SitesBLAST
Comparing WP_092482556.1 NCBI__GCF_900115975.1:WP_092482556.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
Q4WR83 Acyl-CoA ligase sidI; Siderophore biosynthesis protein I; EC 6.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
41% identity, 98% coverage: 5:551/559 of query aligns to 31:580/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
32% identity, 87% coverage: 57:544/559 of query aligns to 68:553/561 of P69451
- Y213 (= Y202) mutation to A: Loss of activity.
- T214 (= T203) mutation to A: 10% of wild-type activity.
- G216 (= G205) mutation to A: Decreases activity.
- T217 (= T206) mutation to A: Decreases activity.
- G219 (= G208) mutation to A: Decreases activity.
- K222 (= K211) mutation to A: Decreases activity.
- E361 (= E347) 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)
31% identity, 90% coverage: 39:541/559 of query aligns to 64:547/556 of Q9S725
- K211 (= K211) mutation to S: Drastically reduces the activity.
- M293 (≠ H289) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ I316) mutation K->L,A: Affects the substrate specificity.
- E401 (= E395) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C397) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R443) mutation to Q: Drastically reduces the activity.
- K457 (≠ G451) mutation to S: Drastically reduces the activity.
- K540 (= K534) mutation to N: Abolishes the activity.
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
32% identity, 91% coverage: 33:541/559 of query aligns to 19:484/486 of 8wevA
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 90% coverage: 38:542/559 of query aligns to 28:499/506 of 4gxqA
- active site: T163 (= T203), N183 (= N223), H207 (= H247), T303 (= T346), E304 (= E347), I403 (= I449), N408 (= N454), A491 (≠ K534)
- binding adenosine-5'-triphosphate: T163 (= T203), S164 (= S204), G165 (= G205), T166 (= T206), T167 (= T207), H207 (= H247), S277 (≠ G319), A278 (= A320), P279 (= P321), E298 (≠ I341), M302 (≠ Q345), T303 (= T346), D382 (= D428), R397 (= R443)
- binding carbonate ion: H207 (= H247), S277 (≠ G319), R299 (≠ T342), G301 (= G344)
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
31% identity, 90% coverage: 39:542/559 of query aligns to 46:527/528 of 3ni2A
- active site: S182 (≠ T203), S202 (≠ N223), H230 (= H247), T329 (= T346), E330 (= E347), K434 (≠ I449), Q439 (≠ N454), K519 (= K534)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: Y232 (≠ F249), S236 (≠ M253), G302 (= G319), A303 (= A320), P304 (= P321), G325 (≠ T342), G327 (= G344), T329 (= T346), P333 (= P350), V334 (≠ G351), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
31% identity, 90% coverage: 39:542/559 of query aligns to 46:527/528 of 3a9vA
- active site: S182 (≠ T203), S202 (≠ N223), H230 (= H247), T329 (= T346), E330 (= E347), K434 (≠ I449), Q439 (≠ N454), K519 (= K534)
- binding adenosine monophosphate: H230 (= H247), G302 (= G319), A303 (= A320), P304 (= P321), Y326 (= Y343), G327 (= G344), M328 (≠ Q345), T329 (= T346), D413 (= D428), K430 (= K445), K434 (≠ I449), Q439 (≠ N454)
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, 90% coverage: 39:541/559 of query aligns to 53:533/542 of O24146
- S189 (≠ T203) binding ATP
- S190 (= S204) binding ATP
- G191 (= G205) binding ATP
- T192 (= T206) binding ATP
- T193 (= T207) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K211) binding ATP; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H247) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F249) 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 (≠ G254) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- K260 (≠ S270) binding CoA
- A309 (≠ G319) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP
- Q331 (≠ I341) binding ATP
- G332 (≠ T342) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- T336 (= T346) 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 (≠ G351) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (= M354) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D428) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; binding ATP
- R435 (= R443) 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 (= K445) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP
- K441 (≠ I449) binding (E)-4-coumaroyl-AMP; binding (E)-caffeoyl-AMP; binding (E)-feruloyl-AMP; binding AMP; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ G451) binding CoA; mutation to A: Normal activity against 4-coumarate.
- G444 (= G452) binding CoA
- Q446 (≠ N454) binding AMP
- K526 (= K534) binding ATP; mutation to A: Abolished activity against 4-coumarate.
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
31% identity, 90% coverage: 39:541/559 of query aligns to 46:526/529 of 5bsvA