SitesBLAST
Comparing WP_089214750.1 NCBI__GCF_900188185.1:WP_089214750.1 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)
52% identity, 98% coverage: 3:525/534 of query aligns to 5:535/539 of P0DX84
- H231 (= H223) mutation to A: Retains 74% of wild-type activity.
- W235 (= W227) mutation to A: Almost completely abolishes the activity.
- G302 (= G293) mutation to P: Almost completely abolishes the activity.
- G303 (= G294) mutation to P: Almost completely abolishes the activity.
- W326 (= W316) mutation to A: Retains 7.7% of wild-type activity.
- P333 (= P323) mutation to A: Retains 69% of wild-type activity.
- R432 (= R422) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K424) mutation to A: Retains 36% of wild-type activity.
- D435 (= D425) mutation to A: Retains 76% of wild-type activity.
- K438 (= K428) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G430) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G431) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E432) mutation to A: Retains 27% of wild-type activity.
- W443 (= W433) mutation to A: Retains 60% of wild-type activity.
- E474 (= E464) mutation to A: Retains 33% of wild-type activity.
- K523 (= K513) 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 (= K516) 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)
51% identity, 98% coverage: 3:525/534 of query aligns to 5:535/538 of 6ijbB
- active site: T185 (= T177), H205 (= H197), H231 (= H223), S329 (≠ T319), E330 (= E320), K438 (= K428), W443 (= W433), A523 (≠ K513)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W227), G303 (= G294), A325 (= A315), W326 (= W316), G327 (= G317), M328 (= M318)
- binding adenosine monophosphate: G303 (= G294), A304 (≠ S295), A305 (= A296), H324 (= H314), W326 (= W316), G327 (= G317), M328 (= M318), S329 (≠ T319), Q359 (= Q349), D417 (= D407)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
51% identity, 98% coverage: 3:525/534 of query aligns to 5:532/533 of 6ihkB
- active site: T185 (= T177), H202 (= H197), H228 (= H223), S326 (≠ T319), E327 (= E320), K435 (= K428), W440 (= W433), K520 (= K513)
- binding adenosine-5'-diphosphate: H228 (= H223), G300 (= G294), A301 (≠ S295), A302 (= A296), H321 (= H314), A322 (= A315), W323 (= W316), G324 (= G317), M325 (= M318), S326 (≠ T319), Q356 (= Q349), D414 (= D407), R429 (= R422), K520 (= K513)
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)
44% identity, 98% coverage: 3:526/534 of query aligns to 13:537/541 of Q5SKN9
- T184 (= T177) binding Mg(2+)
- G302 (= G294) binding tetradecanoyl-AMP
- Q322 (≠ H314) binding tetradecanoyl-AMP
- G323 (≠ A315) binding tetradecanoyl-AMP
- T327 (= T319) binding tetradecanoyl-AMP
- E328 (= E320) binding Mg(2+)
- D418 (= D407) binding tetradecanoyl-AMP
- K435 (= K424) binding tetradecanoyl-AMP
- K439 (= K428) binding tetradecanoyl-AMP
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
42% identity, 98% coverage: 3:526/534 of query aligns to 6:506/510 of 1v26B
- active site: T177 (= T177), H197 (= H197), H223 (= H223), T320 (= T319), E321 (= E320), K432 (= K428), W437 (= W433)
- binding adenosine monophosphate: G295 (= G294), S296 (= S295), A297 (= A296), G316 (≠ A315), Y317 (≠ W316), G318 (= G317), L319 (≠ M318), T320 (= T319), D411 (= D407), K428 (= K424), K432 (= K428), W437 (= W433)
- binding magnesium ion: T177 (= T177), E321 (= E320)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
41% identity, 98% coverage: 3:526/534 of query aligns to 6:487/491 of 1v25A
- active site: T177 (= T177), H197 (= H197), H223 (= H223), T320 (= T319), E321 (= E320), K432 (= K428), W437 (= W433)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H223), V224 (≠ A224), G295 (= G294), S296 (= S295), A297 (= A296), Y317 (≠ W316), G318 (= G317), L319 (≠ M318), T320 (= T319), D411 (= D407), I423 (= I419), K432 (= K428), W437 (= W433)
- binding magnesium ion: T177 (= T177), E321 (= E320)
8i8dA Acyl-acp synthetase structure bound to mc7-acp
33% identity, 96% coverage: 8:520/534 of query aligns to 10:526/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G293), G293 (= G294), A295 (= A296), G314 (≠ A315), Y315 (≠ W316), G316 (= G317), M317 (= M318), S318 (≠ T319), D408 (= D407), K429 (= K428)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H223), W227 (= W227), G292 (= G293), G316 (= G317), P322 (= P323)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R95), P220 (= P220), H223 (= H223), I269 (≠ V269), G432 (= G431)
8i6mA Acyl-acp synthetase structure bound to amp-c18:1
33% identity, 96% coverage: 8:520/534 of query aligns to 8:524/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G294), A293 (= A296), G312 (≠ A315), Y313 (≠ W316), G314 (= G317), M315 (= M318), S316 (≠ T319), D406 (= D407), R421 (= R422)
- binding magnesium ion: M315 (= M318), S316 (≠ T319), E317 (= E320)
8i51A Acyl-acp synthetase structure bound to amp-mc7
33% identity, 96% coverage: 8:520/534 of query aligns to 8:524/528 of 8i51A