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Comparing WP_043745132.1 AMB_RS18210 acetyl-CoA C-acyltransferase 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)
6bn2A Crystal structure of acetyl-coa acetyltransferase from elizabethkingia anophelis nuhp1
48% identity, 98% coverage: 6:392/394 of query aligns to 4:390/393 of 6bn2A
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)
48% identity, 98% coverage: 6:392/394 of query aligns to 4:390/392 of P45359
- V77 (≠ R79) 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 (≠ M98) binding
- N153 (≠ D155) 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 (≠ TN 281:282) binding
- A286 (= A288) 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 (= C380) modified: Disulfide link with 88, In inhibited form
- A386 (= A388) binding
6aqpA Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
50% identity, 100% coverage: 1:393/394 of query aligns to 2:396/397 of 6aqpA
- active site: C93 (= C90), H353 (= H350), C383 (= C380), G385 (= G382)
- binding coenzyme a: C93 (= C90), L153 (= L150), Y188 (≠ L186), N226 (≠ K224), N228 (≠ L226), K231 (= K229), A248 (= A245), P249 (≠ A246), S252 (= S249), A323 (= A320), F324 (= F321), H353 (= H350)
6aqpC Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with coa and potassium ions
50% identity, 100% coverage: 1:393/394 of query aligns to 2:398/399 of 6aqpC
- active site: C93 (= C90), H355 (= H350), C385 (= C380), G387 (= G382)
- binding acetyl coenzyme *a: C93 (= C90), L153 (= L150), M162 (= M160), Y188 (≠ L186), N230 (≠ L226), K233 (= K229), L234 (≠ I230), I237 (≠ L233), A250 (= A245), P251 (≠ A246), S254 (= S249), F295 (= F290), A325 (= A320), F326 (= F321), H355 (= H350)
Q4WCL5 Acetyl-CoA acetyltransferase erg10B, cytosolic; Acetoacetyl-CoA thiolase erg10B; ACAT; Cytosolic thiolase erg10B; CT; Ergosterol biosynthesis protein 10B; EC 2.3.1.9 from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
50% identity, 100% coverage: 1:393/394 of query aligns to 1:397/398 of Q4WCL5
- Y187 (≠ L186) binding
- N229 (≠ L226) binding
- K232 (= K229) binding
- A249 (= A245) binding
- P250 (≠ A246) binding
- S252 (= S248) binding
- S253 (= S249) binding
- V350 (≠ C346) binding
- N385 (≠ I381) binding
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
48% identity, 98% coverage: 6:392/394 of query aligns to 4:390/392 of 4xl4A
- active site: C88 (= C90), H348 (= H350), S378 (≠ C380), G380 (= G382)
- binding coenzyme a: L148 (= L150), H156 (≠ R158), R220 (vs. gap), L231 (= L233), A243 (= A245), S247 (= S249), F319 (= F321), H348 (= H350)
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)
50% identity, 98% coverage: 6:392/394 of query aligns to 4:391/393 of P14611
- C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ R158) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (vs. gap) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (≠ Q221) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S249) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H350) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C380) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
7cw5B Acetyl-coa acetyltransferase from bacillus cereus atcc 14579 (see paper)
47% identity, 98% coverage: 7:393/394 of query aligns to 4:391/394 of 7cw5B
- active site: C87 (= C90), H348 (= H350), C378 (= C380), G380 (= G382)
- binding coenzyme a: L147 (= L150), H155 (≠ L159), M156 (= M160), R220 (≠ G223), T223 (≠ L226), A243 (= A245), P247 (≠ S249), L249 (≠ I251), H348 (= H350)
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
47% identity, 99% coverage: 2:392/394 of query aligns to 1:390/392 of 1ou6A
- active site: C89 (= C90), H348 (= H350), C378 (= C380), G380 (= G382)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (= L150), H156 (≠ L159), M157 (= M160), F235 (= F237), A243 (= A245), S247 (= S249), A318 (= A320), F319 (= F321), H348 (= H350)
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
47% identity, 99% coverage: 3:392/394 of query aligns to 1:389/391 of 2vu1A
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
47% identity, 98% coverage: 6:392/394 of query aligns to 2:387/389 of 2vu2A
- active site: C86 (= C90), H345 (= H350), C375 (= C380), G377 (= G382)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ L159), M154 (= M160), F232 (= F237), S244 (= S249), G245 (≠ S250), F316 (= F321), H345 (= H350)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
47% identity, 98% coverage: 6:392/394 of query aligns to 2:387/389 of 1dm3A
- active site: C86 (= C90), H345 (= H350), C375 (= C380), G377 (= G382)
- binding acetyl coenzyme *a: C86 (= C90), L145 (= L150), H153 (≠ L159), M154 (= M160), R217 (≠ Q221), S224 (≠ K229), M225 (≠ I230), A240 (= A245), S244 (= S249), M285 (≠ F290), A315 (= A320), F316 (= F321), H345 (= H350), C375 (= C380)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
47% identity, 98% coverage: 6:392/394 of query aligns to 2:387/389 of 1dlvA
- active site: C86 (= C90), H345 (= H350), C375 (= C380), G377 (= G382)
- binding coenzyme a: C86 (= C90), L145 (= L150), H153 (≠ L159), M154 (= M160), R217 (≠ Q221), L228 (= L233), A240 (= A245), S244 (= S249), H345 (= H350)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
50% identity, 98% coverage: 6:392/394 of query aligns to 4:391/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H350), C379 (= C380), G381 (= G382)
- binding coenzyme a: S88 (≠ C90), L148 (= L150), R221 (≠ Q221), F236 (= F237), A244 (= A245), S248 (= S249), L250 (≠ I251), A319 (= A320), F320 (= F321), H349 (= H350)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
46% identity, 99% coverage: 3:392/394 of query aligns to 2:390/392 of P07097
- Q64 (= Q65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C380) mutation to G: Loss of activity.
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
47% identity, 98% coverage: 6:392/394 of query aligns to 2:387/389 of 2wkuA
- active site: C86 (= C90), H345 (= H350), C375 (= C380), G377 (= G382)
- binding D-mannose: S6 (≠ G10), A7 (= A11), R38 (= R42), K182 (≠ R188), D194 (≠ A200), V280 (≠ Q285), D281 (≠ E286), T287 (= T292), P331 (≠ H336), S332 (≠ E337), V334 (= V339), V336 (= V341), F360 (≠ S365)
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
47% identity, 98% coverage: 6:392/394 of query aligns to 3:388/390 of 1m1oA
- active site: A87 (≠ C90), H346 (= H350), C376 (= C380), G378 (= G382)
- binding acetoacetyl-coenzyme a: L86 (≠ V89), A87 (≠ C90), L146 (= L150), H154 (≠ L159), M155 (= M160), R218 (≠ Q221), S225 (≠ K229), M226 (≠ I230), A241 (= A245), G242 (≠ A246), S245 (= S249), A316 (= A320), F317 (= F321), H346 (= H350), I377 (= I381), G378 (= G382)
2ib8D Crystallographic and kinetic studies of human mitochondrial acetoacetyl-coa thiolase (t2): the importance of potassium and chloride for its structure and function (see paper)
46% identity, 99% coverage: 2:392/394 of query aligns to 4:391/393 of 2ib8D
P24752 Acetyl-CoA acetyltransferase, mitochondrial; Acetoacetyl-CoA thiolase; T2; EC 2.3.1.9 from Homo sapiens (Human) (see 6 papers)
46% identity, 99% coverage: 2:392/394 of query aligns to 38:425/427 of P24752
- N93 (≠ C57) to S: in 3KTD; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074145
- N158 (= N122) to D: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs148639841
- G183 (= G149) to R: in 3KTD; no activity; dbSNP:rs120074141
- Y219 (≠ L186) binding ; binding
- RVD 258:260 (≠ KAL 224:226) binding
- K263 (= K229) binding
- A280 (= A245) binding
- A281 (= A246) binding
- A283 (≠ S248) binding
- S284 (= S249) binding
- T297 (≠ R262) to M: in 3KTD; decreased protein abundance; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs886041122
- A301 (= A266) to P: in 3KTD; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs1420321267
- I312 (≠ V277) to T: in 3KTD; decreased protein stability; decreased acetyl-CoA C-acyltransferase activity; less than 10% of the degradative/thiolase activity; dbSNP:rs120074146
- A333 (≠ I298) to P: in 3KTD; loss of protein solubility; loss of acetyl-CoA C-acyltransferase activity; no degradative/thiolase activity; dbSNP:rs120074147
- A380 (= A345) to T: in 3KTD; decreased protein stability; dbSNP:rs120074140
- V381 (≠ C346) binding
Sites not aligning to the query:
- 5 A → P: in dbSNP:rs3741056
2f2sA Human mitochondrial acetoacetyl-coa thiolase
46% identity, 98% coverage: 6:392/394 of query aligns to 11:387/389 of 2f2sA
- active site: C95 (= C90), H347 (= H350), C375 (= C380), G377 (= G382)
- binding coenzyme a: C95 (= C90), L153 (= L150), H161 (≠ R158), M162 (= M160), Y188 (≠ L186), R220 (≠ K224), V221 (≠ A225), D222 (≠ L226), K225 (= K229), L229 (= L233), F233 (= F237), A242 (= A245), S246 (= S249), A317 (= A320), F318 (= F321), H347 (= H350)
Query Sequence
>WP_043745132.1 AMB_RS18210 acetyl-CoA C-acyltransferase
MTTDPIVIVGAARTPMGGFQGDFASLAAPQLGAAAIRAAVERSGLAPDQVDEVFMGCVLP
AGVGQAPARQASLGAGLPRSAGCTTISKVCGSGMKAAMLAHDLLVAGTAKVMVAGGMESM
SNAPYLLDKARGGYRLGHGKVLDHMFLDGLEDAYDRGRLMGTFAEECAGSYKFTREAQDG
FALASLSRAKKAIADGLFAAEITPVAVAGRKGETLITIDEQPGKALPDKIPTLKPAFAKD
GTVTAANSSSISDGAAALVMMRRSEAEKRGLKPLATVLGHTNFAQEPALFTTAPVGAIKT
LLDKVGCKAGDIDLWEINEAFAVVTMAAMHDLKLEHERVNVHGGACALGHPIGASGARII
VTLLSALKTYGMKRGVASLCIGGGEATALMVELT
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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