SitesBLAST
Comparing Dsui_0325 FitnessBrowser__PS:Dsui_0325 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
37% identity, 98% coverage: 10:431/432 of query aligns to 10:394/395 of 4c2jD
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)
37% identity, 98% coverage: 10:431/432 of query aligns to 7:395/397 of P42765
- C92 (= C94) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R242) binding
- T227 (≠ A245) binding
- S251 (= S270) binding
- C382 (= C418) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
37% identity, 98% coverage: 9:431/432 of query aligns to 4:391/392 of P07097
- Q64 (≠ V69) mutation to A: Slightly lower activity.
- C89 (= C94) mutation to A: Loss of activity.
- C378 (= C418) mutation to G: Loss of activity.
P45359 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; CaTHL; EC 2.3.1.9 from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) (see paper)
36% identity, 93% coverage: 32:432/432 of query aligns to 26:392/392 of P45359
- V77 (≠ N83) 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 (= C94) modified: Disulfide link with 378, In inhibited form
- S96 (≠ D102) binding
- N153 (≠ V179) 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 (≠ QW 302:303) binding
- A286 (≠ S309) 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 (= C418) modified: Disulfide link with 88, In inhibited form
- A386 (= A426) binding
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
36% identity, 98% coverage: 10:431/432 of query aligns to 2:388/389 of 2vu2A
- active site: C86 (= C94), H345 (= H388), C375 (= C418), G377 (= G420)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ L182), M154 (= M183), F232 (= F257), S244 (= S270), G245 (≠ Q271), F316 (= F342), H345 (= H388)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
36% identity, 98% coverage: 10:431/432 of query aligns to 2:388/389 of 1dm3A
- active site: C86 (= C94), H345 (= H388), C375 (= C418), G377 (= G420)
- binding acetyl coenzyme *a: C86 (= C94), L145 (= L174), H153 (≠ L182), M154 (= M183), R217 (= R242), S224 (≠ G249), M225 (= M250), A240 (≠ P266), S244 (= S270), M285 (= M311), A315 (= A341), F316 (= F342), H345 (= H388), C375 (= C418)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
36% identity, 98% coverage: 10:431/432 of query aligns to 2:388/389 of 1dlvA
- active site: C86 (= C94), H345 (= H388), C375 (= C418), G377 (= G420)
- binding coenzyme a: C86 (= C94), L145 (= L174), H153 (≠ L182), M154 (= M183), R217 (= R242), L228 (= L253), A240 (≠ P266), S244 (= S270), H345 (= H388)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
36% identity, 98% coverage: 10:431/432 of query aligns to 4:390/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
36% identity, 98% coverage: 10:431/432 of query aligns to 5:391/392 of 1ou6A
- active site: C89 (= C94), H348 (= H388), C378 (= C418), G380 (= G420)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L174), H156 (≠ L182), M157 (= M183), F235 (= F257), A243 (≠ P266), S247 (= S270), A318 (= A341), F319 (= F342), H348 (= H388)
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
36% identity, 93% coverage: 32:432/432 of query aligns to 26:392/392 of 4xl4A
- active site: C88 (= C94), H348 (= H388), S378 (≠ C418), G380 (= G420)
- binding coenzyme a: L148 (= L174), H156 (≠ L182), R220 (= R242), L231 (= L253), A243 (≠ P266), S247 (= S270), F319 (= F342), H348 (= H388)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
36% identity, 98% coverage: 10:431/432 of query aligns to 2:388/389 of 2wkuA
- active site: C86 (= C94), H345 (= H388), C375 (= C418), G377 (= G420)
- binding D-mannose: S6 (≠ D14), A7 (≠ G15), R38 (= R46), K182 (≠ R211), D194 (≠ G222), V280 (≠ L306), D281 (= D307), T287 (≠ L313), P331 (≠ Q374), S332 (≠ D375), V334 (≠ L377), V336 (= V379), F360 (≠ H403)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
36% identity, 98% coverage: 10:431/432 of query aligns to 3:389/390 of 1m1oA
- active site: A87 (≠ C94), H346 (= H388), C376 (= C418), G378 (= G420)
- binding acetoacetyl-coenzyme a: L86 (≠ N93), A87 (≠ C94), L146 (= L174), H154 (≠ L182), M155 (= M183), R218 (= R242), S225 (≠ G249), M226 (= M250), A241 (≠ P266), G242 (≠ A267), S245 (= S270), A316 (= A341), F317 (= F342), H346 (= H388), I377 (= I419), G378 (= G420)
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
37% identity, 98% coverage: 8:430/432 of query aligns to 3:392/394 of 1wl4A
- active site: C89 (= C94), H350 (= H388), C380 (= C418), G382 (= G420)
- binding coenzyme a: L148 (= L174), M157 (= M183), R220 (= R242), Y234 (≠ F256), P245 (= P266), A246 (= A267), S249 (= S270), A320 (= A341), F321 (= F342), H350 (= H388)
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)
37% identity, 98% coverage: 8:430/432 of query aligns to 6:395/397 of Q9BWD1
- K211 (≠ D231) to R: in dbSNP:rs25683
- R223 (= R242) binding
- S226 (≠ A245) binding
- S252 (= S270) binding
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
37% identity, 97% coverage: 12:430/432 of query aligns to 6:389/391 of 5f38B
- active site: C88 (= C94), H347 (= H388), C377 (= C418), G379 (= G420)
- binding coenzyme a: C88 (= C94), L149 (= L174), K219 (≠ R242), F234 (= F257), A242 (≠ P266), S246 (= S270), A317 (= A341), F318 (= F342), H347 (= H388)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
37% identity, 97% coverage: 12:430/432 of query aligns to 8:393/394 of 5f38D
- active site: C90 (= C94), A348 (= A385), A378 (= A415), L380 (≠ I417)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C94), L151 (= L174), A246 (≠ P266), S250 (= S270), I252 (= I272), A321 (= A341), F322 (= F342), H351 (= H388)
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
36% identity, 99% coverage: 4:430/432 of query aligns to 1:401/403 of 6pccA
- active site: C93 (= C94), A359 (≠ H388), C389 (= C418), G391 (= G420)
- binding coenzyme a: C93 (= C94), I148 (≠ L148), R229 (= R242), T232 (≠ A245), A252 (≠ P266), S256 (= S270), N325 (= N339), F328 (= F342)
- binding hexanal: N61 (≠ S63), T146 (≠ K146), I148 (≠ L148), G149 (= G149), R151 (≠ K151), L361 (≠ V390)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
36% identity, 99% coverage: 4:430/432 of query aligns to 1:401/403 of 6pcbA
- active site: C93 (= C94), A359 (≠ H388), C389 (= C418), G391 (= G420)
- binding coenzyme a: C93 (= C94), I148 (≠ L148), R229 (= R242), A252 (≠ P266), S256 (= S270), G257 (≠ Q271), N325 (= N339), F328 (= F342)
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)
36% identity, 97% coverage: 10:430/432 of query aligns to 4:391/393 of P14611
- C88 (= C94) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ L182) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ G240) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R242) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S270) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H388) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C418) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
34% identity, 97% coverage: 10:430/432 of query aligns to 7:388/390 of 2d3tC
- active site: C94 (= C94), H346 (= H388), C376 (= C418), G378 (= G420)
- binding acetyl coenzyme *a: C94 (= C94), R214 (= R242), L222 (≠ M250), L225 (= L253), A238 (≠ P266), G239 (≠ A267), S242 (= S270), I244 (= I272), A313 (= A341), F314 (= F342), H346 (= H388), C376 (= C418)
Query Sequence
>Dsui_0325 FitnessBrowser__PS:Dsui_0325
MAQQQAFEPVYVVDGARTPFLKAKNGPGPFSAADLAVQAGRALLARQPFAPEDLDEVVLG
CASPSPDEVNIGRVAALRLGCGNKVTGWTVMRNCASGMQALDSAMANIQSGRSELVLAGG
VDALSRAPLLYNDAMVLWFAGMMQMKTLGQKAGHFLKLRPSVLLNPVIGLMKGLTDPVVG
LLMGQTAENLAWRFGISREEMDAFSVRSHQRVMAGRAKQAFGEIVPLVGNDGTVYAEDDG
VRVDASMDGMKKLKPFFDKKYGRVTPANSSQITDGGAWLLLASESAVKRWKLEPLGRIVD
AQWAGLDPSQMGLGPVHAVTPILQRHGLGLNDVDLMEINEAFAAQVLGCLKAWEDDAYCR
EELGLPGALGSLDQDKLNVDGGAVAQGHPVGASGARIVLHLLHALKARGGKRGVASICIG
GGQGGAMLVETC
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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