SitesBLAST
Comparing RR42_RS31370 FitnessBrowser__Cup4G11:RR42_RS31370 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)
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)
36% identity, 89% coverage: 33:550/584 of query aligns to 24:540/590 of P0DUV9
- G43 (= G52) binding
- Q255 (vs. gap) binding
- RS 273:274 (≠ RT 282:283) binding
- R362 (≠ A376) binding
- GDL 410:412 (≠ GDV 415:417) binding
- R417 (≠ A422) binding
- G433 (= G440) binding
- D460 (= D467) binding
- GA 461:462 (≠ GS 468:469) binding
- N487 (= N494) binding
- NRAWNI 487:492 (≠ NSAMNQ 494:499) binding
- A489 (= A496) binding
- E493 (≠ I500) 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
7pt1A Actinobacterial 2-hydroxyacyl-coa lyase (achacl) structure in complex with substrate 2-hib-coa and inactive cofactor 3-deaza-thdp (see paper)
36% identity, 89% coverage: 33:550/584 of query aligns to 10:526/574 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 (= L136), Q114 (= Q137), G256 (≠ D279), S257 (≠ R280), R259 (= R282), S260 (≠ T283), Q279 (≠ R302), Y352 (≠ L380), R403 (≠ A422), L404 (≠ Q423), G419 (= G440)
- binding magnesium ion: D446 (= D467), N473 (= N494), A475 (= A496)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: E51 (= E74), T74 (= T97), P77 (= P100), G396 (= G415), D397 (= D416), L398 (≠ V417), G419 (= G440), L421 (= L442), G445 (= G466), D446 (= D467), G447 (= G468), A448 (≠ S469), N473 (= N494), A475 (= A496), W476 (≠ M497), N477 (= N498), I478 (≠ Q499), E479 (≠ I500)
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: 547, 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)
36% identity, 89% coverage: 33:550/584 of query aligns to 10:526/584 of 7pt4B
- binding magnesium ion: D446 (= D467), N473 (= N494), A475 (= A496)
- 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 (≠ R280), R259 (= R282), S260 (≠ T283), Q279 (≠ R302), Y352 (≠ L380), G395 (= G414), G396 (= G415), D397 (= D416), L398 (≠ V417), L399 (≠ V418), R403 (≠ A422), L404 (≠ Q423), G419 (= G440), L421 (= L442), G445 (= G466), D446 (= D467), G447 (= G468), A448 (≠ S469), N473 (= N494), A475 (= A496), W476 (≠ M497), N477 (= N498), I478 (≠ Q499), E479 (≠ I500)
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: 547, 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)
36% identity, 89% coverage: 33:550/584 of query aligns to 10:526/580 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 (vs. gap), G256 (≠ D279), S257 (≠ R280), R259 (= R282), S260 (≠ T283), Y278 (≠ F301), Q279 (≠ R302), Y352 (≠ L380), R403 (≠ A422), L404 (≠ Q423)
- binding magnesium ion: D446 (= D467), N473 (= N494), A475 (= A496)
- binding thiamine diphosphate: G396 (= G415), D397 (= D416), L398 (≠ V417), G419 (= G440), L421 (= L442), G445 (= G466), D446 (= D467), G447 (= G468), A448 (≠ S469), N473 (= N494), A475 (= A496), W476 (≠ M497), N477 (= N498), I478 (≠ Q499), E479 (≠ I500)
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
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)
26% identity, 96% coverage: 9:571/584 of query aligns to 2:562/578 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 (≠ G468) 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
28% identity, 92% coverage: 28:566/584 of query aligns to 4:535/540 of 6xn8A
- active site: V25 (≠ L49), G27 (= G51), F28 (≠ G52), P29 (≠ H53), I30 (= I54), E50 (= E74), V73 (≠ T97), F112 (≠ L136), Q113 (= Q137), E114 (≠ D138), D162 (≠ R186), F277 (= F301), G388 (= G414), G414 (= G440), M416 (≠ L442), D441 (= D467), N468 (= N494), G470 (vs. gap), I471 (vs. gap), P473 (vs. gap), G474 (≠ A496), E477 (≠ Q499)
- binding adenosine-5'-diphosphate: R152 (≠ A176), G211 (= G237), K212 (≠ Q238), S237 (≠ N263), G270 (= G296), R272 (≠ P298), D295 (= D319), I296 (≠ M320), G313 (= G337), D314 (= D338), G315 (≠ P339)
- binding magnesium ion: D441 (= D467), N468 (= N494), G470 (vs. gap)
- 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 (= E74), V73 (≠ T97), P76 (= P100), H80 (≠ N104), Y367 (≠ P393), A389 (≠ G415), G390 (≠ D416), T391 (≠ V417), G414 (= G440), M416 (≠ L442), G440 (= G466), D441 (= D467), S442 (≠ G468), A443 (≠ S469), F446 (≠ M472), N468 (= N494), G470 (vs. gap), I471 (vs. gap), G472 (vs. gap)
3d7kA Crystal structure of benzaldehyde lyase in complex with the inhibitor mbp (see paper)
29% identity, 90% coverage: 27:550/584 of query aligns to 2:529/554 of 3d7kA
- active site: L24 (= L49), G26 (= G51), A27 (≠ G52), H28 (= H53), I29 (= I54), E49 (= E74), T72 (= T97), L111 (= L136), Q112 (= Q137), A113 (vs. gap), G114 (≠ D138), W162 (≠ R186), L255 (≠ R282), T283 (≠ M303), G392 (= G414), G418 (= G440), M420 (≠ L442), D447 (= D467), N474 (= N494), S476 (≠ A496), W477 (≠ M497), A479 (≠ Q499), T480 (≠ I500), F483 (≠ G503)
- binding calcium ion: D447 (= D467), N474 (= N494), S476 (≠ A496)
- 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 (≠ C50), G26 (= G51), A27 (≠ G52), E49 (= E74), T72 (= T97), Q112 (= Q137), G392 (= G414), A393 (≠ G415), L394 (≠ D416), T395 (≠ V417), G418 (= G440), M420 (≠ L442), G446 (= G466), D447 (= D467), G448 (= G468), S449 (= S469), Y452 (≠ M472), N474 (= N494), S476 (≠ A496), W477 (≠ M497), G478 (≠ N498), A479 (≠ Q499), T480 (≠ I500)
Sites not aligning to the query:
4qq8C Crystal structure of the formolase fls in space group p 43 21 2 (see paper)
29% identity, 90% coverage: 27:550/584 of query aligns to 2:529/569 of 4qq8C
- active site: L24 (= L49), G26 (= G51), I27 (≠ G52), H28 (= H53), I29 (= I54), E49 (= E74), T72 (= T97), L111 (= L136), Q112 (= Q137), A113 (vs. gap), G114 (≠ D138), W162 (≠ R186), L255 (≠ R282), T283 (≠ M303), G392 (= G414), N418 (≠ G440), M420 (≠ L442), D447 (= D467), N474 (= N494), S476 (≠ A496), W477 (≠ M497), W479 (≠ Q499), T480 (≠ I500), F483 (≠ G503)
- binding magnesium ion: D447 (= D467), N474 (= N494), S476 (≠ A496)
- binding thiamine diphosphate: H25 (≠ C50), E49 (= E74), Q112 (= Q137), G392 (= G414), G393 (= G415), L394 (≠ D416), T395 (≠ V417), N418 (≠ G440), M420 (≠ L442), G446 (= G466), D447 (= D467), G448 (= G468), S449 (= S469), Y452 (≠ M472), N474 (= N494), S476 (≠ A496), W477 (≠ M497), G478 (≠ N498), W479 (≠ Q499), T480 (≠ I500)
Sites not aligning to the query:
7b2eA Quadruple mutant of oxalyl-coa decarboxylase from methylorubrum extorquens with bound tpp and adp (see paper)
28% identity, 93% coverage: 30:570/584 of query aligns to 6:542/548 of 7b2eA
- active site: V25 (≠ L49), G27 (= G51), I28 (≠ G52), P29 (≠ H53), I30 (= I54), E50 (= E74), V73 (≠ T97), Y114 (≠ L139), G115 (≠ P140), A164 (≠ R186), L281 (≠ M303), G394 (= G414), G420 (= G440), M422 (≠ L442), I476 (≠ M497), R478 (= R501), G479 (≠ Y502), T482 (≠ L505)
- binding adenosine-5'-diphosphate: C92 (≠ E116), R154 (≠ A176), G215 (= G237), K216 (≠ Q238), G217 (≠ Q239), M241 (≠ N263), G274 (= G296), R276 (≠ P298), D301 (= D319), I302 (≠ M320), D320 (= D338), I321 (≠ P339)
- binding magnesium ion: D446 (= D467), N473 (= N494), G475 (≠ A496)
- binding thiamine diphosphate: F371 (≠ P393), C395 (≠ G415), N396 (≠ D416), T397 (≠ V417), G420 (= G440), M422 (≠ L442), G445 (= G466), D446 (= D467), S447 (≠ G468), A448 (≠ S469), F451 (≠ M472), N473 (= N494), G475 (≠ A496), I476 (≠ M497), F477 (≠ I500)
P0AFI0 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Escherichia coli (strain K12) (see paper)
25% identity, 95% coverage: 30:584/584 of query aligns to 10:555/564 of P0AFI0
- R158 (≠ A176) binding
- K220 (≠ Q238) binding
- R280 (≠ P298) binding
- D302 (= D319) binding
- I322 (≠ L343) binding
- Y372 (≠ P393) binding
- D447 (= D467) binding
- N474 (= N494) binding
- G476 (≠ A496) binding
- Y478 (≠ I500) binding
2q28A Crystal structure of oxalyl-coa decarboxylase from escherichia coli in complex with adenosine-5`-diphosphate (see paper)
25% identity, 93% coverage: 30:570/584 of query aligns to 6:540/550 of 2q28A
- active site: V25 (≠ L49), G27 (= G51), I28 (≠ G52), P29 (≠ H53), V30 (≠ I54), E50 (= E74), V73 (≠ T97), Y114 (≠ L136), E115 (≠ Q137), E116 (≠ D138), A164 (≠ R186), L281 (≠ M303), G391 (= G414), G417 (= G440), M419 (≠ L442), D443 (= D467), N470 (= N494), G472 (≠ A496), I473 (≠ M497), R475 (= R501), G476 (≠ Y502), V479 (≠ L505), P540 (= P570)
- binding adenosine-5'-diphosphate: R154 (≠ A176), G215 (= G237), K216 (≠ Q238), G217 (≠ Q239), M241 (≠ N263), G274 (= G296), R276 (≠ P298), D298 (= D319), I299 (≠ M320), D317 (= D338), I318 (≠ L343)
- binding magnesium ion: D443 (= D467), N470 (= N494), G472 (≠ A496)
- binding thiamine diphosphate: Y368 (≠ P393), G391 (= G414), A392 (≠ G415), N393 (≠ D416), T394 (≠ V417), M419 (≠ L442), G442 (= G466), D443 (= D467), S444 (≠ G468), A445 (≠ S469), F448 (≠ M472), N470 (= N494), G472 (≠ A496), I473 (≠ M497), Y474 (≠ I500)
2q29A Crystal structure of oxalyl-coa decarboxylase from escherichia coli in complex with acetyl coenzyme a (see paper)
25% identity, 93% coverage: 30:570/584 of query aligns to 6:540/546 of 2q29A
- active site: V25 (≠ L49), G27 (= G51), I28 (≠ G52), P29 (≠ H53), V30 (≠ I54), E50 (= E74), V73 (≠ T97), Y114 (≠ L136), E115 (≠ Q137), E116 (≠ D138), A164 (≠ R186), L281 (≠ M303), G391 (= G414), G417 (= G440), M419 (≠ L442), D443 (= D467), N470 (= N494), G472 (≠ A496), I473 (≠ M497), R475 (= R501), G476 (≠ Y502), V479 (≠ L505), P540 (= P570)
- binding acetyl coenzyme *a: A257 (≠ D279), A258 (≠ R280), R260 (= R282), S261 (≠ T283), N351 (≠ A376), M355 (≠ L380), N400 (≠ Q423)
- binding magnesium ion: D443 (= D467), N470 (= N494), G472 (≠ A496)
- binding thiamine diphosphate: Y368 (≠ P393), A392 (≠ G415), N393 (≠ D416), T394 (≠ V417), M419 (≠ L442), G442 (= G466), D443 (= D467), S444 (≠ G468), A445 (≠ S469), F448 (≠ M472), N470 (= N494), G472 (≠ A496), I473 (≠ M497), Y474 (≠ I500)
6lpiB Crystal structure of ahas holo-enzyme (see paper)
26% identity, 95% coverage: 29:582/584 of query aligns to 7:538/539 of 6lpiB
- active site: I27 (≠ L49), G29 (= G51), G30 (= G52), S31 (≠ H53), I32 (= I54), E53 (= E74), C76 (≠ T97), F115 (≠ L136), Q116 (= Q137), E117 (≠ D138), K165 (≠ R186), M256 (≠ H276), A283 (vs. gap), V375 (≠ G414), G401 (= G440), M403 (≠ L442), D428 (= D467), N455 (= N494), A457 (= A496), L458 (≠ M497), L460 (≠ Q499), V461 (≠ I500), Q464 (≠ G503)
- binding flavin-adenine dinucleotide: R155 (≠ A176), G212 (= G237), G213 (≠ Q238), G214 (≠ Q239), T236 (≠ N263), L237 (≠ G264), M238 (≠ A265), L254 (vs. gap), M256 (≠ H276), H257 (= H277), G276 (= G296), A277 (≠ T297), R278 (≠ P298), D280 (= D300), R282 (= R302), A283 (vs. gap), D300 (= D319), I301 (≠ M320), D319 (= D338), V320 (≠ P339), M380 (≠ T419), G398 (= G437)
- binding magnesium ion: D428 (= D467), N455 (= N494)
- binding thiamine diphosphate: E53 (= E74), C76 (≠ T97), P79 (= P100), G376 (= G415), Q377 (≠ D416), H378 (≠ V417), G401 (= G440), M403 (≠ L442), G427 (= G466), D428 (= D467), G429 (= G468), S430 (= S469), M433 (= M472), N455 (= N494), A457 (= A496), L458 (≠ M497), G459 (≠ N498), L460 (≠ Q499), V461 (≠ I500)
1ozfA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors (see paper)
28% identity, 93% coverage: 30:572/584 of query aligns to 7:536/545 of 1ozfA
- active site: I26 (≠ L49), G28 (= G51), A29 (≠ G52), K30 (≠ H53), I31 (= I54), E51 (= E74), T74 (= T97), H113 (≠ L136), Q114 (= Q137), S115 (≠ D138), Q163 (≠ R186), L253 (≠ A285), E280 (≠ R302), M385 (≠ G414), Q411 (≠ G440), M413 (≠ L442), D438 (= D467), D465 (≠ N494), G467 (≠ A496), Y468 (≠ M497), M470 (≠ Q499), V471 (≠ I500), Q474 (≠ G503), Y534 (≠ P570)
- binding magnesium ion: D438 (= D467), D465 (≠ N494), G467 (≠ A496)
- binding phosphate ion: G249 (vs. gap), R250 (= R282), Q257 (vs. gap), R343 (≠ K358), R394 (≠ Q423), L396 (≠ V425), Y397 (≠ R426)
- binding thiamine diphosphate: G386 (= G415), S387 (≠ D416), F388 (≠ V417), Q411 (≠ G440), M413 (≠ L442), G437 (= G466), D438 (= D467), G439 (= G468), D465 (≠ N494), G467 (≠ A496), Y468 (≠ M497), N469 (= N498), M470 (≠ Q499), V471 (≠ I500), Y534 (≠ P570)
5d6rB Acetolactate synthase from klebsiella pneumoniae in complex with mechanism-based inhibitor
28% identity, 93% coverage: 30:572/584 of query aligns to 7:537/548 of 5d6rB
- active site: I26 (≠ L49), G28 (= G51), A29 (≠ G52), K30 (≠ H53), I31 (= I54), E51 (= E74), T74 (= T97), H113 (≠ L136), Q114 (= Q137), S115 (≠ D138), Q163 (≠ R186), L254 (≠ A285), E281 (≠ R302), M386 (≠ G414), Q412 (≠ G440), M414 (≠ L442), D439 (= D467), D466 (≠ N494), G468 (≠ A496), Y469 (≠ M497), M471 (≠ Q499), V472 (≠ I500), Q475 (≠ G503), Y535 (≠ P570)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-[(Z)-2-fluoro-1-hydroxy-2-phosphonoethenyl]-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: M386 (≠ G414), G387 (= G415), S388 (≠ D416), Q412 (≠ G440), M414 (≠ L442), D439 (= D467), G440 (= G468), G468 (≠ A496), Y469 (≠ M497), N470 (= N498), M471 (≠ Q499), Y535 (≠ P570)
- binding magnesium ion: R63 (= R86), Q212 (≠ T242), D439 (= D467), D466 (≠ N494), G468 (≠ A496)
5dx6B Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
27% identity, 93% coverage: 30:572/584 of query aligns to 19:543/557 of 5dx6B
- active site: I38 (≠ L49), G40 (= G51), A41 (≠ G52), K42 (≠ H53), I43 (= I54), E63 (= E74), T86 (= T97), H125 (≠ L136), Q126 (= Q137), S127 (≠ D138), Q175 (≠ R186), L268 (≠ A285), E295 (≠ R302), M392 (≠ G414), Q418 (≠ G440), M420 (≠ L442), D445 (= D467), D472 (≠ N494), G474 (≠ A496), Y475 (≠ M497), M477 (≠ Q499), V478 (≠ I500), Q481 (≠ G503), Y541 (≠ P570)
- binding 3-fluoro-2-oxopropanoic acid: G264 (vs. gap), R265 (= R282), Q272 (vs. gap), A400 (= A422), R401 (≠ Q423), Y404 (≠ R426)
- binding magnesium ion: S135 (= S146), T138 (= T149), D445 (= D467), D472 (≠ N494), G474 (≠ A496)
- binding thiamine diphosphate: G393 (= G415), S394 (≠ D416), F395 (≠ V417), Q418 (≠ G440), M420 (≠ L442), G444 (= G466), D445 (= D467), G446 (= G468), D472 (≠ N494), G474 (≠ A496), Y475 (≠ M497), N476 (= N498), M477 (≠ Q499), V478 (≠ I500), Y541 (≠ P570)
P40149 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Oxalobacter formigenes (see 2 papers)
28% identity, 93% coverage: 30:570/584 of query aligns to 12:547/568 of P40149
- E56 (= E74) mutation to A: Loss of the decarboxylase activity. The mutant forms a dimer and not a tetramer.
- Y120 (≠ L136) 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 (≠ Q137) 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 (≠ A176) binding
- K222 (≠ Q238) binding
- R282 (≠ P298) binding
- D306 (= D319) binding
- I326 (≠ P339) binding
- Y377 (≠ V396) binding
- D452 (= D467) binding
- N479 (= N494) binding
- G481 (≠ Q504) binding
- Y483 (≠ A506) 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.
Sites not aligning to the query:
- 553 S→A: Does not affect oxalyl-CoA binding, but it reduces 7-fold the catalytic efficiency for oxalyl-CoA.
- 555 R→A: 3-fold reduction in the affinity binding for oxalyl-CoA, but it does not affect the catalytic efficiency.
1ozgA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate (see paper)
27% identity, 93% coverage: 30:572/584 of query aligns to 8:540/549 of 1ozgA
- active site: I27 (≠ L49), G29 (= G51), A30 (≠ G52), K31 (≠ H53), I32 (= I54), E52 (= E74), T75 (= T97), H114 (≠ L136), Q115 (= Q137), S116 (≠ D138), Q164 (≠ R186), L257 (≠ A285), E284 (≠ R302), M389 (≠ G414), Q415 (≠ G440), M417 (≠ L442), D442 (= D467), D469 (≠ N494), G471 (≠ A496), Y472 (≠ M497), M474 (≠ Q499), V475 (≠ I500), Q478 (≠ G503), Y538 (≠ P570)
- binding 2-hydroxyethyl dihydrothiachrome diphosphate: M389 (≠ G414), G390 (= G415), S391 (≠ D416), F392 (≠ V417), Q415 (≠ G440), M417 (≠ L442), G441 (= G466), D442 (= D467), G443 (= G468), D469 (≠ N494), G471 (≠ A496), Y472 (≠ M497), N473 (= N498), M474 (≠ Q499), V475 (≠ I500), Y538 (≠ P570)
- binding magnesium ion: D442 (= D467), D469 (≠ N494), G471 (≠ A496)
- binding phosphate ion: G253 (vs. gap), R254 (= R282), Q261 (vs. gap), R347 (≠ K358), R398 (≠ Q423), Y401 (≠ R426)
2jibA X-ray structure of oxalyl-coa decarboxylase in complex with coenzyme- a (see paper)
28% identity, 93% coverage: 30:570/584 of query aligns to 6:541/559 of 2jibA
- active site: V25 (≠ L49), G27 (= G51), I28 (≠ G52), P29 (≠ H53), I30 (= I54), E50 (= E74), V73 (≠ T97), Y114 (≠ L136), E115 (≠ Q137), E116 (≠ D138), A164 (≠ R186), M281 (= M303), G394 (= G414), G420 (= G440), M422 (≠ L442), D446 (= D467), N473 (= N494), G475 (≠ Q504), I476 (≠ L505), K478 (= K507), G479 (≠ Y508), A482 (= A511), P541 (= P570)
- binding adenosine-5'-diphosphate: C92 (≠ E116), R154 (≠ A176), G215 (= G237), K216 (≠ Q238), G217 (≠ Q239), M241 (≠ N263), G274 (= G296), A275 (≠ T297), R276 (≠ P298), D300 (= D319), I301 (≠ M320), D319 (= D338), I320 (≠ P339)
- binding coenzyme a: A258 (≠ R280), R260 (= R282), A261 (≠ T283), L280 (≠ R302), N352 (≠ A376), K353 (≠ A377), L356 (= L380), L398 (≠ V418), R402 (≠ A422), M403 (≠ Q423)
- binding magnesium ion: D446 (= D467), N473 (= N494), G475 (≠ Q504)
- binding thiamine diphosphate: E50 (= E74), V73 (≠ T97), Y371 (≠ V396), A395 (≠ G415), N396 (≠ D416), A397 (≠ V417), M422 (≠ L442), G445 (= G466), D446 (= D467), S447 (≠ G468), A448 (≠ S469), F451 (≠ M472), N473 (= N494), G475 (≠ Q504), I476 (≠ L505), Y477 (≠ A506)
Sites not aligning to the query:
2ji8A X-ray structure of oxalyl-coa decarboxylase in complex with formyl- coa (see paper)
28% identity, 93% coverage: 30:570/584 of query aligns to 6:541/559 of 2ji8A
- active site: V25 (≠ L49), G27 (= G51), I28 (≠ G52), P29 (≠ H53), I30 (= I54), E50 (= E74), V73 (≠ T97), Y114 (≠ L136), E115 (≠ Q137), E116 (≠ D138), A164 (≠ R186), M281 (= M303), G394 (= G414), G420 (= G440), M422 (≠ L442), D446 (= D467), N473 (= N494), G475 (≠ Q504), I476 (≠ L505), K478 (= K507), G479 (≠ Y508), A482 (= A511), P541 (= P570)
- binding adenosine-5'-diphosphate: C92 (≠ E116), R154 (≠ A176), G215 (= G237), K216 (≠ Q238), G217 (≠ Q239), M241 (≠ N263), G274 (= G296), R276 (≠ P298), D300 (= D319), I301 (≠ M320), D319 (= D338), I320 (≠ P339)
- 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 (≠ D279), A258 (≠ R280), T259 (= T281), R260 (= R282), A261 (≠ T283), W279 (≠ F301), L280 (≠ R302), N352 (≠ A376), L356 (= L380), L398 (≠ V418), R402 (≠ A422), M403 (≠ Q423)
- binding magnesium ion: D446 (= D467), N473 (= N494), G475 (≠ Q504)
- binding thiamine diphosphate: Y371 (≠ V396), A395 (≠ G415), N396 (≠ D416), G420 (= G440), M422 (≠ L442), G445 (= G466), D446 (= D467), S447 (≠ G468), A448 (≠ S469), F451 (≠ M472), N473 (= N494), G475 (≠ Q504), I476 (≠ L505), Y477 (≠ A506)
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 : 547, 549, 550
Query Sequence
>RR42_RS31370 FitnessBrowser__Cup4G11:RR42_RS31370
MSAVAPTRPESTTAEDTLKQKTRDAGVISGGHLVARALKNEGVDTIFTLCGGHIIDIYDG
CVDEGIRIIDVRHEQVAAHAADGYARQTGKLGCVVTTAGPGCTNAVTGVATAFRSESPII
HIGGQGALSQHKMGSLQDLPHVDMMSAITKFAATIPSTERVADMISMAARECFNGAPGPA
YLEIPRDVLDREVDVSRAVIPRPGHYRASTRSIGDPRDIERLADILVNAERPAILYGQQV
WTARGHEEAIALLKGLDIPGYFNGASRGLLPPGDPHHFDRTRTQAFANADVLIIVGTPFD
FRMGYGKRISKELTLVQIDMDYRTVGKNREIDLGLVGDPGAILGAVLQAASGRIKNDKRQ
ARQKWMGQLTEAEAVAAEKLMPLFRSENTPIHPYRVAYELNEFLSEDTVYIGDGGDVVTI
SAQAVRPRRPGQWMDPGALGSLGVGTGFAIAAGLANPNKEILCYYGDGSFGMTAFDMETA
NRFGVPYLAVIGNNSAMNQIRYGQLAKYGEARGNVGNLLSDVPFSKFAEMLGGYGEEVRD
PGKIAGALQRGREAVQRTGKSAVINIWVDPREYAPGTKNQTMYK
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