SitesBLAST
Comparing CCNA_00544 FitnessBrowser__Caulo:CCNA_00544 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)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
70% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C88), 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 (= H155), M154 (= M156), F232 (= F234), S244 (= S246), G245 (= G247), F316 (= F318), H345 (= H347)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
70% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C88), H345 (= H347), C375 (= C377), G377 (= G379)
- binding acetyl coenzyme *a: C86 (= C88), L145 (= L147), H153 (= H155), M154 (= M156), R217 (= R219), S224 (= S226), M225 (≠ V227), 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)
70% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C88), H345 (= H347), C375 (= C377), G377 (= G379)
- binding coenzyme a: C86 (= C88), L145 (= L147), H153 (= H155), M154 (= M156), R217 (= R219), L228 (= L230), A240 (= A242), S244 (= S246), H345 (= H347)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
70% identity, 99% coverage: 4:391/391 of query aligns to 5:392/392 of 1ou6A
- active site: C89 (= C88), H348 (= H347), C378 (= C377), G380 (= G379)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L147), H156 (= H155), M157 (= M156), 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)
70% identity, 99% coverage: 4:391/391 of query aligns to 4:391/391 of 2vu1A
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
70% identity, 99% coverage: 4:391/391 of query aligns to 2:389/389 of 2wkuA
- active site: C86 (= C88), H345 (= H347), C375 (= C377), G377 (= G379)
- binding D-mannose: S6 (= S8), A7 (= A9), R38 (= R40), K182 (≠ R184), D194 (= D196), V280 (= V282), D281 (≠ E283), T287 (= T289), P331 (= P333), S332 (≠ A334), V334 (= V336), V336 (= V338), F360 (≠ H362)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
70% identity, 99% coverage: 4:391/391 of query aligns to 3:390/390 of 1m1oA
- active site: A87 (≠ C88), H346 (= H347), C376 (= C377), G378 (= G379)
- binding acetoacetyl-coenzyme a: L86 (= L87), A87 (≠ C88), L146 (= L147), H154 (= H155), M155 (= M156), R218 (= R219), S225 (= S226), M226 (≠ V227), A241 (= A242), G242 (≠ A243), S245 (= S246), A316 (= A317), F317 (= F318), H346 (= H347), I377 (≠ V378), G378 (= G379)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
69% identity, 99% coverage: 5:391/391 of query aligns to 6:392/392 of P07097
- Q64 (= Q63) mutation to A: Slightly lower activity.
- C89 (= C88) mutation to A: Loss of activity.
- C378 (= C377) 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)
63% identity, 99% coverage: 1:389/391 of query aligns to 1:390/392 of P45359
- V77 (= V77) 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 (≠ A96) binding
- N153 (≠ H152) 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 (≠ AN 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
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
63% identity, 99% coverage: 1:389/391 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C88), H348 (= H347), S378 (≠ C377), G380 (= G379)
- binding coenzyme a: L148 (= L147), H156 (= H155), R220 (= R219), L231 (= L230), A243 (= A242), S247 (= S246), F319 (= F318), H348 (= H347)
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)
65% identity, 99% coverage: 1:389/391 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 (= H155) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (= F217) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R219) 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.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
65% identity, 99% coverage: 1:389/391 of query aligns to 1:391/393 of 4o9cC
- active site: S88 (≠ C88), H349 (= H347), C379 (= C377), G381 (= G379)
- binding coenzyme a: S88 (≠ C88), L148 (= L147), R221 (= R219), F236 (= F234), A244 (= A242), S248 (= S246), L250 (= L248), A319 (= A317), F320 (= F318), H349 (= 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)
61% identity, 99% coverage: 4:389/391 of query aligns to 8:395/397 of Q9BWD1
- K211 (= K207) to R: in dbSNP:rs25683
- R223 (= R219) binding
- S226 (≠ A222) binding
- S252 (= S246) binding
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
61% identity, 99% coverage: 4:389/391 of query aligns to 5:392/394 of 1wl4A
- active site: C89 (= C88), H350 (= H347), C380 (= C377), G382 (= G379)
- binding coenzyme a: L148 (= L147), M157 (= M156), R220 (= R219), Y234 (≠ V233), P245 (≠ A242), A246 (= A243), S249 (= S246), A320 (= A317), F321 (= F318), H350 (= H347)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
55% identity, 99% coverage: 1:389/391 of query aligns to 3:393/394 of 5f38D
- active site: C90 (= C88), A348 (= A344), A378 (= A374), L380 (= L376)
- 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 (= A242), S250 (= S246), I252 (≠ L248), A321 (= A317), F322 (= F318), H351 (= H347)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
54% identity, 99% coverage: 1:389/391 of query aligns to 1:389/391 of 5f38B
- active site: C88 (= C88), H347 (= H347), C377 (= C377), G379 (= G379)
- binding coenzyme a: C88 (= C88), L149 (= L147), K219 (≠ R219), F234 (= F234), A242 (= A242), S246 (= S246), A317 (= A317), F318 (= F318), H347 (= H347)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
47% identity, 100% coverage: 1:391/391 of query aligns to 1:392/393 of 6bn2A
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
51% identity, 99% coverage: 2:389/391 of query aligns to 1:390/394 of 7cw5B
- active site: C87 (= C88), H348 (= H347), C378 (= C377), G380 (= G379)
- binding coenzyme a: L147 (= L147), H155 (= H155), M156 (= M156), R220 (= R219), T223 (≠ A222), A243 (= A242), P247 (≠ S246), L249 (= L248), H348 (= H347)
7feaB Py14 in complex with col-d (see paper)
48% identity, 99% coverage: 3:391/391 of query aligns to 4:393/396 of 7feaB
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)
46% identity, 99% coverage: 4:390/391 of query aligns to 7:395/397 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 (= R219) binding
- T227 (≠ A222) binding
- S251 (= S246) binding
- C382 (= C377) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
Query Sequence
>CCNA_00544 FitnessBrowser__Caulo:CCNA_00544
MSEIVIVSAARTPVGSFNGALASLPASELGKAVIEAAVSRAGIAPSDVDEVILGQVLQAA
AGQGPARQASVKAGIPVEAPAWSLNQLCGSGLRAVALAAQQIADGSAKVVVAGGQESMSQ
APHAQNLRGGQKMGDLQFVDTMIKDGLWDAFHGYHMGQTAENIASRWQITREDQDKFAVT
SQNRAEAAQKAGKFDDEIVPITIKGRKGDTIVDKDEFIRHGATIESVQGLKPVFNKEGSV
TAANASGLNDGAAALVLMSAEEAAKRGLKPLARIASWANAGVEPEIMGTGPIPASKKALE
KAGWSVSDLDLVESNEAFAAQALCVVRELGLDPAKVNVNGGAIAIGHPIGASGARILTTL
VHEMKRSGAKKGLATLCVGGGMGVAMCVEAV
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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