SitesBLAST
Comparing AZOBR_RS20220 AZOBR_RS20220 acetyl-CoA acetyltransferase to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
48% identity, 99% coverage: 6:382/382 of query aligns to 3:390/390 of 2d3tC
- active site: C94 (= C94), H346 (= H338), C376 (= C368), G378 (= G370)
- binding acetyl coenzyme *a: C94 (= C94), R214 (= R210), L222 (= L218), L225 (= L221), A238 (= A233), G239 (= G234), S242 (= S237), I244 (≠ L239), A313 (= A308), F314 (= F309), H346 (= H338), C376 (= C368)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
42% identity, 100% coverage: 2:382/382 of query aligns to 1:392/392 of 1ou6A
- active site: C89 (= C94), H348 (= H338), C378 (= C368), G380 (= G370)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ Y144), H156 (≠ S150), M157 (= M151), F235 (= F225), A243 (= A233), S247 (= S237), A318 (= A308), F319 (= F309), H348 (= H338)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
42% identity, 99% coverage: 3:382/382 of query aligns to 1:391/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
42% identity, 98% coverage: 8:382/382 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C94), H345 (= H338), C375 (= C368), G377 (= G370)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ S150), M154 (= M151), F232 (= F225), S244 (= S237), G245 (≠ P238), F316 (= F309), H345 (= H338)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
42% identity, 98% coverage: 8:382/382 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C94), H345 (= H338), C375 (= C368), G377 (= G370)
- binding acetyl coenzyme *a: C86 (= C94), L145 (≠ Y144), H153 (≠ S150), M154 (= M151), R217 (= R210), S224 (≠ T217), M225 (≠ L218), A240 (= A233), S244 (= S237), M285 (= M278), A315 (= A308), F316 (= F309), H345 (= H338), C375 (= C368)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
42% identity, 98% coverage: 8:382/382 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C94), H345 (= H338), C375 (= C368), G377 (= G370)
- binding coenzyme a: C86 (= C94), L145 (≠ Y144), H153 (≠ S150), M154 (= M151), R217 (= R210), L228 (= L221), A240 (= A233), S244 (= S237), H345 (= H338)
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: 5:382/382 of query aligns to 2:392/392 of P07097
- Q64 (≠ M69) mutation to A: Slightly lower activity.
- C89 (= C94) mutation to A: Loss of activity.
- C378 (= C368) mutation to G: Loss of activity.
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
42% identity, 98% coverage: 8:382/382 of query aligns to 2:389/389 of 2wkuA
- active site: C86 (= C94), H345 (= H338), C375 (= C368), G377 (= G370)
- binding D-mannose: S6 (≠ G12), A7 (≠ Y13), R38 (= R45), K182 (= K179), D194 (≠ E191), V280 (≠ C273), D281 (≠ A274), T287 (≠ L280), P331 (= P324), S332 (≠ A325), V334 (= V327), V336 (≠ L329), F360 (≠ A353)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
42% identity, 98% coverage: 8:382/382 of query aligns to 3:390/390 of 1m1oA
- active site: A87 (≠ C94), H346 (= H338), C376 (= C368), G378 (= G370)
- binding acetoacetyl-coenzyme a: L86 (≠ Y93), A87 (≠ C94), L146 (≠ Y144), H154 (≠ S150), M155 (= M151), R218 (= R210), S225 (≠ T217), M226 (≠ L218), A241 (= A233), G242 (= G234), S245 (= S237), A316 (= A308), F317 (= F309), H346 (= H338), I377 (= I369), G378 (= G370)
Q9BWD1 Acetyl-CoA acetyltransferase, cytosolic; Acetyl-CoA transferase-like protein; Cytosolic acetoacetyl-CoA thiolase; EC 2.3.1.9 from Homo sapiens (Human) (see 2 papers)
39% identity, 98% coverage: 5:380/382 of query aligns to 5:395/397 of Q9BWD1
- K211 (≠ A200) to R: in dbSNP:rs25683
- R223 (= R210) binding
- S226 (≠ T213) binding
- S252 (= S237) binding
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
39% identity, 98% coverage: 5:380/382 of query aligns to 2:392/394 of 1wl4A
- active site: C89 (= C94), H350 (= H338), C380 (= C368), G382 (= G370)
- binding coenzyme a: L148 (≠ Y144), M157 (= M151), R220 (= R210), Y234 (≠ A224), P245 (≠ A233), A246 (≠ G234), S249 (= S237), A320 (= A308), F321 (= F309), H350 (= H338)
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, 98% coverage: 8:380/382 of query aligns to 4:390/392 of P45359
- V77 (≠ L83) 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 (≠ H102) binding
- N153 (≠ P145) 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 269:270) binding
- A286 (≠ E276) 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 (= C368) modified: Disulfide link with 88, In inhibited form
- A386 (= A376) binding
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)
41% identity, 98% coverage: 5:380/382 of query aligns to 36:420/424 of P09110
- V387 (≠ T348) 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.
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
38% identity, 98% coverage: 8:381/382 of query aligns to 10:394/395 of 4c2jD
8opyD Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-b-dnq
38% identity, 96% coverage: 15:382/382 of query aligns to 12:401/401 of 8opyD
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
41% identity, 98% coverage: 8:380/382 of query aligns to 4:390/392 of 4xl4A
- active site: C88 (= C94), H348 (= H338), S378 (≠ C368), G380 (= G370)
- binding coenzyme a: L148 (= L140), H156 (≠ Y148), R220 (= R210), L231 (= L221), A243 (= A233), S247 (= S237), F319 (= F309), H348 (= H338)
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)
43% identity, 98% coverage: 8:380/382 of query aligns to 4:391/393 of P14611
- C88 (= C94) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ Y148) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ C208) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R210) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S237) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H338) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C368) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
44% identity, 94% coverage: 24:382/382 of query aligns to 22:403/403 of 6pccA
- active site: C93 (= C94), A359 (≠ H338), C389 (= C368), G391 (= G370)
- binding coenzyme a: C93 (= C94), I148 (≠ M130), R229 (= R210), T232 (= T213), A252 (= A233), S256 (= S237), N325 (= N306), F328 (= F309)
- binding hexanal: N61 (≠ F62), T146 (vs. gap), I148 (≠ M130), G149 (= G131), R151 (≠ N133), L361 (= L340)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
44% identity, 94% coverage: 24:382/382 of query aligns to 22:403/403 of 6pcbA
- active site: C93 (= C94), A359 (≠ H338), C389 (= C368), G391 (= G370)
- binding coenzyme a: C93 (= C94), I148 (≠ M130), R229 (= R210), A252 (= A233), S256 (= S237), G257 (≠ P238), N325 (= N306), F328 (= F309)
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, 98% coverage: 8:381/382 of query aligns to 7:395/397 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 (= R210) binding
- T227 (= T213) binding
- S251 (= S237) binding
- C382 (= C368) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
Query Sequence
>AZOBR_RS20220 AZOBR_RS20220 acetyl-CoA acetyltransferase
LTTPANPVVIAGYARSPFAFANKGELAKVRPDDLLAHVVAALVERTGVNPQDIEDVVVGC
AFPEGEQGMNIARTVSFLAKLPLTAGATTINRYCGSSMQAIHQAAGAIQMGAGEVFLCGG
IESMSRVPMMGYNPLPHPGLKDHYPEAYCSMGVTAENVARRYEISRADQEAMAAESHAKA
AAAQQAGRLAEEIVAIQTAAGLVERDGCIRPGTSGETLSGLKPAFLADGSVTAGTSSPLT
DGASAVLVTTEAYAKANGLPILARIRSVAVAGCAPEVMGLGPVPAAQKALARAGLSIRDI
DVIELNEAFAAQAIACMRDLDIDPAKVNLDGGAIALGHPLGATGARITGKAAALLKREGK
QFALATQCIGGGQGIATVLEAV
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