SitesBLAST
Comparing GFF3753 FitnessBrowser__WCS417:GFF3753 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)
Q56WD9 3-ketoacyl-CoA thiolase 2, peroxisomal; Acetyl-CoA acyltransferase 2; Beta-ketothiolase 2; Peroxisomal 3-oxoacyl-CoA thiolase 2; Peroxisome defective protein 1; EC 2.3.1.16 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
46% identity, 99% coverage: 3:391/394 of query aligns to 51:437/462 of Q56WD9
- C138 (= C90) modified: Disulfide link with 192
- C192 (≠ L144) modified: Disulfide link with 138
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)
43% identity, 99% coverage: 3:391/394 of query aligns to 37:420/424 of P09110
- V387 (= V359) 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)
41% identity, 99% coverage: 2:393/394 of query aligns to 5:390/390 of 2d3tC
- active site: C94 (= C90), H346 (= H349), C376 (= C379), G378 (= G381)
- binding acetyl coenzyme *a: C94 (= C90), R214 (= R221), L222 (= L229), L225 (= L232), A238 (= A244), G239 (= G245), S242 (= S248), I244 (≠ L250), A313 (= A319), F314 (= F320), H346 (= H349), C376 (= C379)
8gqmA Crystal structure of thiolase complexed with acetyl coenzyme a
40% identity, 99% coverage: 4:393/394 of query aligns to 3:375/377 of 8gqmA
- binding acetyl coenzyme *a: K18 (≠ R19), S89 (≠ C90), M124 (≠ L124), M146 (= M148), R205 (= R221), T208 (= T224), L213 (= L229), L216 (= L232), A226 (= A244), A227 (≠ G245), S229 (= S247), S230 (= S248), M271 (= M289), A301 (= A319), H331 (= H349), L333 (≠ F351)
P45359 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; CaTHL; EC 2.3.1.9 from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W) (see paper)
37% identity, 99% coverage: 1:391/394 of query aligns to 1:390/392 of P45359
- V77 (≠ T79) 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 acetate
- N153 (vs. gap) 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 (≠ TV 280:281) binding acetate
- A286 (≠ D287) 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 (≠ T387) binding acetate
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
37% identity, 99% coverage: 4:393/394 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C90), 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 (≠ P147), M154 (= M148), F232 (= F236), S244 (= S248), G245 (≠ Q249), F316 (= F320), H345 (= H349)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
37% identity, 99% coverage: 4:393/394 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C90), H345 (= H349), C375 (= C379), G377 (= G381)
- binding acetyl coenzyme *a: C86 (= C90), L145 (≠ V141), H153 (≠ P147), M154 (= M148), R217 (= R221), S224 (= S228), 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)
37% identity, 99% coverage: 4:393/394 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C90), H345 (= H349), C375 (= C379), G377 (= G381)
- binding coenzyme a: C86 (= C90), L145 (≠ V141), H153 (≠ P147), M154 (= M148), R217 (= R221), L228 (= L232), A240 (= A244), S244 (= S248), H345 (= H349)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
37% identity, 99% coverage: 4:393/394 of query aligns to 4:391/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
37% identity, 99% coverage: 4:393/394 of query aligns to 5:392/392 of 1ou6A
- active site: C89 (= C90), H348 (= H349), C378 (= C379), G380 (= G381)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ V141), H156 (≠ P147), M157 (= M148), F235 (= F236), A243 (= A244), S247 (= S248), A318 (= A319), F319 (= F320), H348 (= H349)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
37% identity, 99% coverage: 5:393/394 of query aligns to 6:392/392 of P07097
- Q64 (≠ Y65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C379) mutation to G: Loss of activity.
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
39% identity, 100% coverage: 2:394/394 of query aligns to 1:399/400 of 5bz4K
- active site: C87 (= C90), H354 (= H349), C384 (= C379), G386 (= G381)
- binding coenzyme a: C87 (= C90), R146 (≠ K138), M160 (= M148), R220 (= R221), A246 (= A244), G247 (= G245), S250 (= S248), Q252 (≠ L250), M291 (= M289), A321 (= A319), F322 (= F320), H354 (= H349)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
37% identity, 99% coverage: 4:393/394 of query aligns to 2:389/389 of 2wkuA
- active site: C86 (= C90), H345 (= H349), C375 (= C379), G377 (= G381)
- binding D-mannose: S6 (≠ D8), A7 (≠ S9), R38 (= R41), K182 (≠ R176), D194 (= D188), V280 (≠ C284), D281 (≠ E285), T287 (≠ I291), P331 (≠ N335), S332 (≠ A336), V334 (≠ Y338), V336 (= V340), F360 (≠ R364)
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
37% identity, 99% coverage: 1:391/394 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C90), H348 (= H349), S378 (≠ C379), G380 (= G381)
- binding coenzyme a: L148 (= L144), H156 (≠ P147), R220 (= R221), L231 (= L232), 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)
37% identity, 98% coverage: 1:385/394 of query aligns to 4:388/397 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 CoA
- T227 (= T224) binding CoA
- S251 (= S248) binding CoA
- C382 (= C379) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
37% identity, 99% coverage: 4:393/394 of query aligns to 3:390/390 of 1m1oA
- active site: A87 (≠ C90), H346 (= H349), C376 (= C379), G378 (= G381)
- binding acetoacetyl-coenzyme a: L86 (≠ F89), A87 (≠ C90), L146 (≠ V141), H154 (≠ P147), M155 (= M148), R218 (= R221), S225 (= S228), M226 (≠ L229), A241 (= A244), G242 (= G245), S245 (= S248), A316 (= A319), F317 (= F320), H346 (= H349), I377 (≠ V380), G378 (= G381)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
36% identity, 98% coverage: 1:385/394 of query aligns to 7:387/395 of 4c2jD
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)
37% identity, 98% coverage: 1:385/394 of query aligns to 1:385/393 of P14611
- C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ P147) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ C219) 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 (= 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.
8oqmD Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-10 (see paper)
37% identity, 99% coverage: 3:393/394 of query aligns to 4:399/399 of 8oqmD
8jg2A Crystal structure of a biosynthetic thiolase from megasphaera hexanoica soaked with hexanoyl-coa
37% identity, 98% coverage: 1:385/394 of query aligns to 2:384/393 of 8jg2A
Query Sequence
>GFF3753 FitnessBrowser__WCS417:GFF3753
MREVVIVDSVRTGLAKSFRGKFNQTRPDDMAAHCVNALLTRNGIDPATVEDCIVGAGSNE
GAQGYNIGRNVAVLSQLGTGTAGMTLNRFCSSGLQAIAIAANQIASGCSDIIVAGGVESI
SLTLKSVNTDNLINPLLKEQVPGLYFPMGQTAEIVARRYSVSREEQDMYALQSQQRTAQA
QADGLFDDEIVPMAVKYKVEDKNTGEAQVLDGVVDRDDCNRPDTTLASLQGLKPVFAEDG
SVTAGNSSQLSDGASMTLVMSLEKALALGLKPKAFFRGFTVAGCEPDEMGIGPVFSVPKL
LKAKGLQVADIDLWELNEAFASQCLYARNRLEIDNAKYNVNGGSISIGHPFGMTGSRQVG
HLVRELQRRNLRYGIVTMCVGGGMGATGLFEAVR
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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