SitesBLAST
Comparing CCNA_03575 FitnessBrowser__Caulo:CCNA_03575 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)
45% identity, 99% coverage: 3:393/395 of query aligns to 51:437/462 of Q56WD9
- C138 (= C90) modified: Disulfide link with 192
- C192 (≠ A145) 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)
44% identity, 99% coverage: 3:393/395 of query aligns to 37:420/424 of P09110
- V387 (≠ A361) 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: 2:393/395 of query aligns to 5:388/390 of 2d3tC
- active site: C94 (= C90), H346 (= H351), C376 (= C381), G378 (= G383)
- binding acetyl coenzyme *a: C94 (= C90), R214 (= R223), L222 (= L231), L225 (= L234), A238 (= A246), G239 (= G247), S242 (= S250), I244 (≠ L252), A313 (= A321), F314 (= F322), H346 (= H351), C376 (= C381)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
42% identity, 98% coverage: 5:393/395 of query aligns to 6:390/392 of 1ou6A
- active site: C89 (= C90), H348 (= H351), C378 (= C381), G380 (= G383)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (vs. gap), H156 (≠ A149), M157 (= M150), F235 (≠ M238), A243 (= A246), S247 (= S250), A318 (= A321), F319 (= F322), H348 (= H351)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
42% identity, 98% coverage: 5:393/395 of query aligns to 5:389/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
42% identity, 98% coverage: 5:393/395 of query aligns to 3:387/389 of 2vu2A
- active site: C86 (= C90), H345 (= H351), 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 (≠ A149), M154 (= M150), F232 (≠ M238), S244 (= S250), G245 (≠ Q251), F316 (= F322), H345 (= H351)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
42% identity, 98% coverage: 5:393/395 of query aligns to 3:387/389 of 1dm3A
- active site: C86 (= C90), H345 (= H351), C375 (= C381), G377 (= G383)
- binding acetyl coenzyme *a: C86 (= C90), L145 (vs. gap), H153 (≠ A149), M154 (= M150), R217 (= R223), S224 (≠ G230), M225 (≠ L231), A240 (= A246), S244 (= S250), M285 (= M291), A315 (= A321), F316 (= F322), H345 (= H351), C375 (= C381)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
42% identity, 98% coverage: 5:393/395 of query aligns to 3:387/389 of 1dlvA
- active site: C86 (= C90), H345 (= H351), C375 (= C381), G377 (= G383)
- binding coenzyme a: C86 (= C90), L145 (vs. gap), H153 (≠ A149), M154 (= M150), R217 (= R223), L228 (= L234), A240 (= A246), S244 (= S250), H345 (= H351)
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: 4:393/395 of query aligns to 5:390/392 of P07097
- Q64 (≠ M65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C381) mutation to G: Loss of activity.
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
41% identity, 98% coverage: 5:393/395 of query aligns to 3:387/389 of 2wkuA
- active site: C86 (= C90), H345 (= H351), C375 (= C381), G377 (= G383)
- binding D-mannose: S6 (= S8), A7 (≠ Y9), R38 (= R41), K182 (≠ R178), D194 (= D190), V280 (≠ C286), D281 (≠ E287), T287 (≠ I293), P331 (= P337), S332 (≠ E338), V334 (≠ Y340), V336 (= V342), F360 (≠ L366)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
41% identity, 98% coverage: 5:393/395 of query aligns to 4:388/390 of 1m1oA
- active site: A87 (≠ C90), H346 (= H351), C376 (= C381), G378 (= G383)
- binding acetoacetyl-coenzyme a: L86 (≠ F89), A87 (≠ C90), L146 (vs. gap), H154 (≠ A149), M155 (= M150), R218 (= R223), S225 (≠ G230), M226 (≠ L231), A241 (= A246), G242 (= G247), S245 (= S250), A316 (= A321), F317 (= F322), H346 (= H351), I377 (= I382), G378 (= G383)
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)
41% identity, 99% coverage: 1:393/395 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 (≠ I151) 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 282:283) binding
- A286 (≠ D289) 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
8gqmA Crystal structure of thiolase complexed with acetyl coenzyme a
40% identity, 98% coverage: 5:393/395 of query aligns to 4:373/377 of 8gqmA
- binding acetyl coenzyme *a: K18 (≠ R19), S89 (≠ C90), M124 (≠ A125), M146 (= M150), R205 (= R223), T208 (= T226), L213 (= L231), L216 (= L234), A226 (= A246), A227 (≠ G247), S229 (≠ A249), S230 (= S250), M271 (= M291), A301 (= A321), H331 (= H351), L333 (≠ F353)
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
41% identity, 99% coverage: 1:393/395 of query aligns to 1:390/392 of 4xl4A
- active site: C88 (= C90), H348 (= H351), S378 (≠ C381), G380 (= G383)
- binding coenzyme a: L148 (= L146), H156 (vs. gap), R220 (= R223), L231 (= L234), A243 (= A246), S247 (= S250), F319 (= F322), H348 (= H351)
8oqmD Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-10
39% identity, 99% coverage: 3:393/395 of query aligns to 4:397/399 of 8oqmD
Sites not aligning to the query:
8opxC Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with trehalose (fragment-b-tre)
39% identity, 99% coverage: 3:393/395 of query aligns to 3:396/398 of 8opxC
8oqoC Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-49
39% identity, 99% coverage: 3:393/395 of query aligns to 3:396/398 of 8oqoC
8oqlC Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-1
39% identity, 99% coverage: 3:393/395 of query aligns to 3:395/397 of 8oqlC
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)
41% identity, 98% coverage: 1:389/395 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 (≠ A149) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ C221) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R223) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S250) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H351) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C381) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
39% identity, 99% coverage: 1:393/395 of query aligns to 3:393/394 of 5f38D
- active site: C90 (= C90), A348 (= A348), 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 (= C90), L151 (= L139), A246 (= A246), S250 (= S250), I252 (≠ L252), A321 (= A321), F322 (= F322), H351 (= H351)
Query Sequence
>CCNA_03575 FitnessBrowser__Caulo:CCNA_03575
MREAVIVSYARTGLAKSVRGGFNNTHGAAMAGHAIQHAVSRAGLEGAEVEDVVLGCGGPE
GATGMNVARNAAMWAGLPVTTSGQTINRFCSSGLQAIATAANYVRNDGANVAIGGGVESI
SLVNAGGHMNRFHITEEKLMQTHPALWMAMIDTADIVAKRYNVSREYQDEYALRSQQRIA
AAQAAGLFKDEIVPMATKMKVVNKETKEESFVDYVVDKDECNRADTTLEGLASLKPVMGE
GKFITAGNASQLSDGAAAVVVMEAKEAEKRGLTPLGAFRGFAVAGCEPDEMGIGPVFAVP
RLLERHGLKVDDIDIWELNEAFASQCLYSRDRLGIDPEKYNVNGGSIAIGHPFGMTGARC
AGHLLLEGKRRKAKLGVVTMCIGGGMGAAGLFEIF
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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