SitesBLAST
Comparing AZOBR_RS31945 FitnessBrowser__azobra:AZOBR_RS31945 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)
84% identity, 94% coverage: 19:566/585 of query aligns to 1:547/548 of 7b2eA
- active site: V25 (= V43), G27 (= G45), I28 (= I46), P29 (= P47), I30 (= I48), E50 (= E68), V73 (= V91), Y114 (= Y132), G115 (≠ E133), A164 (= A182), L281 (= L299), G394 (= G412), G420 (= G438), M422 (= M440), I476 (= I494), R478 (≠ K496), G479 (= G497), T482 (≠ V500)
- binding adenosine-5'-diphosphate: C92 (= C110), R154 (= R172), G215 (= G233), K216 (= K234), G217 (= G235), M241 (= M259), G274 (= G292), R276 (= R294), D301 (= D319), I302 (= I320), D320 (= D338), I321 (= I339)
- binding magnesium ion: D446 (= D464), N473 (= N491), G475 (= G493)
- binding thiamine diphosphate: F371 (= F389), C395 (≠ A413), N396 (= N414), T397 (= T415), G420 (= G438), M422 (= M440), G445 (= G463), D446 (= D464), S447 (= S465), A448 (= A466), F451 (= F469), N473 (= N491), G475 (= G493), I476 (= I494), F477 (≠ Y495)
P40149 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Oxalobacter formigenes (see 2 papers)
61% identity, 97% coverage: 14:581/585 of query aligns to 2:567/568 of P40149
- E56 (= E68) mutation to A: Loss of the decarboxylase activity. The mutant forms a dimer and not a tetramer.
- Y120 (= Y132) 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 (= E133) 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 (= R172) binding
- K222 (= K234) binding
- R282 (= R294) binding
- D306 (= D319) binding
- I326 (= I339) binding
- Y377 (≠ F389) binding
- D452 (= D464) binding
- N479 (= N491) binding
- G481 (= G493) binding
- Y483 (= Y495) 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 (= S567) mutation to A: Does not affect oxalyl-CoA binding, but it reduces 7-fold the catalytic efficiency for oxalyl-CoA.
- R555 (≠ N569) 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)
61% identity, 96% coverage: 21:579/585 of query aligns to 3:559/559 of 2jibA
- active site: V25 (= V43), G27 (= G45), I28 (= I46), P29 (= P47), I30 (= I48), E50 (= E68), V73 (= V91), Y114 (= Y132), E115 (= E133), E116 (= E134), A164 (= A182), M281 (≠ L299), G394 (= G412), G420 (= G438), M422 (= M440), D446 (= D464), N473 (= N491), G475 (= G493), I476 (= I494), K478 (= K496), G479 (= G497), A482 (≠ S506), P541 (= P561)
- binding adenosine-5'-diphosphate: C92 (= C110), R154 (= R172), G215 (= G233), K216 (= K234), G217 (= G235), M241 (= M259), G274 (= G292), A275 (= A293), R276 (= R294), D300 (= D319), I301 (= I320), D319 (= D338), I320 (= I339)
- binding coenzyme a: A258 (= A276), R260 (= R278), A261 (≠ S279), L280 (= L298), N352 (= N372), K353 (≠ I373), L356 (≠ M376), L398 (= L416), R402 (= R420), M403 (≠ G421), R549 (≠ N569), I550 (= I570)
- binding magnesium ion: D446 (= D464), N473 (= N491), G475 (= G493)
- binding thiamine diphosphate: E50 (= E68), V73 (= V91), Y371 (≠ F389), A395 (= A413), N396 (= N414), A397 (≠ T415), M422 (= M440), G445 (= G463), D446 (= D464), S447 (= S465), A448 (= A466), F451 (= F469), N473 (= N491), G475 (= G493), I476 (= I494), Y477 (= Y495)
2ji8A X-ray structure of oxalyl-coa decarboxylase in complex with formyl- coa (see paper)
61% identity, 96% coverage: 21:579/585 of query aligns to 3:559/559 of 2ji8A
- active site: V25 (= V43), G27 (= G45), I28 (= I46), P29 (= P47), I30 (= I48), E50 (= E68), V73 (= V91), Y114 (= Y132), E115 (= E133), E116 (= E134), A164 (= A182), M281 (≠ L299), G394 (= G412), G420 (= G438), M422 (= M440), D446 (= D464), N473 (= N491), G475 (= G493), I476 (= I494), K478 (= K496), G479 (= G497), A482 (≠ S506), P541 (= P561)
- binding adenosine-5'-diphosphate: C92 (= C110), R154 (= R172), G215 (= G233), K216 (= K234), G217 (= G235), M241 (= M259), G274 (= G292), R276 (= R294), D300 (= D319), I301 (= I320), D319 (= D338), I320 (= I339)
- 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 (≠ G275), A258 (= A276), T259 (≠ A277), R260 (= R278), A261 (≠ S279), W279 (= W297), L280 (= L298), N352 (= N372), L356 (≠ M376), L398 (= L416), R402 (= R420), M403 (≠ G421), S547 (= S567), R549 (≠ N569), I550 (= I570)
- binding magnesium ion: D446 (= D464), N473 (= N491), G475 (= G493)
- binding thiamine diphosphate: Y371 (≠ F389), A395 (= A413), N396 (= N414), G420 (= G438), M422 (= M440), G445 (= G463), D446 (= D464), S447 (= S465), A448 (= A466), F451 (= F469), N473 (= N491), G475 (= G493), I476 (= I494), Y477 (= Y495)
2ji7A X-ray structure of oxalyl-coa decarboxylase with covalent reaction intermediate (see paper)
61% identity, 96% coverage: 21:579/585 of query aligns to 3:559/559 of 2ji7A
- active site: V25 (= V43), G27 (= G45), I28 (= I46), P29 (= P47), I30 (= I48), E50 (= E68), V73 (= V91), Y114 (= Y132), E115 (= E133), E116 (= E134), A164 (= A182), M281 (≠ L299), G394 (= G412), G420 (= G438), M422 (= M440), D446 (= D464), N473 (= N491), G475 (= G493), I476 (= I494), K478 (= K496), G479 (= G497), A482 (≠ S506), P541 (= P561)
- binding adenosine-5'-diphosphate: C92 (= C110), R154 (= R172), G215 (= G233), K216 (= K234), M241 (= M259), G274 (= G292), R276 (= R294), D300 (= D319), I301 (= I320), D319 (= D338), I320 (= I339)
- binding magnesium ion: D446 (= D464), N473 (= N491), G475 (= G493)
- 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 (= E68), V73 (= V91), Y114 (= Y132), E115 (= E133), A257 (≠ G275), A258 (= A276), T259 (≠ A277), R260 (= R278), A261 (≠ S279), L280 (= L298), N352 (= N372), L356 (≠ M376), Y371 (≠ F389), G394 (= G412), A395 (= A413), N396 (= N414), A397 (≠ T415), L398 (= L416), R402 (= R420), M403 (≠ G421), G420 (= G438), M422 (= M440), G445 (= G463), D446 (= D464), S447 (= S465), A448 (= A466), F451 (= F469), N473 (= N491), G475 (= G493), Y477 (= Y495), R549 (≠ N569), I550 (= I570)
2ji6A X-ray structure of oxalyl-coa decarboxylase in complex with 3-deaza- thdp and oxalyl-coa (see paper)
61% identity, 96% coverage: 21:579/585 of query aligns to 3:559/559 of 2ji6A
- active site: V25 (= V43), G27 (= G45), I28 (= I46), P29 (= P47), I30 (= I48), E50 (= E68), V73 (= V91), Y114 (= Y132), E115 (= E133), E116 (= E134), A164 (= A182), M281 (≠ L299), G394 (= G412), G420 (= G438), M422 (= M440), D446 (= D464), N473 (= N491), G475 (= G493), I476 (= I494), K478 (= K496), G479 (= G497), A482 (≠ S506), P541 (= P561)
- binding adenosine-5'-diphosphate: C92 (= C110), R154 (= R172), G215 (= G233), K216 (= K234), G217 (= G235), M241 (= M259), G274 (= G292), A275 (= A293), R276 (= R294), D300 (= D319), I301 (= I320), D319 (= D338), I320 (= I339)
- binding magnesium ion: D446 (= D464), N473 (= N491), G475 (= G493)
- binding oxalyl-coenzyme a: G27 (= G45), I28 (= I46), Y114 (= Y132), A257 (≠ G275), A258 (= A276), T259 (≠ A277), R260 (= R278), A261 (≠ S279), L280 (= L298), N352 (= N372), K353 (≠ I373), L356 (≠ M376), L398 (= L416), R402 (= R420), M403 (≠ G421), M422 (= M440), Y477 (= Y495), S547 (= S567), R549 (≠ N569), I550 (= I570)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: V26 (≠ P44), E50 (= E68), P76 (= P94), Y371 (≠ F389), A395 (= A413), N396 (= N414), A397 (≠ T415), M422 (= M440), G445 (= G463), D446 (= D464), S447 (= S465), A448 (= A466), F451 (= F469), N473 (= N491), G475 (= G493), I476 (= I494), Y477 (= Y495)
P0AFI0 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Escherichia coli (strain K12) (see paper)
61% identity, 95% coverage: 21:575/585 of query aligns to 7:558/564 of P0AFI0
- R158 (= R172) binding
- K220 (= K234) binding
- R280 (= R294) binding
- D302 (= D319) binding
- I322 (= I339) binding
- Y372 (≠ F389) binding
- D447 (= D464) binding
- N474 (= N491) binding
- G476 (= G493) binding
- Y478 (= Y495) binding
2c31A Crystal structure of oxalyl-coa decarboxylase in complex with the cofactor derivative thiamin-2-thiazolone diphosphate and adenosine diphosphate (see paper)
61% identity, 93% coverage: 21:566/585 of query aligns to 3:546/546 of 2c31A
- active site: V25 (= V43), G27 (= G45), I28 (= I46), P29 (= P47), I30 (= I48), E50 (= E68), V73 (= V91), Y114 (= Y132), E115 (= E133), E116 (= E134), A164 (= A182), M281 (≠ L299), G394 (= G412), G420 (= G438), M422 (= M440), D446 (= D464), N473 (= N491), G475 (= G493), I476 (= I494), K478 (= K496), G479 (= G497), A482 (≠ S506), P541 (= P561)
- binding adenosine-5'-diphosphate: C92 (= C110), R154 (= R172), G215 (= G233), K216 (= K234), G217 (= G235), M241 (= M259), G274 (= G292), A275 (= A293), R276 (= R294), D300 (= D319), I301 (= I320), D319 (= D338), I320 (= I339)
- binding magnesium ion: D446 (= D464), N473 (= N491), G475 (= G493)
- 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 (≠ P44), E50 (= E68), Y371 (≠ F389), A395 (= A413), N396 (= N414), A397 (≠ T415), M422 (= M440), G445 (= G463), D446 (= D464), S447 (= S465), A448 (= A466), F451 (= F469), N473 (= N491), G475 (= G493), I476 (= I494), Y477 (= Y495)
2q28A Crystal structure of oxalyl-coa decarboxylase from escherichia coli in complex with adenosine-5`-diphosphate (see paper)
61% identity, 94% coverage: 21:570/585 of query aligns to 3:549/550 of 2q28A
- active site: V25 (= V43), G27 (= G45), I28 (= I46), P29 (= P47), V30 (≠ I48), E50 (= E68), V73 (= V91), Y114 (= Y132), E115 (= E133), E116 (= E134), A164 (= A182), L281 (= L299), G391 (= G412), G417 (= G438), M419 (= M440), D443 (= D464), N470 (= N491), G472 (= G493), I473 (= I494), R475 (≠ K496), G476 (= G497), V479 (= V500), P540 (= P561)
- binding adenosine-5'-diphosphate: R154 (= R172), G215 (= G233), K216 (= K234), G217 (= G235), M241 (= M259), G274 (= G292), R276 (= R294), D298 (= D319), I299 (= I320), D317 (= D338), I318 (= I339)
- binding magnesium ion: D443 (= D464), N470 (= N491), G472 (= G493)
- binding thiamine diphosphate: Y368 (≠ F389), G391 (= G412), A392 (= A413), N393 (= N414), T394 (= T415), M419 (= M440), G442 (= G463), D443 (= D464), S444 (= S465), A445 (= A466), F448 (= F469), N470 (= N491), G472 (= G493), I473 (= I494), Y474 (= Y495)
2q29A Crystal structure of oxalyl-coa decarboxylase from escherichia coli in complex with acetyl coenzyme a (see paper)
61% identity, 94% coverage: 21:567/585 of query aligns to 3:546/546 of 2q29A
- active site: V25 (= V43), G27 (= G45), I28 (= I46), P29 (= P47), V30 (≠ I48), E50 (= E68), V73 (= V91), Y114 (= Y132), E115 (= E133), E116 (= E134), A164 (= A182), L281 (= L299), G391 (= G412), G417 (= G438), M419 (= M440), D443 (= D464), N470 (= N491), G472 (= G493), I473 (= I494), R475 (≠ K496), G476 (= G497), V479 (= V500), P540 (= P561)
- binding acetyl coenzyme *a: A257 (≠ G275), A258 (= A276), R260 (= R278), S261 (= S279), N351 (= N372), M355 (= M376), N400 (≠ G421)
- binding magnesium ion: D443 (= D464), N470 (= N491), G472 (= G493)
- binding thiamine diphosphate: Y368 (≠ F389), A392 (= A413), N393 (= N414), T394 (= T415), M419 (= M440), G442 (= G463), D443 (= D464), S444 (= S465), A445 (= A466), F448 (= F469), N470 (= N491), G472 (= G493), I473 (= I494), Y474 (= Y495)
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, 94% coverage: 24:574/585 of query aligns to 16:574/578 of Q9UJ83
- D455 (= D464) 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 (= S465) 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, 92% coverage: 22:559/585 of query aligns to 4:537/540 of 6xn8A
- active site: V25 (= V43), G27 (= G45), F28 (≠ I46), P29 (= P47), I30 (= I48), E50 (= E68), V73 (= V91), F112 (≠ Y132), Q113 (≠ E133), E114 (= E134), D162 (≠ A182), F277 (≠ L299), G388 (= G412), G414 (= G438), M416 (= M440), D441 (= D464), N468 (= N491), G470 (= G493), I471 (= I494), P473 (≠ K496), G474 (= G497), E477 (vs. gap)
- binding adenosine-5'-diphosphate: R152 (= R172), G211 (= G233), K212 (= K234), S237 (≠ M259), G270 (= G292), R272 (= R294), D295 (= D319), I296 (= I320), G313 (= G337), D314 (= D338), G315 (≠ I339)
- binding magnesium ion: D441 (= D464), N468 (= N491), G470 (= G493)
- 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 (= E68), V73 (= V91), P76 (= P94), H80 (≠ N98), Y367 (≠ F389), A389 (= A413), G390 (≠ N414), T391 (= T415), G414 (= G438), M416 (= M440), G440 (= G463), D441 (= D464), S442 (= S465), A443 (= A466), F446 (= F469), N468 (= N491), G470 (= G493), I471 (= I494), G472 (≠ Y495)
P39994 Putative 2-hydroxyacyl-CoA lyase; Peroxisomal protein 1; EC 4.1.-.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
33% identity, 92% coverage: 22:561/585 of query aligns to 3:544/560 of P39994
Sites not aligning to the query:
- 558:560 Peroxisomal target signal 1 (PTS1)
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)
29% identity, 93% coverage: 27:571/585 of query aligns to 10:551/584 of 7pt4B
- binding magnesium ion: D446 (= D464), N473 (= N491), A475 (≠ G493)
- 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 (≠ A276), R259 (= R278), S260 (= S279), Q279 (≠ L298), Y352 (≠ A374), G395 (= G412), G396 (≠ A413), D397 (≠ N414), L398 (≠ T415), L399 (= L416), R403 (= R420), L404 (≠ I423), G419 (= G438), L421 (≠ M440), G445 (= G463), D446 (= D464), G447 (≠ S465), A448 (= A466), N473 (= N491), A475 (≠ G493), W476 (vs. gap), N477 (vs. gap), I478 (= I494), E479 (≠ Y495), D547 (≠ S567)
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
7pt1A Actinobacterial 2-hydroxyacyl-coa lyase (achacl) structure in complex with substrate 2-hib-coa and inactive cofactor 3-deaza-thdp (see paper)
29% identity, 93% coverage: 27:571/585 of query aligns to 10:551/574 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 (≠ Y132), Q114 (≠ E133), G256 (= G275), S257 (≠ A276), R259 (= R278), S260 (= S279), Q279 (≠ L298), Y352 (≠ A374), R403 (= R420), L404 (≠ I423), G419 (= G438), D547 (≠ S567)
- binding magnesium ion: D446 (= D464), N473 (= N491), A475 (≠ G493)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: E51 (= E68), T74 (≠ V91), P77 (= P94), G396 (≠ A413), D397 (≠ N414), L398 (≠ T415), G419 (= G438), L421 (≠ M440), G445 (= G463), D446 (= D464), G447 (≠ S465), A448 (= A466), N473 (= N491), A475 (≠ G493), W476 (vs. gap), N477 (vs. gap), I478 (= I494), E479 (≠ Y495)
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)
29% identity, 92% coverage: 27:565/585 of query aligns to 24:559/590 of P0DUV9
- G43 (≠ I46) binding
- Q255 (≠ S260) binding
- RS 273:274 (= RS 278:279) binding
- R362 (≠ E370) binding
- GDL 410:412 (≠ ANT 413:415) binding
- R417 (= R420) binding
- G433 (= G438) binding
- D460 (= D464) binding
- GA 461:462 (≠ SA 465:466) binding
- N487 (= N491) binding
- NRAWNI 487:492 (≠ NNG--I 491:494) binding
- A489 (≠ G493) binding
- E493 (≠ Y495) 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
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)
29% identity, 92% coverage: 27:565/585 of query aligns to 10:545/580 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 (≠ S260), G256 (= G275), S257 (≠ A276), R259 (= R278), S260 (= S279), Y278 (≠ W297), Q279 (≠ L298), Y352 (≠ A374), R403 (= R420), L404 (≠ I423)
- binding magnesium ion: D446 (= D464), N473 (= N491), A475 (≠ G493)
- binding thiamine diphosphate: G396 (≠ A413), D397 (≠ N414), L398 (≠ T415), G419 (= G438), L421 (≠ M440), G445 (= G463), D446 (= D464), G447 (≠ S465), A448 (= A466), N473 (= N491), A475 (≠ G493), W476 (vs. gap), N477 (vs. gap), I478 (= I494), E479 (≠ Y495)
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
4qq8C Crystal structure of the formolase fls in space group p 43 21 2 (see paper)
29% identity, 93% coverage: 20:561/585 of query aligns to 1:547/569 of 4qq8C
- active site: L24 (≠ V43), G26 (= G45), I27 (= I46), H28 (≠ P47), I29 (= I48), E49 (= E68), T72 (≠ V91), L111 (= L127), Q112 (= Q128), A113 (≠ Q129), G114 (= G130), W162 (≠ A182), L255 (≠ A276), T283 (≠ L299), G392 (= G412), N418 (≠ G438), M420 (= M440), D447 (= D464), N474 (= N491), S476 (≠ G493), W477 (≠ I494), W479 (vs. gap), T480 (vs. gap), F483 (≠ Y495), L545 (vs. gap)
- binding magnesium ion: D447 (= D464), N474 (= N491), S476 (≠ G493)
- binding thiamine diphosphate: H25 (≠ P44), E49 (= E68), Q112 (= Q128), G392 (= G412), G393 (≠ A413), L394 (≠ N414), T395 (= T415), N418 (≠ G438), M420 (= M440), G446 (= G463), D447 (= D464), G448 (≠ S465), S449 (≠ A466), Y452 (≠ F469), N474 (= N491), S476 (≠ G493), W477 (≠ I494), G478 (vs. gap), W479 (vs. gap), T480 (vs. gap)
3d7kA Crystal structure of benzaldehyde lyase in complex with the inhibitor mbp (see paper)
29% identity, 93% coverage: 20:561/585 of query aligns to 1:547/554 of 3d7kA
- active site: L24 (≠ V43), G26 (= G45), A27 (≠ I46), H28 (≠ P47), I29 (= I48), E49 (= E68), T72 (≠ V91), L111 (= L127), Q112 (= Q128), A113 (≠ Q129), G114 (= G130), W162 (≠ A182), L255 (≠ A276), T283 (≠ L299), G392 (= G412), G418 (= G438), M420 (= M440), D447 (= D464), N474 (= N491), S476 (≠ G493), W477 (≠ I494), A479 (≠ K496), T480 (≠ G497), F483 (≠ V500), L545 (vs. gap)
- binding calcium ion: D447 (= D464), N474 (= N491), S476 (≠ G493)
- 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 (≠ P44), G26 (= G45), A27 (≠ I46), E49 (= E68), T72 (≠ V91), Q112 (= Q128), G392 (= G412), A393 (= A413), L394 (≠ N414), T395 (= T415), G418 (= G438), M420 (= M440), G446 (= G463), D447 (= D464), G448 (≠ S465), S449 (≠ A466), Y452 (≠ F469), N474 (= N491), S476 (≠ G493), W477 (≠ I494), G478 (≠ Y495), A479 (≠ K496), T480 (≠ G497)
4rjkG Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
26% identity, 92% coverage: 24:560/585 of query aligns to 3:532/553 of 4rjkG
- binding magnesium ion: D437 (= D464), D464 (≠ N491), T466 (vs. gap)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-(1-carboxy-1-hydroxyethyl)-5-(2-{[hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: E47 (= E68), Q110 (≠ E133)
- binding thiamine diphosphate: I384 (≠ E411), G385 (= G412), S386 (≠ A413), H387 (≠ N414), Q410 (≠ G438), L412 (≠ M440), G436 (= G463), D437 (= D464), G438 (≠ S465), G439 (≠ A466), T466 (vs. gap), Y467 (vs. gap), D468 (vs. gap), M469 (vs. gap), V470 (vs. gap)
Sites not aligning to the query:
Query Sequence
>AZOBR_RS31945 FitnessBrowser__azobra:AZOBR_RS31945
MSAVTVLNNQATAATDAEPALTDGFQLVIDALKLNGIENLYVVPGIPISDLLRMAQGEGL
RVISFRHEQNAGNAAAIAGFLTKKPGVCMTVSAPGFLNGLTALANATTNCFPMILISGSS
EREIVDLQQGDYEEMDQLAIAKPLCKAAFRVLHAQDIGIAVARAIRAAVSGRPGGVYLDL
PAKLFSQVMDAAEGARSLVKVVDAAPAQLPSPDSVARALEVLKGAKRPLIILGKGAAYAQ
ADEAVRELVEKSGIPFLPMSMAKGLLPDTHPQSAGAARSMVLKDADVVVLVGARLNWLLS
HGKGKTWGEPGSKTFIQIDIEPREMDSNVAIVAPLVGDIGSCVSALTAGMAKGWTPPPAE
WTGAVSARKEANIAKMAPKLMSNASPMNFHGALGALRRVVQERPEALLVNEGANTLDLAR
GIIDMHQPRKRLDVGTWGVMGIGMGFAVAAAVESGKPVLAVEGDSAFGFSGMEVETICRY
NLPVCIVVFNNNGIYKGTDVNPTGGSDPSPMVFVPDSRYDKMMEAFGGAGVNVTTPDELY
RAVSAAMDSGRPTLINAVIDPNAGSESGNIGSLNPTSAVRKGPKT
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