SitesBLAST
Comparing WP_012975779.1 NCBI__GCF_000010725.1:WP_012975779.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
7b2eA Quadruple mutant of oxalyl-coa decarboxylase from methylorubrum extorquens with bound tpp and adp (see paper)
81% identity, 93% coverage: 23:569/587 of query aligns to 1:547/548 of 7b2eA
- active site: V25 (= V47), G27 (= G49), I28 (= I50), P29 (= P51), I30 (= I52), E50 (= E72), V73 (= V95), Y114 (= Y136), G115 (≠ E137), A164 (= A186), L281 (= L303), G394 (= G415), G420 (= G441), M422 (= M443), I476 (= I497), R478 (= R499), G479 (= G500), T482 (= T503)
- binding adenosine-5'-diphosphate: C92 (= C114), R154 (= R176), G215 (= G237), K216 (= K238), G217 (= G239), M241 (= M263), G274 (= G296), R276 (= R298), D301 (= D323), I302 (= I324), D320 (= D342), I321 (= I343)
- binding magnesium ion: D446 (= D467), N473 (= N494), G475 (= G496)
- binding thiamine diphosphate: F371 (= F392), C395 (≠ A416), N396 (= N417), T397 (= T418), G420 (= G441), M422 (= M443), G445 (= G466), D446 (= D467), S447 (= S468), A448 (= A469), F451 (= F472), N473 (= N494), G475 (= G496), I476 (= I497), F477 (≠ Y498)
P40149 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Oxalobacter formigenes (see 2 papers)
61% identity, 96% coverage: 20:584/587 of query aligns to 4:567/568 of P40149
- E56 (= E72) mutation to A: Loss of the decarboxylase activity. The mutant forms a dimer and not a tetramer.
- Y120 (= Y136) 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 (= E137) 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 (= R176) binding ADP
- K222 (= K238) binding ADP
- R282 (= R298) binding ADP
- D306 (= D323) binding ADP
- I326 (= I343) binding ADP
- Y377 (≠ F392) binding thiamine diphosphate
- D452 (= D467) binding Mg(2+)
- N479 (= N494) binding Mg(2+)
- G481 (= G496) binding Mg(2+)
- Y483 (= Y498) binding thiamine diphosphate; mutation to A: Does not affect oxalyl-CoA binding, but it strongly reduces the catalytic efficiency for oxalyl-CoA.; mutation to F: 2-fold reduction in the affinity binding and strong reduction in the catalytic efficiency for oxalyl-CoA.
- S553 (= S570) mutation to A: Does not affect oxalyl-CoA binding, but it reduces 7-fold the catalytic efficiency for oxalyl-CoA.
- R555 (≠ N572) 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, 95% coverage: 25:582/587 of query aligns to 3:559/559 of 2jibA
- active site: V25 (= V47), G27 (= G49), I28 (= I50), P29 (= P51), I30 (= I52), E50 (= E72), V73 (= V95), Y114 (= Y136), E115 (= E137), E116 (= E138), A164 (= A186), M281 (≠ L303), G394 (= G415), G420 (= G441), M422 (= M443), D446 (= D467), N473 (= N494), G475 (= G496), I476 (= I497), K478 (≠ R499), G479 (= G500), A482 (= A509), P541 (= P564)
- binding adenosine-5'-diphosphate: C92 (= C114), R154 (= R176), G215 (= G237), K216 (= K238), G217 (= G239), M241 (= M263), G274 (= G296), A275 (= A297), R276 (= R298), D300 (= D323), I301 (= I324), D319 (= D342), I320 (= I343)
- binding coenzyme a: A258 (= A280), R260 (= R282), A261 (≠ S283), L280 (= L302), N352 (= N375), K353 (≠ V376), L356 (≠ M379), L398 (= L419), R402 (= R423), M403 (≠ G424), R549 (≠ N572), I550 (= I573)
- binding magnesium ion: D446 (= D467), N473 (= N494), G475 (= G496)
- binding thiamine diphosphate: E50 (= E72), V73 (= V95), Y371 (≠ F392), A395 (= A416), N396 (= N417), A397 (≠ T418), M422 (= M443), G445 (= G466), D446 (= D467), S447 (= S468), A448 (= A469), F451 (= F472), N473 (= N494), G475 (= G496), I476 (= I497), Y477 (= Y498)
2ji8A X-ray structure of oxalyl-coa decarboxylase in complex with formyl- coa (see paper)
61% identity, 95% coverage: 25:582/587 of query aligns to 3:559/559 of 2ji8A
- active site: V25 (= V47), G27 (= G49), I28 (= I50), P29 (= P51), I30 (= I52), E50 (= E72), V73 (= V95), Y114 (= Y136), E115 (= E137), E116 (= E138), A164 (= A186), M281 (≠ L303), G394 (= G415), G420 (= G441), M422 (= M443), D446 (= D467), N473 (= N494), G475 (= G496), I476 (= I497), K478 (≠ R499), G479 (= G500), A482 (= A509), P541 (= P564)
- binding adenosine-5'-diphosphate: C92 (= C114), R154 (= R176), G215 (= G237), K216 (= K238), G217 (= G239), M241 (= M263), G274 (= G296), R276 (= R298), D300 (= D323), I301 (= I324), D319 (= D342), I320 (= I343)
- 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 (≠ G279), A258 (= A280), T259 (≠ A281), R260 (= R282), A261 (≠ S283), W279 (= W301), L280 (= L302), N352 (= N375), L356 (≠ M379), L398 (= L419), R402 (= R423), M403 (≠ G424), S547 (= S570), R549 (≠ N572), I550 (= I573)
- binding magnesium ion: D446 (= D467), N473 (= N494), G475 (= G496)
- binding thiamine diphosphate: Y371 (≠ F392), A395 (= A416), N396 (= N417), G420 (= G441), M422 (= M443), G445 (= G466), D446 (= D467), S447 (= S468), A448 (= A469), F451 (= F472), N473 (= N494), G475 (= G496), I476 (= I497), Y477 (= Y498)
2ji7A X-ray structure of oxalyl-coa decarboxylase with covalent reaction intermediate (see paper)
61% identity, 95% coverage: 25:582/587 of query aligns to 3:559/559 of 2ji7A
- active site: V25 (= V47), G27 (= G49), I28 (= I50), P29 (= P51), I30 (= I52), E50 (= E72), V73 (= V95), Y114 (= Y136), E115 (= E137), E116 (= E138), A164 (= A186), M281 (≠ L303), G394 (= G415), G420 (= G441), M422 (= M443), D446 (= D467), N473 (= N494), G475 (= G496), I476 (= I497), K478 (≠ R499), G479 (= G500), A482 (= A509), P541 (= P564)
- binding adenosine-5'-diphosphate: C92 (= C114), R154 (= R176), G215 (= G237), K216 (= K238), M241 (= M263), G274 (= G296), R276 (= R298), D300 (= D323), I301 (= I324), D319 (= D342), I320 (= I343)
- binding magnesium ion: D446 (= D467), N473 (= N494), G475 (= G496)
- 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 (= E72), V73 (= V95), Y114 (= Y136), E115 (= E137), A257 (≠ G279), A258 (= A280), T259 (≠ A281), R260 (= R282), A261 (≠ S283), L280 (= L302), N352 (= N375), L356 (≠ M379), Y371 (≠ F392), G394 (= G415), A395 (= A416), N396 (= N417), A397 (≠ T418), L398 (= L419), R402 (= R423), M403 (≠ G424), G420 (= G441), M422 (= M443), G445 (= G466), D446 (= D467), S447 (= S468), A448 (= A469), F451 (= F472), N473 (= N494), G475 (= G496), Y477 (= Y498), R549 (≠ N572), I550 (= I573)
2ji6A X-ray structure of oxalyl-coa decarboxylase in complex with 3-deaza- thdp and oxalyl-coa (see paper)
61% identity, 95% coverage: 25:582/587 of query aligns to 3:559/559 of 2ji6A
- active site: V25 (= V47), G27 (= G49), I28 (= I50), P29 (= P51), I30 (= I52), E50 (= E72), V73 (= V95), Y114 (= Y136), E115 (= E137), E116 (= E138), A164 (= A186), M281 (≠ L303), G394 (= G415), G420 (= G441), M422 (= M443), D446 (= D467), N473 (= N494), G475 (= G496), I476 (= I497), K478 (≠ R499), G479 (= G500), A482 (= A509), P541 (= P564)
- binding adenosine-5'-diphosphate: C92 (= C114), R154 (= R176), G215 (= G237), K216 (= K238), G217 (= G239), M241 (= M263), G274 (= G296), A275 (= A297), R276 (= R298), D300 (= D323), I301 (= I324), D319 (= D342), I320 (= I343)
- binding magnesium ion: D446 (= D467), N473 (= N494), G475 (= G496)
- binding oxalyl-coenzyme a: G27 (= G49), I28 (= I50), Y114 (= Y136), A257 (≠ G279), A258 (= A280), T259 (≠ A281), R260 (= R282), A261 (≠ S283), L280 (= L302), N352 (= N375), K353 (≠ V376), L356 (≠ M379), L398 (= L419), R402 (= R423), M403 (≠ G424), M422 (= M443), Y477 (= Y498), S547 (= S570), R549 (≠ N572), I550 (= I573)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: V26 (≠ P48), E50 (= E72), P76 (= P98), Y371 (≠ F392), A395 (= A416), N396 (= N417), A397 (≠ T418), M422 (= M443), G445 (= G466), D446 (= D467), S447 (= S468), A448 (= A469), F451 (= F472), N473 (= N494), G475 (= G496), I476 (= I497), Y477 (= Y498)
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: 25:569/587 of query aligns to 3:546/546 of 2c31A
- active site: V25 (= V47), G27 (= G49), I28 (= I50), P29 (= P51), I30 (= I52), E50 (= E72), V73 (= V95), Y114 (= Y136), E115 (= E137), E116 (= E138), A164 (= A186), M281 (≠ L303), G394 (= G415), G420 (= G441), M422 (= M443), D446 (= D467), N473 (= N494), G475 (= G496), I476 (= I497), K478 (≠ R499), G479 (= G500), A482 (= A509), P541 (= P564)
- binding adenosine-5'-diphosphate: C92 (= C114), R154 (= R176), G215 (= G237), K216 (= K238), G217 (= G239), M241 (= M263), G274 (= G296), A275 (= A297), R276 (= R298), D300 (= D323), I301 (= I324), D319 (= D342), I320 (= I343)
- binding magnesium ion: D446 (= D467), N473 (= N494), G475 (= G496)
- 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 (≠ P48), E50 (= E72), Y371 (≠ F392), A395 (= A416), N396 (= N417), A397 (≠ T418), M422 (= M443), G445 (= G466), D446 (= D467), S447 (= S468), A448 (= A469), F451 (= F472), N473 (= N494), G475 (= G496), I476 (= I497), Y477 (= Y498)
P0AFI0 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Escherichia coli (strain K12) (see paper)
60% identity, 95% coverage: 19:578/587 of query aligns to 1:558/564 of P0AFI0
- R158 (= R176) binding ADP
- K220 (= K238) binding ADP
- R280 (= R298) binding ADP
- D302 (= D323) binding ADP
- I322 (= I343) binding ADP
- Y372 (≠ F392) binding thiamine diphosphate
- D447 (= D467) binding Mg(2+)
- N474 (= N494) binding Mg(2+)
- G476 (= G496) binding Mg(2+)
- Y478 (= Y498) binding thiamine diphosphate
2q28A Crystal structure of oxalyl-coa decarboxylase from escherichia coli in complex with adenosine-5`-diphosphate (see paper)
61% identity, 94% coverage: 25:573/587 of query aligns to 3:549/550 of 2q28A
- active site: V25 (= V47), G27 (= G49), I28 (= I50), P29 (= P51), V30 (≠ I52), E50 (= E72), V73 (= V95), Y114 (= Y136), E115 (= E137), E116 (= E138), A164 (= A186), L281 (= L303), G391 (= G415), G417 (= G441), M419 (= M443), D443 (= D467), N470 (= N494), G472 (= G496), I473 (= I497), R475 (= R499), G476 (= G500), V479 (≠ T503), P540 (= P564)
- binding adenosine-5'-diphosphate: R154 (= R176), G215 (= G237), K216 (= K238), G217 (= G239), M241 (= M263), G274 (= G296), R276 (= R298), D298 (= D323), I299 (= I324), D317 (= D342), I318 (= I343)
- binding magnesium ion: D443 (= D467), N470 (= N494), G472 (= G496)
- binding thiamine diphosphate: Y368 (≠ F392), G391 (= G415), A392 (= A416), N393 (= N417), T394 (= T418), M419 (= M443), G442 (= G466), D443 (= D467), S444 (= S468), A445 (= A469), F448 (= F472), N470 (= N494), G472 (= G496), I473 (= I497), Y474 (= Y498)
2q29A Crystal structure of oxalyl-coa decarboxylase from escherichia coli in complex with acetyl coenzyme a (see paper)
61% identity, 93% coverage: 25:570/587 of query aligns to 3:546/546 of 2q29A
- active site: V25 (= V47), G27 (= G49), I28 (= I50), P29 (= P51), V30 (≠ I52), E50 (= E72), V73 (= V95), Y114 (= Y136), E115 (= E137), E116 (= E138), A164 (= A186), L281 (= L303), G391 (= G415), G417 (= G441), M419 (= M443), D443 (= D467), N470 (= N494), G472 (= G496), I473 (= I497), R475 (= R499), G476 (= G500), V479 (≠ T503), P540 (= P564)
- binding acetyl coenzyme *a: A257 (≠ G279), A258 (= A280), R260 (= R282), S261 (= S283), N351 (= N375), M355 (= M379), N400 (≠ G424)
- binding magnesium ion: D443 (= D467), N470 (= N494), G472 (= G496)
- binding thiamine diphosphate: Y368 (≠ F392), A392 (= A416), N393 (= N417), T394 (= T418), M419 (= M443), G442 (= G466), D443 (= D467), S444 (= S468), A445 (= A469), F448 (= F472), N470 (= N494), G472 (= G496), I473 (= I497), Y474 (= Y498)
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)
38% identity, 96% coverage: 15:577/587 of query aligns to 3:574/578 of Q9UJ83
- D455 (= D467) 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 (= S468) 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
41% identity, 91% coverage: 26:562/587 of query aligns to 4:537/540 of 6xn8A
- active site: V25 (= V47), G27 (= G49), F28 (≠ I50), P29 (= P51), I30 (= I52), E50 (= E72), V73 (= V95), F112 (≠ Y136), Q113 (≠ E137), E114 (= E138), D162 (≠ A186), F277 (≠ L303), G388 (= G415), G414 (= G441), M416 (= M443), D441 (= D467), N468 (= N494), G470 (= G496), I471 (= I497), P473 (≠ R499), G474 (= G500), E477 (vs. gap)
- binding adenosine-5'-diphosphate: R152 (= R176), G211 (= G237), K212 (= K238), S237 (≠ M263), G270 (= G296), R272 (= R298), D295 (= D323), I296 (= I324), G313 (= G341), D314 (= D342), G315 (≠ I343)
- binding magnesium ion: D441 (= D467), N468 (= N494), G470 (= G496)
- 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 (= E72), V73 (= V95), P76 (= P98), H80 (≠ N102), Y367 (≠ F392), A389 (= A416), G390 (≠ N417), T391 (= T418), G414 (= G441), M416 (= M443), G440 (= G466), D441 (= D467), S442 (= S468), A443 (= A469), F446 (= F472), N468 (= N494), G470 (= G496), I471 (= I497), G472 (≠ Y498)
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)
33% identity, 89% coverage: 41:564/587 of query aligns to 18:544/560 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)
27% identity, 92% coverage: 31:572/587 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 (≠ S264), G256 (= G279), S257 (≠ A280), R259 (= R282), S260 (= S283), Y278 (≠ W301), Q279 (≠ L302), Y352 (≠ M379), R403 (= R423), L404 (≠ I426)
- binding magnesium ion: D446 (= D467), N473 (= N494), A475 (≠ G496)
- binding thiamine diphosphate: G396 (≠ A416), D397 (≠ N417), L398 (≠ T418), G419 (= G441), L421 (≠ M443), G445 (= G466), D446 (= D467), G447 (≠ S468), A448 (= A469), N473 (= N494), A475 (≠ G496), W476 (vs. gap), N477 (vs. gap), I478 (= I497), E479 (≠ Y498)
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
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, 92% coverage: 31:572/587 of query aligns to 24:564/590 of P0DUV9
- G43 (≠ I50) binding 2-hydroxyisobutanoyl-CoA
- Q255 (≠ S264) binding 2-hydroxyisobutanoyl-CoA
- RS 273:274 (= RS 282:283) binding 2-hydroxyisobutanoyl-CoA
- R362 (≠ N375) binding 2-hydroxyisobutanoyl-CoA
- GDL 410:412 (≠ ANT 416:418) binding thiamine diphosphate
- R417 (= R423) binding 2-hydroxyisobutanoyl-CoA
- G433 (= G441) binding thiamine diphosphate
- D460 (= D467) binding Mg(2+)
- GA 461:462 (≠ SA 468:469) binding thiamine diphosphate
- N487 (= N494) binding Mg(2+)
- NRAWNI 487:492 (≠ NNG--I 494:497) binding thiamine diphosphate
- A489 (≠ G496) binding Mg(2+)
- E493 (≠ Y498) 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 569:572) binding 2-hydroxyisobutanoyl-CoA
Sites not aligning to the query:
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, 92% coverage: 31:572/587 of query aligns to 10:550/584 of 7pt4B
- binding magnesium ion: D446 (= D467), N473 (= N494), A475 (≠ G496)
- 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 (≠ A280), R259 (= R282), S260 (= S283), Q279 (≠ L302), Y352 (≠ M379), G395 (= G415), G396 (≠ A416), D397 (≠ N417), L398 (≠ T418), L399 (= L419), R403 (= R423), L404 (≠ I426), G419 (= G441), L421 (≠ M443), G445 (= G466), D446 (= D467), G447 (≠ S468), A448 (= A469), N473 (= N494), A475 (≠ G496), W476 (vs. gap), N477 (vs. gap), I478 (= I497), E479 (≠ Y498), D547 (≠ E569)
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)
27% identity, 92% coverage: 31:572/587 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 (≠ Y136), Q114 (≠ E137), G256 (= G279), S257 (≠ A280), R259 (= R282), S260 (= S283), Q279 (≠ L302), Y352 (≠ M379), R403 (= R423), L404 (≠ I426), G419 (= G441), D547 (≠ E569)
- binding magnesium ion: D446 (= D467), N473 (= N494), A475 (≠ G496)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: E51 (= E72), T74 (≠ V95), P77 (= P98), G396 (≠ A416), D397 (≠ N417), L398 (≠ T418), G419 (= G441), L421 (≠ M443), G445 (= G466), D446 (= D467), G447 (≠ S468), A448 (= A469), N473 (= N494), A475 (≠ G496), W476 (vs. gap), N477 (vs. gap), I478 (= I497), E479 (≠ Y498)
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
4qq8C Crystal structure of the formolase fls in space group p 43 21 2 (see paper)
29% identity, 92% coverage: 24:564/587 of query aligns to 1:547/569 of 4qq8C
- active site: L24 (≠ V47), G26 (= G49), I27 (= I50), H28 (≠ P51), I29 (= I52), E49 (= E72), T72 (≠ V95), L111 (= L131), Q112 (= Q132), A113 (≠ Q133), G114 (= G134), W162 (≠ A186), L255 (≠ A280), T283 (≠ L303), G392 (= G415), N418 (≠ G441), M420 (= M443), D447 (= D467), N474 (= N494), S476 (≠ G496), W477 (≠ Y498), W479 (≠ G500), T480 (= T501), F483 (≠ N504), L545 (vs. gap)
- binding magnesium ion: D447 (= D467), N474 (= N494), S476 (≠ G496)
- binding thiamine diphosphate: H25 (≠ P48), E49 (= E72), Q112 (= Q132), G392 (= G415), G393 (≠ A416), L394 (≠ N417), T395 (= T418), N418 (≠ G441), M420 (= M443), G446 (= G466), D447 (= D467), G448 (≠ S468), S449 (≠ A469), Y452 (≠ F472), N474 (= N494), S476 (≠ G496), W477 (≠ Y498), G478 (≠ R499), W479 (≠ G500), T480 (= T501)
3d7kA Crystal structure of benzaldehyde lyase in complex with the inhibitor mbp (see paper)
29% identity, 92% coverage: 24:564/587 of query aligns to 1:547/554 of 3d7kA
- active site: L24 (≠ V47), G26 (= G49), A27 (≠ I50), H28 (≠ P51), I29 (= I52), E49 (= E72), T72 (≠ V95), L111 (= L131), Q112 (= Q132), A113 (≠ Q133), G114 (= G134), W162 (≠ A186), L255 (≠ A280), T283 (≠ L303), G392 (= G415), G418 (= G441), M420 (= M443), D447 (= D467), N474 (= N494), S476 (≠ G496), W477 (≠ Y498), A479 (≠ G500), T480 (= T501), F483 (≠ N504), L545 (vs. gap)
- binding calcium ion: D447 (= D467), N474 (= N494), S476 (≠ G496)
- 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 (≠ P48), G26 (= G49), A27 (≠ I50), E49 (= E72), T72 (≠ V95), Q112 (= Q132), G392 (= G415), A393 (= A416), L394 (≠ N417), T395 (= T418), G418 (= G441), M420 (= M443), G446 (= G466), D447 (= D467), G448 (≠ S468), S449 (≠ A469), Y452 (≠ F472), N474 (= N494), S476 (≠ G496), W477 (≠ Y498), G478 (≠ R499), A479 (≠ G500), T480 (= T501)
6lpiB Crystal structure of ahas holo-enzyme (see paper)
27% identity, 80% coverage: 28:497/587 of query aligns to 8:458/539 of 6lpiB
- active site: I27 (≠ V47), G29 (= G49), G30 (vs. gap), S31 (vs. gap), I32 (vs. gap), E53 (= E72), C76 (≠ V95), F115 (≠ Y136), Q116 (≠ E137), E117 (= E138), K165 (≠ A186), M256 (vs. gap), A283 (≠ G306), V375 (vs. gap), G401 (= G441), M403 (= M443), D428 (= D467), N455 (= N494), A457 (≠ G496), L458 (≠ I497)
- binding flavin-adenine dinucleotide: R155 (= R176), G212 (= G237), G213 (≠ K238), G214 (= G239), T236 (≠ M263), L237 (≠ S264), M238 (= M265), L254 (vs. gap), M256 (vs. gap), H257 (vs. gap), G276 (= G296), A277 (= A297), R278 (= R298), D280 (≠ N300), R282 (≠ H305), A283 (≠ G306), D300 (= D323), I301 (= I324), D319 (= D342), V320 (≠ I343), M380 (≠ L419), G398 (= G438)
- binding magnesium ion: D428 (= D467), N455 (= N494)
- binding thiamine diphosphate: E53 (= E72), C76 (≠ V95), P79 (= P98), G376 (= G415), Q377 (≠ A416), H378 (≠ N417), G401 (= G441), M403 (= M443), G427 (= G466), D428 (= D467), G429 (≠ S468), S430 (≠ A469), M433 (≠ F472), N455 (= N494), A457 (≠ G496), L458 (≠ I497)
Sites not aligning to the query:
Query Sequence
>WP_012975779.1 NCBI__GCF_000010725.1:WP_012975779.1
MSTAAATITKNQATEASVVEDAPALTDGFQLVIDALKLNDINNLYVVPGIPISDLLRMAQ
AEGMRVVSFRHEQNAGNAAAIAGFMTKKPGVCMTVSAPGFLNGLTALANATTNCFPMILI
SGSSEREIVDLQQGDYEEMDQLAIAKPLCKAAFRILHAQDIGIGVARAIRAAVSGRPGGV
YLDLPAKLFSQVMDAAEGAKSLVKVVDPTPAQYPSADAVNRALDLLKGAKRPLVIFGKGA
AYAQADETIRSFVEKSGIPFLQMSMAKGLLPDTHPQSAGAARSLVLQEADVVMLVGARLN
WLLSHGKGKTWGKPGSKKFIQVDIEPREMDSNVEIHAPLVGDIASVMEVLLKGIEGGLTP
PADWMATVAAKREQNVAKMAPKLMSNASPMNFHGALGALRRVIKERPDAMLVNEGANTLD
LARGIIDMYEPRKRLDVGTWGVMGVGMGYAVAAAVESGKPVLAVEGDSAFGFSGMEVETI
CRYNLPVCIVIFNNNGIYRGTDTNPTGGADPSPMVFVPGSRYDKMMEAFGGVGVHVTNPD
ELYRAVSEAMDSGRPTLINAVIDPAAGTESGNIGSLNPTSSVRKMPS
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