SitesBLAST
Comparing WP_013420232.1 NCBI__GCF_000166055.1:WP_013420232.1 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)
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)
33% identity, 95% coverage: 20:589/603 of query aligns to 8:551/590 of P0DUV9
- G43 (= G55) binding 2-hydroxyisobutanoyl-CoA
- Q255 (≠ G299) binding 2-hydroxyisobutanoyl-CoA
- RS 273:274 (≠ RR 317:318) binding 2-hydroxyisobutanoyl-CoA
- R362 (= R403) binding 2-hydroxyisobutanoyl-CoA
- GDL 410:412 (≠ GDF 442:444) binding thiamine diphosphate
- R417 (≠ S449) binding 2-hydroxyisobutanoyl-CoA
- G433 (= G467) binding thiamine diphosphate
- D460 (= D494) binding Mg(2+)
- GA 461:462 (= GA 495:496) binding thiamine diphosphate
- N487 (≠ D521) binding Mg(2+)
- NRAWNI 487:492 (≠ DAGWTQ 521:526) binding thiamine diphosphate
- A489 (≠ G523) binding Mg(2+)
- E493 (≠ I527) 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.
Sites not aligning to the query:
- 561:564 binding 2-hydroxyisobutanoyl-CoA
- 566:590 C-terminal lid
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)
33% identity, 92% coverage: 36:589/603 of query aligns to 10:537/584 of 7pt4B
- binding magnesium ion: D446 (= D494), N473 (≠ D521), A475 (≠ G523)
- 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 (≠ H315), R259 (= R317), S260 (≠ R318), Q279 (≠ R337), Y352 (≠ I407), G395 (= G441), G396 (= G442), D397 (= D443), L398 (≠ F444), L399 (≠ V445), R403 (≠ S449), L404 (≠ Y450), G419 (= G467), L421 (= L469), G445 (= G493), D446 (= D494), G447 (= G495), A448 (= A496), N473 (≠ D521), A475 (≠ G523), W476 (= W524), N477 (≠ T525), I478 (≠ Q526), E479 (≠ I527)
Sites not aligning to the query:
- 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: 547, 561
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)
33% identity, 92% coverage: 36:589/603 of query aligns to 10:537/580 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 (≠ G299), G256 (≠ R314), S257 (≠ H315), R259 (= R317), S260 (≠ R318), Y278 (≠ F336), Q279 (≠ R337), Y352 (≠ I407), R403 (≠ S449), L404 (≠ Y450)
- binding magnesium ion: D446 (= D494), N473 (≠ D521), A475 (≠ G523)
- binding thiamine diphosphate: G396 (= G442), D397 (= D443), L398 (≠ F444), G419 (= G467), L421 (= L469), G445 (= G493), D446 (= D494), G447 (= G495), A448 (= A496), N473 (≠ D521), A475 (≠ G523), W476 (= W524), N477 (≠ T525), I478 (≠ Q526), E479 (≠ I527)
Sites not aligning to the query:
- 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 : 552
7pt1A Actinobacterial 2-hydroxyacyl-coa lyase (achacl) structure in complex with substrate 2-hib-coa and inactive cofactor 3-deaza-thdp (see paper)
33% identity, 92% coverage: 36:589/603 of query aligns to 10:537/574 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 (= L139), Q114 (= Q140), G256 (≠ R314), S257 (≠ H315), R259 (= R317), S260 (≠ R318), Q279 (≠ R337), Y352 (≠ I407), R403 (≠ S449), L404 (≠ Y450), G419 (= G467)
- binding magnesium ion: D446 (= D494), N473 (≠ D521), A475 (≠ G523)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: E51 (= E77), T74 (= T100), P77 (= P103), G396 (= G442), D397 (= D443), L398 (≠ F444), G419 (= G467), L421 (= L469), G445 (= G493), D446 (= D494), G447 (= G495), A448 (= A496), N473 (≠ D521), A475 (≠ G523), W476 (= W524), N477 (≠ T525), I478 (≠ Q526), E479 (≠ I527)
Sites not aligning to the query:
- 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: 547, 552
6xn8A Crystal structure of 2-hydroxyacyl coa lyase (hacl) from rhodospirillales bacterium urhd0017
29% identity, 93% coverage: 36:593/603 of query aligns to 9:539/540 of 6xn8A
- active site: V25 (≠ L52), G27 (= G54), F28 (≠ G55), P29 (≠ H56), I30 (= I57), E50 (= E77), V73 (≠ T100), F112 (≠ L139), Q113 (= Q140), E114 (≠ D141), D162 (≠ I189), F277 (≠ L338), G388 (= G441), G414 (= G467), M416 (≠ L469), D441 (= D494), N468 (≠ D521), G470 (= G523), I471 (≠ W524), P473 (≠ Q526), G474 (≠ I527), E477 (= E530)
- binding adenosine-5'-diphosphate: R152 (≠ V179), G211 (= G271), K212 (≠ S272), S237 (= S298), G270 (= G331), R272 (≠ P333), D295 (≠ N354), I296 (≠ R355), G313 (= G372), D314 (= D373), G315 (≠ A374)
- binding magnesium ion: D441 (= D494), N468 (≠ D521), G470 (= G523)
- 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 (= E77), V73 (≠ T100), P76 (= P103), H80 (≠ N107), Y367 (≠ F423), A389 (≠ G442), G390 (≠ D443), T391 (≠ F444), G414 (= G467), M416 (≠ L469), G440 (= G493), D441 (= D494), S442 (≠ G495), A443 (= A496), F446 (≠ Y499), N468 (≠ D521), G470 (= G523), I471 (≠ W524), G472 (≠ T525)
3d7kA Crystal structure of benzaldehyde lyase in complex with the inhibitor mbp (see paper)
30% identity, 92% coverage: 34:589/603 of query aligns to 6:541/554 of 3d7kA
- active site: L24 (= L52), G26 (= G54), A27 (≠ G55), H28 (= H56), I29 (= I57), E49 (= E77), T72 (= T100), L111 (vs. gap), Q112 (vs. gap), A113 (vs. gap), G114 (vs. gap), W162 (≠ I189), L255 (≠ P310), T283 (≠ L338), G392 (= G441), G418 (= G467), M420 (≠ L469), D447 (= D494), N474 (≠ D521), S476 (≠ G523), W477 (= W524), A479 (≠ Q526), T480 (≠ I527), F483 (≠ E530)
- binding calcium ion: D447 (= D494), N474 (≠ D521), S476 (≠ G523)
- 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 (≠ C53), G26 (= G54), A27 (≠ G55), E49 (= E77), T72 (= T100), Q112 (vs. gap), G392 (= G441), A393 (≠ G442), L394 (≠ D443), T395 (≠ F444), G418 (= G467), M420 (≠ L469), G446 (= G493), D447 (= D494), G448 (= G495), S449 (≠ A496), Y452 (= Y499), N474 (≠ D521), S476 (≠ G523), W477 (= W524), G478 (≠ T525), A479 (≠ Q526), T480 (≠ I527)
Sites not aligning to the query:
4qq8C Crystal structure of the formolase fls in space group p 43 21 2 (see paper)
30% identity, 92% coverage: 34:589/603 of query aligns to 6:541/569 of 4qq8C
- active site: L24 (= L52), G26 (= G54), I27 (≠ G55), H28 (= H56), I29 (= I57), E49 (= E77), T72 (= T100), L111 (vs. gap), Q112 (vs. gap), A113 (vs. gap), G114 (vs. gap), W162 (≠ I189), L255 (≠ P310), T283 (≠ L338), G392 (= G441), N418 (≠ G467), M420 (≠ L469), D447 (= D494), N474 (≠ D521), S476 (≠ G523), W477 (= W524), W479 (≠ Q526), T480 (≠ I527), F483 (≠ E530)
- binding magnesium ion: D447 (= D494), N474 (≠ D521), S476 (≠ G523)
- binding thiamine diphosphate: H25 (≠ C53), E49 (= E77), Q112 (vs. gap), G392 (= G441), G393 (= G442), L394 (≠ D443), T395 (≠ F444), N418 (≠ G467), M420 (≠ L469), G446 (= G493), D447 (= D494), G448 (= G495), S449 (≠ A496), Y452 (= Y499), N474 (≠ D521), S476 (≠ G523), W477 (= W524), G478 (≠ T525), W479 (≠ Q526), T480 (≠ I527)
Sites not aligning to the query:
7b2eA Quadruple mutant of oxalyl-coa decarboxylase from methylorubrum extorquens with bound tpp and adp (see paper)
28% identity, 94% coverage: 36:599/603 of query aligns to 9:548/548 of 7b2eA
- active site: V25 (≠ L52), G27 (= G54), I28 (≠ G55), P29 (≠ H56), I30 (= I57), E50 (= E77), V73 (≠ T100), Y114 (≠ L139), G115 (≠ Q140), A164 (≠ I189), L281 (= L338), G394 (= G441), G420 (= G467), M422 (≠ L469), I476 (= I527), R478 (= R529), G479 (≠ E530), T482 (vs. gap)
- binding adenosine-5'-diphosphate: C92 (≠ Q119), R154 (≠ V179), G215 (= G271), K216 (≠ S272), G217 (≠ Q273), M241 (≠ S298), G274 (= G331), R276 (≠ P333), D301 (≠ N354), I302 (≠ R355), D320 (= D373), I321 (≠ A374)
- binding magnesium ion: D446 (= D494), N473 (≠ D521), G475 (= G523)
- binding thiamine diphosphate: F371 (= F423), C395 (≠ G442), N396 (≠ D443), T397 (≠ F444), G420 (= G467), M422 (≠ L469), G445 (= G493), D446 (= D494), S447 (≠ G495), A448 (= A496), F451 (≠ Y499), N473 (≠ D521), G475 (= G523), I476 (= I527), F477 (≠ A528)
2c31A Crystal structure of oxalyl-coa decarboxylase in complex with the cofactor derivative thiamin-2-thiazolone diphosphate and adenosine diphosphate (see paper)
26% identity, 92% coverage: 36:592/603 of query aligns to 9:540/546 of 2c31A
- active site: V25 (≠ L52), G27 (= G54), I28 (≠ G55), P29 (≠ H56), I30 (= I57), E50 (= E77), V73 (≠ T100), Y114 (≠ L139), E115 (≠ Q140), E116 (≠ D141), A164 (≠ I189), M281 (≠ L338), G394 (= G441), G420 (= G467), M422 (≠ L469), D446 (= D494), N473 (≠ D521), G475 (= G523), I476 (≠ W524), K478 (≠ Q526), G479 (≠ A528), A482 (≠ Q531)
- binding adenosine-5'-diphosphate: C92 (≠ Q119), R154 (≠ V179), G215 (= G271), K216 (≠ S272), G217 (≠ Q273), M241 (≠ S298), G274 (= G331), A275 (≠ V332), R276 (≠ P333), D300 (vs. gap), I301 (= I351), D319 (= D373), I320 (vs. gap)
- binding magnesium ion: D446 (= D494), N473 (≠ D521), G475 (= G523)
- 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 (≠ C53), E50 (= E77), Y371 (≠ H417), A395 (≠ G442), N396 (≠ D443), A397 (≠ F444), M422 (≠ L469), G445 (= G493), D446 (= D494), S447 (≠ G495), A448 (= A496), F451 (≠ Y499), N473 (≠ D521), G475 (= G523), I476 (≠ W524), Y477 (≠ T525)
Sites not aligning to the query:
P40149 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Oxalobacter formigenes (see 2 papers)
26% identity, 92% coverage: 36:592/603 of query aligns to 15:546/568 of P40149
- E56 (= E77) mutation to A: Loss of the decarboxylase activity. The mutant forms a dimer and not a tetramer.
- Y120 (≠ L139) 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 (≠ Q140) 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 (≠ V179) binding ADP
- K222 (≠ S272) binding ADP
- R282 (≠ P333) binding ADP
- D306 (vs. gap) binding ADP
- I326 (vs. gap) binding ADP
- Y377 (≠ H417) binding thiamine diphosphate
- D452 (= D494) binding Mg(2+)
- N479 (≠ D521) binding Mg(2+)
- G481 (= G523) binding Mg(2+)
- Y483 (≠ T525) binding thiamine diphosphate; 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.
Sites not aligning to the query:
- 553 S→A: Does not affect oxalyl-CoA binding, but it reduces 7-fold the catalytic efficiency for oxalyl-CoA.
- 555 R→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)
26% identity, 92% coverage: 36:592/603 of query aligns to 9:540/559 of 2jibA
- active site: V25 (≠ L52), G27 (= G54), I28 (≠ G55), P29 (≠ H56), I30 (= I57), E50 (= E77), V73 (≠ T100), Y114 (≠ L139), E115 (≠ Q140), E116 (≠ D141), A164 (≠ I189), M281 (≠ L338), G394 (= G441), G420 (= G467), M422 (≠ L469), D446 (= D494), N473 (≠ D521), G475 (= G523), I476 (≠ W524), K478 (≠ Q526), G479 (≠ A528), A482 (≠ Q531)
- binding adenosine-5'-diphosphate: C92 (≠ Q119), R154 (≠ V179), G215 (= G271), K216 (≠ S272), G217 (≠ Q273), M241 (≠ S298), G274 (= G331), A275 (≠ V332), R276 (≠ P333), D300 (vs. gap), I301 (= I351), D319 (= D373), I320 (vs. gap)
- binding coenzyme a: A258 (≠ H315), R260 (= R317), A261 (≠ R318), L280 (≠ R337), N352 (≠ R403), K353 (≠ E404), L356 (≠ I407), L398 (≠ V445), R402 (≠ S449), M403 (≠ Y450)
- binding magnesium ion: D446 (= D494), N473 (≠ D521), G475 (= G523)
- binding thiamine diphosphate: E50 (= E77), V73 (≠ T100), Y371 (≠ H417), A395 (≠ G442), N396 (≠ D443), A397 (≠ F444), M422 (≠ L469), G445 (= G493), D446 (= D494), S447 (≠ G495), A448 (= A496), F451 (≠ Y499), N473 (≠ D521), G475 (= G523), I476 (≠ W524), Y477 (≠ T525)
Sites not aligning to the query:
2ji8A X-ray structure of oxalyl-coa decarboxylase in complex with formyl- coa (see paper)
26% identity, 92% coverage: 36:592/603 of query aligns to 9:540/559 of 2ji8A
- active site: V25 (≠ L52), G27 (= G54), I28 (≠ G55), P29 (≠ H56), I30 (= I57), E50 (= E77), V73 (≠ T100), Y114 (≠ L139), E115 (≠ Q140), E116 (≠ D141), A164 (≠ I189), M281 (≠ L338), G394 (= G441), G420 (= G467), M422 (≠ L469), D446 (= D494), N473 (≠ D521), G475 (= G523), I476 (≠ W524), K478 (≠ Q526), G479 (≠ A528), A482 (≠ Q531)
- binding adenosine-5'-diphosphate: C92 (≠ Q119), R154 (≠ V179), G215 (= G271), K216 (≠ S272), G217 (≠ Q273), M241 (≠ S298), G274 (= G331), R276 (≠ P333), D300 (vs. gap), I301 (= I351), D319 (= D373), I320 (vs. gap)
- 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 (≠ R314), A258 (≠ H315), T259 (≠ Q316), R260 (= R317), A261 (≠ R318), W279 (≠ F336), L280 (≠ R337), N352 (≠ R403), L356 (≠ I407), L398 (≠ V445), R402 (≠ S449), M403 (≠ Y450)
- binding magnesium ion: D446 (= D494), N473 (≠ D521), G475 (= G523)
- binding thiamine diphosphate: Y371 (≠ H417), A395 (≠ G442), N396 (≠ D443), G420 (= G467), M422 (≠ L469), G445 (= G493), D446 (= D494), S447 (≠ G495), A448 (= A496), F451 (≠ Y499), N473 (≠ D521), G475 (= G523), I476 (≠ W524), Y477 (≠ T525)
Sites not aligning to the query:
- active site: 541
- 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 : 547, 549, 550
2ji7A X-ray structure of oxalyl-coa decarboxylase with covalent reaction intermediate (see paper)
26% identity, 92% coverage: 36:592/603 of query aligns to 9:540/559 of 2ji7A
- active site: V25 (≠ L52), G27 (= G54), I28 (≠ G55), P29 (≠ H56), I30 (= I57), E50 (= E77), V73 (≠ T100), Y114 (≠ L139), E115 (≠ Q140), E116 (≠ D141), A164 (≠ I189), M281 (≠ L338), G394 (= G441), G420 (= G467), M422 (≠ L469), D446 (= D494), N473 (≠ D521), G475 (= G523), I476 (≠ W524), K478 (≠ Q526), G479 (≠ A528), A482 (≠ Q531)
- binding adenosine-5'-diphosphate: C92 (≠ Q119), R154 (≠ V179), G215 (= G271), K216 (≠ S272), M241 (≠ S298), G274 (= G331), R276 (≠ P333), D300 (vs. gap), I301 (= I351), D319 (= D373), I320 (vs. gap)
- binding magnesium ion: D446 (= D494), N473 (≠ D521), G475 (= G523)
- 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 (= E77), V73 (≠ T100), Y114 (≠ L139), E115 (≠ Q140), A257 (≠ R314), A258 (≠ H315), T259 (≠ Q316), R260 (= R317), A261 (≠ R318), L280 (≠ R337), N352 (≠ R403), L356 (≠ I407), Y371 (≠ H417), G394 (= G441), A395 (≠ G442), N396 (≠ D443), A397 (≠ F444), L398 (≠ V445), R402 (≠ S449), M403 (≠ Y450), G420 (= G467), M422 (≠ L469), G445 (= G493), D446 (= D494), S447 (≠ G495), A448 (= A496), F451 (≠ Y499), N473 (≠ D521), G475 (= G523), Y477 (≠ T525)
Sites not aligning to the query:
- active site: 541
- 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: 549, 550
2ji6A X-ray structure of oxalyl-coa decarboxylase in complex with 3-deaza- thdp and oxalyl-coa (see paper)
26% identity, 92% coverage: 36:592/603 of query aligns to 9:540/559 of 2ji6A
- active site: V25 (≠ L52), G27 (= G54), I28 (≠ G55), P29 (≠ H56), I30 (= I57), E50 (= E77), V73 (≠ T100), Y114 (≠ L139), E115 (≠ Q140), E116 (≠ D141), A164 (≠ I189), M281 (≠ L338), G394 (= G441), G420 (= G467), M422 (≠ L469), D446 (= D494), N473 (≠ D521), G475 (= G523), I476 (≠ W524), K478 (≠ Q526), G479 (≠ A528), A482 (≠ Q531)
- binding adenosine-5'-diphosphate: C92 (≠ Q119), R154 (≠ V179), G215 (= G271), K216 (≠ S272), G217 (≠ Q273), M241 (≠ S298), G274 (= G331), A275 (≠ V332), R276 (≠ P333), D300 (vs. gap), I301 (= I351), D319 (= D373), I320 (vs. gap)
- binding magnesium ion: D446 (= D494), N473 (≠ D521), G475 (= G523)
- binding oxalyl-coenzyme a: G27 (= G54), I28 (≠ G55), Y114 (≠ L139), A257 (≠ R314), A258 (≠ H315), T259 (≠ Q316), R260 (= R317), A261 (≠ R318), L280 (≠ R337), N352 (≠ R403), K353 (≠ E404), L356 (≠ I407), L398 (≠ V445), R402 (≠ S449), M403 (≠ Y450), M422 (≠ L469), Y477 (≠ T525)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: V26 (≠ C53), E50 (= E77), P76 (= P103), Y371 (≠ H417), A395 (≠ G442), N396 (≠ D443), A397 (≠ F444), M422 (≠ L469), G445 (= G493), D446 (= D494), S447 (≠ G495), A448 (= A496), F451 (≠ Y499), N473 (≠ D521), G475 (= G523), I476 (≠ W524), Y477 (≠ T525)
Sites not aligning to the query:
2q29A Crystal structure of oxalyl-coa decarboxylase from escherichia coli in complex with acetyl coenzyme a (see paper)
27% identity, 92% coverage: 36:592/603 of query aligns to 9:539/546 of 2q29A
- active site: V25 (≠ L52), G27 (= G54), I28 (≠ G55), P29 (≠ H56), V30 (≠ I57), E50 (= E77), V73 (≠ T100), Y114 (≠ L139), E115 (≠ Q140), E116 (≠ D141), A164 (≠ I189), L281 (= L338), G391 (= G441), G417 (= G467), M419 (≠ L469), D443 (= D494), N470 (≠ D521), G472 (= G523), I473 (= I527), R475 (= R529), G476 (= G536), V479 (= V539)
- binding acetyl coenzyme *a: A257 (≠ R314), A258 (≠ H315), R260 (= R317), S261 (≠ R318), N351 (≠ A412), M355 (≠ A416), N400 (≠ Y450)
- binding magnesium ion: D443 (= D494), N470 (≠ D521), G472 (= G523)
- binding thiamine diphosphate: Y368 (≠ F423), A392 (≠ G442), N393 (≠ D443), T394 (≠ F444), M419 (≠ L469), G442 (= G493), D443 (= D494), S444 (≠ G495), A445 (= A496), F448 (≠ Y499), N470 (≠ D521), G472 (= G523), I473 (= I527), Y474 (≠ A528)
Sites not aligning to the query:
1v5gA Crystal structure of the reaction intermediate between pyruvate oxidase containing fad and tpp, and substrate pyruvate (see paper)
24% identity, 91% coverage: 41:588/603 of query aligns to 13:533/589 of 1v5gA
- binding flavin-adenine dinucleotide: G212 (= G271), I213 (≠ S272), G214 (≠ Q273), T236 (≠ S298), G237 (= G299), K238 (≠ M300), T254 (≠ D308), Y255 (≠ H309), R256 (≠ P310), V257 (≠ L311), G276 (= G331), S277 (≠ V332), N278 (≠ P333), F279 (≠ C334), F281 (= F336), D298 (≠ N354), I299 (≠ R355), M303 (≠ R361), D317 (= D373), A318 (= A374), P409 (≠ G464)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ G441), N388 (≠ D443), M414 (≠ L469), G438 (= G493), G440 (= G495), A441 (= A496), N466 (≠ D521), E468 (≠ G523), Y469 (≠ W524), A470 (≠ T525), F471 (≠ Q526), I472 (= I527)
- binding magnesium ion: D439 (= D494), N466 (≠ D521), E468 (≠ G523)
1v5fA Crystal structure of pyruvate oxidase complexed with fad and tpp, from aerococcus viridans (see paper)
24% identity, 91% coverage: 41:588/603 of query aligns to 13:533/589 of 1v5fA
- binding flavin-adenine dinucleotide: G212 (= G271), I213 (≠ S272), G214 (≠ Q273), T236 (≠ S298), G237 (= G299), K238 (≠ M300), T254 (≠ D308), Y255 (≠ H309), R256 (≠ P310), V257 (≠ L311), G276 (= G331), S277 (≠ V332), N278 (≠ P333), F279 (≠ C334), P280 (≠ D335), F281 (= F336), D298 (≠ N354), I299 (≠ R355), M303 (≠ R361), D317 (= D373), A318 (= A374), P409 (≠ G464)
- binding magnesium ion: D439 (= D494), N466 (≠ D521)
- binding thiamine diphosphate: N388 (≠ D443), S389 (≠ F444), M414 (≠ L469), G438 (= G493), G440 (= G495), N466 (≠ D521), Y469 (≠ W524), A470 (≠ T525), F471 (≠ Q526), I472 (= I527)
2djiA Crystal structure of pyruvate oxidase from aerococcus viridans containing fad (see paper)
24% identity, 91% coverage: 41:588/603 of query aligns to 14:534/590 of 2djiA
- active site: I25 (≠ L52), S27 (≠ G54), G28 (= G55), T29 (≠ H56), L30 (≠ I57), E52 (= E77), S75 (≠ T100), F114 (≠ L139), Q115 (= Q140), G163 (≠ I189), R257 (≠ P310), E284 (≠ L338), V387 (≠ G441), A413 (≠ G467), M415 (≠ L469), D440 (= D494), N467 (≠ D521), E469 (≠ G523), Y470 (≠ W524), F472 (≠ Q526), I473 (= I527), K476 (≠ E530)
- binding flavin-adenine dinucleotide: G213 (= G271), I214 (≠ S272), G215 (≠ Q273), T237 (≠ S298), G238 (= G299), K239 (≠ M300), T255 (≠ D308), Y256 (≠ H309), R257 (≠ P310), V258 (≠ L311), G277 (= G331), S278 (≠ V332), N279 (≠ P333), F280 (≠ C334), P281 (≠ D335), F282 (= F336), D299 (≠ N354), I300 (≠ R355), M304 (≠ R361), D318 (= D373), A319 (= A374), P410 (≠ G464)
Sites not aligning to the query:
3ea4A Arabidopsis thaliana acetohydroxyacid synthase in complex with monosulfuron-ester (see paper)
25% identity, 84% coverage: 28:533/603 of query aligns to 8:491/582 of 3ea4A
- active site: Y32 (≠ L52), G34 (= G54), G35 (= G55), A36 (≠ H56), S37 (≠ I57), E58 (= E77), T81 (= T100), F120 (≠ L139), Q121 (= Q140), E122 (≠ Q144), K170 (≠ I189), M265 (vs. gap), V292 (≠ L338), V399 (≠ G441), G425 (= G467), M427 (≠ L469), D452 (= D494), N479 (≠ D521), H481 (≠ G523), L482 (≠ W524), M484 (≠ Q526), V485 (≠ I527), W488 (≠ E530)
- binding methyl 2-{[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl}benzoate: D290 (≠ F336), R291 (= R337), W488 (≠ E530)
- binding flavin-adenine dinucleotide-n5-isobutyl ketone: R160 (≠ V179), G221 (= G271), G222 (≠ S272), G223 (≠ Q273), T245 (≠ S298), L246 (≠ G299), M247 (= M300), L263 (vs. gap), G264 (vs. gap), M265 (vs. gap), H266 (vs. gap), G285 (= G331), R287 (≠ P333), D289 (= D335), R291 (= R337), D309 (≠ N354), I310 (≠ R355), G327 (= G372), D328 (= D373), V329 (≠ A374), M404 (≠ A446), G422 (= G464)
- binding magnesium ion: D452 (= D494), N479 (≠ D521), H481 (≠ G523)
- binding 2-[(2e)-3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-(1-hydroxyethylidene)-4-methyl-2,3-dihydro-1,3-thiazol-5-yl]ethyltrihydrogen diphosphate: V399 (≠ G441), G400 (= G442), Q401 (≠ D443), H402 (≠ F444), M427 (≠ L469), G451 (= G493), D452 (= D494), G453 (= G495), S454 (≠ A496), N479 (≠ D521), H481 (≠ G523), L482 (≠ W524), G483 (≠ T525), M484 (≠ Q526), V485 (≠ I527)
Sites not aligning to the query:
3e9yA Arabidopsis thaliana acetohydroxyacid synthase in complex with monosulfuron (see paper)
25% identity, 84% coverage: 28:533/603 of query aligns to 8:491/582 of 3e9yA
- active site: Y32 (≠ L52), G34 (= G54), G35 (= G55), A36 (≠ H56), S37 (≠ I57), E58 (= E77), T81 (= T100), F120 (≠ L139), Q121 (= Q140), E122 (≠ Q144), K170 (≠ I189), M265 (vs. gap), V292 (≠ L338), V399 (≠ G441), G425 (= G467), M427 (≠ L469), D452 (= D494), N479 (≠ D521), H481 (≠ G523), L482 (≠ W524), M484 (≠ Q526), V485 (≠ I527), W488 (≠ E530)
- binding N-[(4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide: D290 (≠ F336), R291 (= R337), W488 (≠ E530)
- binding flavin-adenine dinucleotide-n5-isobutyl ketone: R160 (≠ V179), G221 (= G271), G222 (≠ S272), G223 (≠ Q273), T245 (≠ S298), L246 (≠ G299), M247 (= M300), L263 (vs. gap), G285 (= G331), R287 (≠ P333), D289 (= D335), R291 (= R337), D309 (≠ N354), I310 (≠ R355), G327 (= G372), D328 (= D373), V329 (≠ A374), M404 (≠ A446), G422 (= G464)
- binding magnesium ion: D452 (= D494), N479 (≠ D521), H481 (≠ G523)
- binding 2-[(2e)-3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-(1-hydroxyethylidene)-4-methyl-2,3-dihydro-1,3-thiazol-5-yl]ethyltrihydrogen diphosphate: V399 (≠ G441), G400 (= G442), Q401 (≠ D443), H402 (≠ F444), M427 (≠ L469), G451 (= G493), G453 (= G495), S454 (≠ A496), N479 (≠ D521), H481 (≠ G523), L482 (≠ W524), G483 (≠ T525), M484 (≠ Q526), V485 (≠ I527)
Sites not aligning to the query:
Query Sequence
>WP_013420232.1 NCBI__GCF_000166055.1:WP_013420232.1
MAVVLEKGHTRDRVAASRGEAQGEVPANSARHAGDVIAASLKAQGVTAIFTLCGGHISPI
LIGAKDAGIRIVDTRHEATAAFAADAMARLSGVPGVAAVTAGPGLTNIVTPLKNAQLAQS
PLILFGGAAPTMLQGRGALQDIDQRPVVAPHVKIVKQVRRVRDIGPALEDAFAVAREGVQ
GPAFIECPIDLLYPEALVRQWYAEAGGRGQSLGARALRFYLHRHLEKMFGGTKAPATPRP
RKIRIPTPASSSVNAAAAALSKAERPLAIIGSQALATGTDAAALAEAITRLGIPVYLSGM
ARGLLGRDHPLQLRHQRRNALKESDCVILAGVPCDFRLDYGKQIRNTATLIAANRSRKDA
RLNRRATIEAIGDAALFLRALAERGRIHRDDWLASLRARDAARETDIDAQAATEGAHVNP
VAFFRALDREAGENAIFVADGGDFVATASYIVRPRRPLSWLDPGAFGTLGVGAGFALGAA
LARPDAEIWVLFGDGACGYSLAEFDTFVRHGIPVIAVVGNDAGWTQIAREQEKVLGDDVG
TVLARTAYHEVAAGFGAEGILVKTNAEVPEALRRARAAAKAGRPVLVNVWLDRTSFREGS
ISM
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