SitesBLAST
Comparing H281DRAFT_06226 FitnessBrowser__Burk376:H281DRAFT_06226 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)
57% identity, 99% coverage: 1:554/557 of query aligns to 1:551/561 of P69451
- Y213 (= Y211) mutation to A: Loss of activity.
- T214 (= T212) mutation to A: 10% of wild-type activity.
- G216 (= G214) mutation to A: Decreases activity.
- T217 (= T215) mutation to A: Decreases activity.
- G219 (= G217) mutation to A: Decreases activity.
- K222 (= K220) mutation to A: Decreases activity.
- E361 (= E363) 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)
29% identity, 94% coverage: 31:553/557 of query aligns to 44:547/556 of Q9S725
- K211 (= K220) mutation to S: Drastically reduces the activity.
- M293 (≠ P306) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ N333) mutation K->L,A: Affects the substrate specificity.
- E401 (= E408) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C410) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R456) mutation to Q: Drastically reduces the activity.
- K457 (≠ S464) mutation to S: Drastically reduces the activity.
- K540 (= K546) mutation to N: Abolishes the activity.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
31% identity, 92% coverage: 44:554/557 of query aligns to 24:499/506 of 4gxqA
- active site: T163 (= T212), N183 (= N232), H207 (= H263), T303 (≠ S362), E304 (= E363), I403 (≠ L462), N408 (= N467), A491 (≠ K546)
- binding adenosine-5'-triphosphate: T163 (= T212), S164 (≠ G213), G165 (= G214), T166 (= T215), T167 (= T216), K171 (= K220), H207 (= H263), S277 (≠ G336), A278 (≠ M337), P279 (≠ A338), E298 (= E357), R299 (≠ G358), Y300 (= Y359), G301 (= G360), M302 (≠ L361), T303 (≠ S362), V322 (≠ I382), D382 (= D441), I394 (= I453), R397 (= R456)
- binding carbonate ion: H207 (= H263), T208 (≠ V264), H209 (≠ F265), S277 (≠ G336), R299 (≠ G358), G301 (= G360), M302 (≠ L361), M307 (≠ C367)
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)
29% identity, 91% coverage: 46:553/557 of query aligns to 57:542/559 of Q67W82
- G395 (= G407) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
27% identity, 94% coverage: 31:554/557 of query aligns to 26:527/528 of 3ni2A
- active site: S182 (≠ T212), S202 (≠ N232), H230 (= H263), T329 (≠ S362), E330 (= E363), K434 (≠ L462), Q439 (≠ N467), K519 (= K546)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: I231 (≠ V264), Y232 (≠ F265), S236 (≠ V269), K299 (≠ N333), G301 (= G335), G302 (= G336), A303 (≠ M337), P304 (≠ A338), Q324 (≠ E357), G325 (= G358), Y326 (= Y359), G327 (= G360), M328 (≠ L361), T329 (≠ S362), P333 (= P366), V334 (vs. gap), D413 (= D441), I425 (= I453), R428 (= R456), K430 (= K458), K434 (≠ L462), Q439 (≠ N467)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
27% identity, 94% coverage: 31:554/557 of query aligns to 26:527/528 of 3a9vA
- active site: S182 (≠ T212), S202 (≠ N232), H230 (= H263), T329 (≠ S362), E330 (= E363), K434 (≠ L462), Q439 (≠ N467), K519 (= K546)
- binding adenosine monophosphate: H230 (= H263), G302 (= G336), A303 (≠ M337), P304 (≠ A338), G325 (= G358), Y326 (= Y359), G327 (= G360), M328 (≠ L361), T329 (≠ S362), D413 (= D441), I425 (= I453), R428 (= R456), K430 (= K458), K434 (≠ L462), Q439 (≠ N467)
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
29% identity, 94% coverage: 31:553/557 of query aligns to 25:525/528 of 5bsrA
- active site: S181 (≠ T212), S201 (≠ N232), H229 (= H263), T328 (≠ S362), E329 (= E363), K433 (≠ L462), Q438 (≠ N467), K518 (= K546)
- binding adenosine monophosphate: A301 (vs. gap), A302 (vs. gap), P303 (vs. gap), G324 (= G358), Y325 (= Y359), G326 (= G360), M327 (≠ L361), T328 (≠ S362), D412 (= D441), I424 (= I453), R427 (= R456), K429 (= K458), K433 (≠ L462), Q438 (≠ N467)
- binding coenzyme a: L102 (= L106), L225 (= L259), P226 (= P260), H229 (= H263), Y231 (≠ F265), K252 (≠ P287), F253 (≠ R288), V273 (= V308), I276 (≠ L311), K435 (≠ S464), G436 (= G465), F437 (= F466), F498 (≠ G526)
5bsmA Crystal structure of 4-coumarate:coa ligase complexed with magnesium and adenosine triphosphate (see paper)
29% identity, 94% coverage: 31:553/557 of query aligns to 26:526/530 of 5bsmA
- active site: S182 (≠ T212), S202 (≠ N232), H230 (= H263), T329 (≠ S362), E330 (= E363), K434 (≠ L462), Q439 (≠ N467), K519 (= K546)
- binding adenosine-5'-triphosphate: S182 (≠ T212), S183 (≠ G213), G184 (= G214), T185 (= T215), T186 (= T216), K190 (= K220), H230 (= H263), A302 (vs. gap), A303 (vs. gap), P304 (vs. gap), Q324 (≠ E357), G325 (= G358), Y326 (= Y359), G327 (= G360), M328 (≠ L361), T329 (≠ S362), D413 (= D441), I425 (= I453), R428 (= R456), K519 (= K546)
5bsvA Crystal structure of 4-coumarate:coa ligase complexed with feruloyl adenylate (see paper)
29% identity, 94% coverage: 31:553/557 of query aligns to 26:526/529 of 5bsvA