SitesBLAST
Comparing WP_011444468.1 NCBI__GCF_000013325.1:WP_011444468.1 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)
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)
49% identity, 100% coverage: 1:391/392 of query aligns to 1:391/392 of P45359
- V77 (≠ I78) 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 (≠ V97) binding acetate
- N153 (≠ E153) 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 (≠ GH 279:280) binding acetate
- A286 (≠ N286) 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 (= C378) modified: Disulfide link with 88, In inhibited form
- A386 (= A386) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
48% identity, 100% coverage: 1:391/392 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C89), H348 (= H348), S378 (≠ C378), G380 (= G380)
- binding coenzyme a: L148 (= L148), H156 (= H156), R220 (= R220), L231 (= L231), A243 (= A243), S247 (= S247), F319 (= F319), H348 (= H348)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
50% identity, 99% coverage: 4:392/392 of query aligns to 5:392/392 of 1ou6A
- active site: C89 (= C89), H348 (= H348), C378 (= C378), G380 (= G380)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L148), H156 (= H156), M157 (= M157), F235 (= F235), A243 (= A243), S247 (= S247), A318 (= A318), F319 (= F319), H348 (= H348)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
50% identity, 99% coverage: 4:392/392 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C89), H345 (= H348), C375 (= C378), G377 (= G380)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (= H156), M154 (= M157), F232 (= F235), S244 (= S247), G245 (= G248), F316 (= F319), H345 (= H348)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
50% identity, 99% coverage: 4:392/392 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C89), H345 (= H348), C375 (= C378), G377 (= G380)
- binding acetyl coenzyme *a: C86 (= C89), L145 (= L148), H153 (= H156), M154 (= M157), R217 (= R220), S224 (≠ A227), M225 (= M228), A240 (= A243), S244 (= S247), M285 (= M288), A315 (= A318), F316 (= F319), H345 (= H348), C375 (= C378)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
50% identity, 99% coverage: 4:392/392 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C89), H345 (= H348), C375 (= C378), G377 (= G380)
- binding coenzyme a: C86 (= C89), L145 (= L148), H153 (= H156), M154 (= M157), R217 (= R220), L228 (= L231), A240 (= A243), S244 (= S247), H345 (= H348)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
50% identity, 99% coverage: 4:392/392 of query aligns to 4:391/391 of 2vu1A
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
49% identity, 99% coverage: 4:392/392 of query aligns to 2:389/389 of 2wkuA
- active site: C86 (= C89), H345 (= H348), C375 (= C378), G377 (= G380)
- binding D-mannose: S6 (= S8), A7 (≠ G9), R38 (= R40), K182 (≠ R185), D194 (≠ E197), V280 (= V283), D281 (≠ E284), T287 (≠ L290), P331 (= P334), S332 (≠ A335), V334 (≠ T337), V336 (≠ P339), F360 (≠ Y363)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
49% identity, 100% coverage: 2:392/392 of query aligns to 3:392/392 of P07097
- Q64 (≠ A64) mutation to A: Slightly lower activity.
- C89 (= C89) mutation to A: Loss of activity.
- C378 (= C378) mutation to G: Loss of activity.
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
49% identity, 99% coverage: 4:392/392 of query aligns to 3:390/390 of 1m1oA
- active site: A87 (≠ C89), H346 (= H348), C376 (= C378), G378 (= G380)
- binding acetoacetyl-coenzyme a: L86 (= L88), A87 (≠ C89), L146 (= L148), H154 (= H156), M155 (= M157), R218 (= R220), S225 (≠ A227), M226 (= M228), A241 (= A243), G242 (= G244), S245 (= S247), A316 (= A318), F317 (= F319), H346 (= H348), I377 (= I379), G378 (= G380)
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)
50% identity, 100% coverage: 1:391/392 of query aligns to 1:392/393 of P14611
- C88 (= C89) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (= H156) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ H218) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R220) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S247) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H348) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C378) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
50% identity, 100% coverage: 1:391/392 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C89), H349 (= H348), C379 (= C378), G381 (= G380)
- binding coenzyme a: S88 (≠ C89), L148 (= L148), R221 (= R220), F236 (= F235), A244 (= A243), S248 (= S247), L250 (≠ I249), A319 (= A318), F320 (= F319), H349 (= H348)
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)
47% identity, 99% coverage: 4:391/392 of query aligns to 8:396/397 of Q9BWD1
- K211 (= K208) to R: in dbSNP:rs25683
- R223 (= R220) binding CoA
- S226 (≠ A223) binding CoA
- S252 (= S247) binding CoA
8jg2A Crystal structure of a biosynthetic thiolase from megasphaera hexanoica soaked with hexanoyl-coa
48% identity, 99% coverage: 1:390/392 of query aligns to 2:390/393 of 8jg2A
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
47% identity, 99% coverage: 4:391/392 of query aligns to 5:393/394 of 1wl4A
- active site: C89 (= C89), H350 (= H348), C380 (= C378), G382 (= G380)
- binding coenzyme a: L148 (= L148), M157 (= M157), R220 (= R220), Y234 (≠ V234), P245 (≠ A243), A246 (≠ G244), S249 (= S247), A320 (= A318), F321 (= F319), H350 (= H348)
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)
44% identity, 99% coverage: 4:390/392 of query aligns to 7:394/397 of P42765
- C92 (= C89) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R220) binding CoA
- T227 (≠ A223) binding CoA
- S251 (= S247) binding CoA
- C382 (= C378) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
43% identity, 99% coverage: 4:390/392 of query aligns to 10:393/395 of 4c2jD
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
49% identity, 100% coverage: 1:391/392 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C89), A348 (≠ S345), A378 (≠ I375), L380 (≠ M377)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C89), L151 (≠ M144), A246 (= A243), S250 (= S247), I252 (= I249), A321 (= A318), F322 (= F319), H351 (= H348)
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
47% identity, 99% coverage: 3:392/392 of query aligns to 2:398/400 of 5bz4K
- active site: C87 (= C89), H354 (= H348), C384 (= C378), G386 (= G380)
- binding coenzyme a: C87 (= C89), R146 (vs. gap), M160 (= M157), R220 (= R220), A246 (= A243), G247 (= G244), S250 (= S247), Q252 (≠ I249), M291 (= M288), A321 (= A318), F322 (= F319), H354 (= H348)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
48% identity, 100% coverage: 1:392/392 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C89), H347 (= H348), C377 (= C378), G379 (= G380)
- binding coenzyme a: C88 (= C89), L149 (≠ M144), K219 (≠ R220), F234 (= F235), A242 (= A243), S246 (= S247), A317 (= A318), F318 (= F319), H347 (= H348)
Query Sequence
>WP_011444468.1 NCBI__GCF_000013325.1:WP_011444468.1
MTDIYIVSGARTAIGSFGGGLASLRPAESGAIVIKEAIARAGIAPDKVQNVVIGTVVPTQ
PKDAYVSRVAAVNAGIPIEAPAMNVNRLCGSGLQAIVSAAQGIALGEQDIAIGGGAESMS
NAPHMVLTARNGQKMGDQVLMDAMLGALHDPFEGIHMGVTAENVAERCQITREEQDSLAV
ESHKRAAAAIAAGYFKEQIVPVEIKTRKGVVVFDTDEHVRADASVEAMAGLKPVFKKDGT
VTAGNASGINDGAAAVVLASGKAVEEHGLKPMARILGWGHAGVEPNVMGLGPVKAVPVAL
QRAGLDLDQIDVIEANEAFAAQACGVAKELGFDPAKTNPNGSGISLGHPIGATGAILTIK
TMYELHRTGGRYGLITMCIGGGQGIAMVIERV
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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