SitesBLAST
Comparing GFF3382 FitnessBrowser__Phaeo:GFF3382 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)
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)
46% identity, 100% coverage: 1:390/391 of query aligns to 1:391/392 of P45359
- V77 (≠ N78) 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
- N153 (≠ G153) 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 (≠ AH 278:279) binding
- A286 (≠ E285) 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 (= C377) modified: Disulfide link with 88, In inhibited form
- A386 (= A385) binding
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: 1:390/391 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 (≠ K220) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S246) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H347) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C377) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
45% identity, 100% coverage: 1:390/391 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C89), H348 (= H347), S378 (≠ C377), G380 (= G379)
- binding coenzyme a: L148 (= L148), H156 (= H156), R220 (≠ K220), L231 (= L230), A243 (= A242), S247 (= S246), F319 (= F318), H348 (= H347)
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)
47% identity, 99% coverage: 4:389/391 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 (≠ K220) binding
- T227 (≠ S222) binding
- S251 (= S246) binding
- C382 (= C377) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
49% identity, 100% coverage: 1:390/391 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C89), H349 (= H347), C379 (= C377), G381 (= G379)
- binding coenzyme a: S88 (≠ C89), L148 (= L148), R221 (≠ K220), F236 (= F234), A244 (= A242), S248 (= S246), L250 (≠ I248), A319 (= A317), F320 (= F318), H349 (= H347)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
47% identity, 99% coverage: 4:389/391 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)
48% identity, 100% coverage: 1:390/391 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C89), A348 (= A344), A378 (≠ I374), L380 (≠ M376)
- 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 (= L148), A246 (= A242), S250 (= S246), I252 (= I248), A321 (= A317), F322 (= F318), H351 (= H347)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
49% identity, 100% coverage: 1:391/391 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C89), H347 (= H347), C377 (= C377), G379 (= G379)
- binding coenzyme a: C88 (= C89), L149 (= L148), K219 (= K220), F234 (= F234), A242 (= A242), S246 (= S246), A317 (= A317), F318 (= F318), H347 (= H347)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
46% identity, 99% coverage: 4:391/391 of query aligns to 5:392/392 of 1ou6A
- active site: C89 (= C89), H348 (= H347), C378 (= C377), G380 (= G379)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L148), H156 (= H156), M157 (= M157), F235 (= F234), A243 (= A242), S247 (= S246), A318 (= A317), F319 (= F318), H348 (= H347)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
46% identity, 99% coverage: 4:391/391 of query aligns to 4:391/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
46% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C89), H345 (= H347), C375 (= C377), G377 (= G379)
- 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 (= F234), S244 (= S246), G245 (= G247), F316 (= F318), H345 (= H347)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
46% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C89), H345 (= H347), C375 (= C377), G377 (= G379)
- binding acetyl coenzyme *a: C86 (= C89), L145 (= L148), H153 (= H156), M154 (= M157), R217 (≠ K220), S224 (≠ T226), M225 (≠ L227), A240 (= A242), S244 (= S246), M285 (= M287), A315 (= A317), F316 (= F318), H345 (= H347), C375 (= C377)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
46% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C89), H345 (= H347), C375 (= C377), G377 (= G379)
- binding coenzyme a: C86 (= C89), L145 (= L148), H153 (= H156), M154 (= M157), R217 (≠ K220), L228 (= L230), A240 (= A242), S244 (= S246), H345 (= H347)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
46% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 2wkuA
- active site: C86 (= C89), H345 (= H347), C375 (= C377), G377 (= G379)
- binding D-mannose: S6 (≠ D8), A7 (≠ G9), R38 (= R40), K182 (≠ R185), D194 (≠ S197), V280 (= V282), D281 (≠ R283), T287 (≠ I289), P331 (= P333), S332 (≠ A334), V334 (= V336), V336 (≠ P338), F360 (≠ Y362)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
46% identity, 100% coverage: 2:391/391 of query aligns to 3:392/392 of P07097
- Q64 (≠ M64) mutation to A: Slightly lower activity.
- C89 (= C89) mutation to A: Loss of activity.
- C378 (= C377) mutation to G: Loss of activity.
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
46% identity, 99% coverage: 4:391/391 of query aligns to 3:390/390 of 1m1oA
- active site: A87 (≠ C89), H346 (= H347), C376 (= C377), G378 (= G379)
- binding acetoacetyl-coenzyme a: L86 (= L88), A87 (≠ C89), L146 (= L148), H154 (= H156), M155 (= M157), R218 (≠ K220), S225 (≠ T226), M226 (≠ L227), A241 (= A242), G242 (= G243), S245 (= S246), A316 (= A317), F317 (= F318), H346 (= H347), I377 (= I378), G378 (= G379)
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
44% identity, 99% coverage: 4:390/391 of query aligns to 5:393/394 of 1wl4A
- active site: C89 (= C89), H350 (= H347), C380 (= C377), G382 (= G379)
- binding coenzyme a: L148 (= L148), M157 (= M157), R220 (≠ K220), Y234 (≠ V233), P245 (≠ A242), A246 (≠ G243), S249 (= S246), A320 (= A317), F321 (= F318), H350 (= H347)
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)
44% identity, 99% coverage: 4:390/391 of query aligns to 8:396/397 of Q9BWD1
- K211 (≠ R208) to R: in dbSNP:rs25683
- R223 (≠ K220) binding
- S226 (= S222) binding
- S252 (= S246) binding
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
47% identity, 100% coverage: 1:391/391 of query aligns to 4:403/403 of 6pccA
- active site: C93 (= C89), A359 (≠ H347), C389 (= C377), G391 (= G379)
- binding coenzyme a: C93 (= C89), I148 (≠ L145), R229 (≠ K220), T232 (≠ S222), A252 (= A242), S256 (= S246), N325 (= N315), F328 (= F318)
- binding hexanal: N61 (≠ I57), T146 (≠ M143), I148 (≠ L145), G149 (= G146), R151 (vs. gap), L361 (≠ V349)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
47% identity, 100% coverage: 1:391/391 of query aligns to 4:403/403 of 6pcbA
- active site: C93 (= C89), A359 (≠ H347), C389 (= C377), G391 (= G379)
- binding coenzyme a: C93 (= C89), I148 (≠ L145), R229 (≠ K220), A252 (= A242), S256 (= S246), G257 (= G247), N325 (= N315), F328 (= F318)
Query Sequence
>GFF3382 FitnessBrowser__Phaeo:GFF3382
MTDIVILDGARTAIGTFGGSLAGTTPIDLATVASKAAMERSGVAPEQIGNVVFGHVINTE
PRDMYLSRVAAMQAGIPNGTPAMNVNRLCGSGAQAIVSGIQSLMLGDAEFALTGGAENMS
RSPFIVPSARWGQKMGDARALDMMLGALNCPFGTGHMGVTAENVADEHDITRAQMDEFAL
ASQTRAAAAIEAGYFASQITPVEVKVKRDMVPFDVDEHPKASTLETLGGLKAVFKKDGRV
TAGNASGINDGAAAIVMATADAARQAGLKPKARILGYAHAGVRPEVMGIGPVPAVQNLLK
KTGLSASDFDVVESNEAFAAQALAVNKELGLDPAKVNPNGGAIALGHPVGATGAIITLKT
LYELERIGGSKGLITMCIGGGQGIALAIERL
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