SitesBLAST
Comparing WP_011969672.1 NCBI__GCF_000017145.1:WP_011969672.1 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)
3ey9A Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from escherichia coli (see paper)
32% identity, 91% coverage: 8:555/605 of query aligns to 8:545/571 of 3ey9A
- active site: V23 (≠ L23), G25 (= G25), D26 (= D26), S27 (≠ G27), L28 (≠ I28), E49 (= E50), S72 (≠ T73), F111 (≠ Q112), Q112 (= Q113), G160 (≠ N161), L252 (≠ I259), A279 (≠ E286), V379 (≠ S388), G405 (≠ A414), M407 (= M416), D432 (= D441), N459 (= N468), V461 (≠ M470), L462 (= L471), F464 (≠ Q473), V465 (≠ I474), E468 (= E477), K528 (≠ R538)
- binding flavin-adenine dinucleotide: G208 (= G215), S209 (≠ R216), G210 (= G217), A232 (= A239), L233 (= L240), R234 (≠ L241), T250 (≠ I257), G251 (= G258), I253 (≠ L260), G272 (= G279), T273 (≠ S280), Q274 (≠ T281), F275 (= F282), Y277 (= Y284), D291 (= D300), I292 (≠ H301), S296 (≠ R305), G309 (= G318), D310 (≠ A319), I311 (≠ A320), T383 (= T392), F402 (≠ G411), N403 (≠ A412)
- binding magnesium ion: D432 (= D441), N459 (= N468)
- binding thiamine diphosphate: T24 (≠ P24), E49 (= E50), S72 (≠ T73), G76 (= G77), H79 (≠ N80), G380 (= G389), T381 (≠ Q390), P382 (≠ N391), M407 (= M416), G431 (= G440), D432 (= D441), G433 (= G442), G434 (= G443), N459 (= N468), V461 (≠ M470), L462 (= L471), G463 (≠ N472)
Sites not aligning to the query:
P07003 Pyruvate dehydrogenase [ubiquinone]; Pyruvate oxidase; POX; Pyruvate:ubiquinone-8 oxidoreductase; EC 1.2.5.1 from Escherichia coli (strain K12) (see 4 papers)
32% identity, 91% coverage: 8:555/605 of query aligns to 9:546/572 of P07003
- E50 (= E50) binding thiamine diphosphate
- 183:334 (vs. 183:342, 34% identical) FAD-binding domain
- S210 (≠ R216) binding FAD
- LR 234:235 (≠ LL 240:241) binding FAD
- TGLI 251:254 (≠ IGIL 257:260) binding FAD
- TQFPY 274:278 (≠ STFPY 280:284) binding FAD
- D292 (= D300) binding FAD
- S297 (≠ R305) binding FAD
- DI 311:312 (≠ AA 319:320) binding FAD
- 335:530 (vs. 343:539, 31% identical) PP-binding domain
- T382 (≠ Q390) binding thiamine diphosphate
- FN 403:404 (≠ GA 411:412) binding FAD
- GSM 406:408 (≠ ASM 414:416) binding thiamine diphosphate
- D433 (= D441) binding Mg(2+)
- DGG 433:435 (= DGG 441:443) binding thiamine diphosphate
- N460 (= N468) binding Mg(2+)
- 460:466 (vs. 468:474, 29% identical) binding thiamine diphosphate
- V462 (≠ M470) binding Mg(2+)
- F465 (≠ Q473) Moves into active site upon enzyme activation, plays a role in electron transfer
- A533 (≠ L542) 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.
2ezuA Pyruvate oxidase variant f479w in complex with reaction intermediate 2-acetyl-thiamin diphosphate (see paper)
29% identity, 90% coverage: 8:552/605 of query aligns to 9:552/585 of 2ezuA
- active site: I24 (≠ L23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), F113 (= F110), Q114 (= Q113), E115 (≠ D114), V162 (≠ N161), R256 (≠ I259), E283 (= E286), V386 (≠ S388), A412 (= A414), M414 (= M416), D439 (= D441), N466 (= N468), Q468 (≠ M470), Y469 (≠ L471), W471 (≠ Q473), I472 (= I474), E475 (= E477), G538 (≠ R538)
- binding flavin-adenine dinucleotide: H93 (≠ Q92), G212 (= G215), I213 (≠ R216), G214 (= G217), T236 (≠ A239), Y237 (≠ L240), P238 (≠ L241), A254 (≠ I257), N255 (≠ G258), R256 (≠ I259), V257 (≠ L260), G276 (= G279), N277 (≠ S280), N278 (≠ T281), P280 (= P283), F281 (≠ Y284), D298 (= D300), I299 (≠ H301), K303 (≠ R305), D317 (≠ A319), A318 (= A320), N409 (≠ G411)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ S388), D388 (≠ Q390), M414 (= M416), G438 (= G440), G440 (= G442), N466 (= N468), Q468 (≠ M470), Y469 (≠ L471), G470 (≠ N472), W471 (≠ Q473), I472 (= I474)
- binding magnesium ion: D439 (= D441), N466 (= N468), Q468 (≠ M470)
- binding pyruvic acid: L547 (≠ M547), L549 (≠ E549), D550 (= D550)
Sites not aligning to the query:
2ez9A Pyruvate oxidase variant f479w in complex with reaction intermediate analogue 2-phosphonolactyl-thiamin diphosphate (see paper)
29% identity, 90% coverage: 8:552/605 of query aligns to 9:552/585 of 2ez9A
- active site: I24 (≠ L23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), F113 (= F110), Q114 (= Q113), E115 (≠ D114), V162 (≠ N161), R256 (≠ I259), E283 (= E286), V386 (≠ S388), A412 (= A414), M414 (= M416), D439 (= D441), N466 (= N468), Q468 (≠ M470), Y469 (≠ L471), W471 (≠ Q473), I472 (= I474), E475 (= E477), G538 (≠ R538)
- binding flavin-adenine dinucleotide: H93 (≠ Q92), G212 (= G215), I213 (≠ R216), G214 (= G217), T236 (≠ A239), Y237 (≠ L240), P238 (≠ L241), A254 (≠ I257), N255 (≠ G258), R256 (≠ I259), V257 (≠ L260), G276 (= G279), N277 (≠ S280), N278 (≠ T281), P280 (= P283), F281 (≠ Y284), D298 (= D300), I299 (≠ H301), K303 (≠ R305), D317 (≠ A319), A318 (= A320), N409 (≠ G411)
- binding magnesium ion: D439 (= D441), N466 (= N468), Q468 (≠ M470)
- 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 (≠ S388), D388 (≠ Q390), M414 (= M416), G438 (= G440), G440 (= G442), N466 (= N468), Q468 (≠ M470), Y469 (≠ L471), G470 (≠ N472), W471 (≠ Q473), I472 (= I474), E475 (= E477)
2ez8A Pyruvate oxidase variant f479w in complex with reaction intermediate 2-lactyl-thiamin diphosphate (see paper)
29% identity, 90% coverage: 8:552/605 of query aligns to 9:552/585 of 2ez8A
- active site: I24 (≠ L23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), F113 (= F110), Q114 (= Q113), E115 (≠ D114), V162 (≠ N161), R256 (≠ I259), E283 (= E286), V386 (≠ S388), A412 (= A414), M414 (= M416), D439 (= D441), N466 (= N468), Q468 (≠ M470), Y469 (≠ L471), W471 (≠ Q473), I472 (= I474), E475 (= E477), G538 (≠ R538)
- binding flavin-adenine dinucleotide: H93 (≠ Q92), G212 (= G215), I213 (≠ R216), G214 (= G217), T236 (≠ A239), Y237 (≠ L240), P238 (≠ L241), A254 (≠ I257), N255 (≠ G258), R256 (≠ I259), V257 (≠ L260), G276 (= G279), N277 (≠ S280), N278 (≠ T281), P280 (= P283), F281 (≠ Y284), D298 (= D300), I299 (≠ H301), K303 (≠ R305), D317 (≠ A319), A318 (= A320), N390 (≠ T392), N409 (≠ G411)
- binding magnesium ion: D439 (= D441), N466 (= N468), Q468 (≠ M470)
- binding pyruvic acid: L547 (≠ M547), L549 (≠ E549), D550 (= D550)
- 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 (≠ Q390), M414 (= M416), G438 (= G440), G440 (= G442), N466 (= N468), Q468 (≠ M470), Y469 (≠ L471), G470 (≠ N472), W471 (≠ Q473), I472 (= I474)
Sites not aligning to the query:
2ez4B Pyruvate oxidase variant f479w (see paper)
29% identity, 90% coverage: 8:552/605 of query aligns to 9:552/585 of 2ez4B
- active site: I24 (≠ L23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), F113 (= F110), Q114 (= Q113), E115 (≠ D114), V162 (≠ N161), R256 (≠ I259), E283 (= E286), V386 (≠ S388), A412 (= A414), M414 (= M416), D439 (= D441), N466 (= N468), Q468 (≠ M470), Y469 (≠ L471), W471 (≠ Q473), I472 (= I474), E475 (= E477), G538 (≠ R538)
- binding flavin-adenine dinucleotide: H93 (≠ Q92), G212 (= G215), I213 (≠ R216), G214 (= G217), T236 (≠ A239), Y237 (≠ L240), P238 (≠ L241), A254 (≠ I257), N255 (≠ G258), R256 (≠ I259), V257 (≠ L260), G276 (= G279), N277 (≠ S280), N278 (≠ T281), P280 (= P283), F281 (≠ Y284), D298 (= D300), I299 (≠ H301), K303 (≠ R305), D317 (≠ A319), A318 (= A320), N409 (≠ G411)
- binding magnesium ion: D439 (= D441), N466 (= N468), Q468 (≠ M470)
- binding phosphate ion: W471 (≠ Q473), E475 (= E477)
- binding thiamine diphosphate: D388 (≠ Q390), A412 (= A414), M414 (= M416), G438 (= G440), D439 (= D441), G440 (= G442), G441 (= G443), N466 (= N468), Q468 (≠ M470), Y469 (≠ L471), G470 (≠ N472), W471 (≠ Q473), I472 (= I474)
4feeA High-resolution structure of pyruvate oxidase in complex with reaction intermediate 2-hydroxyethyl-thiamin diphosphate carbanion-enamine, crystal b (see paper)
29% identity, 90% coverage: 8:552/605 of query aligns to 9:552/586 of 4feeA
- binding flavin-adenine dinucleotide: H93 (≠ Q92), G212 (= G215), I213 (≠ R216), G214 (= G217), T236 (≠ A239), Y237 (≠ L240), P238 (≠ L241), A254 (≠ I257), N255 (≠ G258), V257 (≠ L260), G276 (= G279), N277 (≠ S280), N278 (≠ T281), P280 (= P283), F281 (≠ Y284), D298 (= D300), I299 (≠ H301), K303 (≠ R305), D317 (≠ A319), A318 (= A320), N390 (≠ T392), N409 (≠ G411)
- binding magnesium ion: D439 (= D441), N466 (= N468), Q468 (≠ M470)
- binding pyruvic acid: N255 (≠ G258), R256 (≠ I259), L547 (≠ M547), L549 (≠ E549), D550 (= D550)
- 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 (≠ S388), D388 (≠ Q390), A412 (= A414), M414 (= M416), G438 (= G440), G440 (= G442), N466 (= N468), Q468 (≠ M470), Y469 (≠ L471), G470 (≠ N472), F471 (≠ Q473), I472 (= I474)
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)
29% identity, 90% coverage: 8:552/605 of query aligns to 9:552/585 of 1powA
- active site: I24 (≠ L23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), F113 (= F110), Q114 (= Q113), E115 (≠ D114), V162 (≠ N161), R256 (≠ I259), E283 (= E286), V386 (≠ S388), A412 (= A414), M414 (= M416), D439 (= D441), N466 (= N468), Q468 (≠ M470), Y469 (≠ L471), F471 (≠ Q473), I472 (= I474), E475 (= E477), G538 (≠ R538)
- binding flavin-adenine dinucleotide: H93 (≠ Q92), G212 (= G215), I213 (≠ R216), G214 (= G217), T236 (≠ A239), Y237 (≠ L240), A254 (≠ I257), V257 (≠ L260), G276 (= G279), N277 (≠ S280), N278 (≠ T281), Y279 (≠ F282), P280 (= P283), F281 (≠ Y284), D298 (= D300), I299 (≠ H301), K303 (≠ R305), D317 (≠ A319), A318 (= A320), N409 (≠ G411)
- binding magnesium ion: D439 (= D441), N466 (= N468), Q468 (≠ M470)
- binding thiamine diphosphate: D388 (≠ Q390), M414 (= M416), G440 (= G442), N466 (= N468), Q468 (≠ M470), Y469 (≠ L471), G470 (≠ N472), F471 (≠ Q473), I472 (= I474)
2djiA Crystal structure of pyruvate oxidase from aerococcus viridans containing fad (see paper)
27% identity, 88% coverage: 8:542/605 of query aligns to 10:543/590 of 2djiA
- active site: I25 (≠ L23), S27 (≠ G25), G28 (≠ D26), T29 (≠ G27), L30 (≠ I28), E52 (= E50), S75 (≠ T73), F114 (≠ Q112), Q115 (= Q113), G163 (≠ N161), R257 (≠ I259), E284 (= E286), V387 (≠ S388), A413 (= A414), M415 (= M416), D440 (= D441), N467 (= N468), E469 (≠ Q478), Y470 (≠ M479), F472 (= F481), I473 (≠ L482), K476 (≠ P485), Q539 (≠ R538)
- binding flavin-adenine dinucleotide: G213 (= G215), I214 (≠ R216), G215 (= G217), T237 (≠ A239), G238 (≠ L240), K239 (≠ L241), T255 (≠ I257), Y256 (≠ G258), R257 (≠ I259), V258 (≠ L260), G277 (= G279), S278 (= S280), N279 (≠ T281), F280 (= F282), P281 (= P283), F282 (≠ Y284), D299 (= D300), I300 (≠ H301), M304 (≠ R305), D318 (≠ A319), A319 (= A320), P410 (≠ G411)
1v5gA Crystal structure of the reaction intermediate between pyruvate oxidase containing fad and tpp, and substrate pyruvate (see paper)
27% identity, 88% coverage: 8:542/605 of query aligns to 9:542/589 of 1v5gA
- binding flavin-adenine dinucleotide: G212 (= G215), I213 (≠ R216), G214 (= G217), T236 (≠ A239), G237 (≠ L240), K238 (≠ L241), T254 (≠ I257), Y255 (≠ G258), R256 (≠ I259), V257 (≠ L260), G276 (= G279), S277 (= S280), N278 (≠ T281), F279 (= F282), F281 (≠ Y284), D298 (= D300), I299 (≠ H301), M303 (≠ R305), D317 (≠ A319), A318 (= A320), P409 (≠ G411)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ S388), N388 (≠ Q390), M414 (= M416), G438 (= G440), G440 (= G442), A441 (≠ G443), N466 (= N468), E468 (≠ Q478), Y469 (≠ M479), A470 (≠ M480), F471 (= F481), I472 (≠ L482)
- binding magnesium ion: D439 (= D441), N466 (= N468), E468 (≠ Q478)
1v5fA Crystal structure of pyruvate oxidase complexed with fad and tpp, from aerococcus viridans (see paper)
27% identity, 88% coverage: 8:542/605 of query aligns to 9:542/589 of 1v5fA
- binding flavin-adenine dinucleotide: G212 (= G215), I213 (≠ R216), G214 (= G217), T236 (≠ A239), G237 (≠ L240), K238 (≠ L241), T254 (≠ I257), Y255 (≠ G258), R256 (≠ I259), V257 (≠ L260), G276 (= G279), S277 (= S280), N278 (≠ T281), F279 (= F282), P280 (= P283), F281 (≠ Y284), D298 (= D300), I299 (≠ H301), M303 (≠ R305), D317 (≠ A319), A318 (= A320), P409 (≠ G411)
- binding magnesium ion: D439 (= D441), N466 (= N468)
- binding thiamine diphosphate: N388 (≠ Q390), S389 (≠ N391), M414 (= M416), G438 (= G440), G440 (= G442), N466 (= N468), Y469 (≠ M479), A470 (≠ M480), F471 (= F481), I472 (≠ L482)
1y9dD Pyruvate oxidase variant v265a from lactobacillus plantarum (see paper)
29% identity, 90% coverage: 8:552/605 of query aligns to 9:527/560 of 1y9dD
- active site: I24 (≠ L23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), E108 (≠ D114), V155 (≠ N161), R241 (≠ I259), V361 (≠ S388), A387 (= A414), M389 (= M416), D414 (= D441), N441 (= N468), Q443 (≠ M470), Y444 (≠ L471), F446 (≠ Q473), I447 (= I474), E450 (= E477), G513 (≠ R538)
- binding flavin-adenine dinucleotide: I198 (≠ R216), G199 (= G217), T221 (≠ A239), P223 (≠ L241), G261 (= G279), N262 (≠ S280), N263 (≠ T281), D273 (= D300), I274 (≠ H301), K278 (≠ R305), D292 (≠ A319), A293 (= A320)
- binding magnesium ion: D414 (= D441), N441 (= N468), Q443 (≠ M470)
- binding thiamine diphosphate: E51 (= E50), S74 (≠ T73), P77 (= P76), H81 (≠ N80), D363 (≠ Q390), M389 (= M416), G413 (= G440), G415 (= G442), N441 (= N468), Q443 (≠ M470), Y444 (≠ L471), G445 (≠ N472), F446 (≠ Q473), I447 (= I474)
6u9dB Saccharomyces cerevisiae acetohydroxyacid synthase (see paper)
28% identity, 95% coverage: 7:580/605 of query aligns to 17:606/607 of 6u9dB
- active site: Y33 (≠ L23), G35 (= G25), G36 (≠ D26), A37 (≠ G27), I38 (= I28), E59 (= E50), T82 (= T73), F121 (≠ Q112), Q122 (= Q113), E123 (≠ D114), K171 (≠ N161), M274 (≠ I259), V301 (vs. gap), V417 (≠ S388), G443 (≠ A414), M445 (= M416), D470 (= D441), N497 (= N468), E499 (vs. gap), Q500 (vs. gap), M502 (= M470), V503 (≠ L471), W506 (= W476)
- binding methyl 2-[(4,6-dimethoxypyrimidin-2-yl)carbamoylsulfamoylmethyl]benzoate: G36 (≠ D26), V111 (≠ Q102), P112 (≠ Y103), F121 (≠ Q112), K171 (≠ N161), D299 (vs. gap), R300 (vs. gap), M502 (= M470), W506 (= W476)
- binding flavin-adenine dinucleotide: R161 (= R152), A228 (≠ R216), G229 (= G217), N232 (vs. gap), T254 (≠ A239), L255 (= L240), Q256 (≠ L241), L272 (≠ I257), M274 (≠ I259), G294 (= G279), R296 (≠ T281), D298 (≠ P283), R300 (vs. gap), V301 (vs. gap), E327 (≠ D300), V328 (≠ H301), N332 (≠ R305), D346 (≠ A319), A347 (= A320), M422 (≠ E393), G440 (= G411), G441 (≠ A412)
- binding magnesium ion: D470 (= D441), N497 (= N468)
- binding thiamine diphosphate: E59 (= E50), P85 (= P76), V417 (≠ S388), G418 (= G389), Q419 (= Q390), H420 (≠ N391), G443 (≠ A414), M445 (= M416), A471 (≠ G442), S472 (≠ G443), N497 (= N468), E499 (vs. gap), Q500 (vs. gap), G501 (vs. gap), M502 (= M470), V503 (≠ L471)
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)
28% identity, 95% coverage: 7:580/605 of query aligns to 97:686/687 of P07342
- R241 (= R152) binding FAD
- 355:376 (vs. 260:281, 23% identical) binding FAD
- 407:426 (vs. 300:319, 15% identical) binding FAD
1t9cA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, sulfometuron methyl (see paper)
28% identity, 95% coverage: 7:580/605 of query aligns to 13:595/596 of 1t9cA
- active site: Y29 (≠ L23), G31 (= G25), G32 (≠ D26), A33 (≠ G27), I34 (= I28), E55 (= E50), T78 (= T73), F117 (≠ Q112), Q118 (= Q113), E119 (≠ D114), K167 (≠ N161), R227 (vs. gap), M263 (≠ I259), V290 (vs. gap), V406 (≠ S388), L431 (= L413), G432 (≠ A414), M434 (= M416), D459 (= D441), N486 (= N468), E488 (vs. gap), Q489 (vs. gap), M491 (= M470), V492 (≠ L471), W495 (= W476), L517 (≠ A499), G522 (= G504), L523 (≠ G505), K556 (≠ R538)
- binding methyl 2-[({[(4,6-dimethylpyrimidin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (≠ D26), V107 (≠ Q102), P108 (≠ Y103), F117 (≠ Q112), K167 (≠ N161), D288 (vs. gap), R289 (vs. gap), W495 (= W476)
- binding flavin-adenine dinucleotide: R157 (= R152), G216 (= G215), A217 (≠ R216), G218 (= G217), N221 (vs. gap), T243 (≠ A239), L244 (= L240), Q245 (≠ L241), L261 (≠ I257), M263 (≠ I259), H264 (≠ L260), G283 (= G279), A284 (≠ S280), R285 (≠ T281), D287 (≠ P283), R289 (vs. gap), V290 (vs. gap), E316 (≠ D300), V317 (≠ H301), N321 (≠ R305), G334 (= G318), D335 (≠ A319), A336 (= A320), M411 (≠ E393), G429 (= G411), G430 (≠ A412)
- binding magnesium ion: D459 (= D441), N486 (= N468), E488 (vs. gap)
1t9bB Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron (see paper)
28% identity, 95% coverage: 7:580/605 of query aligns to 13:594/595 of 1t9bB
- active site: Y29 (≠ L23), G31 (= G25), G32 (≠ D26), A33 (≠ G27), I34 (= I28), E55 (= E50), T78 (= T73), F117 (≠ Q112), Q118 (= Q113), E119 (≠ D114), K167 (≠ N161), R226 (vs. gap), M262 (≠ I259), V289 (vs. gap), V405 (≠ S388), L430 (= L413), G431 (≠ A414), M433 (= M416), D458 (= D441), N485 (= N468), E487 (vs. gap), Q488 (vs. gap), M490 (= M470), V491 (≠ L471), W494 (= W476), L516 (≠ A499), G521 (= G504), L522 (≠ G505), K555 (≠ R538)
- binding 1-(2-chlorophenylsulfonyl)-3-(4-methoxy-6-methyl-l,3,5-triazin-2-yl)urea: V107 (≠ Q102), P108 (≠ Y103), D287 (vs. gap), R288 (vs. gap), M490 (= M470), W494 (= W476)
- binding flavin-adenine dinucleotide: R157 (= R152), G215 (= G215), A216 (≠ R216), G217 (= G217), N220 (vs. gap), T242 (≠ A239), L243 (= L240), Q244 (≠ L241), M259 (≠ G256), L260 (≠ I257), M262 (≠ I259), H263 (≠ L260), G282 (= G279), A283 (≠ S280), R284 (≠ T281), D286 (≠ P283), R288 (vs. gap), V289 (vs. gap), E315 (≠ D300), V316 (≠ H301), N320 (≠ R305), G333 (= G318), D334 (≠ A319), A335 (= A320), Q409 (≠ T392), M410 (≠ E393), G428 (= G411), G429 (≠ A412)
- binding magnesium ion: D458 (= D441), N485 (= N468), E487 (vs. gap)
1t9dA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
28% identity, 95% coverage: 7:580/605 of query aligns to 13:595/596 of 1t9dA
- active site: Y29 (≠ L23), G31 (= G25), G32 (≠ D26), A33 (≠ G27), I34 (= I28), E55 (= E50), T78 (= T73), F117 (≠ Q112), Q118 (= Q113), E119 (≠ D114), K167 (≠ N161), R227 (vs. gap), M263 (≠ I259), V290 (vs. gap), V406 (≠ S388), L431 (= L413), G432 (≠ A414), M434 (= M416), D459 (= D441), N486 (= N468), E488 (vs. gap), Q489 (vs. gap), M491 (= M470), V492 (≠ L471), W495 (= W476), L517 (≠ A499), G522 (= G504), L523 (≠ G505), K556 (≠ R538)
- binding methyl 2-[({[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (≠ D26), A33 (≠ G27), V107 (≠ Q102), P108 (≠ Y103), F117 (≠ Q112), K167 (≠ N161), M263 (≠ I259), D288 (vs. gap), R289 (vs. gap), W495 (= W476)
- binding flavin-adenine dinucleotide: R157 (= R152), G216 (= G215), A217 (≠ R216), G218 (= G217), N221 (vs. gap), T243 (≠ A239), L244 (= L240), Q245 (≠ L241), M260 (≠ G256), L261 (≠ I257), H264 (≠ L260), G283 (= G279), A284 (≠ S280), R285 (≠ T281), D287 (≠ P283), R289 (vs. gap), V290 (vs. gap), E316 (≠ D300), V317 (≠ H301), N321 (≠ R305), G334 (= G318), D335 (≠ A319), A336 (= A320), Q410 (≠ T392), M411 (≠ E393), G429 (= G411), G430 (≠ A412)
- binding magnesium ion: D459 (= D441), N486 (= N468), E488 (vs. gap)
- binding 2,5-dimethyl-pyrimidin-4-ylamine: E55 (= E50), P81 (= P76), Q118 (= Q113), G432 (≠ A414), M434 (= M416), M464 (= M446)
1t9aA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, tribenuron methyl (see paper)
28% identity, 95% coverage: 7:580/605 of query aligns to 14:596/597 of 1t9aA
- active site: Y30 (≠ L23), G32 (= G25), G33 (≠ D26), A34 (≠ G27), I35 (= I28), E56 (= E50), T79 (= T73), F118 (≠ Q112), Q119 (= Q113), E120 (≠ D114), K168 (≠ N161), R228 (vs. gap), M264 (≠ I259), V291 (vs. gap), V407 (≠ S388), L432 (= L413), G433 (≠ A414), M435 (= M416), D460 (= D441), N487 (= N468), E489 (vs. gap), Q490 (vs. gap), M492 (= M470), V493 (≠ L471), W496 (= W476), L518 (≠ A499), G523 (= G504), L524 (≠ G505), K557 (≠ R538)
- binding methyl 2-[4-methoxy-6-methyl-1,3,5-trazin-2-yl(methyl)carbamoylsulfamoyl]benzoate: G33 (≠ D26), V108 (≠ Q102), P109 (≠ Y103), F118 (≠ Q112), K168 (≠ N161), M264 (≠ I259), D289 (vs. gap), R290 (vs. gap), M492 (= M470), V493 (≠ L471), W496 (= W476)
- binding flavin-adenine dinucleotide: R158 (= R152), G217 (= G215), A218 (≠ R216), G219 (= G217), N222 (vs. gap), T244 (≠ A239), L245 (= L240), Q246 (≠ L241), L262 (≠ I257), M264 (≠ I259), H265 (≠ L260), G284 (= G279), A285 (≠ S280), R286 (≠ T281), D288 (≠ P283), R290 (vs. gap), V291 (vs. gap), E317 (≠ D300), V318 (≠ H301), N322 (≠ R305), G335 (= G318), D336 (≠ A319), A337 (= A320), Q411 (≠ T392), M412 (≠ E393), G430 (= G411), G431 (≠ A412)
- binding magnesium ion: D460 (= D441), N487 (= N468), E489 (vs. gap)
- binding propyl trihydrogen diphosphate: V407 (≠ S388), G408 (= G389), Q409 (= Q390), H410 (≠ N391), M435 (= M416), G459 (= G440), D460 (= D441), A461 (≠ G442), S462 (≠ G443), N487 (= N468), E489 (vs. gap), Q490 (vs. gap), G491 (vs. gap), M492 (= M470)
- binding 5-{[ethyl(methyl)amino]methyl}-2-methyl-5,6-dihydropyrimidin-4-amine: G433 (≠ A414), M435 (= M416), M465 (= M446)
1n0hA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorimuron ethyl (see paper)
28% identity, 95% coverage: 7:580/605 of query aligns to 15:598/599 of 1n0hA
- active site: Y31 (≠ L23), G33 (= G25), G34 (≠ D26), A35 (≠ G27), I36 (= I28), E57 (= E50), T80 (= T73), F119 (≠ Q112), Q120 (= Q113), E121 (≠ D114), K169 (≠ N161), R230 (vs. gap), M266 (≠ I259), V293 (vs. gap), V409 (≠ S388), L434 (= L413), G435 (≠ A414), M437 (= M416), D462 (= D441), N489 (= N468), E491 (vs. gap), Q492 (vs. gap), M494 (= M470), V495 (≠ L471), W498 (= W476), L520 (≠ A499), G525 (= G504), L526 (≠ G505), K559 (≠ R538)
- binding 4-{[(4'-amino-2'-methylpyrimidin-5'-yl)methyl]amino}pent-3-enyl diphosphate: V409 (≠ S388), G410 (= G389), Q411 (= Q390), H412 (≠ N391), G435 (≠ A414), M437 (= M416), G461 (= G440), D462 (= D441), A463 (≠ G442), S464 (≠ G443), M467 (= M446), N489 (= N468), E491 (vs. gap), Q492 (vs. gap), G493 (vs. gap), V495 (≠ L471)
- binding 2-[[[[(4-chloro-6-methoxy-2-pyrimidinyl)amino]carbonyl]amino]sulfonyl]benzoic acid ethyl ester: G34 (≠ D26), A35 (≠ G27), V109 (≠ Q102), P110 (≠ Y103), F119 (≠ Q112), K169 (≠ N161), M266 (≠ I259), D291 (vs. gap), R292 (vs. gap), V495 (≠ L471), W498 (= W476)
- binding flavin-adenine dinucleotide: R159 (= R152), G219 (= G215), A220 (≠ R216), G221 (= G217), N224 (vs. gap), T246 (≠ A239), L247 (= L240), Q248 (≠ L241), L264 (≠ I257), G265 (= G258), M266 (≠ I259), H267 (≠ L260), G286 (= G279), A287 (≠ S280), R288 (≠ T281), D290 (≠ P283), R292 (vs. gap), V293 (vs. gap), E319 (≠ D300), V320 (≠ H301), N324 (≠ R305), G337 (= G318), D338 (≠ A319), A339 (= A320), M414 (≠ E393), G432 (= G411), G433 (≠ A412)
- binding magnesium ion: D462 (= D441), N489 (= N468), E491 (vs. gap)
- binding thiamine diphosphate: Y31 (≠ L23), E57 (= E50), P83 (= P76)
1t9dB Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
28% identity, 95% coverage: 7:580/605 of query aligns to 12:581/582 of 1t9dB
- active site: Y28 (≠ L23), G30 (= G25), G31 (≠ D26), A32 (≠ G27), I33 (= I28), E54 (= E50), T77 (= T73), F116 (≠ Q112), Q117 (= Q113), E118 (≠ D114), K166 (≠ N161), R213 (vs. gap), M249 (≠ I259), V276 (vs. gap), V392 (≠ S388), L417 (= L413), G418 (≠ A414), M420 (= M416), D445 (= D441), N472 (= N468), E474 (vs. gap), Q475 (vs. gap), M477 (= M470), V478 (≠ L471), W481 (= W476), L503 (≠ A499), G508 (= G504), L509 (≠ G505), K542 (≠ R538)
- 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 (≠ Y103), F116 (≠ Q112), K166 (≠ N161), M249 (≠ I259), D274 (vs. gap), R275 (vs. gap), W481 (= W476)
- binding flavin-adenine dinucleotide: R156 (= R152), G202 (= G215), A203 (≠ R216), G204 (= G217), N207 (vs. gap), T229 (≠ A239), L230 (= L240), Q231 (≠ L241), L247 (≠ I257), M249 (≠ I259), H250 (≠ L260), G269 (= G279), A270 (≠ S280), R271 (≠ T281), D273 (≠ P283), R275 (vs. gap), V276 (vs. gap), E302 (≠ D300), V303 (≠ H301), N307 (≠ R305), G320 (= G318), D321 (≠ A319), A322 (= A320), Q396 (≠ T392), M397 (≠ E393), G415 (= G411), G416 (≠ A412)
- binding magnesium ion: D445 (= D441), N472 (= N468), E474 (vs. gap)
- binding 2,5-dimethyl-pyrimidin-4-ylamine: E54 (= E50), P80 (= P76), G418 (≠ A414), M420 (= M416), M450 (= M446)
Query Sequence
>WP_011969672.1 NCBI__GCF_000017145.1:WP_011969672.1
MPNASDILIETLIEWKVEVVFGLPGDGINGIMEALRRRQDRIRFVSVRHEQSAAFMACAY
AKFTGRLGVCLATSGPGGTNLLTGLYDAKLDQMPVLAITGMQYHDLIETFSQQDVDLTRV
FENVAVYNAQVNDAAHMENLANLACRSALSKRGVAHLSIANDVQERMAGGGRSRRNREGH
MPSRFFEGRLVPREDDILRAADLLNAGRKVAILAGRGALEAKGLLRETADLLGAPVAKAL
LGKAVLPDDDPFTTGGIGILGTVPSQEIMQQCDTLLIVGSTFPYIEYYPKPHAATGIQID
HDPQRIGLRYPVEVGLVGAAGETLRMLNERLQRKADRTFLEQAQEKTRNWRRELRAMEGD
RSSPLKPQAAVGAFGRRIAANGIVVTDSGQNTELAARHVDLGADHMFAVSGALASMASGL
PYAIAAGIAMPARPIYAVVGDGGFAMQLGEFATAVRYEIPLKLLVIRNDMLNQIAWEQMM
FLGNPQFACELPPIDFAAAAEAMGGRGFTIRSFDEIDGVLDQAFAAEGPVVIQALVDRYE
PLMPPKMPEDYARNFRAALPQTPGHEKIEENLRHSSAGRKVTEEEPQAPHEAAPDANTGD
LPGIP
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