SitesBLAST
Comparing WP_058860019.1 NCBI__GCF_001482365.1:WP_058860019.1 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)
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
53% identity, 100% coverage: 1:399/399 of query aligns to 4:403/403 of 6pccA
- active site: C93 (= C89), A359 (≠ H355), C389 (= C385), G391 (= G387)
- binding coenzyme a: C93 (= C89), I148 (= I144), R229 (= R227), T232 (= T230), A252 (= A250), S256 (= S254), N325 (= N323), F328 (= F326)
- binding hexanal: N61 (= N57), T146 (= T142), I148 (= I144), G149 (= G145), R151 (= R147), L361 (= L357)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
53% identity, 100% coverage: 1:399/399 of query aligns to 4:403/403 of 6pcbA
- active site: C93 (= C89), A359 (≠ H355), C389 (= C385), G391 (= G387)
- binding coenzyme a: C93 (= C89), I148 (= I144), R229 (= R227), A252 (= A250), S256 (= S254), G257 (≠ S255), N325 (= N323), F328 (= F326)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
52% identity, 100% coverage: 1:399/399 of query aligns to 5:401/401 of 6pcdA
- active site: S94 (≠ C89), A357 (≠ H355), C387 (= C385), G389 (= G387)
- binding coenzyme a: I149 (= I144), M167 (= M163), R227 (= R227), T230 (= T230), A250 (= A250), S254 (= S254), G255 (≠ S255), A325 (= A325), A357 (≠ H355)
- binding octanal: N62 (= N57), T147 (= T142), T148 (≠ S143), I149 (= I144), G150 (= G145), R152 (= R147), L359 (= L357)
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)
47% identity, 100% coverage: 1:398/399 of query aligns to 1:391/392 of P45359
- V77 (≠ D78) 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 (= C89) modified: Disulfide link with 378, In inhibited form
- S96 (≠ I97) binding acetate
- 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 (≠ AS 286:287) binding acetate
- A286 (≠ E293) 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 (= C385) modified: Disulfide link with 88, In inhibited form
- A386 (= A393) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
46% identity, 100% coverage: 1:398/399 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C89), H348 (= H355), S378 (≠ C385), G380 (= G387)
- binding coenzyme a: L148 (vs. gap), H156 (≠ S162), R220 (= R227), L231 (= L238), A243 (= A250), S247 (= S254), F319 (= F326), H348 (= H355)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
46% identity, 100% coverage: 2:399/399 of query aligns to 3:392/392 of P07097
- Q64 (≠ R64) mutation to A: Slightly lower activity.
- C89 (= C89) mutation to A: Loss of activity.
- C378 (= C385) mutation to G: Loss of activity.
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
46% identity, 98% coverage: 10:399/399 of query aligns to 11:392/392 of 1ou6A
- active site: C89 (= C89), H348 (= H355), C378 (= C385), G380 (= G387)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ F148), H156 (≠ S162), M157 (= M163), F235 (≠ V242), A243 (= A250), S247 (= S254), A318 (= A325), F319 (= F326), H348 (= H355)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
46% identity, 98% coverage: 10:399/399 of query aligns to 10:391/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
46% identity, 98% coverage: 10:399/399 of query aligns to 8:389/389 of 2vu2A
- active site: C86 (= C89), H345 (= H355), C375 (= C385), G377 (= G387)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ S162), M154 (= M163), F232 (≠ V242), S244 (= S254), G245 (≠ S255), F316 (= F326), H345 (= H355)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
46% identity, 98% coverage: 10:399/399 of query aligns to 8:389/389 of 1dm3A
- active site: C86 (= C89), H345 (= H355), C375 (= C385), G377 (= G387)
- binding acetyl coenzyme *a: C86 (= C89), L145 (≠ F148), H153 (≠ S162), M154 (= M163), R217 (= R227), S224 (≠ V234), M225 (≠ L235), A240 (= A250), S244 (= S254), M285 (= M295), A315 (= A325), F316 (= F326), H345 (= H355), C375 (= C385)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
46% identity, 98% coverage: 10:399/399 of query aligns to 8:389/389 of 1dlvA
- active site: C86 (= C89), H345 (= H355), C375 (= C385), G377 (= G387)
- binding coenzyme a: C86 (= C89), L145 (≠ F148), H153 (≠ S162), M154 (= M163), R217 (= R227), L228 (= L238), A240 (= A250), S244 (= S254), H345 (= H355)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
46% identity, 98% coverage: 10:399/399 of query aligns to 8:389/389 of 2wkuA