SitesBLAST
Comparing WP_058929767.1 NCBI__GCF_001484605.1:WP_058929767.1 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)
6pccA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex hexanoyl coenzyme a (see paper)
47% identity, 100% coverage: 1:389/389 of query aligns to 4:402/403 of 6pccA
- active site: C93 (= C90), A359 (≠ H346), C389 (= C376), G391 (= G378)
- binding coenzyme a: C93 (= C90), I148 (≠ L146), R229 (= R220), T232 (= T223), A252 (= A243), S256 (= S247), N325 (= N313), F328 (= F316)
- binding hexanal: N61 (= N58), T146 (≠ S144), I148 (≠ L146), G149 (= G147), R151 (= R149), L361 (= L348)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
47% identity, 100% coverage: 1:389/389 of query aligns to 4:402/403 of 6pcbA
- active site: C93 (= C90), A359 (≠ H346), C389 (= C376), G391 (= G378)
- binding coenzyme a: C93 (= C90), I148 (≠ L146), R229 (= R220), A252 (= A243), S256 (= S247), G257 (≠ P248), N325 (= N313), F328 (= F316)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
47% identity, 100% coverage: 1:389/389 of query aligns to 5:400/401 of 6pcdA
- active site: S94 (≠ C90), A357 (≠ H346), C387 (= C376), G389 (= G378)
- binding coenzyme a: I149 (≠ L146), M167 (≠ N163), R227 (= R220), T230 (= T223), A250 (= A243), S254 (= S247), G255 (≠ P248), A325 (= A315), A357 (≠ H346)
- binding octanal: N62 (= N58), T147 (≠ S144), T148 (= T145), I149 (≠ L146), G150 (= G147), R152 (= R149), L359 (= L348)
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, 100% coverage: 1:389/389 of query aligns to 1:391/392 of P45359
- V77 (≠ T79) 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 (≠ I98) binding acetate
- N153 (= N163) 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 (≠ GV 276:277) binding acetate
- A286 (≠ D283) 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 (= C376) modified: Disulfide link with 88, In inhibited form
- A386 (= A384) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
40% identity, 100% coverage: 1:389/389 of query aligns to 1:391/392 of 4xl4A
- active site: C88 (= C90), H348 (= H346), S378 (≠ C376), G380 (= G378)
- binding coenzyme a: L148 (≠ A158), H156 (vs. gap), R220 (= R220), L231 (= L231), A243 (= A243), S247 (= S247), F319 (= F316), H348 (= H346)
2d3tC Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form v (see paper)
42% identity, 99% coverage: 6:389/389 of query aligns to 9:389/390 of 2d3tC
- active site: C94 (= C90), H346 (= H346), C376 (= C376), G378 (= G378)
- binding acetyl coenzyme *a: C94 (= C90), R214 (= R220), L222 (= L228), L225 (= L231), A238 (= A243), G239 (= G244), S242 (= S247), I244 (≠ L249), A313 (= A315), F314 (= F316), H346 (= H346), C376 (= C376)
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
41% identity, 99% coverage: 4:389/389 of query aligns to 3:397/400 of 5bz4K
- active site: C87 (= C90), H354 (= H346), C384 (= C376), G386 (= G378)
- binding coenzyme a: C87 (= C90), R146 (≠ W159), M160 (vs. gap), R220 (= R220), A246 (= A243), G247 (= G244), S250 (= S247), Q252 (≠ L249), M291 (≠ F285), A321 (= A315), F322 (= F316), H354 (= H346)
4c2jD Crystal structure of human mitochondrial 3-ketoacyl-coa thiolase in complex with coa (see paper)
40% identity, 99% coverage: 5:388/389 of query aligns to 11:393/395 of 4c2jD
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)
42% identity, 100% coverage: 1:389/389 of query aligns to 1:392/393 of P14611
- C88 (= C90) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (vs. gap) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ G218) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R220) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S247) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H346) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C376) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
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)
39% identity, 99% coverage: 5:388/389 of query aligns to 8:394/397 of P42765
- C92 (= C90) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R220) binding CoA
- T227 (= T223) binding CoA
- S251 (= S247) binding CoA
- C382 (= C376) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
41% identity, 100% coverage: 1:389/389 of query aligns to 1:392/393 of 4o9cC
- active site: S88 (≠ C90), H349 (= H346), C379 (= C376), G381 (= G378)
- binding coenzyme a: S88 (≠ C90), L148 (≠ A158), R221 (= R220), F236 (= F235), A244 (= A243), S248 (= S247), L250 (= L249), A319 (= A315), F320 (= F316), H349 (= H346)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
41% identity, 100% coverage: 1:389/389 of query aligns to 1:390/391 of 5f38B
- active site: C88 (= C90), H347 (= H346), C377 (= C376), G379 (= G378)
- binding coenzyme a: C88 (= C90), L149 (= L141), K219 (≠ R220), F234 (= F235), A242 (= A243), S246 (= S247), A317 (= A315), F318 (= F316), H347 (= H346)
8gqmA Crystal structure of thiolase complexed with acetyl coenzyme a
41% identity, 97% coverage: 11:388/389 of query aligns to 10:373/377 of 8gqmA
- binding acetyl coenzyme *a: K18 (vs. gap), S89 (≠ C90), M124 (≠ W125), M146 (≠ N163), R205 (= R220), T208 (= T223), L213 (= L228), L216 (= L231), A226 (= A243), A227 (≠ G244), S229 (= S246), S230 (= S247), M271 (≠ F285), A301 (= A315), H331 (= H346), L333 (= L348)
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
41% identity, 100% coverage: 1:389/389 of query aligns to 3:394/394 of 5f38D
- active site: C90 (= C90), A348 (= A343), A378 (= A373), L380 (≠ I375)
- 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 (= L141), A246 (= A243), S250 (= S247), I252 (≠ L249), A321 (= A315), F322 (= F316), H351 (= H346)
8jg2A Crystal structure of a biosynthetic thiolase from megasphaera hexanoica soaked with hexanoyl-coa
39% identity, 100% coverage: 1:388/389 of query aligns to 2:390/393 of 8jg2A
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)
42% identity, 99% coverage: 6:389/389 of query aligns to 10:396/397 of Q9BWD1
- K211 (vs. gap) to R: in dbSNP:rs25683
- R223 (= R220) binding CoA
- S226 (≠ T223) binding CoA
- S252 (= S247) binding CoA
1wl4A Human cytosolic acetoacetyl-coa thiolase complexed with coa (see paper)
42% identity, 99% coverage: 6:389/389 of query aligns to 7:393/394 of 1wl4A
- active site: C89 (= C90), H350 (= H346), C380 (= C376), G382 (= G378)
- binding coenzyme a: L148 (≠ M150), M157 (≠ N163), R220 (= R220), Y234 (≠ A234), P245 (≠ A243), A246 (≠ G244), S249 (= S247), A320 (= A315), F321 (= F316), H350 (= H346)
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: 4:388/389 of query aligns to 5:390/392 of P07097
- Q64 (≠ R65) mutation to A: Slightly lower activity.
- C89 (= C90) mutation to A: Loss of activity.
- C378 (= C376) mutation to G: Loss of activity.
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
41% identity, 99% coverage: 3:388/389 of query aligns to 1:387/389 of 2vu2A
- active site: C86 (= C90), H345 (= H346), C375 (= C376), G377 (= G378)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ S162), M154 (≠ N163), F232 (= F235), S244 (= S247), G245 (≠ P248), F316 (= F316), H345 (= H346)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
41% identity, 99% coverage: 3:388/389 of query aligns to 1:387/389 of 1dm3A
- active site: C86 (= C90), H345 (= H346), C375 (= C376), G377 (= G378)
- binding acetyl coenzyme *a: C86 (= C90), L145 (≠ M155), H153 (≠ S162), M154 (≠ N163), R217 (= R220), S224 (≠ A227), M225 (≠ L228), A240 (= A243), S244 (= S247), M285 (≠ F285), A315 (= A315), F316 (= F316), H345 (= H346), C375 (= C376)
Query Sequence
>WP_058929767.1 NCBI__GCF_001484605.1:WP_058929767.1
MASSFIYDGIRTPFGKFGKSMAGIRPDDLASHVIREVVDRQPGLETQRIDDVILGNTNGA
GEDNRNVARMAALLAGLPTSVPGVTVNRLCGSGLEAAIQASRAVEIGDADLVVAGGVESM
SRAPWILAKPERAYPAGPETLHSSTLGWRMVNPKMNQAWTISNGETAENLADKFDISRVE
QDQFAVRSHRLAAKAWSEGIYDDEVVPHPDSQLLTDEGVRPTTSGEALAGLAPAFRDGGS
VTAGNSSPLNDGAAAMLIGREGALETEPLARIVSRGVAGNDPDIFGIAPVEAANQALARA
GKTWADVDVVELNEAFAAQSLACLRLWPDLDPEKVNIHGGALAVGHPLGASGSRVLIHLA
RELKRRGGGVGVAAICIGVGQGLAVVLER
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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