SitesBLAST
Comparing WP_090275065.1 NCBI__GCF_900105005.1:WP_090275065.1 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)
P69451 Long-chain-fatty-acid--CoA ligase; Long-chain acyl-CoA synthetase; Acyl-CoA synthetase; EC 6.2.1.3 from Escherichia coli (strain K12) (see paper)
47% identity, 96% coverage: 18:539/541 of query aligns to 22:557/561 of P69451
- Y213 (= Y193) mutation to A: Loss of activity.
- T214 (= T194) mutation to A: 10% of wild-type activity.
- G216 (= G196) mutation to A: Decreases activity.
- T217 (= T197) mutation to A: Decreases activity.
- G219 (= G199) mutation to A: Decreases activity.
- K222 (= K202) mutation to A: Decreases activity.
- E361 (= E342) mutation to A: Loss of activity.
Q9S725 4-coumarate--CoA ligase 2; 4CL 2; 4-coumarate--CoA ligase isoform 2; At4CL2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; EC 6.2.1.12; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
32% identity, 95% coverage: 17:532/541 of query aligns to 34:547/556 of Q9S725
- K211 (= K202) mutation to S: Drastically reduces the activity.
- M293 (≠ T285) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ N312) mutation K->L,A: Affects the substrate specificity.
- E401 (= E387) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ L389) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R435) mutation to Q: Drastically reduces the activity.
- K457 (≠ S443) mutation to S: Drastically reduces the activity.
- K540 (= K525) mutation to N: Abolishes the activity.
O24146 4-coumarate--CoA ligase 2; 4CL 2; Nt4CL-19; Nt4CL-2; 4-coumaroyl-CoA synthase 2; Caffeate--CoA ligase; Cinnamate--CoA ligase; Ferulate--CoA ligase; EC 6.2.1.12; EC 6.2.1.-; EC 6.2.1.-; EC 6.2.1.34 from Nicotiana tabacum (Common tobacco) (see paper)
31% identity, 96% coverage: 18:537/541 of query aligns to 24:538/542 of O24146
- S189 (≠ T194) binding ATP
- S190 (≠ G195) binding ATP
- G191 (= G196) binding ATP
- T192 (= T197) binding ATP
- T193 (= T198) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K202) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H242) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F244) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ A248) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ P266) binding CoA
- A309 (≠ G315) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E336) binding ATP
- G332 (= G337) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T341) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V346) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (vs. gap) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D420) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R435) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding ATP; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K437) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ L441) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S443) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G444) binding CoA
- Q446 (≠ N446) binding AMP
- K526 (= K525) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
31% identity, 95% coverage: 18:532/541 of query aligns to 17:526/530 of 5bsmA
- active site: S182 (≠ T194), S202 (≠ N214), H230 (= H242), T329 (= T341), E330 (= E342), K434 (≠ L441), Q439 (≠ N446), K519 (= K525)
- binding adenosine-5'-triphosphate: S182 (≠ T194), S183 (≠ G195), G184 (= G196), T185 (= T197), T186 (= T198), K190 (= K202), H230 (= H242), A302 (≠ G315), A303 (= A316), P304 (= P317), Y326 (≠ F338), G327 (= G339), M328 (= M340), T329 (= T341), D413 (= D420), I425 (≠ L432), R428 (= R435), K519 (= K525)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
31% identity, 95% coverage: 18:532/541 of query aligns to 16:525/528 of 5bsrA
- active site: S181 (≠ T194), S201 (≠ N214), H229 (= H242), T328 (= T341), E329 (= E342), K433 (≠ L441), Q438 (≠ N446), K518 (= K525)
- binding adenosine monophosphate: A301 (≠ G315), G326 (= G339), T328 (= T341), D412 (= D420), K429 (= K437), K433 (≠ L441), Q438 (≠ N446)
- binding coenzyme a: L102 (≠ Q103), P226 (= P239), H229 (= H242), Y231 (≠ F244), F253 (≠ R267), K435 (≠ S443), G436 (= G444), F437 (= F445), F498 (≠ G505)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
31% identity, 95% coverage: 18:532/541 of query aligns to 17:526/529 of 5bsvA
- active site: S182 (≠ T194), S202 (≠ N214), H230 (= H242), T329 (= T341), E330 (= E342), K434 (≠ L441), Q439 (≠ N446), K519 (= K525)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H242), Y232 (≠ F244), S236 (≠ A248), A302 (≠ G315), A303 (= A316), P304 (= P317), G325 (= G337), G327 (= G339), M328 (= M340), T329 (= T341), P333 (= P345), V334 (= V346), D413 (= D420), K430 (= K437), K434 (≠ L441), Q439 (≠ N446)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
31% identity, 95% coverage: 18:532/541 of query aligns to 17:526/529 of 5bsuA
- active site: S182 (≠ T194), S202 (≠ N214), H230 (= H242), T329 (= T341), E330 (= E342), K434 (≠ L441), Q439 (≠ N446), K519 (= K525)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H242), Y232 (≠ F244), S236 (≠ A248), M299 (≠ N312), A302 (≠ G315), A303 (= A316), P304 (= P317), G325 (= G337), G327 (= G339), M328 (= M340), T329 (= T341), P333 (= P345), D413 (= D420), K430 (= K437), K434 (≠ L441), Q439 (≠ N446)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
31% identity, 95% coverage: 18:532/541 of query aligns to 17:526/529 of 5bstA
- active site: S182 (≠ T194), S202 (≠ N214), H230 (= H242), T329 (= T341), E330 (= E342), K434 (≠ L441), Q439 (≠ N446), K519 (= K525)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H242), Y232 (≠ F244), S236 (≠ A248), A302 (≠ G315), A303 (= A316), P304 (= P317), G325 (= G337), Y326 (≠ F338), G327 (= G339), M328 (= M340), T329 (= T341), P333 (= P345), V334 (= V346), D413 (= D420), K430 (= K437), K434 (≠ L441), Q439 (≠ N446)
Q67W82 4-coumarate--CoA ligase 4; 4CL 4; Os4CL4; (E)-ferulate--CoA ligase; 4-coumaroyl-CoA synthase 4; Protein RESISTANCE TO ALUMINUM 1; EC 6.2.1.12; EC 6.2.1.34 from Oryza sativa subsp. japonica (Rice) (see paper)
31% identity, 91% coverage: 46:539/541 of query aligns to 61:549/559 of Q67W82