SitesBLAST
Comparing 5210417 FitnessBrowser__PV4:5210417 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)
P09110 3-ketoacyl-CoA thiolase, peroxisomal; Acetyl-CoA C-myristoyltransferase; Acetyl-CoA acyltransferase; Beta-ketothiolase; Peroxisomal 3-oxoacyl-CoA thiolase; EC 2.3.1.16; EC 2.3.1.155; EC 2.3.1.9 from Homo sapiens (Human) (see 3 papers)
42% identity, 99% coverage: 3:392/394 of query aligns to 37:420/424 of P09110
- V387 (= V360) to A: in dbSNP:rs2229528
Sites not aligning to the query:
- 1:26 PTS2-type peroxisomal targeting signal
- 5 mutation Q->D,K,L: Does not affect localization to peroxisomes.
- 6 V→D: Abolished localization to peroxisomes.; V→K: Does not affect localization to peroxisomes.
- 7 mutation V->D,K: Abolished localization to peroxisomes.
- 8 mutation L->D,K: Does not affect localization to peroxisomes.
- 9 mutation G->D,R,L: Does not affect localization to peroxisomes.
- 10 H→E: In S3E mutant; Abolished localization to peroxisomes.
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)
43% identity, 98% coverage: 1:388/394 of query aligns to 1:387/393 of P14611
- C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ P149) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ C221) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R223) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S249) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H350) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C380) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
42% identity, 98% coverage: 1:388/394 of query aligns to 1:387/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H350), C379 (= C380), G381 (= G382)
- binding coenzyme a: S88 (≠ C90), L148 (vs. gap), R221 (= R223), F236 (≠ I238), A244 (= A245), S248 (= S249), L250 (= L251), A319 (= A320), F320 (= F321), H349 (= H350)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
40% identity, 98% coverage: 5:392/394 of query aligns to 3:387/389 of 2vu2A
- active site: C86 (= C90), H345 (= H350), C375 (= C380), G377 (= G382)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ P149), M154 (= M150), F232 (≠ I238), S244 (= S249), G245 (≠ Q250), F316 (= F321), H345 (= H350)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
40% identity, 98% coverage: 5:392/394 of query aligns to 3:387/389 of 1dm3A
- active site: C86 (= C90), H345 (= H350), C375 (= C380), G377 (= G382)
- binding acetyl coenzyme *a: C86 (= C90), L145 (vs. gap), H153 (≠ P149), M154 (= M150), R217 (= R223), S224 (= S230), M225 (≠ L231), A240 (= A245), S244 (= S249), M285 (= M290), A315 (= A320), F316 (= F321), H345 (= H350), C375 (= C380)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
40% identity, 98% coverage: 5:392/394 of query aligns to 3:387/389 of 1dlvA
- active site: C86 (= C90), H345 (= H350), C375 (= C380), G377 (= G382)
- binding coenzyme a: C86 (= C90), L145 (vs. gap), H153 (≠ P149), M154 (= M150), R217 (= R223), L228 (= L234), A240 (= A245), S244 (= S249), H345 (= H350)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
40% identity, 98% coverage: 5:392/394 of query aligns to 5:389/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
40% identity, 98% coverage: 5:392/394 of query aligns to 6:390/392 of 1ou6A
- active site: C89 (= C90), H348 (= H350), C378 (= C380), G380 (= G382)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (vs. gap), H156 (≠ P149), M157 (= M150), F235 (≠ I238), A243 (= A245), S247 (= S249), A318 (= A320), F319 (= F321), H348 (= H350)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
39% identity, 99% coverage: 4:392/394 of query aligns to 5:390/392 of P07097
- Q64 (≠ M65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C380) mutation to G: Loss of activity.
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
39% identity, 98% coverage: 5:392/394 of query aligns to 3:387/389 of 2wkuA
- active site: C86 (= C90), H345 (= H350), C375 (= C380), G377 (= G382)
- binding D-mannose: S6 (= S8), A7 (≠ T9), R38 (= R41), K182 (≠ R178), D194 (= D190), V280 (≠ C285), D281 (≠ A286), T287 (≠ I292), P331 (= P336), S332 (≠ A337), V334 (≠ Y339), V336 (= V341), F360 (≠ I365)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
39% identity, 98% coverage: 5:392/394 of query aligns to 4:388/390 of 1m1oA
- active site: A87 (≠ C90), H346 (= H350), C376 (= C380), G378 (= G382)
- binding acetoacetyl-coenzyme a: L86 (≠ Q89), A87 (≠ C90), L146 (vs. gap), H154 (≠ P149), M155 (= M150), R218 (= R223), S225 (= S230), M226 (≠ L231), A241 (= A245), G242 (= G246), S245 (= S249), A316 (= A320), F317 (= F321), H346 (= H350), I377 (= I381), G378 (= G382)
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)
38% identity, 98% coverage: 1:388/394 of query aligns to 4:390/397 of P42765
- C92 (= C90) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R223) binding
- T227 (= T226) binding
- S251 (= S249) binding
- C382 (= C380) 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)
37% identity, 98% coverage: 1:388/394 of query aligns to 7:389/395 of 4c2jD
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
39% identity, 99% coverage: 2:392/394 of query aligns to 5:388/390 of 2d3tC
- active site: C94 (= C90), H346 (= H350), C376 (= C380), G378 (= G382)
- binding acetyl coenzyme *a: C94 (= C90), R214 (= R223), L222 (= L231), L225 (= L234), A238 (= A245), G239 (= G246), S242 (= S249), I244 (≠ L251), A313 (= A320), F314 (= F321), H346 (= H350), C376 (= C380)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
40% identity, 99% coverage: 1:392/394 of query aligns to 1:389/391 of 5f38B
- active site: C88 (= C90), H347 (= H350), C377 (= C380), G379 (= G382)
- binding coenzyme a: C88 (= C90), L149 (≠ M140), K219 (≠ R223), F234 (≠ I238), A242 (= A245), S246 (= S249), A317 (= A320), F318 (= F321), H347 (= H350)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
39% identity, 99% coverage: 1:392/394 of query aligns to 3:393/394 of 5f38D
- active site: C90 (= C90), A348 (≠ S347), A378 (≠ V377), L380 (≠ M379)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C90), L151 (≠ M140), A246 (= A245), S250 (= S249), I252 (≠ L251), A321 (= A320), F322 (= F321), H351 (= H350)
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, 99% coverage: 1:392/394 of query aligns to 1:390/392 of P45359
- V77 (≠ N79) 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 (= C90) modified: Disulfide link with 378, In inhibited form
- S96 (≠ G98) binding
- N153 (≠ A146) 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 (≠ AV 281:282) binding
- A286 (≠ E288) 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 (= C380) modified: Disulfide link with 88, In inhibited form
- A386 (= A388) binding
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
36% identity, 99% coverage: 3:393/394 of query aligns to 2:391/394 of 7cw5B
- active site: C87 (= C90), H348 (= H350), C378 (= C380), G380 (= G382)
- binding coenzyme a: L147 (≠ M148), H155 (= H156), M156 (vs. gap), R220 (= R223), T223 (= T226), A243 (= A245), P247 (≠ S249), L249 (= L251), H348 (= H350)
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
36% identity, 99% coverage: 1:392/394 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C90), H348 (= H350), S378 (≠ C380), G380 (= G382)
- binding coenzyme a: L148 (vs. gap), H156 (≠ P149), R220 (= R223), L231 (= L234), A243 (= A245), S247 (= S249), F319 (= F321), H348 (= H350)
2f2sA Human mitochondrial acetoacetyl-coa thiolase
35% identity, 99% coverage: 3:392/394 of query aligns to 10:387/389 of 2f2sA
- active site: C95 (= C90), H347 (= H350), C375 (= C380), G377 (= G382)
- binding coenzyme a: C95 (= C90), L153 (vs. gap), H161 (≠ P149), M162 (= M150), Y188 (≠ Q176), R220 (≠ A208), V221 (≠ I209), D222 (≠ S210), K225 (≠ Q213), L229 (≠ P224), F233 (≠ M228), A242 (= A245), S246 (= S249), A317 (= A320), F318 (= F321), H347 (= H350)
Query Sequence
>5210417 FitnessBrowser__PV4:5210417
MREAVIVSTARTGMAKSFRGSLNNTKSPTMLGHCIKQAVQRAGVEGGEIDDAIMGTVLTA
GTAGMNIARNAVLAAGLPNTVSAQTIDRQCSSGLMAIGMAAKQIIVDQQQIVVAGGQENI
TAVQNEYMKWAADNADPNVMQFEPHAYMPMLKTAEHVAKVYGVSREAQDIYALMSQQRTA
AAQEAGYFDDEIVPFTTTMAIQDRETKAISYQQVTLDRDECNRPSTTMESLQNLAPVIEG
GFITAGNASQLSDGASACVVMERKLAEQRGLAPLGIYRGIAVAGCAPEEMGIGPIYAIPK
LLKQHGLTIDDIGLWEINEAFAVQALYCRDHLGIDPARYNVNGGGISIGHPYGMTGSRLV
GHALIEGKRRGVKYVVVGMCIGGGMGAAGLFEVA
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