SitesBLAST
Comparing WP_089752071.1 NCBI__GCF_900113125.1:WP_089752071.1 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)
40% identity, 98% coverage: 5:517/526 of query aligns to 18:534/541 of Q5SKN9
- T184 (= T170) binding Mg(2+)
- G302 (= G285) binding tetradecanoyl-AMP
- Q322 (= Q306) binding tetradecanoyl-AMP
- G323 (≠ V307) binding tetradecanoyl-AMP
- T327 (= T311) binding tetradecanoyl-AMP
- E328 (= E312) binding Mg(2+)
- D418 (= D401) binding tetradecanoyl-AMP
- K435 (= K418) binding tetradecanoyl-AMP
- K439 (≠ I422) 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)
35% identity, 98% coverage: 1:517/526 of query aligns to 6:533/539 of P0DX84
- H231 (= H214) mutation to A: Retains 74% of wild-type activity.
- W235 (= W218) mutation to A: Almost completely abolishes the activity.
- G302 (≠ A284) mutation to P: Almost completely abolishes the activity.
- G303 (= G285) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y308) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P315) mutation to A: Retains 69% of wild-type activity.
- R432 (= R416) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K418) mutation to A: Retains 36% of wild-type activity.
- D435 (= D419) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I422) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G424) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G425) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E426) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N427) mutation to A: Retains 60% of wild-type activity.
- E474 (= E458) mutation to A: Retains 33% of wild-type activity.
- K523 (= K507) 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 (= K510) 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)
34% identity, 98% coverage: 1:517/526 of query aligns to 6:533/538 of 6ijbB
- active site: T185 (= T170), H205 (= H190), H231 (= H214), S329 (≠ T311), E330 (= E312), K438 (≠ I422), W443 (≠ N427), A523 (≠ K507)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W218), G303 (= G285), A325 (≠ V307), W326 (≠ Y308), G327 (= G309), M328 (= M310)
- binding adenosine monophosphate: G303 (= G285), A304 (≠ S286), A305 (= A287), H324 (≠ Q306), W326 (≠ Y308), G327 (= G309), M328 (= M310), S329 (≠ T311), Q359 (≠ A341), D417 (= D401)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
34% identity, 98% coverage: 1:517/526 of query aligns to 6:530/533 of 6ihkB
- active site: T185 (= T170), H202 (= H190), H228 (= H214), S326 (≠ T311), E327 (= E312), K435 (≠ I422), W440 (≠ N427), K520 (= K507)
- binding adenosine-5'-diphosphate: H228 (= H214), G300 (= G285), A301 (≠ S286), A302 (= A287), H321 (≠ Q306), A322 (≠ V307), W323 (≠ Y308), G324 (= G309), M325 (= M310), S326 (≠ T311), Q356 (≠ A341), D414 (= D401), R429 (= R416), K520 (= K507)
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
38% identity, 96% coverage: 5:509/526 of query aligns to 11:502/510 of 1v26B
- active site: T177 (= T170), H197 (= H190), H223 (= H214), T320 (= T311), E321 (= E312), K432 (≠ I422), W437 (≠ N427)
- binding adenosine monophosphate: G295 (= G285), S296 (= S286), A297 (= A287), G316 (≠ V307), Y317 (= Y308), G318 (= G309), L319 (≠ M310), T320 (= T311), D411 (= D401), K428 (= K418), K432 (≠ I422), W437 (≠ N427)
- binding magnesium ion: T177 (= T170), E321 (= E312)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
40% identity, 87% coverage: 5:464/526 of query aligns to 11:464/491 of 1v25A
- active site: T177 (= T170), H197 (= H190), H223 (= H214), T320 (= T311), E321 (= E312), K432 (≠ I422), W437 (≠ N427)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H214), V224 (= V215), G295 (= G285), S296 (= S286), A297 (= A287), Y317 (= Y308), G318 (= G309), L319 (≠ M310), T320 (= T311), D411 (= D401), I423 (= I413), K432 (≠ I422), W437 (≠ N427)
- binding magnesium ion: T177 (= T170), E321 (= E312)
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2
31% identity, 97% coverage: 5:515/526 of query aligns to 10:519/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T170), G174 (= G172), T175 (= T173), T176 (= T174), K180 (= K178), G293 (= G285), A294 (≠ S286), A295 (= A287), Y315 (= Y308), M317 (= M310), S318 (≠ T311), D408 (= D401), R423 (= R416)
8jylA Acyl-acp synthetase structure bound to c10-ams
31% identity, 97% coverage: 5:515/526 of query aligns to 8:525/527 of 8jylA
- binding magnesium ion: S316 (≠ T311), E317 (= E312)
- binding [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl N-decanoylsulfamate: W225 (= W218), G290 (≠ A284), G291 (= G285), A292 (≠ S286), A293 (= A287), G312 (≠ V307), Y313 (= Y308), G314 (= G309), M315 (= M310), S316 (≠ T311), I321 (≠ L316), D406 (= D401), R421 (= R416), K427 (≠ I422), W432 (≠ N427)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
31% identity, 97% coverage: 5:515/526 of query aligns to 8:525/528 of 8i6mA