SitesBLAST
Comparing RR42_RS25360 FitnessBrowser__Cup4G11:RR42_RS25360 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)
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
32% identity, 94% coverage: 19:536/554 of query aligns to 9:530/538 of 6ijbB
- active site: T185 (= T191), H205 (≠ M211), H231 (= H235), S329 (≠ T331), E330 (= E332), K438 (≠ I444), W443 (≠ N449), A523 (≠ K529)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W239), G303 (= G306), A325 (≠ V327), W326 (≠ Y328), G327 (= G329), M328 (≠ I330)
- binding adenosine monophosphate: G303 (= G306), A304 (≠ S307), A305 (≠ P308), H324 (= H326), W326 (≠ Y328), G327 (= G329), M328 (≠ I330), S329 (≠ T331), Q359 (= Q361), D417 (= D423)
Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
35% identity, 92% coverage: 25:536/554 of query aligns to 23:531/541 of Q5SKN9
- T184 (= T191) binding
- G302 (= G306) binding
- Q322 (≠ H326) binding
- G323 (≠ V327) binding
- T327 (= T331) binding
- E328 (= E332) binding
- D418 (= D423) binding
- K435 (= K440) binding
- K439 (≠ I444) binding
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
32% identity, 94% coverage: 19:536/554 of query aligns to 9:527/533 of 6ihkB
- active site: T185 (= T191), H202 (≠ M211), H228 (= H235), S326 (≠ T331), E327 (= E332), K435 (≠ I444), W440 (≠ N449), K520 (= K529)
- binding adenosine-5'-diphosphate: H228 (= H235), G300 (= G306), A301 (≠ S307), A302 (≠ P308), H321 (= H326), A322 (≠ V327), W323 (≠ Y328), G324 (= G329), M325 (≠ I330), S326 (≠ T331), Q356 (= Q361), D414 (= D423), R429 (= R438), K520 (= K529)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 83% coverage: 25:486/554 of query aligns to 16:464/491 of 1v25A
- active site: T177 (= T191), H197 (≠ M211), H223 (= H235), T320 (= T331), E321 (= E332), K432 (≠ I444), W437 (≠ N449)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H235), V224 (≠ A236), G295 (= G306), S296 (= S307), A297 (≠ P308), Y317 (= Y328), G318 (= G329), L319 (≠ I330), T320 (= T331), D411 (= D423), I423 (= I435), K432 (≠ I444), W437 (≠ N449)
- binding magnesium ion: T177 (= T191), E321 (= E332)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 83% coverage: 25:484/554 of query aligns to 16:463/510 of 1v26B
- active site: T177 (= T191), H197 (≠ M211), H223 (= H235), T320 (= T331), E321 (= E332), K432 (≠ I444), W437 (≠ N449)
- binding adenosine monophosphate: G295 (= G306), S296 (= S307), A297 (≠ P308), G316 (≠ V327), Y317 (= Y328), G318 (= G329), L319 (≠ I330), T320 (= T331), D411 (= D423), K428 (= K440), K432 (≠ I444), W437 (≠ N449)
- binding magnesium ion: T177 (= T191), E321 (= E332)
P9WQ37 Long-chain-fatty-acid--CoA ligase FadD13; Fatty acyl-CoA ligase; FACL; FACL13; Fatty acyl-CoA synthetase; ACS; FACS; Very-long-chain fatty-acyl-CoA synthetase; ACSVL; EC 6.2.1.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
29% identity, 89% coverage: 44:536/554 of query aligns to 28:494/503 of P9WQ37
- K172 (= K199) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ P222) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ A224) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ A236) mutation to D: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. Slight increase of susceptibility to proteolysis.
- A211 (≠ G238) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ F241) mutation to W: Shows a marked decrease in the activity with lauric and palmitic acid (C12 and C16 fatty acid) with a simultaneous increase in the activity with caprylic acid (C8 fatty acid).
- R244 (≠ G271) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G329) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.; mutation to W: Does not show activity with small, medium or long acyl chains.
- W377 (= W418) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. No significant change in the total expression level, however the cytoplasmic expression is low. Slight increase of susceptibility to proteolysis.
- D382 (= D423) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced.
- R397 (= R438) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S445) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G447) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K529) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
Sites not aligning to the query:
- 9 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- 17 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
28% identity, 92% coverage: 30:536/554 of query aligns to 12:477/484 of 5gtdA
- active site: T151 (= T191), S171 (≠ M211), H195 (= H235), T288 (= T331), E289 (= E332)
- binding adenosine-5'-monophosphate: G263 (= G306), G264 (≠ S307), Y285 (= Y328), G286 (= G329), M287 (≠ I330), T288 (= T331), D366 (= D423), V378 (≠ I435)
- binding magnesium ion: F314 (≠ E369), S315 (≠ G370)
- binding 2-succinylbenzoate: H195 (= H235), S197 (≠ N237), A237 (= A277), L260 (≠ R303), G262 (≠ A305), G263 (= G306), G286 (= G329), M287 (≠ I330), S292 (≠ G335), Q293 (≠ T336)
5x8fB Ternary complex structure of a double mutant i454ra456k of o- succinylbenzoate coa synthetase (mene) from bacillus subtilis bound with amp and its product analogue osb-ncoa at 1.76 angstrom (see paper)
28% identity, 92% coverage: 30:536/554 of query aligns to 12:477/485 of 5x8fB
- active site: T151 (= T191), S171 (≠ M211), H195 (= H235), T288 (= T331), E289 (= E332), I387 (= I444), N392 (= N449), K470 (= K529)
- binding magnesium ion: Y23 (≠ H41), E24 (≠ G42), H70 (= H88), N178 (≠ D218), L202 (≠ S242), L214 (≠ C254), T296 (≠ S339), L297 (≠ A342), S298 (≠ N343)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R103), L191 (= L231), P192 (= P232), H195 (= H235), I196 (≠ A236), S197 (≠ N237), A237 (= A277), V238 (≠ A278), L260 (≠ R303), G262 (≠ A305), G286 (= G329), M287 (≠ I330), S292 (≠ G335), Q293 (≠ T336), S388 (= S445), G389 (= G446), G390 (= G447), E391 (= E448), K420 (= K477), W421 (= W478), K450 (≠ H510), Y451 (= Y511)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
29% identity, 89% coverage: 44:536/554 of query aligns to 31:494/502 of 3r44A