SitesBLAST
Comparing WP_068009600.1 NCBI__GCF_001623255.1:WP_068009600.1 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)
50% identity, 99% coverage: 6:543/544 of query aligns to 8:551/561 of P69451
- Y213 (= Y204) mutation to A: Loss of activity.
- T214 (= T205) mutation to A: 10% of wild-type activity.
- G216 (= G207) mutation to A: Decreases activity.
- T217 (= T208) mutation to A: Decreases activity.
- G219 (= G210) mutation to A: Decreases activity.
- K222 (= K213) mutation to A: Decreases activity.
- E361 (= E352) mutation to A: Loss of activity.
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
33% identity, 94% coverage: 35:544/544 of query aligns to 13:486/486 of 8wevA
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 92% coverage: 45:543/544 of query aligns to 23:499/506 of 4gxqA
- active site: T163 (= T205), N183 (= N225), H207 (= H252), T303 (≠ S351), E304 (= E352), I403 (≠ L451), N408 (= N456), A491 (≠ K535)
- binding adenosine-5'-triphosphate: T163 (= T205), S164 (≠ G206), G165 (= G207), T166 (= T208), T167 (= T209), H207 (= H252), S277 (≠ G325), A278 (≠ S326), P279 (≠ A327), E298 (= E346), M302 (≠ L350), T303 (≠ S351), D382 (= D430), R397 (= R445)
- binding carbonate ion: H207 (= H252), S277 (≠ G325), R299 (≠ G347), G301 (= G349)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 94% coverage: 33:544/544 of query aligns to 26:528/529 of 5bsvA
- active site: S182 (≠ T205), S202 (≠ N225), H230 (= H252), T329 (≠ S351), E330 (= E352), K434 (≠ L451), Q439 (≠ N456), K519 (= K535)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H252), Y232 (≠ F254), S236 (≠ V258), A302 (≠ G325), A303 (≠ S326), P304 (≠ A327), G325 (= G347), G327 (= G349), M328 (≠ L350), T329 (≠ S351), P333 (= P355), V334 (≠ I356), D413 (= D430), K430 (= K447), K434 (≠ L451), Q439 (≠ N456)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 94% coverage: 33:544/544 of query aligns to 26:528/529 of 5bsuA
- active site: S182 (≠ T205), S202 (≠ N225), H230 (= H252), T329 (≠ S351), E330 (= E352), K434 (≠ L451), Q439 (≠ N456), K519 (= K535)
- binding 5'-O-[(R)-{[(2E)-3-(3,4-dioxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}(hydroxy)phosphoryl]adenosine: H230 (= H252), Y232 (≠ F254), S236 (≠ V258), M299 (= M322), A302 (≠ G325), A303 (≠ S326), P304 (≠ A327), G325 (= G347), G327 (= G349), M328 (≠ L350), T329 (≠ S351), P333 (= P355), D413 (= D430), K430 (= K447), K434 (≠ L451), Q439 (≠ N456)
5bstA Crystal structure of 4-coumarate:coa ligase complexed with coumaroyl adenylate (see paper)
30% identity, 94% coverage: 33:544/544 of query aligns to 26:528/529 of 5bstA
- active site: S182 (≠ T205), S202 (≠ N225), H230 (= H252), T329 (≠ S351), E330 (= E352), K434 (≠ L451), Q439 (≠ N456), K519 (= K535)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H252), Y232 (≠ F254), S236 (≠ V258), A302 (≠ G325), A303 (≠ S326), P304 (≠ A327), G325 (= G347), Y326 (= Y348), G327 (= G349), M328 (≠ L350), T329 (≠ S351), P333 (= P355), V334 (≠ I356), D413 (= D430), K430 (= K447), K434 (≠ L451), Q439 (≠ N456)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
30% identity, 94% coverage: 33:544/544 of query aligns to 26:528/530 of 5bsmA
- active site: S182 (≠ T205), S202 (≠ N225), H230 (= H252), T329 (≠ S351), E330 (= E352), K434 (≠ L451), Q439 (≠ N456), K519 (= K535)
- binding adenosine-5'-triphosphate: S182 (≠ T205), S183 (≠ G206), G184 (= G207), T185 (= T208), T186 (= T209), K190 (= K213), H230 (= H252), A302 (≠ G325), A303 (≠ S326), P304 (≠ A327), Y326 (= Y348), G327 (= G349), M328 (≠ L350), T329 (≠ S351), D413 (= D430), I425 (= I442), R428 (= R445), K519 (= K535)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 94% coverage: 33:544/544 of query aligns to 25:527/528 of 5bsrA
- active site: S181 (≠ T205), S201 (≠ N225), H229 (= H252), T328 (≠ S351), E329 (= E352), K433 (≠ L451), Q438 (≠ N456), K518 (= K535)
- binding adenosine monophosphate: A301 (≠ G325), G326 (= G349), T328 (≠ S351), D412 (= D430), K429 (= K447), K433 (≠ L451), Q438 (≠ N456)
- binding coenzyme a: L102 (= L109), P226 (= P249), H229 (= H252), Y231 (≠ F254), F253 (≠ R277), K435 (≠ S453), G436 (= G454), F437 (= F455), F498 (≠ A515)
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, 94% coverage: 36:544/544 of query aligns to 36:535/542 of O24146