SitesBLAST
Comparing 5209735 FitnessBrowser__PV4:5209735 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)
68% identity, 100% coverage: 1:555/557 of query aligns to 1:554/561 of P69451
- Y213 (= Y213) mutation to A: Loss of activity.
- T214 (= T214) mutation to A: 10% of wild-type activity.
- G216 (= G216) mutation to A: Decreases activity.
- T217 (= T217) mutation to A: Decreases activity.
- G219 (= G219) mutation to A: Decreases activity.
- K222 (= K222) mutation to A: Decreases activity.
- E361 (= E361) 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)
30% identity, 94% coverage: 28:551/557 of query aligns to 42:547/556 of Q9S725
- K211 (= K222) mutation to S: Drastically reduces the activity.
- M293 (≠ T304) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I331) mutation K->L,A: Affects the substrate specificity.
- E401 (= E406) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ F408) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R454) mutation to Q: Drastically reduces the activity.
- K457 (≠ S462) mutation to S: Drastically reduces the activity.
- K540 (= K544) 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)
32% identity, 93% coverage: 32:551/557 of query aligns to 34:533/542 of O24146
- S189 (≠ T214) binding
- S190 (≠ G215) binding
- G191 (= G216) binding
- T192 (= T217) binding
- T193 (= T218) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K222) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H261) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F263) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ V267) binding ; binding ; binding
- K260 (≠ P285) binding
- A309 (≠ G334) binding ; binding ; binding
- Q331 (≠ E355) binding
- G332 (= G356) binding ; binding ; binding ; binding ; binding
- T336 (= T360) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (≠ L365) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ C368) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D439) binding ; binding ; binding ; binding ; binding
- R435 (= R454) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K456) binding ; binding ; binding ; binding
- K441 (≠ L460) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S462) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G463) binding
- Q446 (≠ N465) binding
- K526 (= K544) binding ; 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, 93% coverage: 32:551/557 of query aligns to 26:525/528 of 5bsrA
- active site: S181 (≠ T214), S201 (≠ N234), H229 (= H261), T328 (= T360), E329 (= E361), K433 (≠ L460), Q438 (≠ N465), K518 (= K544)
- binding adenosine monophosphate: A301 (≠ G334), A302 (≠ M335), P303 (≠ A336), G324 (= G356), Y325 (= Y357), G326 (= G358), M327 (≠ L359), T328 (= T360), D412 (= D439), I424 (= I451), R427 (= R454), K429 (= K456), K433 (≠ L460), Q438 (≠ N465)
- binding coenzyme a: L102 (= L107), L225 (= L257), P226 (= P258), H229 (= H261), Y231 (≠ F263), K252 (≠ P285), F253 (≠ R286), V273 (= V306), I276 (≠ L309), K435 (≠ S462), G436 (= G463), F437 (= F464), F498 (≠ G524)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
32% identity, 93% coverage: 32:551/557 of query aligns to 27:526/529 of 5bsvA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H261), Y232 (≠ F263), S236 (≠ V267), S300 (≠ G332), G301 (= G333), A302 (≠ G334), A303 (≠ M335), P304 (≠ A336), Q324 (≠ E355), G325 (= G356), Y326 (= Y357), G327 (= G358), M328 (≠ L359), T329 (= T360), P333 (= P364), V334 (≠ L365), M337 (≠ C368), D413 (= D439), I425 (= I451), R428 (= R454), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
32% identity, 93% coverage: 32:551/557 of query aligns to 27:526/529 of 5bsuA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H261), Y232 (≠ F263), S236 (≠ V267), M299 (≠ I331), G301 (= G333), A302 (≠ G334), A303 (≠ M335), P304 (≠ A336), Q324 (≠ E355), G325 (= G356), Y326 (= Y357), G327 (= G358), M328 (≠ L359), T329 (= T360), P333 (= P364), V334 (≠ L365), D413 (= D439), I425 (= I451), R428 (= R454), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
32% identity, 93% coverage: 32:551/557 of query aligns to 27:526/529 of 5bstA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H261), Y232 (≠ F263), S236 (≠ V267), M299 (≠ I331), G301 (= G333), A302 (≠ G334), A303 (≠ M335), P304 (≠ A336), Q324 (≠ E355), G325 (= G356), Y326 (= Y357), G327 (= G358), M328 (≠ L359), T329 (= T360), P333 (= P364), V334 (≠ L365), D413 (= D439), I425 (= I451), R428 (= R454), K430 (= K456), K434 (≠ L460), Q439 (≠ N465)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
32% identity, 93% coverage: 32:551/557 of query aligns to 27:526/530 of 5bsmA
- active site: S182 (≠ T214), S202 (≠ N234), H230 (= H261), T329 (= T360), E330 (= E361), K434 (≠ L460), Q439 (≠ N465), K519 (= K544)
- binding adenosine-5'-triphosphate: S182 (≠ T214), S183 (≠ G215), G184 (= G216), T185 (= T217), T186 (= T218), K190 (= K222), H230 (= H261), A302 (≠ G334), A303 (≠ M335), P304 (≠ A336), Q324 (≠ E355), G325 (= G356), Y326 (= Y357), G327 (= G358), M328 (≠ L359), T329 (= T360), D413 (= D439), I425 (= I451), R428 (= R454), K519 (= K544)
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, 93% coverage: 35:551/557 of query aligns to 44:542/559 of Q67W82