SitesBLAST
Comparing HSERO_RS19285 HSERO_RS19285 long-chain fatty acid--CoA ligase 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, 98% coverage: 1:556/566 of query aligns to 1:552/561 of P69451
- Y213 (= Y212) mutation to A: Loss of activity.
- T214 (= T213) mutation to A: 10% of wild-type activity.
- G216 (= G215) mutation to A: Decreases activity.
- T217 (= T216) mutation to A: Decreases activity.
- G219 (= G218) mutation to A: Decreases activity.
- K222 (= K221) mutation to A: Decreases activity.
- E361 (= E364) mutation to A: Loss of activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 90% coverage: 46:555/566 of query aligns to 26:499/506 of 4gxqA
- active site: T163 (= T213), N183 (= N233), H207 (= H264), T303 (≠ S363), E304 (= E364), I403 (≠ L463), N408 (= N468), A491 (≠ K547)
- binding adenosine-5'-triphosphate: T163 (= T213), S164 (≠ G214), G165 (= G215), T166 (= T216), T167 (= T217), K171 (= K221), H207 (= H264), S277 (≠ G337), A278 (≠ M338), P279 (≠ A339), E298 (= E358), R299 (≠ G359), Y300 (= Y360), G301 (= G361), M302 (≠ L362), T303 (≠ S363), V322 (≠ I383), D382 (= D442), I394 (= I454), R397 (= R457)
- binding carbonate ion: H207 (= H264), T208 (≠ I265), H209 (≠ F266), S277 (≠ G337), R299 (≠ G359), G301 (= G361), M302 (≠ L362), M307 (≠ I368)
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, 90% coverage: 46:554/566 of query aligns to 61:547/556 of Q9S725
- K211 (= K221) mutation to S: Drastically reduces the activity.
- M293 (≠ P307) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ V334) mutation K->L,A: Affects the substrate specificity.
- E401 (= E409) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (≠ A411) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R457) mutation to Q: Drastically reduces the activity.
- K457 (≠ S465) mutation to S: Drastically reduces the activity.
- K540 (= K547) mutation to N: Abolishes the activity.
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)
28% identity, 92% coverage: 36:553/566 of query aligns to 43:536/546 of Q84P21
- K530 (= K547) mutation to N: Lossed enzymatic activity.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 92% coverage: 33:554/566 of query aligns to 36:525/528 of 5bsrA
- active site: S181 (≠ T213), S201 (≠ N233), H229 (= H264), T328 (≠ S363), E329 (= E364), K433 (≠ L463), Q438 (≠ N468), K518 (= K547)
- binding adenosine monophosphate: A301 (≠ G337), A302 (≠ M338), P303 (≠ A339), G324 (= G359), Y325 (= Y360), G326 (= G361), M327 (≠ L362), T328 (≠ S363), D412 (= D442), I424 (= I454), R427 (= R457), K429 (= K459), K433 (≠ L463), Q438 (≠ N468)
- binding coenzyme a: L102 (= L106), L225 (= L260), P226 (= P261), H229 (= H264), Y231 (≠ F266), K252 (≠ P288), F253 (≠ R289), V273 (= V309), I276 (≠ L312), K435 (≠ S465), G436 (= G466), F437 (= F467), F498 (≠ G527)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 92% coverage: 33:554/566 of query aligns to 37:526/529 of 5bsvA
- active site: S182 (≠ T213), S202 (≠ N233), H230 (= H264), T329 (≠ S363), E330 (= E364), K434 (≠ L463), Q439 (≠ N468), K519 (= K547)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H264), Y232 (≠ F266), S236 (≠ V270), S300 (≠ G335), G301 (= G336), A302 (≠ G337), A303 (≠ M338), P304 (≠ A339), Q324 (≠ E358), G325 (= G359), Y326 (= Y360), G327 (= G361), M328 (≠ L362), T329 (≠ S363), P333 (= P367), V334 (≠ I368), M337 (vs. gap), D413 (= D442), I425 (= I454), R428 (= R457), K430 (= K459), K434 (≠ L463), Q439 (≠ N468)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 92% coverage: 33:554/566 of query aligns to 37:526/529 of 5bsuA
- active site: S182 (≠ T213), S202 (≠ N233), H230 (= H264), T329 (≠ S363), E330 (= E364), K434 (≠ L463), Q439 (≠ N468), K519 (= K547)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H264), Y232 (≠ F266), S236 (≠ V270), M299 (≠ V334), G301 (= G336), A302 (≠ G337), A303 (≠ M338), P304 (≠ A339), Q324 (≠ E358), G325 (= G359), Y326 (= Y360), G327 (= G361), M328 (≠ L362), T329 (≠ S363), P333 (= P367), V334 (≠ I368), D413 (= D442), I425 (= I454), R428 (= R457), K430 (= K459), K434 (≠ L463), Q439 (≠ N468)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 92% coverage: 33:554/566 of query aligns to 37:526/529 of 5bstA
- active site: S182 (≠ T213), S202 (≠ N233), H230 (= H264), T329 (≠ S363), E330 (= E364), K434 (≠ L463), Q439 (≠ N468), K519 (= K547)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H264), Y232 (≠ F266), S236 (≠ V270), M299 (≠ V334), G301 (= G336), A302 (≠ G337), A303 (≠ M338), P304 (≠ A339), Q324 (≠ E358), G325 (= G359), Y326 (= Y360), G327 (= G361), M328 (≠ L362), T329 (≠ S363), P333 (= P367), V334 (≠ I368), D413 (= D442), I425 (= I454), R428 (= R457), K430 (= K459), K434 (≠ L463), Q439 (≠ N468)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 92% coverage: 33:554/566 of query aligns to 37:526/530 of 5bsmA