SitesBLAST
Comparing WP_012168999.1 NCBI__GCF_000010525.1:WP_012168999.1 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)
87% identity, 94% coverage: 17:562/579 of query aligns to 2:547/548 of 7b2eA
- active site: V25 (= V40), G27 (= G42), I28 (= I43), P29 (= P44), I30 (= I45), E50 (= E65), V73 (= V88), Y114 (= Y129), G115 (≠ E130), A164 (= A179), L281 (= L296), G394 (= G409), G420 (= G435), M422 (= M437), I476 (= I491), R478 (= R493), G479 (= G494), T482 (= T497)
- binding adenosine-5'-diphosphate: C92 (= C107), R154 (= R169), G215 (= G230), K216 (= K231), G217 (= G232), M241 (= M256), G274 (= G289), R276 (= R291), D301 (= D316), I302 (= I317), D320 (= D335), I321 (= I336)
- binding magnesium ion: D446 (= D461), N473 (= N488), G475 (= G490)
- binding thiamine diphosphate: F371 (= F386), C395 (≠ A410), N396 (= N411), T397 (= T412), G420 (= G435), M422 (= M437), G445 (= G460), D446 (= D461), S447 (= S462), A448 (= A463), F451 (= F466), N473 (= N488), G475 (= G490), I476 (= I491), F477 (≠ Y492)
P40149 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Oxalobacter formigenes (see 2 papers)
62% identity, 98% coverage: 13:578/579 of query aligns to 4:568/568 of P40149
- E56 (= E65) mutation to A: Loss of the decarboxylase activity. The mutant forms a dimer and not a tetramer.
- Y120 (= Y129) 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 (= E130) 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 (= R169) binding
- K222 (= K231) binding
- R282 (= R291) binding
- D306 (= D316) binding
- I326 (= I336) binding
- Y377 (≠ F386) binding
- D452 (= D461) binding
- N479 (= N488) binding
- G481 (= G490) binding
- Y483 (= Y492) 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 (= S563) mutation to A: Does not affect oxalyl-CoA binding, but it reduces 7-fold the catalytic efficiency for oxalyl-CoA.
- R555 (≠ N565) 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, 97% coverage: 17:575/579 of query aligns to 2:559/559 of 2jibA
- active site: V25 (= V40), G27 (= G42), I28 (= I43), P29 (= P44), I30 (= I45), E50 (= E65), V73 (= V88), Y114 (= Y129), E115 (= E130), E116 (= E131), A164 (= A179), M281 (≠ L296), G394 (= G409), G420 (= G435), M422 (= M437), D446 (= D461), N473 (= N488), G475 (= G490), I476 (= I491), K478 (≠ R493), G479 (= G494), A482 (≠ T497), P541 (= P557)
- binding adenosine-5'-diphosphate: C92 (= C107), R154 (= R169), G215 (= G230), K216 (= K231), G217 (= G232), M241 (= M256), G274 (= G289), A275 (= A290), R276 (= R291), D300 (= D316), I301 (= I317), D319 (= D335), I320 (= I336)
- binding coenzyme a: A258 (= A273), R260 (= R275), A261 (≠ S276), L280 (= L295), N352 (= N369), K353 (≠ I370), L356 (≠ M373), L398 (= L413), R402 (= R417), M403 (≠ G418), R549 (≠ N565), I550 (= I566)
- binding magnesium ion: D446 (= D461), N473 (= N488), G475 (= G490)
- binding thiamine diphosphate: E50 (= E65), V73 (= V88), Y371 (≠ F386), A395 (= A410), N396 (= N411), A397 (≠ T412), M422 (= M437), G445 (= G460), D446 (= D461), S447 (= S462), A448 (= A463), F451 (= F466), N473 (= N488), G475 (= G490), I476 (= I491), Y477 (= Y492)
2ji8A X-ray structure of oxalyl-coa decarboxylase in complex with formyl- coa (see paper)
63% identity, 97% coverage: 17:575/579 of query aligns to 2:559/559 of 2ji8A
- active site: V25 (= V40), G27 (= G42), I28 (= I43), P29 (= P44), I30 (= I45), E50 (= E65), V73 (= V88), Y114 (= Y129), E115 (= E130), E116 (= E131), A164 (= A179), M281 (≠ L296), G394 (= G409), G420 (= G435), M422 (= M437), D446 (= D461), N473 (= N488), G475 (= G490), I476 (= I491), K478 (≠ R493), G479 (= G494), A482 (≠ T497), P541 (= P557)
- binding adenosine-5'-diphosphate: C92 (= C107), R154 (= R169), G215 (= G230), K216 (= K231), G217 (= G232), M241 (= M256), G274 (= G289), R276 (= R291), D300 (= D316), I301 (= I317), D319 (= D335), I320 (= I336)
- 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 (≠ G272), A258 (= A273), T259 (≠ A274), R260 (= R275), A261 (≠ S276), W279 (= W294), L280 (= L295), N352 (= N369), L356 (≠ M373), L398 (= L413), R402 (= R417), M403 (≠ G418), S547 (= S563), R549 (≠ N565), I550 (= I566)
- binding magnesium ion: D446 (= D461), N473 (= N488), G475 (= G490)
- binding thiamine diphosphate: Y371 (≠ F386), A395 (= A410), N396 (= N411), G420 (= G435), M422 (= M437), G445 (= G460), D446 (= D461), S447 (= S462), A448 (= A463), F451 (= F466), N473 (= N488), G475 (= G490), I476 (= I491), Y477 (= Y492)
2ji7A X-ray structure of oxalyl-coa decarboxylase with covalent reaction intermediate (see paper)
63% identity, 97% coverage: 17:575/579 of query aligns to 2:559/559 of 2ji7A
- active site: V25 (= V40), G27 (= G42), I28 (= I43), P29 (= P44), I30 (= I45), E50 (= E65), V73 (= V88), Y114 (= Y129), E115 (= E130), E116 (= E131), A164 (= A179), M281 (≠ L296), G394 (= G409), G420 (= G435), M422 (= M437), D446 (= D461), N473 (= N488), G475 (= G490), I476 (= I491), K478 (≠ R493), G479 (= G494), A482 (≠ T497), P541 (= P557)
- binding adenosine-5'-diphosphate: C92 (= C107), R154 (= R169), G215 (= G230), K216 (= K231), M241 (= M256), G274 (= G289), R276 (= R291), D300 (= D316), I301 (= I317), D319 (= D335), I320 (= I336)
- binding magnesium ion: D446 (= D461), N473 (= N488), G475 (= G490)
- 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 (= E65), V73 (= V88), Y114 (= Y129), E115 (= E130), A257 (≠ G272), A258 (= A273), T259 (≠ A274), R260 (= R275), A261 (≠ S276), L280 (= L295), N352 (= N369), L356 (≠ M373), Y371 (≠ F386), G394 (= G409), A395 (= A410), N396 (= N411), A397 (≠ T412), L398 (= L413), R402 (= R417), M403 (≠ G418), G420 (= G435), M422 (= M437), G445 (= G460), D446 (= D461), S447 (= S462), A448 (= A463), F451 (= F466), N473 (= N488), G475 (= G490), Y477 (= Y492), R549 (≠ N565), I550 (= I566)
2ji6A X-ray structure of oxalyl-coa decarboxylase in complex with 3-deaza- thdp and oxalyl-coa (see paper)
63% identity, 97% coverage: 17:575/579 of query aligns to 2:559/559 of 2ji6A
- active site: V25 (= V40), G27 (= G42), I28 (= I43), P29 (= P44), I30 (= I45), E50 (= E65), V73 (= V88), Y114 (= Y129), E115 (= E130), E116 (= E131), A164 (= A179), M281 (≠ L296), G394 (= G409), G420 (= G435), M422 (= M437), D446 (= D461), N473 (= N488), G475 (= G490), I476 (= I491), K478 (≠ R493), G479 (= G494), A482 (≠ T497), P541 (= P557)
- binding adenosine-5'-diphosphate: C92 (= C107), R154 (= R169), G215 (= G230), K216 (= K231), G217 (= G232), M241 (= M256), G274 (= G289), A275 (= A290), R276 (= R291), D300 (= D316), I301 (= I317), D319 (= D335), I320 (= I336)
- binding magnesium ion: D446 (= D461), N473 (= N488), G475 (= G490)
- binding oxalyl-coenzyme a: G27 (= G42), I28 (= I43), Y114 (= Y129), A257 (≠ G272), A258 (= A273), T259 (≠ A274), R260 (= R275), A261 (≠ S276), L280 (= L295), N352 (= N369), K353 (≠ I370), L356 (≠ M373), L398 (= L413), R402 (= R417), M403 (≠ G418), M422 (= M437), Y477 (= Y492), S547 (= S563), R549 (≠ N565), I550 (= I566)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: V26 (≠ P41), E50 (= E65), P76 (= P91), Y371 (≠ F386), A395 (= A410), N396 (= N411), A397 (≠ T412), M422 (= M437), G445 (= G460), D446 (= D461), S447 (= S462), A448 (= A463), F451 (= F466), N473 (= N488), G475 (= G490), I476 (= I491), Y477 (= Y492)
2c31A Crystal structure of oxalyl-coa decarboxylase in complex with the cofactor derivative thiamin-2-thiazolone diphosphate and adenosine diphosphate (see paper)
63% identity, 94% coverage: 17:562/579 of query aligns to 2:546/546 of 2c31A
- active site: V25 (= V40), G27 (= G42), I28 (= I43), P29 (= P44), I30 (= I45), E50 (= E65), V73 (= V88), Y114 (= Y129), E115 (= E130), E116 (= E131), A164 (= A179), M281 (≠ L296), G394 (= G409), G420 (= G435), M422 (= M437), D446 (= D461), N473 (= N488), G475 (= G490), I476 (= I491), K478 (≠ R493), G479 (= G494), A482 (≠ T497), P541 (= P557)
- binding adenosine-5'-diphosphate: C92 (= C107), R154 (= R169), G215 (= G230), K216 (= K231), G217 (= G232), M241 (= M256), G274 (= G289), A275 (= A290), R276 (= R291), D300 (= D316), I301 (= I317), D319 (= D335), I320 (= I336)
- binding magnesium ion: D446 (= D461), N473 (= N488), G475 (= G490)
- 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 (≠ P41), E50 (= E65), Y371 (≠ F386), A395 (= A410), N396 (= N411), A397 (≠ T412), M422 (= M437), G445 (= G460), D446 (= D461), S447 (= S462), A448 (= A463), F451 (= F466), N473 (= N488), G475 (= G490), I476 (= I491), Y477 (= Y492)
P0AFI0 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Escherichia coli (strain K12) (see paper)
62% identity, 97% coverage: 15:574/579 of query aligns to 4:561/564 of P0AFI0
- R158 (= R169) binding
- K220 (= K231) binding
- R280 (= R291) binding
- D302 (= D316) binding
- I322 (= I336) binding
- Y372 (≠ F386) binding
- D447 (= D461) binding
- N474 (= N488) binding
- G476 (= G490) binding
- Y478 (= Y492) binding
2q28A Crystal structure of oxalyl-coa decarboxylase from escherichia coli in complex with adenosine-5`-diphosphate (see paper)
62% identity, 95% coverage: 17:566/579 of query aligns to 2:549/550 of 2q28A
- active site: V25 (= V40), G27 (= G42), I28 (= I43), P29 (= P44), V30 (≠ I45), E50 (= E65), V73 (= V88), Y114 (= Y129), E115 (= E130), E116 (= E131), A164 (= A179), L281 (= L296), G391 (= G409), G417 (= G435), M419 (= M437), D443 (= D461), N470 (= N488), G472 (= G490), I473 (= I491), R475 (= R493), G476 (= G494), V479 (≠ T497), P540 (= P557)
- binding adenosine-5'-diphosphate: R154 (= R169), G215 (= G230), K216 (= K231), G217 (= G232), M241 (= M256), G274 (= G289), R276 (= R291), D298 (= D316), I299 (= I317), D317 (= D335), I318 (= I336)
- binding magnesium ion: D443 (= D461), N470 (= N488), G472 (= G490)
- binding thiamine diphosphate: Y368 (≠ F386), G391 (= G409), A392 (= A410), N393 (= N411), T394 (= T412), M419 (= M437), G442 (= G460), D443 (= D461), S444 (= S462), A445 (= A463), F448 (= F466), N470 (= N488), G472 (= G490), I473 (= I491), Y474 (= Y492)
2q29A Crystal structure of oxalyl-coa decarboxylase from escherichia coli in complex with acetyl coenzyme a (see paper)
62% identity, 94% coverage: 17:563/579 of query aligns to 2:546/546 of 2q29A
- active site: V25 (= V40), G27 (= G42), I28 (= I43), P29 (= P44), V30 (≠ I45), E50 (= E65), V73 (= V88), Y114 (= Y129), E115 (= E130), E116 (= E131), A164 (= A179), L281 (= L296), G391 (= G409), G417 (= G435), M419 (= M437), D443 (= D461), N470 (= N488), G472 (= G490), I473 (= I491), R475 (= R493), G476 (= G494), V479 (≠ T497), P540 (= P557)
- binding acetyl coenzyme *a: A257 (≠ G272), A258 (= A273), R260 (= R275), S261 (= S276), N351 (= N369), M355 (= M373), N400 (≠ G418)
- binding magnesium ion: D443 (= D461), N470 (= N488), G472 (= G490)
- binding thiamine diphosphate: Y368 (≠ F386), A392 (= A410), N393 (= N411), T394 (= T412), M419 (= M437), G442 (= G460), D443 (= D461), S444 (= S462), A445 (= A463), F448 (= F466), N470 (= N488), G472 (= G490), I473 (= I491), Y474 (= Y492)
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)
41% identity, 97% coverage: 12:570/579 of query aligns to 7:574/578 of Q9UJ83
- D455 (= D461) 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 (= S462) mutation to R: Does not affect subcellular localization. Abolishes lyase activity. Does not affect subcellular localization, abolishes lyase activity, does not affect oligomerisation and does not bind TTP; when associated with S-455.
Sites not aligning to the query:
- 576:578 Microbody targeting signal
6xn8A Crystal structure of 2-hydroxyacyl coa lyase (hacl) from rhodospirillales bacterium urhd0017
39% identity, 93% coverage: 19:555/579 of query aligns to 4:537/540 of 6xn8A
- active site: V25 (= V40), G27 (= G42), F28 (≠ I43), P29 (= P44), I30 (= I45), E50 (= E65), V73 (= V88), F112 (≠ Y129), Q113 (≠ E130), E114 (= E131), D162 (≠ A179), F277 (≠ L296), G388 (= G409), G414 (= G435), M416 (= M437), D441 (= D461), N468 (= N488), G470 (= G490), I471 (= I491), P473 (≠ R493), G474 (= G494), E477 (≠ T497)
- binding adenosine-5'-diphosphate: R152 (= R169), G211 (= G230), K212 (= K231), S237 (≠ M256), G270 (= G289), R272 (= R291), D295 (= D316), I296 (= I317), G313 (= G334), D314 (= D335), G315 (= G337)
- binding magnesium ion: D441 (= D461), N468 (= N488), G470 (= G490)
- 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 (= E65), V73 (= V88), P76 (= P91), H80 (≠ N95), Y367 (≠ F386), A389 (= A410), G390 (≠ N411), T391 (= T412), G414 (= G435), M416 (= M437), G440 (= G460), D441 (= D461), S442 (= S462), A443 (= A463), F446 (= F466), N468 (= N488), G470 (= G490), I471 (= I491), G472 (≠ Y492)
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)
36% identity, 91% coverage: 29:557/579 of query aligns to 13:544/560 of P39994
Sites not aligning to the query:
- 558:560 Peroxisomal target signal 1 (PTS1)
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, 94% coverage: 24:565/579 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 (≠ S257), G256 (= G272), S257 (≠ A273), R259 (= R275), S260 (= S276), Y278 (≠ W294), Q279 (≠ L295), Y352 (≠ A371), R403 (= R417), L404 (≠ I420)
- binding magnesium ion: D446 (= D461), N473 (= N488), A475 (≠ G490)
- binding thiamine diphosphate: G396 (≠ A410), D397 (≠ N411), L398 (≠ T412), G419 (= G435), L421 (≠ M437), G445 (= G460), D446 (= D461), G447 (≠ S462), A448 (= A463), N473 (= N488), A475 (≠ G490), W476 (vs. gap), N477 (vs. gap), I478 (= I491), E479 (≠ Y492)
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)
29% identity, 94% coverage: 24:565/579 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 (≠ Y129), Q114 (≠ E130), G256 (= G272), S257 (≠ A273), R259 (= R275), S260 (= S276), Q279 (≠ L295), Y352 (≠ A371), R403 (= R417), L404 (≠ I420), G419 (= G435), D547 (≠ E562)
- binding magnesium ion: D446 (= D461), N473 (= N488), A475 (≠ G490)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: E51 (= E65), T74 (≠ V88), P77 (= P91), G396 (≠ A410), D397 (≠ N411), L398 (≠ T412), G419 (= G435), L421 (≠ M437), G445 (= G460), D446 (= D461), G447 (≠ S462), A448 (= A463), N473 (= N488), A475 (≠ G490), W476 (vs. gap), N477 (vs. gap), I478 (= I491), E479 (≠ Y492)
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
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, 94% coverage: 24:565/579 of query aligns to 10:550/584 of 7pt4B
- binding magnesium ion: D446 (= D461), N473 (= N488), A475 (≠ G490)
- 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 (≠ A273), R259 (= R275), S260 (= S276), Q279 (≠ L295), Y352 (≠ A371), G395 (= G409), G396 (≠ A410), D397 (≠ N411), L398 (≠ T412), L399 (= L413), R403 (= R417), L404 (≠ I420), G419 (= G435), L421 (≠ M437), G445 (= G460), D446 (= D461), G447 (≠ S462), A448 (= A463), N473 (= N488), A475 (≠ G490), W476 (vs. gap), N477 (vs. gap), I478 (= I491), E479 (≠ Y492), D547 (≠ E562)
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)
29% identity, 94% coverage: 24:565/579 of query aligns to 24:564/590 of P0DUV9
- G43 (≠ I43) binding
- Q255 (≠ S257) binding
- RS 273:274 (= RS 275:276) binding
- R362 (≠ E367) binding
- GDL 410:412 (≠ ANT 410:412) binding
- R417 (= R417) binding
- G433 (= G435) binding
- D460 (= D461) binding
- GA 461:462 (≠ SA 462:463) binding
- N487 (= N488) binding
- NRAWNI 487:492 (≠ NNG--I 488:491) binding
- A489 (≠ G490) binding
- E493 (≠ Y492) 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 562:565) binding
Sites not aligning to the query:
4qq8C Crystal structure of the formolase fls in space group p 43 21 2 (see paper)
31% identity, 93% coverage: 18:557/579 of query aligns to 2:547/569 of 4qq8C
- active site: L24 (≠ V40), G26 (= G42), I27 (= I43), H28 (≠ P44), I29 (= I45), E49 (= E65), T72 (≠ V88), L111 (= L124), Q112 (= Q125), A113 (≠ Q126), G114 (= G127), W162 (≠ A179), L255 (≠ A273), T283 (≠ L296), G392 (= G409), N418 (≠ G435), M420 (= M437), D447 (= D461), N474 (= N488), S476 (vs. gap), W477 (vs. gap), W479 (≠ I491), T480 (≠ Y492), F483 (≠ T495), L545 (vs. gap)
- binding magnesium ion: D447 (= D461), N474 (= N488), S476 (vs. gap)
- binding thiamine diphosphate: H25 (≠ P41), E49 (= E65), Q112 (= Q125), G392 (= G409), G393 (≠ A410), L394 (≠ N411), T395 (= T412), N418 (≠ G435), M420 (= M437), G446 (= G460), D447 (= D461), G448 (≠ S462), S449 (≠ A463), Y452 (≠ F466), N474 (= N488), S476 (vs. gap), W477 (vs. gap), G478 (= G490), W479 (≠ I491), T480 (≠ Y492)
3d7kA Crystal structure of benzaldehyde lyase in complex with the inhibitor mbp (see paper)
31% identity, 93% coverage: 18:557/579 of query aligns to 2:547/554 of 3d7kA
- active site: L24 (≠ V40), G26 (= G42), A27 (≠ I43), H28 (≠ P44), I29 (= I45), E49 (= E65), T72 (≠ V88), L111 (= L124), Q112 (= Q125), A113 (≠ Q126), G114 (= G127), W162 (≠ A179), L255 (≠ A273), T283 (≠ L296), G392 (= G409), G418 (= G435), M420 (= M437), D447 (= D461), N474 (= N488), S476 (vs. gap), W477 (vs. gap), A479 (≠ I491), T480 (≠ Y492), F483 (≠ T495), L545 (vs. gap)
- binding calcium ion: D447 (= D461), N474 (= N488), 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 (≠ P41), G26 (= G42), A27 (≠ I43), E49 (= E65), T72 (≠ V88), Q112 (= Q125), G392 (= G409), A393 (= A410), L394 (≠ N411), T395 (= T412), G418 (= G435), M420 (= M437), G446 (= G460), D447 (= D461), G448 (≠ S462), S449 (≠ A463), Y452 (≠ F466), N474 (= N488), S476 (vs. gap), W477 (vs. gap), G478 (= G490), A479 (≠ I491), T480 (≠ Y492)
6lpiB Crystal structure of ahas holo-enzyme (see paper)
28% identity, 81% coverage: 21:491/579 of query aligns to 8:458/539 of 6lpiB
- active site: I27 (≠ V40), G29 (= G42), G30 (vs. gap), S31 (vs. gap), I32 (vs. gap), E53 (= E65), C76 (≠ V88), F115 (≠ Y129), Q116 (≠ E130), E117 (= E131), K165 (≠ A179), M256 (vs. gap), A283 (≠ G299), V375 (vs. gap), G401 (= G435), M403 (= M437), D428 (= D461), N455 (= N488), A457 (≠ G490), L458 (≠ I491)
- binding flavin-adenine dinucleotide: R155 (= R169), G212 (= G230), G213 (≠ K231), G214 (= G232), T236 (≠ M256), L237 (≠ S257), M238 (= M258), L254 (vs. gap), M256 (vs. gap), H257 (vs. gap), G276 (= G289), A277 (= A290), R278 (= R291), D280 (≠ N293), R282 (≠ H298), A283 (≠ G299), D300 (= D316), I301 (= I317), D319 (= D335), V320 (≠ I336), M380 (≠ L413), G398 (= G432)
- binding magnesium ion: D428 (= D461), N455 (= N488)
- binding thiamine diphosphate: E53 (= E65), C76 (≠ V88), P79 (= P91), G376 (= G409), Q377 (≠ A410), H378 (≠ N411), G401 (= G435), M403 (= M437), G427 (= G460), D428 (= D461), G429 (≠ S462), S430 (≠ A463), M433 (≠ F466), N455 (= N488), A457 (≠ G490), L458 (≠ I491)
Sites not aligning to the query:
Query Sequence
>WP_012168999.1 NCBI__GCF_000010525.1:WP_012168999.1
MSAVAQRVETEADAQQELTDGFHLVIDALKLNGIETIYGVPGIPITDLGRMAQAEGIRVV
SFRHEQNAGNAAAIAGFLTKKPGVCLTVSAPGFLNGLTALANATTNCFPMILISGSSERE
IVDLQQGDYEEMDQLAIAKPLCKAAFRVLHAADIGIGVARAIRAAVSGRPGGVYLDLPAK
LFSQVMDAAAGEKSLVKVIDPAPAQIPGPAAVDRAINLLKGAKRPLIILGKGAAYAQADE
EIRAFVEKSGIPFLPMSMAKGLLPDTHPQSAGAARSTALKDSDVVILLGARLNWLLSHGK
GKTWGEPGSKQFIQVDIEPKEMDSNVEIAAPLVGDIGSVVSALLDRIDGSWQAPPADWIE
SIRSKKEANIAKMAPKLLKNSSPMDFHGALGSLKKVIAERPDAILVNEGANTLDLARGII
DMYQPRKRLDVGTWGVMGIGMGFAIAAAVETGKPVLAVEGDSAFGFSGMEVETICRYDLP
VTIVIFNNNGIYRGTDTDPTGRDPGTTVFVKDSRYDKMMEAFGGVGVNVTTPDELYRAVS
AAMDSGKPTLINAVIDPAAGSESGNIGSLNPQSVVVRKK
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