SitesBLAST
Comparing BPHYT_RS33355 FitnessBrowser__BFirm:BPHYT_RS33355 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)
7b2eA Quadruple mutant of oxalyl-coa decarboxylase from methylorubrum extorquens with bound tpp and adp (see paper)
72% identity, 94% coverage: 19:564/580 of query aligns to 2:547/548 of 7b2eA
- active site: V25 (≠ L42), G27 (= G44), I28 (= I45), P29 (= P46), I30 (= I47), E50 (= E67), V73 (= V90), Y114 (= Y131), G115 (≠ E132), A164 (= A181), L281 (= L298), G394 (= G410), G420 (= G436), M422 (= M438), I476 (≠ V492), R478 (= R494), G479 (= G495), T482 (≠ V498)
- binding adenosine-5'-diphosphate: C92 (= C109), R154 (= R171), G215 (= G232), K216 (= K233), G217 (= G234), M241 (= M258), G274 (= G291), R276 (= R293), D301 (= D317), I302 (= I318), D320 (= D336), I321 (= I337)
- binding magnesium ion: D446 (= D462), N473 (= N489), G475 (= G491)
- binding thiamine diphosphate: F371 (= F387), C395 (≠ A411), N396 (= N412), T397 (= T413), G420 (= G436), M422 (= M438), G445 (= G461), D446 (= D462), S447 (= S463), A448 (= A464), F451 (= F467), N473 (= N489), G475 (= G491), I476 (≠ V492), F477 (≠ Y493)
P40149 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Oxalobacter formigenes (see 2 papers)
61% identity, 98% coverage: 13:580/580 of query aligns to 2:568/568 of P40149
- E56 (= E67) mutation to A: Loss of the decarboxylase activity. The mutant forms a dimer and not a tetramer.
- Y120 (= Y131) mutation to A: 3-fold reduction in the affinity binding and strong reduction in the catalytic efficiency for oxalyl-CoA.; mutation to F: 2 and 12-fold reduction in the affinity binding and in the catalytic efficiency for oxalyl-CoA, respectively.
- E121 (= E132) mutation to A: 2-fold reduction in the affinity binding and strong reduction in the catalytic efficiency for oxalyl-CoA.; mutation to Q: Slight increase of the affinity binding and strong reduction in the catalytic efficiency for oxalyl-CoA.
- R160 (= R171) binding
- K222 (= K233) binding
- R282 (= R293) binding
- D306 (= D317) binding
- I326 (= I337) binding
- Y377 (≠ F387) binding
- D452 (= D462) binding
- N479 (= N489) binding
- G481 (= G491) binding
- Y483 (= Y493) binding ; mutation to A: Does not affect oxalyl-CoA binding, but it strongly reduces the catalytic efficiency for oxalyl-CoA.; mutation to F: 2-fold reduction in the affinity binding and strong reduction in the catalytic efficiency for oxalyl-CoA.
- S553 (= S565) mutation to A: Does not affect oxalyl-CoA binding, but it reduces 7-fold the catalytic efficiency for oxalyl-CoA.
- R555 (= R567) mutation to A: 3-fold reduction in the affinity binding for oxalyl-CoA, but it does not affect the catalytic efficiency.
2jibA X-ray structure of oxalyl-coa decarboxylase in complex with coenzyme- a (see paper)
62% identity, 96% coverage: 18:572/580 of query aligns to 1:554/559 of 2jibA
- active site: V25 (≠ L42), G27 (= G44), I28 (= I45), P29 (= P46), I30 (= I47), E50 (= E67), V73 (= V90), Y114 (= Y131), E115 (= E132), E116 (= E133), A164 (= A181), M281 (≠ L298), G394 (= G410), G420 (= G436), M422 (= M438), D446 (= D462), N473 (= N489), G475 (= G491), I476 (≠ V492), K478 (≠ R494), G479 (= G495), A482 (≠ V498), P541 (≠ E559)
- binding adenosine-5'-diphosphate: C92 (= C109), R154 (= R171), G215 (= G232), K216 (= K233), G217 (= G234), M241 (= M258), G274 (= G291), A275 (= A292), R276 (= R293), D300 (= D317), I301 (= I318), D319 (= D336), I320 (= I337)
- binding coenzyme a: A258 (= A275), R260 (= R277), A261 (≠ S278), L280 (= L297), N352 (= N370), K353 (≠ L371), L356 (≠ M374), L398 (= L414), R402 (= R418), M403 (≠ S419), R549 (= R567), I550 (≠ L568)
- binding magnesium ion: D446 (= D462), N473 (= N489), G475 (= G491)
- binding thiamine diphosphate: E50 (= E67), V73 (= V90), Y371 (≠ F387), A395 (= A411), N396 (= N412), A397 (≠ T413), M422 (= M438), G445 (= G461), D446 (= D462), S447 (= S463), A448 (= A464), F451 (= F467), N473 (= N489), G475 (= G491), I476 (≠ V492), Y477 (= Y493)
2ji8A X-ray structure of oxalyl-coa decarboxylase in complex with formyl- coa (see paper)
62% identity, 96% coverage: 18:572/580 of query aligns to 1:554/559 of 2ji8A
- active site: V25 (≠ L42), G27 (= G44), I28 (= I45), P29 (= P46), I30 (= I47), E50 (= E67), V73 (= V90), Y114 (= Y131), E115 (= E132), E116 (= E133), A164 (= A181), M281 (≠ L298), G394 (= G410), G420 (= G436), M422 (= M438), D446 (= D462), N473 (= N489), G475 (= G491), I476 (≠ V492), K478 (≠ R494), G479 (= G495), A482 (≠ V498), P541 (≠ E559)
- binding adenosine-5'-diphosphate: C92 (= C109), R154 (= R171), G215 (= G232), K216 (= K233), G217 (= G234), M241 (= M258), G274 (= G291), R276 (= R293), D300 (= D317), I301 (= I318), D319 (= D336), I320 (= I337)
- binding s-{(9r,13s,15r)-17-[(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-9,13,15-trihydroxy-10,10-dimethyl-13,15-dioxido-4,8-dioxo-12,14,16-trioxa-3,7-diaza-13,15-diphosphaheptadec-1-yl} thioformate : A257 (≠ S274), A258 (= A275), T259 (≠ A276), R260 (= R277), A261 (≠ S278), W279 (= W296), L280 (= L297), N352 (= N370), L356 (≠ M374), L398 (= L414), R402 (= R418), M403 (≠ S419), S547 (= S565), R549 (= R567), I550 (≠ L568)
- binding magnesium ion: D446 (= D462), N473 (= N489), G475 (= G491)
- binding thiamine diphosphate: Y371 (≠ F387), A395 (= A411), N396 (= N412), G420 (= G436), M422 (= M438), G445 (= G461), D446 (= D462), S447 (= S463), A448 (= A464), F451 (= F467), N473 (= N489), G475 (= G491), I476 (≠ V492), Y477 (= Y493)
2ji7A X-ray structure of oxalyl-coa decarboxylase with covalent reaction intermediate (see paper)
62% identity, 96% coverage: 18:572/580 of query aligns to 1:554/559 of 2ji7A
- active site: V25 (≠ L42), G27 (= G44), I28 (= I45), P29 (= P46), I30 (= I47), E50 (= E67), V73 (= V90), Y114 (= Y131), E115 (= E132), E116 (= E133), A164 (= A181), M281 (≠ L298), G394 (= G410), G420 (= G436), M422 (= M438), D446 (= D462), N473 (= N489), G475 (= G491), I476 (≠ V492), K478 (≠ R494), G479 (= G495), A482 (≠ V498), P541 (≠ E559)
- binding adenosine-5'-diphosphate: C92 (= C109), R154 (= R171), G215 (= G232), K216 (= K233), M241 (= M258), G274 (= G291), R276 (= R293), D300 (= D317), I301 (= I318), D319 (= D336), I320 (= I337)
- binding magnesium ion: D446 (= D462), N473 (= N489), G475 (= G491)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(1r,11r,15s,17r)-19-[(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-1,11,15,17-tetrahydroxy-12,12-dimethyl-15,17-dioxido-6,10-dioxo-14,16,18-trioxa-2-thia-5,9-diaza-15,17-diphosphanonadec-1-yl}-5-(2-{[(r)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: E50 (= E67), V73 (= V90), Y114 (= Y131), E115 (= E132), A257 (≠ S274), A258 (= A275), T259 (≠ A276), R260 (= R277), A261 (≠ S278), L280 (= L297), N352 (= N370), L356 (≠ M374), Y371 (≠ F387), G394 (= G410), A395 (= A411), N396 (= N412), A397 (≠ T413), L398 (= L414), R402 (= R418), M403 (≠ S419), G420 (= G436), M422 (= M438), G445 (= G461), D446 (= D462), S447 (= S463), A448 (= A464), F451 (= F467), N473 (= N489), G475 (= G491), Y477 (= Y493), R549 (= R567), I550 (≠ L568)
2ji6A X-ray structure of oxalyl-coa decarboxylase in complex with 3-deaza- thdp and oxalyl-coa (see paper)
62% identity, 96% coverage: 18:572/580 of query aligns to 1:554/559 of 2ji6A
- active site: V25 (≠ L42), G27 (= G44), I28 (= I45), P29 (= P46), I30 (= I47), E50 (= E67), V73 (= V90), Y114 (= Y131), E115 (= E132), E116 (= E133), A164 (= A181), M281 (≠ L298), G394 (= G410), G420 (= G436), M422 (= M438), D446 (= D462), N473 (= N489), G475 (= G491), I476 (≠ V492), K478 (≠ R494), G479 (= G495), A482 (≠ V498), P541 (≠ E559)
- binding adenosine-5'-diphosphate: C92 (= C109), R154 (= R171), G215 (= G232), K216 (= K233), G217 (= G234), M241 (= M258), G274 (= G291), A275 (= A292), R276 (= R293), D300 (= D317), I301 (= I318), D319 (= D336), I320 (= I337)
- binding magnesium ion: D446 (= D462), N473 (= N489), G475 (= G491)
- binding oxalyl-coenzyme a: G27 (= G44), I28 (= I45), Y114 (= Y131), A257 (≠ S274), A258 (= A275), T259 (≠ A276), R260 (= R277), A261 (≠ S278), L280 (= L297), N352 (= N370), K353 (≠ L371), L356 (≠ M374), L398 (= L414), R402 (= R418), M403 (≠ S419), M422 (= M438), Y477 (= Y493), S547 (= S565), R549 (= R567), I550 (≠ L568)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: V26 (= V43), E50 (= E67), P76 (= P93), Y371 (≠ F387), A395 (= A411), N396 (= N412), A397 (≠ T413), M422 (= M438), G445 (= G461), D446 (= D462), S447 (= S463), A448 (= A464), F451 (= F467), N473 (= N489), G475 (= G491), I476 (≠ V492), Y477 (= Y493)
2c31A Crystal structure of oxalyl-coa decarboxylase in complex with the cofactor derivative thiamin-2-thiazolone diphosphate and adenosine diphosphate (see paper)
62% identity, 94% coverage: 18:564/580 of query aligns to 1:546/546 of 2c31A
- active site: V25 (≠ L42), G27 (= G44), I28 (= I45), P29 (= P46), I30 (= I47), E50 (= E67), V73 (= V90), Y114 (= Y131), E115 (= E132), E116 (= E133), A164 (= A181), M281 (≠ L298), G394 (= G410), G420 (= G436), M422 (= M438), D446 (= D462), N473 (= N489), G475 (= G491), I476 (≠ V492), K478 (≠ R494), G479 (= G495), A482 (≠ V498), P541 (≠ E559)
- binding adenosine-5'-diphosphate: C92 (= C109), R154 (= R171), G215 (= G232), K216 (= K233), G217 (= G234), M241 (= M258), G274 (= G291), A275 (= A292), R276 (= R293), D300 (= D317), I301 (= I318), D319 (= D336), I320 (= I337)
- binding magnesium ion: D446 (= D462), N473 (= N489), G475 (= G491)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: V26 (= V43), E50 (= E67), Y371 (≠ F387), A395 (= A411), N396 (= N412), A397 (≠ T413), M422 (= M438), G445 (= G461), D446 (= D462), S447 (= S463), A448 (= A464), F451 (= F467), N473 (= N489), G475 (= G491), I476 (≠ V492), Y477 (= Y493)
P0AFI0 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Escherichia coli (strain K12) (see paper)
62% identity, 96% coverage: 19:577/580 of query aligns to 6:562/564 of P0AFI0
- R158 (= R171) binding
- K220 (= K233) binding
- R280 (= R293) binding
- D302 (= D317) binding
- I322 (= I337) binding
- Y372 (≠ F387) binding
- D447 (= D462) binding
- N474 (= N489) binding
- G476 (= G491) binding
- Y478 (= Y493) binding
2q28A Crystal structure of oxalyl-coa decarboxylase from escherichia coli in complex with adenosine-5`-diphosphate (see paper)
62% identity, 95% coverage: 19:569/580 of query aligns to 2:550/550 of 2q28A
- active site: V25 (≠ L42), G27 (= G44), I28 (= I45), P29 (= P46), V30 (≠ I47), E50 (= E67), V73 (= V90), Y114 (= Y131), E115 (= E132), E116 (= E133), A164 (= A181), L281 (= L298), G391 (= G410), G417 (= G436), M419 (= M438), D443 (= D462), N470 (= N489), G472 (= G491), I473 (≠ V492), R475 (= R494), G476 (= G495), V479 (= V498), P540 (≠ E559)
- binding adenosine-5'-diphosphate: R154 (= R171), G215 (= G232), K216 (= K233), G217 (= G234), M241 (= M258), G274 (= G291), R276 (= R293), D298 (= D317), I299 (= I318), D317 (= D336), I318 (= I337)
- binding magnesium ion: D443 (= D462), N470 (= N489), G472 (= G491)
- binding thiamine diphosphate: Y368 (≠ F387), G391 (= G410), A392 (= A411), N393 (= N412), T394 (= T413), M419 (= M438), G442 (= G461), D443 (= D462), S444 (= S463), A445 (= A464), F448 (= F467), N470 (= N489), G472 (= G491), I473 (≠ V492), Y474 (= Y493)
2q29A Crystal structure of oxalyl-coa decarboxylase from escherichia coli in complex with acetyl coenzyme a (see paper)
62% identity, 94% coverage: 19:565/580 of query aligns to 2:546/546 of 2q29A
- active site: V25 (≠ L42), G27 (= G44), I28 (= I45), P29 (= P46), V30 (≠ I47), E50 (= E67), V73 (= V90), Y114 (= Y131), E115 (= E132), E116 (= E133), A164 (= A181), L281 (= L298), G391 (= G410), G417 (= G436), M419 (= M438), D443 (= D462), N470 (= N489), G472 (= G491), I473 (≠ V492), R475 (= R494), G476 (= G495), V479 (= V498), P540 (≠ E559)
- binding acetyl coenzyme *a: A257 (≠ S274), A258 (= A275), R260 (= R277), S261 (= S278), N351 (= N370), M355 (= M374), N400 (≠ S419)
- binding magnesium ion: D443 (= D462), N470 (= N489), G472 (= G491)
- binding thiamine diphosphate: Y368 (≠ F387), A392 (= A411), N393 (= N412), T394 (= T413), M419 (= M438), G442 (= G461), D443 (= D462), S444 (= S463), A445 (= A464), F448 (= F467), N470 (= N489), G472 (= G491), I473 (≠ V492), Y474 (= Y493)
Q9UJ83 2-hydroxyacyl-CoA lyase 1; 2-hydroxyphytanoyl-CoA lyase; 2-HPCL; Phytanoyl-CoA 2-hydroxylase 2; EC 4.1.2.63 from Homo sapiens (Human) (see 2 papers)
40% identity, 95% coverage: 10:561/580 of query aligns to 3:563/578 of Q9UJ83
- D455 (= D462) mutation D->S,R: Does not affect subcellular localization. Abolishes lyase activity. Does not affect subcellular localization, abolishes lyase activity, does not affect oligomerisation and does not bind TTP; when associated with S-456.
- S456 (= S463) mutation to R: Does not affect subcellular localization. Abolishes lyase activity. Does not affect subcellular localization, abolishes lyase activity, does not affect oligomerisation and does not bind TTP; when associated with S-455.
Sites not aligning to the query:
- 576:578 Microbody targeting signal
6xn8A Crystal structure of 2-hydroxyacyl coa lyase (hacl) from rhodospirillales bacterium urhd0017
39% identity, 93% coverage: 18:559/580 of query aligns to 1:539/540 of 6xn8A
- active site: V25 (≠ L42), G27 (= G44), F28 (≠ I45), P29 (= P46), I30 (= I47), E50 (= E67), V73 (= V90), F112 (≠ Y131), Q113 (≠ E132), E114 (= E133), D162 (≠ A181), F277 (≠ L298), G388 (= G410), G414 (= G436), M416 (= M438), D441 (= D462), N468 (= N489), G470 (= G491), I471 (≠ V492), P473 (≠ R494), G474 (= G495), E477 (≠ V498)
- binding adenosine-5'-diphosphate: R152 (= R171), G211 (= G232), K212 (= K233), S237 (≠ M258), G270 (= G291), R272 (= R293), D295 (= D317), I296 (= I318), G313 (= G335), D314 (= D336), G315 (≠ I337)
- binding magnesium ion: D441 (= D462), N468 (= N489), G470 (= G491)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: E50 (= E67), V73 (= V90), P76 (= P93), H80 (≠ N97), Y367 (≠ F387), A389 (= A411), G390 (≠ N412), T391 (= T413), G414 (= G436), M416 (= M438), G440 (= G461), D441 (= D462), S442 (= S463), A443 (= A464), F446 (= F467), N468 (= N489), G470 (= G491), I471 (≠ V492), G472 (≠ Y493)
P39994 Putative 2-hydroxyacyl-CoA lyase; Peroxisomal protein 1; EC 4.1.-.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
34% identity, 90% coverage: 36:558/580 of query aligns to 18:543/560 of P39994
Sites not aligning to the query:
- 558:560 Peroxisomal target signal 1 (PTS1)
4qq8C Crystal structure of the formolase fls in space group p 43 21 2 (see paper)
29% identity, 92% coverage: 23:557/580 of query aligns to 5:543/569 of 4qq8C
- active site: L24 (= L42), G26 (= G44), I27 (= I45), H28 (≠ P46), I29 (= I47), E49 (= E67), T72 (≠ V90), L111 (= L126), Q112 (= Q127), A113 (≠ Q128), G114 (= G129), W162 (≠ A181), L255 (vs. gap), T283 (≠ L298), G392 (= G410), N418 (≠ G436), M420 (= M438), D447 (= D462), N474 (= N489), S476 (≠ G491), W477 (≠ V492), W479 (vs. gap), T480 (vs. gap), F483 (≠ Y493)
- binding magnesium ion: D447 (= D462), N474 (= N489), S476 (≠ G491)
- binding thiamine diphosphate: H25 (≠ V43), E49 (= E67), Q112 (= Q127), G392 (= G410), G393 (≠ A411), L394 (≠ N412), T395 (= T413), N418 (≠ G436), M420 (= M438), G446 (= G461), D447 (= D462), G448 (≠ S463), S449 (≠ A464), Y452 (≠ F467), N474 (= N489), S476 (≠ G491), W477 (≠ V492), G478 (vs. gap), W479 (vs. gap), T480 (vs. gap)
Sites not aligning to the query:
3d7kA Crystal structure of benzaldehyde lyase in complex with the inhibitor mbp (see paper)
29% identity, 92% coverage: 23:557/580 of query aligns to 5:543/554 of 3d7kA
- active site: L24 (= L42), G26 (= G44), A27 (≠ I45), H28 (≠ P46), I29 (= I47), E49 (= E67), T72 (≠ V90), L111 (= L126), Q112 (= Q127), A113 (≠ Q128), G114 (= G129), W162 (≠ A181), L255 (vs. gap), T283 (≠ L298), G392 (= G410), G418 (= G436), M420 (= M438), D447 (= D462), N474 (= N489), S476 (≠ G491), W477 (≠ V492), A479 (vs. gap), T480 (vs. gap), F483 (≠ Y493)
- binding calcium ion: D447 (= D462), N474 (= N489), S476 (≠ G491)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(S)-hydroxy[(R)-hydroxy(methoxy)phosphoryl]phenylmethyl}-5-(2-{[(R)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: H25 (≠ V43), G26 (= G44), A27 (≠ I45), E49 (= E67), T72 (≠ V90), Q112 (= Q127), G392 (= G410), A393 (= A411), L394 (≠ N412), T395 (= T413), G418 (= G436), M420 (= M438), G446 (= G461), D447 (= D462), G448 (≠ S463), S449 (≠ A464), Y452 (≠ F467), N474 (= N489), S476 (≠ G491), W477 (≠ V492), G478 (vs. gap), A479 (vs. gap), T480 (vs. gap)
Sites not aligning to the query:
7pt1A Actinobacterial 2-hydroxyacyl-coa lyase (achacl) structure in complex with substrate 2-hib-coa and inactive cofactor 3-deaza-thdp (see paper)
26% identity, 95% coverage: 26:578/580 of query aligns to 10:561/574 of 7pt1A
- binding S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} 2-hydroxy-2-methylpropanethioate: L113 (≠ Y131), Q114 (≠ E132), G256 (≠ S274), S257 (≠ A275), R259 (= R277), S260 (= S278), Q279 (≠ L297), Y352 (≠ W359), R403 (= R418), L404 (≠ I421), G419 (= G436), D547 (≠ E564), L552 (≠ T569)
- binding magnesium ion: D446 (= D462), N473 (= N489), A475 (≠ G491)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: E51 (= E67), T74 (≠ V90), P77 (= P93), G396 (≠ A411), D397 (≠ N412), L398 (≠ T413), G419 (= G436), L421 (≠ M438), G445 (= G461), D446 (= D462), G447 (≠ S463), A448 (= A464), N473 (= N489), A475 (≠ G491), W476 (vs. gap), N477 (vs. gap), I478 (≠ V492), E479 (≠ Y493)
P0DUV9 2-hydroxyacyl-CoA lyase; AcHACL; HACL; 2-hydroxyisobutyryl-CoA lyase; EC 4.1.-.- from Actinomycetospora chiangmaiensis (strain DSM 45062 / JCM 15998 / CCTCC AA 205017 / NBRC 104400 / YIM 0006) (see paper)
26% identity, 99% coverage: 4:578/580 of query aligns to 2:575/590 of P0DUV9
- G43 (≠ I45) binding
- Q255 (≠ S259) binding
- RS 273:274 (= RS 277:278) binding
- R362 (≠ P355) binding
- GDL 410:412 (≠ ANT 411:413) binding
- R417 (= R418) binding
- G433 (= G436) binding
- D460 (= D462) binding
- GA 461:462 (≠ SA 463:464) binding
- N487 (= N489) binding
- NRAWNI 487:492 (≠ NNG--V 489:492) binding
- A489 (≠ G491) binding
- E493 (≠ Y493) mutation to A: 10-fold decrease of 2-HIB-CoA cleavage rate, 6-fold increase in KM.; mutation to K: No cleavage of 2-HIB-CoA.; mutation to Q: 50-fold decrease of 2-HIB-CoA cleavage rate, 1.5-fold increase in KM.
- DSGK 561:564 (≠ ESGR 564:567) binding
Sites not aligning to the query:
7pt4A Actinobacterial 2-hydroxyacyl-coa lyase (achacl) structure in complex with a covalently bound reaction intermediate as well as products formyl-coa and acetone (see paper)
26% identity, 95% coverage: 26:578/580 of query aligns to 10:561/580 of 7pt4A
- binding s-{(9r,13s,15r)-17-[(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-9,13,15-trihydroxy-10,10-dimethyl-13,15-dioxido-4,8-dioxo-12,14,16-trioxa-3,7-diaza-13,15-diphosphaheptadec-1-yl} thioformate : Q241 (≠ S259), G256 (≠ S274), S257 (≠ A275), R259 (= R277), S260 (= S278), Y278 (≠ W296), Q279 (≠ L297), Y352 (≠ W359), R403 (= R418), L404 (≠ I421), L552 (≠ T569)
- binding magnesium ion: D446 (= D462), N473 (= N489), A475 (≠ G491)
- binding thiamine diphosphate: G396 (≠ A411), D397 (≠ N412), L398 (≠ T413), G419 (= G436), L421 (≠ M438), G445 (= G461), D446 (= D462), G447 (≠ S463), A448 (= A464), N473 (= N489), A475 (≠ G491), W476 (vs. gap), N477 (vs. gap), I478 (≠ V492), E479 (≠ Y493)
7pt4B Actinobacterial 2-hydroxyacyl-coa lyase (achacl) structure in complex with a covalently bound reaction intermediate as well as products formyl-coa and acetone (see paper)
26% identity, 95% coverage: 26:578/580 of query aligns to 10:561/584 of 7pt4B
- binding magnesium ion: D446 (= D462), N473 (= N489), A475 (≠ G491)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(1r,11r,15s,17r)-19-[(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-1,11,15,17-tetrahydroxy-12,12-dimethyl-15,17-dioxido-6,10-dioxo-14,16,18-trioxa-2-thia-5,9-diaza-15,17-diphosphanonadec-1-yl}-5-(2-{[(r)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: S257 (≠ A275), R259 (= R277), S260 (= S278), Q279 (≠ L297), Y352 (≠ W359), G395 (= G410), G396 (≠ A411), D397 (≠ N412), L398 (≠ T413), L399 (= L414), R403 (= R418), L404 (≠ I421), G419 (= G436), L421 (≠ M438), G445 (= G461), D446 (= D462), G447 (≠ S463), A448 (= A464), N473 (= N489), A475 (≠ G491), W476 (vs. gap), N477 (vs. gap), I478 (≠ V492), E479 (≠ Y493), D547 (≠ E564), L561 (≠ M578)
6lpiB Crystal structure of ahas holo-enzyme (see paper)
27% identity, 81% coverage: 23:492/580 of query aligns to 8:458/539 of 6lpiB
- active site: I27 (≠ L42), G29 (= G44), G30 (vs. gap), S31 (vs. gap), I32 (vs. gap), E53 (= E67), C76 (≠ V90), F115 (≠ Y131), Q116 (≠ E132), E117 (= E133), K165 (= K192), M256 (vs. gap), A283 (≠ G301), V375 (≠ E409), G401 (= G436), M403 (= M438), D428 (= D462), N455 (= N489), A457 (≠ G491), L458 (≠ V492)
- binding flavin-adenine dinucleotide: R155 (= R171), G212 (= G232), G213 (≠ K233), G214 (= G234), T236 (≠ M258), L237 (≠ S259), M238 (= M260), L254 (vs. gap), M256 (vs. gap), H257 (vs. gap), G276 (= G291), A277 (= A292), R278 (= R293), D280 (≠ N295), R282 (≠ H300), A283 (≠ G301), D300 (= D317), I301 (= I318), D319 (= D336), V320 (≠ I337), M380 (≠ L414), G398 (= G433)
- binding magnesium ion: D428 (= D462), N455 (= N489)
- binding thiamine diphosphate: E53 (= E67), C76 (≠ V90), P79 (= P93), G376 (= G410), Q377 (≠ A411), H378 (≠ N412), G401 (= G436), M403 (= M438), G427 (= G461), D428 (= D462), G429 (≠ S463), S430 (≠ A464), M433 (≠ F467), N455 (= N489), A457 (≠ G491), L458 (≠ V492)
Sites not aligning to the query:
Query Sequence
>BPHYT_RS33355 FitnessBrowser__BFirm:BPHYT_RS33355
MAEADQPTTDNTSTQQATETTDGFHLVIDALKLNDIKTIFGLVGIPITDLARLAQAEGMR
FIGFRHEQHAGNAAAVSGYMTKKPGICLTVSAPGFLNGLTALANATTNCFPMILISGSSE
REIVDLQQGDYEEMDQLNAAKPYAKAAYRVLHAEDIGIGVARAIRAAVSGRPGGVYLDLP
AKLLAQTMDAVKAQQSLVRVVDAAPRQLPAPESVKRAIDVLKSAKRPLILLGKGAAYAQA
DAEIRGFVEQSGIPYLPMSMAKGLLPDTHEQSASAARSFVLQEADVVVLIGARLNWLLSH
GKGKTWGAEPKKFVQIDISPTEIDSNVAIAAPVIGDIGSCVAALREGLDASYKKPGTEWT
GAIAERKNKNLAKMAATLDKNPSPMNFHSALRAIRDVLKTRPDINVVNEGANTLDYARSI
IDMYEPRKRFDSGTWGIMGIGMGFAIGAAVTSGKPVVAIEGDSAFGFSGMELETICRYDL
PVCTIVFNNNGVYRGTDVNPTGGKDVAPTVFVKNARYDKMIEAFGGIGYHATTPEELTKA
LLESIASGKPSLINAVIDEAAGTESGRLTNLNPQSAAMKK
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory