SitesBLAST
Comparing 16478 FitnessBrowser__Keio:16478 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)
P0AFI0 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Escherichia coli (strain K12) (see paper)
100% identity, 100% coverage: 1:564/564 of query aligns to 1:564/564 of P0AFI0
- R158 (= R158) binding
- K220 (= K220) binding
- R280 (= R280) binding
- D302 (= D302) binding
- I322 (= I322) binding
- Y372 (= Y372) binding
- D447 (= D447) binding
- N474 (= N474) binding
- G476 (= G476) binding
- Y478 (= Y478) binding
2q28A Crystal structure of oxalyl-coa decarboxylase from escherichia coli in complex with adenosine-5`-diphosphate (see paper)
100% identity, 98% coverage: 5:554/564 of query aligns to 1:550/550 of 2q28A
- active site: V25 (= V29), G27 (= G31), I28 (= I32), P29 (= P33), V30 (= V34), E50 (= E54), V73 (= V77), Y114 (= Y118), E115 (= E119), E116 (= E120), A164 (= A168), L281 (= L285), G391 (= G395), G417 (= G421), M419 (= M423), D443 (= D447), N470 (= N474), G472 (= G476), I473 (= I477), R475 (= R479), G476 (= G480), V479 (= V483), P540 (= P544)
- binding adenosine-5'-diphosphate: R154 (= R158), G215 (= G219), K216 (= K220), G217 (= G221), M241 (= M245), G274 (= G278), R276 (= R280), D298 (= D302), I299 (= I303), D317 (= D321), I318 (= I322)
- binding magnesium ion: D443 (= D447), N470 (= N474), G472 (= G476)
- binding thiamine diphosphate: Y368 (= Y372), G391 (= G395), A392 (= A396), N393 (= N397), T394 (= T398), M419 (= M423), G442 (= G446), D443 (= D447), S444 (= S448), A445 (= A449), F448 (= F452), N470 (= N474), G472 (= G476), I473 (= I477), Y474 (= Y478)
2q29A Crystal structure of oxalyl-coa decarboxylase from escherichia coli in complex with acetyl coenzyme a (see paper)
100% identity, 97% coverage: 5:550/564 of query aligns to 1:546/546 of 2q29A
- active site: V25 (= V29), G27 (= G31), I28 (= I32), P29 (= P33), V30 (= V34), E50 (= E54), V73 (= V77), Y114 (= Y118), E115 (= E119), E116 (= E120), A164 (= A168), L281 (= L285), G391 (= G395), G417 (= G421), M419 (= M423), D443 (= D447), N470 (= N474), G472 (= G476), I473 (= I477), R475 (= R479), G476 (= G480), V479 (= V483), P540 (= P544)
- binding acetyl coenzyme *a: A257 (= A261), A258 (= A262), R260 (= R264), S261 (= S265), N351 (= N355), M355 (= M359), N400 (= N404)
- binding magnesium ion: D443 (= D447), N470 (= N474), G472 (= G476)
- binding thiamine diphosphate: Y368 (= Y372), A392 (= A396), N393 (= N397), T394 (= T398), M419 (= M423), G442 (= G446), D443 (= D447), S444 (= S448), A445 (= A449), F448 (= F452), N470 (= N474), G472 (= G476), I473 (= I477), Y474 (= Y478)
7b2eA Quadruple mutant of oxalyl-coa decarboxylase from methylorubrum extorquens with bound tpp and adp (see paper)
61% identity, 96% coverage: 6:549/564 of query aligns to 2:547/548 of 7b2eA
- active site: V25 (= V29), G27 (= G31), I28 (= I32), P29 (= P33), I30 (≠ V34), E50 (= E54), V73 (= V77), Y114 (= Y118), G115 (≠ E119), A164 (= A168), L281 (= L285), G394 (= G395), G420 (= G421), M422 (= M423), I476 (= I477), R478 (= R479), G479 (= G480), T482 (≠ V483)
- binding adenosine-5'-diphosphate: C92 (≠ G96), R154 (= R158), G215 (= G219), K216 (= K220), G217 (= G221), M241 (= M245), G274 (= G278), R276 (= R280), D301 (= D302), I302 (= I303), D320 (= D321), I321 (= I322)
- binding magnesium ion: D446 (= D447), N473 (= N474), G475 (= G476)
- binding thiamine diphosphate: F371 (≠ Y372), C395 (≠ A396), N396 (= N397), T397 (= T398), G420 (= G421), M422 (= M423), G445 (= G446), D446 (= D447), S447 (= S448), A448 (= A449), F451 (= F452), N473 (= N474), G475 (= G476), I476 (= I477), F477 (≠ Y478)
P40149 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Oxalobacter formigenes (see 2 papers)
54% identity, 98% coverage: 3:557/564 of query aligns to 5:560/568 of P40149
- E56 (= E54) mutation to A: Loss of the decarboxylase activity. The mutant forms a dimer and not a tetramer.
- Y120 (= Y118) 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 (= E119) 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 (= R158) binding
- K222 (= K220) binding
- R282 (= R280) binding
- D306 (= D302) binding
- I326 (= I322) binding
- Y377 (= Y372) binding
- D452 (= D447) binding
- N479 (= N474) binding
- G481 (= G476) binding
- Y483 (= Y478) 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 (= S550) mutation to A: Does not affect oxalyl-CoA binding, but it reduces 7-fold the catalytic efficiency for oxalyl-CoA.
- R555 (≠ H552) 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)
54% identity, 98% coverage: 5:557/564 of query aligns to 1:554/559 of 2jibA
- active site: V25 (= V29), G27 (= G31), I28 (= I32), P29 (= P33), I30 (≠ V34), E50 (= E54), V73 (= V77), Y114 (= Y118), E115 (= E119), E116 (= E120), A164 (= A168), M281 (≠ L285), G394 (= G395), G420 (= G421), M422 (= M423), D446 (= D447), N473 (= N474), G475 (= G476), I476 (= I477), K478 (≠ R479), G479 (= G480), A482 (≠ V483), P541 (= P544)
- binding adenosine-5'-diphosphate: C92 (≠ G96), R154 (= R158), G215 (= G219), K216 (= K220), G217 (= G221), M241 (= M245), G274 (= G278), A275 (= A279), R276 (= R280), D300 (= D302), I301 (= I303), D319 (= D321), I320 (= I322)
- binding coenzyme a: A258 (= A262), R260 (= R264), A261 (≠ S265), L280 (= L284), N352 (= N355), K353 (≠ A356), L356 (≠ M359), L398 (= L399), R402 (= R403), M403 (≠ N404), R549 (≠ H552), I550 (= I553)
- binding magnesium ion: D446 (= D447), N473 (= N474), G475 (= G476)
- binding thiamine diphosphate: E50 (= E54), V73 (= V77), Y371 (= Y372), A395 (= A396), N396 (= N397), A397 (≠ T398), M422 (= M423), G445 (= G446), D446 (= D447), S447 (= S448), A448 (= A449), F451 (= F452), N473 (= N474), G475 (= G476), I476 (= I477), Y477 (= Y478)
2ji8A X-ray structure of oxalyl-coa decarboxylase in complex with formyl- coa (see paper)
54% identity, 98% coverage: 5:557/564 of query aligns to 1:554/559 of 2ji8A
- active site: V25 (= V29), G27 (= G31), I28 (= I32), P29 (= P33), I30 (≠ V34), E50 (= E54), V73 (= V77), Y114 (= Y118), E115 (= E119), E116 (= E120), A164 (= A168), M281 (≠ L285), G394 (= G395), G420 (= G421), M422 (= M423), D446 (= D447), N473 (= N474), G475 (= G476), I476 (= I477), K478 (≠ R479), G479 (= G480), A482 (≠ V483), P541 (= P544)
- binding adenosine-5'-diphosphate: C92 (≠ G96), R154 (= R158), G215 (= G219), K216 (= K220), G217 (= G221), M241 (= M245), G274 (= G278), R276 (= R280), D300 (= D302), I301 (= I303), D319 (= D321), I320 (= I322)
- 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 (= A261), A258 (= A262), T259 (≠ A263), R260 (= R264), A261 (≠ S265), W279 (= W283), L280 (= L284), N352 (= N355), L356 (≠ M359), L398 (= L399), R402 (= R403), M403 (≠ N404), S547 (= S550), R549 (≠ H552), I550 (= I553)
- binding magnesium ion: D446 (= D447), N473 (= N474), G475 (= G476)
- binding thiamine diphosphate: Y371 (= Y372), A395 (= A396), N396 (= N397), G420 (= G421), M422 (= M423), G445 (= G446), D446 (= D447), S447 (= S448), A448 (= A449), F451 (= F452), N473 (= N474), G475 (= G476), I476 (= I477), Y477 (= Y478)
2ji7A X-ray structure of oxalyl-coa decarboxylase with covalent reaction intermediate (see paper)
54% identity, 98% coverage: 5:557/564 of query aligns to 1:554/559 of 2ji7A
- active site: V25 (= V29), G27 (= G31), I28 (= I32), P29 (= P33), I30 (≠ V34), E50 (= E54), V73 (= V77), Y114 (= Y118), E115 (= E119), E116 (= E120), A164 (= A168), M281 (≠ L285), G394 (= G395), G420 (= G421), M422 (= M423), D446 (= D447), N473 (= N474), G475 (= G476), I476 (= I477), K478 (≠ R479), G479 (= G480), A482 (≠ V483), P541 (= P544)
- binding adenosine-5'-diphosphate: C92 (≠ G96), R154 (= R158), G215 (= G219), K216 (= K220), M241 (= M245), G274 (= G278), R276 (= R280), D300 (= D302), I301 (= I303), D319 (= D321), I320 (= I322)
- binding magnesium ion: D446 (= D447), N473 (= N474), G475 (= G476)
- 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 (= E54), V73 (= V77), Y114 (= Y118), E115 (= E119), A257 (= A261), A258 (= A262), T259 (≠ A263), R260 (= R264), A261 (≠ S265), L280 (= L284), N352 (= N355), L356 (≠ M359), Y371 (= Y372), G394 (= G395), A395 (= A396), N396 (= N397), A397 (≠ T398), L398 (= L399), R402 (= R403), M403 (≠ N404), G420 (= G421), M422 (= M423), G445 (= G446), D446 (= D447), S447 (= S448), A448 (= A449), F451 (= F452), N473 (= N474), G475 (= G476), Y477 (= Y478), R549 (≠ H552), I550 (= I553)
2ji6A X-ray structure of oxalyl-coa decarboxylase in complex with 3-deaza- thdp and oxalyl-coa (see paper)
54% identity, 98% coverage: 5:557/564 of query aligns to 1:554/559 of 2ji6A
- active site: V25 (= V29), G27 (= G31), I28 (= I32), P29 (= P33), I30 (≠ V34), E50 (= E54), V73 (= V77), Y114 (= Y118), E115 (= E119), E116 (= E120), A164 (= A168), M281 (≠ L285), G394 (= G395), G420 (= G421), M422 (= M423), D446 (= D447), N473 (= N474), G475 (= G476), I476 (= I477), K478 (≠ R479), G479 (= G480), A482 (≠ V483), P541 (= P544)
- binding adenosine-5'-diphosphate: C92 (≠ G96), R154 (= R158), G215 (= G219), K216 (= K220), G217 (= G221), M241 (= M245), G274 (= G278), A275 (= A279), R276 (= R280), D300 (= D302), I301 (= I303), D319 (= D321), I320 (= I322)
- binding magnesium ion: D446 (= D447), N473 (= N474), G475 (= G476)
- binding oxalyl-coenzyme a: G27 (= G31), I28 (= I32), Y114 (= Y118), A257 (= A261), A258 (= A262), T259 (≠ A263), R260 (= R264), A261 (≠ S265), L280 (= L284), N352 (= N355), K353 (≠ A356), L356 (≠ M359), L398 (= L399), R402 (= R403), M403 (≠ N404), M422 (= M423), Y477 (= Y478), S547 (= S550), R549 (≠ H552), I550 (= I553)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: V26 (= V30), E50 (= E54), P76 (= P80), Y371 (= Y372), A395 (= A396), N396 (= N397), A397 (≠ T398), M422 (= M423), G445 (= G446), D446 (= D447), S447 (= S448), A448 (= A449), F451 (= F452), N473 (= N474), G475 (= G476), I476 (= I477), Y477 (= Y478)
2c31A Crystal structure of oxalyl-coa decarboxylase in complex with the cofactor derivative thiamin-2-thiazolone diphosphate and adenosine diphosphate (see paper)
54% identity, 97% coverage: 5:549/564 of query aligns to 1:546/546 of 2c31A
- active site: V25 (= V29), G27 (= G31), I28 (= I32), P29 (= P33), I30 (≠ V34), E50 (= E54), V73 (= V77), Y114 (= Y118), E115 (= E119), E116 (= E120), A164 (= A168), M281 (≠ L285), G394 (= G395), G420 (= G421), M422 (= M423), D446 (= D447), N473 (= N474), G475 (= G476), I476 (= I477), K478 (≠ R479), G479 (= G480), A482 (≠ V483), P541 (= P544)
- binding adenosine-5'-diphosphate: C92 (≠ G96), R154 (= R158), G215 (= G219), K216 (= K220), G217 (= G221), M241 (= M245), G274 (= G278), A275 (= A279), R276 (= R280), D300 (= D302), I301 (= I303), D319 (= D321), I320 (= I322)
- binding magnesium ion: D446 (= D447), N473 (= N474), G475 (= G476)
- 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 (= V30), E50 (= E54), Y371 (= Y372), A395 (= A396), N396 (= N397), A397 (≠ T398), M422 (= M423), G445 (= G446), D446 (= D447), S447 (= S448), A448 (= A449), F451 (= F452), N473 (= N474), G475 (= G476), I476 (= I477), Y477 (= Y478)
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)
39% identity, 96% coverage: 6:546/564 of query aligns to 12:563/578 of Q9UJ83
- D455 (= D447) 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 (= S448) 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, 95% coverage: 8:542/564 of query aligns to 4:537/540 of 6xn8A
- active site: V25 (= V29), G27 (= G31), F28 (≠ I32), P29 (= P33), I30 (≠ V34), E50 (= E54), V73 (= V77), F112 (≠ Y118), Q113 (≠ E119), E114 (= E120), D162 (≠ A168), F277 (≠ L285), G388 (= G395), G414 (= G421), M416 (= M423), D441 (= D447), N468 (= N474), G470 (= G476), I471 (= I477), P473 (≠ A488), G474 (= G489), E477 (vs. gap)
- binding adenosine-5'-diphosphate: R152 (= R158), G211 (= G219), K212 (= K220), S237 (≠ M245), G270 (= G278), R272 (= R280), D295 (= D302), I296 (= I303), G313 (= G320), D314 (= D321), G315 (≠ I322)
- binding magnesium ion: D441 (= D447), N468 (= N474), G470 (= G476)
- 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 (= E54), V73 (= V77), P76 (= P80), H80 (≠ N84), Y367 (= Y372), A389 (= A396), G390 (≠ N397), T391 (= T398), G414 (= G421), M416 (= M423), G440 (= G446), D441 (= D447), S442 (= S448), A443 (= A449), F446 (= F452), N468 (= N474), G470 (= G476), I471 (= I477), G472 (= G487)
P39994 Putative 2-hydroxyacyl-CoA lyase; Peroxisomal protein 1; EC 4.1.-.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
35% identity, 94% coverage: 16:545/564 of query aligns to 11:545/560 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, 96% coverage: 13:551/564 of query aligns to 10:549/574 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 (≠ Y118), Q114 (≠ E119), G256 (≠ A261), S257 (≠ A262), R259 (= R264), S260 (= S265), Q279 (≠ L284), Y352 (≠ M359), R403 (= R403), L404 (≠ I406), G419 (= G421), D547 (≠ E549)
- binding magnesium ion: D446 (= D447), N473 (= N474), A475 (≠ G476)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: E51 (= E54), T74 (≠ V77), P77 (= P80), G396 (≠ A396), D397 (≠ N397), L398 (≠ T398), G419 (= G421), L421 (≠ M423), G445 (= G446), D446 (= D447), G447 (≠ S448), A448 (= A449), N473 (= N474), A475 (≠ G476), W476 (vs. gap), N477 (vs. gap), I478 (= I477), E479 (≠ Y478)
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
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, 96% coverage: 13:551/564 of query aligns to 24:563/590 of P0DUV9
- G43 (≠ I32) binding
- Q255 (≠ S246) binding
- RS 273:274 (= RS 264:265) binding
- R362 (≠ N355) binding
- GDL 410:412 (≠ ANT 396:398) binding
- R417 (= R403) binding
- G433 (= G421) binding
- D460 (= D447) binding
- GA 461:462 (≠ SA 448:449) binding
- N487 (= N474) binding
- NRAWNI 487:492 (≠ NGG--I 474:477) binding
- A489 (≠ G476) binding
- E493 (≠ Y478) 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
- 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)
27% identity, 96% coverage: 13:551/564 of query aligns to 10:549/584 of 7pt4B
- binding magnesium ion: D446 (= D447), N473 (= N474), A475 (≠ G476)
- 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 (≠ A262), R259 (= R264), S260 (= S265), Q279 (≠ L284), Y352 (≠ M359), G395 (= G395), G396 (≠ A396), D397 (≠ N397), L398 (≠ T398), L399 (= L399), R403 (= R403), L404 (≠ I406), G419 (= G421), L421 (≠ M423), G445 (= G446), D446 (= D447), G447 (≠ S448), A448 (= A449), N473 (= N474), A475 (≠ G476), W476 (vs. gap), N477 (vs. gap), I478 (= I477), E479 (≠ Y478), D547 (≠ E549)
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
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, 96% coverage: 13:551/564 of query aligns to 10:549/580 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 (≠ S246), G256 (≠ A261), S257 (≠ A262), R259 (= R264), S260 (= S265), Y278 (≠ W283), Q279 (≠ L284), Y352 (≠ M359), R403 (= R403), L404 (≠ I406)
- binding magnesium ion: D446 (= D447), N473 (= N474), A475 (≠ G476)
- binding thiamine diphosphate: G396 (≠ A396), D397 (≠ N397), L398 (≠ T398), G419 (= G421), L421 (≠ M423), G445 (= G446), D446 (= D447), G447 (≠ S448), A448 (= A449), N473 (= N474), A475 (≠ G476), W476 (vs. gap), N477 (vs. gap), I478 (= I477), E479 (≠ Y478)
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
6lpiB Crystal structure of ahas holo-enzyme (see paper)
27% identity, 95% coverage: 10:543/564 of query aligns to 8:520/539 of 6lpiB
- active site: I27 (≠ V29), G29 (= G31), G30 (vs. gap), S31 (vs. gap), I32 (vs. gap), E53 (= E54), C76 (≠ V77), F115 (≠ Y118), Q116 (≠ E119), E117 (= E120), K165 (≠ A168), M256 (vs. gap), A283 (≠ L285), V375 (≠ E394), G401 (= G421), M403 (= M423), D428 (= D447), N455 (= N474), A457 (vs. gap), L458 (vs. gap), L460 (≠ G476), V461 (≠ I477), Q464 (≠ G480)
- binding flavin-adenine dinucleotide: R155 (= R158), G212 (= G219), G213 (≠ K220), G214 (= G221), T236 (≠ M245), L237 (≠ S246), M238 (= M247), L254 (vs. gap), M256 (vs. gap), H257 (vs. gap), G276 (= G278), A277 (= A279), R278 (= R280), D280 (≠ N282), R282 (≠ L284), A283 (≠ L285), D300 (= D302), I301 (= I303), D319 (= D321), V320 (≠ I322), M380 (≠ L399), G398 (= G418)
- binding magnesium ion: D428 (= D447), N455 (= N474)
- binding thiamine diphosphate: E53 (= E54), C76 (≠ V77), P79 (= P80), G376 (= G395), Q377 (≠ A396), H378 (≠ N397), G401 (= G421), M403 (= M423), G427 (= G446), D428 (= D447), G429 (≠ S448), S430 (≠ A449), M433 (≠ F452), N455 (= N474), A457 (vs. gap), L458 (vs. gap), G459 (= G475), L460 (≠ G476), V461 (≠ I477)
7tzzA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase p197t mutant in complex with bispyribac-sodium (see paper)
27% identity, 83% coverage: 6:474/564 of query aligns to 10:480/582 of 7tzzA
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: M266 (vs. gap), R292 (≠ L284)
- binding 2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-2-[(1~{S})-1-(dioxidanyl)-1-oxidanyl-ethyl]-4-methyl-1,3-thiazol-5-yl]ethyl phosphono hydrogen phosphate: V400 (≠ E394), G401 (= G395), Q402 (≠ A396), H403 (≠ N397), G426 (= G421), M428 (= M423), G452 (= G446), D453 (= D447), G454 (≠ S448), S455 (≠ A449)
- binding flavin-adenine dinucleotide: R161 (= R158), G222 (= G219), G223 (≠ K220), G224 (= G221), T246 (≠ M245), L247 (≠ S246), M248 (= M247), M263 (vs. gap), L264 (vs. gap), M266 (vs. gap), H267 (vs. gap), G286 (= G278), R288 (= R280), V293 (≠ L285), D310 (= D302), I311 (= I303), D329 (= D321), V330 (≠ I322), M405 (≠ L399), G423 (= G418)
- binding magnesium ion: A37 (≠ P33), T82 (≠ V77), S83 (= S78), Q122 (≠ E119), Y381 (= Y372), D453 (= D447), M458 (≠ F452), Q461 (≠ M455), N480 (= N474)
Sites not aligning to the query:
8et4A Crystal structure of wild-type arabidopsis thaliana acetohydroxyacid synthase in complex with amidosulfuron (see paper)
27% identity, 83% coverage: 6:474/564 of query aligns to 10:480/582 of 8et4A
- binding 2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-2-[(1~{S})-1-(dioxidanyl)-1-oxidanyl-ethyl]-4-methyl-1,3-thiazol-5-yl]ethyl phosphono hydrogen phosphate: V400 (≠ E394), G401 (= G395), Q402 (≠ A396), H403 (≠ N397), G426 (= G421), M428 (= M423), G452 (= G446), D453 (= D447), G454 (≠ S448), S455 (≠ A449), M458 (≠ F452), N480 (= N474)
- binding flavin-adenine dinucleotide: R161 (= R158), G222 (= G219), G223 (≠ K220), G224 (= G221), T246 (≠ M245), L247 (≠ S246), M248 (= M247), L264 (vs. gap), M266 (vs. gap), H267 (vs. gap), G286 (= G278), V287 (≠ A279), R288 (= R280), D290 (≠ N282), R292 (≠ L284), V293 (≠ L285), D310 (= D302), I311 (= I303), D329 (= D321), V330 (≠ I322), M405 (≠ L399), G423 (= G418)
- binding magnesium ion: F370 (≠ E361), D453 (= D447), M458 (≠ F452), Q461 (≠ M455), N480 (= N474)
- binding N-{[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl}-N-methylmethanesulfonamide: M266 (vs. gap), R292 (≠ L284)
Sites not aligning to the query:
Query Sequence
>16478 FitnessBrowser__Keio:16478
MSDQLQMTDGMHIIVEALKQNNIDTIYGVVGIPVTDMARHAQAEGIRYIGFRHEQSAGYA
AAASGFLTQKPGICLTVSAPGFLNGLTALANATVNGFPMIMISGSSDRAIVDLQQGDYEE
LDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLDLPANVLAATMEKDEA
LTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQI
PFLPMSMAKGILEDTHPLSAAAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQ
LDIEPQEIDSNRPIAVPVVGDIASSMQGMLAELKQNTFTTPLVWRDILNIHKQQNAQKMH
EKLSTDTQPLNYFNALSAVRDVLRENQDIYLVNEGANTLDNARNIIDMYKPRRRLDCGTW
GVMGIGMGYAIGASVTSGSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNNGGIYRG
DGVDLSGAGAPSPTDLLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRKPTIINV
VIDPAAGTESGHITKLNPKQVAGN
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