SitesBLAST
Comparing WP_054256932.1 NCBI__GCF_001298675.1:WP_054256932.1 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)
P0DX84 3-methylmercaptopropionyl-CoA ligase; MMPA-CoA ligase; EC 6.2.1.44 from Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis) (see paper)
55% identity, 99% coverage: 1:538/545 of query aligns to 1:534/539 of P0DX84
- H231 (= H232) mutation to A: Retains 74% of wild-type activity.
- W235 (= W236) mutation to A: Almost completely abolishes the activity.
- G302 (= G303) mutation to P: Almost completely abolishes the activity.
- G303 (= G304) mutation to P: Almost completely abolishes the activity.
- W326 (= W327) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P334) mutation to A: Retains 69% of wild-type activity.
- R432 (= R436) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K438) mutation to A: Retains 36% of wild-type activity.
- D435 (= D439) mutation to A: Retains 76% of wild-type activity.
- K438 (= K442) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G444) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G445) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E446) mutation to A: Retains 27% of wild-type activity.
- W443 (= W447) mutation to A: Retains 60% of wild-type activity.
- E474 (= E478) mutation to A: Retains 33% of wild-type activity.
- K523 (= K527) Plays an important role in catalysis; mutation to A: Retains 1.6% of wild-type activity.; mutation to E: Retains 1.4% of wild-type activity.; mutation to R: Retains 57% of wild-type activity.
- K526 (= K530) mutation to A: Retains 48% of wild-type activity.
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
55% identity, 99% coverage: 1:538/545 of query aligns to 1:534/538 of 6ijbB
- active site: T185 (= T186), H205 (= H206), H231 (= H232), S329 (≠ T330), E330 (= E331), K438 (= K442), W443 (= W447), A523 (≠ K527)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W236), G303 (= G304), A325 (= A326), W326 (= W327), G327 (= G328), M328 (= M329)
- binding adenosine monophosphate: G303 (= G304), A304 (≠ S305), A305 (= A306), H324 (= H325), W326 (= W327), G327 (= G328), M328 (= M329), S329 (≠ T330), Q359 (= Q360), D417 (= D421)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
54% identity, 99% coverage: 1:538/545 of query aligns to 1:531/533 of 6ihkB
- active site: T185 (= T186), H202 (= H206), H228 (= H232), S326 (≠ T330), E327 (= E331), K435 (= K442), W440 (= W447), K520 (= K527)
- binding adenosine-5'-diphosphate: H228 (= H232), G300 (= G304), A301 (≠ S305), A302 (= A306), H321 (= H325), A322 (= A326), W323 (= W327), G324 (= G328), M325 (= M329), S326 (≠ T330), Q356 (= Q360), D414 (= D421), R429 (= R436), K520 (= K527)
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)
46% identity, 98% coverage: 5:540/545 of query aligns to 13:537/541 of Q5SKN9
- T184 (= T186) binding Mg(2+)
- G302 (= G304) binding tetradecanoyl-AMP
- Q322 (≠ H325) binding tetradecanoyl-AMP
- G323 (≠ A326) binding tetradecanoyl-AMP
- T327 (= T330) binding tetradecanoyl-AMP
- E328 (= E331) binding Mg(2+)
- D418 (= D421) binding tetradecanoyl-AMP
- K435 (= K438) binding tetradecanoyl-AMP
- K439 (= K442) binding tetradecanoyl-AMP
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
44% identity, 98% coverage: 5:540/545 of query aligns to 6:506/510 of 1v26B
- active site: T177 (= T186), H197 (= H206), H223 (= H232), T320 (= T330), E321 (= E331), K432 (= K442), W437 (= W447)
- binding adenosine monophosphate: G295 (= G304), S296 (= S305), A297 (= A306), G316 (≠ A326), Y317 (≠ W327), G318 (= G328), L319 (≠ M329), T320 (= T330), D411 (= D421), K428 (= K438), K432 (= K442), W437 (= W447)
- binding magnesium ion: T177 (= T186), E321 (= E331)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
43% identity, 98% coverage: 5:540/545 of query aligns to 6:487/491 of 1v25A
- active site: T177 (= T186), H197 (= H206), H223 (= H232), T320 (= T330), E321 (= E331), K432 (= K442), W437 (= W447)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H232), V224 (= V233), G295 (= G304), S296 (= S305), A297 (= A306), Y317 (≠ W327), G318 (= G328), L319 (≠ M329), T320 (= T330), D411 (= D421), I423 (= I433), K432 (= K442), W437 (= W447)
- binding magnesium ion: T177 (= T186), E321 (= E331)
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2
37% identity, 97% coverage: 10:535/545 of query aligns to 10:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T186), G174 (= G188), T175 (= T189), T176 (= T190), K180 (= K194), G293 (= G304), A294 (≠ S305), A295 (= A306), Y315 (≠ W327), M317 (= M329), S318 (≠ T330), D408 (= D421), R423 (= R436)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
37% identity, 97% coverage: 10:535/545 of query aligns to 8:525/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G304), A293 (= A306), G312 (≠ A326), Y313 (≠ W327), G314 (= G328), M315 (= M329), S316 (≠ T330), D406 (= D421), R421 (= R436)
- binding magnesium ion: M315 (= M329), S316 (≠ T330), E317 (= E331)
8i51A Acyl-acp synthetase structure bound to amp-mc7
37% identity, 97% coverage: 10:535/545 of query aligns to 8:525/528 of 8i51A