SitesBLAST
Comparing Ac3H11_2522 FitnessBrowser__acidovorax_3H11:Ac3H11_2522 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)
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: 2:389/391 of query aligns to 3:390/392 of P07097
- Q64 (≠ S65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C377) mutation to G: Loss of activity.
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
41% identity, 99% coverage: 3:389/391 of query aligns to 1:387/389 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: C86 (= C90), L145 (≠ Q140), H153 (≠ S147), M154 (= M148), F232 (≠ L235), A240 (= A242), S244 (= S246), G245 (≠ Q247), L246 (≠ F248), A315 (= A317), F316 (= F318), H345 (= H347)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
41% identity, 99% coverage: 3:389/391 of query aligns to 1:387/389 of 1dm3A
- active site: C86 (= C90), H345 (= H347), C375 (= C377), G377 (= G379)
- binding acetyl coenzyme *a: C86 (= C90), L145 (≠ Q140), H153 (≠ S147), M154 (= M148), R217 (= R220), S224 (≠ A227), M225 (≠ I228), L228 (= L231), F232 (≠ L235), A240 (= A242), G241 (= G243), A243 (= A245), S244 (= S246), G245 (≠ Q247), L246 (≠ F248), M285 (= M287), A315 (= A317), F316 (= F318), H345 (= H347), C375 (= C377), I376 (= I378)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
41% identity, 99% coverage: 3:389/391 of query aligns to 1:387/389 of 1dlvA
- active site: C86 (= C90), H345 (= H347), C375 (= C377), G377 (= G379)
- binding coenzyme a: C86 (= C90), L145 (≠ Q140), H153 (≠ S147), M154 (= M148), R217 (= R220), S224 (≠ A227), M225 (≠ I228), L228 (= L231), F232 (≠ L235), A240 (= A242), G241 (= G243), S244 (= S246), G245 (≠ Q247), L246 (≠ F248), F316 (= F318), H345 (= H347)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
41% identity, 99% coverage: 3:389/391 of query aligns to 3:389/391 of 2vu1A
- active site: C88 (= C90), H347 (= H347), C377 (= C377), G379 (= G379)
- binding pantothenyl-aminoethanol-11-pivalic acid: L147 (≠ Q140), H155 (≠ S147), F234 (≠ L235), A242 (= A242), S246 (= S246), G247 (≠ Q247), L248 (≠ F248), A317 (= A317), F318 (= F318), H347 (= H347)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
41% identity, 99% coverage: 3:389/391 of query aligns to 4:390/392 of 1ou6A
- active site: C89 (= C90), H348 (= H347), C378 (= C377), G380 (= G379)
- binding pantothenyl-aminoethanol-acetate pivalic acid: I144 (≠ A136), L148 (≠ Q140), H156 (≠ S147), M157 (= M148), A234 (= A234), F235 (≠ L235), A243 (= A242), S247 (= S246), G248 (≠ Q247), L249 (≠ F248), A318 (= A317), F319 (= F318), H348 (= H347)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
41% identity, 99% coverage: 3:389/391 of query aligns to 1:387/389 of 2wkuA
- active site: C86 (= C90), H345 (= H347), C375 (= C377), G377 (= G379)
- binding D-mannose: A5 (≠ V7), S6 (= S8), A7 (≠ T9), R38 (= R41), K182 (= K176), D194 (≠ A188), L269 (= L271), V280 (≠ C282), D281 (≠ E283), V284 (≠ E286), T287 (≠ I289), P331 (≠ A333), S332 (≠ D334), V334 (≠ L336), N335 (= N337), V336 (= V338), F360 (≠ I362), R365 (= R367)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
41% identity, 99% coverage: 3:389/391 of query aligns to 2:388/390 of 1m1oA
- active site: A87 (≠ C90), H346 (= H347), C376 (= C377), G378 (= G379)
- binding acetoacetyl-coenzyme a: L86 (≠ F89), A87 (≠ C90), L146 (≠ Q140), H154 (≠ S147), M155 (= M148), R218 (= R220), S225 (≠ A227), M226 (≠ I228), L229 (= L231), F233 (≠ L235), A241 (= A242), G242 (= G243), S245 (= S246), G246 (≠ Q247), L247 (≠ F248), A316 (= A317), F317 (= F318), H346 (= H347), C376 (= C377), I377 (= I378), G378 (= G379)
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)
41% identity, 98% coverage: 1:385/391 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 (≠ S147) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ G218) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R220) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S246) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H347) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C377) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
41% identity, 98% coverage: 1:385/391 of query aligns to 1:387/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H347), C379 (= C377), G381 (= G379)
- binding coenzyme a: S88 (≠ C90), L148 (≠ K141), H156 (≠ S147), R221 (= R220), S228 (≠ A227), L232 (= L231), F236 (≠ L235), A244 (= A242), A247 (= A245), S248 (= S246), G249 (≠ Q247), L250 (≠ F248), A319 (= A317), F320 (= F318), H349 (= H347), I351 (≠ Y349), C379 (= C377)
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)
40% identity, 98% coverage: 5:389/391 of query aligns to 39:420/424 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)
38% identity, 99% coverage: 1:389/391 of query aligns to 1:390/392 of P45359