SitesBLAST
Comparing WP_047216123.1 NCBI__GCF_001931675.1:WP_047216123.1 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)
37% identity, 92% coverage: 23:536/557 of query aligns to 22:533/541 of Q5SKN9
- T184 (= T190) binding Mg(2+)
- G302 (= G305) binding tetradecanoyl-AMP
- Q322 (≠ H325) binding tetradecanoyl-AMP
- G323 (≠ V326) binding tetradecanoyl-AMP
- T327 (= T330) binding tetradecanoyl-AMP
- E328 (= E331) binding Mg(2+)
- D418 (= D422) binding tetradecanoyl-AMP
- K435 (= K439) binding tetradecanoyl-AMP
- K439 (≠ I443) binding tetradecanoyl-AMP
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
36% identity, 90% coverage: 23:523/557 of query aligns to 15:496/510 of 1v26B
- active site: T177 (= T190), H197 (≠ N210), H223 (= H234), T320 (= T330), E321 (= E331), K432 (≠ I443), W437 (≠ N448)
- binding adenosine monophosphate: G295 (= G305), S296 (≠ A306), A297 (= A307), G316 (≠ V326), Y317 (= Y327), G318 (= G328), L319 (= L329), T320 (= T330), D411 (= D422), K428 (= K439), K432 (≠ I443), W437 (≠ N448)
- binding magnesium ion: T177 (= T190), E321 (= E331)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
37% identity, 83% coverage: 23:485/557 of query aligns to 15:464/491 of 1v25A
- active site: T177 (= T190), H197 (≠ N210), H223 (= H234), T320 (= T330), E321 (= E331), K432 (≠ I443), W437 (≠ N448)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H234), V224 (≠ C235), G295 (= G305), S296 (≠ A306), A297 (= A307), Y317 (= Y327), G318 (= G328), L319 (= L329), T320 (= T330), D411 (= D422), I423 (= I434), K432 (≠ I443), W437 (≠ N448)
- binding magnesium ion: T177 (= T190), E321 (= E331)
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)
33% identity, 93% coverage: 18:534/557 of query aligns to 9:530/539 of P0DX84
- H231 (= H234) mutation to A: Retains 74% of wild-type activity.
- W235 (= W238) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A304) mutation to P: Almost completely abolishes the activity.
- G303 (= G305) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y327) mutation to A: Retains 7.7% of wild-type activity.
- P333 (vs. gap) mutation to A: Retains 69% of wild-type activity.
- R432 (= R437) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K439) mutation to A: Retains 36% of wild-type activity.
- D435 (= D440) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I443) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G445) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G446) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E447) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N448) mutation to A: Retains 60% of wild-type activity.
- E474 (= E479) 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)
32% identity, 93% coverage: 18:534/557 of query aligns to 9:530/538 of 6ijbB
- active site: T185 (= T190), H205 (≠ N210), H231 (= H234), S329 (≠ T330), E330 (= E331), K438 (≠ I443), W443 (≠ N448), A523 (≠ K527)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W238), G303 (= G305), A325 (≠ V326), W326 (≠ Y327), G327 (= G328), M328 (≠ L329)
- binding adenosine monophosphate: G303 (= G305), A304 (= A306), A305 (= A307), H324 (= H325), W326 (≠ Y327), G327 (= G328), M328 (≠ L329), S329 (≠ T330), Q359 (= Q360), D417 (= D422)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
32% identity, 93% coverage: 18:534/557 of query aligns to 9:527/533 of 6ihkB
- active site: T185 (= T190), H202 (≠ N210), H228 (= H234), S326 (≠ T330), E327 (= E331), K435 (≠ I443), W440 (≠ N448), K520 (= K527)
- binding adenosine-5'-diphosphate: H228 (= H234), G300 (= G305), A301 (= A306), A302 (= A307), H321 (= H325), A322 (≠ V326), W323 (≠ Y327), G324 (= G328), M325 (≠ L329), S326 (≠ T330), Q356 (= Q360), D414 (= D422), R429 (= R437), K520 (= K527)
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
35% identity, 90% coverage: 37:536/557 of query aligns to 22:486/486 of 8wevA
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
29% identity, 93% coverage: 19:534/557 of query aligns to 17:526/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G305), G293 (≠ A306), A294 (= A307), A295 (≠ P308), G314 (≠ V326), Y315 (= Y327), M317 (≠ L329), S318 (≠ T330), D408 (= D422), R423 (= R437)
- binding 4'-phosphopantetheine: R93 (= R102), P220 (= P231), H223 (= H234)
8i49A Acyl-acp synthetase structure bound to atp
29% identity, 93% coverage: 19:534/557 of query aligns to 17:526/530 of 8i49A