SitesBLAST
Comparing AZOBR_RS31155 AZOBR_RS31155 AMP-dependent synthetase 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)
37% identity, 96% coverage: 14:559/567 of query aligns to 5:552/561 of P69451
- Y213 (= Y219) mutation to A: Loss of activity.
- T214 (= T220) mutation to A: 10% of wild-type activity.
- G216 (= G222) mutation to A: Decreases activity.
- T217 (= T223) mutation to A: Decreases activity.
- G219 (= G225) mutation to A: Decreases activity.
- K222 (= K228) mutation to A: Decreases activity.
- E361 (= E365) 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, 93% coverage: 32:556/567 of query aligns to 37:546/556 of Q9S725
- K211 (= K228) mutation to S: Drastically reduces the activity.
- M293 (≠ P308) mutation M->A,P: Affects the substrate specificity.
- K320 (≠ L335) mutation K->L,A: Affects the substrate specificity.
- E401 (= E412) mutation to Q: Slighlty reduces the substrate specificity.
- C403 (= C414) mutation to A: Significantly reduces the substrate specificity.
- R449 (= R459) mutation to Q: Drastically reduces the activity.
- K457 (≠ S467) mutation to S: Drastically reduces the activity.
- K540 (= K550) 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)
30% identity, 94% coverage: 27:557/567 of query aligns to 23:537/546 of Q84P21
- K530 (= K550) mutation to N: Lossed enzymatic activity.
3ni2A Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate:coa ligase (see paper)
33% identity, 93% coverage: 32:556/567 of query aligns to 19:525/528 of 3ni2A
- active site: S182 (≠ T220), S202 (≠ N240), H230 (= H266), T329 (≠ S364), E330 (= E365), K434 (≠ L465), Q439 (≠ N470), K519 (= K550)
- binding 5'-O-{(S)-hydroxy[3-(4-hydroxyphenyl)propoxy]phosphoryl}adenosine: I231 (≠ V267), Y232 (≠ F268), S236 (≠ V272), K299 (≠ L335), G301 (= G337), G302 (= G338), A303 (= A339), P304 (= P340), Q324 (≠ E359), G325 (= G360), Y326 (= Y361), G327 (= G362), M328 (≠ L363), T329 (≠ S364), P333 (= P368), V334 (= V369), D413 (= D444), I425 (= I456), R428 (= R459), K430 (= K461), K434 (≠ L465), Q439 (≠ N470)
3a9vA Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--coa ligase (see paper)
33% identity, 93% coverage: 32:556/567 of query aligns to 19:525/528 of 3a9vA
- active site: S182 (≠ T220), S202 (≠ N240), H230 (= H266), T329 (≠ S364), E330 (= E365), K434 (≠ L465), Q439 (≠ N470), K519 (= K550)
- binding adenosine monophosphate: H230 (= H266), G302 (= G338), A303 (= A339), P304 (= P340), G325 (= G360), Y326 (= Y361), G327 (= G362), M328 (≠ L363), T329 (≠ S364), D413 (= D444), I425 (= I456), R428 (= R459), K430 (= K461), K434 (≠ L465), Q439 (≠ N470)
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)
30% identity, 90% coverage: 45:556/567 of query aligns to 46:541/559 of Q67W82
- G395 (= G411) mutation to R: In ral1; reduced lignin content and increased accumulation of 4-coumarate and ferulate in roots; confers increased tolerance to aluminum.
4gxqA Crystal structure of atp bound rpmatb-bxbclm chimera b1 (see paper)
30% identity, 89% coverage: 54:556/567 of query aligns to 26:497/506 of 4gxqA
- active site: T163 (= T220), N183 (= N240), H207 (= H266), T303 (≠ S364), E304 (= E365), I403 (≠ L465), N408 (= N470), A491 (≠ K550)
- binding adenosine-5'-triphosphate: T163 (= T220), S164 (≠ G221), G165 (= G222), T166 (= T223), T167 (= T224), K171 (= K228), H207 (= H266), S277 (≠ G338), A278 (= A339), P279 (= P340), E298 (= E359), R299 (≠ G360), Y300 (= Y361), G301 (= G362), M302 (≠ L363), T303 (≠ S364), V322 (≠ I384), D382 (= D444), I394 (= I456), R397 (= R459)
- binding carbonate ion: H207 (= H266), T208 (≠ V267), H209 (≠ F268), S277 (≠ G338), R299 (≠ G360), G301 (= G362), M302 (≠ L363), M307 (≠ V369)
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, 93% coverage: 32:556/567 of query aligns to 26:532/542 of O24146
- S189 (≠ T220) binding
- S190 (≠ G221) binding
- G191 (= G222) binding
- T192 (= T223) binding
- T193 (= T224) binding ; mutation to A: Reduced activity against 4-coumarate.
- K197 (= K228) binding ; mutation to A: Reduced activity against 4-coumarate.
- H237 (= H266) mutation to A: Strongly reduced activity against 4-coumarate.
- Y239 (≠ F268) binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.; mutation to F: Reduced activity against 4-coumarate.
- S243 (≠ V272) binding ; binding ; binding
- K260 (≠ R289) binding
- A309 (≠ G338) binding ; binding ; binding
- Q331 (≠ E359) binding
- G332 (= G360) binding ; binding ; binding ; binding ; binding
- T336 (≠ S364) binding ; binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- V341 (= V369) mutation to G: Reduced activity against 4-coumarate.; mutation Missing: Reduced activity against 4-coumarate, but acquired ability to use sinapate as substrate.
- M344 (≠ A372) binding ; binding ; binding ; mutation to A: Reduced activity against 4-coumarate.
- D420 (= D444) binding ; binding ; binding ; binding ; binding
- R435 (= R459) binding ; binding ; binding ; binding ; mutation to A: Strongly reduced activity against 4-coumarate.
- K437 (= K461) binding ; binding ; binding ; binding
- K441 (≠ L465) binding ; binding ; binding ; binding ; mutation to A: Abolished activity against 4-coumarate.
- K443 (≠ S467) binding ; mutation to A: Normal activity against 4-coumarate.
- G444 (= G468) binding
- Q446 (≠ N470) binding
- K526 (= K550) binding ; mutation to A: Abolished activity against 4-coumarate.
5bsrA Crystal structure of 4-coumarate:coa ligase complexed with adenosine monophosphate and coenzyme a (see paper)
31% identity, 93% coverage: 32:556/567 of query aligns to 18:524/528 of 5bsrA