SitesBLAST
Comparing WP_057508480.1 NCBI__GCF_001431535.1:WP_057508480.1 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)
67% identity, 100% coverage: 1:402/402 of query aligns to 4:403/403 of 6pccA
- active site: C93 (= C90), A359 (≠ H358), C389 (= C388), G391 (= G390)
- binding coenzyme a: C93 (= C90), I148 (≠ M145), R229 (= R228), T232 (= T231), A252 (= A251), S256 (= S255), N325 (= N324), F328 (= F327)
- binding hexanal: N61 (= N58), T146 (= T143), I148 (≠ M145), G149 (= G146), R151 (= R148), L361 (= L360)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
67% identity, 100% coverage: 1:402/402 of query aligns to 4:403/403 of 6pcbA
- active site: C93 (= C90), A359 (≠ H358), C389 (= C388), G391 (= G390)
- binding coenzyme a: C93 (= C90), I148 (≠ M145), R229 (= R228), A252 (= A251), S256 (= S255), G257 (= G256), N325 (= N324), F328 (= F327)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
67% identity, 100% coverage: 1:402/402 of query aligns to 5:401/401 of 6pcdA
- active site: S94 (≠ C90), A357 (≠ H358), C387 (= C388), G389 (= G390)
- binding coenzyme a: I149 (≠ M145), M167 (= M163), R227 (= R228), T230 (= T231), A250 (= A251), S254 (= S255), G255 (= G256), A325 (= A326), A357 (≠ H358)
- binding octanal: N62 (= N58), T147 (= T143), T148 (= T144), I149 (≠ M145), G150 (= G146), R152 (= R148), L359 (= L360)
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)
45% identity, 100% coverage: 1:401/402 of query aligns to 1:391/392 of P45359
- V77 (= V79) 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 (≠ G98) binding acetate
- N153 (= N151) 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 287:288) binding acetate
- A286 (≠ S294) 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 (= C388) modified: Disulfide link with 88, In inhibited form
- A386 (= A396) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
45% identity, 100% coverage: 1:401/402 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C90), H348 (= H358), S378 (≠ C388), G380 (= G390)
- binding coenzyme a: L148 (≠ T144), H156 (= H158), R220 (= R228), L231 (= L239), A243 (= A251), S247 (= S255), F319 (= F327), H348 (= H358)
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)
46% identity, 100% coverage: 1:401/402 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 (≠ T162) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ H226) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R228) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S255) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H358) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C388) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
46% identity, 100% coverage: 1:401/402 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H358), C379 (= C388), G381 (= G390)
- binding coenzyme a: S88 (≠ C90), L148 (= L154), R221 (= R228), F236 (= F243), A244 (= A251), S248 (= S255), L250 (≠ I257), A319 (= A326), F320 (= F327), H349 (= H358)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
48% identity, 100% coverage: 1:401/402 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C90), A348 (= A355), A378 (= A385), L380 (≠ M387)
- 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 (≠ T144), A246 (= A251), S250 (= S255), I252 (= I257), A321 (= A326), F322 (= F327), H351 (= H358)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
47% identity, 100% coverage: 1:402/402 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C90), H347 (= H358), C377 (= C388), G379 (= G390)
- binding coenzyme a: C88 (= C90), L149 (≠ T144), K219 (≠ R228), F234 (= F243), A242 (= A251), S246 (= S255), A317 (= A326), F318 (= F327), H347 (= H358)
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
44% identity, 100% coverage: 3:402/402 of query aligns to 6:390/390 of 2d3tC
- active site: C94 (= C90), H346 (= H358), C376 (= C388), G378 (= G390)
- binding acetyl coenzyme *a: C94 (= C90), R214 (= R228), L222 (= L236), L225 (= L239), A238 (= A251), G239 (= G252), S242 (= S255), I244 (= I257), A313 (= A326), F314 (= F327), H346 (= H358), C376 (= C388)
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)
43% identity, 99% coverage: 5:400/402 of query aligns to 8:394/397 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 (= R228) binding CoA
- T227 (= T231) binding CoA
- S251 (= S255) binding CoA
- C382 (= C388) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
8jg2A Crystal structure of a biosynthetic thiolase from megasphaera hexanoica soaked with hexanoyl-coa
44% identity, 100% coverage: 1:400/402 of query aligns to 2:390/393 of 8jg2A
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
45% identity, 99% coverage: 4:402/402 of query aligns to 5:392/392 of P07097
- Q64 (≠ R65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C388) mutation to G: Loss of activity.
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
43% identity, 99% coverage: 5:400/402 of query aligns to 11:393/395 of 4c2jD
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
45% identity, 99% coverage: 6:402/402 of query aligns to 4:389/389 of 2vu2A
- active site: C86 (= C90), H345 (= H358), C375 (= C388), G377 (= G390)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ T162), M154 (= M163), F232 (= F243), S244 (= S255), G245 (= G256), F316 (= F327), H345 (= H358)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
45% identity, 99% coverage: 6:402/402 of query aligns to 4:389/389 of 1dm3A
- active site: C86 (= C90), H345 (= H358), C375 (= C388), G377 (= G390)
- binding acetyl coenzyme *a: C86 (= C90), L145 (= L154), H153 (≠ T162), M154 (= M163), R217 (= R228), S224 (≠ A235), M225 (≠ L236), A240 (= A251), S244 (= S255), M285 (= M296), A315 (= A326), F316 (= F327), H345 (= H358), C375 (= C388)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
45% identity, 99% coverage: 6:402/402 of query aligns to 4:389/389 of 1dlvA
- active site: C86 (= C90), H345 (= H358), C375 (= C388), G377 (= G390)
- binding coenzyme a: C86 (= C90), L145 (= L154), H153 (≠ T162), M154 (= M163), R217 (= R228), L228 (= L239), A240 (= A251), S244 (= S255), H345 (= H358)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
45% identity, 99% coverage: 6:402/402 of query aligns to 7:392/392 of 1ou6A
- active site: C89 (= C90), H348 (= H358), C378 (= C388), G380 (= G390)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L154), H156 (≠ T162), M157 (= M163), F235 (= F243), A243 (= A251), S247 (= S255), A318 (= A326), F319 (= F327), H348 (= H358)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
45% identity, 99% coverage: 6:402/402 of query aligns to 6:391/391 of 2vu1A
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
44% identity, 99% coverage: 6:402/402 of query aligns to 4:389/389 of 2wkuA
- active site: C86 (= C90), H345 (= H358), C375 (= C388), G377 (= G390)
- binding D-mannose: S6 (≠ D8), A7 (≠ G9), R38 (= R40), K182 (≠ R191), D194 (≠ G203), V280 (= V291), D281 (≠ E292), T287 (≠ M298), P331 (≠ A344), S332 (≠ P345), V334 (= V347), V336 (≠ A349), F360 (≠ R373)
Query Sequence
>WP_057508480.1 NCBI__GCF_001431535.1:WP_057508480.1
MHDTYIIDGIRTPIGRYAGALAGVRADDLGAIPLQALLARHPGLDPALIEEVYLGCTNQA
GEDNRNVARMSLLLAGLPVTVPGSTVNRLCGSGLDAIGTVARGIAAGELGLAIAGGVESM
SRAPMVMGKAGTPFARDQVLEDTTMGWRFINPRLRELHGVETMGQTAENVAERHAISRED
QDRFALRSQQRAAAAQQAGFFDGEIIAVDVPGRRRGETVRVEHDEHPRADTTLEALARLK
PLFRQPGSVTAGNASGINDGAAALLLASAAQVQALGLTPRARILGFASAGVEPSVMGMGP
VPATRRLLARLGLSIADFDAIELNEAFASQGLACLRELGLADDAPHVNANGGAIALGHPL
GMSGARIALTLMRQLEASGGRRGLATMCIGVGQGVALAIERV
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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