SitesBLAST
Comparing WP_035238683.1 NCBI__GCF_000745975.1:WP_035238683.1 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)
47% identity, 100% coverage: 1:414/416 of query aligns to 1:390/392 of P45359
- V77 (≠ D77) 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 (= C88) modified: Disulfide link with 378, In inhibited form
- S96 (≠ L96) binding acetate
- N153 (≠ K175) 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 (≠ GM 303:304) binding acetate
- A286 (≠ S310) 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 (= C402) modified: Disulfide link with 88, In inhibited form
- A386 (= A410) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
47% identity, 100% coverage: 1:414/416 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C88), H348 (= H372), S378 (≠ C402), G380 (= G404)
- binding coenzyme a: L148 (≠ P168), H156 (≠ I178), R220 (= R243), L231 (= L254), A243 (= A267), S247 (= S271), F319 (= F343), H348 (= H372)
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)
45% identity, 100% coverage: 1:414/416 of query aligns to 1:391/393 of P14611
- C88 (= C88) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ I178) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ H241) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R243) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S271) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H372) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C402) 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, 100% coverage: 1:414/416 of query aligns to 1:391/393 of 4o9cC
- active site: S88 (≠ C88), H349 (= H372), C379 (= C402), G381 (= G404)
- binding coenzyme a: S88 (≠ C88), L148 (≠ T165), R221 (= R243), F236 (= F258), A244 (= A267), S248 (= S271), L250 (≠ I273), A319 (= A342), F320 (= F343), H349 (= H372)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
45% identity, 100% coverage: 1:414/416 of query aligns to 3:393/394 of 5f38D
- active site: C90 (= C88), A348 (≠ G369), A378 (= A399), L380 (= L401)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C88), L151 (= L147), A246 (= A267), S250 (= S271), I252 (= I273), A321 (= A342), F322 (= F343), H351 (= H372)
8jg2A Crystal structure of a biosynthetic thiolase from megasphaera hexanoica soaked with hexanoyl-coa
43% identity, 100% coverage: 1:415/416 of query aligns to 2:391/393 of 8jg2A
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
44% identity, 100% coverage: 1:416/416 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C88), H347 (= H372), C377 (= C402), G379 (= G404)
- binding coenzyme a: C88 (= C88), L149 (= L147), K219 (≠ R243), F234 (= F258), A242 (= A267), S246 (= S271), A317 (= A342), F318 (= F343), H347 (= H372)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
40% identity, 99% coverage: 4:416/416 of query aligns to 5:392/392 of 1ou6A
- active site: C89 (= C88), H348 (= H372), C378 (= C402), G380 (= G404)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ P168), H156 (≠ I178), M157 (= M179), F235 (= F258), A243 (= A267), S247 (= S271), A318 (= A342), F319 (= F343), H348 (= H372)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
40% identity, 99% coverage: 4:416/416 of query aligns to 4:391/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
40% identity, 99% coverage: 4:416/416 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C88), H345 (= H372), C375 (= C402), G377 (= G404)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ I178), M154 (= M179), F232 (= F258), S244 (= S271), G245 (= G272), F316 (= F343), H345 (= H372)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
40% identity, 99% coverage: 4:416/416 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C88), H345 (= H372), C375 (= C402), G377 (= G404)
- binding acetyl coenzyme *a: C86 (= C88), L145 (≠ P168), H153 (≠ I178), M154 (= M179), R217 (= R243), S224 (≠ K250), M225 (≠ L251), A240 (= A267), S244 (= S271), M285 (= M312), A315 (= A342), F316 (= F343), H345 (= H372), C375 (= C402)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
40% identity, 99% coverage: 4:416/416 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C88), H345 (= H372), C375 (= C402), G377 (= G404)
- binding coenzyme a: C86 (= C88), L145 (≠ P168), H153 (≠ I178), M154 (= M179), R217 (= R243), L228 (= L254), A240 (= A267), S244 (= S271), H345 (= H372)
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, 100% coverage: 1:414/416 of query aligns to 4:394/397 of P42765
- C92 (= C88) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R243) binding CoA
- T227 (≠ M246) binding CoA
- S251 (= S271) binding CoA
- C382 (= C402) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
37% identity, 100% coverage: 1:414/416 of query aligns to 1:390/393 of 6bn2A
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
40% identity, 99% coverage: 4:416/416 of query aligns to 2:389/389 of 2wkuA
- active site: C86 (= C88), H345 (= H372), C375 (= C402), G377 (= G404)
- binding D-mannose: S6 (= S8), A7 (= A9), R38 (= R40), K182 (≠ N207), D194 (= D219), V280 (≠ C307), D281 (≠ H308), T287 (≠ L314), P331 (≠ R358), S332 (≠ E359), V334 (≠ T361), V336 (≠ I363), F360 (≠ Y387)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
38% identity, 100% coverage: 1:414/416 of query aligns to 7:393/395 of 4c2jD
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
40% identity, 99% coverage: 4:416/416 of query aligns to 3:390/390 of 1m1oA
- active site: A87 (≠ C88), H346 (= H372), C376 (= C402), G378 (= G404)
- binding acetoacetyl-coenzyme a: L86 (≠ V87), A87 (≠ C88), L146 (≠ P168), H154 (≠ I178), M155 (= M179), R218 (= R243), S225 (≠ K250), M226 (≠ L251), A241 (= A267), G242 (= G268), S245 (= S271), A316 (= A342), F317 (= F343), H346 (= H372), I377 (≠ G403), G378 (= G404)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
39% identity, 99% coverage: 5:415/416 of query aligns to 4:391/394 of 7cw5B
- active site: C87 (= C88), H348 (= H372), C378 (= C402), G380 (= G404)
- binding coenzyme a: L147 (≠ Y152), H155 (≠ S160), M156 (= M179), R220 (= R243), T223 (≠ M246), A243 (= A267), P247 (≠ S271), L249 (≠ I273), H348 (= H372)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
39% identity, 99% coverage: 5:416/416 of query aligns to 6:392/392 of P07097
- Q64 (≠ L63) mutation to A: Slightly lower activity.
- C89 (= C88) mutation to A: Loss of activity.
- C378 (= C402) mutation to G: Loss of activity.
A0R1Y7 Probable acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; EC 2.3.1.9 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
39% identity, 97% coverage: 5:406/416 of query aligns to 1:379/388 of A0R1Y7
- K187 (≠ N213) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Query Sequence
>WP_035238683.1 NCBI__GCF_000745975.1:WP_035238683.1
MKDVVIVSACRTAIGAFGGTLKDLNGACLASITMKEAIKRAGIDPAIIDDVRYGTCLEHH
DTLNTARVGALMAGIPDTVPAATINRVCISGMEAVLSGMAMIQAGMAHVILAGGTEHMSG
VPYTVPKARWGCRLQDANFVDALIHALHCGSYTLPFDETSPVDTTQAPASYFLGKPYIMG
HTAEFTAQLLDISREEMDEVALRSHNNAERATNDGSFADEIVPVEVPRRKKDPIIFDEDE
HFRPGMTLEKLAALPPAFIPKTGKVTAGNASGINDGSTGMVIMSAEKAKELGLTPIAKIK
ATGMGACHPSVMGLSPVPAVKDLMAKSGITIDDFDLIEVNEAFAAQYLGCEKELNLNREI
TNINGSGIGLGHPIGATGARVMTTLMYAMKNKRKNLGLATLCGGGGVSMACAIEML
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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