SitesBLAST
Comparing AZOBR_RS29985 FitnessBrowser__azobra:AZOBR_RS29985 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)
34% identity, 100% coverage: 1:584/584 of query aligns to 1:563/572 of P07003
- 1:182 (vs. 1:192, 34% identical) Pyr domain
- E50 (= E51) binding
- 183:334 (vs. 193:344, 36% identical) FAD-binding domain
- S210 (≠ Q218) binding
- LR 234:235 (≠ LL 242:243) binding
- TGLI 251:254 (≠ VGLL 259:262) binding
- TQFPY 274:278 (≠ STFPY 282:286) binding
- D292 (= D302) binding
- S297 (≠ R307) binding
- DI 311:312 (≠ DC 321:322) binding
- 335:530 (vs. 345:541, 35% identical) PP-binding domain
- T382 (= T392) binding
- FN 403:404 (≠ GN 413:414) binding
- GSM 406:408 (≠ ATM 416:418) binding
- D433 (= D443) binding
- DGG 433:435 (= DGG 443:445) binding
- N460 (= N470) binding
- 460:466 (vs. 470:476, 43% identical) binding
- V462 (≠ S472) binding
- F465 (≠ Q475) Moves into active site upon enzyme activation, plays a role in electron transfer
- A533 (≠ P544) mutation to T: In poxB11; poor activity in vivo, no longer activated by lipids.
- YM 549:550 (≠ AL 560:561) In vitro cleavage to yield alpha-peptide
- A553 (≠ G564) mutation to V: In poxB14; poor activity in vivo, no longer activated by lipids.
- D560 (≠ R581) mutation to P: In poxB15; normal activity.
Sites not aligning to the query:
- 531:572 Membrane-binding domain
- 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.
- 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)
34% identity, 99% coverage: 4:584/584 of query aligns to 3:562/571 of 3ey9A
- active site: V23 (≠ M24), G25 (= G26), D26 (= D27), S27 (≠ G28), L28 (≠ I29), E49 (= E51), S72 (≠ T74), F111 (≠ Q113), Q112 (= Q114), G160 (≠ V162), L252 (= L261), A279 (≠ E288), V379 (≠ S390), G405 (≠ A416), M407 (= M418), D432 (= D443), N459 (= N470), V461 (≠ S472), L462 (= L473), F464 (≠ Q475), V465 (≠ I476), E468 (= E479), K528 (≠ T540)
- binding flavin-adenine dinucleotide: G208 (= G217), S209 (≠ Q218), G210 (= G219), A232 (= A241), L233 (= L242), R234 (≠ L243), T250 (≠ V259), G251 (= G260), I253 (≠ L262), G272 (= G281), T273 (≠ S282), Q274 (≠ T283), F275 (= F284), Y277 (= Y286), D291 (= D302), I292 (= I303), S296 (≠ R307), G309 (= G320), D310 (= D321), I311 (≠ C322), T383 (≠ A394), F402 (≠ G413), N403 (= N414), Y548 (≠ A560)
- binding magnesium ion: D432 (= D443), N459 (= N470)
- binding thiamine diphosphate: T24 (≠ P25), E49 (= E51), S72 (≠ T74), G76 (= G78), H79 (= H81), G380 (= G391), T381 (= T392), P382 (≠ I393), M407 (= M418), G431 (= G442), D432 (= D443), G433 (= G444), G434 (= G445), N459 (= N470), V461 (≠ S472), L462 (= L473), G463 (= G474)
2ezuA Pyruvate oxidase variant f479w in complex with reaction intermediate 2-acetyl-thiamin diphosphate (see paper)
34% identity, 92% coverage: 9:546/584 of query aligns to 9:543/585 of 2ezuA
- active site: I24 (≠ M24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E51), S74 (≠ T74), F113 (≠ Q113), Q114 (= Q114), E115 (≠ D115), V162 (= V162), R256 (≠ L261), E283 (= E288), V386 (≠ S390), A412 (= A416), M414 (= M418), D439 (= D443), N466 (= N470), Q468 (≠ S472), Y469 (≠ L473), W471 (≠ Q475), I472 (= I476), E475 (= E479), G538 (≠ N541)
- binding flavin-adenine dinucleotide: H93 (= H93), G212 (= G217), I213 (≠ Q218), G214 (= G219), T236 (≠ A241), Y237 (≠ L242), P238 (≠ L243), A254 (≠ V259), N255 (≠ G260), R256 (≠ L261), V257 (≠ L262), G276 (= G281), N277 (≠ S282), N278 (≠ T283), P280 (= P285), F281 (≠ Y286), D298 (= D302), I299 (= I303), K303 (≠ R307), D317 (= D321), A318 (≠ C322), N409 (≠ G413)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ S390), D388 (≠ T392), M414 (= M418), G438 (= G442), G440 (= G444), N466 (= N470), Q468 (≠ S472), Y469 (≠ L473), G470 (= G474), W471 (≠ Q475), I472 (= I476)
- binding magnesium ion: D439 (= D443), N466 (= N470), Q468 (≠ S472)
Sites not aligning to the query:
2ez9A Pyruvate oxidase variant f479w in complex with reaction intermediate analogue 2-phosphonolactyl-thiamin diphosphate (see paper)
34% identity, 92% coverage: 9:546/584 of query aligns to 9:543/585 of 2ez9A
- active site: I24 (≠ M24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E51), S74 (≠ T74), F113 (≠ Q113), Q114 (= Q114), E115 (≠ D115), V162 (= V162), R256 (≠ L261), E283 (= E288), V386 (≠ S390), A412 (= A416), M414 (= M418), D439 (= D443), N466 (= N470), Q468 (≠ S472), Y469 (≠ L473), W471 (≠ Q475), I472 (= I476), E475 (= E479), G538 (≠ N541)
- binding flavin-adenine dinucleotide: H93 (= H93), G212 (= G217), I213 (≠ Q218), G214 (= G219), T236 (≠ A241), Y237 (≠ L242), P238 (≠ L243), A254 (≠ V259), N255 (≠ G260), R256 (≠ L261), V257 (≠ L262), G276 (= G281), N277 (≠ S282), N278 (≠ T283), P280 (= P285), F281 (≠ Y286), D298 (= D302), I299 (= I303), K303 (≠ R307), D317 (= D321), A318 (≠ C322), N409 (≠ G413)
- binding magnesium ion: D439 (= D443), N466 (= N470), Q468 (≠ S472)
- 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 (≠ S390), D388 (≠ T392), M414 (= M418), G438 (= G442), G440 (= G444), N466 (= N470), Q468 (≠ S472), Y469 (≠ L473), G470 (= G474), W471 (≠ Q475), I472 (= I476), E475 (= E479)
2ez8A Pyruvate oxidase variant f479w in complex with reaction intermediate 2-lactyl-thiamin diphosphate (see paper)
34% identity, 92% coverage: 9:546/584 of query aligns to 9:543/585 of 2ez8A
- active site: I24 (≠ M24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E51), S74 (≠ T74), F113 (≠ Q113), Q114 (= Q114), E115 (≠ D115), V162 (= V162), R256 (≠ L261), E283 (= E288), V386 (≠ S390), A412 (= A416), M414 (= M418), D439 (= D443), N466 (= N470), Q468 (≠ S472), Y469 (≠ L473), W471 (≠ Q475), I472 (= I476), E475 (= E479), G538 (≠ N541)
- binding flavin-adenine dinucleotide: H93 (= H93), G212 (= G217), I213 (≠ Q218), G214 (= G219), T236 (≠ A241), Y237 (≠ L242), P238 (≠ L243), A254 (≠ V259), N255 (≠ G260), R256 (≠ L261), V257 (≠ L262), G276 (= G281), N277 (≠ S282), N278 (≠ T283), P280 (= P285), F281 (≠ Y286), D298 (= D302), I299 (= I303), K303 (≠ R307), D317 (= D321), A318 (≠ C322), N390 (≠ A394), N409 (≠ G413)
- binding magnesium ion: D439 (= D443), N466 (= N470), Q468 (≠ S472)
- 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 (≠ T392), M414 (= M418), G438 (= G442), G440 (= G444), N466 (= N470), Q468 (≠ S472), Y469 (≠ L473), G470 (= G474), W471 (≠ Q475), I472 (= I476)
Sites not aligning to the query:
2ez4B Pyruvate oxidase variant f479w (see paper)
34% identity, 92% coverage: 9:546/584 of query aligns to 9:543/585 of 2ez4B
- active site: I24 (≠ M24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E51), S74 (≠ T74), F113 (≠ Q113), Q114 (= Q114), E115 (≠ D115), V162 (= V162), R256 (≠ L261), E283 (= E288), V386 (≠ S390), A412 (= A416), M414 (= M418), D439 (= D443), N466 (= N470), Q468 (≠ S472), Y469 (≠ L473), W471 (≠ Q475), I472 (= I476), E475 (= E479), G538 (≠ N541)
- binding flavin-adenine dinucleotide: H93 (= H93), G212 (= G217), I213 (≠ Q218), G214 (= G219), T236 (≠ A241), Y237 (≠ L242), P238 (≠ L243), A254 (≠ V259), N255 (≠ G260), R256 (≠ L261), V257 (≠ L262), G276 (= G281), N277 (≠ S282), N278 (≠ T283), P280 (= P285), F281 (≠ Y286), D298 (= D302), I299 (= I303), K303 (≠ R307), D317 (= D321), A318 (≠ C322), N409 (≠ G413)
- binding magnesium ion: D439 (= D443), N466 (= N470), Q468 (≠ S472)
- binding phosphate ion: W471 (≠ Q475), E475 (= E479)
- binding thiamine diphosphate: D388 (≠ T392), A412 (= A416), M414 (= M418), G438 (= G442), D439 (= D443), G440 (= G444), G441 (= G445), N466 (= N470), Q468 (≠ S472), Y469 (≠ L473), G470 (= G474), W471 (≠ Q475), I472 (= I476)
4feeA High-resolution structure of pyruvate oxidase in complex with reaction intermediate 2-hydroxyethyl-thiamin diphosphate carbanion-enamine, crystal b (see paper)
34% identity, 92% coverage: 9:546/584 of query aligns to 9:543/586 of 4feeA
- binding flavin-adenine dinucleotide: H93 (= H93), G212 (= G217), I213 (≠ Q218), G214 (= G219), T236 (≠ A241), Y237 (≠ L242), P238 (≠ L243), A254 (≠ V259), N255 (≠ G260), V257 (≠ L262), G276 (= G281), N277 (≠ S282), N278 (≠ T283), P280 (= P285), F281 (≠ Y286), D298 (= D302), I299 (= I303), K303 (≠ R307), D317 (= D321), A318 (≠ C322), N390 (≠ A394), N409 (≠ G413)
- binding magnesium ion: D439 (= D443), N466 (= N470), Q468 (≠ S472)
- binding pyruvic acid: N255 (≠ G260), R256 (≠ L261)
- 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 (≠ S390), D388 (≠ T392), A412 (= A416), M414 (= M418), G438 (= G442), G440 (= G444), N466 (= N470), Q468 (≠ S472), Y469 (≠ L473), G470 (= G474), F471 (≠ Q475), I472 (= I476)
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)
34% identity, 92% coverage: 9:546/584 of query aligns to 9:543/585 of 1powA
- active site: I24 (≠ M24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E51), S74 (≠ T74), F113 (≠ Q113), Q114 (= Q114), E115 (≠ D115), V162 (= V162), R256 (≠ L261), E283 (= E288), V386 (≠ S390), A412 (= A416), M414 (= M418), D439 (= D443), N466 (= N470), Q468 (≠ S472), Y469 (≠ L473), F471 (≠ Q475), I472 (= I476), E475 (= E479), G538 (≠ N541)
- binding flavin-adenine dinucleotide: H93 (= H93), G212 (= G217), I213 (≠ Q218), G214 (= G219), T236 (≠ A241), Y237 (≠ L242), A254 (≠ V259), V257 (≠ L262), G276 (= G281), N277 (≠ S282), N278 (≠ T283), Y279 (≠ F284), P280 (= P285), F281 (≠ Y286), D298 (= D302), I299 (= I303), K303 (≠ R307), D317 (= D321), A318 (≠ C322), N409 (≠ G413)
- binding magnesium ion: D439 (= D443), N466 (= N470), Q468 (≠ S472)
- binding thiamine diphosphate: D388 (≠ T392), M414 (= M418), G440 (= G444), N466 (= N470), Q468 (≠ S472), Y469 (≠ L473), G470 (= G474), F471 (≠ Q475), I472 (= I476)
1y9dD Pyruvate oxidase variant v265a from lactobacillus plantarum (see paper)
33% identity, 92% coverage: 9:546/584 of query aligns to 9:518/560 of 1y9dD
- active site: I24 (≠ M24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E51), S74 (≠ T74), E108 (≠ D115), V155 (= V162), R241 (≠ L261), V361 (≠ S390), A387 (= A416), M389 (= M418), D414 (= D443), N441 (= N470), Q443 (≠ S472), Y444 (≠ L473), F446 (≠ Q475), I447 (= I476), E450 (= E479), G513 (≠ N541)
- binding flavin-adenine dinucleotide: I198 (≠ Q218), G199 (= G219), T221 (≠ A241), P223 (≠ L243), G261 (= G281), N262 (≠ S282), N263 (≠ T283), D273 (= D302), I274 (= I303), K278 (≠ R307), D292 (= D321), A293 (≠ C322)
- binding magnesium ion: D414 (= D443), N441 (= N470), Q443 (≠ S472)
- binding thiamine diphosphate: E51 (= E51), S74 (≠ T74), P77 (= P77), H81 (= H81), D363 (≠ T392), M389 (= M418), G413 (= G442), G415 (= G444), N441 (= N470), Q443 (≠ S472), Y444 (≠ L473), G445 (= G474), F446 (≠ Q475), I447 (= I476)
2djiA Crystal structure of pyruvate oxidase from aerococcus viridans containing fad (see paper)
30% identity, 92% coverage: 9:546/584 of query aligns to 10:544/590 of 2djiA
- active site: I25 (≠ M24), S27 (≠ G26), G28 (≠ D27), T29 (≠ G28), L30 (≠ I29), E52 (= E51), S75 (≠ T74), F114 (≠ Q113), Q115 (= Q114), G163 (≠ V162), R257 (≠ L261), E284 (= E288), V387 (≠ S390), A413 (= A416), M415 (= M418), D440 (= D443), N467 (= N470), E469 (≠ S472), Y470 (≠ L473), F472 (≠ Q475), I473 (= I476), K476 (≠ Q480), Q539 (≠ N541)
- binding flavin-adenine dinucleotide: G213 (= G217), I214 (≠ Q218), G215 (= G219), T237 (≠ A241), G238 (≠ L242), K239 (≠ L243), T255 (≠ V259), Y256 (≠ G260), R257 (≠ L261), V258 (≠ L262), G277 (= G281), S278 (= S282), N279 (≠ T283), F280 (= F284), P281 (= P285), F282 (≠ Y286), D299 (= D302), I300 (= I303), M304 (≠ R307), D318 (= D321), A319 (≠ C322), P410 (≠ G413)
1v5gA Crystal structure of the reaction intermediate between pyruvate oxidase containing fad and tpp, and substrate pyruvate (see paper)
30% identity, 92% coverage: 9:546/584 of query aligns to 9:543/589 of 1v5gA
- binding flavin-adenine dinucleotide: G212 (= G217), I213 (≠ Q218), G214 (= G219), T236 (≠ A241), G237 (≠ L242), K238 (≠ L243), T254 (≠ V259), Y255 (≠ G260), R256 (≠ L261), V257 (≠ L262), G276 (= G281), S277 (= S282), N278 (≠ T283), F279 (= F284), F281 (≠ Y286), D298 (= D302), I299 (= I303), M303 (≠ R307), D317 (= D321), A318 (≠ C322), P409 (≠ G413)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ S390), N388 (≠ T392), M414 (= M418), G438 (= G442), G440 (= G444), A441 (≠ G445), N466 (= N470), E468 (≠ S472), Y469 (≠ L473), A470 (≠ G474), F471 (≠ Q475), I472 (= I476)
- binding magnesium ion: D439 (= D443), N466 (= N470), E468 (≠ S472)
1v5fA Crystal structure of pyruvate oxidase complexed with fad and tpp, from aerococcus viridans (see paper)
30% identity, 92% coverage: 9:546/584 of query aligns to 9:543/589 of 1v5fA
- binding flavin-adenine dinucleotide: G212 (= G217), I213 (≠ Q218), G214 (= G219), T236 (≠ A241), G237 (≠ L242), K238 (≠ L243), T254 (≠ V259), Y255 (≠ G260), R256 (≠ L261), V257 (≠ L262), G276 (= G281), S277 (= S282), N278 (≠ T283), F279 (= F284), P280 (= P285), F281 (≠ Y286), D298 (= D302), I299 (= I303), M303 (≠ R307), D317 (= D321), A318 (≠ C322), P409 (≠ G413)
- binding magnesium ion: D439 (= D443), N466 (= N470)
- binding thiamine diphosphate: N388 (≠ T392), S389 (≠ I393), M414 (= M418), G438 (= G442), G440 (= G444), N466 (= N470), Y469 (≠ L473), A470 (≠ G474), F471 (≠ Q475), I472 (= I476)
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)
31% identity, 93% coverage: 6:546/584 of query aligns to 97:646/667 of P09342
- C161 (= C71) modified: Disulfide link with 307
- P194 (≠ Y104) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ A220) modified: Disulfide link with 161
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)
31% identity, 93% coverage: 6:546/584 of query aligns to 94:643/664 of P09114
- P191 (≠ Y104) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
- W568 (= W478) mutation to L: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191.
7tzzA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase p197t mutant in complex with bispyribac-sodium (see paper)
29% identity, 93% coverage: 6:546/584 of query aligns to 15:564/582 of 7tzzA
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: M266 (≠ L261), R292 (vs. gap), W489 (= W478)
- 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 (≠ S390), G401 (= G391), Q402 (≠ T392), H403 (≠ I393), G426 (≠ A416), M428 (= M418), G452 (= G442), D453 (= D443), G454 (= G444), S455 (≠ G445), L483 (= L473), G484 (= G474), M485 (≠ Q475), V486 (≠ I476)
- binding flavin-adenine dinucleotide: R161 (= R153), G222 (= G217), G223 (≠ Q218), G224 (= G219), T246 (≠ A241), L247 (= L242), M248 (≠ L243), M263 (≠ Q258), L264 (≠ V259), M266 (≠ L261), H267 (≠ L262), G286 (= G281), R288 (≠ T283), V293 (vs. gap), D310 (= D302), I311 (= I303), D329 (= D321), V330 (≠ C322), M405 (≠ T395), G423 (= G413)
- binding magnesium ion: A37 (≠ G28), T82 (= T74), S83 (= S75), Q122 (= Q114), Y381 (≠ V371), D453 (= D443), M458 (= M448), Q461 (≠ A451), N480 (= N470), H482 (≠ S472), K533 (≠ P515)
Sites not aligning to the query:
5k3sA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a pyrimidinyl-benzoate herbicide, bispyribac-sodium (see paper)
29% identity, 93% coverage: 6:546/584 of query aligns to 15:564/583 of 5k3sA
- active site: Y33 (≠ M24), G35 (= G26), G36 (≠ D27), A37 (≠ G28), S38 (≠ I29), E59 (= E51), T82 (= T74), F121 (≠ Q113), Q122 (= Q114), E123 (≠ D115), K171 (≠ V162), M266 (≠ L261), V293 (vs. gap), V400 (≠ S390), G426 (≠ A416), M428 (= M418), D453 (= D443), N480 (= N470), H482 (≠ S472), L483 (= L473), M485 (≠ Q475), V486 (≠ I476), W489 (= W478), H558 (≠ T540)
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: R292 (vs. gap), M485 (≠ Q475), W489 (= W478)
- binding flavin-adenine dinucleotide: R161 (= R153), G222 (= G217), G223 (≠ Q218), G224 (= G219), T246 (≠ A241), L247 (= L242), M248 (≠ L243), L264 (≠ V259), M266 (≠ L261), G286 (= G281), R288 (≠ T283), D290 (≠ P285), V293 (vs. gap), D310 (= D302), I311 (= I303), D329 (= D321), V330 (≠ C322), M405 (≠ T395), G423 (= G413)
- binding magnesium ion: D453 (= D443), N480 (= N470), H482 (≠ S472)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (≠ S390), G401 (= G391), Q402 (≠ T392), H403 (≠ I393), G426 (≠ A416), M428 (= M418), D453 (= D443), G454 (= G444), S455 (≠ G445), N480 (= N470), H482 (≠ S472), L483 (= L473), G484 (= G474), M485 (≠ Q475), V486 (≠ I476)
Sites not aligning to the query:
5k2oA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a pyrimidinyl-benzoate herbicide, pyrithiobac (see paper)
29% identity, 93% coverage: 6:546/584 of query aligns to 15:564/585 of 5k2oA
- active site: Y33 (≠ M24), G35 (= G26), G36 (≠ D27), A37 (≠ G28), S38 (≠ I29), E59 (= E51), T82 (= T74), F121 (≠ Q113), Q122 (= Q114), E123 (≠ D115), K171 (≠ V162), M266 (≠ L261), V293 (vs. gap), V400 (≠ S390), G426 (≠ A416), M428 (= M418), D453 (= D443), N480 (= N470), H482 (≠ S472), L483 (= L473), M485 (≠ Q475), V486 (≠ I476), W489 (= W478), H558 (≠ T540)
- binding 2-chloranyl-6-(4,6-dimethoxypyrimidin-2-yl)sulfanyl-benzoic acid: M266 (≠ L261), R292 (vs. gap), W489 (= W478)
- binding flavin-adenine dinucleotide: R161 (= R153), G222 (= G217), G223 (≠ Q218), G224 (= G219), T246 (≠ A241), L247 (= L242), M248 (≠ L243), L264 (≠ V259), G286 (= G281), R288 (≠ T283), D290 (≠ P285), V293 (vs. gap), D310 (= D302), I311 (= I303), D329 (= D321), V330 (≠ C322), Q404 (≠ A394), M405 (≠ T395), G423 (= G413)
- binding magnesium ion: D453 (= D443), N480 (= N470), H482 (≠ S472)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (≠ S390), G401 (= G391), Q402 (≠ T392), H403 (≠ I393), M428 (= M418), D453 (= D443), G454 (= G444), S455 (≠ G445), N480 (= N470), H482 (≠ S472), L483 (= L473), G484 (= G474), M485 (≠ Q475), V486 (≠ I476)
Sites not aligning to the query:
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, 93% coverage: 6:546/584 of query aligns to 100:649/670 of P17597
- A122 (≠ G28) mutation to V: Reduced catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- M124 (≠ N30) 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 (= E51) binding
- S186 (≠ H93) binding
- P197 (≠ Y104) mutation to S: In csr1-1/GH50; resistant to sulfonylurea but not to imidazolinone herbicides.
- R199 (≠ D106) mutation R->A,E: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- Q207 (= Q114) binding
- K220 (≠ L127) binding
- R246 (= R153) binding ; binding
- K256 (≠ V162) binding
- G308 (≠ Q218) binding
- TL 331:332 (≠ AL 241:242) binding
- C340 (≠ D250) modified: Cysteine sulfinic acid (-SO2H)
- LGMH 349:352 (≠ VGLL 259:262) binding
- GVRFD 371:375 (≠ GSTFP 281:285) binding
- DR 376:377 (vs. gap) binding
- DI 395:396 (= DI 302:303) binding
- DV 414:415 (≠ DC 321:322) binding
- QH 487:488 (≠ TI 392:393) binding
- GG 508:509 (≠ GN 413:414) binding
- GAM 511:513 (≠ ATM 416:418) binding
- D538 (= D443) binding
- DGS 538:540 (≠ DGG 443:445) binding
- N565 (= N470) binding
- NQHLGM 565:570 (≠ NNSLGQ 470:475) binding
- H567 (≠ S472) binding
- W574 (= W478) 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.
8et4A Crystal structure of wild-type arabidopsis thaliana acetohydroxyacid synthase in complex with amidosulfuron (see paper)
29% identity, 93% coverage: 6:546/584 of query aligns to 15:564/582 of 8et4A
- 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 (≠ S390), G401 (= G391), Q402 (≠ T392), H403 (≠ I393), G426 (≠ A416), M428 (= M418), G452 (= G442), D453 (= D443), G454 (= G444), S455 (≠ G445), M458 (= M448), N480 (= N470), H482 (≠ S472), L483 (= L473), G484 (= G474), M485 (≠ Q475), V486 (≠ I476)
- binding flavin-adenine dinucleotide: R161 (= R153), G222 (= G217), G223 (≠ Q218), G224 (= G219), T246 (≠ A241), L247 (= L242), M248 (≠ L243), L264 (≠ V259), M266 (≠ L261), H267 (≠ L262), G286 (= G281), V287 (≠ S282), R288 (≠ T283), D290 (≠ P285), R292 (vs. gap), V293 (vs. gap), D310 (= D302), I311 (= I303), D329 (= D321), V330 (≠ C322), M405 (≠ T395), G423 (= G413)
- binding magnesium ion: F370 (≠ M367), D453 (= D443), M458 (= M448), Q461 (≠ A451), N480 (= N470), H482 (≠ S472), K533 (≠ P515)
- binding N-{[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl}-N-methylmethanesulfonamide: M266 (≠ L261), R292 (vs. gap), M485 (≠ Q475), W489 (= W478)
Sites not aligning to the query:
5wj1A Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a triazolopyrimidine herbicide, penoxsulam (see paper)
29% identity, 93% coverage: 6:546/584 of query aligns to 15:564/582 of 5wj1A
- active site: Y33 (≠ M24), G35 (= G26), G36 (≠ D27), A37 (≠ G28), S38 (≠ I29), E59 (= E51), T82 (= T74), F121 (≠ Q113), Q122 (= Q114), E123 (≠ D115), K171 (≠ V162), M266 (≠ L261), V293 (vs. gap), V400 (≠ S390), G426 (≠ A416), M428 (= M418), D453 (= D443), N480 (= N470), H482 (≠ S472), L483 (= L473), M485 (≠ Q475), V486 (≠ I476), W489 (= W478), H558 (≠ T540)
- binding flavin-adenine dinucleotide: R161 (= R153), G222 (= G217), G223 (≠ Q218), G224 (= G219), T246 (≠ A241), L247 (= L242), M248 (≠ L243), M263 (≠ Q258), L264 (≠ V259), G286 (= G281), R288 (≠ T283), V293 (vs. gap), D310 (= D302), I311 (= I303), D329 (= D321), V330 (≠ C322), M405 (≠ T395), G423 (= G413), G424 (≠ N414)
- binding magnesium ion: D453 (= D443), N480 (= N470), H482 (≠ S472)
- binding 2-(2,2-difluoroethoxy)-N-(5,8-dimethoxy[1,2,4]triazolo[1,5-c]pyrimidin-2-yl)-6-(trifluoromethyl)benzenesulfonamide: M266 (≠ L261), D291 (vs. gap), R292 (vs. gap), M485 (≠ Q475), W489 (= W478)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (≠ S390), G401 (= G391), Q402 (≠ T392), H403 (≠ I393), M428 (= M418), D453 (= D443), G454 (= G444), S455 (≠ G445), M458 (= M448), N480 (= N470), H482 (≠ S472), L483 (= L473), G484 (= G474), M485 (≠ Q475), V486 (≠ I476)
Sites not aligning to the query:
Query Sequence
>AZOBR_RS29985 FitnessBrowser__azobra:AZOBR_RS29985
MASTASDILVDVLVDWGVDTIFGMPGDGINGIVEALRRRQDEIRFIQVRHEEAAAFAACG
YAKFTGRLGVCIATSGPGGLHLLNGLYDAKLDHQPVLAITGLQYHDLVGTYTQQDVELDK
VFQDVALYNQRVMGAAHVRNIANLACRTALAHRGVSHITIPVDLQEQGIGADMRAPRNVK
GHNTALFAPQLPVPSEAQTRRAVEILDAGKRVVILAGQGALKATDQLERLADKLGAVIVK
ALLGKAAVPDDSPFTTGQVGLLGTAPSQEALETCDTLLIAGSTFPYIEYYPKPGQARAIQ
IDIDAARIGLRYPVEAGLVGDCGLALDILTERVRRHEDRSFLKTAQAGKAEWMKLMEERG
TRPDLPMKPQVVAWELGKRLSDTAIVACDSGTIATWWARQIPARRGQMHSLSGNLATMAP
GVPYAIAAQLAHPGRQVVAYVGDGGFSMLMADFATAVKYKLPIKVIISNNNSLGQIKWEQ
IAMLGNPEYVCDLQPIDFAKVAEACGGRGFTITDPKDCGATLDAALAHPGPVVVDCLVDT
NEPPMPPKVQAKQALHFTEALARGTPDALKIAATVFKGRAREVI
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