SitesBLAST
Comparing WP_068002231.1 NCBI__GCF_001623255.1:WP_068002231.1 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)
40% identity, 95% coverage: 20:547/555 of query aligns to 29:556/561 of P69451
- Y213 (= Y202) mutation to A: Loss of activity.
- T214 (= T203) mutation to A: 10% of wild-type activity.
- G216 (= G205) mutation to A: Decreases activity.
- T217 (= T206) mutation to A: Decreases activity.
- G219 (= G208) mutation to A: Decreases activity.
- K222 (= K211) mutation to A: Decreases activity.
- E361 (= E348) 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: 16:540/555 of query aligns to 38:546/556 of Q9S725
- K211 (= K211) mutation to S: Drastically reduces the activity.
- M293 (≠ A291) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ M318) mutation K->L,A: Affects the substrate specificity.
- E401 (= E395) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C397) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R443) mutation to Q: Drastically reduces the activity.
- K457 (≠ S451) mutation to S: Drastically reduces the activity.
- K540 (= K534) mutation to N: Abolishes the activity.
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)
32% identity, 97% coverage: 15:553/555 of query aligns to 33:554/559 of Q67W82
- G395 (= G394) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
Q84P21 Peroxisomal OPC-8:0-CoA ligase 1; 4-coumarate--CoA ligase isoform 9; At4CL9; 4-coumarate--CoA ligase-like 5; EC 6.2.1.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 94% coverage: 24:542/555 of query aligns to 38:538/546 of Q84P21
- K530 (= K534) mutation to N: Lossed enzymatic 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)
32% identity, 95% coverage: 16:540/555 of query aligns to 27:532/542 of O24146
- S189 (≠ T203) binding ATP
- S190 (≠ G204) binding ATP
- G191 (= G205) binding ATP
- T192 (= T206) binding ATP
- T193 (= T207) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K211) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H249) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F251) 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 (≠ V255) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ R272) binding CoA
- A309 (≠ G321) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E342) binding ATP
- G332 (= G343) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T347) 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 (= V352) 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 (= D428) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R443) 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 (= K445) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I449) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S451) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G452) binding CoA
- Q446 (≠ N454) binding AMP
- K526 (= K534) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
32% identity, 95% coverage: 16:540/555 of query aligns to 19:524/528 of 5bsrA
- active site: S181 (≠ T203), S201 (= S222), H229 (= H249), T328 (= T347), E329 (= E348), K433 (≠ I449), Q438 (≠ N454), K518 (= K534)
- binding adenosine monophosphate: A301 (≠ G321), G326 (= G345), T328 (= T347), D412 (= D428), K429 (= K445), K433 (≠ I449), Q438 (≠ N454)
- binding coenzyme a: L102 (= L97), P226 (= P246), H229 (= H249), Y231 (≠ F251), F253 (= F273), K435 (≠ S451), G436 (= G452), F437 (≠ Y453), F498 (≠ K514)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
32% identity, 95% coverage: 16:540/555 of query aligns to 20:525/529 of 5bsvA
- active site: S182 (≠ T203), S202 (= S222), H230 (= H249), T329 (= T347), E330 (= E348), K434 (≠ I449), Q439 (≠ N454), K519 (= K534)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H249), Y232 (≠ F251), S236 (≠ V255), A302 (≠ G321), A303 (= A322), P304 (= P323), G325 (= G343), G327 (= G345), M328 (≠ L346), T329 (= T347), P333 (= P351), V334 (= V352), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
32% identity, 95% coverage: 16:540/555 of query aligns to 20:525/529 of 5bsuA
- active site: S182 (≠ T203), S202 (= S222), H230 (= H249), T329 (= T347), E330 (= E348), K434 (≠ I449), Q439 (≠ N454), K519 (= K534)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H249), Y232 (≠ F251), S236 (≠ V255), M299 (= M318), A302 (≠ G321), A303 (= A322), P304 (= P323), G325 (= G343), G327 (= G345), M328 (≠ L346), T329 (= T347), P333 (= P351), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
32% identity, 95% coverage: 16:540/555 of query aligns to 20:525/529 of 5bstA