimonin c (see paper)
49% identity, 98% coverage: 9:398/398 of query aligns to 3:389/392 of 7ei4A
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
49% identity, 97% coverage: 11:397/398 of query aligns to 4:390/394 of 7cw5B
- active site: C87 (= C94), H348 (= H355), C378 (= C385), G380 (= G387)
- binding coenzyme a: L147 (= L154), H155 (= H162), M156 (= M163), R220 (= R227), T223 (≠ V230), A243 (= A250), P247 (≠ S254), L249 (= L256), H348 (= H355)
Query Sequence
>GFF3052 FitnessBrowser__Marino:GFF3052
MIRRIPMRDVVIVAARRTAIGTFGGGLSSLSADQLGTAVIKAILEETGVAGDQINEVVLG
QVLTAGCGQNPARQSAINAGIPASVPAMTINKVCGSGLKAVHMAVQAIRCGDAEMMIAGG
QESMSQAPHVLPNSRNGQRMGNWSMVDTMIKDGLWDAFNDYHMGITAENIVEKYGISRDE
QDEFAAASQQKAAAAREAGYFDGQIVPVSIPQRKGDPIVVDRDEGPRDGVTAEGLGKLRA
AFKKDGTVTAGNASSLNDGAAAVMVCSAEKAEELGLTPIATIKAYANAGVDPTIMGTGPI
PASQRCLKLAGWSTEDLDLVEANEAFAAQAISVNRDMGWDTGKVNVNGGAIALGHPIGAS
GCRILVSLLHEMVRRDVHKGLATLCIGGGMGVALAVER
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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