SitesBLAST
Comparing GFF1184 FitnessBrowser__Phaeo:GFF1184 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)
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, 95% coverage: 26:540/542 of query aligns to 24:535/541 of Q5SKN9
- T184 (= T192) binding
- G302 (≠ A308) binding
- Q322 (= Q327) binding
- G323 (≠ V328) binding
- T327 (= T332) binding
- E328 (= E333) binding
- D418 (= D424) binding
- K435 (= K441) binding
- K439 (≠ I445) binding
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
34% identity, 95% coverage: 26:540/542 of query aligns to 17:504/510 of 1v26B
- active site: T177 (= T192), H197 (≠ M212), H223 (= H236), T320 (= T332), E321 (= E333), K432 (≠ I445), W437 (≠ N450)
- binding adenosine monophosphate: G295 (≠ A308), S296 (≠ P309), A297 (≠ P310), Q315 (= Q327), G316 (≠ V328), Y317 (= Y329), G318 (= G330), L319 (= L331), T320 (= T332), D411 (= D424), I423 (= I436), K428 (= K441), K432 (≠ I445), W437 (≠ N450)
- binding magnesium ion: T177 (= T192), E321 (= E333)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 85% coverage: 26:487/542 of query aligns to 17:464/491 of 1v25A
- active site: T177 (= T192), H197 (≠ M212), H223 (= H236), T320 (= T332), E321 (= E333), K432 (≠ I445), W437 (≠ N450)
- binding phosphoaminophosphonic acid-adenylate ester: F222 (= F235), H223 (= H236), V224 (≠ C237), W227 (= W240), G295 (≠ A308), S296 (≠ P309), A297 (≠ P310), Q315 (= Q327), G316 (≠ V328), Y317 (= Y329), G318 (= G330), L319 (= L331), T320 (= T332), D411 (= D424), I423 (= I436), R426 (= R439), K428 (= K441), K432 (≠ I445), W437 (≠ N450)
- binding magnesium ion: T177 (= T192), E321 (= E333)
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)
32% identity, 92% coverage: 45:541/542 of query aligns to 29:499/503 of P9WQ37
- K172 (= K200) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (≠ K227) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (vs. gap) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C237) 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 (≠ G239) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ H242) 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 (≠ G272) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G330) 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 (≠ Y419) 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 (= D424) 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 (= R439) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S446) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G448) 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.
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
29% identity, 92% coverage: 45:540/542 of query aligns to 39:534/538 of 6ijbB
- active site: T185 (= T192), H205 (≠ M212), H231 (= H236), S329 (≠ T332), E330 (= E333), K438 (≠ I445), W443 (≠ N450), A523 (≠ K529)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W240), G303 (= G307), A325 (≠ V328), W326 (≠ Y329), G327 (= G330), M328 (≠ L331), P333 (vs. gap), L334 (≠ Y335)
- binding adenosine monophosphate: T185 (= T192), H231 (= H236), G302 (≠ A306), G303 (= G307), A304 (= A308), A305 (≠ P309), H324 (≠ Q327), A325 (≠ V328), W326 (≠ Y329), G327 (= G330), M328 (≠ L331), S329 (≠ T332), Q359 (= Q363), D417 (= D424), I429 (= I436), R432 (= R439)
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
32% identity, 92% coverage: 45:541/542 of query aligns to 32:499/502 of 3r44A
Sites not aligning to the query:
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
29% identity, 92% coverage: 45:540/542 of query aligns to 39:531/533 of 6ihkB
- active site: T185 (= T192), H202 (≠ M212), H228 (= H236), S326 (≠ T332), E327 (= E333), K435 (≠ I445), W440 (≠ N450), K520 (= K529)
- binding adenosine-5'-diphosphate: T185 (= T192), H228 (= H236), G299 (≠ A306), G300 (= G307), A301 (= A308), A302 (≠ P309), H321 (≠ Q327), A322 (≠ V328), W323 (≠ Y329), G324 (= G330), M325 (≠ L331), S326 (≠ T332), Q356 (= Q363), D414 (= D424), I426 (= I436), R429 (= R439), K520 (= K529)
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, 95% coverage: 26:540/542 of query aligns to 8:481/485 of 5x8fB
- active site: T151 (= T192), S171 (≠ M212), H195 (= H236), T288 (= T332), E289 (= E333), I387 (= I445), N392 (= N450), K470 (= K529)
- binding magnesium ion: Y23 (= Y41), E24 (≠ G42), H70 (≠ P91), N178 (≠ S219), L202 (≠ T243), L214 (≠ C255), F282 (≠ T326), T296 (≠ C341), L297 (= L342), S298 (≠ W343)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R103), L191 (≠ V232), P192 (= P233), H195 (= H236), I196 (≠ C237), S197 (≠ N238), F218 (≠ I259), S236 (≠ G277), A237 (≠ G278), V238 (= V282), M241 (= M285), L260 (≠ F304), G262 (≠ A306), G263 (= G307), G286 (= G330), M287 (≠ L331), S292 (≠ G336), Q293 (≠ H337), S388 (= S446), G389 (= G447), G390 (= G448), E391 (= E449), K420 (= K478), W421 (= W479), K450 (≠ G510), Y451 (≠ F511)
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
28% identity, 95% coverage: 26:540/542 of query aligns to 8:481/484 of 5gtdA