SitesBLAST
Comparing WP_003554655.1 NCBI__GCF_000023185.1:WP_003554655.1 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)
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, 92% coverage: 5:554/600 of query aligns to 6:546/572 of P07003
- E50 (= E50) binding thiamine diphosphate
- 183:334 (vs. 190:341, 38% identical) FAD-binding domain
- S210 (≠ R215) binding FAD
- LR 234:235 (≠ LL 239:240) binding FAD
- TGLI 251:254 (≠ IGIL 256:259) binding FAD
- TQFPY 274:278 (≠ SSFPY 279:283) binding FAD
- D292 (= D299) binding FAD
- S297 (≠ R304) binding FAD
- DI 311:312 (≠ DA 318:319) binding FAD
- 335:530 (vs. 342:538, 30% identical) PP-binding domain
- T382 (≠ Q389) binding thiamine diphosphate
- FN 403:404 (≠ GA 410:411) binding FAD
- GSM 406:408 (≠ ASM 413:415) binding thiamine diphosphate
- D433 (= D440) binding Mg(2+)
- DGG 433:435 (= DGG 440:442) binding thiamine diphosphate
- N460 (= N467) binding Mg(2+)
- 460:466 (vs. 467:473, 29% identical) binding thiamine diphosphate
- V462 (≠ M469) binding Mg(2+)
- F465 (≠ Q472) Moves into active site upon enzyme activation, plays a role in electron transfer
- A533 (≠ M541) 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, 92% coverage: 5:554/600 of query aligns to 5:545/571 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 (≠ I258), A279 (≠ E285), V379 (≠ S387), G405 (≠ A413), M407 (= M415), D432 (= D440), N459 (= N467), V461 (≠ M469), L462 (= L470), F464 (≠ Q472), V465 (≠ I473), E468 (= E476), K528 (≠ Q537)
- binding flavin-adenine dinucleotide: G208 (= G214), S209 (≠ R215), G210 (= G216), A232 (= A238), L233 (= L239), R234 (≠ L240), T250 (≠ I256), G251 (= G257), I253 (≠ L259), G272 (= G278), T273 (≠ S279), Q274 (≠ S280), F275 (= F281), Y277 (= Y283), D291 (= D299), I292 (≠ S300), S296 (≠ R304), G309 (= G317), D310 (= D318), I311 (≠ A319), T383 (= T391), F402 (≠ G410), N403 (≠ A411)
- binding magnesium ion: D432 (= D440), N459 (= N467)
- binding thiamine diphosphate: T24 (≠ P24), E49 (= E50), S72 (≠ T73), G76 (= G77), H79 (≠ N80), G380 (= G388), T381 (≠ Q389), P382 (≠ N390), M407 (= M415), G431 (= G439), D432 (= D440), G433 (= G441), G434 (= G442), N459 (= N467), V461 (≠ M469), L462 (= L470), G463 (≠ N471)
Sites not aligning to the query:
2ezuA Pyruvate oxidase variant f479w in complex with reaction intermediate 2-acetyl-thiamin diphosphate (see paper)
30% identity, 91% coverage: 8:553/600 of query aligns to 9:554/585 of 2ezuA
- active site: I24 (≠ L23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), F113 (≠ Q112), Q114 (= Q113), E115 (≠ D114), V162 (≠ N161), R256 (≠ I258), E283 (= E285), V386 (≠ S387), A412 (= A413), M414 (= M415), D439 (= D440), N466 (= N467), Q468 (≠ M469), Y469 (≠ L470), W471 (≠ Q472), I472 (= I473), E475 (= E476), G538 (≠ Q537)
- binding flavin-adenine dinucleotide: H93 (≠ Q92), G212 (= G214), I213 (≠ R215), G214 (= G216), T236 (≠ A238), Y237 (≠ L239), P238 (≠ L240), A254 (≠ I256), N255 (≠ G257), R256 (≠ I258), V257 (≠ L259), G276 (= G278), N277 (≠ S279), N278 (≠ S280), P280 (= P282), F281 (≠ Y283), D298 (= D299), I299 (≠ S300), K303 (≠ R304), D317 (= D318), A318 (= A319), N409 (≠ G410)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ S387), D388 (≠ Q389), M414 (= M415), G438 (= G439), G440 (= G441), N466 (= N467), Q468 (≠ M469), Y469 (≠ L470), G470 (≠ N471), W471 (≠ Q472), I472 (= I473)
- binding magnesium ion: D439 (= D440), N466 (= N467), Q468 (≠ M469)
- binding pyruvic acid: L547 (≠ M546), L549 (≠ K548), D550 (= D549), S554 (= S553)
2ez9A Pyruvate oxidase variant f479w in complex with reaction intermediate analogue 2-phosphonolactyl-thiamin diphosphate (see paper)
30% identity, 91% coverage: 8:553/600 of query aligns to 9:554/585 of 2ez9A
- active site: I24 (≠ L23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), F113 (≠ Q112), Q114 (= Q113), E115 (≠ D114), V162 (≠ N161), R256 (≠ I258), E283 (= E285), V386 (≠ S387), A412 (= A413), M414 (= M415), D439 (= D440), N466 (= N467), Q468 (≠ M469), Y469 (≠ L470), W471 (≠ Q472), I472 (= I473), E475 (= E476), G538 (≠ Q537)
- binding flavin-adenine dinucleotide: H93 (≠ Q92), G212 (= G214), I213 (≠ R215), G214 (= G216), T236 (≠ A238), Y237 (≠ L239), P238 (≠ L240), A254 (≠ I256), N255 (≠ G257), R256 (≠ I258), V257 (≠ L259), G276 (= G278), N277 (≠ S279), N278 (≠ S280), P280 (= P282), F281 (≠ Y283), D298 (= D299), I299 (≠ S300), K303 (≠ R304), D317 (= D318), A318 (= A319), N409 (≠ G410)
- binding magnesium ion: D439 (= D440), N466 (= N467), Q468 (≠ M469)
- 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 (≠ S387), D388 (≠ Q389), M414 (= M415), G438 (= G439), G440 (= G441), N466 (= N467), Q468 (≠ M469), Y469 (≠ L470), G470 (≠ N471), W471 (≠ Q472), I472 (= I473), E475 (= E476)
2ez8A Pyruvate oxidase variant f479w in complex with reaction intermediate 2-lactyl-thiamin diphosphate (see paper)
30% identity, 91% coverage: 8:553/600 of query aligns to 9:554/585 of 2ez8A
- active site: I24 (≠ L23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), F113 (≠ Q112), Q114 (= Q113), E115 (≠ D114), V162 (≠ N161), R256 (≠ I258), E283 (= E285), V386 (≠ S387), A412 (= A413), M414 (= M415), D439 (= D440), N466 (= N467), Q468 (≠ M469), Y469 (≠ L470), W471 (≠ Q472), I472 (= I473), E475 (= E476), G538 (≠ Q537)
- binding flavin-adenine dinucleotide: H93 (≠ Q92), G212 (= G214), I213 (≠ R215), G214 (= G216), T236 (≠ A238), Y237 (≠ L239), P238 (≠ L240), A254 (≠ I256), N255 (≠ G257), R256 (≠ I258), V257 (≠ L259), G276 (= G278), N277 (≠ S279), N278 (≠ S280), P280 (= P282), F281 (≠ Y283), D298 (= D299), I299 (≠ S300), K303 (≠ R304), D317 (= D318), A318 (= A319), N390 (≠ T391), N409 (≠ G410)
- binding magnesium ion: D439 (= D440), N466 (= N467), Q468 (≠ M469)
- binding pyruvic acid: L547 (≠ M546), L549 (≠ K548), D550 (= D549), M553 (≠ K552), S554 (= S553)
- 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 (≠ Q389), M414 (= M415), G438 (= G439), G440 (= G441), N466 (= N467), Q468 (≠ M469), Y469 (≠ L470), G470 (≠ N471), W471 (≠ Q472), I472 (= I473)
2ez4B Pyruvate oxidase variant f479w (see paper)
30% identity, 91% coverage: 8:553/600 of query aligns to 9:554/585 of 2ez4B
- active site: I24 (≠ L23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), F113 (≠ Q112), Q114 (= Q113), E115 (≠ D114), V162 (≠ N161), R256 (≠ I258), E283 (= E285), V386 (≠ S387), A412 (= A413), M414 (= M415), D439 (= D440), N466 (= N467), Q468 (≠ M469), Y469 (≠ L470), W471 (≠ Q472), I472 (= I473), E475 (= E476), G538 (≠ Q537)
- binding flavin-adenine dinucleotide: H93 (≠ Q92), G212 (= G214), I213 (≠ R215), G214 (= G216), T236 (≠ A238), Y237 (≠ L239), P238 (≠ L240), A254 (≠ I256), N255 (≠ G257), R256 (≠ I258), V257 (≠ L259), G276 (= G278), N277 (≠ S279), N278 (≠ S280), P280 (= P282), F281 (≠ Y283), D298 (= D299), I299 (≠ S300), K303 (≠ R304), D317 (= D318), A318 (= A319), N409 (≠ G410)
- binding magnesium ion: D439 (= D440), N466 (= N467), Q468 (≠ M469)
- binding phosphate ion: W471 (≠ Q472), E475 (= E476)
- binding thiamine diphosphate: D388 (≠ Q389), A412 (= A413), M414 (= M415), G438 (= G439), D439 (= D440), G440 (= G441), G441 (= G442), N466 (= N467), Q468 (≠ M469), Y469 (≠ L470), G470 (≠ N471), W471 (≠ Q472), I472 (= I473)
4feeA High-resolution structure of pyruvate oxidase in complex with reaction intermediate 2-hydroxyethyl-thiamin diphosphate carbanion-enamine, crystal b (see paper)
30% identity, 91% coverage: 8:553/600 of query aligns to 9:554/586 of 4feeA
- binding flavin-adenine dinucleotide: H93 (≠ Q92), G212 (= G214), I213 (≠ R215), G214 (= G216), T236 (≠ A238), Y237 (≠ L239), P238 (≠ L240), A254 (≠ I256), N255 (≠ G257), V257 (≠ L259), G276 (= G278), N277 (≠ S279), N278 (≠ S280), P280 (= P282), F281 (≠ Y283), D298 (= D299), I299 (≠ S300), K303 (≠ R304), D317 (= D318), A318 (= A319), N390 (≠ T391), N409 (≠ G410)
- binding magnesium ion: D439 (= D440), N466 (= N467), Q468 (≠ M469)
- binding pyruvic acid: N255 (≠ G257), R256 (≠ I258), L547 (≠ M546), L549 (≠ K548), D550 (= D549), M553 (≠ K552), S554 (= S553)
- 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 (≠ S387), D388 (≠ Q389), A412 (= A413), M414 (= M415), G438 (= G439), G440 (= G441), N466 (= N467), Q468 (≠ M469), Y469 (≠ L470), G470 (≠ N471), F471 (≠ Q472), I472 (= I473)
1powA The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from lactobacillus plantarum (see paper)
30% identity, 91% coverage: 8:553/600 of query aligns to 9:554/585 of 1powA
- active site: I24 (≠ L23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), F113 (≠ Q112), Q114 (= Q113), E115 (≠ D114), V162 (≠ N161), R256 (≠ I258), E283 (= E285), V386 (≠ S387), A412 (= A413), M414 (= M415), D439 (= D440), N466 (= N467), Q468 (≠ M469), Y469 (≠ L470), F471 (≠ Q472), I472 (= I473), E475 (= E476), G538 (≠ Q537)
- binding flavin-adenine dinucleotide: H93 (≠ Q92), G212 (= G214), I213 (≠ R215), G214 (= G216), T236 (≠ A238), Y237 (≠ L239), A254 (≠ I256), V257 (≠ L259), G276 (= G278), N277 (≠ S279), N278 (≠ S280), Y279 (≠ F281), P280 (= P282), F281 (≠ Y283), D298 (= D299), I299 (≠ S300), K303 (≠ R304), D317 (= D318), A318 (= A319), N409 (≠ G410)
- binding magnesium ion: D439 (= D440), N466 (= N467), Q468 (≠ M469)
- binding thiamine diphosphate: D388 (≠ Q389), M414 (= M415), G440 (= G441), N466 (= N467), Q468 (≠ M469), Y469 (≠ L470), G470 (≠ N471), F471 (≠ Q472), I472 (= I473)
2djiA Crystal structure of pyruvate oxidase from aerococcus viridans containing fad (see paper)
28% identity, 96% coverage: 8:582/600 of query aligns to 10:581/590 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 (≠ I258), E284 (= E285), V387 (≠ S387), A413 (= A413), M415 (= M415), D440 (= D440), N467 (= N467), E469 (≠ Q477), Y470 (≠ M478), F472 (= F480), I473 (≠ L481), K476 (≠ P484), Q539 (= Q537)
- binding flavin-adenine dinucleotide: G213 (= G214), I214 (≠ R215), G215 (= G216), T237 (≠ A238), G238 (≠ L239), K239 (≠ L240), T255 (≠ I256), Y256 (≠ G257), R257 (≠ I258), V258 (≠ L259), G277 (= G278), S278 (= S279), N279 (≠ S280), F280 (= F281), P281 (= P282), F282 (≠ Y283), D299 (= D299), I300 (≠ S300), M304 (≠ R304), D318 (= D318), A319 (= A319), P410 (≠ G410)
1v5gA Crystal structure of the reaction intermediate between pyruvate oxidase containing fad and tpp, and substrate pyruvate (see paper)
28% identity, 96% coverage: 8:582/600 of query aligns to 9:580/589 of 1v5gA
- binding flavin-adenine dinucleotide: G212 (= G214), I213 (≠ R215), G214 (= G216), T236 (≠ A238), G237 (≠ L239), K238 (≠ L240), T254 (≠ I256), Y255 (≠ G257), R256 (≠ I258), V257 (≠ L259), G276 (= G278), S277 (= S279), N278 (≠ S280), F279 (= F281), F281 (≠ Y283), D298 (= D299), I299 (≠ S300), M303 (≠ R304), D317 (= D318), A318 (= A319), P409 (≠ G410)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ S387), N388 (≠ Q389), M414 (= M415), G438 (= G439), G440 (= G441), A441 (≠ G442), N466 (= N467), E468 (≠ Q477), Y469 (≠ M478), A470 (≠ M479), F471 (= F480), I472 (≠ L481)
- binding magnesium ion: D439 (= D440), N466 (= N467), E468 (≠ Q477)
1v5fA Crystal structure of pyruvate oxidase complexed with fad and tpp, from aerococcus viridans (see paper)
28% identity, 96% coverage: 8:582/600 of query aligns to 9:580/589 of 1v5fA
- binding flavin-adenine dinucleotide: G212 (= G214), I213 (≠ R215), G214 (= G216), T236 (≠ A238), G237 (≠ L239), K238 (≠ L240), T254 (≠ I256), Y255 (≠ G257), R256 (≠ I258), V257 (≠ L259), G276 (= G278), S277 (= S279), N278 (≠ S280), F279 (= F281), P280 (= P282), F281 (≠ Y283), D298 (= D299), I299 (≠ S300), M303 (≠ R304), D317 (= D318), A318 (= A319), P409 (≠ G410)
- binding magnesium ion: D439 (= D440), N466 (= N467)
- binding thiamine diphosphate: N388 (≠ Q389), S389 (≠ N390), M414 (= M415), G438 (= G439), G440 (= G441), N466 (= N467), Y469 (≠ M478), A470 (≠ M479), F471 (= F480), I472 (≠ L481)
1y9dD Pyruvate oxidase variant v265a from lactobacillus plantarum (see paper)
30% identity, 91% coverage: 8:553/600 of query aligns to 9:529/560 of 1y9dD
- active site: I24 (≠ L23), G26 (= G25), G27 (≠ D26), S28 (≠ G27), I29 (= I28), E51 (= E50), S74 (≠ T73), E108 (≠ D114), V155 (≠ N161), R241 (≠ I258), V361 (≠ S387), A387 (= A413), M389 (= M415), D414 (= D440), N441 (= N467), Q443 (≠ M469), Y444 (≠ L470), F446 (≠ Q472), I447 (= I473), E450 (= E476), G513 (≠ Q537)
- binding flavin-adenine dinucleotide: I198 (≠ R215), G199 (= G216), T221 (≠ A238), P223 (≠ L240), G261 (= G278), N262 (≠ S279), N263 (≠ S280), D273 (= D299), I274 (≠ S300), K278 (≠ R304), D292 (= D318), A293 (= A319)
- binding magnesium ion: D414 (= D440), N441 (= N467), Q443 (≠ M469)
- binding thiamine diphosphate: E51 (= E50), S74 (≠ T73), P77 (= P76), H81 (≠ N80), D363 (≠ Q389), M389 (= M415), G413 (= G439), G415 (= G441), N441 (= N467), Q443 (≠ M469), Y444 (≠ L470), G445 (≠ N471), F446 (≠ Q472), I447 (= I473)
9ev3A Corynebacterium glutamicum pyruvate:quinone oxidoreductase (pqo) purified from bacteria grown in acetate minimal medium (see paper)
31% identity, 96% coverage: 5:579/600 of query aligns to 5:575/577 of 9ev3A
- binding flavin-adenine dinucleotide: G208 (= G214), G210 (= G216), A232 (= A238), L233 (= L239), G234 (≠ L240), G251 (= G257), L253 (= L259), G272 (= G278), T273 (≠ S279), D274 (≠ S280), F275 (= F281), P276 (= P282), Y277 (= Y283), D290 (= D299), I291 (≠ S300), H295 (≠ R304), D309 (= D318), V310 (≠ A319), N385 (≠ T391), F405 (≠ G410), R406 (≠ A411)
- binding magnesium ion: D435 (= D440), N462 (= N467), S464 (≠ M469)
- binding thiamine diphosphate: G382 (= G388), M383 (≠ Q389), M410 (= M415), G434 (= G439), D435 (= D440), G436 (= G441), G437 (= G442), M440 (= M445), S464 (≠ M469), L465 (= L470), G466 (≠ N471), M467 (≠ Q472), V468 (≠ I473)
P09114 Acetolactate synthase 2, chloroplastic; ALS II; Acetohydroxy-acid synthase II; Acetolactate synthase II; EC 2.2.1.6 from Nicotiana tabacum (Common tobacco) (see paper)
28% identity, 90% coverage: 3:543/600 of query aligns to 92:643/664 of P09114
- P191 (≠ Y103) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
- W568 (= W475) mutation to L: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191.
P09342 Acetolactate synthase 1, chloroplastic; ALS I; Acetohydroxy-acid synthase I; Acetolactate synthase I; EC 2.2.1.6 from Nicotiana tabacum (Common tobacco) (see 2 papers)
28% identity, 90% coverage: 3:543/600 of query aligns to 95:646/667 of P09342
- C161 (= C70) modified: Disulfide link with 307
- P194 (≠ Y103) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ V217) modified: Disulfide link with 161
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, 88% coverage: 16:543/600 of query aligns to 106:653/687 of P07342
- R241 (= R152) binding FAD
- 355:376 (vs. 259:280, 23% identical) binding FAD
- 407:426 (vs. 299:318, 20% identical) binding FAD
6u9dB Saccharomyces cerevisiae acetohydroxyacid synthase (see paper)
28% identity, 88% coverage: 16:543/600 of query aligns to 26:573/607 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 (≠ I258), V301 (vs. gap), V417 (≠ S387), G443 (≠ A413), M445 (= M415), D470 (= D440), N497 (= N467), E499 (vs. gap), Q500 (vs. gap), M502 (= M469), V503 (≠ L470), W506 (= W475)
- 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 (= M469), W506 (= W475)
- binding flavin-adenine dinucleotide: R161 (= R152), A228 (≠ R215), G229 (= G216), N232 (≠ G219), T254 (≠ A238), L255 (= L239), Q256 (≠ L240), L272 (≠ I256), M274 (≠ I258), G294 (= G278), R296 (≠ S280), D298 (≠ P282), R300 (vs. gap), V301 (vs. gap), E327 (≠ D299), V328 (≠ S300), N332 (≠ R304), D346 (= D318), A347 (= A319), M422 (≠ E392), G440 (= G410), G441 (≠ A411)
- binding magnesium ion: D470 (= D440), N497 (= N467)
- binding thiamine diphosphate: E59 (= E50), P85 (= P76), V417 (≠ S387), G418 (= G388), Q419 (= Q389), H420 (≠ N390), G443 (≠ A413), M445 (= M415), A471 (≠ G441), S472 (≠ G442), N497 (= N467), E499 (vs. gap), Q500 (vs. gap), G501 (= G468), M502 (= M469), V503 (≠ L470)
1t9bB Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron (see paper)
27% identity, 88% coverage: 16:543/600 of query aligns to 22:561/595 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 (≠ I258), V289 (vs. gap), V405 (≠ S387), L430 (= L412), G431 (≠ A413), M433 (= M415), D458 (= D440), N485 (= N467), E487 (vs. gap), Q488 (vs. gap), M490 (= M469), V491 (≠ L470), W494 (= W475), L516 (≠ A498), G521 (= G503), L522 (≠ G504), K555 (≠ Q537)
- 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 (= M469), W494 (= W475)
- binding flavin-adenine dinucleotide: R157 (= R152), G215 (= G214), A216 (≠ R215), G217 (= G216), N220 (≠ G219), T242 (≠ A238), L243 (= L239), Q244 (≠ L240), M259 (≠ G255), L260 (≠ I256), M262 (≠ I258), H263 (≠ L259), G282 (= G278), A283 (≠ S279), R284 (≠ S280), D286 (≠ P282), R288 (vs. gap), V289 (vs. gap), E315 (≠ D299), V316 (≠ S300), N320 (≠ R304), G333 (= G317), D334 (= D318), A335 (= A319), Q409 (≠ T391), M410 (≠ E392), G428 (= G410), G429 (≠ A411)
- binding magnesium ion: D458 (= D440), N485 (= N467), E487 (vs. gap)
1t9cA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, sulfometuron methyl (see paper)
28% identity, 88% coverage: 16:543/600 of query aligns to 22:562/596 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 (≠ I258), V290 (vs. gap), V406 (≠ S387), L431 (= L412), G432 (≠ A413), M434 (= M415), D459 (= D440), N486 (= N467), E488 (vs. gap), Q489 (vs. gap), M491 (= M469), V492 (≠ L470), W495 (= W475), L517 (≠ A498), G522 (= G503), L523 (≠ G504), K556 (≠ Q537)
- 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 (= W475)
- binding flavin-adenine dinucleotide: R157 (= R152), G216 (= G214), A217 (≠ R215), G218 (= G216), N221 (≠ G219), T243 (≠ A238), L244 (= L239), Q245 (≠ L240), L261 (≠ I256), M263 (≠ I258), H264 (≠ L259), G283 (= G278), A284 (≠ S279), R285 (≠ S280), D287 (≠ P282), R289 (vs. gap), V290 (vs. gap), E316 (≠ D299), V317 (≠ S300), N321 (≠ R304), G334 (= G317), D335 (= D318), A336 (= A319), M411 (≠ E392), G429 (= G410), G430 (≠ A411)
- binding magnesium ion: D459 (= D440), N486 (= N467), E488 (vs. gap)
1t9dA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
28% identity, 88% coverage: 16:543/600 of query aligns to 22:562/596 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 (≠ I258), V290 (vs. gap), V406 (≠ S387), L431 (= L412), G432 (≠ A413), M434 (= M415), D459 (= D440), N486 (= N467), E488 (vs. gap), Q489 (vs. gap), M491 (= M469), V492 (≠ L470), W495 (= W475), L517 (≠ A498), G522 (= G503), L523 (≠ G504), K556 (≠ Q537)
- 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 (≠ I258), D288 (vs. gap), R289 (vs. gap), W495 (= W475)
- binding flavin-adenine dinucleotide: R157 (= R152), G216 (= G214), A217 (≠ R215), G218 (= G216), N221 (≠ G219), T243 (≠ A238), L244 (= L239), Q245 (≠ L240), M260 (≠ G255), L261 (≠ I256), H264 (≠ L259), G283 (= G278), A284 (≠ S279), R285 (≠ S280), D287 (≠ P282), R289 (vs. gap), V290 (vs. gap), E316 (≠ D299), V317 (≠ S300), N321 (≠ R304), G334 (= G317), D335 (= D318), A336 (= A319), Q410 (≠ T391), M411 (≠ E392), G429 (= G410), G430 (≠ A411)
- binding magnesium ion: D459 (= D440), N486 (= N467), E488 (vs. gap)
- binding 2,5-dimethyl-pyrimidin-4-ylamine: E55 (= E50), P81 (= P76), Q118 (= Q113), G432 (≠ A413), M434 (= M415), M464 (= M445)
Query Sequence
>WP_003554655.1 NCBI__GCF_000023185.1:WP_003554655.1
MPNAADILIDTLIEWDVKVIFGLPGDGINGVMEALRKRQDQIRFIQVRHEESAAFMASAY
AKFTGNLGVCLATSGPGGTNLLTGLYDAKLDQMPVLAITGTQYHDLIETFTQQDVDLTRV
FDNVALYNAHVSDASHMENVASLACRSALSRRGVAHLSIANDVQEMDGKSRSKRNRPKHV
PNRYFHGRQVPEEIELDRAARILNDARKVAILAGRGVVGAAEELREIADLLAAPVAKALL
GKTALADDDPLTTGGIGILGTAPSQEIMEQCDAVLIVGSSFPYIEYYPRPEAARGVQIDS
DPQRIGLRFPVDAGLVGDARETLRLLRPRLTRKTDRSFLEKAQTAMSEWRRKMETMETER
SAPLKPQAVVRAFGRRIAADGVLVADSGQNTELAARHIDLRTTNQFAVSGALASMASGLP
YAIAAGAADPKRPIYAVIGDGGFGMQLGEFSTAVRMALPLKLLVICNGMLNQIAWEQMMF
LGNPQFACELAPIDFAKAAEAMGGRGFTIRRFDQIEPTLTEAFSVAGPVVIQAMVDQYEP
MMPPKMPKDYAKSFRQALPETPGHRAIEANVSRSPLREMMDAGEQEKELSENTTDLPGIP
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