SitesBLAST
Comparing GFF2428 FitnessBrowser__psRCH2:GFF2428 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)
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)
45% identity, 98% coverage: 7:397/398 of query aligns to 1:391/392 of P45359
- V77 (≠ E84) 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 (= C95) modified: Disulfide link with 378, In inhibited form
- S96 (≠ I103) binding
- N153 (≠ G159) 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 (≠ AF 285:286) binding
- A286 (≠ Q292) 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 (= C384) modified: Disulfide link with 88, In inhibited form
- A386 (= A392) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
44% identity, 98% coverage: 7:397/398 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C95), H348 (= H354), S378 (≠ C384), G380 (= G386)
- binding coenzyme a: L148 (= L154), H156 (= H162), R220 (= R226), L231 (= L237), A243 (= A249), S247 (= S253), F319 (= F325), H348 (= H354)
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, 98% coverage: 7:397/398 of query aligns to 1:392/393 of P14611
- C88 (= C95) 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 (≠ H224) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R226) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S253) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H354) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C384) 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)
49% identity, 98% coverage: 7:398/398 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C95), H347 (= H354), C377 (= C384), G379 (= G386)
- binding coenzyme a: C88 (= C95), L149 (≠ I153), K219 (≠ R226), F234 (= F241), A242 (= A249), S246 (= S253), A317 (= A324), F318 (= F325), H347 (= H354)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
48% identity, 98% coverage: 6:397/398 of query aligns to 2:394/394 of 5f38D
- active site: C90 (= C95), A348 (= A351), A378 (≠ I381), L380 (≠ M383)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C95), L151 (≠ I153), A246 (= A249), S250 (= S253), I252 (≠ L255), A321 (= A324), F322 (= F325), H351 (= H354)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
48% identity, 98% coverage: 7:397/398 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C95), H349 (= H354), C379 (= C384), G381 (= G386)
- binding coenzyme a: S88 (≠ C95), L148 (= L154), R221 (= R226), F236 (= F241), A244 (= A249), S248 (= S253), L250 (= L255), A319 (= A324), F320 (= F325), H349 (= H354)
P42765 3-ketoacyl-CoA thiolase, mitochondrial; Acetyl-CoA acetyltransferase; Acetyl-CoA acyltransferase; Acyl-CoA hydrolase, mitochondrial; Beta-ketothiolase; Mitochondrial 3-oxoacyl-CoA thiolase; T1; EC 2.3.1.16; EC 2.3.1.9; EC 3.1.2.-; EC 3.1.2.1; EC 3.1.2.2 from Homo sapiens (Human) (see paper)
41% identity, 98% coverage: 7:396/398 of query aligns to 4:394/397 of P42765
- C92 (= C95) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R226) binding
- T227 (= T229) binding
- S251 (= S253) binding
- C382 (= C384) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
41% identity, 98% coverage: 7:396/398 of query aligns to 7:393/395 of 4c2jD
7feaB Py14 in complex with col-d (see paper)
45% identity, 98% coverage: 9:398/398 of query aligns to 4:393/396 of 7feaB
7ei4A Crystal structure of masl in complex with a novel covalent inhibitor, collimonin c (see paper)
45% identity, 98% coverage: 9:398/398 of query aligns to 3:390/392 of 7ei4A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
44% identity, 98% coverage: 10:398/398 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C95), H345 (= H354), C375 (= C384), G377 (= G386)
- 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 (= F241), S244 (= S253), G245 (≠ P254), F316 (= F325), H345 (= H354)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
44% identity, 98% coverage: 10:398/398 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C95), H345 (= H354), C375 (= C384), G377 (= G386)
- binding acetyl coenzyme *a: C86 (= C95), L145 (= L154), H153 (= H162), M154 (= M163), R217 (= R226), S224 (≠ G233), M225 (≠ L234), A240 (= A249), S244 (= S253), M285 (= M294), A315 (= A324), F316 (= F325), H345 (= H354), C375 (= C384)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
44% identity, 98% coverage: 10:398/398 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C95), H345 (= H354), C375 (= C384), G377 (= G386)
- binding coenzyme a: C86 (= C95), L145 (= L154), H153 (= H162), M154 (= M163), R217 (= R226), L228 (= L237), A240 (= A249), S244 (= S253), H345 (= H354)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
44% identity, 98% coverage: 10:398/398 of query aligns to 4:391/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
44% identity, 98% coverage: 10:398/398 of query aligns to 5:392/392 of 1ou6A
- active site: C89 (= C95), H348 (= H354), C378 (= C384), G380 (= G386)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L154), H156 (= H162), M157 (= M163), F235 (= F241), A243 (= A249), S247 (= S253), A318 (= A324), F319 (= F325), H348 (= H354)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
44% identity, 98% coverage: 10:398/398 of query aligns to 2:389/389 of 2wkuA
- active site: C86 (= C95), H345 (= H354), C375 (= C384), G377 (= G386)
- binding D-mannose: S6 (= S14), A7 (≠ G15), R38 (= R46), K182 (= K191), D194 (≠ T203), V280 (= V289), D281 (≠ E290), T287 (≠ L296), P331 (= P340), S332 (≠ D341), V334 (= V343), V336 (= V345), F360 (≠ Y369)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
44% identity, 98% coverage: 10:398/398 of query aligns to 3:390/390 of 1m1oA
- active site: A87 (≠ C95), H346 (= H354), C376 (= C384), G378 (= G386)
- binding acetoacetyl-coenzyme a: L86 (= L94), A87 (≠ C95), L146 (= L154), H154 (= H162), M155 (= M163), R218 (= R226), S225 (≠ G233), M226 (≠ L234), A241 (= A249), G242 (= G250), S245 (= S253), A316 (= A324), F317 (= F325), H346 (= H354), I377 (= I385), G378 (= G386)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
43% identity, 97% coverage: 11:398/398 of query aligns to 6:392/392 of P07097
- Q64 (≠ A70) mutation to A: Slightly lower activity.
- C89 (= C95) mutation to A: Loss of activity.
- C378 (= C384) mutation to G: Loss of activity.
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
40% identity, 97% coverage: 10:397/398 of query aligns to 5:393/394 of 1wl4A
- active site: C89 (= C95), H350 (= H354), C380 (= C384), G382 (= G386)
- binding coenzyme a: L148 (= L154), M157 (= M163), R220 (= R226), Y234 (≠ A240), P245 (≠ A249), A246 (≠ G250), S249 (= S253), A320 (= A324), F321 (= F325), H350 (= H354)
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)
40% identity, 97% coverage: 10:397/398 of query aligns to 8:396/397 of Q9BWD1
- K211 (≠ R214) to R: in dbSNP:rs25683
- R223 (= R226) binding
- S226 (≠ T229) binding
- S252 (= S253) binding
Query Sequence
>GFF2428 FitnessBrowser__psRCH2:GFF2428
MNDTVALQDVVILSGARTAIGDFGASLSGYSPAELGTFAGRAAIERAGVAAEEIDHCIFG
HIITTSPQDAYLARHVALNCGLAEHSAAMNVNRLCGSSVQSLISAAQMIQAGASRLALAG
GAESMSQGAYLLPKLRFGQRMGDAAAVDLTIGILSDPFGSGHMGITAENVAARYGFTREQ
LDQYACDSHRKAANAMAAGHLTTQIVSVPINKGRAAGEFSQDEHVRPDTTLEGLQKLRAA
FKKDGMVTAGNASPLNDGAAALVLGSAQEAARLGLRPRARFLSYAFAGVEPQLMGLGPIP
AVQRALTAANLRLADIDIIESNEAFAAQALAVAQSLEFDPDKVNVNGGAIAHGHPVGSTG
SILTLKALYELERLGKRHALITMCIGGGQGIALILERL
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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