SitesBLAST
Comparing WP_020173438.1 NCBI__GCF_000385335.1:WP_020173438.1 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)
7b2eA Quadruple mutant of oxalyl-coa decarboxylase from methylorubrum extorquens with bound tpp and adp (see paper)
86% identity, 90% coverage: 41:586/605 of query aligns to 2:547/548 of 7b2eA
- active site: V25 (= V64), G27 (= G66), I28 (= I67), P29 (= P68), I30 (≠ V69), E50 (= E89), V73 (= V112), Y114 (= Y153), G115 (≠ E154), A164 (= A203), L281 (= L320), G394 (= G433), G420 (= G459), M422 (= M461), I476 (= I515), R478 (= R517), G479 (= G518), T482 (= T521)
- binding adenosine-5'-diphosphate: C92 (= C131), R154 (= R193), G215 (= G254), K216 (= K255), G217 (= G256), M241 (= M280), G274 (= G313), R276 (= R315), D301 (= D340), I302 (= I341), D320 (= D359), I321 (= I360)
- binding magnesium ion: D446 (= D485), N473 (= N512), G475 (= G514)
- binding thiamine diphosphate: F371 (= F410), C395 (≠ A434), N396 (= N435), T397 (= T436), G420 (= G459), M422 (= M461), G445 (= G484), D446 (= D485), S447 (= S486), A448 (= A487), F451 (= F490), N473 (= N512), G475 (= G514), I476 (= I515), F477 (≠ Y516)
P40149 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Oxalobacter formigenes (see 2 papers)
63% identity, 93% coverage: 41:602/605 of query aligns to 8:568/568 of P40149
- E56 (= E89) mutation to A: Loss of the decarboxylase activity. The mutant forms a dimer and not a tetramer.
- Y120 (= Y153) 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 (= E154) 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 (= R193) binding
- K222 (= K255) binding
- R282 (= R315) binding
- D306 (= D340) binding
- I326 (= I360) binding
- Y377 (≠ F410) binding
- D452 (= D485) binding
- N479 (= N512) binding
- G481 (= G514) binding
- Y483 (= Y516) 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 (= S587) mutation to A: Does not affect oxalyl-CoA binding, but it reduces 7-fold the catalytic efficiency for oxalyl-CoA.
- R555 (≠ N589) 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)
63% identity, 92% coverage: 41:599/605 of query aligns to 2:559/559 of 2jibA
- active site: V25 (= V64), G27 (= G66), I28 (= I67), P29 (= P68), I30 (≠ V69), E50 (= E89), V73 (= V112), Y114 (= Y153), E115 (= E154), E116 (= E155), A164 (= A203), M281 (≠ L320), G394 (= G433), G420 (= G459), M422 (= M461), D446 (= D485), N473 (= N512), G475 (= G514), I476 (= I515), K478 (≠ R517), G479 (= G518), A482 (≠ T521), P541 (= P581)
- binding adenosine-5'-diphosphate: C92 (= C131), R154 (= R193), G215 (= G254), K216 (= K255), G217 (= G256), M241 (= M280), G274 (= G313), A275 (= A314), R276 (= R315), D300 (= D340), I301 (= I341), D319 (= D359), I320 (= I360)
- binding coenzyme a: A258 (= A297), R260 (= R299), A261 (≠ S300), L280 (= L319), N352 (= N393), K353 (≠ L394), L356 (≠ M397), L398 (= L437), R402 (= R441), M403 (≠ G442), R549 (≠ N589), I550 (= I590)
- binding magnesium ion: D446 (= D485), N473 (= N512), G475 (= G514)
- binding thiamine diphosphate: E50 (= E89), V73 (= V112), Y371 (≠ F410), A395 (= A434), N396 (= N435), A397 (≠ T436), M422 (= M461), G445 (= G484), D446 (= D485), S447 (= S486), A448 (= A487), F451 (= F490), N473 (= N512), G475 (= G514), I476 (= I515), Y477 (= Y516)
2ji8A X-ray structure of oxalyl-coa decarboxylase in complex with formyl- coa (see paper)
63% identity, 92% coverage: 41:599/605 of query aligns to 2:559/559 of 2ji8A
- active site: V25 (= V64), G27 (= G66), I28 (= I67), P29 (= P68), I30 (≠ V69), E50 (= E89), V73 (= V112), Y114 (= Y153), E115 (= E154), E116 (= E155), A164 (= A203), M281 (≠ L320), G394 (= G433), G420 (= G459), M422 (= M461), D446 (= D485), N473 (= N512), G475 (= G514), I476 (= I515), K478 (≠ R517), G479 (= G518), A482 (≠ T521), P541 (= P581)
- binding adenosine-5'-diphosphate: C92 (= C131), R154 (= R193), G215 (= G254), K216 (= K255), G217 (= G256), M241 (= M280), G274 (= G313), R276 (= R315), D300 (= D340), I301 (= I341), D319 (= D359), I320 (= I360)
- 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 (≠ S296), A258 (= A297), T259 (≠ A298), R260 (= R299), A261 (≠ S300), W279 (= W318), L280 (= L319), N352 (= N393), L356 (≠ M397), L398 (= L437), R402 (= R441), M403 (≠ G442), S547 (= S587), R549 (≠ N589), I550 (= I590)
- binding magnesium ion: D446 (= D485), N473 (= N512), G475 (= G514)
- binding thiamine diphosphate: Y371 (≠ F410), A395 (= A434), N396 (= N435), G420 (= G459), M422 (= M461), G445 (= G484), D446 (= D485), S447 (= S486), A448 (= A487), F451 (= F490), N473 (= N512), G475 (= G514), I476 (= I515), Y477 (= Y516)
2ji7A X-ray structure of oxalyl-coa decarboxylase with covalent reaction intermediate (see paper)
63% identity, 92% coverage: 41:599/605 of query aligns to 2:559/559 of 2ji7A
- active site: V25 (= V64), G27 (= G66), I28 (= I67), P29 (= P68), I30 (≠ V69), E50 (= E89), V73 (= V112), Y114 (= Y153), E115 (= E154), E116 (= E155), A164 (= A203), M281 (≠ L320), G394 (= G433), G420 (= G459), M422 (= M461), D446 (= D485), N473 (= N512), G475 (= G514), I476 (= I515), K478 (≠ R517), G479 (= G518), A482 (≠ T521), P541 (= P581)
- binding adenosine-5'-diphosphate: C92 (= C131), R154 (= R193), G215 (= G254), K216 (= K255), M241 (= M280), G274 (= G313), R276 (= R315), D300 (= D340), I301 (= I341), D319 (= D359), I320 (= I360)
- binding magnesium ion: D446 (= D485), N473 (= N512), G475 (= G514)
- 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 (= E89), V73 (= V112), Y114 (= Y153), E115 (= E154), A257 (≠ S296), A258 (= A297), T259 (≠ A298), R260 (= R299), A261 (≠ S300), L280 (= L319), N352 (= N393), L356 (≠ M397), Y371 (≠ F410), G394 (= G433), A395 (= A434), N396 (= N435), A397 (≠ T436), L398 (= L437), R402 (= R441), M403 (≠ G442), G420 (= G459), M422 (= M461), G445 (= G484), D446 (= D485), S447 (= S486), A448 (= A487), F451 (= F490), N473 (= N512), G475 (= G514), Y477 (= Y516), R549 (≠ N589), I550 (= I590)
2ji6A X-ray structure of oxalyl-coa decarboxylase in complex with 3-deaza- thdp and oxalyl-coa (see paper)
63% identity, 92% coverage: 41:599/605 of query aligns to 2:559/559 of 2ji6A
- active site: V25 (= V64), G27 (= G66), I28 (= I67), P29 (= P68), I30 (≠ V69), E50 (= E89), V73 (= V112), Y114 (= Y153), E115 (= E154), E116 (= E155), A164 (= A203), M281 (≠ L320), G394 (= G433), G420 (= G459), M422 (= M461), D446 (= D485), N473 (= N512), G475 (= G514), I476 (= I515), K478 (≠ R517), G479 (= G518), A482 (≠ T521), P541 (= P581)
- binding adenosine-5'-diphosphate: C92 (= C131), R154 (= R193), G215 (= G254), K216 (= K255), G217 (= G256), M241 (= M280), G274 (= G313), A275 (= A314), R276 (= R315), D300 (= D340), I301 (= I341), D319 (= D359), I320 (= I360)
- binding magnesium ion: D446 (= D485), N473 (= N512), G475 (= G514)
- binding oxalyl-coenzyme a: G27 (= G66), I28 (= I67), Y114 (= Y153), A257 (≠ S296), A258 (= A297), T259 (≠ A298), R260 (= R299), A261 (≠ S300), L280 (= L319), N352 (= N393), K353 (≠ L394), L356 (≠ M397), L398 (= L437), R402 (= R441), M403 (≠ G442), M422 (= M461), Y477 (= Y516), S547 (= S587), R549 (≠ N589), I550 (= I590)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: V26 (≠ P65), E50 (= E89), P76 (= P115), Y371 (≠ F410), A395 (= A434), N396 (= N435), A397 (≠ T436), M422 (= M461), G445 (= G484), D446 (= D485), S447 (= S486), A448 (= A487), F451 (= F490), N473 (= N512), G475 (= G514), I476 (= I515), Y477 (= Y516)
2c31A Crystal structure of oxalyl-coa decarboxylase in complex with the cofactor derivative thiamin-2-thiazolone diphosphate and adenosine diphosphate (see paper)
63% identity, 90% coverage: 41:586/605 of query aligns to 2:546/546 of 2c31A
- active site: V25 (= V64), G27 (= G66), I28 (= I67), P29 (= P68), I30 (≠ V69), E50 (= E89), V73 (= V112), Y114 (= Y153), E115 (= E154), E116 (= E155), A164 (= A203), M281 (≠ L320), G394 (= G433), G420 (= G459), M422 (= M461), D446 (= D485), N473 (= N512), G475 (= G514), I476 (= I515), K478 (≠ R517), G479 (= G518), A482 (≠ T521), P541 (= P581)
- binding adenosine-5'-diphosphate: C92 (= C131), R154 (= R193), G215 (= G254), K216 (= K255), G217 (= G256), M241 (= M280), G274 (= G313), A275 (= A314), R276 (= R315), D300 (= D340), I301 (= I341), D319 (= D359), I320 (= I360)
- binding magnesium ion: D446 (= D485), N473 (= N512), G475 (= G514)
- 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 (≠ P65), E50 (= E89), Y371 (≠ F410), A395 (= A434), N396 (= N435), A397 (≠ T436), M422 (= M461), G445 (= G484), D446 (= D485), S447 (= S486), A448 (= A487), F451 (= F490), N473 (= N512), G475 (= G514), I476 (= I515), Y477 (= Y516)
P0AFI0 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Escherichia coli (strain K12) (see paper)
61% identity, 92% coverage: 41:598/605 of query aligns to 6:561/564 of P0AFI0
- R158 (= R193) binding
- K220 (= K255) binding
- R280 (= R315) binding
- D302 (= D340) binding
- I322 (= I360) binding
- Y372 (≠ F410) binding
- D447 (= D485) binding
- N474 (= N512) binding
- G476 (= G514) binding
- Y478 (= Y516) binding
2q28A Crystal structure of oxalyl-coa decarboxylase from escherichia coli in complex with adenosine-5`-diphosphate (see paper)
61% identity, 91% coverage: 41:590/605 of query aligns to 2:549/550 of 2q28A
- active site: V25 (= V64), G27 (= G66), I28 (= I67), P29 (= P68), V30 (= V69), E50 (= E89), V73 (= V112), Y114 (= Y153), E115 (= E154), E116 (= E155), A164 (= A203), L281 (= L320), G391 (= G433), G417 (= G459), M419 (= M461), D443 (= D485), N470 (= N512), G472 (= G514), I473 (= I515), R475 (= R517), G476 (= G518), V479 (≠ T521), P540 (= P581)
- binding adenosine-5'-diphosphate: R154 (= R193), G215 (= G254), K216 (= K255), G217 (= G256), M241 (= M280), G274 (= G313), R276 (= R315), D298 (= D340), I299 (= I341), D317 (= D359), I318 (= I360)
- binding magnesium ion: D443 (= D485), N470 (= N512), G472 (= G514)
- binding thiamine diphosphate: Y368 (≠ F410), G391 (= G433), A392 (= A434), N393 (= N435), T394 (= T436), M419 (= M461), G442 (= G484), D443 (= D485), S444 (= S486), A445 (= A487), F448 (= F490), N470 (= N512), G472 (= G514), I473 (= I515), Y474 (= Y516)
2q29A Crystal structure of oxalyl-coa decarboxylase from escherichia coli in complex with acetyl coenzyme a (see paper)
61% identity, 90% coverage: 41:587/605 of query aligns to 2:546/546 of 2q29A
- active site: V25 (= V64), G27 (= G66), I28 (= I67), P29 (= P68), V30 (= V69), E50 (= E89), V73 (= V112), Y114 (= Y153), E115 (= E154), E116 (= E155), A164 (= A203), L281 (= L320), G391 (= G433), G417 (= G459), M419 (= M461), D443 (= D485), N470 (= N512), G472 (= G514), I473 (= I515), R475 (= R517), G476 (= G518), V479 (≠ T521), P540 (= P581)
- binding acetyl coenzyme *a: A257 (≠ S296), A258 (= A297), R260 (= R299), S261 (= S300), N351 (= N393), M355 (= M397), N400 (≠ G442)
- binding magnesium ion: D443 (= D485), N470 (= N512), G472 (= G514)
- binding thiamine diphosphate: Y368 (≠ F410), A392 (= A434), N393 (= N435), T394 (= T436), M419 (= M461), G442 (= G484), D443 (= D485), S444 (= S486), A445 (= A487), F448 (= F490), N470 (= N512), G472 (= G514), I473 (= I515), Y474 (= Y516)
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, 92% coverage: 40:594/605 of query aligns to 11:574/578 of Q9UJ83
- D455 (= D485) 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 (= S486) 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
40% identity, 89% coverage: 43:579/605 of query aligns to 4:537/540 of 6xn8A
- active site: V25 (= V64), G27 (= G66), F28 (≠ I67), P29 (= P68), I30 (≠ V69), E50 (= E89), V73 (= V112), F112 (≠ Y153), Q113 (≠ E154), E114 (= E155), D162 (≠ A203), F277 (≠ L320), G388 (= G433), G414 (= G459), M416 (= M461), D441 (= D485), N468 (= N512), G470 (= G514), I471 (= I515), P473 (≠ R517), G474 (= G518), E477 (≠ T521)
- binding adenosine-5'-diphosphate: R152 (= R193), G211 (= G254), K212 (= K255), S237 (≠ M280), G270 (= G313), R272 (= R315), D295 (= D340), I296 (= I341), G313 (= G358), D314 (= D359), G315 (≠ I360)
- binding magnesium ion: D441 (= D485), N468 (= N512), G470 (= G514)
- 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 (= E89), V73 (= V112), P76 (= P115), H80 (≠ N119), Y367 (≠ F410), A389 (= A434), G390 (≠ N435), T391 (= T436), G414 (= G459), M416 (= M461), G440 (= G484), D441 (= D485), S442 (= S486), A443 (= A487), F446 (= F490), N468 (= N512), G470 (= G514), I471 (= I515), G472 (≠ Y516)
P39994 2-hydroxyacyl-CoA lyase; Peroxisomal protein 1; EC 4.1.2.63 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
35% identity, 87% coverage: 53:581/605 of query aligns to 13:544/560 of P39994
Sites not aligning to the query:
- 558:560 Peroxisomal target signal 1 (PTS1)
7pt1A Actinobacterial 2-hydroxyacyl-coa lyase (achacl) structure in complex with substrate 2-hib-coa and inactive cofactor 3-deaza-thdp (see paper)
27% identity, 90% coverage: 48:589/605 of query aligns to 10:550/574 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 (≠ Y153), Q114 (≠ E154), G256 (≠ S296), S257 (≠ A297), R259 (= R299), S260 (= S300), Q279 (≠ L319), Y352 (≠ A395), R403 (= R441), L404 (≠ I444), G419 (= G459), D547 (≠ E586)
- binding magnesium ion: D446 (= D485), N473 (= N512), A475 (vs. gap)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: E51 (= E89), T74 (≠ V112), P77 (= P115), G396 (≠ A434), D397 (≠ N435), L398 (≠ T436), G419 (= G459), L421 (≠ M461), G445 (= G484), D446 (= D485), G447 (≠ S486), A448 (= A487), N473 (= N512), A475 (vs. gap), W476 (vs. gap), N477 (≠ G514), I478 (= I515), E479 (≠ Y516)
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: 552
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)
27% identity, 90% coverage: 48:589/605 of query aligns to 10:550/580 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 (≠ S281), G256 (≠ S296), S257 (≠ A297), R259 (= R299), S260 (= S300), Y278 (≠ W318), Q279 (≠ L319), Y352 (≠ A395), R403 (= R441), L404 (≠ I444)
- binding magnesium ion: D446 (= D485), N473 (= N512), A475 (vs. gap)
- binding thiamine diphosphate: G396 (≠ A434), D397 (≠ N435), L398 (≠ T436), G419 (= G459), L421 (≠ M461), G445 (= G484), D446 (= D485), G447 (≠ S486), A448 (= A487), N473 (= N512), A475 (vs. gap), W476 (vs. gap), N477 (≠ G514), I478 (= I515), E479 (≠ Y516)
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
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)
27% identity, 90% coverage: 48:589/605 of query aligns to 10:550/584 of 7pt4B
- binding magnesium ion: D446 (= D485), N473 (= N512), A475 (vs. gap)
- 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 (≠ A297), R259 (= R299), S260 (= S300), Q279 (≠ L319), Y352 (≠ A395), G395 (= G433), G396 (≠ A434), D397 (≠ N435), L398 (≠ T436), L399 (= L437), R403 (= R441), L404 (≠ I444), G419 (= G459), L421 (≠ M461), G445 (= G484), D446 (= D485), G447 (≠ S486), A448 (= A487), N473 (= N512), A475 (vs. gap), W476 (vs. gap), N477 (≠ G514), I478 (= I515), E479 (≠ Y516), D547 (≠ E586)
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: 561
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)
27% identity, 90% coverage: 48:589/605 of query aligns to 24:564/590 of P0DUV9
- G43 (≠ I67) binding
- Q255 (≠ S281) binding
- RS 273:274 (= RS 299:300) binding
- R362 (≠ E391) binding
- GDL 410:412 (≠ ANT 434:436) binding
- R417 (= R441) binding
- G433 (= G459) binding
- D460 (= D485) binding
- GA 461:462 (≠ SA 486:487) binding
- N487 (= N512) binding
- NRAWNI 487:492 (≠ NN--GI 512:515) binding
- A489 (vs. gap) binding
- E493 (≠ Y516) 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 (≠ ESGN 586:589) binding
Sites not aligning to the query:
4qq8C Crystal structure of the formolase fls in space group p 43 21 2 (see paper)
29% identity, 89% coverage: 42:581/605 of query aligns to 2:547/569 of 4qq8C
- active site: L24 (≠ V64), G26 (= G66), I27 (= I67), H28 (≠ P68), I29 (≠ V69), E49 (= E89), T72 (≠ V112), L111 (= L148), Q112 (= Q149), A113 (≠ Q150), G114 (= G151), W162 (≠ A203), L255 (≠ S294), T283 (≠ L320), G392 (= G433), N418 (≠ G459), M420 (= M461), D447 (= D485), N474 (= N512), S476 (vs. gap), W477 (vs. gap), W479 (≠ I515), T480 (≠ Y516), F483 (≠ T519), L545 (vs. gap)
- binding magnesium ion: D447 (= D485), N474 (= N512), S476 (vs. gap)
- binding thiamine diphosphate: H25 (≠ P65), E49 (= E89), Q112 (= Q149), G392 (= G433), G393 (≠ A434), L394 (≠ N435), T395 (= T436), N418 (≠ G459), M420 (= M461), G446 (= G484), D447 (= D485), G448 (≠ S486), S449 (≠ A487), Y452 (≠ F490), N474 (= N512), S476 (vs. gap), W477 (vs. gap), G478 (= G514), W479 (≠ I515), T480 (≠ Y516)
3d7kA Crystal structure of benzaldehyde lyase in complex with the inhibitor mbp (see paper)
29% identity, 89% coverage: 42:581/605 of query aligns to 2:547/554 of 3d7kA
- active site: L24 (≠ V64), G26 (= G66), A27 (≠ I67), H28 (≠ P68), I29 (≠ V69), E49 (= E89), T72 (≠ V112), L111 (= L148), Q112 (= Q149), A113 (≠ Q150), G114 (= G151), W162 (≠ A203), L255 (≠ S294), T283 (≠ L320), G392 (= G433), G418 (= G459), M420 (= M461), D447 (= D485), N474 (= N512), S476 (vs. gap), W477 (vs. gap), A479 (≠ I515), T480 (≠ Y516), F483 (≠ T519), L545 (vs. gap)
- binding calcium ion: D447 (= D485), N474 (= N512), S476 (vs. gap)
- 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 (≠ P65), G26 (= G66), A27 (≠ I67), E49 (= E89), T72 (≠ V112), Q112 (= Q149), G392 (= G433), A393 (= A434), L394 (≠ N435), T395 (= T436), G418 (= G459), M420 (= M461), G446 (= G484), D447 (= D485), G448 (≠ S486), S449 (≠ A487), Y452 (≠ F490), N474 (= N512), S476 (vs. gap), W477 (vs. gap), G478 (= G514), A479 (≠ I515), T480 (≠ Y516)
4rjiC Acetolactate synthase from bacillus subtilis bound to thdp - crystal form i (see paper)
25% identity, 89% coverage: 45:580/605 of query aligns to 4:533/555 of 4rjiC
- binding magnesium ion: D438 (= D485), D465 (≠ N512), T467 (≠ G514)
- binding thiamine diphosphate: P24 (= P65), E48 (= E89), P74 (= P115), S387 (≠ A434), H388 (≠ N435), Q411 (≠ G459), G437 (= G484), D438 (= D485), G439 (≠ S486), G440 (≠ A487), T467 (≠ G514), Y468 (≠ I515), D469 (≠ Y516), M470 (≠ R517), V471 (≠ G518)
Sites not aligning to the query:
Query Sequence
>WP_020173438.1 NCBI__GCF_000385335.1:WP_020173438.1
MLKEAARAEVRQGETTGAEDALKAKPRDAGIVVAEAGAEQELTDGFHLVIDALKLNGIDT
IYGVPGIPVTDLGRLAQAEGMRVISFRHEQHAGNAAAIAGYLTKKPGICLTVSAPGFLNG
LTALANATTNCFPMIQISGSSEREIVDLQQGDYEEMDQLAIAKPLCKAAFRVLHAADIGI
GVARAIRAAVSGRPGGVYLDLPAKLFSQVMDAKAGAKSLVKVIDPAPAVLPAPAAVERAL
DVLKSAKRPLIILGKGAAYAQADSEIRALVEQSGIPYLPMSMAKGLLPDTHPQSASAARS
MVLKEADVVMLIGARLNWLLSHGKGKTWGEPGTQKFIQIDIEPKEMDSNIEIAAPLVGDI
GSCVSALLKGIDGNWSVPPVEWTSAINARKEANLAKMASKLLKNSSPMDFHSALGALRTV
IKERPDAILVNEGANTLDLARGVIDMYQPRKRLDVGTWGVMGIGMGFAVAAAVETGKPVL
AIEGDSAFGFSGMEVETICRYNLPICIVVFNNNGIYRGTDTDPTGRDPGTTVFVKDSRYD
KMMEAFGGVGVHVATPDELSRAVNEAMDSGRPTLINAAIDPAAGSESGNIGNLNPQSVVR
KKAAA
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