SitesBLAST
Comparing WP_097030475.1 NCBI__GCF_900207575.1:WP_097030475.1 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)
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: 26:535/553 of query aligns to 24:531/541 of Q5SKN9
- T184 (= T192) binding Mg(2+)
- G302 (= G307) binding tetradecanoyl-AMP
- Q322 (= Q327) binding tetradecanoyl-AMP
- G323 (≠ V328) binding tetradecanoyl-AMP
- T327 (= T332) binding tetradecanoyl-AMP
- E328 (= E333) binding Mg(2+)
- D418 (= D423) binding tetradecanoyl-AMP
- K435 (= K440) binding tetradecanoyl-AMP
- K439 (≠ I444) binding tetradecanoyl-AMP
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)
32% identity, 90% coverage: 44:543/553 of query aligns to 38:538/539 of P0DX84
- H231 (= H236) mutation to A: Retains 74% of wild-type activity.
- W235 (= W240) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A306) mutation to P: Almost completely abolishes the activity.
- G303 (= G307) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y329) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ G336) mutation to A: Retains 69% of wild-type activity.
- R432 (= R438) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K440) mutation to A: Retains 36% of wild-type activity.
- D435 (= D441) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I444) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G446) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G447) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E448) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N449) mutation to A: Retains 60% of wild-type activity.
- E474 (= E480) mutation to A: Retains 33% of wild-type activity.
- K523 (= K528) 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 (= K531) 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)
32% identity, 90% coverage: 44:543/553 of query aligns to 38:538/538 of 6ijbB
- active site: T185 (= T192), H205 (≠ A212), H231 (= H236), S329 (≠ T332), E330 (= E333), K438 (≠ I444), W443 (≠ N449), A523 (≠ K528)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W240), G303 (= G307), A325 (≠ V328), W326 (≠ Y329), G327 (= G330), M328 (≠ L331)
- binding adenosine monophosphate: G303 (= G307), A304 (= A308), A305 (≠ P309), H324 (≠ Q327), W326 (≠ Y329), G327 (= G330), M328 (≠ L331), S329 (≠ T332), Q359 (≠ T362), D417 (= D423)
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2
33% identity, 89% coverage: 45:537/553 of query aligns to 35:520/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T192), G174 (= G194), T175 (= T195), T176 (= T196), K180 (= K200), G293 (≠ A306), A294 (≠ G307), A295 (= A308), Y315 (= Y329), M317 (≠ L331), S318 (≠ T332), D408 (= D423), R423 (= R438)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
34% identity, 88% coverage: 26:510/553 of query aligns to 17:487/491 of 1v25A
- active site: T177 (= T192), H197 (≠ A212), H223 (= H236), T320 (= T332), E321 (= E333), K432 (≠ I444), W437 (≠ N449)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H236), V224 (≠ C237), G295 (= G307), S296 (≠ A308), A297 (≠ P309), Y317 (= Y329), G318 (= G330), L319 (= L331), T320 (= T332), D411 (= D423), I423 (= I435), K432 (≠ I444), W437 (≠ N449)
- binding magnesium ion: T177 (= T192), E321 (= E333)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
35% identity, 83% coverage: 26:484/553 of query aligns to 17:463/510 of 1v26B
- active site: T177 (= T192), H197 (≠ A212), H223 (= H236), T320 (= T332), E321 (= E333), K432 (≠ I444), W437 (≠ N449)
- binding adenosine monophosphate: G295 (= G307), S296 (≠ A308), A297 (≠ P309), G316 (≠ V328), Y317 (= Y329), G318 (= G330), L319 (= L331), T320 (= T332), D411 (= D423), K428 (= K440), K432 (≠ I444), W437 (≠ N449)
- binding magnesium ion: T177 (= T192), E321 (= E333)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
32% identity, 89% coverage: 45:537/553 of query aligns to 33:526/528 of 8i6mA
- binding adenosine monophosphate: G291 (≠ A306), A293 (= A308), G312 (≠ V328), Y313 (= Y329), G314 (= G330), M315 (≠ L331), S316 (≠ T332), D406 (= D423), R421 (= R438)
- binding magnesium ion: M315 (≠ L331), S316 (≠ T332), E317 (= E333)
8i51A Acyl-acp synthetase structure bound to amp-mc7
32% identity, 89% coverage: 45:537/553 of query aligns to 33:526/528 of 8i51A
- binding adenosine monophosphate: G291 (≠ A306), A293 (= A308), Y313 (= Y329), M315 (≠ L331), S316 (≠ T332), D406 (= D423), R421 (= R438)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W240), G290 (≠ T305), G312 (≠ V328), G314 (= G330), M315 (≠ L331), P320 (= P337), I321 (≠ A338)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
32% identity, 89% coverage: 45:537/553 of query aligns to 35:528/529 of 8i8dA