SitesBLAST
Comparing WP_028489631.1 NCBI__GCF_000621325.1:WP_028489631.1 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)
59% identity, 100% coverage: 1:554/555 of query aligns to 1:551/561 of P69451
- Y213 (= Y215) mutation to A: Loss of activity.
- T214 (= T216) mutation to A: 10% of wild-type activity.
- G216 (= G218) mutation to A: Decreases activity.
- T217 (= T219) mutation to A: Decreases activity.
- G219 (= G221) mutation to A: Decreases activity.
- K222 (= K224) mutation to A: Decreases activity.
- E361 (= E363) mutation to A: Loss of activity.
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
34% identity, 92% coverage: 41:553/555 of query aligns to 22:484/486 of 8wevA
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)
28% identity, 98% coverage: 12:553/555 of query aligns to 31:547/556 of Q9S725
- K211 (= K224) mutation to S: Drastically reduces the activity.
- M293 (≠ T306) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ L333) mutation K->L,A: Affects the substrate specificity.
- E401 (= E408) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ W410) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R456) mutation to Q: Drastically reduces the activity.
- K457 (≠ S464) mutation to S: Drastically reduces the activity.
- K540 (= K546) mutation to N: Abolishes the activity.
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
28% identity, 98% coverage: 12:553/555 of query aligns to 13:526/530 of 5bsmA
- active site: S182 (≠ T216), S202 (≠ N236), H230 (= H263), T329 (= T362), E330 (= E363), K434 (≠ L462), Q439 (≠ N467), K519 (= K546)
- binding adenosine-5'-triphosphate: S182 (≠ T216), S183 (≠ G217), G184 (= G218), T185 (= T219), T186 (= T220), K190 (= K224), H230 (= H263), A302 (≠ G336), A303 (≠ M337), P304 (≠ A338), Y326 (= Y359), G327 (= G360), M328 (≠ L361), T329 (= T362), D413 (= D441), I425 (≠ L453), R428 (= R456), K519 (= K546)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
28% identity, 98% coverage: 12:553/555 of query aligns to 13:526/529 of 5bsvA
- active site: S182 (≠ T216), S202 (≠ N236), H230 (= H263), T329 (= T362), E330 (= E363), K434 (≠ L462), Q439 (≠ N467), K519 (= K546)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H263), Y232 (≠ F265), S236 (≠ A269), A302 (≠ G336), A303 (≠ M337), P304 (≠ A338), G325 (≠ A358), G327 (= G360), M328 (≠ L361), T329 (= T362), P333 (= P366), V334 (≠ A367), D413 (= D441), K430 (= K458), K434 (≠ L462), Q439 (≠ N467)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
28% identity, 98% coverage: 12:553/555 of query aligns to 13:526/529 of 5bsuA
- active site: S182 (≠ T216), S202 (≠ N236), H230 (= H263), T329 (= T362), E330 (= E363), K434 (≠ L462), Q439 (≠ N467), K519 (= K546)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H263), Y232 (≠ F265), S236 (≠ A269), M299 (≠ L333), A302 (≠ G336), A303 (≠ M337), P304 (≠ A338), G325 (≠ A358), G327 (= G360), M328 (≠ L361), T329 (= T362), P333 (= P366), D413 (= D441), K430 (= K458), K434 (≠ L462), Q439 (≠ N467)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
28% identity, 98% coverage: 12:553/555 of query aligns to 13:526/529 of 5bstA
- active site: S182 (≠ T216), S202 (≠ N236), H230 (= H263), T329 (= T362), E330 (= E363), K434 (≠ L462), Q439 (≠ N467), K519 (= K546)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H263), Y232 (≠ F265), S236 (≠ A269), A302 (≠ G336), A303 (≠ M337), P304 (≠ A338), G325 (≠ A358), Y326 (= Y359), G327 (= G360), M328 (≠ L361), T329 (= T362), P333 (= P366), V334 (≠ A367), D413 (= D441), K430 (= K458), K434 (≠ L462), Q439 (≠ N467)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
28% identity, 98% coverage: 12:553/555 of query aligns to 12:525/528 of 5bsrA
- active site: S181 (≠ T216), S201 (≠ N236), H229 (= H263), T328 (= T362), E329 (= E363), K433 (≠ L462), Q438 (≠ N467), K518 (= K546)
- binding adenosine monophosphate: A301 (≠ G336), G326 (= G360), T328 (= T362), D412 (= D441), K429 (= K458), K433 (≠ L462), Q438 (≠ N467)
- binding coenzyme a: L102 (= L107), P226 (= P260), H229 (= H263), Y231 (≠ F265), F253 (≠ R288), K435 (≠ S464), G436 (= G465), F437 (= F466), F498 (≠ A526)
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)
28% identity, 98% coverage: 12:553/555 of query aligns to 20:533/542 of O24146