SitesBLAST
Comparing WP_015929439.1 NCBI__GCF_000022085.1:WP_015929439.1 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)
71% identity, 100% coverage: 2:403/404 of query aligns to 2:403/403 of 6pccA
- active site: C93 (= C92), A359 (≠ H359), C389 (= C389), G391 (= G391)
- binding coenzyme a: C93 (= C92), I148 (= I147), R229 (= R229), T232 (= T232), A252 (= A252), S256 (= S256), N325 (= N325), F328 (= F328)
- binding hexanal: N61 (= N60), T146 (= T145), I148 (= I147), G149 (= G148), R151 (= R150), L361 (= L361)
6pcbA Crystal structure of beta-ketoadipyl-coa thiolase mutant (h356a) in complex with coa (see paper)
71% identity, 100% coverage: 2:403/404 of query aligns to 2:403/403 of 6pcbA
- active site: C93 (= C92), A359 (≠ H359), C389 (= C389), G391 (= G391)
- binding coenzyme a: C93 (= C92), I148 (= I147), R229 (= R229), A252 (= A252), S256 (= S256), G257 (= G257), N325 (= N325), F328 (= F328)
6pcdA Crystal structure of beta-ketoadipyl-coa thiolase mutant (c90s-h356a) in complex octanoyl coenzyme a (see paper)
70% identity, 100% coverage: 2:403/404 of query aligns to 3:401/401 of 6pcdA
- active site: S94 (≠ C92), A357 (≠ H359), C387 (= C389), G389 (= G391)
- binding coenzyme a: I149 (= I147), M167 (= M165), R227 (= R229), T230 (= T232), A250 (= A252), S254 (= S256), G255 (= G257), A325 (= A327), A357 (≠ H359)
- binding octanal: N62 (= N60), T147 (= T145), T148 (= T146), I149 (= I147), G150 (= G148), R152 (= R150), L359 (= L361)
5bz4K Crystal structure of a t1-like thiolase (coa-complex) from mycobacterium smegmatis (see paper)
45% identity, 99% coverage: 5:403/404 of query aligns to 1:398/400 of 5bz4K
- active site: C87 (= C92), H354 (= H359), C384 (= C389), G386 (= G391)
- binding coenzyme a: C87 (= C92), R146 (vs. gap), M160 (= M165), R220 (= R229), A246 (= A252), G247 (= G253), S250 (= S256), Q252 (≠ V258), M291 (= M297), A321 (= A327), F322 (= F328), H354 (= H359)
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)
44% identity, 99% coverage: 5:402/404 of query aligns to 2:391/392 of P45359
- V77 (≠ E81) 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 (= C92) modified: Disulfide link with 378, In inhibited form
- S96 (≠ G100) binding acetate
- N153 (≠ L156) 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 (≠ AS 288:289) binding acetate
- A286 (≠ R295) 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 (= C389) modified: Disulfide link with 88, In inhibited form
- A386 (= A397) binding acetate
4xl4A Crystal structure of thiolase from clostridium acetobutylicum in complex with coa (see paper)
44% identity, 99% coverage: 5:402/404 of query aligns to 2:391/392 of 4xl4A
- active site: C88 (= C92), H348 (= H359), S378 (≠ C389), G380 (= G391)
- binding coenzyme a: L148 (≠ F151), H156 (≠ Q159), R220 (= R229), L231 (= L240), A243 (= A252), S247 (= S256), F319 (= F328), H348 (= H359)
8jg2A Crystal structure of a biosynthetic thiolase from megasphaera hexanoica soaked with hexanoyl-coa
43% identity, 98% coverage: 5:401/404 of query aligns to 3:390/393 of 8jg2A
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)
46% identity, 98% coverage: 6:402/404 of query aligns to 3:392/393 of P14611
- C88 (= C92) active site, Acyl-thioester intermediate; mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
- H156 (≠ S164) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- F219 (≠ H227) mutation to A: About 50% loss of acetoacetyl-CoA thiolase activity.; mutation to Y: 2-fold increase of acetoacetyl-CoA thiolase activity.
- R221 (= R229) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- S248 (= S256) mutation to A: About 40% loss of acetoacetyl-CoA thiolase activity.
- H349 (= H359) mutation to A: Almost complete loss of acetoacetyl-CoA thiolase activity.
- C379 (= C389) mutation to S: Almost complete loss of acetoacetyl-CoA thiolase activity.
2vu1A Biosynthetic thiolase from z. Ramigera. Complex of with o-pantheteine- 11-pivalate. (see paper)
43% identity, 99% coverage: 4:403/404 of query aligns to 1:391/391 of 2vu1A
1ou6A Biosynthetic thiolase from zoogloea ramigera in complex with acetyl-o- pantetheine-11-pivalate
43% identity, 99% coverage: 4:403/404 of query aligns to 2:392/392 of 1ou6A
- active site: C89 (= C92), H348 (= H359), C378 (= C389), G380 (= G391)
- binding pantothenyl-aminoethanol-acetate pivalic acid: L148 (≠ F151), H156 (≠ Q159), M157 (≠ Y160), F235 (≠ V244), A243 (= A252), S247 (= S256), A318 (= A327), F319 (= F328), H348 (= H359)
4o9cC Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha h16 (see paper)
45% identity, 98% coverage: 6:402/404 of query aligns to 3:392/393 of 4o9cC
- active site: S88 (≠ C92), H349 (= H359), C379 (= C389), G381 (= G391)
- binding coenzyme a: S88 (≠ C92), L148 (vs. gap), R221 (= R229), F236 (≠ V244), A244 (= A252), S248 (= S256), L250 (≠ V258), A319 (= A327), F320 (= F328), H349 (= H359)
2vu2A Biosynthetic thiolase from z. Ramigera. Complex with s-pantetheine-11- pivalate. (see paper)
43% identity, 98% coverage: 7:403/404 of query aligns to 2:389/389 of 2vu2A
- active site: C86 (= C92), H345 (= H359), C375 (= C389), G377 (= G391)
- binding (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate: H153 (≠ Q159), M154 (≠ Y160), F232 (≠ V244), S244 (= S256), G245 (= G257), F316 (= F328), H345 (= H359)
1dm3A Acetylated biosynthetic thiolase from zoogloea ramigera in complex with acetyl-coa (see paper)
43% identity, 98% coverage: 7:403/404 of query aligns to 2:389/389 of 1dm3A
- active site: C86 (= C92), H345 (= H359), C375 (= C389), G377 (= G391)
- binding acetyl coenzyme *a: C86 (= C92), L145 (≠ F151), H153 (≠ Q159), M154 (≠ Y160), R217 (= R229), S224 (≠ G236), M225 (≠ L237), A240 (= A252), S244 (= S256), M285 (= M297), A315 (= A327), F316 (= F328), H345 (= H359), C375 (= C389)
1dlvA Biosynthetic thiolase from zoogloea ramigera in complex with coa (see paper)
43% identity, 98% coverage: 7:403/404 of query aligns to 2:389/389 of 1dlvA
- active site: C86 (= C92), H345 (= H359), C375 (= C389), G377 (= G391)
- binding coenzyme a: C86 (= C92), L145 (≠ F151), H153 (≠ Q159), M154 (≠ Y160), R217 (= R229), L228 (= L240), A240 (= A252), S244 (= S256), H345 (= H359)
P07097 Acetyl-CoA acetyltransferase; Acetoacetyl-CoA thiolase; Beta-ketothiolase; EC 2.3.1.9 from Shinella zoogloeoides (Crabtreella saccharophila) (see 2 papers)
44% identity, 97% coverage: 14:403/404 of query aligns to 12:392/392 of P07097
- Q64 (≠ R67) mutation to A: Slightly lower activity.
- C89 (= C92) mutation to A: Loss of activity.
- C378 (= C389) mutation to G: Loss of activity.
5f38D X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
44% identity, 99% coverage: 5:402/404 of query aligns to 4:394/394 of 5f38D
- active site: C90 (= C92), A348 (= A356), A378 (= A386), L380 (= L388)
- binding [(3~{S})-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-4-[[3-oxidanylidene-3-(2-sulfanylethylamino)propyl]amino]butyl] phosphono hydrogen phosphate: C90 (= C92), L151 (≠ F151), A246 (= A252), S250 (= S256), I252 (≠ V258), A321 (= A327), F322 (= F328), H351 (= H359)
2wkuA Biosynthetic thiolase from z. Ramigera. The n316h mutant. (see paper)
43% identity, 98% coverage: 7:403/404 of query aligns to 2:389/389 of 2wkuA
- active site: C86 (= C92), H345 (= H359), C375 (= C389), G377 (= G391)
- binding D-mannose: S6 (≠ D11), A7 (≠ F12), R38 (= R43), K182 (≠ R193), D194 (≠ Q205), V280 (= V292), D281 (≠ P293), T287 (≠ I299), P331 (≠ A345), S332 (≠ E346), V334 (= V348), V336 (≠ P350), F360 (≠ R374)
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: 1:401/404 of query aligns to 1:394/397 of P42765
- C92 (= C92) mutation to A: Decreased acyl-CoA hydrolase activity.; mutation to S: Decreased acyl-CoA hydrolase activity; when associated with A-382.
- R224 (= R229) binding CoA
- T227 (= T232) binding CoA
- S251 (= S256) binding CoA
- C382 (= C389) mutation to S: Decreased acyl-CoA hydrolase activity; when associated with S-92.
1m1oA Crystal structure of biosynthetic thiolase, c89a mutant, complexed with acetoacetyl-coa (see paper)
43% identity, 98% coverage: 7:403/404 of query aligns to 3:390/390 of 1m1oA
- active site: A87 (≠ C92), H346 (= H359), C376 (= C389), G378 (= G391)
- binding acetoacetyl-coenzyme a: L86 (= L91), A87 (≠ C92), L146 (≠ F151), H154 (≠ Q159), M155 (≠ Y160), R218 (= R229), S225 (≠ G236), M226 (≠ L237), A241 (= A252), G242 (= G253), S245 (= S256), A316 (= A327), F317 (= F328), H346 (= H359), I377 (≠ V390), G378 (= G391)
5f38B X-ray crystal structure of a thiolase from escherichia coli at 1.8 a resolution (see paper)
44% identity, 99% coverage: 5:403/404 of query aligns to 2:391/391 of 5f38B
- active site: C88 (= C92), H347 (= H359), C377 (= C389), G379 (= G391)
- binding coenzyme a: C88 (= C92), L149 (≠ F151), K219 (≠ R229), F234 (≠ V244), A242 (= A252), S246 (= S256), A317 (= A327), F318 (= F328), H347 (= H359)
Query Sequence
>WP_015929439.1 NCBI__GCF_000022085.1:WP_015929439.1
MGETRDVYICDFVRTPIGRYGGALASVRADDLAAIPLAALLHRNPSLKDGVEEVFLGCAN
QAGEDNRNVARMALLLAGLPETVPGLTLNRLCASGLDAVGAAARAIRSGDIDLALAGGVE
SMTRAPFVMGKSEGAWQRQAEIHDTTIGWRFINPMLKHQYGVDSMPETAENVAEDFQISR
ADQDAFALRSQERAARAQADGILAQEITAVAIPTRQGDHRRVDRDEHPRPETTAEGLAKL
KPFVRRDGTVTAGNASGVNDGAAALVLASAEAAARHGLTPLTRVLGLASAGVPPRVMGIG
PVPAVTALCARLGLKPSDFDVIELNEAFASQSLACLRGLGLPDDAEHVNPHGGAIAFGHP
LGMSGARIAGAATRELVRRGGRLGLATLCVGVGQGVALAVERVG
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