SitesBLAST
Comparing WP_057506889.1 NCBI__GCF_001431535.1:WP_057506889.1 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)
45% identity, 100% coverage: 1:571/572 of query aligns to 1:572/572 of P07003
- 1:182 (vs. 1:180, 43% identical) Pyr domain
- E50 (= E49) binding
- 183:334 (vs. 181:332, 45% identical) FAD-binding domain
- S210 (≠ A208) binding
- LR 234:235 (≠ SR 232:233) binding
- TGLI 251:254 (≠ TGIF 249:252) binding
- TQFPY 274:278 (≠ ADFAW 272:276) binding
- D292 (= D290) binding
- S297 (≠ H295) binding
- DI 311:312 (= DI 309:310) binding
- 335:530 (vs. 333:529, 47% identical) PP-binding domain
- T382 (≠ S381) binding
- FN 403:404 (≠ LL 402:403) binding
- GSM 406:408 (≠ GTM 405:407) binding
- D433 (= D432) binding
- DGG 433:435 (= DGG 432:434) binding
- N460 (= N459) binding
- 460:466 (vs. 459:465, 57% identical) binding
- V462 (≠ S461) binding
- F465 (= F464) Moves into active site upon enzyme activation, plays a role in electron transfer
- 531:572 (vs. 530:571, 43% identical) Membrane-binding domain
- A533 (≠ V532) mutation to T: In poxB11; poor activity in vivo, no longer activated by lipids.
- YM 549:550 (= YM 548:549) In vitro cleavage to yield alpha-peptide
- 549:572 (vs. 548:571, 46% 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 (= A552) mutation to V: In poxB14; poor activity in vivo, no longer activated by lipids.
- D560 (≠ G559) mutation to P: In poxB15; normal activity.
- E564 (= E563) mutation to P: In poxB16; loss of activity, weakly activated by cleavage.
- 564:572 (vs. 563:571, 44% identical) mutation Missing: In poxB7 Inactive in vivo, reduced activity in vitro.
- WLR 570:572 (≠ FLK 569:571) mutation Missing: In poxB8; reduced activity in vitro, not activated by lipids.
- R572 (≠ K571) 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)
45% identity, 100% coverage: 2:571/572 of query aligns to 1:571/571 of 3ey9A
- active site: V23 (≠ I24), G25 (= G26), D26 (= D27), S27 (≠ T28), L28 (= L29), E49 (= E49), S72 (= S72), F111 (≠ P111), Q112 (= Q112), G160 (≠ S160), L252 (≠ I251), A279 (≠ Q278), V379 (≠ C379), G405 (= G405), M407 (= M407), D432 (= D432), N459 (= N459), V461 (≠ S461), L462 (= L462), F464 (= F464), V465 (= V465), E468 (= E468), K528 (≠ P528)
- binding flavin-adenine dinucleotide: G208 (= G207), S209 (≠ A208), G210 (= G209), A232 (≠ T231), L233 (≠ S232), R234 (= R233), T250 (= T249), G251 (= G250), I253 (≠ F252), G272 (= G271), T273 (≠ A272), Q274 (≠ D273), F275 (= F274), Y277 (≠ W276), D291 (= D290), I292 (≠ H291), S296 (≠ H295), G309 (= G308), D310 (= D309), I311 (= I310), T383 (≠ M383), F402 (≠ L402), N403 (≠ L403), Y548 (= Y548)
- binding magnesium ion: D432 (= D432), N459 (= N459)
- binding thiamine diphosphate: T24 (≠ V25), E49 (= E49), S72 (= S72), G76 (= G76), H79 (= H79), G380 (= G380), T381 (≠ S381), P382 (= P382), M407 (= M407), G431 (= G431), D432 (= D432), G433 (= G433), G434 (= G434), N459 (= N459), V461 (≠ S461), L462 (= L462), G463 (≠ N463)
2djiA Crystal structure of pyruvate oxidase from aerococcus viridans containing fad (see paper)
30% identity, 87% coverage: 9:506/572 of query aligns to 10:514/590 of 2djiA
- active site: I25 (= I24), S27 (≠ G26), G28 (≠ D27), T29 (= T28), L30 (= L29), E52 (= E49), S75 (= S72), F114 (≠ P111), Q115 (= Q112), G163 (≠ S160), R257 (≠ I251), E284 (≠ Q278), V387 (≠ C379), A413 (≠ G405), M415 (= M407), D440 (= D432), N467 (= N459), E469 (≠ S461), Y470 (≠ L462), F472 (= F464), I473 (≠ V465), K476 (≠ E468)
- binding flavin-adenine dinucleotide: G213 (= G207), I214 (≠ A208), G215 (= G209), T237 (= T231), G238 (≠ S232), K239 (≠ R233), T255 (= T249), Y256 (≠ G250), R257 (≠ I251), V258 (≠ F252), G277 (= G271), S278 (≠ A272), N279 (≠ D273), F280 (= F274), P281 (≠ A275), F282 (≠ W276), D299 (= D290), I300 (≠ H291), M304 (≠ H295), D318 (= D309), A319 (≠ I310), P410 (≠ L402)
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)
30% identity, 87% coverage: 9:506/572 of query aligns to 9:513/589 of 1v5gA
- binding flavin-adenine dinucleotide: G212 (= G207), I213 (≠ A208), G214 (= G209), T236 (= T231), G237 (≠ S232), K238 (≠ R233), T254 (= T249), Y255 (≠ G250), R256 (≠ I251), V257 (≠ F252), G276 (= G271), S277 (≠ A272), N278 (≠ D273), F279 (= F274), F281 (≠ W276), D298 (= D290), I299 (≠ H291), M303 (≠ H295), D317 (= D309), A318 (≠ I310), P409 (≠ L402)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ C379), N388 (≠ S381), M414 (= M407), G438 (= G431), G440 (= G433), A441 (≠ G434), N466 (= N459), E468 (≠ S461), Y469 (≠ L462), A470 (≠ N463), F471 (= F464), I472 (≠ V465)
- binding magnesium ion: D439 (= D432), N466 (= N459), E468 (≠ S461)
1v5fA Crystal structure of pyruvate oxidase complexed with fad and tpp, from aerococcus viridans (see paper)
30% identity, 87% coverage: 9:506/572 of query aligns to 9:513/589 of 1v5fA
- binding flavin-adenine dinucleotide: G212 (= G207), I213 (≠ A208), G214 (= G209), T236 (= T231), G237 (≠ S232), K238 (≠ R233), T254 (= T249), Y255 (≠ G250), R256 (≠ I251), V257 (≠ F252), G276 (= G271), S277 (≠ A272), N278 (≠ D273), F279 (= F274), P280 (≠ A275), F281 (≠ W276), D298 (= D290), I299 (≠ H291), M303 (≠ H295), D317 (= D309), A318 (≠ I310), P409 (≠ L402)
- binding magnesium ion: D439 (= D432), N466 (= N459)
- binding thiamine diphosphate: N388 (≠ S381), S389 (≠ P382), M414 (= M407), G438 (= G431), G440 (= G433), N466 (= N459), Y469 (≠ L462), A470 (≠ N463), F471 (= F464), I472 (≠ V465)
1powA The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from lactobacillus plantarum (see paper)
30% identity, 90% coverage: 9:523/572 of query aligns to 9:533/585 of 1powA
- active site: I24 (= I24), G26 (= G26), G27 (≠ D27), S28 (≠ T28), I29 (≠ L29), E51 (= E49), S74 (= S72), F113 (≠ P111), Q114 (= Q112), E115 (= E113), V162 (≠ S160), R256 (≠ I251), E283 (≠ Q278), V386 (≠ C379), A412 (≠ G405), M414 (= M407), D439 (= D432), N466 (= N459), Q468 (≠ S461), Y469 (≠ L462), F471 (= F464), I472 (≠ V465), E475 (= E468)
- binding flavin-adenine dinucleotide: H93 (≠ K91), G212 (= G207), I213 (≠ A208), G214 (= G209), T236 (= T231), Y237 (≠ S232), A254 (≠ T249), V257 (≠ F252), G276 (= G271), N277 (≠ A272), N278 (≠ D273), Y279 (≠ F274), P280 (≠ A275), F281 (≠ W276), D298 (= D290), I299 (≠ H291), K303 (≠ H295), D317 (= D309), A318 (≠ I310), N409 (≠ L402)
- binding magnesium ion: D439 (= D432), N466 (= N459), Q468 (≠ S461)
- binding thiamine diphosphate: D388 (≠ S381), M414 (= M407), G440 (= G433), N466 (= N459), Q468 (≠ S461), Y469 (≠ L462), G470 (≠ N463), F471 (= F464), I472 (≠ V465)
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, 90% coverage: 9:523/572 of query aligns to 9:533/586 of 4feeA
- binding flavin-adenine dinucleotide: H93 (≠ K91), G212 (= G207), I213 (≠ A208), G214 (= G209), T236 (= T231), Y237 (≠ S232), P238 (≠ R233), A254 (≠ T249), N255 (≠ G250), V257 (≠ F252), G276 (= G271), N277 (≠ A272), N278 (≠ D273), P280 (≠ A275), F281 (≠ W276), D298 (= D290), I299 (≠ H291), K303 (≠ H295), D317 (= D309), A318 (≠ I310), N390 (≠ M383), N409 (≠ L402)
- binding magnesium ion: D439 (= D432), N466 (= N459), Q468 (≠ S461)
- binding pyruvic acid: N255 (≠ G250), R256 (≠ I251)
- 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 (≠ C379), D388 (≠ S381), A412 (≠ G405), M414 (= M407), G438 (= G431), G440 (= G433), N466 (= N459), Q468 (≠ S461), Y469 (≠ L462), G470 (≠ N463), F471 (= F464), I472 (≠ V465)
Sites not aligning to the query:
2ezuA Pyruvate oxidase variant f479w in complex with reaction intermediate 2-acetyl-thiamin diphosphate (see paper)
29% identity, 90% coverage: 9:523/572 of query aligns to 9:533/585 of 2ezuA
- active site: I24 (= I24), G26 (= G26), G27 (≠ D27), S28 (≠ T28), I29 (≠ L29), E51 (= E49), S74 (= S72), F113 (≠ P111), Q114 (= Q112), E115 (= E113), V162 (≠ S160), R256 (≠ I251), E283 (≠ Q278), V386 (≠ C379), A412 (≠ G405), M414 (= M407), D439 (= D432), N466 (= N459), Q468 (≠ S461), Y469 (≠ L462), W471 (≠ F464), I472 (≠ V465), E475 (= E468)
- binding flavin-adenine dinucleotide: H93 (≠ K91), G212 (= G207), I213 (≠ A208), G214 (= G209), T236 (= T231), Y237 (≠ S232), P238 (≠ R233), A254 (≠ T249), N255 (≠ G250), R256 (≠ I251), V257 (≠ F252), G276 (= G271), N277 (≠ A272), N278 (≠ D273), P280 (≠ A275), F281 (≠ W276), D298 (= D290), I299 (≠ H291), K303 (≠ H295), D317 (= D309), A318 (≠ I310), N409 (≠ L402)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ C379), D388 (≠ S381), M414 (= M407), G438 (= G431), G440 (= G433), N466 (= N459), Q468 (≠ S461), Y469 (≠ L462), G470 (≠ N463), W471 (≠ F464), I472 (≠ V465)
- binding magnesium ion: D439 (= D432), N466 (= N459), Q468 (≠ S461)
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, 90% coverage: 9:523/572 of query aligns to 9:533/585 of 2ez9A
- active site: I24 (= I24), G26 (= G26), G27 (≠ D27), S28 (≠ T28), I29 (≠ L29), E51 (= E49), S74 (= S72), F113 (≠ P111), Q114 (= Q112), E115 (= E113), V162 (≠ S160), R256 (≠ I251), E283 (≠ Q278), V386 (≠ C379), A412 (≠ G405), M414 (= M407), D439 (= D432), N466 (= N459), Q468 (≠ S461), Y469 (≠ L462), W471 (≠ F464), I472 (≠ V465), E475 (= E468)
- binding flavin-adenine dinucleotide: H93 (≠ K91), G212 (= G207), I213 (≠ A208), G214 (= G209), T236 (= T231), Y237 (≠ S232), P238 (≠ R233), A254 (≠ T249), N255 (≠ G250), R256 (≠ I251), V257 (≠ F252), G276 (= G271), N277 (≠ A272), N278 (≠ D273), P280 (≠ A275), F281 (≠ W276), D298 (= D290), I299 (≠ H291), K303 (≠ H295), D317 (= D309), A318 (≠ I310), N409 (≠ L402)
- binding magnesium ion: D439 (= D432), N466 (= N459), Q468 (≠ S461)
- 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 (≠ C379), D388 (≠ S381), M414 (= M407), G438 (= G431), G440 (= G433), N466 (= N459), Q468 (≠ S461), Y469 (≠ L462), G470 (≠ N463), W471 (≠ F464), I472 (≠ V465), E475 (= E468)
Sites not aligning to the query:
2ez8A Pyruvate oxidase variant f479w in complex with reaction intermediate 2-lactyl-thiamin diphosphate (see paper)
29% identity, 90% coverage: 9:523/572 of query aligns to 9:533/585 of 2ez8A
- active site: I24 (= I24), G26 (= G26), G27 (≠ D27), S28 (≠ T28), I29 (≠ L29), E51 (= E49), S74 (= S72), F113 (≠ P111), Q114 (= Q112), E115 (= E113), V162 (≠ S160), R256 (≠ I251), E283 (≠ Q278), V386 (≠ C379), A412 (≠ G405), M414 (= M407), D439 (= D432), N466 (= N459), Q468 (≠ S461), Y469 (≠ L462), W471 (≠ F464), I472 (≠ V465), E475 (= E468)
- binding flavin-adenine dinucleotide: H93 (≠ K91), G212 (= G207), I213 (≠ A208), G214 (= G209), T236 (= T231), Y237 (≠ S232), P238 (≠ R233), A254 (≠ T249), N255 (≠ G250), R256 (≠ I251), V257 (≠ F252), G276 (= G271), N277 (≠ A272), N278 (≠ D273), P280 (≠ A275), F281 (≠ W276), D298 (= D290), I299 (≠ H291), K303 (≠ H295), D317 (= D309), A318 (≠ I310), N390 (≠ M383), N409 (≠ L402)
- binding magnesium ion: D439 (= D432), N466 (= N459), Q468 (≠ S461)
- 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 (≠ S381), M414 (= M407), G438 (= G431), G440 (= G433), N466 (= N459), Q468 (≠ S461), Y469 (≠ L462), G470 (≠ N463), W471 (≠ F464), I472 (≠ V465)
Sites not aligning to the query:
2ez4B Pyruvate oxidase variant f479w (see paper)
29% identity, 90% coverage: 9:523/572 of query aligns to 9:533/585 of 2ez4B
- active site: I24 (= I24), G26 (= G26), G27 (≠ D27), S28 (≠ T28), I29 (≠ L29), E51 (= E49), S74 (= S72), F113 (≠ P111), Q114 (= Q112), E115 (= E113), V162 (≠ S160), R256 (≠ I251), E283 (≠ Q278), V386 (≠ C379), A412 (≠ G405), M414 (= M407), D439 (= D432), N466 (= N459), Q468 (≠ S461), Y469 (≠ L462), W471 (≠ F464), I472 (≠ V465), E475 (= E468)
- binding flavin-adenine dinucleotide: H93 (≠ K91), G212 (= G207), I213 (≠ A208), G214 (= G209), T236 (= T231), Y237 (≠ S232), P238 (≠ R233), A254 (≠ T249), N255 (≠ G250), R256 (≠ I251), V257 (≠ F252), G276 (= G271), N277 (≠ A272), N278 (≠ D273), P280 (≠ A275), F281 (≠ W276), D298 (= D290), I299 (≠ H291), K303 (≠ H295), D317 (= D309), A318 (≠ I310), N409 (≠ L402)
- binding magnesium ion: D439 (= D432), N466 (= N459), Q468 (≠ S461)
- binding phosphate ion: W471 (≠ F464), E475 (= E468)
- binding thiamine diphosphate: D388 (≠ S381), A412 (≠ G405), M414 (= M407), G438 (= G431), D439 (= D432), G440 (= G433), G441 (= G434), N466 (= N459), Q468 (≠ S461), Y469 (≠ L462), G470 (≠ N463), W471 (≠ F464), I472 (≠ V465)
Sites not aligning to the query:
1y9dD Pyruvate oxidase variant v265a from lactobacillus plantarum (see paper)
29% identity, 90% coverage: 9:523/572 of query aligns to 9:508/560 of 1y9dD
- active site: I24 (= I24), G26 (= G26), G27 (≠ D27), S28 (≠ T28), I29 (≠ L29), E51 (= E49), S74 (= S72), E108 (= E113), V155 (≠ S160), R241 (≠ I251), V361 (≠ C379), A387 (≠ G405), M389 (= M407), D414 (= D432), N441 (= N459), Q443 (≠ S461), Y444 (≠ L462), F446 (= F464), I447 (≠ V465), E450 (= E468)
- binding flavin-adenine dinucleotide: I198 (≠ A208), G199 (= G209), T221 (= T231), P223 (≠ R233), G261 (= G271), N262 (≠ A272), N263 (≠ D273), D273 (= D290), I274 (≠ H291), K278 (≠ H295), D292 (= D309), A293 (≠ I310)
- binding magnesium ion: D414 (= D432), N441 (= N459), Q443 (≠ S461)
- binding thiamine diphosphate: E51 (= E49), S74 (= S72), P77 (= P75), H81 (= H79), D363 (≠ S381), M389 (= M407), G413 (= G431), G415 (= G433), N441 (= N459), Q443 (≠ S461), Y444 (≠ L462), G445 (≠ N463), F446 (= F464), I447 (≠ V465)
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)
28% identity, 93% coverage: 3:534/572 of query aligns to 91:643/664 of P09114
- P191 (≠ V102) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
- W568 (≠ L467) mutation to L: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191.
P09342 Acetolactate synthase 1, chloroplastic; ALS I; Acetohydroxy-acid synthase I; Acetolactate synthase I; EC 2.2.1.6 from Nicotiana tabacum (Common tobacco) (see 2 papers)
28% identity, 93% coverage: 3:534/572 of query aligns to 94:646/667 of P09342
- C161 (= C69) modified: Disulfide link with 307
- P194 (≠ V102) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (= C210) modified: Disulfide link with 161
7tzzA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase p197t mutant in complex with bispyribac-sodium (see paper)
27% identity, 93% coverage: 3:534/572 of query aligns to 12:564/582 of 7tzzA
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: M266 (≠ I251), R292 (vs. gap), W489 (≠ L467)
- 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 (≠ C379), G401 (= G380), Q402 (≠ S381), H403 (≠ P382), G426 (= G405), M428 (= M407), G452 (= G431), D453 (= D432), G454 (= G433), S455 (≠ G434), L483 (= L462), G484 (≠ N463), M485 (≠ F464), V486 (= V465)
- binding flavin-adenine dinucleotide: R161 (= R150), G222 (= G207), G223 (≠ A208), G224 (= G209), T246 (= T231), L247 (≠ S232), M248 (≠ R233), M263 (= M248), L264 (≠ T249), M266 (≠ I251), H267 (≠ F252), G286 (= G271), R288 (≠ D273), V293 (vs. gap), D310 (= D290), I311 (≠ H291), D329 (= D309), V330 (≠ I310), M405 (≠ V384), G423 (≠ L402)
- binding magnesium ion: A37 (≠ T28), T82 (≠ S72), S83 (≠ C73), Q122 (= Q112), Y381 (= Y360), D453 (= D432), M458 (= M437), Q461 (≠ G440), N480 (= N459), H482 (≠ S461), K533 (≠ S503)
Sites not aligning to the query:
6desA Crystal structure of candida albicans acetohydroxyacid synthase in complex with the herbicide propoxycarbazone (see paper)
27% identity, 94% coverage: 7:543/572 of query aligns to 16:572/598 of 6desA
- active site: Y33 (≠ I24), G35 (= G26), G36 (≠ D27), A37 (≠ T28), I38 (≠ L29), E59 (= E49), T82 (≠ S72), F121 (≠ P111), Q122 (= Q112), E123 (= E113), K171 (≠ S160), K229 (≠ L217), M265 (≠ I251), V292 (vs. gap), V408 (≠ C379), L433 (≠ H404), G434 (= G405), M436 (= M407), D461 (= D432), N488 (= N459), E490 (≠ S461), Q491 (≠ L462), M493 (≠ F464), V494 (= V465), W497 (≠ E468), L519 (= L489), N524 (≠ G494), V525 (≠ F495)
- binding methyl 2-[(4-methyl-5-oxidanylidene-3-propoxy-1,2,4-triazol-1-yl)carbonylsulfamoyl]benzoate: M265 (≠ I251), D290 (vs. gap), R291 (vs. gap), W497 (≠ E468)
- binding flavin-adenine dinucleotide: R161 (= R150), G218 (= G207), A219 (= A208), G220 (= G209), N223 (≠ Q211), T245 (= T231), L246 (≠ S232), Q247 (≠ R233), L263 (≠ T249), G285 (= G271), A286 (= A272), R287 (≠ D273), D289 (vs. gap), R291 (vs. gap), V292 (vs. gap), E318 (≠ D290), I319 (≠ H291), N323 (≠ H295), D337 (= D309), V338 (≠ I310), Q412 (≠ M383), M413 (≠ V384), G431 (≠ L402)
- binding magnesium ion: D461 (= D432), N488 (= N459), E490 (≠ S461)
- 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 (≠ C379), G409 (= G380), Q410 (≠ S381), H411 (≠ P382), G434 (= G405), M436 (= M407), G460 (= G431), D461 (= D432), A462 (≠ G433), S463 (≠ G434), N488 (= N459), E490 (≠ S461), Q491 (≠ L462), G492 (≠ N463), M493 (≠ F464), V494 (= V465)
6depA Crystal structure of candida albicans acetohydroxyacid synthase in complex with the herbicide sulfometuron methyl (see paper)
27% identity, 94% coverage: 7:543/572 of query aligns to 16:572/598 of 6depA
- active site: Y33 (≠ I24), G35 (= G26), G36 (≠ D27), A37 (≠ T28), I38 (≠ L29), E59 (= E49), T82 (≠ S72), F121 (≠ P111), Q122 (= Q112), E123 (= E113), K171 (≠ S160), K229 (≠ L217), M265 (≠ I251), V292 (vs. gap), V408 (≠ C379), L433 (≠ H404), G434 (= G405), M436 (= M407), D461 (= D432), N488 (= N459), E490 (≠ S461), Q491 (≠ L462), M493 (≠ F464), V494 (= V465), W497 (≠ E468), L519 (= L489), N524 (≠ G494), V525 (≠ F495)
- binding methyl 2-[({[(4,6-dimethylpyrimidin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: D290 (vs. gap), R291 (vs. gap), M493 (≠ F464), W497 (≠ E468)
- binding flavin-adenine dinucleotide: R161 (= R150), G218 (= G207), A219 (= A208), G220 (= G209), N223 (≠ Q211), T245 (= T231), L246 (≠ S232), Q247 (≠ R233), L263 (≠ T249), G264 (= G250), G285 (= G271), A286 (= A272), R287 (≠ D273), D289 (vs. gap), R291 (vs. gap), V292 (vs. gap), E318 (≠ D290), I319 (≠ H291), N323 (≠ H295), D337 (= D309), V338 (≠ I310), M413 (≠ V384), G431 (≠ L402)
- binding magnesium ion: D461 (= D432), N488 (= N459), E490 (≠ S461)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V408 (≠ C379), G409 (= G380), Q410 (≠ S381), H411 (≠ P382), G434 (= G405), M436 (= M407), G460 (= G431), D461 (= D432), A462 (≠ G433), S463 (≠ G434), M466 (= M437), N488 (= N459), E490 (≠ S461), Q491 (≠ L462), G492 (≠ N463), M493 (≠ F464), V494 (= V465)
- 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 (≠ C379), G409 (= G380), Q410 (≠ S381), H411 (≠ P382), G434 (= G405), M436 (= M407), G460 (= G431), D461 (= D432), A462 (≠ G433), S463 (≠ G434), M466 (= M437), N488 (= N459), E490 (≠ S461), Q491 (≠ L462), G492 (≠ N463), M493 (≠ F464), V494 (= V465)
6derA Crystal structure of candida albicans acetohydroxyacid synthase in complex with the herbicide metosulam (see paper)
27% identity, 94% coverage: 7:543/572 of query aligns to 18:574/600 of 6derA
- active site: Y35 (≠ I24), G37 (= G26), G38 (≠ D27), A39 (≠ T28), I40 (≠ L29), E61 (= E49), T84 (≠ S72), F123 (≠ P111), Q124 (= Q112), E125 (= E113), K173 (≠ S160), K231 (≠ L217), M267 (≠ I251), V294 (vs. gap), V410 (≠ C379), L435 (≠ H404), G436 (= G405), M438 (= M407), D463 (= D432), N490 (= N459), E492 (≠ S461), Q493 (≠ L462), M495 (≠ F464), V496 (= V465), W499 (≠ E468), L521 (= L489), N526 (≠ G494), V527 (≠ F495)
- binding flavin-adenine dinucleotide: R163 (= R150), G220 (= G207), A221 (= A208), G222 (= G209), N225 (≠ Q211), T247 (= T231), L248 (≠ S232), Q249 (≠ R233), L265 (≠ T249), H268 (≠ F252), G287 (= G271), A288 (= A272), R289 (≠ D273), D291 (vs. gap), R293 (vs. gap), V294 (vs. gap), E320 (≠ D290), I321 (≠ H291), N325 (≠ H295), G338 (= G308), D339 (= D309), V340 (≠ I310), Q414 (≠ M383), M415 (≠ V384), G433 (≠ L402)
- binding Metosulam: R293 (vs. gap), M495 (≠ F464), W499 (≠ E468), A570 (= A539)
- binding magnesium ion: D463 (= D432), N490 (= N459), E492 (≠ S461)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V410 (≠ C379), G411 (= G380), Q412 (≠ S381), H413 (≠ P382), G436 (= G405), M438 (= M407), G462 (= G431), D463 (= D432), A464 (≠ G433), S465 (≠ G434), N490 (= N459), E492 (≠ S461), Q493 (≠ L462), G494 (≠ N463), M495 (≠ F464), V496 (= V465)
- 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 (≠ C379), G411 (= G380), Q412 (≠ S381), H413 (≠ P382), G436 (= G405), M438 (= M407), G462 (= G431), D463 (= D432), A464 (≠ G433), S465 (≠ G434), M468 (= M437), N490 (= N459), E492 (≠ S461), Q493 (≠ L462), G494 (≠ N463), V496 (= V465)
5k3sA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a pyrimidinyl-benzoate herbicide, bispyribac-sodium (see paper)
27% identity, 93% coverage: 3:534/572 of query aligns to 12:564/583 of 5k3sA
- active site: Y33 (≠ I24), G35 (= G26), G36 (≠ D27), A37 (≠ T28), S38 (≠ L29), E59 (= E49), T82 (≠ S72), F121 (≠ P111), Q122 (= Q112), E123 (= E113), K171 (≠ S160), M266 (≠ I251), V293 (vs. gap), V400 (≠ C379), G426 (= G405), M428 (= M407), D453 (= D432), N480 (= N459), H482 (≠ S461), L483 (= L462), M485 (≠ F464), V486 (= V465), W489 (≠ L467), H558 (≠ P528)
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: R292 (vs. gap), M485 (≠ F464), W489 (≠ L467)
- binding flavin-adenine dinucleotide: R161 (= R150), G222 (= G207), G223 (≠ A208), G224 (= G209), T246 (= T231), L247 (≠ S232), M248 (≠ R233), L264 (≠ T249), M266 (≠ I251), G286 (= G271), R288 (≠ D273), D290 (vs. gap), V293 (vs. gap), D310 (= D290), I311 (≠ H291), D329 (= D309), V330 (≠ I310), M405 (≠ V384), G423 (≠ L402)
- binding magnesium ion: D453 (= D432), N480 (= N459), H482 (≠ S461)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (≠ C379), G401 (= G380), Q402 (≠ S381), H403 (≠ P382), G426 (= G405), M428 (= M407), D453 (= D432), G454 (= G433), S455 (≠ G434), N480 (= N459), H482 (≠ S461), L483 (= L462), G484 (≠ N463), M485 (≠ F464), V486 (= V465)
Sites not aligning to the query:
5k2oA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a pyrimidinyl-benzoate herbicide, pyrithiobac (see paper)
27% identity, 93% coverage: 3:534/572 of query aligns to 12:564/585 of 5k2oA
- active site: Y33 (≠ I24), G35 (= G26), G36 (≠ D27), A37 (≠ T28), S38 (≠ L29), E59 (= E49), T82 (≠ S72), F121 (≠ P111), Q122 (= Q112), E123 (= E113), K171 (≠ S160), M266 (≠ I251), V293 (vs. gap), V400 (≠ C379), G426 (= G405), M428 (= M407), D453 (= D432), N480 (= N459), H482 (≠ S461), L483 (= L462), M485 (≠ F464), V486 (= V465), W489 (≠ L467), H558 (≠ P528)
- binding 2-chloranyl-6-(4,6-dimethoxypyrimidin-2-yl)sulfanyl-benzoic acid: M266 (≠ I251), R292 (vs. gap), W489 (≠ L467)
- binding flavin-adenine dinucleotide: R161 (= R150), G222 (= G207), G223 (≠ A208), G224 (= G209), T246 (= T231), L247 (≠ S232), M248 (≠ R233), L264 (≠ T249), G286 (= G271), R288 (≠ D273), D290 (vs. gap), V293 (vs. gap), D310 (= D290), I311 (≠ H291), D329 (= D309), V330 (≠ I310), Q404 (≠ M383), M405 (≠ V384), G423 (≠ L402)
- binding magnesium ion: D453 (= D432), N480 (= N459), H482 (≠ S461)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (≠ C379), G401 (= G380), Q402 (≠ S381), H403 (≠ P382), M428 (= M407), D453 (= D432), G454 (= G433), S455 (≠ G434), N480 (= N459), H482 (≠ S461), L483 (= L462), G484 (≠ N463), M485 (≠ F464), V486 (= V465)
Sites not aligning to the query:
Query Sequence
>WP_057506889.1 NCBI__GCF_001431535.1:WP_057506889.1
MSKRVADIVVETLQQAGVRRCYGIVGDTLNHVTTAIHGSDIDWVHVRHEEVAAFAAGADS
LISGQLTACAGSCGPGSLHFINGVFENNRNKAPMVLIASQVVTSELGMEFPQEVDFKAVY
SSCSVFCEQVYSAEQARRVVTLACQAAISRRGVAVVILPSDISEQVVKHDPPFAVHYTQP
VLRPGDDELLRIAELLGQGKRIGIYAGAGCQGAHAPLLELARRLQAPIAHTSRAKDFVEP
DNPFNMGMTGIFGIESGFHAVMECDTLLLLGADFAWGQYYPDKATIIQVDHDGSHLGRRH
PVTLGVVGDIGPTLEALLPMLPPREDTDFLDECIGHREKALAKRAEEEAPGEGELIHPQY
LTALLDQHAADDALFTADCGSPMVWVLRHIRVNGRRRTLTSLLHGTMANAMPQALGLQKA
FPGRQVVALCGDGGLSMLMGDLLTAVQENLPIKIVVYNNGSLNFVELEQKVEGLLDYYTE
LKNPDFGKLAEVIGFHGRTVTRSQDLALAVQDLLAQPGPALLDVHTAPTELVMPPQVEAG
QVIGTARYMAKAVLAGRIGEVKELLADNFLKR
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