SitesBLAST
Comparing N515DRAFT_1567 FitnessBrowser__Dyella79:N515DRAFT_1567 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)
P07003 Pyruvate dehydrogenase [ubiquinone]; Pyruvate oxidase; POX; Pyruvate:ubiquinone-8 oxidoreductase; EC 1.2.5.1 from Escherichia coli (strain K12) (see 4 papers)
33% identity, 95% coverage: 2:563/594 of query aligns to 3:546/572 of P07003
- E50 (= E50) binding
- 183:334 (vs. 191:342, 34% identical) FAD-binding domain
- S210 (≠ A216) binding
- LR 234:235 (≠ LL 240:241) binding
- TGLI 251:254 (≠ IGLL 257:260) binding
- TQFPY 274:278 (≠ TTFPY 280:284) binding
- D292 (= D300) binding
- S297 (≠ N305) binding
- DI 311:312 (≠ DA 319:320) binding
- 335:530 (vs. 343:547, 28% identical) PP-binding domain
- T382 (≠ S390) binding
- FN 403:404 (≠ LS 409:410) binding
- G--SM 406:408 (≠ GLATM 412:416) binding
- D433 (= D441) binding
- DGG 433:435 (≠ DGA 441:443) binding
- N460 (= N474) binding
- 460:466 (vs. 474:480, 43% identical) binding
- V462 (≠ D476) binding
- F465 (≠ Q479) Moves into active site upon enzyme activation, plays a role in electron transfer
- A533 (≠ P550) mutation to T: In poxB11; poor activity in vivo, no longer activated by lipids.
Sites not aligning to the query:
- 1:182 Pyr domain
- 531:572 Membrane-binding domain
- 549:550 In vitro cleavage to yield alpha-peptide
- 549:572 mutation Missing: In poxB6. Inactive in vivo, does not complement inactive mutants. Active in vitro, no longer activated by nor binds to, detergents.
- 553 A→V: In poxB14; poor activity in vivo, no longer activated by lipids.
- 560 D→P: In poxB15; normal activity.
- 564 E→P: In poxB16; loss of activity, weakly activated by cleavage.
- 564:572 mutation Missing: In poxB7 Inactive in vivo, reduced activity in vitro.
- 570:572 mutation Missing: In poxB8; reduced activity in vitro, not activated by lipids.
- 572 R→G: In poxB10; reduced activity in vivo and in vitro; may interact less with membranes.
3ey9A Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from escherichia coli (see paper)
33% identity, 95% coverage: 2:563/594 of query aligns to 2:545/571 of 3ey9A
- active site: V23 (≠ Y23), G25 (= G25), D26 (= D26), S27 (≠ G27), L28 (≠ I28), E49 (= E50), S72 (≠ T73), F111 (≠ Q112), Q112 (= Q113), G160 (≠ H161), L252 (= L259), A279 (≠ E286), V379 (≠ C388), G405 (= G412), M407 (= M416), D432 (= D441), N459 (= N474), V461 (≠ D476), L462 (= L477), F464 (≠ Q479), V465 (= V480), E468 (= E483), K528 (≠ P546)
- binding flavin-adenine dinucleotide: G208 (= G215), S209 (≠ A216), G210 (= G217), A232 (= A239), L233 (= L240), R234 (≠ L241), T250 (≠ I257), G251 (= G258), I253 (≠ L260), G272 (= G279), T273 (= T280), Q274 (≠ T281), F275 (= F282), Y277 (= Y284), D291 (= D300), I292 (= I301), S296 (≠ N305), G309 (= G318), D310 (= D319), I311 (≠ A320), T383 (= T392), F402 (≠ L409), N403 (≠ S410)
- binding magnesium ion: D432 (= D441), N459 (= N474)
- binding thiamine diphosphate: T24 (≠ P24), E49 (= E50), S72 (≠ T73), G76 (= G77), H79 (= H80), G380 (= G389), T381 (≠ S390), P382 (≠ H391), M407 (= M416), G431 (= G440), D432 (= D441), G433 (= G442), G434 (≠ A443), N459 (= N474), V461 (≠ D476), L462 (= L477), G463 (≠ N478)
Sites not aligning to the query:
1powA The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from lactobacillus plantarum (see paper)
32% identity, 91% coverage: 5:542/594 of query aligns to 6:534/585 of 1powA
- active site: I24 (≠ Y23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), F113 (≠ Q112), Q114 (= Q113), E115 (= E114), V162 (≠ H161), R256 (≠ L259), E283 (= E286), V386 (≠ C388), A412 (= A414), M414 (= M416), D439 (= D441), N466 (≠ W482), Q468 (= Q484), Y469 (≠ R485), F471 (≠ L487), I472 (≠ A488), E475 (≠ P491)
- binding flavin-adenine dinucleotide: H93 (= H92), G212 (= G215), I213 (≠ A216), G214 (= G217), T236 (≠ A239), Y237 (≠ L240), A254 (≠ I257), V257 (≠ L260), G276 (= G279), N277 (≠ T280), N278 (≠ T281), Y279 (≠ F282), P280 (= P283), F281 (≠ Y284), D298 (= D300), I299 (= I301), K303 (≠ N305), D317 (= D319), A318 (= A320), N409 (≠ G411)
- binding magnesium ion: D439 (= D441), N466 (≠ W482), Q468 (= Q484)
- binding thiamine diphosphate: D388 (≠ S390), M414 (= M416), G440 (= G442), N466 (≠ W482), Q468 (= Q484), Y469 (≠ R485), G470 (≠ A486), F471 (≠ L487), I472 (≠ A488)
Sites not aligning to the query:
4feeA High-resolution structure of pyruvate oxidase in complex with reaction intermediate 2-hydroxyethyl-thiamin diphosphate carbanion-enamine, crystal b (see paper)
32% identity, 91% coverage: 5:542/594 of query aligns to 6:534/586 of 4feeA
- binding flavin-adenine dinucleotide: H93 (= H92), G212 (= G215), I213 (≠ A216), G214 (= G217), T236 (≠ A239), Y237 (≠ L240), P238 (≠ L241), A254 (≠ I257), N255 (≠ G258), V257 (≠ L260), G276 (= G279), N277 (≠ T280), N278 (≠ T281), P280 (= P283), F281 (≠ Y284), D298 (= D300), I299 (= I301), K303 (≠ N305), D317 (= D319), A318 (= A320), N390 (≠ T392), N409 (≠ G411)
- binding magnesium ion: D439 (= D441), N466 (≠ W482), Q468 (= Q484)
- binding pyruvic acid: N255 (≠ G258), R256 (≠ L259)
- binding 2-[(2e)-3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-(1-hydroxyethylidene)-4-methyl-2,3-dihydro-1,3-thiazol-5-yl]ethyltrihydrogen diphosphate: V386 (≠ C388), D388 (≠ S390), A412 (= A414), M414 (= M416), G438 (= G440), G440 (= G442), N466 (≠ W482), Q468 (= Q484), Y469 (≠ R485), G470 (≠ A486), F471 (≠ L487), I472 (≠ A488)
Sites not aligning to the query:
2ezuA Pyruvate oxidase variant f479w in complex with reaction intermediate 2-acetyl-thiamin diphosphate (see paper)
31% identity, 91% coverage: 5:542/594 of query aligns to 6:534/585 of 2ezuA
- active site: I24 (≠ Y23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), F113 (≠ Q112), Q114 (= Q113), E115 (= E114), V162 (≠ H161), R256 (≠ L259), E283 (= E286), V386 (≠ C388), A412 (= A414), M414 (= M416), D439 (= D441), N466 (= N474), Q468 (≠ D476), Y469 (≠ L477), W471 (≠ Q479), I472 (≠ V480), E475 (= E483)
- binding flavin-adenine dinucleotide: H93 (= H92), G212 (= G215), I213 (≠ A216), G214 (= G217), T236 (≠ A239), Y237 (≠ L240), P238 (≠ L241), A254 (≠ I257), N255 (≠ G258), R256 (≠ L259), V257 (≠ L260), G276 (= G279), N277 (≠ T280), N278 (≠ T281), P280 (= P283), F281 (≠ Y284), D298 (= D300), I299 (= I301), K303 (≠ N305), D317 (= D319), A318 (= A320), N409 (≠ G411)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ C388), D388 (≠ S390), M414 (= M416), G438 (= G440), G440 (= G442), N466 (= N474), Q468 (≠ D476), Y469 (≠ L477), G470 (≠ N478), W471 (≠ Q479), I472 (≠ V480)
- binding magnesium ion: D439 (= D441), N466 (= N474), Q468 (≠ D476)
Sites not aligning to the query:
2ez9A Pyruvate oxidase variant f479w in complex with reaction intermediate analogue 2-phosphonolactyl-thiamin diphosphate (see paper)
31% identity, 91% coverage: 5:542/594 of query aligns to 6:534/585 of 2ez9A
- active site: I24 (≠ Y23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), F113 (≠ Q112), Q114 (= Q113), E115 (= E114), V162 (≠ H161), R256 (≠ L259), E283 (= E286), V386 (≠ C388), A412 (= A414), M414 (= M416), D439 (= D441), N466 (= N474), Q468 (≠ D476), Y469 (≠ L477), W471 (≠ Q479), I472 (≠ V480), E475 (= E483)
- binding flavin-adenine dinucleotide: H93 (= H92), G212 (= G215), I213 (≠ A216), G214 (= G217), T236 (≠ A239), Y237 (≠ L240), P238 (≠ L241), A254 (≠ I257), N255 (≠ G258), R256 (≠ L259), V257 (≠ L260), G276 (= G279), N277 (≠ T280), N278 (≠ T281), P280 (= P283), F281 (≠ Y284), D298 (= D300), I299 (= I301), K303 (≠ N305), D317 (= D319), A318 (= A320), N409 (≠ G411)
- binding magnesium ion: D439 (= D441), N466 (= N474), Q468 (≠ D476)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(1s)-1-hydroxy-1-[(r)-hydroxy(methoxy)phosphoryl]ethyl}-5-(2-{[(s)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: V386 (≠ C388), D388 (≠ S390), M414 (= M416), G438 (= G440), G440 (= G442), N466 (= N474), Q468 (≠ D476), Y469 (≠ L477), G470 (≠ N478), W471 (≠ Q479), I472 (≠ V480), E475 (= E483)
Sites not aligning to the query:
2ez8A Pyruvate oxidase variant f479w in complex with reaction intermediate 2-lactyl-thiamin diphosphate (see paper)
31% identity, 91% coverage: 5:542/594 of query aligns to 6:534/585 of 2ez8A
- active site: I24 (≠ Y23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), F113 (≠ Q112), Q114 (= Q113), E115 (= E114), V162 (≠ H161), R256 (≠ L259), E283 (= E286), V386 (≠ C388), A412 (= A414), M414 (= M416), D439 (= D441), N466 (= N474), Q468 (≠ D476), Y469 (≠ L477), W471 (≠ Q479), I472 (≠ V480), E475 (= E483)
- binding flavin-adenine dinucleotide: H93 (= H92), G212 (= G215), I213 (≠ A216), G214 (= G217), T236 (≠ A239), Y237 (≠ L240), P238 (≠ L241), A254 (≠ I257), N255 (≠ G258), R256 (≠ L259), V257 (≠ L260), G276 (= G279), N277 (≠ T280), N278 (≠ T281), P280 (= P283), F281 (≠ Y284), D298 (= D300), I299 (= I301), K303 (≠ N305), D317 (= D319), A318 (= A320), N390 (≠ T392), N409 (≠ G411)
- binding magnesium ion: D439 (= D441), N466 (= N474), Q468 (≠ D476)
- 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: D388 (≠ S390), M414 (= M416), G438 (= G440), G440 (= G442), N466 (= N474), Q468 (≠ D476), Y469 (≠ L477), G470 (≠ N478), W471 (≠ Q479), I472 (≠ V480)
Sites not aligning to the query:
2ez4B Pyruvate oxidase variant f479w (see paper)
31% identity, 91% coverage: 5:542/594 of query aligns to 6:534/585 of 2ez4B
- active site: I24 (≠ Y23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), F113 (≠ Q112), Q114 (= Q113), E115 (= E114), V162 (≠ H161), R256 (≠ L259), E283 (= E286), V386 (≠ C388), A412 (= A414), M414 (= M416), D439 (= D441), N466 (= N474), Q468 (≠ D476), Y469 (≠ L477), W471 (≠ Q479), I472 (≠ V480), E475 (= E483)
- binding flavin-adenine dinucleotide: H93 (= H92), G212 (= G215), I213 (≠ A216), G214 (= G217), T236 (≠ A239), Y237 (≠ L240), P238 (≠ L241), A254 (≠ I257), N255 (≠ G258), R256 (≠ L259), V257 (≠ L260), G276 (= G279), N277 (≠ T280), N278 (≠ T281), P280 (= P283), F281 (≠ Y284), D298 (= D300), I299 (= I301), K303 (≠ N305), D317 (= D319), A318 (= A320), N409 (≠ G411)
- binding magnesium ion: D439 (= D441), N466 (= N474), Q468 (≠ D476)
- binding phosphate ion: W471 (≠ Q479), E475 (= E483)
- binding thiamine diphosphate: D388 (≠ S390), A412 (= A414), M414 (= M416), G438 (= G440), D439 (= D441), G440 (= G442), G441 (≠ A443), N466 (= N474), Q468 (≠ D476), Y469 (≠ L477), G470 (≠ N478), W471 (≠ Q479), I472 (≠ V480)
Sites not aligning to the query:
1y9dD Pyruvate oxidase variant v265a from lactobacillus plantarum (see paper)
31% identity, 91% coverage: 5:542/594 of query aligns to 6:509/560 of 1y9dD
- active site: I24 (≠ Y23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), E108 (= E114), V155 (≠ H161), R241 (≠ L259), V361 (≠ C388), A387 (= A414), M389 (= M416), D414 (= D441), N441 (≠ W482), Q443 (= Q484), Y444 (≠ R485), F446 (≠ L487), I447 (≠ A488), E450 (≠ P491)
- binding flavin-adenine dinucleotide: I198 (≠ A216), G199 (= G217), T221 (≠ A239), P223 (≠ L241), G261 (= G279), N262 (≠ T280), N263 (≠ T281), D273 (= D300), I274 (= I301), K278 (≠ N305), D292 (= D319), A293 (= A320)
- binding magnesium ion: D414 (= D441), N441 (≠ W482), Q443 (= Q484)
- binding thiamine diphosphate: E51 (= E50), S74 (≠ T73), P77 (= P76), H81 (= H80), D363 (≠ S390), M389 (= M416), G413 (= G440), G415 (= G442), N441 (≠ W482), Q443 (= Q484), Y444 (≠ R485), G445 (≠ A486), F446 (≠ L487), I447 (≠ A488)
Sites not aligning to the query:
1v5gA Crystal structure of the reaction intermediate between pyruvate oxidase containing fad and tpp, and substrate pyruvate (see paper)
28% identity, 92% coverage: 3:549/594 of query aligns to 4:541/589 of 1v5gA
- binding flavin-adenine dinucleotide: G212 (= G215), I213 (≠ A216), G214 (= G217), T236 (≠ A239), G237 (≠ L240), K238 (≠ L241), T254 (≠ I257), Y255 (≠ G258), R256 (≠ L259), V257 (≠ L260), G276 (= G279), S277 (≠ T280), N278 (≠ T281), F279 (= F282), F281 (≠ Y284), D298 (= D300), I299 (= I301), M303 (≠ N305), D317 (= D319), A318 (= A320), P409 (≠ G411)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ C388), N388 (≠ S390), M414 (= M416), G438 (= G440), G440 (= G442), A441 (= A443), N466 (= N474), E468 (≠ D476), Y469 (≠ L477), A470 (vs. gap), F471 (vs. gap), I472 (vs. gap)
- binding magnesium ion: D439 (= D441), N466 (= N474), E468 (≠ D476)
1v5fA Crystal structure of pyruvate oxidase complexed with fad and tpp, from aerococcus viridans (see paper)
28% identity, 92% coverage: 3:549/594 of query aligns to 4:541/589 of 1v5fA
- binding flavin-adenine dinucleotide: G212 (= G215), I213 (≠ A216), G214 (= G217), T236 (≠ A239), G237 (≠ L240), K238 (≠ L241), T254 (≠ I257), Y255 (≠ G258), R256 (≠ L259), V257 (≠ L260), G276 (= G279), S277 (≠ T280), N278 (≠ T281), F279 (= F282), P280 (= P283), F281 (≠ Y284), D298 (= D300), I299 (= I301), M303 (≠ N305), D317 (= D319), A318 (= A320), P409 (≠ G411)
- binding magnesium ion: D439 (= D441), N466 (= N474)
- binding thiamine diphosphate: N388 (≠ S390), S389 (≠ H391), M414 (= M416), G438 (= G440), G440 (= G442), N466 (= N474), Y469 (≠ L477), A470 (vs. gap), F471 (vs. gap), I472 (vs. gap)
2djiA Crystal structure of pyruvate oxidase from aerococcus viridans containing fad (see paper)
28% identity, 92% coverage: 3:549/594 of query aligns to 5:542/590 of 2djiA
- active site: I25 (≠ Y23), S27 (≠ G25), G28 (≠ D26), T29 (≠ G27), L30 (≠ I28), E52 (= E50), S75 (≠ T73), F114 (≠ Q112), Q115 (= Q113), G163 (≠ H161), R257 (≠ L259), E284 (= E286), V387 (≠ C388), A413 (= A414), M415 (= M416), D440 (= D441), N467 (= N474), E469 (≠ D476), Y470 (≠ L477), F472 (vs. gap), I473 (vs. gap), K476 (≠ Q479), Q539 (≠ P546)
- binding flavin-adenine dinucleotide: G213 (= G215), I214 (≠ A216), G215 (= G217), T237 (≠ A239), G238 (≠ L240), K239 (≠ L241), T255 (≠ I257), Y256 (≠ G258), R257 (≠ L259), V258 (≠ L260), G277 (= G279), S278 (≠ T280), N279 (≠ T281), F280 (= F282), P281 (= P283), F282 (≠ Y284), D299 (= D300), I300 (= I301), M304 (≠ N305), D318 (= D319), A319 (= A320), P410 (≠ G411)
1t9dB Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
26% identity, 93% coverage: 3:552/594 of query aligns to 8:548/582 of 1t9dB
- active site: Y28 (= Y23), G30 (= G25), G31 (≠ D26), A32 (≠ G27), I33 (= I28), E54 (= E50), T77 (= T73), F116 (≠ Q112), Q117 (= Q113), E118 (= E114), K166 (≠ H161), R213 (≠ T223), M249 (≠ L259), V276 (vs. gap), V392 (≠ C388), L417 (= L413), G418 (≠ A414), M420 (= M416), D445 (= D441), N472 (= N474), E474 (≠ D476), Q475 (≠ L477), M477 (≠ Q479), V478 (= V480), W481 (≠ Q484), L503 (≠ Y507), G508 (= G512), L509 (≠ F513), K542 (≠ P546)
- binding methyl 2-[({[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G31 (≠ D26), A32 (≠ G27), V106 (≠ Q102), P107 (≠ A103), F116 (≠ Q112), K166 (≠ H161), M249 (≠ L259), D274 (vs. gap), R275 (vs. gap), W481 (≠ Q484)
- binding flavin-adenine dinucleotide: R156 (= R152), G202 (= G215), A203 (= A216), G204 (= G217), N207 (vs. gap), T229 (≠ A239), L230 (= L240), Q231 (≠ L241), L247 (≠ I257), M249 (≠ L259), H250 (≠ L260), G269 (= G279), A270 (≠ T280), R271 (≠ T281), D273 (vs. gap), R275 (vs. gap), V276 (vs. gap), E302 (≠ D300), V303 (≠ I301), N307 (= N305), G320 (= G318), D321 (= D319), A322 (= A320), Q396 (≠ T392), M397 (≠ G393), G415 (= G411), G416 (= G412)
- binding magnesium ion: D445 (= D441), N472 (= N474), E474 (≠ D476)
- binding 2,5-dimethyl-pyrimidin-4-ylamine: E54 (= E50), P80 (= P76), G418 (≠ A414), M420 (= M416), M450 (= M446)
1t9bA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron (see paper)
26% identity, 93% coverage: 3:552/594 of query aligns to 9:549/583 of 1t9bA
- active site: Y29 (= Y23), G31 (= G25), G32 (≠ D26), A33 (≠ G27), I34 (= I28), E55 (= E50), T78 (= T73), F117 (≠ Q112), Q118 (= Q113), E119 (= E114), K167 (≠ H161), R214 (≠ T223), M250 (≠ L259), V277 (vs. gap), V393 (≠ C388), L418 (= L413), G419 (≠ A414), M421 (= M416), D446 (= D441), N473 (= N474), E475 (≠ D476), Q476 (≠ L477), M478 (≠ Q479), V479 (= V480), W482 (≠ Q484), L504 (≠ Y507), G509 (= G512), L510 (≠ F513), K543 (≠ P546)
- binding 1-(2-chlorophenylsulfonyl)-3-(4-methoxy-6-methyl-l,3,5-triazin-2-yl)urea: V107 (≠ Q102), P108 (≠ A103), F117 (≠ Q112), D275 (vs. gap), R276 (vs. gap), M478 (≠ Q479), W482 (≠ Q484)
- binding flavin-adenine dinucleotide: R157 (= R152), G203 (= G215), A204 (= A216), G205 (= G217), N208 (vs. gap), T230 (≠ A239), L231 (= L240), Q232 (≠ L241), M247 (≠ P256), L248 (≠ I257), M250 (≠ L259), H251 (≠ L260), G270 (= G279), A271 (≠ T280), R272 (≠ T281), D274 (vs. gap), R276 (vs. gap), V277 (vs. gap), E303 (≠ D300), V304 (≠ I301), N308 (= N305), D322 (= D319), A323 (= A320), Q397 (≠ T392), M398 (≠ G393), G416 (= G411), G417 (= G412)
- binding magnesium ion: D446 (= D441), N473 (= N474), E475 (≠ D476)
6u9dB Saccharomyces cerevisiae acetohydroxyacid synthase (see paper)
26% identity, 93% coverage: 3:552/594 of query aligns to 13:573/607 of 6u9dB
- active site: Y33 (= Y23), G35 (= G25), G36 (≠ D26), A37 (≠ G27), I38 (= I28), E59 (= E50), T82 (= T73), F121 (≠ Q112), Q122 (= Q113), E123 (= E114), K171 (≠ H161), M274 (≠ L259), V301 (vs. gap), V417 (≠ C388), G443 (≠ A414), M445 (= M416), D470 (= D441), N497 (= N474), E499 (≠ D476), Q500 (≠ L477), M502 (≠ Q479), V503 (= V480), W506 (≠ E483)
- binding methyl 2-[(4,6-dimethoxypyrimidin-2-yl)carbamoylsulfamoylmethyl]benzoate: G36 (≠ D26), V111 (≠ Q102), P112 (≠ A103), F121 (≠ Q112), K171 (≠ H161), D299 (vs. gap), R300 (vs. gap), M502 (≠ Q479), W506 (≠ E483)
- binding flavin-adenine dinucleotide: R161 (= R152), A228 (= A216), G229 (= G217), N232 (vs. gap), T254 (≠ A239), L255 (= L240), Q256 (≠ L241), L272 (≠ I257), M274 (≠ L259), G294 (= G279), R296 (≠ T281), D298 (≠ P283), R300 (vs. gap), V301 (vs. gap), E327 (≠ D300), V328 (≠ I301), N332 (= N305), D346 (= D319), A347 (= A320), M422 (≠ G393), G440 (= G411), G441 (= G412)
- binding magnesium ion: D470 (= D441), N497 (= N474)
- binding thiamine diphosphate: E59 (= E50), P85 (= P76), V417 (≠ C388), G418 (= G389), Q419 (≠ S390), H420 (= H391), G443 (≠ A414), M445 (= M416), A471 (≠ G442), S472 (≠ A443), N497 (= N474), E499 (≠ D476), Q500 (≠ L477), G501 (≠ N478), M502 (≠ Q479), V503 (= V480)
P07342 Acetolactate synthase catalytic subunit, mitochondrial; Acetohydroxy-acid synthase catalytic subunit; AHAS; ALS; EC 2.2.1.6 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 93% coverage: 3:552/594 of query aligns to 93:653/687 of P07342
- R241 (= R152) binding
- 355:376 (vs. 260:281, 14% identical) binding
- 407:426 (vs. 300:319, 20% identical) binding
6lpiB Crystal structure of ahas holo-enzyme (see paper)
29% identity, 75% coverage: 3:447/594 of query aligns to 7:434/539 of 6lpiB
- active site: I27 (≠ Y23), G29 (= G25), G30 (≠ D26), S31 (≠ G27), I32 (= I28), E53 (= E50), C76 (≠ T73), F115 (≠ Q112), Q116 (= Q113), E117 (= E114), K165 (≠ H161), M256 (≠ L259), A283 (vs. gap), V375 (≠ C388), G401 (≠ A414), M403 (= M416), D428 (= D441)
- binding flavin-adenine dinucleotide: R155 (= R152), G212 (= G215), G213 (≠ A216), G214 (= G217), T236 (≠ A239), L237 (= L240), M238 (≠ L241), L254 (≠ I257), M256 (≠ L259), H257 (≠ L260), G276 (= G279), A277 (≠ T280), R278 (≠ T281), D280 (vs. gap), R282 (vs. gap), A283 (vs. gap), D300 (= D300), I301 (= I301), D319 (= D319), V320 (≠ A320), M380 (≠ G393), G398 (= G411)
- binding magnesium ion: D428 (= D441)
- binding thiamine diphosphate: E53 (= E50), C76 (≠ T73), P79 (= P76), G376 (= G389), Q377 (≠ S390), H378 (= H391), G401 (≠ A414), M403 (= M416), G427 (= G440), D428 (= D441), G429 (= G442), S430 (≠ A443), M433 (= M446)
Sites not aligning to the query:
- active site: 455, 457, 458, 460, 461, 464
- binding magnesium ion: 455
- binding thiamine diphosphate: 455, 457, 458, 459, 460, 461
7tzzA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase p197t mutant in complex with bispyribac-sodium (see paper)
29% identity, 90% coverage: 6:541/594 of query aligns to 16:553/582 of 7tzzA
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: M266 (≠ L259), R292 (vs. gap), W489 (= W482)
- binding 2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-2-[(1~{S})-1-(dioxidanyl)-1-oxidanyl-ethyl]-4-methyl-1,3-thiazol-5-yl]ethyl phosphono hydrogen phosphate: V400 (≠ C388), G401 (= G389), Q402 (≠ S390), H403 (= H391), G426 (≠ A414), M428 (= M416), G452 (= G440), D453 (= D441), G454 (= G442), S455 (≠ A443), L483 (= L477), G484 (≠ N478), M485 (≠ Q479), V486 (= V480)
- binding flavin-adenine dinucleotide: R161 (= R152), G222 (= G215), G223 (≠ A216), G224 (= G217), T246 (≠ A239), L247 (= L240), M248 (≠ L241), M263 (≠ P256), L264 (≠ I257), M266 (≠ L259), H267 (≠ L260), G286 (= G279), R288 (≠ T281), V293 (vs. gap), D310 (= D300), I311 (= I301), D329 (= D319), V330 (vs. gap), M405 (≠ G393), G423 (= G411)
- binding magnesium ion: A37 (≠ G27), T82 (= T73), S83 (= S74), Q122 (= Q113), Y381 (≠ R369), D453 (= D441), M458 (= M446), Q461 (≠ N449), N480 (= N474), H482 (≠ D476), K533 (≠ P521)
Sites not aligning to the query:
1n0hA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorimuron ethyl (see paper)
26% identity, 93% coverage: 3:552/594 of query aligns to 11:565/599 of 1n0hA
- active site: Y31 (= Y23), G33 (= G25), G34 (≠ D26), A35 (≠ G27), I36 (= I28), E57 (= E50), T80 (= T73), F119 (≠ Q112), Q120 (= Q113), E121 (= E114), K169 (vs. gap), R230 (≠ T223), M266 (≠ L259), V293 (vs. gap), V409 (≠ C388), L434 (= L413), G435 (≠ A414), M437 (= M416), D462 (= D441), N489 (= N474), E491 (≠ D476), Q492 (≠ L477), M494 (≠ Q479), V495 (= V480), W498 (≠ E483), L520 (≠ Y507), G525 (= G512), L526 (≠ F513), K559 (≠ P546)
- binding 4-{[(4'-amino-2'-methylpyrimidin-5'-yl)methyl]amino}pent-3-enyl diphosphate: V409 (≠ C388), G410 (= G389), Q411 (≠ S390), H412 (= H391), G435 (≠ A414), M437 (= M416), G461 (= G440), D462 (= D441), A463 (≠ G442), S464 (≠ A443), M467 (= M446), N489 (= N474), E491 (≠ D476), Q492 (≠ L477), G493 (≠ N478), V495 (= V480)
- binding 2-[[[[(4-chloro-6-methoxy-2-pyrimidinyl)amino]carbonyl]amino]sulfonyl]benzoic acid ethyl ester: G34 (≠ D26), A35 (≠ G27), V109 (≠ Q102), P110 (≠ A103), F119 (≠ Q112), K169 (vs. gap), M266 (≠ L259), D291 (vs. gap), R292 (vs. gap), V495 (= V480), W498 (≠ E483)
- binding flavin-adenine dinucleotide: R159 (= R152), G219 (= G215), A220 (= A216), G221 (= G217), N224 (vs. gap), T246 (≠ A239), L247 (= L240), Q248 (≠ L241), L264 (≠ I257), G265 (= G258), M266 (≠ L259), H267 (≠ L260), G286 (= G279), A287 (≠ T280), R288 (≠ T281), D290 (≠ P283), R292 (vs. gap), V293 (vs. gap), E319 (≠ D300), V320 (≠ I301), N324 (= N305), G337 (= G318), D338 (= D319), A339 (= A320), M414 (≠ G393), G432 (= G411), G433 (= G412)
- binding magnesium ion: D462 (= D441), N489 (= N474), E491 (≠ D476)
- binding thiamine diphosphate: Y31 (= Y23), E57 (= E50), P83 (= P76)
P17597 Acetolactate synthase, chloroplastic; AtALS; Acetohydroxy-acid synthase; Protein CHLORSULFURON RESISTANT 1; EC 2.2.1.6 from Arabidopsis thaliana (Mouse-ear cress) (see 8 papers)
29% identity, 90% coverage: 6:541/594 of query aligns to 101:638/670 of P17597
- A122 (≠ G27) mutation to V: Reduced catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- M124 (≠ N29) mutation to E: Reduced catalytic activity. Resistant to imidazolinone herbicides and reduced sensitivity to sulfonylurea herbicides.; mutation to I: No effect on catalytic activity. Increased resistance to imidazolinone herbicides.
- E144 (= E50) binding
- S186 (≠ H92) binding
- P197 (≠ A103) mutation to S: In csr1-1/GH50; resistant to sulfonylurea but not to imidazolinone herbicides.
- R199 (≠ A105) mutation R->A,E: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- Q207 (= Q113) binding
- K220 (≠ N126) binding
- R246 (= R152) binding ; binding
- K256 (≠ H161) binding
- G308 (≠ A216) binding
- TL 331:332 (≠ AL 239:240) binding
- C340 (≠ D248) modified: Cysteine sulfinic acid (-SO2H)
- LGMH 349:352 (≠ IGLL 257:260) binding
- GVRFD 371:375 (≠ GTTFP 279:283) binding
- DR 376:377 (vs. gap) binding
- DI 395:396 (= DI 300:301) binding
- DV 414:415 (≠ D- 319) binding
- QH 487:488 (≠ SH 390:391) binding
- GG 508:509 (= GG 411:412) binding
- GAM 511:513 (≠ ATM 414:416) binding
- D538 (= D441) binding
- DGS 538:540 (≠ DGA 441:443) binding
- N565 (= N474) binding
- NQHLGM 565:570 (≠ NRDLNQ 474:479) binding
- H567 (≠ D476) binding
- W574 (= W482) binding ; mutation to L: Increased catalytic activity. Resistant to imidazolinone and sulfonylurea herbicides.; mutation to S: Slightly decreased catalytic activity. Resistant to imidazolinone and sulfonylurea herbicides.
Sites not aligning to the query:
- 653 binding ; S→A: No effect on catalytic activity or sensitivity to herbicides.; S→F: No effect on catalytic activity. Resistant to imidazolinone herbicides and also slightly sulfonylurea-resistant.; S→N: In csr1-2/GH90; no effect on catalytic activity. Resistant to imidazolinone but not to sulfonylurea herbicides.; S→T: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
Query Sequence
>N515DRAFT_1567 FitnessBrowser__Dyella79:N515DRAFT_1567
MQTVGDFILERLSDWGIQRVFGYPGDGINGLMGAMGRAAERFDYVRVRHEEMAAFMACGH
AKFTGRIGVCLATSGPGAIHLLNGLYDARLDHMPVLAIVGQQARAALGSDYQQEVDLQAL
FKDVANYAQTVTTPAQVRHVLDRAIRIAQAERAVTVVIVPHDLQLMPAVPSPPRKHGNVY
SGVGLALPHPQPTAMELERAASVINASERVAILVGAGALDASTEVRQLAERLDAGVAKAL
LGKTVLPDDLPYVTGPIGLLGSKPSWRLMNGCDTLLMIGTTFPYSEFLPPDGQARAVQID
IAPRNMSLRYPAEVNLVGDAAQTIRRLLPLLSEKRNADWRERIEVDVRKWWRLLEGRAMA
PASPINPQRVFWELSDCLPDRAIVCGDCGSHTGWFARDVKLREGMLASLSGGLATMGGGV
PYAIAAKMAWPDRPVLAIVGDGAMQMNGNAELVTVKQYWRRWSDPRFVVLVVSNRDLNQV
TWEQRALAGDPKFDAAQDVEPFPYARYAELLGFRGLRVDRPEQITDAWRQAFAADCPVVI
EAETDPNVPPLPPHVNWQQAREYLAALAGPDSDRGPVARQTVRQVLAGLFGAED
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