SitesBLAST
Comparing RR42_RS31890 FitnessBrowser__Cup4G11:RR42_RS31890 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)
P09110 3-ketoacyl-CoA thiolase, peroxisomal; Acetyl-CoA C-myristoyltransferase; Acetyl-CoA acyltransferase; Beta-ketothiolase; Peroxisomal 3-oxoacyl-CoA thiolase; EC 2.3.1.16; EC 2.3.1.155; EC 2.3.1.9 from Homo sapiens (Human) (see 3 papers)
42% identity, 99% coverage: 3:398/400 of query aligns to 37:420/424 of P09110
- V387 (≠ T366) to A: in dbSNP:rs2229528
Sites not aligning to the query:
- 1:26 PTS2-type peroxisomal targeting signal
- 5 mutation Q->D,K,L: Does not affect localization to peroxisomes.
- 6 V→D: Abolished localization to peroxisomes.; V→K: Does not affect localization to peroxisomes.
- 7 mutation V->D,K: Abolished localization to peroxisomes.
- 8 mutation L->D,K: Does not affect localization to peroxisomes.
- 9 mutation G->D,R,L: Does not affect localization to peroxisomes.
- 10 H→E: In S3E mutant; Abolished localization to peroxisomes.
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
37% identity, 99% coverage: 2:398/400 of query aligns to 5:388/390 of 2d3tC
- active site: C94 (= C90), H346 (= H356), C376 (= C386), G378 (= G388)
- binding acetyl coenzyme *a: C94 (= C90), R214 (= R222), L222 (= L230), L225 (= L233), A238 (= A251), G239 (= G252), S242 (= S255), I244 (≠ L257), A313 (= A326), F314 (= F327), H346 (= H356), C376 (= C386)
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)
42% identity, 99% coverage: 1:394/400 of query aligns to 1:387/393 of P14611
- C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ A148) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ C220) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R222) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S255) 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.
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
40% identity, 99% coverage: 4:400/400 of query aligns to 5:392/392 of P07097
- Q64 (≠ Y65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C386) mutation to G: Loss of activity.
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
40% identity, 99% coverage: 5:400/400 of query aligns to 3:389/389 of 2vu2A
- active site: C86 (= C90), 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 (vs. gap), M154 (= M149), F232 (≠ W237), S244 (= S255), G245 (≠ Q256), F316 (= F327), H345 (= H356)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
40% identity, 99% coverage: 5:400/400 of query aligns to 3:389/389 of 1dm3A
- active site: C86 (= C90), H345 (= H356), C375 (= C386), G377 (= G388)
- binding acetyl coenzyme *a: C86 (= C90), L145 (≠ Q142), H153 (vs. gap), M154 (= M149), R217 (= R222), S224 (= S229), M225 (≠ L230), A240 (= A251), S244 (= S255), M285 (= M296), A315 (= A326), F316 (= F327), H345 (= H356), C375 (= C386)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
40% identity, 99% coverage: 5:400/400 of query aligns to 3:389/389 of 1dlvA
- active site: C86 (= C90), H345 (= H356), C375 (= C386), G377 (= G388)
- binding coenzyme a: C86 (= C90), L145 (≠ Q142), H153 (vs. gap), M154 (= M149), R217 (= R222), L228 (= L233), A240 (= A251), S244 (= S255), H345 (= H356)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
40% identity, 99% coverage: 5:400/400 of query aligns to 5:391/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
40% identity, 99% coverage: 5:400/400 of query aligns to 6:392/392 of 1ou6A
- active site: C89 (= C90), H348 (= H356), C378 (= C386), G380 (= G388)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ Q142), H156 (vs. gap), M157 (= M149), F235 (≠ W237), A243 (= A251), S247 (= S255), A318 (= A326), F319 (= F327), H348 (= H356)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
41% identity, 99% coverage: 1:394/400 of query aligns to 1:387/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H356), C379 (= C386), G381 (= G388)
- binding coenzyme a: S88 (≠ C90), L148 (vs. gap), R221 (= R222), F236 (≠ W237), A244 (= A251), S248 (= S255), L250 (= L257), A319 (= A326), F320 (= F327), H349 (= H356)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
40% identity, 99% coverage: 5:400/400 of query aligns to 3:389/389 of 2wkuA
- active site: C86 (= C90), H345 (= H356), C375 (= C386), G377 (= G388)
- binding D-mannose: S6 (≠ A8), A7 (≠ V9), R38 (= R41), K182 (≠ R177), D194 (= D189), V280 (≠ C291), D281 (≠ A292), T287 (≠ I298), P331 (≠ D342), S332 (≠ A343), V334 (≠ L345), V336 (= V347), F360 (≠ L371)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
40% identity, 99% coverage: 5:400/400 of query aligns to 4:390/390 of 1m1oA
- active site: A87 (≠ C90), H346 (= H356), C376 (= C386), G378 (= G388)
- binding acetoacetyl-coenzyme a: L86 (≠ M89), A87 (≠ C90), L146 (≠ Q142), H154 (vs. gap), M155 (= M149), R218 (= R222), S225 (= S229), M226 (≠ L230), A241 (= A251), G242 (= G252), S245 (= S255), A316 (= A326), F317 (= F327), H346 (= H356), I377 (≠ V387), G378 (= G388)
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)
37% identity, 99% coverage: 1:397/400 of query aligns to 4:393/397 of P42765
- C92 (= C90) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R222) binding
- T227 (= T225) binding
- S251 (= S255) binding
- C382 (= C386) 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)
36% identity, 99% coverage: 1:397/400 of query aligns to 7:392/395 of 4c2jD
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)
38% identity, 100% coverage: 1:398/400 of query aligns to 1:390/392 of P45359
- V77 (≠ D79) 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 (= C90) modified: Disulfide link with 378, In inhibited form
- S96 (≠ A98) binding
- N153 (vs. gap) 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 (≠ AV 287:288) binding
- A286 (≠ D294) 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)
38% identity, 100% coverage: 1:398/400 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C90), H348 (= H356), S378 (≠ C386), G380 (= G388)
- binding coenzyme a: L148 (≠ Q142), H156 (≠ A148), R220 (= R222), L231 (= L233), A243 (= A251), S247 (= S255), F319 (= F327), H348 (= H356)
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
41% identity, 99% coverage: 1:394/400 of query aligns to 4:397/403 of 6pccA
- active site: C93 (= C90), A359 (≠ H356), C389 (= C386), G391 (= G388)
- binding coenzyme a: C93 (= C90), I148 (≠ V138), R229 (= R222), T232 (= T225), A252 (= A251), S256 (= S255), N325 (= N324), F328 (= F327)
- binding hexanal: N61 (≠ A58), T146 (≠ E136), I148 (≠ V138), G149 (≠ L139), R151 (= R141), L361 (≠ F358)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
41% identity, 99% coverage: 1:394/400 of query aligns to 4:397/403 of 6pcbA
- active site: C93 (= C90), A359 (≠ H356), C389 (= C386), G391 (= G388)
- binding coenzyme a: C93 (= C90), I148 (≠ V138), R229 (= R222), A252 (= A251), S256 (= S255), G257 (≠ Q256), N325 (= N324), F328 (= F327)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
40% identity, 100% coverage: 1:398/400 of query aligns to 3:393/394 of 5f38D
- active site: C90 (= C90), A348 (= A353), A378 (≠ V383), L380 (≠ M385)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C90), L151 (≠ Y146), A246 (= A251), S250 (= S255), I252 (≠ L257), A321 (= A326), F322 (= F327), H351 (= H356)
7ei4A Crystal structure of masl in complex with a novel covalent inhibitor, collimonin c (see paper)
42% identity, 98% coverage: 3:394/400 of query aligns to 3:384/392 of 7ei4A
Query Sequence
>RR42_RS31890 FitnessBrowser__Cup4G11:RR42_RS31890
MREAVIVAVARTPIGKAFRGAFNDTEAPALGAHVVRAVVERAGIDPAEVDDVLIGAAAQQ
GTQGYNLGRLCAVAAGLPDSVPGMTMDRMCSSGLMTIATAAKSIICGEADIVVAGGAESI
SLTQNKHKNAYRAQSEAVLARQPDAYMAMIETAEVVAQRYGIARAAQDEYALRSQQRTAE
AQRQGLFDDEIVPLETRRALFDKAGALTGYETVRLALDECNRPDTSADSLAALKPVWSGG
RTVPQGLHITAGNASQLSDGAAAVLLMSGEQAERRGLRPLGRYRGMAVAGCAADEMGIGP
VFAVPRLLARHGLTVKDVGLWELNEAFACQVLYCRDTLGIPDARLNVNGGAIAIGHPFGM
SGARMTAHALLEARRRGAAHAVVTMCVGGGMGAAALFDVL
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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