SitesBLAST
Comparing WP_058857116.1 NCBI__GCF_001482365.1:WP_058857116.1 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)
38% identity, 96% coverage: 15:558/568 of query aligns to 5:550/561 of P69451
- Y213 (= Y222) mutation to A: Loss of activity.
- T214 (= T223) mutation to A: 10% of wild-type activity.
- G216 (= G225) mutation to A: Decreases activity.
- T217 (= T226) mutation to A: Decreases activity.
- G219 (= G228) mutation to A: Decreases activity.
- K222 (= K231) mutation to A: Decreases activity.
- E361 (= E366) 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, 89% coverage: 55:561/568 of query aligns to 61:550/556 of Q9S725
- K211 (= K231) mutation to S: Drastically reduces the activity.
- M293 (≠ P309) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V336) mutation K->L,A: Affects the substrate specificity.
- E401 (= E412) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ W414) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R460) mutation to Q: Drastically reduces the activity.
- K457 (≠ G468) mutation to S: Drastically reduces the activity.
- K540 (= K551) 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)
34% identity, 90% coverage: 55:563/568 of query aligns to 57:547/559 of Q67W82
- G395 (= G411) 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)
31% identity, 91% coverage: 42:557/568 of query aligns to 38:536/546 of Q84P21
- K530 (= K551) mutation to N: Lossed enzymatic activity.
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
35% identity, 90% coverage: 47:560/568 of query aligns to 19:486/486 of 8wevA
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 90% coverage: 47:558/568 of query aligns to 17:498/506 of 4gxqA
- active site: T163 (= T223), N183 (= N243), H207 (= H267), T303 (= T365), E304 (= E366), I403 (= I466), N408 (= N471), A491 (≠ K551)
- binding adenosine-5'-triphosphate: T163 (= T223), S164 (= S224), G165 (= G225), T166 (= T226), T167 (= T227), H207 (= H267), S277 (≠ A339), A278 (≠ M340), P279 (≠ T341), E298 (= E360), M302 (≠ L364), T303 (= T365), D382 (= D445), R397 (= R460)
- binding carbonate ion: H207 (= H267), S277 (≠ A339), R299 (≠ G361), G301 (= G363)
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)
30% identity, 95% coverage: 26:563/568 of query aligns to 18:538/542 of O24146
- S189 (≠ T223) binding ATP
- S190 (= S224) binding ATP
- G191 (= G225) binding ATP
- T192 (= T226) binding ATP
- T193 (= T227) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K231) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H267) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F269) 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 (≠ L273) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ T290) binding CoA
- A309 (= A339) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ E360) binding ATP
- G332 (= G361) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T365) 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 (≠ L370) 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 (= D445) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R460) 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 (= K462) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I466) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G468) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G469) binding CoA
- Q446 (≠ N471) binding AMP
- K526 (= K551) 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)
30% identity, 94% coverage: 26:561/568 of query aligns to 10:528/528 of 5bsrA
- active site: S181 (≠ T223), S201 (≠ N243), H229 (= H267), T328 (= T365), E329 (= E366), K433 (≠ I466), Q438 (≠ N471), K518 (= K551)
- binding adenosine monophosphate: A301 (= A339), G326 (= G363), T328 (= T365), D412 (= D445), K429 (= K462), K433 (≠ I466), Q438 (≠ N471)
- binding coenzyme a: L102 (= L115), P226 (= P264), H229 (= H267), Y231 (≠ F269), F253 (≠ V291), K435 (≠ G468), G436 (= G469), F437 (= F470), F498 (≠ R531)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 94% coverage: 26:561/568 of query aligns to 11:529/530 of 5bsmA