SitesBLAST
Comparing WP_041642232.1 NCBI__GCF_000061505.1:WP_041642232.1 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)
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)
47% identity, 98% coverage: 7:397/398 of query aligns to 51:438/462 of Q56WD9
- C138 (= C94) modified: Disulfide link with 192
- C192 (≠ I148) 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)
45% identity, 98% coverage: 7:396/398 of query aligns to 37:420/424 of P09110
- V387 (≠ T364) 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.
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
45% identity, 99% coverage: 5:398/398 of query aligns to 4:403/403 of 6pccA
- active site: C93 (= C94), A359 (≠ H354), C389 (= C384), G391 (= G386)
- binding coenzyme a: C93 (= C94), I148 (vs. gap), R229 (= R226), T232 (≠ A229), A252 (= A249), S256 (= S253), N325 (= N322), F328 (= F325)
- binding hexanal: N61 (≠ M62), T146 (vs. gap), I148 (vs. gap), G149 (vs. gap), R151 (vs. gap), L361 (= L356)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
45% identity, 99% coverage: 5:398/398 of query aligns to 4:403/403 of 6pcbA
- active site: C93 (= C94), A359 (≠ H354), C389 (= C384), G391 (= G386)
- binding coenzyme a: C93 (= C94), I148 (vs. gap), R229 (= R226), A252 (= A249), S256 (= S253), G257 (≠ Q254), N325 (= N322), F328 (= F325)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
42% identity, 98% coverage: 8:398/398 of query aligns to 5:392/392 of P07097
- Q64 (≠ M69) mutation to A: Slightly lower activity.
- C89 (= C94) mutation to A: Loss of activity.
- C378 (= C384) mutation to G: Loss of activity.
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
43% identity, 98% coverage: 10:398/398 of query aligns to 4:389/389 of 2vu2A
- active site: C86 (= C94), H345 (= H354), C375 (= C384), G377 (= G386)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ G153), M154 (= M154), F232 (= F241), S244 (= S253), G245 (≠ Q254), F316 (= F325), H345 (= H354)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
43% identity, 98% coverage: 10:398/398 of query aligns to 4:389/389 of 1dm3A
- active site: C86 (= C94), H345 (= H354), C375 (= C384), G377 (= G386)
- binding acetyl coenzyme *a: C86 (= C94), L145 (≠ Q145), H153 (≠ G153), M154 (= M154), R217 (= R226), S224 (≠ A233), M225 (≠ L234), A240 (= A249), S244 (= S253), M285 (= M294), A315 (= A324), F316 (= F325), H345 (= H354), C375 (= C384)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
43% identity, 98% coverage: 10:398/398 of query aligns to 4:389/389 of 1dlvA
- active site: C86 (= C94), H345 (= H354), C375 (= C384), G377 (= G386)
- binding coenzyme a: C86 (= C94), L145 (≠ Q145), H153 (≠ G153), M154 (= M154), R217 (= R226), L228 (= L237), A240 (= A249), S244 (= S253), H345 (= H354)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
43% identity, 98% coverage: 10:398/398 of query aligns to 6:391/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
43% identity, 98% coverage: 10:398/398 of query aligns to 7:392/392 of 1ou6A
- active site: C89 (= C94), H348 (= H354), C378 (= C384), G380 (= G386)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ Q145), H156 (≠ G153), M157 (= M154), F235 (= F241), A243 (= A249), S247 (= S253), A318 (= A324), F319 (= F325), H348 (= H354)
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
44% identity, 99% coverage: 6:398/398 of query aligns to 5:390/390 of 2d3tC
- active site: C94 (= C94), H346 (= H354), C376 (= C384), G378 (= G386)
- binding acetyl coenzyme *a: C94 (= C94), R214 (= R226), L222 (= L234), L225 (= L237), A238 (= A249), G239 (= G250), S242 (= S253), I244 (≠ M255), A313 (= A324), F314 (= F325), H346 (= H354), C376 (= C384)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
43% identity, 98% coverage: 10:398/398 of query aligns to 4:389/389 of 2wkuA
- active site: C86 (= C94), H345 (= H354), C375 (= C384), G377 (= G386)
- binding D-mannose: S6 (≠ A12), A7 (= A13), R38 (≠ Q44), K182 (≠ R182), D194 (= D194), V280 (= V289), D281 (≠ P290), T287 (≠ I296), P331 (= P340), S332 (≠ A341), V334 (= V343), V336 (≠ P345), F360 (≠ R369)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
45% identity, 99% coverage: 5:398/398 of query aligns to 5:401/401 of 6pcdA
- active site: S94 (≠ C94), A357 (≠ H354), C387 (= C384), G389 (= G386)
- binding coenzyme a: I149 (vs. gap), M167 (= M154), R227 (= R226), T230 (≠ A229), A250 (= A249), S254 (= S253), G255 (≠ Q254), A325 (= A324), A357 (≠ H354)
- binding octanal: N62 (≠ M62), T147 (vs. gap), T148 (vs. gap), I149 (vs. gap), G150 (vs. gap), R152 (vs. gap), L359 (= L356)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
43% identity, 98% coverage: 10:398/398 of query aligns to 5:390/390 of 1m1oA
- active site: A87 (≠ C94), H346 (= H354), C376 (= C384), G378 (= G386)
- binding acetoacetyl-coenzyme a: L86 (≠ F93), A87 (≠ C94), L146 (≠ Q145), H154 (≠ G153), M155 (= M154), R218 (= R226), S225 (≠ A233), M226 (≠ L234), A241 (= A249), G242 (= G250), S245 (= S253), A316 (= A324), F317 (= F325), H346 (= H354), I377 (≠ V385), G378 (= G386)
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)
41% identity, 99% coverage: 5:397/398 of query aligns to 1:391/392 of P45359
- V77 (≠ E83) 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 (= C94) modified: Disulfide link with 378, In inhibited form
- S96 (≠ A102) binding acetate
- N153 (≠ I150) 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 285:286) binding acetate
- A286 (≠ R292) 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 (= C384) modified: Disulfide link with 88, In inhibited form
- A386 (= A392) binding acetate
8gqmA Crystal structure of thiolase complexed with acetyl coenzyme a
43% identity, 98% coverage: 10:398/398 of query aligns to 5:375/377 of 8gqmA
- binding acetyl coenzyme *a: K18 (≠ N22), S89 (≠ C94), M124 (≠ I130), M146 (= M154), R205 (= R213), T208 (≠ A229), L213 (= L234), L216 (= L237), A226 (= A249), A227 (≠ G250), S229 (= S252), S230 (= S253), M271 (= M294), A301 (= A324), H331 (= H354), L333 (= L356)
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
40% identity, 99% coverage: 5:397/398 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C94), H348 (= H354), S378 (≠ C384), G380 (= G386)
- binding coenzyme a: L148 (≠ Q145), H156 (≠ G153), R220 (= R226), L231 (= L237), A243 (= A249), S247 (= S253), F319 (= F325), H348 (= H354)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
42% identity, 99% coverage: 5:397/398 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C94), A348 (= A351), A378 (≠ I381), L380 (≠ M383)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C94), L151 (vs. gap), A246 (= A249), S250 (= S253), I252 (≠ M255), A321 (= A324), F322 (= F325), H351 (= H354)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
42% identity, 99% coverage: 5:398/398 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C94), H347 (= H354), C377 (= C384), G379 (= G386)
- binding coenzyme a: C88 (= C94), L149 (vs. gap), K219 (≠ R226), F234 (= F241), A242 (= A249), S246 (= S253), A317 (= A324), F318 (= F325), H347 (= H354)
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, 97% coverage: 9:396/398 of query aligns to 8:394/397 of P42765
- C92 (= C94) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R226) binding CoA
- T227 (≠ A229) binding CoA
- S251 (= S253) binding CoA
- C382 (= C384) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
Query Sequence
>WP_041642232.1 NCBI__GCF_000061505.1:WP_041642232.1
MSTQIQDAYIVAAVRTPVAKRNGAFRHVRPDDMLAHVLRAVVAQVPALDAGEIGDVITGC
AMPEAEQGMNVARIGLLLAGLPERVPGVTLNRFCASSLQAVADAANRIRLGEADVMIAAG
TESMSAMPQIMGNKVSLNPEIFARQENIDIAYGMGLTAEKVAEEWKVSRADQDAFALQSH
QRASAAIADGSFGDEIAPYTVRSHLPGEGGTVRIAERIVDTDEGPRADATLEALARLKPV
FAARGSVTAGNSSQMSDGAGAVLLMSETALQRYGVTPLARFRSYAVAGVPPRVMGIGPVE
AIPRALRLAGLGLDALDRIELNEAFAAQALAVIRTLGLDPARVNPQGGAIALGHPLGATG
AIRTATLMRAMRQGGVRHGMITMCVGTGMGAAAIFERV
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