SitesBLAST
Comparing PfGW456L13_2411 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2411 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)
50% identity, 99% coverage: 5:392/393 of query aligns to 3:391/392 of P45359
- V77 (≠ K80) 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 (≠ I99) binding
- N153 (≠ H155) 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 280:281) binding
- A286 (≠ E287) 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 (= C379) modified: Disulfide link with 88, In inhibited form
- A386 (= A387) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
49% identity, 99% coverage: 5:392/393 of query aligns to 3:391/392 of 4xl4A
- active site: C88 (= C91), H348 (= H349), S378 (≠ C379), G380 (= G381)
- binding coenzyme a: L148 (= L150), H156 (= H158), R220 (= R222), L231 (≠ M232), A243 (= A244), S247 (= S248), F319 (= F320), H348 (= H349)
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, 98% coverage: 6:391/393 of query aligns to 7:394/397 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 (= R222) binding
- T227 (= T224) binding
- S251 (= S248) binding
- C382 (= C379) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
46% identity, 98% coverage: 6:391/393 of query aligns to 10:393/395 of 4c2jD
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
46% identity, 100% coverage: 2:393/393 of query aligns to 1:392/392 of 1ou6A
- active site: C89 (= C91), H348 (= H349), C378 (= C379), G380 (= G381)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L150), H156 (= H158), M157 (= M159), F235 (= F236), A243 (= A244), S247 (= S248), A318 (= A319), F319 (= F320), H348 (= H349)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
46% identity, 99% coverage: 3:393/393 of query aligns to 1:391/391 of 2vu1A
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)
49% identity, 99% coverage: 5:392/393 of query aligns to 3:392/393 of P14611
- C88 (= C91) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (= H158) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ H220) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R222) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S248) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H349) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C379) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
50% identity, 98% coverage: 8:392/393 of query aligns to 8:394/394 of 5f38D
- active site: C90 (= C91), A348 (= A346), A378 (≠ V376), L380 (≠ M378)
- 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 (≠ F154), A246 (= A244), S250 (= S248), I252 (≠ L250), A321 (= A319), F322 (= F320), H351 (= H349)
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: 1:393/393 of query aligns to 1:392/392 of P07097
- Q64 (≠ R64) mutation to A: Slightly lower activity.
- C89 (= C91) mutation to A: Loss of activity.
- C378 (= C379) mutation to G: Loss of activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
48% identity, 99% coverage: 5:392/393 of query aligns to 3:392/393 of 4o9cC
- active site: S88 (≠ C91), H349 (= H349), C379 (= C379), G381 (= G381)
- binding coenzyme a: S88 (≠ C91), L148 (= L150), R221 (= R222), F236 (= F236), A244 (= A244), S248 (= S248), L250 (= L250), A319 (= A319), F320 (= F320), H349 (= H349)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
46% identity, 99% coverage: 6:393/393 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C91), H345 (= H349), C375 (= C379), G377 (= G381)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (= H158), M154 (= M159), F232 (= F236), S244 (= S248), G245 (= G249), F316 (= F320), H345 (= H349)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
46% identity, 99% coverage: 6:393/393 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C91), H345 (= H349), C375 (= C379), G377 (= G381)
- binding acetyl coenzyme *a: C86 (= C91), L145 (= L150), H153 (= H158), M154 (= M159), R217 (= R222), S224 (≠ Q228), M225 (≠ L229), A240 (= A244), S244 (= S248), M285 (= M289), A315 (= A319), F316 (= F320), H345 (= H349), C375 (= C379)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
46% identity, 99% coverage: 6:393/393 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C91), H345 (= H349), C375 (= C379), G377 (= G381)
- binding coenzyme a: C86 (= C91), L145 (= L150), H153 (= H158), M154 (= M159), R217 (= R222), L228 (≠ M232), A240 (= A244), S244 (= S248), H345 (= H349)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
46% identity, 99% coverage: 4:393/393 of query aligns to 1:390/390 of 1m1oA
- active site: A87 (≠ C91), H346 (= H349), C376 (= C379), G378 (= G381)
- binding acetoacetyl-coenzyme a: L86 (= L90), A87 (≠ C91), L146 (= L150), H154 (= H158), M155 (= M159), R218 (= R222), S225 (≠ Q228), M226 (≠ L229), A241 (= A244), G242 (= G245), S245 (= S248), A316 (= A319), F317 (= F320), H346 (= H349), I377 (= I380), G378 (= G381)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
46% identity, 99% coverage: 6:393/393 of query aligns to 2:389/389 of 2wkuA
- active site: C86 (= C91), H345 (= H349), C375 (= C379), G377 (= G381)
- binding D-mannose: S6 (= S10), A7 (= A11), R38 (= R42), K182 (≠ R187), D194 (≠ E199), V280 (= V284), D281 (≠ E285), T287 (≠ L291), P331 (= P335), S332 (≠ A336), V334 (= V338), V336 (≠ P340), F360 (≠ H364)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
50% identity, 98% coverage: 8:393/393 of query aligns to 6:391/391 of 5f38B
- active site: C88 (= C91), H347 (= H349), C377 (= C379), G379 (= G381)
- binding coenzyme a: C88 (= C91), L149 (≠ F154), K219 (≠ R222), F234 (= F236), A242 (= A244), S246 (= S248), A317 (= A319), F318 (= F320), H347 (= H349)
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
43% identity, 98% coverage: 6:392/393 of query aligns to 5:393/394 of 1wl4A
- active site: C89 (= C91), H350 (= H349), C380 (= C379), G382 (= G381)
- binding coenzyme a: L148 (= L150), M157 (= M159), R220 (= R222), Y234 (≠ A235), P245 (≠ A244), A246 (≠ G245), S249 (= S248), A320 (= A319), F321 (= F320), H350 (= H349)
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)
43% identity, 98% coverage: 6:392/393 of query aligns to 8:396/397 of Q9BWD1
- K211 (= K210) to R: in dbSNP:rs25683
- R223 (= R222) binding
- S226 (≠ T224) binding
- S252 (= S248) binding
7feaB Py14 in complex with col-d (see paper)
45% identity, 99% coverage: 5:393/393 of query aligns to 4:393/396 of 7feaB
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
44% identity, 98% coverage: 8:393/393 of query aligns to 5:398/400 of 5bz4K
- active site: C87 (= C91), H354 (= H349), C384 (= C379), G386 (= G381)
- binding coenzyme a: C87 (= C91), R146 (≠ L147), M160 (≠ I161), R220 (= R222), A246 (= A244), G247 (= G245), S250 (= S248), Q252 (≠ L250), M291 (= M289), A321 (= A319), F322 (= F320), H354 (= H349)
Query Sequence
>PfGW456L13_2411 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2411
MNTPEIYVVSAARTAIGTFGGSLKDVPLADLATTAVKAALERAAVDPALVGHLVMGNVIP
TETRDAYISRVAAMNAGIPKETPAYNVNRLCGSGLQAIINAAQTLMLGDADIVVGAGAES
MSRGPYLMPAARWGSRMGNAQVIDYMLGILHDPFHGIHMGITAENVAARNGITREMQDAL
AFEDQQRAAHAIANGYFSEQIATVEIQDRKGVKLFSVDEHPRATSLEQLAAMKPAFKKDG
SVTAGNASGLNDGAAALVMASGNAVQANNLKPLARLVSYAHAGVEPEFMGLGPIPATRLA
LKRAGLTVADLDVIEANIAFAAQACAVSQELDLDPAKVNPNGSGIALGHPVGATGAIIAT
KAIHELHRTGGRYALVTMCIGGGQGIAAIFERV
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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