SitesBLAST
Comparing HSERO_RS20660 FitnessBrowser__HerbieS:HSERO_RS20660 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)
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
70% identity, 100% coverage: 2:400/401 of query aligns to 6:403/403 of 6pccA
- active site: C93 (= C89), A359 (≠ H356), C389 (= C386), G391 (= G388)
- binding coenzyme a: C93 (= C89), I148 (= I144), R229 (= R226), T232 (= T229), A252 (= A249), S256 (= S253), N325 (= N322), F328 (= F325)
- binding hexanal: N61 (= N57), T146 (= T142), I148 (= I144), G149 (= G145), R151 (= R147), L361 (= L358)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
70% identity, 100% coverage: 2:400/401 of query aligns to 6:403/403 of 6pcbA
- active site: C93 (= C89), A359 (≠ H356), C389 (= C386), G391 (= G388)
- binding coenzyme a: C93 (= C89), I148 (= I144), R229 (= R226), A252 (= A249), S256 (= S253), G257 (= G254), N325 (= N322), F328 (= F325)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
69% identity, 100% coverage: 2:400/401 of query aligns to 7:401/401 of 6pcdA
- active site: S94 (≠ C89), A357 (≠ H356), C387 (= C386), G389 (= G388)
- binding coenzyme a: I149 (= I144), M167 (= M162), R227 (= R226), T230 (= T229), A250 (= A249), S254 (= S253), G255 (= G254), A325 (= A324), A357 (≠ H356)
- binding octanal: N62 (= N57), T147 (= T142), T148 (= T143), I149 (= I144), G150 (= G145), R152 (= R147), L359 (= L358)
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
44% identity, 100% coverage: 2:400/401 of query aligns to 2:398/400 of 5bz4K
- active site: C87 (= C89), H354 (= H356), C384 (= C386), G386 (= G388)
- binding coenzyme a: C87 (= C89), R146 (vs. gap), M160 (= M162), R220 (= R226), A246 (= A249), G247 (= G250), S250 (= S253), Q252 (≠ V255), M291 (= M294), A321 (= A324), F322 (= F325), H354 (= H356)
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)
43% identity, 99% coverage: 2:399/401 of query aligns to 3:391/392 of P45359
- V77 (≠ I78) 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 (= C89) modified: Disulfide link with 378, In inhibited form
- S96 (≠ G97) binding
- N153 (≠ M153) 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 (≠ AT 285:286) binding
- A286 (≠ R292) 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 (= C386) modified: Disulfide link with 88, In inhibited form
- A386 (= A394) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
43% identity, 99% coverage: 2:399/401 of query aligns to 3:391/392 of 4xl4A
- active site: C88 (= C89), H348 (= H356), S378 (≠ C386), G380 (= G388)
- binding coenzyme a: L148 (≠ F148), H156 (≠ Q156), R220 (= R226), L231 (= L237), A243 (= A249), S247 (= S253), F319 (= F325), H348 (= H356)
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)
42% identity, 99% coverage: 4:401/401 of query aligns to 8:397/397 of P42765
- C92 (= C89) 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 (= C386) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
44% identity, 100% coverage: 2:400/401 of query aligns to 6:390/390 of 2d3tC
- active site: C94 (= C89), H346 (= H356), C376 (= C386), G378 (= G388)
- binding acetyl coenzyme *a: C94 (= C89), R214 (= R226), L222 (= L234), L225 (= L237), A238 (= A249), G239 (= G250), S242 (= S253), I244 (≠ V255), A313 (= A324), F314 (= F325), H346 (= H356), C376 (= C386)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
41% identity, 99% coverage: 4:398/401 of query aligns to 11:393/395 of 4c2jD
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)
43% identity, 99% coverage: 2:399/401 of query aligns to 3:392/393 of P14611
- C88 (= C89) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ S161) 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 (= H356) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C386) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
43% identity, 99% coverage: 2:399/401 of query aligns to 3:392/393 of 4o9cC
- active site: S88 (≠ C89), H349 (= H356), C379 (= C386), G381 (= G388)
- binding coenzyme a: S88 (≠ C89), L148 (vs. gap), R221 (= R226), F236 (≠ V241), A244 (= A249), S248 (= S253), L250 (≠ V255), A319 (= A324), F320 (= F325), H349 (= H356)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
43% identity, 99% coverage: 4:400/401 of query aligns to 3:389/389 of 2vu2A
- active site: C86 (= C89), H345 (= H356), C375 (= C386), G377 (= G388)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ S161), M154 (= M162), F232 (≠ V241), S244 (= S253), G245 (= G254), F316 (= F325), H345 (= H356)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
43% identity, 99% coverage: 4:400/401 of query aligns to 3:389/389 of 1dm3A
- active site: C86 (= C89), H345 (= H356), C375 (= C386), G377 (= G388)
- binding acetyl coenzyme *a: C86 (= C89), L145 (= L152), H153 (≠ S161), M154 (= M162), R217 (= R226), S224 (≠ T233), M225 (≠ L234), A240 (= A249), S244 (= S253), M285 (= M294), A315 (= A324), F316 (= F325), H345 (= H356), C375 (= C386)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
43% identity, 99% coverage: 4:400/401 of query aligns to 3:389/389 of 1dlvA
- active site: C86 (= C89), H345 (= H356), C375 (= C386), G377 (= G388)
- binding coenzyme a: C86 (= C89), L145 (= L152), H153 (≠ S161), M154 (= M162), R217 (= R226), L228 (= L237), A240 (= A249), S244 (= S253), H345 (= H356)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
43% identity, 99% coverage: 4:400/401 of query aligns to 6:392/392 of 1ou6A
- active site: C89 (= C89), H348 (= H356), C378 (= C386), G380 (= G388)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L152), H156 (≠ S161), M157 (= M162), F235 (≠ V241), A243 (= A249), S247 (= S253), A318 (= A324), F319 (= F325), H348 (= H356)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
43% identity, 99% coverage: 3:400/401 of query aligns to 5:392/392 of P07097
- Q64 (≠ R64) mutation to A: Slightly lower activity.
- C89 (= C89) mutation to A: Loss of activity.
- C378 (= C386) mutation to G: Loss of activity.
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
43% identity, 99% coverage: 4:400/401 of query aligns to 5:391/391 of 2vu1A
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
43% identity, 99% coverage: 4:400/401 of query aligns to 3:389/389 of 2wkuA
- active site: C86 (= C89), H345 (= H356), C375 (= C386), G377 (= G388)
- binding D-mannose: S6 (≠ D7), A7 (= A8), R38 (= R39), K182 (≠ R190), D194 (≠ G202), V280 (= V289), D281 (≠ A290), T287 (≠ F296), P331 (≠ A342), S332 (≠ A343), V334 (= V345), V336 (≠ P347), F360 (≠ N371)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
43% identity, 99% coverage: 4:400/401 of query aligns to 4:390/390 of 1m1oA
- active site: A87 (≠ C89), H346 (= H356), C376 (= C386), G378 (= G388)
- binding acetoacetyl-coenzyme a: L86 (= L88), A87 (≠ C89), L146 (= L152), H154 (≠ S161), M155 (= M162), R218 (= R226), S225 (≠ T233), M226 (≠ L234), A241 (= A249), G242 (= G250), S245 (= S253), A316 (= A324), F317 (= F325), H346 (= H356), I377 (= I387), G378 (= G388)
8oqlC Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-1
40% identity, 100% coverage: 2:400/401 of query aligns to 3:397/397 of 8oqlC
Query Sequence
>HSERO_RS20660 FitnessBrowser__HerbieS:HSERO_RS20660
MEALICDAIRTPFGRYGGALGAVRADDLAAAPIRSLMERNPGVDWSRVEDILYGCANQAG
EDNRNVARMAGLLAGLPIAVPGSTVNRLCGSSLDAVGMAARAIKSGEVQLMIAGGVESMT
RAPFVMGKAESAFARSAAIFDTTIGWRFVNPLMKAQYGIDSMPETAENVATDFQINRADQ
DAFALRSQQRWAAAQAAGFFAGEIAPLTIPQKKGDPLVVTTDEHPRPDTTLATLAKLKGV
VRPDGTVTAGNASGVNDGACALLLASPKAADLYRLKPRARVLGMATAGVAPRIMGFGPAP
AVRKVLAQVGLTLAQMDVIELNEAFAAQGLAVMRDLGLPDDAAHVNPNGGAIAIGHPLGA
SGARLVTTAINQLERSGGRYALCTMCIGVGQGIALVIERVA
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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