SitesBLAST
Comparing WP_085218260.1 NCBI__GCF_900177405.1:WP_085218260.1 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)
40% identity, 98% coverage: 11:525/528 of query aligns to 10:533/539 of P0DX84
- H231 (= H234) mutation to A: Retains 74% of wild-type activity.
- W235 (= W238) mutation to A: Almost completely abolishes the activity.
- G302 (= G305) mutation to P: Almost completely abolishes the activity.
- G303 (= G306) mutation to P: Almost completely abolishes the activity.
- W326 (= W328) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P335) mutation to A: Retains 69% of wild-type activity.
- R432 (= R424) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K426) mutation to A: Retains 36% of wild-type activity.
- D435 (= D427) mutation to A: Retains 76% of wild-type activity.
- K438 (= K430) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G432) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G433) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E434) mutation to A: Retains 27% of wild-type activity.
- W443 (= W435) mutation to A: Retains 60% of wild-type activity.
- E474 (= E466) mutation to A: Retains 33% of wild-type activity.
- K523 (= K515) 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 (= K518) 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)
39% identity, 98% coverage: 11:525/528 of query aligns to 10:533/538 of 6ijbB
- active site: T185 (= T188), H205 (= H208), H231 (= H234), S329 (≠ T331), E330 (= E332), K438 (= K430), W443 (= W435), A523 (≠ K515)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W238), G303 (= G306), A325 (≠ T327), W326 (= W328), G327 (= G329), M328 (= M330)
- binding adenosine monophosphate: G303 (= G306), A304 (= A307), A305 (≠ P308), H324 (≠ T326), W326 (= W328), G327 (= G329), M328 (= M330), S329 (≠ T331), Q359 (≠ S352), D417 (= D409)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
39% identity, 99% coverage: 4:525/528 of query aligns to 3:530/533 of 6ihkB
- active site: T185 (= T188), H202 (= H208), H228 (= H234), S326 (≠ T331), E327 (= E332), K435 (= K430), W440 (= W435), K520 (= K515)
- binding adenosine-5'-diphosphate: H228 (= H234), G300 (= G306), A301 (= A307), A302 (≠ P308), H321 (≠ T326), A322 (≠ T327), W323 (= W328), G324 (= G329), M325 (= M330), S326 (≠ T331), Q356 (≠ S352), D414 (= D409), R429 (= R424), K520 (= K515)
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)
39% identity, 97% coverage: 16:525/528 of query aligns to 23:534/541 of Q5SKN9
- T184 (= T188) binding Mg(2+)
- G302 (= G306) binding tetradecanoyl-AMP
- Q322 (≠ T326) binding tetradecanoyl-AMP
- G323 (≠ T327) binding tetradecanoyl-AMP
- T327 (= T331) binding tetradecanoyl-AMP
- E328 (= E332) binding Mg(2+)
- D418 (= D409) binding tetradecanoyl-AMP
- K435 (= K426) binding tetradecanoyl-AMP
- K439 (= K430) binding tetradecanoyl-AMP
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
38% identity, 94% coverage: 16:509/528 of query aligns to 16:494/510 of 1v26B
- active site: T177 (= T188), H197 (= H208), H223 (= H234), T320 (= T331), E321 (= E332), K432 (= K430), W437 (= W435)
- binding adenosine monophosphate: G295 (= G306), S296 (≠ A307), A297 (≠ P308), G316 (≠ T327), Y317 (≠ W328), G318 (= G329), L319 (≠ M330), T320 (= T331), D411 (= D409), K428 (= K426), K432 (= K430), W437 (= W435)
- binding magnesium ion: T177 (= T188), E321 (= E332)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
39% identity, 87% coverage: 16:472/528 of query aligns to 16:464/491 of 1v25A
- active site: T177 (= T188), H197 (= H208), H223 (= H234), T320 (= T331), E321 (= E332), K432 (= K430), W437 (= W435)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H234), V224 (≠ A235), G295 (= G306), S296 (≠ A307), A297 (≠ P308), Y317 (≠ W328), G318 (= G329), L319 (≠ M330), T320 (= T331), D411 (= D409), I423 (= I421), K432 (= K430), W437 (= W435)
- binding magnesium ion: T177 (= T188), E321 (= E332)
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2
28% identity, 98% coverage: 8:523/528 of query aligns to 7:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T188), G174 (= G190), T175 (= T191), T176 (= T192), K180 (= K196), G293 (= G306), A294 (= A307), A295 (≠ P308), Y315 (≠ W328), M317 (= M330), S318 (≠ T331), D408 (= D409), R423 (= R424)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp
28% identity, 98% coverage: 8:523/528 of query aligns to 7:527/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G305), G293 (= G306), A294 (= A307), A295 (≠ P308), G314 (≠ T327), Y315 (≠ W328), M317 (= M330), S318 (≠ T331), D408 (= D409), R423 (= R424)
- binding 4'-phosphopantetheine: R93 (= R98), P220 (= P231), H223 (= H234)
8i49A Acyl-acp synthetase structure bound to atp
28% identity, 98% coverage: 8:523/528 of query aligns to 7:527/530 of 8i49A