SitesBLAST
Comparing PfGW456L13_1910 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1910 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)
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)
53% identity, 99% coverage: 6:562/562 of query aligns to 5:553/561 of P69451
- Y213 (= Y214) mutation to A: Loss of activity.
- T214 (= T215) mutation to A: 10% of wild-type activity.
- G216 (= G217) mutation to A: Decreases activity.
- T217 (= T218) mutation to A: Decreases activity.
- G219 (= G220) mutation to A: Decreases activity.
- K222 (= K223) mutation to A: Decreases activity.
- E361 (= E369) mutation to A: Loss of activity.
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)
31% identity, 97% coverage: 16:562/562 of query aligns to 35:573/590 of Q4WR83
Sites not aligning to the query:
- 6:14 PTS2-type peroxisomal targeting signal
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)
28% identity, 94% coverage: 29:559/562 of query aligns to 42:547/556 of Q9S725
- K211 (= K223) mutation to S: Drastically reduces the activity.
- M293 (≠ L312) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ N339) mutation K->L,A: Affects the substrate specificity.
- E401 (= E414) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C416) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R462) mutation to Q: Drastically reduces the activity.
- K457 (≠ S470) mutation to S: Drastically reduces the activity.
- K540 (= K552) 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)
29% identity, 99% coverage: 5:562/562 of query aligns to 17:540/546 of Q84P21
- K530 (= K552) mutation to N: Lossed enzymatic activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
30% identity, 97% coverage: 14:560/562 of query aligns to 14:527/528 of 3ni2A
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473), K519 (= K552)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: I231 (= I270), Y232 (= Y271), S236 (≠ A275), K299 (≠ N339), G301 (= G341), G302 (= G342), A303 (≠ T343), P304 (≠ A344), Q324 (≠ E363), G325 (= G364), Y326 (= Y365), G327 (= G366), M328 (≠ L367), T329 (= T368), P333 (= P372), V334 (= V373), D413 (= D447), I425 (= I459), R428 (= R462), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
30% identity, 97% coverage: 14:560/562 of query aligns to 14:527/528 of 3a9vA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473), K519 (= K552)
- binding adenosine monophosphate: H230 (= H269), G302 (= G342), A303 (≠ T343), P304 (≠ A344), G325 (= G364), Y326 (= Y365), G327 (= G366), M328 (≠ L367), T329 (= T368), D413 (= D447), I425 (= I459), R428 (= R462), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
30% identity, 93% coverage: 36:559/562 of query aligns to 29:525/528 of 5bsrA
- active site: S181 (≠ T215), S201 (≠ N235), H229 (= H269), T328 (= T368), E329 (= E369), K433 (≠ I468), Q438 (≠ N473), K518 (= K552)
- binding adenosine monophosphate: A301 (≠ G342), A302 (≠ T343), P303 (≠ A344), G324 (= G364), Y325 (= Y365), G326 (= G366), M327 (≠ L367), T328 (= T368), D412 (= D447), I424 (= I459), R427 (= R462), K429 (= K464), K433 (≠ I468), Q438 (≠ N473)
- binding coenzyme a: L102 (= L108), L225 (= L265), P226 (= P266), H229 (= H269), Y231 (= Y271), K252 (≠ P293), F253 (≠ R294), V273 (≠ L314), I276 (≠ L317), K435 (≠ S470), G436 (= G471), F437 (= F472), F498 (≠ A532)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
30% identity, 93% coverage: 36:559/562 of query aligns to 30:526/529 of 5bsvA
- active site: S182 (≠ T215), S202 (≠ N235), H230 (= H269), T329 (= T368), E330 (= E369), K434 (≠ I468), Q439 (≠ N473), K519 (= K552)
- binding 5'-O-[(R)-hydroxy{[(2E)-3-(5-methoxy-4-oxocyclohexa-1,5-dien-1-yl)prop-2-enoyl]oxy}phosphoryl]adenosine: H230 (= H269), Y232 (= Y271), S236 (≠ A275), S300 (= S340), G301 (= G341), A302 (≠ G342), A303 (≠ T343), P304 (≠ A344), Q324 (≠ E363), G325 (= G364), Y326 (= Y365), G327 (= G366), M328 (≠ L367), T329 (= T368), P333 (= P372), V334 (= V373), M337 (vs. gap), D413 (= D447), I425 (= I459), R428 (= R462), K430 (= K464), K434 (≠ I468), Q439 (≠ N473)
5bsuA Crystal structure of 4-coumarate:coa ligase complexed with caffeoyl adenylate (see paper)
30% identity, 93% coverage: 36:559/562 of query aligns to 30:526/529 of 5bsuA