SitesBLAST
Comparing H281DRAFT_00917 FitnessBrowser__Burk376:H281DRAFT_00917 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)
44% identity, 99% coverage: 3:390/392 of query aligns to 37:420/424 of P09110
- V387 (≠ T358) 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.
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
42% identity, 99% coverage: 3:390/392 of query aligns to 6:388/390 of 2d3tC
- active site: C94 (= C90), H346 (= H348), C376 (= C378), G378 (= G380)
- binding acetyl coenzyme *a: C94 (= C90), R214 (= R221), L222 (≠ V229), L225 (≠ I232), A238 (= A243), G239 (= G244), S242 (= S247), I244 (≠ F249), A313 (= A318), F314 (= F319), H346 (= H348), C376 (= C378)
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)
40% identity, 99% coverage: 1:390/392 of query aligns to 1:390/392 of P45359
- V77 (= V79) 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 (≠ A98) binding
- N153 (= N140) 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 279:280) binding
- A286 (≠ D286) 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 (= C378) modified: Disulfide link with 88, In inhibited form
- A386 (= A386) binding
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
41% identity, 99% coverage: 2:390/392 of query aligns to 3:390/392 of P07097
- Q64 (≠ M65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C378) mutation to G: Loss of activity.
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
42% identity, 98% coverage: 5:390/392 of query aligns to 5:389/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
42% identity, 98% coverage: 5:390/392 of query aligns to 6:390/392 of 1ou6A
- active site: C89 (= C90), H348 (= H348), C378 (= C378), G380 (= G380)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ K141), H156 (≠ S147), M157 (= M148), F235 (≠ L236), A243 (= A243), S247 (= S247), A318 (= A318), F319 (= F319), H348 (= H348)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
42% identity, 98% coverage: 5:390/392 of query aligns to 3:387/389 of 2vu2A
- active site: C86 (= C90), H345 (= H348), C375 (= C378), G377 (= G380)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ S147), M154 (= M148), F232 (≠ L236), S244 (= S247), G245 (≠ Q248), F316 (= F319), H345 (= H348)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
42% identity, 98% coverage: 5:390/392 of query aligns to 3:387/389 of 1dm3A
- active site: C86 (= C90), H345 (= H348), C375 (= C378), G377 (= G380)
- binding acetyl coenzyme *a: C86 (= C90), L145 (≠ K141), H153 (≠ S147), M154 (= M148), R217 (= R221), S224 (≠ G228), M225 (≠ V229), A240 (= A243), S244 (= S247), M285 (= M288), A315 (= A318), F316 (= F319), H345 (= H348), C375 (= C378)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
42% identity, 98% coverage: 5:390/392 of query aligns to 3:387/389 of 1dlvA
- active site: C86 (= C90), H345 (= H348), C375 (= C378), G377 (= G380)
- binding coenzyme a: C86 (= C90), L145 (≠ K141), H153 (≠ S147), M154 (= M148), R217 (= R221), L228 (≠ I232), A240 (= A243), S244 (= S247), H345 (= H348)
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
40% identity, 99% coverage: 1:390/392 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C90), H348 (= H348), S378 (≠ C378), G380 (= G380)
- binding coenzyme a: L148 (vs. gap), H156 (≠ S147), R220 (= R221), L231 (≠ I232), A243 (= A243), S247 (= S247), F319 (= F319), H348 (= H348)
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: 1:386/392 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 (≠ S147) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ G219) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R221) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S247) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H348) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C378) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
41% identity, 98% coverage: 5:390/392 of query aligns to 3:387/389 of 2wkuA
- active site: C86 (= C90), H345 (= H348), C375 (= C378), G377 (= G380)
- binding D-mannose: S6 (= S8), A7 (≠ T9), R38 (= R41), K182 (≠ R176), D194 (= D188), V280 (≠ C283), D281 (≠ E284), T287 (≠ I290), P331 (≠ H334), S332 (≠ D335), V334 (≠ L337), V336 (= V339), F360 (≠ I363)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
41% identity, 98% coverage: 5:390/392 of query aligns to 4:388/390 of 1m1oA
- active site: A87 (≠ C90), H346 (= H348), C376 (= C378), G378 (= G380)
- binding acetoacetyl-coenzyme a: L86 (≠ F89), A87 (≠ C90), L146 (≠ K141), H154 (≠ S147), M155 (= M148), R218 (= R221), S225 (≠ G228), M226 (≠ V229), A241 (= A243), G242 (= G244), S245 (= S247), A316 (= A318), F317 (= F319), H346 (= H348), I377 (= I379), G378 (= G380)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
43% identity, 98% coverage: 1:386/392 of query aligns to 1:387/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H348), C379 (= C378), G381 (= G380)
- binding coenzyme a: S88 (≠ C90), L148 (≠ K141), R221 (= R221), F236 (≠ L236), A244 (= A243), S248 (= S247), L250 (≠ F249), A319 (= A318), F320 (= F319), H349 (= H348)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
42% identity, 99% coverage: 1:390/392 of query aligns to 1:389/391 of 5f38B
- active site: C88 (= C90), H347 (= H348), C377 (= C378), G379 (= G380)
- binding coenzyme a: C88 (= C90), L149 (≠ W136), K219 (≠ R221), F234 (≠ L236), A242 (= A243), S246 (= S247), A317 (= A318), F318 (= F319), H347 (= H348)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
42% identity, 99% coverage: 1:390/392 of query aligns to 3:393/394 of 5f38D
- active site: C90 (= C90), A348 (= A345), A378 (≠ V375), L380 (≠ M377)
- 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 (≠ W136), A246 (= A243), S250 (= S247), I252 (≠ F249), A321 (= A318), F322 (= F319), H351 (= H348)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
40% identity, 91% coverage: 36:390/392 of query aligns to 41:393/395 of 4c2jD
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)
40% identity, 91% coverage: 36:390/392 of query aligns to 38:394/397 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 (= R221) binding
- T227 (= T224) binding
- S251 (= S247) binding
- C382 (= C378) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
41% identity, 99% coverage: 3:390/392 of query aligns to 2:396/400 of 5bz4K
- active site: C87 (= C90), H354 (= H348), C384 (= C378), G386 (= G380)
- binding coenzyme a: C87 (= C90), R146 (vs. gap), M160 (= M148), R220 (= R221), A246 (= A243), G247 (= G244), S250 (= S247), Q252 (≠ F249), M291 (= M288), A321 (= A318), F322 (= F319), H354 (= H348)
P24752 Acetyl-CoA acetyltransferase, mitochondrial; Acetoacetyl-CoA thiolase; T2; EC 2.3.1.9 from Homo sapiens (Human) (see 6 papers)
38% identity, 99% coverage: 1:390/392 of query aligns to 39:425/427 of P24752
- N93 (≠ C56) to S: in 3KTD; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074145
- N158 (≠ C122) to D: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs148639841
- G183 (≠ N140) to R: in 3KTD; no activity; dbSNP:rs120074141
- Y219 (≠ Q174) binding ; binding
- RVD 258:260 (≠ RAD 221:223) binding
- K263 (≠ G228) binding
- A280 (= A243) binding
- A281 (≠ G244) binding
- A283 (= A246) binding
- S284 (= S247) binding
- T297 (≠ N260) to M: in 3KTD; decreased protein abundance; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs886041122
- A301 (= A264) to P: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs1420321267
- I312 (≠ F275) to T: in 3KTD; decreased protein stability; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074146
- A333 (≠ V296) to P: in 3KTD; loss of protein solubility; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs120074147
- A380 (= A343) to T: in 3KTD; decreased protein stability; dbSNP:rs120074140
- V381 (≠ I344) binding
Sites not aligning to the query:
- 5 A → P: in dbSNP:rs3741056
Query Sequence
>H281DRAFT_00917 FitnessBrowser__Burk376:H281DRAFT_00917
MTDAVIVSTARTGLAKSWRGGFNMTHGATLGGHVTQAAVERAKLDPARVEDVIMGCANPE
GATGMNIARQIALRAGLPVSVPGMTVNRFCSSGLQTIALAAQRVMAGEGDVFVAGGVESI
SCVQNEMNQHMLTDGWLSKNKPEIYWSMLQTAENVAKRYSISKERQDEYGVRSQQRAAAA
LEAGKFKDEIVPLTVLAGVADKATGRLYTKEVTVSGDEGIRADTTLEGVSKIRTALPGGV
ITAGNASQFSDGASACVVMNAKVAEREGLQPLGIFRGFAVAGCEPDEMGIGPVFAVPKLL
KQAGLKVEDIDLWELNEAFAVQVLYCADKLGIPHDRLNVNGGAIAVGHPYGVSGARLTGH
ALIEGKRRGAKLVVVTMCIGGGQGAAGLFEVA
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