SitesBLAST
Comparing WP_002967402.1 NCBI__GCF_000022745.1:WP_002967402.1 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)
54% identity, 95% coverage: 28:581/581 of query aligns to 1:551/561 of P69451
- Y213 (= Y238) mutation to A: Loss of activity.
- T214 (= T239) mutation to A: 10% of wild-type activity.
- G216 (= G241) mutation to A: Decreases activity.
- T217 (= T242) mutation to A: Decreases activity.
- G219 (= G244) mutation to A: Decreases activity.
- K222 (= K247) mutation to A: Decreases activity.
- E361 (= E390) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
32% identity, 88% coverage: 70:581/581 of query aligns to 23:499/506 of 4gxqA
- active site: T163 (= T239), N183 (= N259), H207 (= H290), T303 (≠ S389), E304 (= E390), I403 (≠ L489), N408 (= N494), A491 (≠ K573)
- binding adenosine-5'-triphosphate: T163 (= T239), S164 (≠ G240), G165 (= G241), T166 (= T242), T167 (= T243), H207 (= H290), S277 (≠ G363), A278 (≠ M364), P279 (≠ A365), E298 (= E384), M302 (≠ L388), T303 (≠ S389), D382 (= D468), R397 (= R483)
- binding carbonate ion: H207 (= H290), S277 (≠ G363), R299 (≠ G385), G301 (= G387)
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)
29% identity, 93% coverage: 43:580/581 of query aligns to 29:547/556 of Q9S725
- K211 (= K247) mutation to S: Drastically reduces the activity.
- M293 (≠ P333) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ L360) mutation K->L,A: Affects the substrate specificity.
- E401 (= E435) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C437) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R483) mutation to Q: Drastically reduces the activity.
- K457 (≠ S491) mutation to S: Drastically reduces the activity.
- K540 (= K573) 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)
31% identity, 87% coverage: 73:580/581 of query aligns to 57:542/559 of Q67W82
- G395 (= G434) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
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, 87% coverage: 77:580/581 of query aligns to 54:533/542 of O24146
- S189 (≠ T239) binding ATP
- S190 (≠ G240) binding ATP
- G191 (= G241) binding ATP
- T192 (= T242) binding ATP
- T193 (= T243) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K247) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H290) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F292) 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 (≠ V296) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ P314) binding CoA
- A309 (≠ G363) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E384) binding ATP
- G332 (= G385) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (≠ S389) 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 (= V394) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ C396) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D468) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R483) 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 (= K485) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ L489) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S491) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G492) binding CoA
- Q446 (≠ N494) binding AMP
- K526 (= K573) 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)
31% identity, 87% coverage: 77:580/581 of query aligns to 46:525/528 of 5bsrA
- active site: S181 (≠ T239), S201 (≠ N259), H229 (= H290), T328 (≠ S389), E329 (= E390), K433 (≠ L489), Q438 (≠ N494), K518 (= K573)
- binding adenosine monophosphate: A301 (≠ G363), G326 (= G387), T328 (≠ S389), D412 (= D468), K429 (= K485), K433 (≠ L489), Q438 (≠ N494)
- binding coenzyme a: L102 (= L133), P226 (= P287), H229 (= H290), Y231 (≠ F292), F253 (≠ R315), K435 (≠ S491), G436 (= G492), F437 (= F493), F498 (≠ N553)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
31% identity, 87% coverage: 77:580/581 of query aligns to 47:526/529 of 5bsvA
- active site: S182 (≠ T239), S202 (≠ N259), H230 (= H290), T329 (≠ S389), E330 (= E390), K434 (≠ L489), Q439 (≠ N494), K519 (= K573)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H290), Y232 (≠ F292), S236 (≠ V296), A302 (≠ G363), A303 (≠ M364), P304 (≠ A365), G325 (= G385), G327 (= G387), M328 (≠ L388), T329 (≠ S389), P333 (= P393), V334 (= V394), D413 (= D468), K430 (= K485), K434 (≠ L489), Q439 (≠ N494)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
31% identity, 87% coverage: 77:580/581 of query aligns to 47:526/529 of 5bsuA
- active site: S182 (≠ T239), S202 (≠ N259), H230 (= H290), T329 (≠ S389), E330 (= E390), K434 (≠ L489), Q439 (≠ N494), K519 (= K573)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H290), Y232 (≠ F292), S236 (≠ V296), M299 (≠ L360), A302 (≠ G363), A303 (≠ M364), P304 (≠ A365), G325 (= G385), G327 (= G387), M328 (≠ L388), T329 (≠ S389), P333 (= P393), D413 (= D468), K430 (= K485), K434 (≠ L489), Q439 (≠ N494)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
31% identity, 87% coverage: 77:580/581 of query aligns to 47:526/529 of 5bstA