SitesBLAST
Comparing CA265_RS17585 FitnessBrowser__Pedo557:CA265_RS17585 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)
44% identity, 98% coverage: 5:389/391 of query aligns to 40:420/424 of P09110
- V387 (≠ T357) 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.
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)
42% identity, 99% coverage: 2:389/391 of query aligns to 3:390/392 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 (≠ GI 278:279) binding
- A286 (≠ R285) 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 (= C377) modified: Disulfide link with 88, In inhibited form
- A386 (= A385) binding
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
42% identity, 97% coverage: 10:389/391 of query aligns to 14:388/390 of 2d3tC
- active site: C94 (= C90), H346 (= H347), C376 (= C377), G378 (= G379)
- binding acetyl coenzyme *a: C94 (= C90), R214 (= R219), L222 (= L227), L225 (= L230), A238 (= A242), G239 (= G243), S242 (= S246), I244 (≠ T248), A313 (= A317), F314 (= F318), H346 (= H347), C376 (= C377)
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
42% identity, 99% coverage: 2:389/391 of query aligns to 3:390/392 of 4xl4A
- active site: C88 (= C90), H348 (= H347), S378 (≠ C377), G380 (= G379)
- binding coenzyme a: L148 (≠ Y144), H156 (vs. gap), R220 (= R219), L231 (= L230), A243 (= A242), S247 (= S246), F319 (= F318), H348 (= H347)
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: 5:391/391 of query aligns to 7:392/392 of P07097
- Q64 (≠ L65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C377) mutation to G: Loss of activity.
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
40% identity, 99% coverage: 5:391/391 of query aligns to 6:391/391 of 5f38B
- active site: C88 (= C90), H347 (= H347), C377 (= C377), G379 (= G379)
- binding coenzyme a: C88 (= C90), L149 (≠ K138), K219 (≠ R219), F234 (= F234), A242 (= A242), S246 (= S246), A317 (= A317), F318 (= F318), H347 (= H347)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
40% identity, 98% coverage: 5:389/391 of query aligns to 8:393/394 of 5f38D
- active site: C90 (= C90), A348 (= A344), A378 (≠ V374), L380 (≠ M376)
- 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 (≠ K138), A246 (= A242), S250 (= S246), I252 (≠ T248), A321 (= A317), F322 (= F318), H351 (= H347)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
39% identity, 99% coverage: 5:391/391 of query aligns to 6:391/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
39% identity, 99% coverage: 5:391/391 of query aligns to 7:392/392 of 1ou6A
- active site: C89 (= C90), H348 (= H347), C378 (= C377), G380 (= G379)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ N140), H156 (vs. gap), M157 (= M147), F235 (= F234), A243 (= A242), S247 (= S246), A318 (= A317), F319 (= F318), H348 (= H347)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
39% identity, 99% coverage: 5:391/391 of query aligns to 4:389/389 of 2vu2A
- active site: C86 (= C90), H345 (= H347), C375 (= C377), G377 (= G379)
- 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 (= M147), F232 (= F234), S244 (= S246), G245 (≠ Q247), F316 (= F318), H345 (= H347)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
39% identity, 99% coverage: 5:391/391 of query aligns to 4:389/389 of 1dm3A
- active site: C86 (= C90), H345 (= H347), C375 (= C377), G377 (= G379)
- binding acetyl coenzyme *a: C86 (= C90), L145 (≠ N140), H153 (vs. gap), M154 (= M147), R217 (= R219), S224 (≠ K226), M225 (≠ L227), A240 (= A242), S244 (= S246), M285 (= M287), A315 (= A317), F316 (= F318), H345 (= H347), C375 (= C377)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
39% identity, 99% coverage: 5:391/391 of query aligns to 4:389/389 of 1dlvA
- active site: C86 (= C90), H345 (= H347), C375 (= C377), G377 (= G379)
- binding coenzyme a: C86 (= C90), L145 (≠ N140), H153 (vs. gap), M154 (= M147), R217 (= R219), L228 (= L230), A240 (= A242), S244 (= S246), H345 (= H347)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
39% identity, 99% coverage: 5:391/391 of query aligns to 4:389/389 of 2wkuA
- active site: C86 (= C90), H345 (= H347), C375 (= C377), G377 (= G379)
- binding D-mannose: S6 (≠ A7), A7 (≠ G8), R38 (≠ S40), K182 (= K175), D194 (= D187), V280 (= V282), D281 (≠ P283), T287 (≠ I289), P331 (= P333), S332 (≠ D334), V334 (≠ I336), V336 (= V338), F360 (≠ N362)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
39% identity, 99% coverage: 5:391/391 of query aligns to 5:390/390 of 1m1oA
- active site: A87 (≠ C90), H346 (= H347), C376 (= C377), G378 (= G379)
- binding acetoacetyl-coenzyme a: L86 (≠ Y89), A87 (≠ C90), L146 (≠ N140), H154 (vs. gap), M155 (= M147), R218 (= R219), S225 (≠ K226), M226 (≠ L227), A241 (= A242), G242 (= G243), S245 (= S246), A316 (= A317), F317 (= F318), H346 (= H347), I377 (≠ V378), G378 (= G379)
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)
38% identity, 99% coverage: 4:389/391 of query aligns to 8:394/397 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 (= R219) binding
- T227 (= T222) binding
- S251 (= S246) binding
- C382 (= C377) 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)
38% identity, 99% coverage: 4:389/391 of query aligns to 11:393/395 of 4c2jD
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
40% identity, 98% coverage: 2:385/391 of query aligns to 6:397/403 of 6pccA
- active site: C93 (= C90), A359 (≠ H347), C389 (= C377), G391 (= G379)
- binding coenzyme a: C93 (= C90), I148 (vs. gap), R229 (= R219), T232 (= T222), A252 (= A242), S256 (= S246), N325 (= N315), F328 (= F318)
- binding hexanal: N61 (≠ T58), T146 (vs. gap), I148 (vs. gap), G149 (= G127), R151 (≠ K129), L361 (= L349)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
40% identity, 98% coverage: 2:385/391 of query aligns to 6:397/403 of 6pcbA
- active site: C93 (= C90), A359 (≠ H347), C389 (= C377), G391 (= G379)
- binding coenzyme a: C93 (= C90), I148 (vs. gap), R229 (= R219), A252 (= A242), S256 (= S246), G257 (≠ Q247), N325 (= N315), F328 (= F318)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
39% identity, 98% coverage: 2:385/391 of query aligns to 7:395/401 of 6pcdA
- active site: S94 (≠ C90), A357 (≠ H347), C387 (= C377), G389 (= G379)
- binding coenzyme a: I149 (vs. gap), M167 (= M147), R227 (= R219), T230 (= T222), A250 (= A242), S254 (= S246), G255 (≠ Q247), A325 (= A317), A357 (≠ H347)
- binding octanal: N62 (≠ T58), T147 (vs. gap), T148 (vs. gap), I149 (vs. gap), G150 (= G127), R152 (≠ K129), L359 (= L349)
8opuC Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with sulfamethoxazole (fragment-b-e1)
37% identity, 99% coverage: 2:389/391 of query aligns to 3:397/399 of 8opuC
Query Sequence
>CA265_RS17585 FitnessBrowser__Pedo557:CA265_RS17585
MEAYIIAGYRTAVGKAPRGVFRFTRADDLAAEVIRALVASVPNLDNEQIDDVIVGNATPE
AEQGLNIGRMISLMGLDTDKVPGVTVNRYCASGLDTIATAVAKIKAGMADCIIAGGVEVM
SGMPFGGWKLVPNAEVAKNNPDWYWGMGLTAEAVAKEYNVSREDQDAFSLKSHEKAIHAI
KNGHLKDGILPITVNENYLDANLKKKTRSYVVDTDEGPRADTTLDKLAKLKPVFDAVGSV
TAGNSSQTSDGAAFVLVVSEKKMKELNAEPIARLVSYGIAGVPPRIMGIGPIEAIPKALK
QAGLKKEDIDLIELNEAFASQSLAVIRTLDLNPDVINVNGGAIALGHPLGCTGAKLTVQI
MNELKRQNKKYGMVTMCVGTGQGAAGIFELL
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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