SitesBLAST
Comparing BPHYT_RS21955 FitnessBrowser__BFirm:BPHYT_RS21955 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)
7feaB Py14 in complex with col-d (see paper)
62% identity, 99% coverage: 4:393/395 of query aligns to 2:391/396 of 7feaB
7ei4A Crystal structure of masl in complex with a novel covalent inhibitor, collimonin c (see paper)
61% identity, 99% coverage: 4:393/395 of query aligns to 1:388/392 of 7ei4A
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)
49% identity, 98% coverage: 5:393/395 of query aligns to 2:390/392 of P45359
- V77 (= V80) 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 (= C91) modified: Disulfide link with 378, In inhibited form
- S96 (≠ A99) binding
- N153 (≠ S156) 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 (≠ GV 282:283) binding
- A286 (≠ G289) 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 (= C381) modified: Disulfide link with 88, In inhibited form
- A386 (= A389) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
49% identity, 98% coverage: 5:393/395 of query aligns to 2:390/392 of 4xl4A
- active site: C88 (= C91), H348 (= H351), S378 (≠ C381), G380 (= G383)
- binding coenzyme a: L148 (= L151), H156 (= H159), R220 (= R223), L231 (= L234), A243 (= A246), S247 (≠ P250), F319 (= F322), H348 (= H351)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
49% identity, 99% coverage: 2:393/395 of query aligns to 1:393/394 of 5f38D
- active site: C90 (= C91), A348 (= A348), A378 (≠ V378), L380 (= L380)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C91), L151 (= L151), A246 (= A246), S250 (≠ P250), I252 (≠ L252), A321 (= A321), F322 (= F322), H351 (= H351)
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, 98% coverage: 7:393/395 of query aligns to 8:395/397 of Q9BWD1
- K211 (= K211) to R: in dbSNP:rs25683
- R223 (= R223) binding
- S226 (≠ T226) binding
- S252 (≠ P250) binding
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
45% identity, 98% coverage: 7:393/395 of query aligns to 5:392/394 of 1wl4A
- active site: C89 (= C91), H350 (= H351), C380 (= C381), G382 (= G383)
- binding coenzyme a: L148 (= L151), M157 (≠ S160), R220 (= R223), Y234 (≠ A237), P245 (≠ A246), A246 (≠ G247), S249 (≠ P250), A320 (= A321), F321 (= F322), H350 (= H351)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
48% identity, 99% coverage: 5:395/395 of query aligns to 2:391/391 of 5f38B
- active site: C88 (= C91), H347 (= H351), C377 (= C381), G379 (= G383)
- binding coenzyme a: C88 (= C91), L149 (= L151), K219 (≠ R223), F234 (= F238), A242 (= A246), S246 (≠ P250), A317 (= A321), F318 (= F322), H347 (= H351)
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)
47% identity, 98% coverage: 6:393/395 of query aligns to 3:391/393 of P14611
- C88 (= C91) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (= H159) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ Q221) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R223) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (≠ P250) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H351) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C381) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
47% identity, 98% coverage: 6:393/395 of query aligns to 3:391/393 of 4o9cC
- active site: S88 (≠ C91), H349 (= H351), C379 (= C381), G381 (= G383)
- binding coenzyme a: S88 (≠ C91), L148 (= L151), R221 (= R223), F236 (= F238), A244 (= A246), S248 (≠ P250), L250 (= L252), A319 (= A321), F320 (= F322), H349 (= H351)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
46% identity, 98% coverage: 6:394/395 of query aligns to 2:391/394 of 7cw5B
- active site: C87 (= C91), H348 (= H351), C378 (= C381), G380 (= G383)
- binding coenzyme a: L147 (= L151), H155 (= H159), M156 (≠ S160), R220 (= R223), T223 (= T226), A243 (= A246), P247 (= P250), L249 (= L252), H348 (= H351)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
45% identity, 99% coverage: 6:395/395 of query aligns to 1:389/389 of 2vu2A
- active site: C86 (= C91), H345 (= H351), C375 (= C381), G377 (= G383)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (= H159), M154 (≠ S160), F232 (= F238), S244 (≠ P250), G245 (= G251), F316 (= F322), H345 (= H351)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
45% identity, 99% coverage: 6:395/395 of query aligns to 1:389/389 of 1dm3A
- active site: C86 (= C91), H345 (= H351), C375 (= C381), G377 (= G383)
- binding acetyl coenzyme *a: C86 (= C91), L145 (= L151), H153 (= H159), M154 (≠ S160), R217 (= R223), S224 (≠ T230), M225 (≠ L231), A240 (= A246), S244 (≠ P250), M285 (≠ F291), A315 (= A321), F316 (= F322), H345 (= H351), C375 (= C381)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
45% identity, 99% coverage: 6:395/395 of query aligns to 1:389/389 of 1dlvA
- active site: C86 (= C91), H345 (= H351), C375 (= C381), G377 (= G383)
- binding coenzyme a: C86 (= C91), L145 (= L151), H153 (= H159), M154 (≠ S160), R217 (= R223), L228 (= L234), A240 (= A246), S244 (≠ P250), H345 (= H351)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
45% identity, 99% coverage: 6:395/395 of query aligns to 4:392/392 of 1ou6A
- active site: C89 (= C91), H348 (= H351), C378 (= C381), G380 (= G383)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L151), H156 (= H159), M157 (≠ S160), F235 (= F238), A243 (= A246), S247 (≠ P250), A318 (= A321), F319 (= F322), H348 (= H351)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
45% identity, 99% coverage: 6:395/395 of query aligns to 3:391/391 of 2vu1A
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
44% identity, 99% coverage: 6:395/395 of query aligns to 1:389/389 of 2wkuA
- active site: C86 (= C91), H345 (= H351), C375 (= C381), G377 (= G383)
- binding D-mannose: S6 (≠ N11), A7 (≠ P12), R38 (= R43), K182 (≠ R188), D194 (≠ A200), V280 (= V286), D281 (≠ E287), T287 (≠ L293), P331 (≠ D337), S332 (≠ E338), V334 (≠ I340), V336 (= V342), F360 (≠ H366)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
44% identity, 99% coverage: 6:395/395 of query aligns to 2:390/390 of 1m1oA
- active site: A87 (≠ C91), H346 (= H351), C376 (= C381), G378 (= G383)
- binding acetoacetyl-coenzyme a: L86 (≠ V90), A87 (≠ C91), L146 (= L151), H154 (= H159), M155 (≠ S160), R218 (= R223), S225 (≠ T230), M226 (≠ L231), A241 (= A246), G242 (= G247), S245 (≠ P250), A316 (= A321), F317 (= F322), H346 (= H351), I377 (= I382), G378 (= G383)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
44% identity, 98% coverage: 8:395/395 of query aligns to 6:392/392 of P07097
- Q64 (≠ M66) mutation to A: Slightly lower activity.
- C89 (= C91) mutation to A: Loss of activity.
- C378 (= C381) mutation to G: Loss of activity.
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
41% identity, 98% coverage: 5:393/395 of query aligns to 2:390/393 of 6bn2A
Query Sequence
>BPHYT_RS21955 FitnessBrowser__BFirm:BPHYT_RS21955
MANQREVVICNPVRTPIGAFGGALKEVPATTLGAVAVRETLRRSRLDAAELASVVMGNVI
QAGNKMNAARQASIGGGVPVAVPALTVNRVCGSGAQAIASAAQEILLGLGDAAVAGGMEN
MDRAPYLLDGGRWGYRMGNAQIHDSLLRDGLNDAFSGEHSGWHTEDLVAQFDITRETQDR
WAARSQQRFSEAQARGDFDAELVGVEIAGRKGPQHFTRDEQPRPDTTVETLAKLRPAFRP
DGTITAGNAPGLNSGAAAMLVAERGFAEARGIAPLARLVSYGVAAVEPGMFGLGPVPAVQ
MALARAGWQLHDVERFEINEAFAAVPIAVARKLGIADELINVRGGAIAHGHPIGATGAVL
TTRLLHSMQRDGIKRGIVTLCIGGGQGIALALEML
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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