SitesBLAST
Comparing WP_037577100.1 NCBI__GCF_000744815.1:WP_037577100.1 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, 98% coverage: 1:586/600 of query aligns to 1:569/572 of P07003
- 1:182 (vs. 1:191, 36% identical) Pyr domain
- E50 (= E51) binding thiamine diphosphate
- 183:334 (vs. 192:343, 38% identical) FAD-binding domain
- S210 (≠ Q217) binding FAD
- LR 234:235 (≠ LL 241:242) binding FAD
- TGLI 251:254 (≠ SGLL 258:261) binding FAD
- TQFPY 274:278 (≠ SSFPY 281:285) binding FAD
- D292 (= D301) binding FAD
- S297 (≠ R306) binding FAD
- DI 311:312 (≠ DA 320:321) binding FAD
- 335:530 (vs. 344:548, 27% identical) PP-binding domain
- T382 (≠ S391) binding thiamine diphosphate
- FN 403:404 (≠ LS 410:411) binding FAD
- GSM 406:408 (≠ ATM 415:417) binding thiamine diphosphate
- D433 (= D442) binding Mg(2+)
- DGG 433:435 (≠ DGA 442:444) binding thiamine diphosphate
- N460 (= N475) binding Mg(2+)
- 460:466 (vs. 475:481, 43% identical) binding thiamine diphosphate
- V462 (≠ D477) binding Mg(2+)
- F465 (≠ Q480) Moves into active site upon enzyme activation, plays a role in electron transfer
- A533 (≠ P551) mutation to T: In poxB11; poor activity in vivo, no longer activated by lipids.
- YM 549:550 (≠ SL 567:568) In vitro cleavage to yield alpha-peptide
- A553 (≠ G571) mutation to V: In poxB14; poor activity in vivo, no longer activated by lipids.
- D560 (≠ H577) mutation to P: In poxB15; normal activity.
- E564 (≠ Q581) 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)
33% identity, 97% coverage: 3:586/600 of query aligns to 2:568/571 of 3ey9A
- active site: V23 (≠ Y24), G25 (= G26), D26 (= D27), S27 (≠ G28), L28 (≠ I29), E49 (= E51), S72 (≠ T74), F111 (≠ Q113), Q112 (= Q114), G160 (≠ A163), L252 (= L260), A279 (≠ Q287), V379 (≠ S389), G405 (≠ A415), M407 (= M417), D432 (= D442), N459 (= N475), V461 (≠ D477), L462 (= L478), F464 (≠ Q480), V465 (= V481), E468 (= E484), K528 (≠ P547)
- binding flavin-adenine dinucleotide: G208 (= G216), S209 (≠ Q217), G210 (= G218), A232 (= A240), L233 (= L241), R234 (≠ L242), T250 (≠ S258), G251 (= G259), I253 (≠ L261), G272 (= G280), T273 (≠ S281), Q274 (≠ S282), F275 (= F283), Y277 (= Y285), D291 (= D301), I292 (= I302), S296 (≠ R306), G309 (= G319), D310 (= D320), I311 (≠ A321), T383 (≠ A393), F402 (≠ L410), N403 (≠ S411), Y548 (≠ S567)
- binding magnesium ion: D432 (= D442), N459 (= N475)
- binding thiamine diphosphate: T24 (≠ P25), E49 (= E51), S72 (≠ T74), G76 (= G78), H79 (= H81), G380 (= G390), T381 (≠ S391), P382 (≠ A392), M407 (= M417), G431 (= G441), D432 (= D442), G433 (= G443), G434 (≠ A444), N459 (= N475), V461 (≠ D477), L462 (= L478), G463 (≠ N479)
9ev3A Corynebacterium glutamicum pyruvate:quinone oxidoreductase (pqo) purified from bacteria grown in acetate minimal medium (see paper)
30% identity, 92% coverage: 9:561/600 of query aligns to 8:545/577 of 9ev3A
- binding flavin-adenine dinucleotide: G208 (= G216), G210 (= G218), A232 (= A240), L233 (= L241), G234 (≠ L242), G251 (= G259), L253 (= L261), G272 (= G280), T273 (≠ S281), D274 (≠ S282), F275 (= F283), P276 (= P284), Y277 (= Y285), D290 (= D301), I291 (= I302), H295 (≠ R306), D309 (= D320), V310 (≠ A321), N385 (≠ A393), F405 (≠ G412), R406 (≠ T413)
- binding magnesium ion: D435 (= D442), N462 (= N475), S464 (≠ D477)
- binding thiamine diphosphate: G382 (= G390), M383 (≠ S391), M410 (= M417), G434 (= G441), D435 (= D442), G436 (= G443), G437 (≠ A444), M440 (= M447), S464 (≠ D477), L465 (= L478), G466 (≠ N479), M467 (≠ Q480), V468 (= V481)
2ezuA Pyruvate oxidase variant f479w in complex with reaction intermediate 2-acetyl-thiamin diphosphate (see paper)
29% identity, 89% coverage: 9:544/600 of query aligns to 9:535/585 of 2ezuA
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E51), S74 (≠ T74), F113 (≠ Q113), Q114 (= Q114), E115 (= E115), V162 (≠ A163), R256 (≠ L260), E283 (≠ Q287), V386 (≠ S389), A412 (= A415), M414 (= M417), D439 (= D442), N466 (= N474), Q468 (= Q480), Y469 (≠ V481), W471 (= W483), I472 (≠ E484), E475 (≠ S487)
- binding flavin-adenine dinucleotide: H93 (= H93), G212 (= G216), I213 (≠ Q217), G214 (= G218), T236 (≠ A240), Y237 (≠ L241), P238 (≠ L242), A254 (≠ S258), N255 (≠ G259), R256 (≠ L260), V257 (≠ L261), G276 (= G280), N277 (≠ S281), N278 (≠ S282), P280 (= P284), F281 (≠ Y285), D298 (= D301), I299 (= I302), K303 (≠ R306), D317 (= D320), A318 (= A321), N409 (≠ G412)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ S389), D388 (≠ S391), M414 (= M417), G438 (= G441), G440 (= G443), N466 (= N474), Q468 (= Q480), Y469 (≠ V481), G470 (≠ T482), W471 (= W483), I472 (≠ E484)
- binding magnesium ion: D439 (= D442), N466 (= N474), Q468 (= Q480)
Sites not aligning to the query:
2ez9A Pyruvate oxidase variant f479w in complex with reaction intermediate analogue 2-phosphonolactyl-thiamin diphosphate (see paper)
29% identity, 89% coverage: 9:544/600 of query aligns to 9:535/585 of 2ez9A
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E51), S74 (≠ T74), F113 (≠ Q113), Q114 (= Q114), E115 (= E115), V162 (≠ A163), R256 (≠ L260), E283 (≠ Q287), V386 (≠ S389), A412 (= A415), M414 (= M417), D439 (= D442), N466 (= N474), Q468 (= Q480), Y469 (≠ V481), W471 (= W483), I472 (≠ E484), E475 (≠ S487)
- binding flavin-adenine dinucleotide: H93 (= H93), G212 (= G216), I213 (≠ Q217), G214 (= G218), T236 (≠ A240), Y237 (≠ L241), P238 (≠ L242), A254 (≠ S258), N255 (≠ G259), R256 (≠ L260), V257 (≠ L261), G276 (= G280), N277 (≠ S281), N278 (≠ S282), P280 (= P284), F281 (≠ Y285), D298 (= D301), I299 (= I302), K303 (≠ R306), D317 (= D320), A318 (= A321), N409 (≠ G412)
- binding magnesium ion: D439 (= D442), N466 (= N474), Q468 (= Q480)
- 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 (≠ S389), D388 (≠ S391), M414 (= M417), G438 (= G441), G440 (= G443), N466 (= N474), Q468 (= Q480), Y469 (≠ V481), G470 (≠ T482), W471 (= W483), I472 (≠ E484), E475 (≠ S487)
Sites not aligning to the query:
2ez8A Pyruvate oxidase variant f479w in complex with reaction intermediate 2-lactyl-thiamin diphosphate (see paper)
29% identity, 89% coverage: 9:544/600 of query aligns to 9:535/585 of 2ez8A
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E51), S74 (≠ T74), F113 (≠ Q113), Q114 (= Q114), E115 (= E115), V162 (≠ A163), R256 (≠ L260), E283 (≠ Q287), V386 (≠ S389), A412 (= A415), M414 (= M417), D439 (= D442), N466 (= N474), Q468 (= Q480), Y469 (≠ V481), W471 (= W483), I472 (≠ E484), E475 (≠ S487)
- binding flavin-adenine dinucleotide: H93 (= H93), G212 (= G216), I213 (≠ Q217), G214 (= G218), T236 (≠ A240), Y237 (≠ L241), P238 (≠ L242), A254 (≠ S258), N255 (≠ G259), R256 (≠ L260), V257 (≠ L261), G276 (= G280), N277 (≠ S281), N278 (≠ S282), P280 (= P284), F281 (≠ Y285), D298 (= D301), I299 (= I302), K303 (≠ R306), D317 (= D320), A318 (= A321), N390 (≠ A393), N409 (≠ G412)
- binding magnesium ion: D439 (= D442), N466 (= N474), Q468 (= Q480)
- 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 (≠ S391), M414 (= M417), G438 (= G441), G440 (= G443), N466 (= N474), Q468 (= Q480), Y469 (≠ V481), G470 (≠ T482), W471 (= W483), I472 (≠ E484)
Sites not aligning to the query:
2ez4B Pyruvate oxidase variant f479w (see paper)
29% identity, 89% coverage: 9:544/600 of query aligns to 9:535/585 of 2ez4B
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E51), S74 (≠ T74), F113 (≠ Q113), Q114 (= Q114), E115 (= E115), V162 (≠ A163), R256 (≠ L260), E283 (≠ Q287), V386 (≠ S389), A412 (= A415), M414 (= M417), D439 (= D442), N466 (= N474), Q468 (= Q480), Y469 (≠ V481), W471 (= W483), I472 (≠ E484), E475 (≠ S487)
- binding flavin-adenine dinucleotide: H93 (= H93), G212 (= G216), I213 (≠ Q217), G214 (= G218), T236 (≠ A240), Y237 (≠ L241), P238 (≠ L242), A254 (≠ S258), N255 (≠ G259), R256 (≠ L260), V257 (≠ L261), G276 (= G280), N277 (≠ S281), N278 (≠ S282), P280 (= P284), F281 (≠ Y285), D298 (= D301), I299 (= I302), K303 (≠ R306), D317 (= D320), A318 (= A321), N409 (≠ G412)
- binding magnesium ion: D439 (= D442), N466 (= N474), Q468 (= Q480)
- binding phosphate ion: W471 (= W483), E475 (≠ S487)
- binding thiamine diphosphate: D388 (≠ S391), A412 (= A415), M414 (= M417), G438 (= G441), D439 (= D442), G440 (= G443), G441 (vs. gap), N466 (= N474), Q468 (= Q480), Y469 (≠ V481), G470 (≠ T482), W471 (= W483), I472 (≠ E484)
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)
28% identity, 89% coverage: 9:544/600 of query aligns to 9:535/586 of 4feeA
- binding flavin-adenine dinucleotide: H93 (= H93), G212 (= G216), I213 (≠ Q217), G214 (= G218), T236 (≠ A240), Y237 (≠ L241), P238 (≠ L242), A254 (≠ S258), N255 (≠ G259), V257 (≠ L261), G276 (= G280), N277 (≠ S281), N278 (≠ S282), P280 (= P284), F281 (≠ Y285), D298 (= D301), I299 (= I302), K303 (≠ R306), D317 (= D320), A318 (= A321), N390 (≠ A393), N409 (≠ G412)
- binding magnesium ion: D439 (= D442), N466 (= N474), Q468 (= Q476)
- binding pyruvic acid: N255 (≠ G259), R256 (≠ L260)
- 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 (≠ S389), D388 (≠ S391), A412 (= A415), M414 (= M417), G438 (= G441), G440 (= G443), N466 (= N474), Q468 (= Q476), Y469 (≠ N479), G470 (≠ Q480), F471 (≠ V481), I472 (≠ T482)
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)
28% identity, 89% coverage: 9:544/600 of query aligns to 9:535/585 of 1powA
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E51), S74 (≠ T74), F113 (≠ Q113), Q114 (= Q114), E115 (= E115), V162 (≠ A163), R256 (≠ L260), E283 (≠ Q287), V386 (≠ S389), A412 (= A415), M414 (= M417), D439 (= D442), N466 (= N474), Q468 (= Q476), Y469 (≠ N479), F471 (≠ V481), I472 (≠ T482), E475 (≠ M485)
- binding flavin-adenine dinucleotide: H93 (= H93), G212 (= G216), I213 (≠ Q217), G214 (= G218), T236 (≠ A240), Y237 (≠ L241), A254 (≠ S258), V257 (≠ L261), G276 (= G280), N277 (≠ S281), N278 (≠ S282), Y279 (≠ F283), P280 (= P284), F281 (≠ Y285), D298 (= D301), I299 (= I302), K303 (≠ R306), D317 (= D320), A318 (= A321), N409 (≠ G412)
- binding magnesium ion: D439 (= D442), N466 (= N474), Q468 (= Q476)
- binding thiamine diphosphate: D388 (≠ S391), M414 (= M417), G440 (= G443), N466 (= N474), Q468 (= Q476), Y469 (≠ N479), G470 (≠ Q480), F471 (≠ V481), I472 (≠ T482)
Sites not aligning to the query:
9ev4A Pyruvate:quinone oxidoreductase (pqo) from corynebacterium glutamicum cs176 (see paper)
30% identity, 92% coverage: 9:561/600 of query aligns to 7:522/553 of 9ev4A
- binding flavin-adenine dinucleotide: G207 (= G216), A208 (≠ Q217), G209 (= G218), A231 (= A240), L232 (= L241), G233 (≠ L242), G250 (= G259), L252 (= L261), G271 (= G280), T272 (≠ S281), D273 (≠ S282), F274 (= F283), Y276 (= Y285), D289 (= D301), I290 (= I302), H294 (≠ R306), D308 (= D320), V309 (≠ A321), N384 (≠ A393), F404 (≠ G412), R405 (≠ T413)
1v5gA Crystal structure of the reaction intermediate between pyruvate oxidase containing fad and tpp, and substrate pyruvate (see paper)
28% identity, 88% coverage: 9:537/600 of query aligns to 9:525/589 of 1v5gA
- binding flavin-adenine dinucleotide: G212 (= G216), I213 (≠ Q217), G214 (= G218), T236 (≠ A240), G237 (≠ L241), K238 (≠ L242), T254 (≠ S258), Y255 (≠ G259), R256 (≠ L260), V257 (≠ L261), G276 (= G280), S277 (= S281), N278 (≠ S282), F279 (= F283), F281 (≠ Y285), D298 (= D301), I299 (= I302), M303 (≠ R306), D317 (= D320), A318 (= A321), P409 (≠ G412)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ S389), N388 (≠ S391), M414 (= M417), G438 (= G441), G440 (= G443), A441 (= A444), N466 (= N475), E468 (≠ D477), Y469 (≠ L478), A470 (≠ N479), F471 (≠ Q480), I472 (≠ V481)
- binding magnesium ion: D439 (= D442), N466 (= N475), E468 (≠ D477)
1v5fA Crystal structure of pyruvate oxidase complexed with fad and tpp, from aerococcus viridans (see paper)
28% identity, 88% coverage: 9:537/600 of query aligns to 9:525/589 of 1v5fA
- binding flavin-adenine dinucleotide: G212 (= G216), I213 (≠ Q217), G214 (= G218), T236 (≠ A240), G237 (≠ L241), K238 (≠ L242), T254 (≠ S258), Y255 (≠ G259), R256 (≠ L260), V257 (≠ L261), G276 (= G280), S277 (= S281), N278 (≠ S282), F279 (= F283), P280 (= P284), F281 (≠ Y285), D298 (= D301), I299 (= I302), M303 (≠ R306), D317 (= D320), A318 (= A321), P409 (≠ G412)
- binding magnesium ion: D439 (= D442), N466 (= N475)
- binding thiamine diphosphate: N388 (≠ S391), S389 (≠ A392), M414 (= M417), G438 (= G441), G440 (= G443), N466 (= N475), Y469 (≠ L478), A470 (≠ N479), F471 (≠ Q480), I472 (≠ V481)
2djiA Crystal structure of pyruvate oxidase from aerococcus viridans containing fad (see paper)
28% identity, 88% coverage: 9:537/600 of query aligns to 10:526/590 of 2djiA
- active site: I25 (≠ Y24), S27 (≠ G26), G28 (≠ D27), T29 (≠ G28), L30 (≠ I29), E52 (= E51), S75 (≠ T74), F114 (≠ Q113), Q115 (= Q114), G163 (≠ A163), R257 (≠ L260), E284 (≠ Q287), V387 (≠ S389), A413 (= A415), M415 (= M417), D440 (= D442), N467 (= N475), E469 (≠ D477), Y470 (≠ L478), F472 (≠ Q480), I473 (≠ V481), K476 (≠ S487)
- binding flavin-adenine dinucleotide: G213 (= G216), I214 (≠ Q217), G215 (= G218), T237 (≠ A240), G238 (≠ L241), K239 (≠ L242), T255 (≠ S258), Y256 (≠ G259), R257 (≠ L260), V258 (≠ L261), G277 (= G280), S278 (= S281), N279 (≠ S282), F280 (= F283), P281 (= P284), F282 (≠ Y285), D299 (= D301), I300 (= I302), M304 (≠ R306), D318 (= D320), A319 (= A321), P410 (≠ G412)
Sites not aligning to the query:
1y9dD Pyruvate oxidase variant v265a from lactobacillus plantarum (see paper)
28% identity, 89% coverage: 9:544/600 of query aligns to 9:510/560 of 1y9dD
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E51), S74 (≠ T74), E108 (= E115), V155 (≠ A163), R241 (≠ L260), V361 (≠ S389), A387 (= A415), M389 (= M417), D414 (= D442), N441 (= N474), Q443 (= Q476), Y444 (≠ N479), F446 (≠ V481), I447 (≠ T482), E450 (≠ M485)
- binding flavin-adenine dinucleotide: I198 (≠ Q217), G199 (= G218), T221 (≠ A240), P223 (≠ L242), G261 (= G280), N262 (≠ S281), N263 (≠ S282), D273 (= D301), I274 (= I302), K278 (≠ R306), D292 (= D320), A293 (= A321)
- binding magnesium ion: D414 (= D442), N441 (= N474), Q443 (= Q476)
- binding thiamine diphosphate: E51 (= E51), S74 (≠ T74), P77 (= P77), H81 (= H81), D363 (≠ S391), M389 (= M417), G413 (= G441), G415 (= G443), N441 (= N474), Q443 (= Q476), Y444 (≠ N479), G445 (≠ Q480), F446 (≠ V481), I447 (≠ T482)
Sites not aligning to the query:
8x3xB Thdp-dependent hka synthase
33% identity, 91% coverage: 7:551/600 of query aligns to 7:523/537 of 8x3xB
- binding adenosine-5'-diphosphate: R157 (= R153), G214 (= G216), H215 (≠ Q217), C219 (≠ G221), A220 (= A222), T240 (≠ A240), K242 (≠ L242), G282 (= G280), S283 (= S281), S284 (= S282), Q289 (≠ P284), D307 (= D301), I308 (= I302), D326 (= D320), A327 (= A321)
- binding 3-(4-hydroxy-phenyl)pyruvic acid: G27 (≠ D27), M30 (≠ N30), V454 (= V481), G457 (≠ E484), Q461 (≠ M488)
- binding magnesium ion: D421 (= D442), N448 (= N475), G450 (≠ D477)
- binding thiamine diphosphate: E50 (= E51), T73 (= T74), S370 (= S391), M396 (= M417), G420 (= G441), D421 (= D442), A422 (≠ G443), A423 (= A444), N448 (= N475), G450 (≠ D477), H451 (≠ L478), G452 (≠ N479), L453 (≠ Q480)
Sites not aligning to the query:
8xodA BbmA-G484F complex with CBOA
33% identity, 91% coverage: 7:551/600 of query aligns to 8:524/532 of 8xodA
- binding 2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-2-[(~{R})-cyclobutyl(oxidanyl)methyl]-4-methyl-1,3-thiazol-5-yl]ethyl phosphono hydrogen phosphate: G28 (≠ D27), E51 (= E51), P77 (= P77), S371 (= S391), M397 (= M417), G421 (= G441), D422 (= D442), A423 (≠ G443), A424 (= A444), N449 (= N475), H452 (≠ L478), G453 (≠ N479), L454 (≠ Q480)
- binding adenosine-5'-diphosphate: R158 (= R153), G215 (= G216), H216 (≠ Q217), G217 (= G218), A221 (= A222), T241 (≠ A240), G283 (= G280), S284 (= S281), S285 (= S282), Q290 (≠ P284), D308 (= D301), I309 (= I302), E313 (≠ R306), A328 (= A321)
- binding magnesium ion: D422 (= D442), N449 (= N475)
7tzzA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase p197t mutant in complex with bispyribac-sodium (see paper)
31% identity, 93% coverage: 6:561/600 of query aligns to 15:575/582 of 7tzzA
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: M266 (≠ L260), R292 (vs. gap), W489 (= W483), S568 (≠ P554)
- 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 (≠ S389), G401 (= G390), Q402 (≠ S391), H403 (≠ A392), G426 (≠ A415), M428 (= M417), G452 (= G441), D453 (= D442), G454 (= G443), S455 (≠ A444), L483 (= L478), G484 (≠ N479), M485 (≠ Q480), V486 (= V481)
- binding flavin-adenine dinucleotide: R161 (= R153), G222 (= G216), G223 (≠ Q217), G224 (= G218), T246 (≠ A240), L247 (= L241), M248 (≠ L242), M263 (≠ A257), L264 (≠ S258), M266 (≠ L260), H267 (≠ L261), G286 (= G280), R288 (≠ S282), V293 (≠ Y285), D310 (= D301), I311 (= I302), D329 (= D320), V330 (≠ A321), M405 (≠ N394), G423 (= G412)
- binding magnesium ion: A37 (≠ G28), T82 (= T74), S83 (= S75), Q122 (= Q114), Y381 (= Y370), D453 (= D442), M458 (= M447), Q461 (≠ A451), N480 (= N475), H482 (≠ D477), K533 (≠ P522)
5k2oA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a pyrimidinyl-benzoate herbicide, pyrithiobac (see paper)
31% identity, 93% coverage: 6:561/600 of query aligns to 15:575/585 of 5k2oA
- active site: Y33 (= Y24), G35 (= G26), G36 (≠ D27), A37 (≠ G28), S38 (≠ I29), E59 (= E51), T82 (= T74), F121 (≠ Q113), Q122 (= Q114), E123 (= E115), K171 (≠ A163), M266 (≠ L260), V293 (≠ Y285), V400 (≠ S389), G426 (≠ A415), M428 (= M417), D453 (= D442), N480 (= N475), H482 (≠ D477), L483 (= L478), M485 (≠ Q480), V486 (= V481), W489 (= W483), H558 (vs. gap)
- binding 2-chloranyl-6-(4,6-dimethoxypyrimidin-2-yl)sulfanyl-benzoic acid: M266 (≠ L260), R292 (vs. gap), W489 (= W483), S568 (≠ P554)
- binding flavin-adenine dinucleotide: R161 (= R153), G222 (= G216), G223 (≠ Q217), G224 (= G218), T246 (≠ A240), L247 (= L241), M248 (≠ L242), L264 (≠ S258), G286 (= G280), R288 (≠ S282), D290 (≠ P284), V293 (≠ Y285), D310 (= D301), I311 (= I302), D329 (= D320), V330 (≠ A321), Q404 (≠ A393), M405 (≠ N394), G423 (= G412)
- binding magnesium ion: D453 (= D442), N480 (= N475), H482 (≠ D477)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (≠ S389), G401 (= G390), Q402 (≠ S391), H403 (≠ A392), M428 (= M417), D453 (= D442), G454 (= G443), S455 (≠ A444), N480 (= N475), H482 (≠ D477), L483 (= L478), G484 (≠ N479), M485 (≠ Q480), V486 (= V481)
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)
31% identity, 93% coverage: 6:561/600 of query aligns to 100:660/670 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 thiamine diphosphate
- S186 (≠ H93) binding FAD
- P197 (≠ A104) mutation to S: In csr1-1/GH50; resistant to sulfonylurea but not to imidazolinone herbicides.
- R199 (≠ T106) mutation R->A,E: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- Q207 (= Q114) binding thiamine diphosphate
- K220 (≠ E128) binding (R)-imazaquin
- R246 (= R153) binding (R)-imazaquin; binding FAD
- K256 (≠ A163) binding chlorimuron-ethyl
- G308 (≠ Q217) binding FAD
- TL 331:332 (≠ AL 240:241) binding FAD
- C340 (≠ D249) modified: Cysteine sulfinic acid (-SO2H)
- LGMH 349:352 (≠ SGLL 258:261) binding FAD
- GVRFD 371:375 (≠ GSSFP 280:284) binding FAD
- DR 376:377 (vs. gap) binding chlorimuron-ethyl
- DI 395:396 (= DI 301:302) binding FAD
- DV 414:415 (≠ DA 320:321) binding FAD
- QH 487:488 (≠ SA 391:392) binding thiamine diphosphate
- GG 508:509 (≠ GT 412:413) binding FAD
- GAM 511:513 (≠ ATM 415:417) binding thiamine diphosphate
- D538 (= D442) binding Mg(2+)
- DGS 538:540 (≠ DGA 442:444) binding thiamine diphosphate
- N565 (= N475) binding Mg(2+)
- NQHLGM 565:570 (≠ NQDLNQ 475:480) binding thiamine diphosphate
- H567 (≠ D477) binding Mg(2+)
- W574 (= W483) binding chlorimuron-ethyl; 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.
- S653 (≠ P554) binding chlorimuron-ethyl; mutation to A: No effect on catalytic activity or sensitivity to herbicides.; mutation to F: No effect on catalytic activity. Resistant to imidazolinone herbicides and also slightly sulfonylurea-resistant.; mutation to N: In csr1-2/GH90; no effect on catalytic activity. Resistant to imidazolinone but not to sulfonylurea herbicides.; mutation to T: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
9c4rA Acetolactate synthase, chloroplastic (see paper)
31% identity, 93% coverage: 6:561/600 of query aligns to 15:575/582 of 9c4rA
- binding 2-(2-chloroethoxy)-N-[(4-methoxy-6-methylpyrimidin-2-yl)carbamoyl]benzene-1-sulfonamide: M266 (≠ L260), R292 (vs. gap), W489 (= W483), S568 (≠ P554)
- 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 (≠ S389), G401 (= G390), Q402 (≠ S391), H403 (≠ A392), G426 (≠ A415), M428 (= M417), G452 (= G441), G454 (= G443), S455 (≠ A444), M458 (= M447), N480 (= N475), H482 (≠ D477), L483 (= L478), G484 (≠ N479), M485 (≠ Q480), V486 (= V481)
- binding flavin-adenine dinucleotide: R161 (= R153), G222 (= G216), G223 (≠ Q217), G224 (= G218), T246 (≠ A240), L247 (= L241), M248 (≠ L242), L264 (≠ S258), M266 (≠ L260), H267 (≠ L261), G286 (= G280), V287 (≠ S281), R288 (≠ S282), D290 (≠ P284), V293 (≠ Y285), D310 (= D301), I311 (= I302), D329 (= D320), V330 (≠ A321), M405 (≠ N394), G423 (= G412)
- binding magnesium ion: D453 (= D442), N480 (= N475), H482 (≠ D477)
Query Sequence
>WP_037577100.1 NCBI__GCF_000744815.1:WP_037577100.1
MSEQVSDFILRRLREWDVDYVFGYPGDGINGLLSAWERAGDQPRFIQARHEEMAAFEAVG
YAKFSGRVGVCAATSGPGAIHLLNGLYDAKLDHVPVVALVGQTAQTAIGGSYQQEVDLPN
LYKDVASEYCQLVTTPEQLPNVLDRAMRIAQARKTVTAVIVPADVQDLEYSAPTHAFKMV
PSSLGFSGSAYVPHEDDLARAAEVLNSGSKVAILAGQGARGASAELIETAEVLGAGVAKA
LLGKDVLPDDLPFVTGASGLLGTRPTYELMKDCDTLLVIGSSFPYSQFLPEFGQARAVQI
DIDPGRIGMRYPFEVNLVGDARETLRRLLPLLSRKEDRGWREKIEQNNSRWWEVMKRRAS
VEADPINPEYAVHVLDGLLPGRAIITADSGSAANWYARHLRIREGINGSLSGTLATMGPG
VPYAIGAKFSCPDRPAIALVGDGAMQMNGLAELITVGKYWQEWRDPRLVVCVLNNQDLNQ
VTWEMRSMSGSPQFLPSQQLPDVRYADFARGLGLHGIRVEKPEEVEPAWRAALESDRPCV
LDVLTDPAVPPIPPHATWDQIEATASSLLHGDSDRGHVIKQGAKAKIQDFLHGRRGEDDS
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