SitesBLAST
Comparing WP_058929093.1 NCBI__GCF_001484605.1:WP_058929093.1 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)
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)
44% identity, 100% coverage: 1:403/405 of query aligns to 1:391/392 of P45359
- V77 (≠ F80) 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 (≠ R98) binding acetate
- N153 (≠ T168) 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 (≠ GV 291:292) binding acetate
- A286 (≠ E298) 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 (= C390) modified: Disulfide link with 88, In inhibited form
- A386 (= A398) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
44% identity, 100% coverage: 1:403/405 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C90), H348 (= H360), S378 (≠ C390), G380 (= G392)
- binding coenzyme a: L148 (≠ T155), H156 (≠ A171), R220 (= R232), L231 (= L243), A243 (= A255), S247 (≠ C259), F319 (= F331), H348 (= H360)
8gqmA Crystal structure of thiolase complexed with acetyl coenzyme a
41% identity, 98% coverage: 5:402/405 of query aligns to 4:373/377 of 8gqmA
- binding acetyl coenzyme *a: K18 (= K19), S89 (≠ C90), M124 (≠ K125), M146 (= M172), R205 (= R232), T208 (= T235), L213 (≠ V240), L216 (= L243), A226 (= A255), A227 (≠ G256), S229 (≠ A258), S230 (≠ C259), M271 (= M300), A301 (= A330), H331 (= H360), L333 (≠ F362)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
43% identity, 100% coverage: 1:404/405 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C90), H347 (= H360), C377 (= C390), G379 (= G392)
- binding coenzyme a: C88 (= C90), L149 (= L164), K219 (≠ R232), F234 (= F247), A242 (= A255), S246 (≠ C259), A317 (= A330), F318 (= F331), H347 (= H360)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
42% identity, 100% coverage: 1:403/405 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C90), A348 (= A357), A378 (≠ E387), L380 (≠ M389)
- 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 (= L164), A246 (= A255), S250 (≠ C259), I252 (≠ L261), A321 (= A330), F322 (= F331), H351 (= H360)
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
39% identity, 99% coverage: 3:404/405 of query aligns to 6:390/390 of 2d3tC
- active site: C94 (= C90), H346 (= H360), C376 (= C390), G378 (= G392)
- binding acetyl coenzyme *a: C94 (= C90), R214 (= R232), L222 (≠ V240), L225 (= L243), A238 (= A255), G239 (= G256), S242 (≠ C259), I244 (≠ L261), A313 (= A330), F314 (= F331), H346 (= H360), C376 (= C390)
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, 100% coverage: 1:403/405 of query aligns to 1:392/393 of P14611
- C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ A171) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ G230) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R232) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (≠ C259) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H360) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C390) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
42% identity, 100% coverage: 1:403/405 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H360), C379 (= C390), G381 (= G392)
- binding coenzyme a: S88 (≠ C90), L148 (≠ T155), R221 (= R232), F236 (= F247), A244 (= A255), S248 (≠ C259), L250 (= L261), A319 (= A330), F320 (= F331), H349 (= H360)
Q9BWD1 Acetyl-CoA acetyltransferase, cytosolic; Acetyl-CoA transferase-like protein; Cytosolic acetoacetyl-CoA thiolase; EC 2.3.1.9 from Homo sapiens (Human) (see 2 papers)
38% identity, 99% coverage: 5:403/405 of query aligns to 9:396/397 of Q9BWD1
- K211 (≠ D221) to R: in dbSNP:rs25683
- R223 (= R232) binding CoA
- S226 (≠ T235) binding CoA
- S252 (≠ C259) binding CoA
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
38% identity, 99% coverage: 5:403/405 of query aligns to 6:393/394 of 1wl4A
- active site: C89 (= C90), H350 (= H360), C380 (= C390), G382 (= G392)
- binding coenzyme a: L148 (vs. gap), M157 (= M172), R220 (= R232), Y234 (≠ I246), P245 (≠ A255), A246 (≠ G256), S249 (≠ C259), A320 (= A330), F321 (= F331), H350 (= H360)
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)
38% identity, 99% coverage: 3:403/405 of query aligns to 51:438/462 of Q56WD9
- C138 (= C90) modified: Disulfide link with 192
- C192 (≠ T168) modified: Disulfide link with 138
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
38% identity, 99% coverage: 3:404/405 of query aligns to 2:398/400 of 5bz4K