SitesBLAST
Comparing 14996 FitnessBrowser__Keio:14996 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)
100% identity, 100% coverage: 1:572/572 of query aligns to 1:572/572 of P07003
- 1:182 (vs. 1:182, 100% identical) Pyr domain
- E50 (= E50) binding
- 183:334 (vs. 183:334, 100% identical) FAD-binding domain
- S210 (= S210) binding
- LR 234:235 (= LR 234:235) binding
- TGLI 251:254 (= TGLI 251:254) binding
- TQFPY 274:278 (= TQFPY 274:278) binding
- D292 (= D292) binding
- S297 (= S297) binding
- DI 311:312 (= DI 311:312) binding
- 335:530 (vs. 335:530, 100% identical) PP-binding domain
- T382 (= T382) binding
- FN 403:404 (= FN 403:404) binding
- GSM 406:408 (= GSM 406:408) binding
- D433 (= D433) binding
- DGG 433:435 (= DGG 433:435) binding
- N460 (= N460) binding
- 460:466 (vs. 460:466, 100% identical) binding
- V462 (= V462) binding
- F465 (= F465) Moves into active site upon enzyme activation, plays a role in electron transfer
- 531:572 (vs. 531:572, 100% identical) Membrane-binding domain
- A533 (= A533) mutation to T: In poxB11; poor activity in vivo, no longer activated by lipids.
- YM 549:550 (= YM 549:550) In vitro cleavage to yield alpha-peptide
- 549:572 (vs. 549:572, 100% identical) mutation Missing: In poxB6. Inactive in vivo, does not complement inactive mutants. Active in vitro, no longer activated by nor binds to, detergents.
- A553 (= A553) mutation to V: In poxB14; poor activity in vivo, no longer activated by lipids.
- D560 (= D560) mutation to P: In poxB15; normal activity.
- E564 (= E564) mutation to P: In poxB16; loss of activity, weakly activated by cleavage.
- 564:572 (vs. 564:572, 100% identical) mutation Missing: In poxB7 Inactive in vivo, reduced activity in vitro.
- WLR 570:572 (= WLR 570:572) mutation Missing: In poxB8; reduced activity in vitro, not activated by lipids.
- R572 (= R572) mutation to 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)
100% identity, 100% coverage: 2:572/572 of query aligns to 1:571/571 of 3ey9A
- active site: V23 (= V24), G25 (= G26), D26 (= D27), S27 (= S28), L28 (= L29), E49 (= E50), S72 (= S73), F111 (= F112), Q112 (= Q113), G160 (= G161), L252 (= L253), A279 (= A280), V379 (= V380), G405 (= G406), M407 (= M408), D432 (= D433), N459 (= N460), V461 (= V462), L462 (= L463), F464 (= F465), V465 (= V466), E468 (= E469), K528 (= K529)
- binding flavin-adenine dinucleotide: G208 (= G209), S209 (= S210), G210 (= G211), A232 (= A233), L233 (= L234), R234 (= R235), T250 (= T251), G251 (= G252), I253 (= I254), G272 (= G273), T273 (= T274), Q274 (= Q275), F275 (= F276), Y277 (= Y278), D291 (= D292), I292 (= I293), S296 (= S297), G309 (= G310), D310 (= D311), I311 (= I312), T383 (= T384), F402 (= F403), N403 (= N404), Y548 (= Y549)
- binding magnesium ion: D432 (= D433), N459 (= N460)
- binding thiamine diphosphate: T24 (= T25), E49 (= E50), S72 (= S73), G76 (= G77), H79 (= H80), G380 (= G381), T381 (= T382), P382 (= P383), M407 (= M408), G431 (= G432), D432 (= D433), G433 (= G434), G434 (= G435), N459 (= N460), V461 (= V462), L462 (= L463), G463 (= G464)
1powA The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from lactobacillus plantarum (see paper)
31% identity, 94% coverage: 7:543/572 of query aligns to 7:552/585 of 1powA
- active site: I24 (≠ V24), G26 (= G26), G27 (≠ D27), S28 (= S28), I29 (≠ L29), E51 (= E50), S74 (= S73), F113 (= F112), Q114 (= Q113), E115 (= E114), V162 (≠ G161), R256 (≠ L253), E283 (vs. gap), V386 (= V380), A412 (≠ G406), M414 (= M408), D439 (= D433), N466 (= N460), Q468 (≠ V462), Y469 (≠ L463), F471 (= F465), I472 (≠ V466), E475 (= E469), G538 (≠ K529)
- binding flavin-adenine dinucleotide: H93 (= H92), G212 (= G209), I213 (≠ S210), G214 (= G211), T236 (≠ A233), Y237 (≠ L234), A254 (≠ T251), V257 (≠ I254), G276 (= G273), N277 (≠ T274), N278 (≠ Q275), Y279 (≠ F276), P280 (= P277), F281 (≠ Y278), D298 (= D292), I299 (= I293), K303 (≠ S297), D317 (= D311), A318 (≠ I312), N409 (≠ F403)
- binding magnesium ion: D439 (= D433), N466 (= N460), Q468 (≠ V462)
- binding thiamine diphosphate: D388 (≠ T382), M414 (= M408), G440 (= G434), N466 (= N460), Q468 (≠ V462), Y469 (≠ L463), G470 (= G464), F471 (= F465), I472 (≠ V466)
4feeA High-resolution structure of pyruvate oxidase in complex with reaction intermediate 2-hydroxyethyl-thiamin diphosphate carbanion-enamine, crystal b (see paper)
31% identity, 94% coverage: 7:543/572 of query aligns to 7:552/586 of 4feeA
- binding flavin-adenine dinucleotide: H93 (= H92), G212 (= G209), I213 (≠ S210), G214 (= G211), T236 (≠ A233), Y237 (≠ L234), P238 (≠ R235), A254 (≠ T251), N255 (≠ G252), V257 (≠ I254), G276 (= G273), N277 (≠ T274), N278 (≠ Q275), P280 (= P277), F281 (≠ Y278), D298 (= D292), I299 (= I293), K303 (≠ S297), D317 (= D311), A318 (≠ I312), N390 (≠ T384), N409 (≠ F403)
- binding magnesium ion: D439 (= D433), N466 (= N460), Q468 (≠ V462)
- binding pyruvic acid: N255 (≠ G252), R256 (≠ L253), L547 (≠ I538), L549 (= L540), D550 (≠ E541)
- 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 (= V380), D388 (≠ T382), A412 (≠ G406), M414 (= M408), G438 (= G432), G440 (= G434), N466 (= N460), Q468 (≠ V462), Y469 (≠ L463), G470 (= G464), F471 (= F465), I472 (≠ V466)
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)
31% identity, 90% coverage: 2:514/572 of query aligns to 2:520/589 of 1v5gA
- binding flavin-adenine dinucleotide: G212 (= G209), I213 (≠ S210), G214 (= G211), T236 (≠ A233), G237 (≠ L234), K238 (≠ R235), T254 (= T251), Y255 (≠ G252), R256 (≠ L253), V257 (≠ I254), G276 (= G273), S277 (≠ T274), N278 (≠ Q275), F279 (= F276), F281 (≠ Y278), D298 (= D292), I299 (= I293), M303 (≠ S297), D317 (= D311), A318 (≠ I312), P409 (≠ F403)
- binding 2-acetyl-thiamine diphosphate: V386 (= V380), N388 (≠ T382), M414 (= M408), G438 (= G432), G440 (= G434), A441 (≠ G435), N466 (= N460), E468 (≠ V462), Y469 (≠ L463), A470 (≠ G464), F471 (= F465), I472 (≠ V466)
- binding magnesium ion: D439 (= D433), N466 (= N460), E468 (≠ V462)
1v5fA Crystal structure of pyruvate oxidase complexed with fad and tpp, from aerococcus viridans (see paper)
31% identity, 90% coverage: 2:514/572 of query aligns to 2:520/589 of 1v5fA
- binding flavin-adenine dinucleotide: G212 (= G209), I213 (≠ S210), G214 (= G211), T236 (≠ A233), G237 (≠ L234), K238 (≠ R235), T254 (= T251), Y255 (≠ G252), R256 (≠ L253), V257 (≠ I254), G276 (= G273), S277 (≠ T274), N278 (≠ Q275), F279 (= F276), P280 (= P277), F281 (≠ Y278), D298 (= D292), I299 (= I293), M303 (≠ S297), D317 (= D311), A318 (≠ I312), P409 (≠ F403)
- binding magnesium ion: D439 (= D433), N466 (= N460)
- binding thiamine diphosphate: N388 (≠ T382), S389 (≠ P383), M414 (= M408), G438 (= G432), G440 (= G434), N466 (= N460), Y469 (≠ L463), A470 (≠ G464), F471 (= F465), I472 (≠ V466)
2djiA Crystal structure of pyruvate oxidase from aerococcus viridans containing fad (see paper)
31% identity, 90% coverage: 2:514/572 of query aligns to 3:521/590 of 2djiA
- active site: I25 (≠ V24), S27 (≠ G26), G28 (≠ D27), T29 (≠ S28), L30 (= L29), E52 (= E50), S75 (= S73), F114 (= F112), Q115 (= Q113), G163 (= G161), R257 (≠ L253), E284 (vs. gap), V387 (= V380), A413 (≠ G406), M415 (= M408), D440 (= D433), N467 (= N460), E469 (≠ V462), Y470 (≠ L463), F472 (= F465), I473 (≠ V466), K476 (≠ E469)
- binding flavin-adenine dinucleotide: G213 (= G209), I214 (≠ S210), G215 (= G211), T237 (≠ A233), G238 (≠ L234), K239 (≠ R235), T255 (= T251), Y256 (≠ G252), R257 (≠ L253), V258 (≠ I254), G277 (= G273), S278 (≠ T274), N279 (≠ Q275), F280 (= F276), P281 (= P277), F282 (≠ Y278), D299 (= D292), I300 (= I293), M304 (≠ S297), D318 (= D311), A319 (≠ I312), P410 (≠ F403)
Sites not aligning to the query:
2ezuA Pyruvate oxidase variant f479w in complex with reaction intermediate 2-acetyl-thiamin diphosphate (see paper)
30% identity, 94% coverage: 7:543/572 of query aligns to 7:552/585 of 2ezuA
- active site: I24 (≠ V24), G26 (= G26), G27 (≠ D27), S28 (= S28), I29 (≠ L29), E51 (= E50), S74 (= S73), F113 (= F112), Q114 (= Q113), E115 (= E114), V162 (≠ G161), R256 (≠ L253), E283 (vs. gap), V386 (= V380), A412 (≠ G406), M414 (= M408), D439 (= D433), N466 (= N460), Q468 (≠ V462), Y469 (≠ L463), W471 (≠ F465), I472 (≠ V466), E475 (= E469), G538 (≠ K529)
- binding flavin-adenine dinucleotide: H93 (= H92), G212 (= G209), I213 (≠ S210), G214 (= G211), T236 (≠ A233), Y237 (≠ L234), P238 (≠ R235), A254 (≠ T251), N255 (≠ G252), R256 (≠ L253), V257 (≠ I254), G276 (= G273), N277 (≠ T274), N278 (≠ Q275), P280 (= P277), F281 (≠ Y278), D298 (= D292), I299 (= I293), K303 (≠ S297), D317 (= D311), A318 (≠ I312), N409 (≠ F403)
- binding 2-acetyl-thiamine diphosphate: V386 (= V380), D388 (≠ T382), M414 (= M408), G438 (= G432), G440 (= G434), N466 (= N460), Q468 (≠ V462), Y469 (≠ L463), G470 (= G464), W471 (≠ F465), I472 (≠ V466)
- binding magnesium ion: D439 (= D433), N466 (= N460), Q468 (≠ V462)
- binding pyruvic acid: L547 (≠ I538), L549 (= L540), D550 (≠ E541)
Sites not aligning to the query:
2ez9A Pyruvate oxidase variant f479w in complex with reaction intermediate analogue 2-phosphonolactyl-thiamin diphosphate (see paper)
30% identity, 94% coverage: 7:543/572 of query aligns to 7:552/585 of 2ez9A
- active site: I24 (≠ V24), G26 (= G26), G27 (≠ D27), S28 (= S28), I29 (≠ L29), E51 (= E50), S74 (= S73), F113 (= F112), Q114 (= Q113), E115 (= E114), V162 (≠ G161), R256 (≠ L253), E283 (vs. gap), V386 (= V380), A412 (≠ G406), M414 (= M408), D439 (= D433), N466 (= N460), Q468 (≠ V462), Y469 (≠ L463), W471 (≠ F465), I472 (≠ V466), E475 (= E469), G538 (≠ K529)
- binding flavin-adenine dinucleotide: H93 (= H92), G212 (= G209), I213 (≠ S210), G214 (= G211), T236 (≠ A233), Y237 (≠ L234), P238 (≠ R235), A254 (≠ T251), N255 (≠ G252), R256 (≠ L253), V257 (≠ I254), G276 (= G273), N277 (≠ T274), N278 (≠ Q275), P280 (= P277), F281 (≠ Y278), D298 (= D292), I299 (= I293), K303 (≠ S297), D317 (= D311), A318 (≠ I312), N409 (≠ F403)
- binding magnesium ion: D439 (= D433), N466 (= N460), Q468 (≠ V462)
- 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 (= V380), D388 (≠ T382), M414 (= M408), G438 (= G432), G440 (= G434), N466 (= N460), Q468 (≠ V462), Y469 (≠ L463), G470 (= G464), W471 (≠ F465), I472 (≠ V466), E475 (= E469)
2ez8A Pyruvate oxidase variant f479w in complex with reaction intermediate 2-lactyl-thiamin diphosphate (see paper)
30% identity, 94% coverage: 7:543/572 of query aligns to 7:552/585 of 2ez8A
- active site: I24 (≠ V24), G26 (= G26), G27 (≠ D27), S28 (= S28), I29 (≠ L29), E51 (= E50), S74 (= S73), F113 (= F112), Q114 (= Q113), E115 (= E114), V162 (≠ G161), R256 (≠ L253), E283 (vs. gap), V386 (= V380), A412 (≠ G406), M414 (= M408), D439 (= D433), N466 (= N460), Q468 (≠ V462), Y469 (≠ L463), W471 (≠ F465), I472 (≠ V466), E475 (= E469), G538 (≠ K529)
- binding flavin-adenine dinucleotide: H93 (= H92), G212 (= G209), I213 (≠ S210), G214 (= G211), T236 (≠ A233), Y237 (≠ L234), P238 (≠ R235), A254 (≠ T251), N255 (≠ G252), R256 (≠ L253), V257 (≠ I254), G276 (= G273), N277 (≠ T274), N278 (≠ Q275), P280 (= P277), F281 (≠ Y278), D298 (= D292), I299 (= I293), K303 (≠ S297), D317 (= D311), A318 (≠ I312), N390 (≠ T384), N409 (≠ F403)
- binding magnesium ion: D439 (= D433), N466 (= N460), Q468 (≠ V462)
- binding pyruvic acid: L547 (≠ I538), L549 (= L540), D550 (≠ E541)
- 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 (≠ T382), M414 (= M408), G438 (= G432), G440 (= G434), N466 (= N460), Q468 (≠ V462), Y469 (≠ L463), G470 (= G464), W471 (≠ F465), I472 (≠ V466)
Sites not aligning to the query:
2ez4B Pyruvate oxidase variant f479w (see paper)
30% identity, 94% coverage: 7:543/572 of query aligns to 7:552/585 of 2ez4B
- active site: I24 (≠ V24), G26 (= G26), G27 (≠ D27), S28 (= S28), I29 (≠ L29), E51 (= E50), S74 (= S73), F113 (= F112), Q114 (= Q113), E115 (= E114), V162 (≠ G161), R256 (≠ L253), E283 (vs. gap), V386 (= V380), A412 (≠ G406), M414 (= M408), D439 (= D433), N466 (= N460), Q468 (≠ V462), Y469 (≠ L463), W471 (≠ F465), I472 (≠ V466), E475 (= E469), G538 (≠ K529)
- binding flavin-adenine dinucleotide: H93 (= H92), G212 (= G209), I213 (≠ S210), G214 (= G211), T236 (≠ A233), Y237 (≠ L234), P238 (≠ R235), A254 (≠ T251), N255 (≠ G252), R256 (≠ L253), V257 (≠ I254), G276 (= G273), N277 (≠ T274), N278 (≠ Q275), P280 (= P277), F281 (≠ Y278), D298 (= D292), I299 (= I293), K303 (≠ S297), D317 (= D311), A318 (≠ I312), N409 (≠ F403)
- binding magnesium ion: D439 (= D433), N466 (= N460), Q468 (≠ V462)
- binding phosphate ion: W471 (≠ F465), E475 (= E469)
- binding thiamine diphosphate: D388 (≠ T382), A412 (≠ G406), M414 (= M408), G438 (= G432), D439 (= D433), G440 (= G434), G441 (= G435), N466 (= N460), Q468 (≠ V462), Y469 (≠ L463), G470 (= G464), W471 (≠ F465), I472 (≠ V466)
1y9dD Pyruvate oxidase variant v265a from lactobacillus plantarum (see paper)
31% identity, 94% coverage: 7:543/572 of query aligns to 7:527/560 of 1y9dD
- active site: I24 (≠ V24), G26 (= G26), G27 (≠ D27), S28 (= S28), I29 (≠ L29), E51 (= E50), S74 (= S73), E108 (= E114), V155 (≠ G161), R241 (≠ L253), V361 (= V380), A387 (≠ G406), M389 (= M408), D414 (= D433), N441 (= N460), Q443 (≠ V462), Y444 (≠ L463), F446 (= F465), I447 (≠ V466), E450 (= E469), G513 (≠ K529)
- binding flavin-adenine dinucleotide: I198 (≠ S210), G199 (= G211), T221 (≠ A233), P223 (≠ R235), G261 (= G273), N262 (≠ T274), N263 (≠ Q275), D273 (= D292), I274 (= I293), K278 (≠ S297), D292 (= D311), A293 (≠ I312)
- binding magnesium ion: D414 (= D433), N441 (= N460), Q443 (≠ V462)
- binding thiamine diphosphate: E51 (= E50), S74 (= S73), P77 (= P76), H81 (= H80), D363 (≠ T382), M389 (= M408), G413 (= G432), G415 (= G434), N441 (= N460), Q443 (≠ V462), Y444 (≠ L463), G445 (= G464), F446 (= F465), I447 (≠ V466)
8et4A Crystal structure of wild-type arabidopsis thaliana acetohydroxyacid synthase in complex with amidosulfuron (see paper)
29% identity, 93% coverage: 6:535/572 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 (= V380), G401 (= G381), Q402 (≠ T382), H403 (≠ P383), G426 (= G406), M428 (= M408), G452 (= G432), D453 (= D433), G454 (= G434), S455 (≠ G435), M458 (= M438), N480 (= N460), H482 (≠ V462), L483 (= L463), G484 (= G464), M485 (≠ F465), V486 (= V466)
- binding flavin-adenine dinucleotide: R161 (= R152), G222 (= G209), G223 (≠ S210), G224 (= G211), T246 (≠ A233), L247 (= L234), M248 (≠ R235), L264 (≠ T251), M266 (≠ L253), H267 (≠ I254), G286 (= G273), V287 (≠ T274), R288 (≠ Q275), D290 (≠ P277), R292 (= R279), V293 (≠ A280), D310 (= D292), I311 (= I293), D329 (= D311), V330 (≠ I312), M405 (≠ V385), G423 (≠ F403)
- binding magnesium ion: F370 (vs. gap), D453 (= D433), M458 (= M438), Q461 (≠ G441), N480 (= N460), H482 (≠ V462), K533 (≠ A504)
- binding N-{[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl}-N-methylmethanesulfonamide: M266 (≠ L253), R292 (= R279), M485 (≠ F465), W489 (vs. gap)
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: 6:535/572 of query aligns to 15:564/582 of 5wj1A
- active site: Y33 (≠ V24), G35 (= G26), G36 (≠ D27), A37 (≠ S28), S38 (≠ L29), E59 (= E50), T82 (≠ S73), F121 (= F112), Q122 (= Q113), E123 (= E114), K171 (≠ G161), M266 (≠ L253), V293 (≠ A280), V400 (= V380), G426 (= G406), M428 (= M408), D453 (= D433), N480 (= N460), H482 (≠ V462), L483 (= L463), M485 (≠ F465), V486 (= V466), W489 (vs. gap), H558 (≠ K529)
- binding flavin-adenine dinucleotide: R161 (= R152), G222 (= G209), G223 (≠ S210), G224 (= G211), T246 (≠ A233), L247 (= L234), M248 (≠ R235), M263 (= M250), L264 (≠ T251), G286 (= G273), R288 (≠ Q275), V293 (≠ A280), D310 (= D292), I311 (= I293), D329 (= D311), V330 (≠ I312), M405 (≠ V385), G423 (≠ F403), G424 (≠ N404)
- binding magnesium ion: D453 (= D433), N480 (= N460), H482 (≠ V462)
- binding 2-(2,2-difluoroethoxy)-N-(5,8-dimethoxy[1,2,4]triazolo[1,5-c]pyrimidin-2-yl)-6-(trifluoromethyl)benzenesulfonamide: M266 (≠ L253), D291 (≠ Y278), R292 (= R279), M485 (≠ F465), W489 (vs. gap)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (= V380), G401 (= G381), Q402 (≠ T382), H403 (≠ P383), M428 (= M408), D453 (= D433), G454 (= G434), S455 (≠ G435), M458 (= M438), N480 (= N460), H482 (≠ V462), L483 (= L463), G484 (= G464), M485 (≠ F465), V486 (= V466)
Sites not aligning to the query:
5k6tA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a sulfonylamino-carbonyl-triazolinone herbicide, propoxycarbazone-sodium (see paper)
29% identity, 93% coverage: 6:535/572 of query aligns to 15:564/582 of 5k6tA
- active site: Y33 (≠ V24), G35 (= G26), G36 (≠ D27), A37 (≠ S28), S38 (≠ L29), E59 (= E50), T82 (≠ S73), F121 (= F112), Q122 (= Q113), E123 (= E114), K171 (≠ G161), M266 (≠ L253), V293 (≠ A280), V400 (= V380), G426 (= G406), M428 (= M408), D453 (= D433), N480 (= N460), H482 (≠ V462), L483 (= L463), M485 (≠ F465), V486 (= V466), W489 (vs. gap), H558 (≠ K529)
- binding methyl 2-[(4-methyl-5-oxidanylidene-3-propoxy-1,2,4-triazol-1-yl)carbonylsulfamoyl]benzoate: H267 (≠ I254), R292 (= R279), M485 (≠ F465), W489 (vs. gap)
- binding flavin-adenine dinucleotide: R161 (= R152), G222 (= G209), G223 (≠ S210), G224 (= G211), T246 (≠ A233), L247 (= L234), M248 (≠ R235), L264 (≠ T251), G286 (= G273), R288 (≠ Q275), D290 (≠ P277), R292 (= R279), V293 (≠ A280), D310 (= D292), I311 (= I293), D329 (= D311), V330 (≠ I312), Q404 (≠ T384), M405 (≠ V385), G423 (≠ F403)
- binding magnesium ion: D453 (= D433), N480 (= N460), H482 (≠ V462)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: V400 (= V380), G401 (= G381), Q402 (≠ T382), H403 (≠ P383), G426 (= G406), M428 (= M408), G452 (= G432), G454 (= G434), S455 (≠ G435), N480 (= N460), H482 (≠ V462), L483 (= L463), G484 (= G464)
Sites not aligning to the query:
5k6rA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a sulfonylamino-carbonyl-triazolinone herbicide, thiencarbazone-methyl (see paper)
29% identity, 93% coverage: 6:535/572 of query aligns to 15:564/582 of 5k6rA
- active site: Y33 (≠ V24), G35 (= G26), G36 (≠ D27), A37 (≠ S28), S38 (≠ L29), E59 (= E50), T82 (≠ S73), F121 (= F112), Q122 (= Q113), E123 (= E114), K171 (≠ G161), M266 (≠ L253), V293 (≠ A280), V400 (= V380), G426 (= G406), M428 (= M408), D453 (= D433), N480 (= N460), H482 (≠ V462), L483 (= L463), M485 (≠ F465), V486 (= V466), W489 (vs. gap), H558 (≠ K529)
- binding methyl 4-[(3-methoxy-4-methyl-5-oxidanylidene-1,2,4-triazol-1-yl)carbonylsulfamoyl]-5-methyl-thiophene-3-carboxylate: R292 (= R279), W489 (vs. gap)
- binding flavin-adenine dinucleotide: R161 (= R152), G222 (= G209), G223 (≠ S210), G224 (= G211), T246 (≠ A233), L247 (= L234), M248 (≠ R235), L264 (≠ T251), M266 (≠ L253), G286 (= G273), R288 (≠ Q275), R292 (= R279), V293 (≠ A280), D310 (= D292), I311 (= I293), G328 (= G310), D329 (= D311), V330 (≠ I312), M405 (≠ V385), G423 (≠ F403)
- binding magnesium ion: D453 (= D433), N480 (= N460), H482 (≠ V462)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: V400 (= V380), G401 (= G381), Q402 (≠ T382), H403 (≠ P383), G426 (= G406), M428 (= M408), D453 (= D433), G454 (= G434), S455 (≠ G435), M458 (= M438), N480 (= N460), H482 (≠ V462), L483 (= L463), G484 (= G464), M485 (≠ F465), V486 (= V466)
Sites not aligning to the query:
1z8nA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with an imidazolinone herbicide, imazaquin (see paper)
29% identity, 93% coverage: 6:535/572 of query aligns to 15:564/582 of 1z8nA
- active site: Y33 (≠ V24), G35 (= G26), G36 (≠ D27), A37 (≠ S28), S38 (≠ L29), E59 (= E50), T82 (≠ S73), F121 (= F112), Q122 (= Q113), E123 (= E114), K171 (≠ G161), M266 (≠ L253), V293 (≠ A280), V400 (= V380), G426 (= G406), M428 (= M408), D453 (= D433), N480 (= N460), H482 (≠ V462), L483 (= L463), M485 (≠ F465), V486 (= V466), W489 (vs. gap), H558 (≠ K529)
- binding 2-(4-isopropyl-4-methyl-5-oxo-4,5-dihydro-1h-imidazol-2-yl)quinoline-3-carboxylic acid: K135 (≠ H126), R161 (= R152), Y191 (vs. gap), R194 (vs. gap), D291 (≠ Y278), R292 (= R279), D312 (≠ N294), W489 (vs. gap)
- binding flavin-adenine dinucleotide: R161 (= R152), G222 (= G209), G224 (= G211), T246 (≠ A233), L247 (= L234), M248 (≠ R235), L264 (≠ T251), G265 (= G252), M266 (≠ L253), H267 (≠ I254), G286 (= G273), V287 (≠ T274), R288 (≠ Q275), D290 (≠ P277), R292 (= R279), V293 (≠ A280), D310 (= D292), I311 (= I293), D329 (= D311), V330 (≠ I312), M405 (≠ V385), G423 (≠ F403), G424 (≠ N404)
- binding magnesium ion: D453 (= D433), N480 (= N460)
- binding thiamine diphosphate: V400 (= V380), G401 (= G381), Q402 (≠ T382), H403 (≠ P383), G426 (= G406), M428 (= M408), G452 (= G432), G454 (= G434), S455 (≠ G435), N480 (= N460), H482 (≠ V462), L483 (= L463), G484 (= G464), M485 (≠ F465), V486 (= V466)
Sites not aligning to the query:
1yi1A Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a sulfonylurea herbicide, tribenuron methyl (see paper)
29% identity, 93% coverage: 6:535/572 of query aligns to 15:564/582 of 1yi1A
- active site: Y33 (≠ V24), G35 (= G26), G36 (≠ D27), A37 (≠ S28), S38 (≠ L29), E59 (= E50), T82 (≠ S73), F121 (= F112), Q122 (= Q113), E123 (= E114), K171 (≠ G161), M266 (≠ L253), V293 (≠ A280), V400 (= V380), G426 (= G406), M428 (= M408), D453 (= D433), N480 (= N460), H482 (≠ V462), L483 (= L463), M485 (≠ F465), V486 (= V466), W489 (vs. gap), H558 (≠ K529)
- binding methyl 2-[4-methoxy-6-methyl-1,3,5-trazin-2-yl(methyl)carbamoylsulfamoyl]benzoate: D291 (≠ Y278), R292 (= R279), W489 (vs. gap)
- binding flavin-adenine dinucleotide: R161 (= R152), G223 (≠ S210), G224 (= G211), T246 (≠ A233), L247 (= L234), M248 (≠ R235), M263 (= M250), L264 (≠ T251), G265 (= G252), M266 (≠ L253), H267 (≠ I254), G286 (= G273), V287 (≠ T274), R288 (≠ Q275), D290 (≠ P277), V293 (≠ A280), D310 (= D292), I311 (= I293), D329 (= D311), V330 (≠ I312), M405 (≠ V385), G423 (≠ F403), G424 (≠ N404)
- binding magnesium ion: D453 (= D433), N480 (= N460), H482 (≠ V462)
Sites not aligning to the query:
1yi0A Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a sulfonylurea herbicide, sulfometuron methyl (see paper)
29% identity, 93% coverage: 6:535/572 of query aligns to 15:564/582 of 1yi0A
- active site: Y33 (≠ V24), G35 (= G26), G36 (≠ D27), A37 (≠ S28), S38 (≠ L29), E59 (= E50), T82 (≠ S73), F121 (= F112), Q122 (= Q113), E123 (= E114), K171 (≠ G161), M266 (≠ L253), V293 (≠ A280), V400 (= V380), G426 (= G406), M428 (= M408), D453 (= D433), N480 (= N460), H482 (≠ V462), L483 (= L463), M485 (≠ F465), V486 (= V466), W489 (vs. gap), H558 (≠ K529)
- binding methyl 2-[({[(4,6-dimethylpyrimidin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: D291 (≠ Y278), R292 (= R279), W489 (vs. gap)
- binding flavin-adenine dinucleotide: R161 (= R152), G222 (= G209), G223 (≠ S210), G224 (= G211), T246 (≠ A233), L247 (= L234), M248 (≠ R235), L264 (≠ T251), G265 (= G252), M266 (≠ L253), H267 (≠ I254), G286 (= G273), V287 (≠ T274), R288 (≠ Q275), D290 (≠ P277), R292 (= R279), V293 (≠ A280), D310 (= D292), I311 (= I293), G328 (= G310), D329 (= D311), V330 (≠ I312), M405 (≠ V385), G423 (≠ F403), G424 (≠ N404)
- binding magnesium ion: D453 (= D433), N480 (= N460), H482 (≠ V462)
Sites not aligning to the query:
1yhzA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron (see paper)
29% identity, 93% coverage: 6:535/572 of query aligns to 15:564/582 of 1yhzA
- active site: Y33 (≠ V24), G35 (= G26), G36 (≠ D27), A37 (≠ S28), S38 (≠ L29), E59 (= E50), T82 (≠ S73), F121 (= F112), Q122 (= Q113), E123 (= E114), K171 (≠ G161), M266 (≠ L253), V293 (≠ A280), V400 (= V380), G426 (= G406), M428 (= M408), D453 (= D433), N480 (= N460), H482 (≠ V462), L483 (= L463), M485 (≠ F465), V486 (= V466), W489 (vs. gap), H558 (≠ K529)
- binding 1-(2-chlorophenylsulfonyl)-3-(4-methoxy-6-methyl-l,3,5-triazin-2-yl)urea: D291 (≠ Y278), R292 (= R279), M485 (≠ F465), W489 (vs. gap)
- binding flavin-adenine dinucleotide: R161 (= R152), G223 (≠ S210), G224 (= G211), T246 (≠ A233), L247 (= L234), M248 (≠ R235), L264 (≠ T251), M266 (≠ L253), H267 (≠ I254), G286 (= G273), V287 (≠ T274), R288 (≠ Q275), D290 (≠ P277), V293 (≠ A280), D310 (= D292), I311 (= I293), D329 (= D311), V330 (≠ I312), Q404 (≠ T384), M405 (≠ V385), G423 (≠ F403), G424 (≠ N404)
- binding magnesium ion: D453 (= D433), N480 (= N460), H482 (≠ V462)
Sites not aligning to the query:
Query Sequence
>14996 FitnessBrowser__Keio:14996
MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHEEVAAFAAGAE
AQLSGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAAHIPSSEIGSGYFQETHPQEL
FRECSHYCELVSSPEQIPQVLAIAMRKAVLNRGVSVVVLPGDVALKPAPEGATMHWYHAP
QPVVTPEEEELRKLAQLLRYSSNIALMCGSGCAGAHKELVEFAGKIKAPIVHALRGKEHV
EYDNPYDVGMTGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPASIGA
HSKVDMALVGDIKSTLRALLPLVEEKADRKFLDKALEDYRDARKGLDDLAKPSEKAIHPQ
YLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLLGSFNHGSMANAMPQALGAQA
TEPERQVVAMCGDGGFSMLMGDFLSVVQMKLPVKIVVFNNSVLGFVAMEMKAGGYLTDGT
ELHDTNFARIAEACGITGIRVEKASEVDEALQRAFSIDGPVLVDVVVAKEELAIPPQIKL
EQAKGFSLYMLRAIISGRGDEVIELAKTNWLR
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