SitesBLAST
Comparing WP_091380023.1 NCBI__GCF_900105165.1:WP_091380023.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
45% identity, 98% coverage: 5:389/391 of query aligns to 40:420/424 of P09110
- V387 (≠ S357) 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.
Q56WD9 3-ketoacyl-CoA thiolase 2, peroxisomal; Acetyl-CoA acyltransferase 2; Beta-ketothiolase 2; Peroxisomal 3-oxoacyl-CoA thiolase 2; Peroxisome defective protein 1; EC 2.3.1.16 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
42% identity, 98% coverage: 5:389/391 of query aligns to 54:437/462 of Q56WD9
- C138 (= C90) modified: Disulfide link with 192
- C192 (≠ Y143) modified: Disulfide link with 138
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
43% identity, 98% coverage: 5:389/391 of query aligns to 9:388/390 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)
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.
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
43% identity, 99% coverage: 2:389/391 of query aligns to 5:393/394 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 (= L138), A246 (= A242), S250 (= S246), I252 (≠ T248), A321 (= A317), F322 (= F318), H351 (= H347)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
40% 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 (= L138), H156 (≠ G146), M157 (= M147), F235 (= F234), A243 (= A242), S247 (= S246), A318 (= A317), F319 (= F318), H348 (= H347)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
40% identity, 99% coverage: 5:391/391 of query aligns to 6:391/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
40% 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 (≠ G146), 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)
40% 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 (= L138), H153 (≠ G146), M154 (= M147), R217 (= R219), S224 (≠ A226), 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)
40% 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 (= L138), H153 (≠ G146), M154 (= M147), R217 (= R219), L228 (= L230), A240 (= A242), S244 (= S246), H345 (= H347)
P45359 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; CaTHL; EC 2.3.1.9 from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W) (see paper)
42% identity, 98% coverage: 5:389/391 of query aligns to 6:390/392 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 acetate
- N153 (≠ P141) 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 278:279) binding acetate
- 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 acetate
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
43% identity, 100% coverage: 2:391/391 of query aligns to 3:391/391 of 5f38B