SitesBLAST
Comparing H281DRAFT_03240 FitnessBrowser__Burk376:H281DRAFT_03240 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, 98% coverage: 1:598/611 of query aligns to 1:567/572 of P07003
- 1:182 (vs. 1:203, 36% identical) Pyr domain
- E50 (= E64) binding
- 183:334 (vs. 204:355, 35% identical) FAD-binding domain
- S210 (≠ A230) binding
- LR 234:235 (≠ LL 254:255) binding
- TGLI 251:254 (≠ IGLL 271:274) binding
- TQFPY 274:278 (≠ SGFPY 294:298) binding
- D292 (= D314) binding
- S297 (≠ M319) binding
- DI 311:312 (≠ DS 333:334) binding
- 335:530 (vs. 356:562, 30% identical) PP-binding domain
- T382 (≠ S405) binding
- FN 403:404 (≠ LS 424:425) binding
- G--SM 406:408 (≠ GLASM 427:431) binding
- D433 (= D456) binding
- DGG 433:435 (≠ DGA 456:458) binding
- N460 (= N489) binding
- 460:466 (vs. 489:495, 43% identical) binding
- V462 (≠ D491) binding
- F465 (≠ Q494) Moves into active site upon enzyme activation, plays a role in electron transfer
- A533 (≠ P565) mutation to T: In poxB11; poor activity in vivo, no longer activated by lipids.
- YM 549:550 (≠ TL 581:582) In vitro cleavage to yield alpha-peptide
- A553 (≠ G585) mutation to V: In poxB14; poor activity in vivo, no longer activated by lipids.
- D560 (≠ N591) mutation to P: In poxB15; normal activity.
- E564 (≠ Q595) mutation to P: In poxB16; loss of activity, weakly activated by cleavage.
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.
- 564:572 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, 97% coverage: 4:598/611 of query aligns to 3:566/571 of 3ey9A
- active site: V23 (≠ Y24), G25 (= G26), D26 (= D27), S27 (≠ G28), L28 (≠ I29), E49 (= E64), S72 (≠ T87), F111 (≠ Q126), Q112 (= Q127), G160 (≠ N176), L252 (= L273), A279 (≠ E300), V379 (≠ S403), G405 (= G427), M407 (= M431), D432 (= D456), N459 (= N489), V461 (≠ D491), L462 (= L492), F464 (≠ Q494), V465 (= V495), E468 (= E498), K528 (≠ P561)
- binding flavin-adenine dinucleotide: G208 (= G229), S209 (≠ A230), G210 (= G231), A232 (= A253), L233 (= L254), R234 (≠ L255), T250 (≠ I271), G251 (= G272), I253 (≠ L274), G272 (= G293), T273 (≠ S294), Q274 (≠ G295), F275 (= F296), Y277 (= Y298), D291 (= D314), I292 (≠ L315), S296 (≠ M319), G309 (= G332), D310 (= D333), I311 (≠ S334), T383 (≠ A407), F402 (≠ L424), N403 (≠ S425), Y548 (≠ T581)
- binding magnesium ion: D432 (= D456), N459 (= N489)
- binding thiamine diphosphate: T24 (≠ P25), E49 (= E64), S72 (≠ T87), G76 (= G91), H79 (= H94), G380 (= G404), T381 (≠ S405), P382 (≠ C406), M407 (= M431), G431 (= G455), D432 (= D456), G433 (= G457), G434 (≠ A458), N459 (= N489), V461 (≠ D491), L462 (= L492), G463 (≠ N493)
2djiA Crystal structure of pyruvate oxidase from aerococcus viridans containing fad (see paper)
28% identity, 95% coverage: 3:584/611 of query aligns to 4:561/590 of 2djiA
- active site: I25 (≠ Y24), S27 (≠ G26), G28 (≠ D27), T29 (≠ G28), L30 (≠ I29), E52 (= E64), S75 (≠ T87), F114 (≠ Q126), Q115 (= Q127), G163 (≠ N176), R257 (≠ L273), E284 (= E300), V387 (≠ S403), A413 (= A429), M415 (= M431), D440 (= D456), N467 (= N489), E469 (≠ Q494), Y470 (≠ V495), F472 (≠ W497), I473 (≠ E498), K476 (≠ V501), Q539 (≠ P561)
- binding flavin-adenine dinucleotide: G213 (= G229), I214 (≠ A230), G215 (= G231), T237 (≠ A253), G238 (≠ L254), K239 (≠ L255), T255 (≠ I271), Y256 (≠ G272), R257 (≠ L273), V258 (≠ L274), G277 (= G293), S278 (= S294), N279 (≠ G295), F280 (= F296), P281 (= P297), F282 (≠ Y298), D299 (= D314), I300 (≠ L315), M304 (= M319), D318 (= D333), A319 (≠ S334), P410 (≠ G426)
1v5gA Crystal structure of the reaction intermediate between pyruvate oxidase containing fad and tpp, and substrate pyruvate (see paper)
28% identity, 95% coverage: 3:584/611 of query aligns to 3:560/589 of 1v5gA
- binding flavin-adenine dinucleotide: G212 (= G229), I213 (≠ A230), G214 (= G231), T236 (≠ A253), G237 (≠ L254), K238 (≠ L255), T254 (≠ I271), Y255 (≠ G272), R256 (≠ L273), V257 (≠ L274), G276 (= G293), S277 (= S294), N278 (≠ G295), F279 (= F296), F281 (≠ Y298), D298 (= D314), I299 (≠ L315), M303 (= M319), D317 (= D333), A318 (≠ S334), P409 (≠ G426)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ S403), N388 (≠ S405), M414 (= M431), G438 (= G455), G440 (= G457), A441 (= A458), N466 (= N489), E468 (≠ Q494), Y469 (≠ V495), A470 (≠ T496), F471 (≠ W497), I472 (≠ E498)
- binding magnesium ion: D439 (= D456), N466 (= N489), E468 (≠ Q494)
1v5fA Crystal structure of pyruvate oxidase complexed with fad and tpp, from aerococcus viridans (see paper)
28% identity, 95% coverage: 3:584/611 of query aligns to 3:560/589 of 1v5fA
- binding flavin-adenine dinucleotide: G212 (= G229), I213 (≠ A230), G214 (= G231), T236 (≠ A253), G237 (≠ L254), K238 (≠ L255), T254 (≠ I271), Y255 (≠ G272), R256 (≠ L273), V257 (≠ L274), G276 (= G293), S277 (= S294), N278 (≠ G295), F279 (= F296), P280 (= P297), F281 (≠ Y298), D298 (= D314), I299 (≠ L315), M303 (= M319), D317 (= D333), A318 (≠ S334), P409 (≠ G426)
- binding magnesium ion: D439 (= D456), N466 (= N489)
- binding thiamine diphosphate: N388 (≠ S405), S389 (≠ C406), M414 (= M431), G438 (= G455), G440 (= G457), N466 (= N489), Y469 (≠ V495), A470 (≠ T496), F471 (≠ W497), I472 (≠ E498)
1powA The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from lactobacillus plantarum (see paper)
30% identity, 91% coverage: 2:556/611 of query aligns to 2:533/585 of 1powA
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E64), S74 (≠ T87), F113 (≠ Q126), Q114 (= Q127), E115 (= E128), V162 (≠ N176), R256 (≠ L273), E283 (= E300), V386 (≠ S403), A412 (= A429), M414 (= M431), D439 (= D456), N466 (= N489), Q468 (≠ D491), Y469 (≠ L492), F471 (≠ Q494), I472 (≠ V495), E475 (= E498)
- binding flavin-adenine dinucleotide: H93 (= H106), G212 (= G229), I213 (≠ A230), G214 (= G231), T236 (≠ A253), Y237 (≠ L254), A254 (≠ I271), V257 (≠ L274), G276 (= G293), N277 (≠ S294), N278 (≠ G295), Y279 (≠ F296), P280 (= P297), F281 (≠ Y298), D298 (= D314), I299 (≠ L315), K303 (≠ M319), D317 (= D333), A318 (≠ S334), N409 (≠ G426)
- binding magnesium ion: D439 (= D456), N466 (= N489), Q468 (≠ D491)
- binding thiamine diphosphate: D388 (≠ S405), M414 (= M431), G440 (= G457), N466 (= N489), Q468 (≠ D491), Y469 (≠ L492), G470 (≠ N493), F471 (≠ Q494), I472 (≠ V495)
Sites not aligning to the query:
4feeA High-resolution structure of pyruvate oxidase in complex with reaction intermediate 2-hydroxyethyl-thiamin diphosphate carbanion-enamine, crystal b (see paper)
30% identity, 91% coverage: 2:556/611 of query aligns to 2:533/586 of 4feeA
- binding flavin-adenine dinucleotide: H93 (= H106), G212 (= G229), I213 (≠ A230), G214 (= G231), T236 (≠ A253), Y237 (≠ L254), P238 (≠ L255), A254 (≠ I271), N255 (≠ G272), V257 (≠ L274), G276 (= G293), N277 (≠ S294), N278 (≠ G295), P280 (= P297), F281 (≠ Y298), D298 (= D314), I299 (≠ L315), K303 (≠ M319), D317 (= D333), A318 (≠ S334), N390 (≠ A407), N409 (≠ G426)
- binding magnesium ion: D439 (= D456), N466 (= N489), Q468 (≠ D491)
- binding pyruvic acid: N255 (≠ G272), R256 (≠ L273)
- 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 (≠ S403), D388 (≠ S405), A412 (= A429), M414 (= M431), G438 (= G455), G440 (= G457), N466 (= N489), Q468 (≠ D491), Y469 (≠ L492), G470 (≠ N493), F471 (≠ Q494), I472 (≠ V495)
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: 2:556/611 of query aligns to 2:533/585 of 2ezuA
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E64), S74 (≠ T87), F113 (≠ Q126), Q114 (= Q127), E115 (= E128), V162 (≠ N176), R256 (≠ L273), E283 (= E300), V386 (≠ S403), A412 (= A429), M414 (= M431), D439 (= D456), N466 (= N489), Q468 (≠ D491), Y469 (≠ L492), W471 (≠ Q494), I472 (≠ V495), E475 (= E498)
- binding flavin-adenine dinucleotide: H93 (= H106), G212 (= G229), I213 (≠ A230), G214 (= G231), T236 (≠ A253), Y237 (≠ L254), P238 (≠ L255), A254 (≠ I271), N255 (≠ G272), R256 (≠ L273), V257 (≠ L274), G276 (= G293), N277 (≠ S294), N278 (≠ G295), P280 (= P297), F281 (≠ Y298), D298 (= D314), I299 (≠ L315), K303 (≠ M319), D317 (= D333), A318 (≠ S334), N409 (≠ G426)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ S403), D388 (≠ S405), M414 (= M431), G438 (= G455), G440 (= G457), N466 (= N489), Q468 (≠ D491), Y469 (≠ L492), G470 (≠ N493), W471 (≠ Q494), I472 (≠ V495)
- binding magnesium ion: D439 (= D456), N466 (= N489), Q468 (≠ D491)
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, 91% coverage: 2:556/611 of query aligns to 2:533/585 of 2ez9A
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E64), S74 (≠ T87), F113 (≠ Q126), Q114 (= Q127), E115 (= E128), V162 (≠ N176), R256 (≠ L273), E283 (= E300), V386 (≠ S403), A412 (= A429), M414 (= M431), D439 (= D456), N466 (= N489), Q468 (≠ D491), Y469 (≠ L492), W471 (≠ Q494), I472 (≠ V495), E475 (= E498)
- binding flavin-adenine dinucleotide: H93 (= H106), G212 (= G229), I213 (≠ A230), G214 (= G231), T236 (≠ A253), Y237 (≠ L254), P238 (≠ L255), A254 (≠ I271), N255 (≠ G272), R256 (≠ L273), V257 (≠ L274), G276 (= G293), N277 (≠ S294), N278 (≠ G295), P280 (= P297), F281 (≠ Y298), D298 (= D314), I299 (≠ L315), K303 (≠ M319), D317 (= D333), A318 (≠ S334), N409 (≠ G426)
- binding magnesium ion: D439 (= D456), N466 (= N489), Q468 (≠ D491)
- 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 (≠ S403), D388 (≠ S405), M414 (= M431), G438 (= G455), G440 (= G457), N466 (= N489), Q468 (≠ D491), Y469 (≠ L492), G470 (≠ N493), W471 (≠ Q494), I472 (≠ V495), E475 (= E498)
Sites not aligning to the query:
2ez8A Pyruvate oxidase variant f479w in complex with reaction intermediate 2-lactyl-thiamin diphosphate (see paper)
30% identity, 91% coverage: 2:556/611 of query aligns to 2:533/585 of 2ez8A
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E64), S74 (≠ T87), F113 (≠ Q126), Q114 (= Q127), E115 (= E128), V162 (≠ N176), R256 (≠ L273), E283 (= E300), V386 (≠ S403), A412 (= A429), M414 (= M431), D439 (= D456), N466 (= N489), Q468 (≠ D491), Y469 (≠ L492), W471 (≠ Q494), I472 (≠ V495), E475 (= E498)
- binding flavin-adenine dinucleotide: H93 (= H106), G212 (= G229), I213 (≠ A230), G214 (= G231), T236 (≠ A253), Y237 (≠ L254), P238 (≠ L255), A254 (≠ I271), N255 (≠ G272), R256 (≠ L273), V257 (≠ L274), G276 (= G293), N277 (≠ S294), N278 (≠ G295), P280 (= P297), F281 (≠ Y298), D298 (= D314), I299 (≠ L315), K303 (≠ M319), D317 (= D333), A318 (≠ S334), N390 (≠ A407), N409 (≠ G426)
- binding magnesium ion: D439 (= D456), N466 (= N489), Q468 (≠ D491)
- 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 (≠ S405), M414 (= M431), G438 (= G455), G440 (= G457), N466 (= N489), Q468 (≠ D491), Y469 (≠ L492), G470 (≠ N493), W471 (≠ Q494), I472 (≠ V495)
Sites not aligning to the query:
2ez4B Pyruvate oxidase variant f479w (see paper)
30% identity, 91% coverage: 2:556/611 of query aligns to 2:533/585 of 2ez4B
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E64), S74 (≠ T87), F113 (≠ Q126), Q114 (= Q127), E115 (= E128), V162 (≠ N176), R256 (≠ L273), E283 (= E300), V386 (≠ S403), A412 (= A429), M414 (= M431), D439 (= D456), N466 (= N489), Q468 (≠ D491), Y469 (≠ L492), W471 (≠ Q494), I472 (≠ V495), E475 (= E498)
- binding flavin-adenine dinucleotide: H93 (= H106), G212 (= G229), I213 (≠ A230), G214 (= G231), T236 (≠ A253), Y237 (≠ L254), P238 (≠ L255), A254 (≠ I271), N255 (≠ G272), R256 (≠ L273), V257 (≠ L274), G276 (= G293), N277 (≠ S294), N278 (≠ G295), P280 (= P297), F281 (≠ Y298), D298 (= D314), I299 (≠ L315), K303 (≠ M319), D317 (= D333), A318 (≠ S334), N409 (≠ G426)
- binding magnesium ion: D439 (= D456), N466 (= N489), Q468 (≠ D491)
- binding phosphate ion: W471 (≠ Q494), E475 (= E498)
- binding thiamine diphosphate: D388 (≠ S405), A412 (= A429), M414 (= M431), G438 (= G455), D439 (= D456), G440 (= G457), G441 (≠ A458), N466 (= N489), Q468 (≠ D491), Y469 (≠ L492), G470 (≠ N493), W471 (≠ Q494), I472 (≠ V495)
Sites not aligning to the query:
1y9dD Pyruvate oxidase variant v265a from lactobacillus plantarum (see paper)
29% identity, 91% coverage: 2:556/611 of query aligns to 2:508/560 of 1y9dD
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E64), S74 (≠ T87), E108 (= E128), V155 (≠ N176), R241 (≠ L273), V361 (≠ S403), A387 (= A429), M389 (= M431), D414 (= D456), N441 (= N489), Q443 (≠ D491), Y444 (≠ L492), F446 (≠ Q494), I447 (≠ V495), E450 (= E498)
- binding flavin-adenine dinucleotide: I198 (≠ A230), G199 (= G231), T221 (≠ A253), P223 (≠ L255), G261 (= G293), N262 (≠ S294), N263 (≠ G295), D273 (= D314), I274 (≠ L315), K278 (≠ M319), D292 (= D333), A293 (≠ S334)
- binding magnesium ion: D414 (= D456), N441 (= N489), Q443 (≠ D491)
- binding thiamine diphosphate: E51 (= E64), S74 (≠ T87), P77 (= P90), H81 (= H94), D363 (≠ S405), M389 (= M431), G413 (= G455), G415 (= G457), N441 (= N489), Q443 (≠ D491), Y444 (≠ L492), G445 (≠ N493), F446 (≠ Q494), I447 (≠ V495)
Sites not aligning to the query:
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)
29% identity, 95% coverage: 7:586/611 of query aligns to 95:659/664 of P09114
- P191 (≠ A117) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
- W568 (= W497) 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)
29% identity, 95% coverage: 7:586/611 of query aligns to 98:662/667 of P09342
- C161 (= C84) modified: Disulfide link with 307
- P194 (≠ A117) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ A232) modified: Disulfide link with 161
6lpiB Crystal structure of ahas holo-enzyme (see paper)
28% identity, 83% coverage: 3:511/611 of query aligns to 6:477/539 of 6lpiB
- active site: I27 (≠ Y24), G29 (= G26), G30 (≠ D27), S31 (≠ G28), I32 (= I29), E53 (= E64), C76 (≠ T87), F115 (≠ Q126), Q116 (= Q127), E117 (= E128), K165 (≠ N176), M256 (≠ L273), A283 (vs. gap), V375 (≠ S403), G401 (≠ A429), M403 (= M431), D428 (= D456), N455 (= N489), A457 (≠ D491), L458 (= L492), L460 (≠ Q494), V461 (= V495), Q464 (≠ E498)
- binding flavin-adenine dinucleotide: R155 (= R167), G212 (= G229), G213 (≠ A230), G214 (= G231), T236 (≠ A253), L237 (= L254), M238 (≠ L255), L254 (≠ I271), M256 (≠ L273), H257 (≠ L274), G276 (= G293), A277 (≠ S294), R278 (≠ G295), D280 (vs. gap), R282 (vs. gap), A283 (vs. gap), D300 (= D314), I301 (≠ L315), D319 (= D333), V320 (≠ S334), M380 (≠ N408), G398 (= G426)
- binding magnesium ion: D428 (= D456), N455 (= N489)
- binding thiamine diphosphate: E53 (= E64), C76 (≠ T87), P79 (= P90), G376 (= G404), Q377 (≠ S405), H378 (≠ C406), G401 (≠ A429), M403 (= M431), G427 (= G455), D428 (= D456), G429 (= G457), S430 (≠ A458), M433 (= M461), N455 (= N489), A457 (≠ D491), L458 (= L492), G459 (≠ N493), L460 (≠ Q494), V461 (= V495)
1ozfA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors (see paper)
28% identity, 92% coverage: 7:566/611 of query aligns to 9:539/545 of 1ozfA
- active site: I26 (≠ Y24), G28 (= G26), A29 (≠ D27), K30 (≠ G28), I31 (= I29), E51 (= E64), T74 (= T87), H113 (≠ Q126), Q114 (= Q127), S115 (≠ E128), Q163 (≠ N176), L253 (= L273), E280 (≠ A299), M385 (≠ S403), Q411 (≠ A429), M413 (= M431), D438 (= D456), D465 (≠ C484), G467 (≠ V486), Y468 (≠ L487), M470 (≠ N489), V471 (≠ Q490), Q474 (≠ N493), Y534 (≠ P561)
- binding magnesium ion: D438 (= D456), D465 (≠ C484), G467 (≠ V486)
- binding phosphate ion: G249 (= G269), R250 (≠ S270), Q257 (≠ K277), R343 (= R351), R394 (= R412), L396 (= L414), Y397 (≠ K415)
- binding thiamine diphosphate: G386 (= G404), S387 (= S405), F388 (≠ C406), Q411 (≠ A429), M413 (= M431), G437 (= G455), D438 (= D456), G439 (= G457), D465 (≠ C484), G467 (≠ V486), Y468 (≠ L487), N469 (= N488), M470 (≠ N489), V471 (≠ Q490), Y534 (≠ P561)
1ozgA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate (see paper)
28% identity, 92% coverage: 7:566/611 of query aligns to 10:543/549 of 1ozgA
- active site: I27 (≠ Y24), G29 (= G26), A30 (≠ D27), K31 (≠ G28), I32 (= I29), E52 (= E64), T75 (= T87), H114 (≠ Q126), Q115 (= Q127), S116 (≠ E128), Q164 (≠ N176), L257 (= L273), E284 (≠ A299), M389 (≠ S403), Q415 (≠ A429), M417 (= M431), D442 (= D456), D469 (≠ C484), G471 (≠ V486), Y472 (≠ L487), M474 (≠ N489), V475 (≠ Q490), Q478 (≠ N493), Y538 (≠ P561)
- binding 2-hydroxyethyl dihydrothiachrome diphosphate: M389 (≠ S403), G390 (= G404), S391 (= S405), F392 (≠ C406), Q415 (≠ A429), M417 (= M431), G441 (= G455), D442 (= D456), G443 (= G457), D469 (≠ C484), G471 (≠ V486), Y472 (≠ L487), N473 (= N488), M474 (≠ N489), V475 (≠ Q490), Y538 (≠ P561)
- binding magnesium ion: D442 (= D456), D469 (≠ C484), G471 (≠ V486)
- binding phosphate ion: G253 (= G269), R254 (≠ S270), Q261 (≠ K277), R347 (= R351), R398 (= R412), Y401 (≠ K415)
6desA Crystal structure of candida albicans acetohydroxyacid synthase in complex with the herbicide propoxycarbazone (see paper)
26% identity, 93% coverage: 1:567/611 of query aligns to 10:564/598 of 6desA
- active site: Y33 (= Y24), G35 (= G26), G36 (≠ D27), A37 (≠ G28), I38 (= I29), E59 (= E64), T82 (= T87), F121 (≠ Q126), Q122 (= Q127), E123 (= E128), K171 (≠ N176), K229 (vs. gap), M265 (≠ L273), V292 (vs. gap), V408 (≠ S403), L433 (= L428), G434 (≠ A429), M436 (= M431), D461 (= D456), N488 (= N489), E490 (≠ D491), Q491 (≠ L492), M493 (≠ Q494), V494 (= V495), W497 (≠ E498), L519 (≠ F522), N524 (≠ G527), V525 (≠ L528)
- binding methyl 2-[(4-methyl-5-oxidanylidene-3-propoxy-1,2,4-triazol-1-yl)carbonylsulfamoyl]benzoate: M265 (≠ L273), D290 (vs. gap), R291 (vs. gap), W497 (≠ E498)
- binding flavin-adenine dinucleotide: R161 (= R167), G218 (= G229), A219 (= A230), G220 (= G231), N223 (≠ H234), T245 (≠ A253), L246 (= L254), Q247 (≠ L255), L263 (≠ I271), G285 (= G293), A286 (≠ S294), R287 (≠ G295), D289 (vs. gap), R291 (vs. gap), V292 (vs. gap), E318 (≠ D314), I319 (≠ L315), N323 (≠ M319), D337 (= D333), V338 (≠ S334), Q412 (≠ A407), M413 (≠ N408), G431 (= G426)
- binding magnesium ion: D461 (= D456), N488 (= N489), E490 (≠ D491)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: V408 (≠ S403), G409 (= G404), Q410 (≠ S405), H411 (≠ C406), G434 (≠ A429), M436 (= M431), G460 (= G455), D461 (= D456), A462 (≠ G457), S463 (≠ A458), N488 (= N489), E490 (≠ D491), Q491 (≠ L492), G492 (≠ N493), M493 (≠ Q494), V494 (= V495)
6depA Crystal structure of candida albicans acetohydroxyacid synthase in complex with the herbicide sulfometuron methyl (see paper)
26% identity, 93% coverage: 1:567/611 of query aligns to 10:564/598 of 6depA
- active site: Y33 (= Y24), G35 (= G26), G36 (≠ D27), A37 (≠ G28), I38 (= I29), E59 (= E64), T82 (= T87), F121 (≠ Q126), Q122 (= Q127), E123 (= E128), K171 (≠ N176), K229 (vs. gap), M265 (≠ L273), V292 (vs. gap), V408 (≠ S403), L433 (= L428), G434 (≠ A429), M436 (= M431), D461 (= D456), N488 (= N489), E490 (≠ D491), Q491 (≠ L492), M493 (≠ Q494), V494 (= V495), W497 (≠ E498), L519 (≠ F522), N524 (≠ G527), V525 (≠ L528)
- binding methyl 2-[({[(4,6-dimethylpyrimidin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: D290 (vs. gap), R291 (vs. gap), M493 (≠ Q494), W497 (≠ E498)
- binding flavin-adenine dinucleotide: R161 (= R167), G218 (= G229), A219 (= A230), G220 (= G231), N223 (≠ H234), T245 (≠ A253), L246 (= L254), Q247 (≠ L255), L263 (≠ I271), G264 (= G272), G285 (= G293), A286 (≠ S294), R287 (≠ G295), D289 (vs. gap), R291 (vs. gap), V292 (vs. gap), E318 (≠ D314), I319 (≠ L315), N323 (≠ M319), D337 (= D333), V338 (≠ S334), M413 (≠ N408), G431 (= G426)
- binding magnesium ion: D461 (= D456), N488 (= N489), E490 (≠ D491)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V408 (≠ S403), G409 (= G404), Q410 (≠ S405), H411 (≠ C406), G434 (≠ A429), M436 (= M431), G460 (= G455), D461 (= D456), A462 (≠ G457), S463 (≠ A458), M466 (= M461), N488 (= N489), E490 (≠ D491), Q491 (≠ L492), G492 (≠ N493), M493 (≠ Q494), V494 (= V495)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: V408 (≠ S403), G409 (= G404), Q410 (≠ S405), H411 (≠ C406), G434 (≠ A429), M436 (= M431), G460 (= G455), D461 (= D456), A462 (≠ G457), S463 (≠ A458), M466 (= M461), N488 (= N489), E490 (≠ D491), Q491 (≠ L492), G492 (≠ N493), M493 (≠ Q494), V494 (= V495)
6derA Crystal structure of candida albicans acetohydroxyacid synthase in complex with the herbicide metosulam (see paper)
26% identity, 93% coverage: 1:567/611 of query aligns to 12:566/600 of 6derA
- active site: Y35 (= Y24), G37 (= G26), G38 (≠ D27), A39 (≠ G28), I40 (= I29), E61 (= E64), T84 (= T87), F123 (≠ Q126), Q124 (= Q127), E125 (= E128), K173 (≠ N176), K231 (vs. gap), M267 (≠ L273), V294 (vs. gap), V410 (≠ S403), L435 (= L428), G436 (≠ A429), M438 (= M431), D463 (= D456), N490 (= N489), E492 (≠ D491), Q493 (≠ L492), M495 (≠ Q494), V496 (= V495), W499 (≠ E498), L521 (≠ F522), N526 (≠ G527), V527 (≠ L528)
- binding flavin-adenine dinucleotide: R163 (= R167), G220 (= G229), A221 (= A230), G222 (= G231), N225 (≠ H234), T247 (≠ A253), L248 (= L254), Q249 (≠ L255), L265 (≠ I271), H268 (≠ L274), G287 (= G293), A288 (≠ S294), R289 (≠ G295), D291 (vs. gap), R293 (vs. gap), V294 (vs. gap), E320 (≠ D314), I321 (≠ L315), N325 (≠ M319), G338 (= G332), D339 (= D333), V340 (≠ S334), Q414 (≠ A407), M415 (≠ N408), G433 (= G426)
- binding Metosulam: R293 (vs. gap), M495 (≠ Q494), W499 (≠ E498)
- binding magnesium ion: D463 (= D456), N490 (= N489), E492 (≠ D491)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V410 (≠ S403), G411 (= G404), Q412 (≠ S405), H413 (≠ C406), G436 (≠ A429), M438 (= M431), G462 (= G455), D463 (= D456), A464 (≠ G457), S465 (≠ A458), N490 (= N489), E492 (≠ D491), Q493 (≠ L492), G494 (≠ N493), M495 (≠ Q494), V496 (= V495)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: V410 (≠ S403), G411 (= G404), Q412 (≠ S405), H413 (≠ C406), G436 (≠ A429), M438 (= M431), G462 (= G455), D463 (= D456), A464 (≠ G457), S465 (≠ A458), M468 (= M461), N490 (= N489), E492 (≠ D491), Q493 (≠ L492), G494 (≠ N493), V496 (= V495)
Sites not aligning to the query:
Query Sequence
>H281DRAFT_03240 FitnessBrowser__Burk376:H281DRAFT_03240
MSITVGDFIIERLQAWGVRRIFGYPGDGINGVFGALNRAQTEAKKHRKTTGQPEPIEFIQ
VRHEEMAAFMASAHAKFTGELGVCIATSGPGASHLVTGLYDARMDHMPVLAITGQQARSA
LGGHYQQEVDLVSLFKDVAGAFVQQATVPAQVRHLVDRAIRTALSERKVTALVLPNDLQD
LPYEPPARKHGTLHSGVGYRAPRLVPQAEDLQQAADVLNAGKKVAILVGAGALHATDEVI
AVAEKLGAGVAKALLGKAALPDDLPWVTGSIGLLGTKPSYDLMTECDTLLMIGSGFPYAE
FLPKEGAARGVQIDLKADMLSLRYPMEVNLVGDSVETLRALLPLLEHKQDREWRKTIEGW
TADWWKTLDKRAHEPGKDAVNPQRTVWELSPRVPSNAIVTSDSGSCANWYARDLKVQRGM
MCSLSGGLASMGAAVPYAIAAKFAYPERPVIALVGDGAMQMSNMAELITVSKYWKGWADP
RWICMVLNNQDLNQVTWEQRVMEGDPKFEASQDIPSVPYHKFAELIGLKGIYVDDAEQMG
AAWDTALAADRPVVIEVKADPNIAPLPPHITLAQAKAFASTLLKGDPDEGNVIVQTAKQV
LGAVLPGHHDE
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