SitesBLAST
Comparing YP_426398.1 NCBI__GCF_000013085.1:YP_426398.1 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)
8gqmA Crystal structure of thiolase complexed with acetyl coenzyme a
62% identity, 99% coverage: 4:380/380 of query aligns to 3:375/377 of 8gqmA
- binding acetyl coenzyme *a: K18 (= K19), S89 (≠ C90), M124 (= M125), M146 (= M147), R205 (= R208), T208 (= T211), L213 (= L216), L216 (= L219), A226 (= A231), A227 (≠ G232), S229 (= S234), S230 (= S235), M271 (= M276), A301 (= A306), H331 (= H336), L333 (= L338)
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
47% identity, 99% coverage: 4:380/380 of query aligns to 7:390/390 of 2d3tC
- active site: C94 (= C90), H346 (= H336), C376 (= C366), G378 (= G368)
- binding acetyl coenzyme *a: C94 (= C90), R214 (= R208), L222 (= L216), L225 (= L219), A238 (= A231), G239 (= G232), S242 (= S235), I244 (≠ L237), A313 (= A306), F314 (= F307), H346 (= H336), C376 (= C366)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
42% identity, 99% coverage: 4:380/380 of query aligns to 4:391/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
42% identity, 99% coverage: 4:380/380 of query aligns to 5:392/392 of 1ou6A
- active site: C89 (= C90), H348 (= H336), C378 (= C366), G380 (= G368)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ M140), H156 (vs. gap), M157 (= M147), F235 (= F223), A243 (= A231), S247 (= S235), A318 (= A306), F319 (= F307), H348 (= H336)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
42% identity, 99% coverage: 4:380/380 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C90), H345 (= H336), C375 (= C366), G377 (= G368)
- 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 (= F223), S244 (= S235), G245 (≠ P236), F316 (= F307), H345 (= H336)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
42% identity, 99% coverage: 4:380/380 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C90), H345 (= H336), C375 (= C366), G377 (= G368)
- binding acetyl coenzyme *a: C86 (= C90), L145 (≠ M140), H153 (vs. gap), M154 (= M147), R217 (= R208), S224 (≠ G215), M225 (≠ L216), A240 (= A231), S244 (= S235), M285 (= M276), A315 (= A306), F316 (= F307), H345 (= H336), C375 (= C366)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
42% identity, 99% coverage: 4:380/380 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C90), H345 (= H336), C375 (= C366), G377 (= G368)
- binding coenzyme a: C86 (= C90), L145 (≠ M140), H153 (vs. gap), M154 (= M147), R217 (= R208), L228 (= L219), A240 (= A231), S244 (= S235), H345 (= H336)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
43% identity, 95% coverage: 19:380/380 of query aligns to 19:392/392 of P07097
- Q64 (≠ L65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C366) mutation to G: Loss of activity.
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
42% identity, 99% coverage: 4:380/380 of query aligns to 2:389/389 of 2wkuA
- active site: C86 (= C90), H345 (= H336), C375 (= C366), G377 (= G368)
- binding D-mannose: S6 (= S8), A7 (≠ Y9), R38 (= R41), K182 (≠ R175), D194 (= D187), V280 (≠ C271), D281 (= D272), T287 (≠ I278), P331 (≠ A322), S332 (≠ D323), V334 (= V325), V336 (≠ I327), F360 (≠ S351)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
42% identity, 99% coverage: 4:380/380 of query aligns to 3:390/390 of 1m1oA
- active site: A87 (≠ C90), H346 (= H336), C376 (= C366), G378 (= G368)
- binding acetoacetyl-coenzyme a: L86 (≠ F89), A87 (≠ C90), L146 (≠ M140), H154 (vs. gap), M155 (= M147), R218 (= R208), S225 (≠ G215), M226 (≠ L216), A241 (= A231), G242 (= G232), S245 (= S235), A316 (= A306), F317 (= F307), H346 (= H336), I377 (= I367), G378 (= G368)
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, 99% coverage: 1:378/380 of query aligns to 1:390/392 of P45359
- V77 (≠ Q79) 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 (≠ H98) 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 (≠ AV 267:268) binding acetate
- A286 (≠ E274) 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 (= C366) modified: Disulfide link with 88, In inhibited form
- A386 (= A374) binding acetate
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)
39% identity, 99% coverage: 4:379/380 of query aligns to 7:395/397 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 (= R208) binding CoA
- T227 (= T211) binding CoA
- S251 (= S235) binding CoA
- C382 (= C366) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
42% identity, 99% coverage: 1:378/380 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C90), H348 (= H336), S378 (≠ C366), G380 (= G368)
- binding coenzyme a: L148 (≠ A143), H156 (≠ G146), R220 (= R208), L231 (= L219), A243 (= A231), S247 (= S235), F319 (= F307), H348 (= H336)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
40% identity, 97% coverage: 11:379/380 of query aligns to 17:394/395 of 4c2jD
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)
40% identity, 99% coverage: 4:378/380 of query aligns to 52:437/462 of Q56WD9
- C138 (= C90) modified: Disulfide link with 192
- C192 (≠ A143) modified: Disulfide link with 138
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
45% identity, 100% coverage: 1:380/380 of query aligns to 4:403/403 of 6pccA
- active site: C93 (= C90), A359 (≠ H336), C389 (= C366), G391 (= G368)
- binding coenzyme a: C93 (= C90), I148 (vs. gap), R229 (= R208), T232 (= T211), A252 (= A231), S256 (= S235), N325 (= N304), F328 (= F307)
- binding hexanal: N61 (≠ F58), T146 (vs. gap), I148 (vs. gap), G149 (vs. gap), R151 (vs. gap), L361 (= L338)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
45% identity, 100% coverage: 1:380/380 of query aligns to 4:403/403 of 6pcbA
- active site: C93 (= C90), A359 (≠ H336), C389 (= C366), G391 (= G368)
- binding coenzyme a: C93 (= C90), I148 (vs. gap), R229 (= R208), A252 (= A231), S256 (= S235), G257 (≠ P236), N325 (= N304), F328 (= F307)
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)
44% identity, 99% coverage: 1:378/380 of query aligns to 1:391/393 of P14611
- C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ G146) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ C206) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R208) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S235) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H336) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C366) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
44% identity, 99% coverage: 1:378/380 of query aligns to 1:391/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H336), C379 (= C366), G381 (= G368)
- binding coenzyme a: S88 (≠ C90), L148 (≠ M140), R221 (= R208), F236 (= F223), A244 (= A231), S248 (= S235), L250 (= L237), A319 (= A306), F320 (= F307), H349 (= H336)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
45% identity, 100% coverage: 1:380/380 of query aligns to 5:401/401 of 6pcdA
- active site: S94 (≠ C90), A357 (≠ H336), C387 (= C366), G389 (= G368)
- binding coenzyme a: I149 (vs. gap), M167 (= M140), R227 (= R208), T230 (= T211), A250 (= A231), S254 (= S235), G255 (≠ P236), A325 (= A306), A357 (≠ H336)
- binding octanal: N62 (≠ F58), T147 (vs. gap), T148 (vs. gap), I149 (vs. gap), G150 (vs. gap), R152 (vs. gap), L359 (= L338)
Query Sequence
>YP_426398.1 NCBI__GCF_000013085.1:YP_426398.1
MTQVVLASYVRSPFTPARKGALARVRPDDLAAQVIKALVARTGVDPATIEDLILGCAFPE
GEQGLNVARLIGLMAGLPQSTAGVTVNRFCGSSMQSIHMAAGAIALGAGEAFVCAGVESM
SRVPMMGFNPLPNPAFAKAMPGAYMGMGDTAENVAKRWKIDRKAQEEFALRSHQRAKTAQ
DAGHLSDEIVAITDPRGGASVETDGCVRPETTLDGLAELKPAFSTEGVVTAGTSSPLTDG
ASAVFVCSREYADRHGLTPLAALKSIAVAGCDPEIMGIGPVAASRKALERAGIDAGALDV
IELNEAFASQALACLGELGLDADKVNIDGGAIALGHPLGATGARIVGKAASLLKRQGGRY
ALATQCIGGGQGIATILEAV
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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