SitesBLAST
Comparing WP_068458935.1 NCBI__GCF_001541235.1:WP_068458935.1 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)
8jg2A Crystal structure of a biosynthetic thiolase from megasphaera hexanoica soaked with hexanoyl-coa
32% identity, 97% coverage: 5:423/434 of query aligns to 2:390/393 of 8jg2A
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
31% identity, 96% coverage: 8:424/434 of query aligns to 2:388/389 of 2wkuA
- active site: C86 (= C92), H345 (= H382), C375 (= C411), G377 (≠ A413)
- binding D-mannose: S6 (≠ G12), A7 (≠ G13), R38 (= R44), K182 (= K205), D194 (= D217), V280 (≠ A296), D281 (≠ N297), T287 (≠ D303), P331 (= P368), S332 (≠ A369), V334 (≠ I371), V336 (= V373), F360 (≠ K397)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
31% identity, 96% coverage: 10:424/434 of query aligns to 7:391/392 of P07097
- Q64 (≠ F67) mutation to A: Slightly lower activity.
- C89 (= C92) mutation to A: Loss of activity.
- C378 (= C411) mutation to G: Loss of activity.
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
31% identity, 96% coverage: 8:424/434 of query aligns to 2:388/389 of 2vu2A
- active site: C86 (= C92), H345 (= H382), C375 (= C411), G377 (≠ A413)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ S176), M154 (= M177), F232 (= F247), S244 (≠ T261), G245 (≠ P262), F316 (= F336), H345 (= H382)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
31% identity, 96% coverage: 8:424/434 of query aligns to 2:388/389 of 1dm3A
- active site: C86 (= C92), H345 (= H382), C375 (= C411), G377 (≠ A413)
- binding acetyl coenzyme *a: C86 (= C92), L145 (≠ K151), H153 (≠ S176), M154 (= M177), R217 (= R232), S224 (≠ K239), M225 (≠ L240), A240 (= A257), S244 (≠ T261), M285 (≠ A301), A315 (= A335), F316 (= F336), H345 (= H382), C375 (= C411)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
31% identity, 96% coverage: 8:424/434 of query aligns to 2:388/389 of 1dlvA
- active site: C86 (= C92), H345 (= H382), C375 (= C411), G377 (≠ A413)
- binding coenzyme a: C86 (= C92), L145 (≠ K151), H153 (≠ S176), M154 (= M177), R217 (= R232), L228 (= L243), A240 (= A257), S244 (≠ T261), H345 (= H382)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
31% identity, 96% coverage: 8:424/434 of query aligns to 5:391/392 of 1ou6A
- active site: C89 (= C92), H348 (= H382), C378 (= C411), G380 (≠ A413)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ K151), H156 (≠ S176), M157 (= M177), F235 (= F247), A243 (= A257), S247 (≠ T261), A318 (= A335), F319 (= F336), H348 (= H382)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
31% identity, 96% coverage: 8:424/434 of query aligns to 4:390/391 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)
32% identity, 97% coverage: 5:425/434 of query aligns to 1:393/393 of P14611
- C88 (= C92) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ S176) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ N230) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R232) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (≠ T261) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H382) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C411) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
31% identity, 96% coverage: 8:424/434 of query aligns to 3:389/390 of 1m1oA
- active site: A87 (≠ C92), H346 (= H382), C376 (= C411), G378 (≠ A413)
- binding acetoacetyl-coenzyme a: L86 (≠ A91), A87 (≠ C92), L146 (≠ K151), H154 (≠ S176), M155 (= M177), R218 (= R232), S225 (≠ K239), M226 (≠ L240), A241 (= A257), G242 (= G258), S245 (≠ T261), A316 (= A335), F317 (= F336), H346 (= H382), I377 (≠ T412), G378 (≠ A413)
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
30% identity, 94% coverage: 15:423/434 of query aligns to 10:396/400 of 5bz4K
- active site: C87 (= C92), H354 (= H382), C384 (= C411), G386 (≠ A413)
- binding coenzyme a: C87 (= C92), R146 (≠ K154), M160 (= M177), R220 (= R232), A246 (= A257), G247 (= G258), S250 (≠ T261), Q252 (≠ L263), M291 (≠ L305), A321 (= A335), F322 (= F336), H354 (= H382)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
32% identity, 97% coverage: 5:425/434 of query aligns to 1:393/393 of 4o9cC
- active site: S88 (≠ C92), H349 (= H382), C379 (= C411), G381 (≠ A413)
- binding coenzyme a: S88 (≠ C92), L148 (= L150), R221 (= R232), F236 (= F247), A244 (= A257), S248 (≠ T261), L250 (= L263), A319 (= A335), F320 (= F336), H349 (= H382)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
32% identity, 97% coverage: 5:423/434 of query aligns to 3:393/394 of 5f38D
- active site: C90 (= C92), A348 (= A379), A378 (≠ I408), L380 (≠ I410)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C92), L151 (= L150), A246 (= A257), S250 (≠ T261), I252 (≠ L263), A321 (= A335), F322 (= F336), H351 (= H382)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
32% identity, 97% coverage: 5:423/434 of query aligns to 1:389/391 of 5f38B
- active site: C88 (= C92), H347 (= H382), C377 (= C411), G379 (≠ A413)
- binding coenzyme a: C88 (= C92), L149 (= L150), K219 (≠ R232), F234 (= F247), A242 (= A257), S246 (≠ T261), A317 (= A335), F318 (= F336), H347 (= H382)
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)
31% identity, 97% coverage: 8:429/434 of query aligns to 52:443/462 of Q56WD9
- C138 (= C92) modified: Disulfide link with 192
- C192 (≠ F146) 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)
30% identity, 96% coverage: 8:423/434 of query aligns to 38:420/424 of P09110
- V387 (= V392) 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.
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)
30% identity, 97% coverage: 5:423/434 of query aligns to 1:390/392 of P45359
- V77 (≠ P81) 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 (= C92) modified: Disulfide link with 378, In inhibited form
- S96 (≠ L100) binding acetate
- N153 (≠ T173) 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 (≠ SQ 292:293) binding acetate
- A286 (≠ F299) 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 (= C411) modified: Disulfide link with 88, In inhibited form
- A386 (= A419) binding acetate
8gqmA Crystal structure of thiolase complexed with acetyl coenzyme a
32% identity, 97% coverage: 8:426/434 of query aligns to 3:376/377 of 8gqmA
- binding acetyl coenzyme *a: K18 (≠ S21), S89 (≠ C92), M124 (≠ I127), M146 (= M177), R205 (= R232), T208 (≠ A235), L213 (= L240), L216 (= L243), A226 (= A257), A227 (≠ G258), S229 (= S260), S230 (≠ T261), M271 (≠ L305), A301 (= A335), H331 (= H382), L333 (≠ F384)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
29% identity, 97% coverage: 4:424/434 of query aligns to 6:394/395 of 4c2jD
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
29% identity, 96% coverage: 7:423/434 of query aligns to 2:390/394 of 7cw5B
- active site: C87 (= C92), H348 (= H382), C378 (= C411), G380 (≠ A413)
- binding coenzyme a: L147 (≠ F156), H155 (≠ S176), M156 (= M177), R220 (= R232), T223 (≠ A235), A243 (= A257), P247 (≠ T261), L249 (= L263), H348 (= H382)
Query Sequence
>WP_068458935.1 NCBI__GCF_001541235.1:WP_068458935.1
MQRFMRRVAVIGGARIPFCRSNTFYADLTNLDLMTGALNALIDRYGLKGQHIDEVVGGAV
ITHSKDFNLTREAVLSTALAPSTPGITMMQACGTSLQAALGSAAKIATGDIDCAIAVGSD
TTSDAPIVVSKKLAKRLTQAAQRKTFMDKLKTFKGFAPGELVPQAPANAEPRTGLSMGEH
AEMMAREWGITRDAQDRFALESHLKAAEAYRSGYMDDIVTPFAGVFRDNNIRADASIDKL
SSLKASFDKSGKGTLTAGNSTPLTDGAAAVLLASEDWAEKHGLPVAAYLTYSQSAANDFV
AGDGLLMAPTIAVSRMLDRAGLKLQDFDFYEIHEAFAAQVLATLKAWEDPTYCRQVLGRP
EAMGAIDPAKINVHGSSIALGHPFAATGARIVGNMAKLLAGHHGRGLISICTAGGMGVAA
ILESKDAAEIHQAA
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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