SitesBLAST
Comparing GFF2479 FitnessBrowser__Marino:GFF2479 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 / LMG 5710 / VKM B-1787) (see paper)
49% identity, 99% coverage: 1:377/379 of query aligns to 14:390/392 of P45359
- V77 (≠ D64) 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 (= C75) modified: Disulfide link with 378, In inhibited form
- S96 (≠ M83) binding
- N153 (≠ T141) 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 (≠ ST 266:267) binding
- A286 (≠ S273) 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 (= C365) modified: Disulfide link with 88, In inhibited form
- A386 (= A373) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
48% identity, 99% coverage: 1:377/379 of query aligns to 14:390/392 of 4xl4A
- active site: C88 (= C75), H348 (= H335), S378 (≠ C365), G380 (= G367)
- binding coenzyme a: L148 (= L136), H156 (≠ L144), R220 (≠ H208), L231 (= L218), A243 (= A230), S247 (= S234), F319 (= F306), H348 (= H335)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
48% identity, 100% coverage: 1:379/379 of query aligns to 14:392/393 of 6bn2A
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
48% identity, 99% coverage: 1:377/379 of query aligns to 15:392/394 of 1wl4A
- active site: C89 (= C75), H350 (= H335), C380 (= C365), G382 (= G367)
- binding coenzyme a: L148 (= L136), M157 (= M145), R220 (vs. gap), Y234 (≠ A221), P245 (≠ A230), A246 (= A231), S249 (= S234), A320 (= A305), F321 (= F306), H350 (= H335)
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)
48% identity, 99% coverage: 1:377/379 of query aligns to 18:395/397 of Q9BWD1
- K211 (= K196) to R: in dbSNP:rs25683
- R223 (vs. gap) binding
- S226 (≠ A210) binding
- S252 (= S234) binding
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
47% identity, 100% coverage: 1:378/379 of query aligns to 13:391/394 of 7cw5B
- active site: C87 (= C75), H348 (= H335), C378 (= C365), G380 (= G367)
- binding coenzyme a: L147 (= L136), H155 (≠ L144), M156 (= M145), R220 (≠ H208), T223 (≠ A210), A243 (= A230), P247 (≠ S234), L249 (≠ I236), H348 (= H335)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
46% identity, 100% coverage: 1:379/379 of query aligns to 12:389/389 of 2vu2A
- active site: C86 (= C75), H345 (= H335), C375 (= C365), G377 (= G367)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ L144), M154 (= M145), F232 (= F222), S244 (= S234), G245 (≠ S235), F316 (= F306), H345 (= H335)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
46% identity, 100% coverage: 1:379/379 of query aligns to 12:389/389 of 1dm3A
- active site: C86 (= C75), H345 (= H335), C375 (= C365), G377 (= G367)
- binding acetyl coenzyme *a: C86 (= C75), L145 (= L136), H153 (≠ L144), M154 (= M145), R217 (≠ P207), S224 (≠ K214), M225 (≠ I215), A240 (= A230), S244 (= S234), M285 (≠ F275), A315 (= A305), F316 (= F306), H345 (= H335), C375 (= C365)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
46% identity, 100% coverage: 1:379/379 of query aligns to 12:389/389 of 1dlvA
- active site: C86 (= C75), H345 (= H335), C375 (= C365), G377 (= G367)
- binding coenzyme a: C86 (= C75), L145 (= L136), H153 (≠ L144), M154 (= M145), R217 (≠ P207), L228 (= L218), A240 (= A230), S244 (= S234), H345 (= H335)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
46% identity, 100% coverage: 1:379/379 of query aligns to 14:391/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
46% identity, 100% coverage: 1:379/379 of query aligns to 15:392/392 of 1ou6A
- active site: C89 (= C75), H348 (= H335), C378 (= C365), G380 (= G367)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L136), H156 (≠ L144), M157 (= M145), F235 (= F222), A243 (= A230), S247 (= S234), A318 (= A305), F319 (= F306), H348 (= H335)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
46% identity, 100% coverage: 1:379/379 of query aligns to 12:389/389 of 2wkuA
- active site: C86 (= C75), H345 (= H335), C375 (= C365), G377 (= G367)
- binding D-mannose: R38 (= R27), K182 (≠ R173), D194 (= D185), V280 (≠ Q270), D281 (≠ H271), T287 (≠ C277), P331 (= P321), S332 (≠ E322), V334 (= V324), V336 (≠ I326), F360 (≠ Y350)
Sites not aligning to the query:
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: 1:379/379 of query aligns to 15:392/392 of P07097
- Q64 (= Q50) mutation to A: Slightly lower activity.
- C89 (= C75) mutation to A: Loss of activity.
- C378 (= C365) mutation to G: Loss of activity.
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
46% identity, 100% coverage: 1:379/379 of query aligns to 13:390/390 of 1m1oA
- active site: A87 (≠ C75), H346 (= H335), C376 (= C365), G378 (= G367)
- binding acetoacetyl-coenzyme a: L86 (= L74), A87 (≠ C75), L146 (= L136), H154 (≠ L144), M155 (= M145), R218 (≠ P207), S225 (≠ K214), M226 (≠ I215), A241 (= A230), G242 (≠ A231), S245 (= S234), A316 (= A305), F317 (= F306), H346 (= H335), I377 (= I366), G378 (= G367)
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
45% identity, 100% coverage: 1:379/379 of query aligns to 18:397/397 of 6aqpA
- active site: C93 (= C75), H353 (= H335), C383 (= C365), G385 (= G367)
- binding coenzyme a: C93 (= C75), L153 (= L136), Y188 (≠ L171), N226 (= N209), N228 (= N211), K231 (= K214), A248 (= A230), P249 (≠ A231), S252 (= S234), A323 (= A305), F324 (= F306), H353 (= H335)
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
45% identity, 100% coverage: 1:379/379 of query aligns to 18:399/399 of 6aqpC
- active site: C93 (= C75), H355 (= H335), C385 (= C365), G387 (= G367)
- binding acetyl coenzyme *a: C93 (= C75), L153 (= L136), M162 (= M145), Y188 (≠ L171), N230 (= N211), K233 (= K214), L234 (≠ I215), I237 (≠ L218), A250 (= A230), P251 (≠ A231), S254 (= S234), F295 (= F275), A325 (= A305), F326 (= F306), H355 (= H335)
Q4WCL5 Acetyl-CoA acetyltransferase erg10B, cytosolic; Acetoacetyl-CoA thiolase erg10B; ACAT; Cytosolic thiolase erg10B; CT; Ergosterol biosynthesis protein 10B; EC 2.3.1.9 from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
45% identity, 100% coverage: 1:379/379 of query aligns to 17:398/398 of Q4WCL5
- Y187 (≠ L171) binding
- N229 (= N211) binding
- K232 (= K214) binding
- A249 (= A230) binding
- P250 (≠ A231) binding
- S252 (≠ A233) binding
- S253 (= S234) binding
- V350 (≠ C331) binding
- N385 (≠ I366) binding
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
49% identity, 99% coverage: 1:377/379 of query aligns to 16:393/394 of 5f38D
- active site: C90 (= C75), A348 (= A332), A378 (= A362), L380 (= L364)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C75), L151 (= L136), A246 (= A230), S250 (= S234), I252 (= I236), A321 (= A305), F322 (= F306), H351 (= H335)
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)
47% identity, 99% coverage: 1:377/379 of query aligns to 14:391/393 of P14611
- C88 (= C75) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ L144) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ E205) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ P207) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S234) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H335) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C365) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
46% identity, 99% coverage: 1:377/379 of query aligns to 14:391/393 of 4o9cC
- active site: S88 (≠ C75), H349 (= H335), C379 (= C365), G381 (= G367)
- binding coenzyme a: S88 (≠ C75), L148 (= L136), R221 (≠ P207), F236 (= F222), A244 (= A230), S248 (= S234), L250 (≠ I236), A319 (= A305), F320 (= F306), H349 (= H335)
Query Sequence
>GFF2479 FitnessBrowser__Marino:GFF2479
MGGFQGSLASVSATDLGAITIAEAVRRAGLQPADVQEVIMGNVLPAGLKQGPARQAMRKA
GLPDHTGATTINKLCGSGMKAAMFAHDLIKAGSNDIMVAGGMESMSNAPYILQGVRSGYR
MGPGQAPQDHMFLDGLEDAETGRLMGAFAQEMADKKGYTREEMDEYAITSLTRAKKAIEE
GLLKDEIIPVTVKSRKGEVVVEDDEQPHNANIDKIPSLRPAFAKDGTVTAANASSISDGA
SALLLMRESEAEKRGLKPLARIVGHSTQSQHPSEFTCAPVGAIETLFGKTGWSKDDVDLF
EINEAFAMVAMMPIRELGLDPEKVNIHGGACAQGHPVGSTGSRLLVTLMYALQRYGKKKG
IAALCIGGGEATAMAIEML
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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