SitesBLAST
Comparing WP_054557392.1 NCBI__GCF_001306415.1:WP_054557392.1 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)
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, 98% coverage: 6:394/396 of query aligns to 40:421/424 of P09110
- V387 (≠ S359) 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)
42% identity, 99% coverage: 1:393/396 of query aligns to 1:390/392 of P45359
- V77 (= V80) 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 (= C91) modified: Disulfide link with 378, In inhibited form
- S96 (≠ G99) binding acetate
- N153 (≠ E143) 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 (≠ AA 280:281) binding acetate
- A286 (≠ R287) 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 (= C381) modified: Disulfide link with 88, In inhibited form
- A386 (= A389) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
41% identity, 99% coverage: 1:393/396 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C91), H348 (= H349), S378 (≠ C381), G380 (= G383)
- binding coenzyme a: L148 (≠ V138), H156 (≠ Y146), R220 (= R221), L231 (= L232), A243 (= A244), S247 (= S248), F319 (= F320), H348 (= H349)
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)
41% identity, 98% coverage: 6:393/396 of query aligns to 54:437/462 of Q56WD9
- C138 (= C91) modified: Disulfide link with 192
- C192 (≠ Y145) modified: Disulfide link with 138
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
41% identity, 99% coverage: 2:393/396 of query aligns to 5:388/390 of 2d3tC
- active site: C94 (= C91), H346 (= H349), C376 (= C381), G378 (= G383)
- binding acetyl coenzyme *a: C94 (= C91), R214 (= R221), L222 (= L229), L225 (= L232), A238 (= A244), G239 (= G245), S242 (= S248), I244 (≠ T250), A313 (= A319), F314 (= F320), H346 (= H349), C376 (= C381)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
42% identity, 100% coverage: 1:395/396 of query aligns to 1:391/391 of 5f38B
- active site: C88 (= C91), H347 (= H349), C377 (= C381), G379 (= G383)
- binding coenzyme a: C88 (= C91), L149 (vs. gap), K219 (≠ R221), F234 (= F236), A242 (= A244), S246 (= S248), A317 (= A319), F318 (= F320), H347 (= H349)
8gqmA Crystal structure of thiolase complexed with acetyl coenzyme a
40% identity, 98% coverage: 6:393/396 of query aligns to 4:373/377 of 8gqmA
- binding acetyl coenzyme *a: K18 (≠ R19), S89 (≠ C91), M124 (= M126), M146 (= M149), R205 (= R221), T208 (= T224), L213 (= L229), L216 (= L232), A226 (= A244), A227 (≠ G245), S229 (= S247), S230 (= S248), M271 (= M289), A301 (= A319), H331 (= H349), L333 (= L351)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
39% identity, 98% coverage: 6:395/396 of query aligns to 4:389/389 of 2vu2A
- active site: C86 (= C91), H345 (= H349), C375 (= C381), G377 (= G383)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (vs. gap), M154 (= M149), F232 (= F236), S244 (= S248), G245 (≠ Q249), F316 (= F320), H345 (= H349)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
39% identity, 98% coverage: 6:395/396 of query aligns to 4:389/389 of 1dm3A
- active site: C86 (= C91), H345 (= H349), C375 (= C381), G377 (= G383)
- binding acetyl coenzyme *a: C86 (= C91), L145 (≠ H142), H153 (vs. gap), M154 (= M149), R217 (= R221), S224 (≠ A228), M225 (≠ L229), A240 (= A244), S244 (= S248), M285 (= M289), A315 (= A319), F316 (= F320), H345 (= H349), C375 (= C381)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
39% identity, 98% coverage: 6:395/396 of query aligns to 4:389/389 of 1dlvA
- active site: C86 (= C91), H345 (= H349), C375 (= C381), G377 (= G383)
- binding coenzyme a: C86 (= C91), L145 (≠ H142), H153 (vs. gap), M154 (= M149), R217 (= R221), L228 (= L232), A240 (= A244), S244 (= S248), H345 (= H349)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
39% identity, 98% coverage: 6:395/396 of query aligns to 7:392/392 of P07097
- Q64 (≠ L66) mutation to A: Slightly lower activity.
- C89 (= C91) mutation to A: Loss of activity.
- C378 (= C381) mutation to G: Loss of activity.
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
39% identity, 98% coverage: 6:395/396 of query aligns to 6:391/391 of 2vu1A
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
40% identity, 99% coverage: 1:393/396 of query aligns to 7:393/395 of 4c2jD
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
39% identity, 98% coverage: 6:395/396 of query aligns to 7:392/392 of 1ou6A
- active site: C89 (= C91), H348 (= H349), C378 (= C381), G380 (= G383)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ H142), H156 (vs. gap), M157 (= M149), F235 (= F236), A243 (= A244), S247 (= S248), A318 (= A319), 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)
40% identity, 99% coverage: 1:393/396 of query aligns to 4:394/397 of P42765
- C92 (= C91) 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 (= C381) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
41% identity, 99% coverage: 1:393/396 of query aligns to 3:393/394 of 5f38D
- active site: C90 (= C91), A348 (= A346), A378 (≠ V378), L380 (≠ M380)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C91), L151 (vs. gap), A246 (= A244), S250 (= S248), I252 (≠ T250), A321 (= A319), F322 (= F320), H351 (= H349)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
39% identity, 98% coverage: 6:395/396 of query aligns to 4:389/389 of 2wkuA
- active site: C86 (= C91), H345 (= H349), C375 (= C381), G377 (= G383)
- binding D-mannose: S6 (≠ K8), A7 (≠ G9), R38 (≠ M42), K182 (= K177), D194 (= D189), V280 (= V284), D281 (≠ P285), T287 (≠ I291), P331 (= P335), S332 (≠ D336), V334 (≠ I338), V336 (= V340), F360 (≠ D364)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
39% identity, 98% coverage: 6:395/396 of query aligns to 5:390/390 of 1m1oA
- active site: A87 (≠ C91), H346 (= H349), C376 (= C381), G378 (= G383)
- binding acetoacetyl-coenzyme a: L86 (≠ F90), A87 (≠ C91), L146 (≠ H142), H154 (vs. gap), M155 (= M149), R218 (= R221), S225 (≠ A228), M226 (≠ L229), A241 (= A244), G242 (= G245), S245 (= S248), A316 (= A319), F317 (= F320), H346 (= H349), I377 (≠ V382), G378 (= G383)
8jg2A Crystal structure of a biosynthetic thiolase from megasphaera hexanoica soaked with hexanoyl-coa
36% identity, 98% coverage: 1:389/396 of query aligns to 2:386/393 of 8jg2A
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
38% identity, 99% coverage: 2:393/396 of query aligns to 1:396/400 of 5bz4K
- active site: C87 (= C91), H354 (= H349), C384 (= C381), G386 (= G383)
- binding coenzyme a: C87 (= C91), R146 (vs. gap), M160 (= M149), R220 (= R221), A246 (= A244), G247 (= G245), S250 (= S248), Q252 (≠ T250), M291 (= M289), A321 (= A319), F322 (= F320), H354 (= H349)
Query Sequence
>WP_054557392.1 NCBI__GCF_001306415.1:WP_054557392.1
MRTAYIVKGYRTAVGKSGRGGFRFKRADELAAETIAHLVGKMPEFDKKRIDDVIVGNAMP
EGSQGLNMARLISLMGLDIVDVPGVTVNRFCSSGLETIGIASAKIQAGMADCIIAGGVES
MSSVPMTGFKTELNYDIVKSGHEDYYWGMGNTAEAVAQEYKVSREDQDEFAFNSHMKALK
ALDENRFQDQIVPIEVEQTYVDTNGKKATKKFTVNKDEGPRRGTSMEALAKLRPVFAANG
SVTAGNSSQTSDGAAFVMVMSEEMVKELNVEPIARLVNYAAAGVPPRIMGIGPVAAVPKA
LKQAGLQQQDIALIELNEAFASQSLAVIRELDLNPDIINVNGGAIALGHPLGCTGAKLSV
QLFDEMRKRDMKGKHGMVTMCVGTGQGAAGIFEFLN
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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