SitesBLAST
Comparing WP_011444881.1 NCBI__GCF_000013325.1:WP_011444881.1 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)
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
53% identity, 99% coverage: 5:402/404 of query aligns to 1:396/400 of 5bz4K
- active site: C87 (= C91), H354 (= H360), C384 (= C390), G386 (= G392)
- binding coenzyme a: C87 (= C91), R146 (= R150), M160 (= M165), R220 (= R229), A246 (= A250), G247 (= G251), S250 (= S254), Q252 (= Q256), M291 (= M295), A321 (= A325), F322 (= F326), H354 (= H360)
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, 98% coverage: 9:402/404 of query aligns to 6:391/393 of P14611
- C88 (= C91) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ Y159) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ G227) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R229) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S254) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H360) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C390) 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, 98% coverage: 9:402/404 of query aligns to 6:391/393 of 4o9cC
- active site: S88 (≠ C91), H349 (= H360), C379 (= C390), G381 (= G392)
- binding coenzyme a: S88 (≠ C91), L148 (≠ V151), R221 (= R229), F236 (vs. gap), A244 (= A250), S248 (= S254), L250 (≠ Q256), A319 (= A325), F320 (= F326), H349 (= H360)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
43% identity, 99% coverage: 4:402/404 of query aligns to 3:393/394 of 5f38D
- active site: C90 (= C91), A348 (≠ S357), A378 (≠ E387), L380 (≠ M389)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C91), L151 (≠ V151), A246 (= A250), S250 (= S254), I252 (≠ Q256), A321 (= A325), F322 (= F326), H351 (= H360)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
43% identity, 99% coverage: 4:402/404 of query aligns to 1:389/391 of 5f38B
- active site: C88 (= C91), H347 (= H360), C377 (= C390), G379 (= G392)
- binding coenzyme a: C88 (= C91), L149 (≠ V151), K219 (≠ R229), F234 (vs. gap), A242 (= A250), S246 (= S254), A317 (= A325), F318 (= F326), H347 (= H360)
8jg2A Crystal structure of a biosynthetic thiolase from megasphaera hexanoica soaked with hexanoyl-coa
39% identity, 99% coverage: 3:402/404 of query aligns to 1:390/393 of 8jg2A
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
40% identity, 98% coverage: 9:403/404 of query aligns to 6:390/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
40% identity, 98% coverage: 9:403/404 of query aligns to 7:391/392 of 1ou6A
- active site: C89 (= C91), H348 (= H360), C378 (= C390), G380 (= G392)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ V151), H156 (≠ I162), M157 (≠ S163), F235 (vs. gap), A243 (= A250), S247 (= S254), A318 (= A325), F319 (= F326), H348 (= H360)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
40% identity, 98% coverage: 9:403/404 of query aligns to 4:388/389 of 2vu2A
- active site: C86 (= C91), H345 (= H360), C375 (= C390), G377 (= G392)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ I162), M154 (≠ S163), F232 (vs. gap), S244 (= S254), G245 (≠ Q255), F316 (= F326), H345 (= H360)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
40% identity, 98% coverage: 9:403/404 of query aligns to 4:388/389 of 1dm3A
- active site: C86 (= C91), H345 (= H360), C375 (= C390), G377 (= G392)
- binding acetyl coenzyme *a: C86 (= C91), L145 (≠ V151), H153 (≠ I162), M154 (≠ S163), R217 (= R229), S224 (≠ T236), M225 (≠ L237), A240 (= A250), S244 (= S254), M285 (= M295), A315 (= A325), F316 (= F326), H345 (= H360), C375 (= C390)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
40% identity, 98% coverage: 9:403/404 of query aligns to 4:388/389 of 1dlvA
- active site: C86 (= C91), H345 (= H360), C375 (= C390), G377 (= G392)
- binding coenzyme a: C86 (= C91), L145 (≠ V151), H153 (≠ I162), M154 (≠ S163), R217 (= R229), L228 (= L240), A240 (= A250), S244 (= S254), H345 (= H360)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
40% identity, 98% coverage: 9:403/404 of query aligns to 7:391/392 of P07097
- Q64 (≠ P66) mutation to A: Slightly lower activity.
- C89 (= C91) mutation to A: Loss of activity.
- C378 (= C390) mutation to G: Loss of activity.
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
40% identity, 98% coverage: 9:403/404 of query aligns to 4:388/389 of 2wkuA
- active site: C86 (= C91), H345 (= H360), C375 (= C390), G377 (= G392)
- binding D-mannose: S6 (≠ A11), A7 (≠ P12), R38 (= R43), K182 (≠ R193), D194 (= D205), V280 (≠ C290), D281 (= D291), T287 (≠ Y297), P331 (≠ D341), S332 (≠ E347), V334 (≠ L349), V336 (= V351), F360 (≠ R375)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
40% identity, 98% coverage: 9:403/404 of query aligns to 5:389/390 of 1m1oA
- active site: A87 (≠ C91), H346 (= H360), C376 (= C390), G378 (= G392)
- binding acetoacetyl-coenzyme a: L86 (≠ R90), A87 (≠ C91), L146 (≠ V151), H154 (≠ I162), M155 (≠ S163), R218 (= R229), S225 (≠ T236), M226 (≠ L237), A241 (= A250), G242 (= G251), S245 (= S254), A316 (= A325), F317 (= F326), H346 (= H360), I377 (= I391), G378 (= G392)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
39% identity, 99% coverage: 4:402/404 of query aligns to 1:390/393 of 6bn2A
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)
40% identity, 100% coverage: 1:403/404 of query aligns to 1:395/397 of P42765
- C92 (= C91) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R229) binding CoA
- T227 (≠ A232) binding CoA
- S251 (= S254) binding CoA
- C382 (= C390) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
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)
39% identity, 99% coverage: 4:402/404 of query aligns to 1:390/392 of P45359
- V77 (≠ E80) 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 (= C91) modified: Disulfide link with 378, In inhibited form
- S96 (≠ V99) binding acetate
- N153 (≠ I156) 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 (≠ AA 286:287) binding acetate
- A286 (≠ S293) 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 (= C390) modified: Disulfide link with 88, In inhibited form
- A386 (= A398) binding acetate
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
39% identity, 100% coverage: 1:403/404 of query aligns to 4:394/395 of 4c2jD
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
38% identity, 99% coverage: 4:402/404 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C91), H348 (= H360), S378 (≠ C390), G380 (= G392)
- binding coenzyme a: L148 (≠ V151), H156 (≠ Y159), R220 (= R229), L231 (= L240), A243 (= A250), S247 (= S254), F319 (= F326), H348 (= H360)
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
39% identity, 98% coverage: 9:402/404 of query aligns to 5:390/394 of 7cw5B
- active site: C87 (= C91), H348 (= H360), C378 (= C390), G380 (= G392)
- binding coenzyme a: L147 (≠ R150), H155 (≠ R158), M156 (≠ Y159), R220 (= R229), T223 (≠ A232), A243 (= A250), P247 (≠ S254), L249 (≠ Q256), H348 (= H360)
Query Sequence
>WP_011444881.1 NCBI__GCF_000013325.1:WP_011444881.1
MTQLRHAAIVAPIRTAVGKFGGSLSPLTAGQLGATILTALMDRTRIDPARVDDVIFAQGY
GNGEAPCISHWSWLLAGLPEEVPGYQLDRRCGSGLQSIVNAAMMVQTGVSDVVVAGGVES
MSNVEHYTTDVRKGVRAGSLTLHDRLTRGRVMSQPIERYGVISGMIETAENLAKDFAITR
EACDAYAVRSHQRAAAAWANGLFDDELVPVSIPQKKGDPVLFAHDEGYRADASMETLGKL
RPLEGGVVTAGNASQQNDAAAACLVVAEDKLAELGLEPIAWFHSWAAAGCDPSRMGYGPV
PATERLFARNGLTWNDIDLIELNEAFAPQVLACLKGWGWSDDDSRHEMLNVNGSGISLGH
PIGATGGRILANLTRELKRRGGRYGLETMCIGGGQGIAAVFEAA
Or try a new SitesBLAST search
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