SitesBLAST
Comparing WP_019557431.1 NCBI__GCF_000381085.1:WP_019557431.1 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)
1ozgA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate (see paper)
34% identity, 95% coverage: 4:537/560 of query aligns to 9:547/549 of 1ozgA
- active site: I27 (= I22), G29 (= G24), A30 (≠ E25), K31 (≠ E26), I32 (≠ N27), E52 (= E47), T75 (= T70), H114 (≠ F109), Q115 (= Q110), S116 (≠ I111), Q164 (≠ E159), L257 (= L250), E284 (≠ P277), M389 (≠ N379), Q415 (≠ A405), M417 (= M407), D442 (= D432), D469 (= D459), G471 (≠ A461), Y472 (≠ F462), M474 (= M464), V475 (≠ I465), Q478 (≠ K468), Y538 (= Y528)
- binding 2-hydroxyethyl dihydrothiachrome diphosphate: M389 (≠ N379), G390 (= G380), S391 (≠ V381), F392 (≠ Y382), Q415 (≠ A405), M417 (= M407), G441 (= G431), D442 (= D432), G443 (= G433), D469 (= D459), G471 (≠ A461), Y472 (≠ F462), N473 (≠ G463), M474 (= M464), V475 (≠ I465), Y538 (= Y528)
- binding magnesium ion: D442 (= D432), D469 (= D459), G471 (≠ A461)
- binding phosphate ion: G253 (= G246), R254 (≠ C247), Q261 (≠ D254), R347 (= R343), R398 (= R388), Y401 (≠ L391)
5d6rB Acetolactate synthase from klebsiella pneumoniae in complex with mechanism-based inhibitor
34% identity, 95% coverage: 4:537/560 of query aligns to 8:544/548 of 5d6rB
- active site: I26 (= I22), G28 (= G24), A29 (≠ E25), K30 (≠ E26), I31 (≠ N27), E51 (= E47), T74 (= T70), H113 (≠ F109), Q114 (= Q110), S115 (≠ I111), Q163 (≠ E159), L254 (= L250), E281 (≠ P277), M386 (≠ N379), Q412 (≠ A405), M414 (= M407), D439 (= D432), D466 (= D459), G468 (≠ A461), Y469 (≠ F462), M471 (= M464), V472 (≠ I465), Q475 (≠ K468), Y535 (= Y528)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-[(Z)-2-fluoro-1-hydroxy-2-phosphonoethenyl]-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: M386 (≠ N379), G387 (= G380), S388 (≠ V381), Q412 (≠ A405), M414 (= M407), D439 (= D432), G440 (= G433), G468 (≠ A461), Y469 (≠ F462), N470 (≠ G463), M471 (= M464), Y535 (= Y528)
- binding magnesium ion: R63 (= R59), Q212 (≠ R209), D439 (= D432), D466 (= D459), G468 (≠ A461)
1ozfA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors (see paper)
34% identity, 95% coverage: 4:537/560 of query aligns to 8:543/545 of 1ozfA
- active site: I26 (= I22), G28 (= G24), A29 (≠ E25), K30 (≠ E26), I31 (≠ N27), E51 (= E47), T74 (= T70), H113 (≠ F109), Q114 (= Q110), S115 (≠ I111), Q163 (≠ E159), L253 (= L250), E280 (≠ P277), M385 (≠ N379), Q411 (≠ A405), M413 (= M407), D438 (= D432), D465 (= D459), G467 (≠ A461), Y468 (≠ F462), M470 (= M464), V471 (≠ I465), Q474 (≠ K468), Y534 (= Y528)
- binding magnesium ion: D438 (= D432), D465 (= D459), G467 (≠ A461)
- binding phosphate ion: G249 (= G246), R250 (≠ C247), Q257 (≠ D254), R343 (= R343), R394 (= R388), L396 (≠ F390), Y397 (≠ L391)
- binding thiamine diphosphate: G386 (= G380), S387 (≠ V381), F388 (≠ Y382), Q411 (≠ A405), M413 (= M407), G437 (= G431), D438 (= D432), G439 (= G433), D465 (= D459), G467 (≠ A461), Y468 (≠ F462), N469 (≠ G463), M470 (= M464), V471 (≠ I465), Y534 (= Y528)
5dx6B Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
34% identity, 95% coverage: 4:537/560 of query aligns to 20:550/557 of 5dx6B
- active site: I38 (= I22), G40 (= G24), A41 (≠ E25), K42 (≠ E26), I43 (≠ N27), E63 (= E47), T86 (= T70), H125 (≠ F109), Q126 (= Q110), S127 (≠ I111), Q175 (≠ E159), L268 (= L250), E295 (≠ P277), M392 (≠ N379), Q418 (≠ A405), M420 (= M407), D445 (= D432), D472 (= D459), G474 (≠ A461), Y475 (≠ F462), M477 (= M464), V478 (≠ I465), Q481 (≠ K468), Y541 (= Y528)
- binding 3-fluoro-2-oxopropanoic acid: G264 (= G246), R265 (≠ C247), Q272 (≠ D254), A400 (= A387), R401 (= R388), Y404 (≠ L391)
- binding magnesium ion: S135 (≠ H119), T138 (= T122), D445 (= D432), D472 (= D459), G474 (≠ A461)
- binding thiamine diphosphate: G393 (= G380), S394 (≠ V381), F395 (≠ Y382), Q418 (≠ A405), M420 (= M407), G444 (= G431), D445 (= D432), G446 (= G433), D472 (= D459), G474 (≠ A461), Y475 (≠ F462), N476 (≠ G463), M477 (= M464), V478 (≠ I465), Y541 (= Y528)
5dx6A Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
34% identity, 95% coverage: 4:537/560 of query aligns to 9:539/541 of 5dx6A
- active site: I27 (= I22), G29 (= G24), A30 (≠ E25), K31 (≠ E26), I32 (≠ N27), E52 (= E47), T75 (= T70), Q159 (≠ E159), L249 (= L250), E276 (≠ P277), M381 (≠ N379), Q407 (≠ A405), M409 (= M407), D434 (= D432), D461 (= D459), G463 (≠ A461), Y464 (≠ F462), M466 (= M464), V467 (≠ I465), Q470 (≠ K468), Y530 (= Y528)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-[(1R)-2-fluoro-1-hydroxyethyl]-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: M381 (≠ N379), G382 (= G380), S383 (≠ V381), F384 (≠ Y382), Q407 (≠ A405), M409 (= M407), G433 (= G431), D434 (= D432), G435 (= G433), D461 (= D459), G463 (≠ A461), Y464 (≠ F462), N465 (≠ G463), Y530 (= Y528)
- binding magnesium ion: S119 (≠ H119), T122 (= T122), D434 (= D432), D461 (= D459), G463 (≠ A461)
5wdgA Acetolactate synthase from klebsiella pneumoniae in complex with a reaction intermediate
34% identity, 95% coverage: 4:537/560 of query aligns to 9:536/538 of 5wdgA
- active site: I27 (= I22), G29 (= G24), A30 (≠ E25), K31 (≠ E26), I32 (≠ N27), E52 (= E47), T75 (= T70), Q157 (≠ E159), L246 (= L250), E273 (≠ P277), M378 (≠ N379), Q404 (≠ A405), M406 (= M407), D431 (= D432), D458 (= D459), G460 (≠ A461), Y461 (≠ F462), M463 (= M464), V464 (≠ I465), Q467 (≠ K468), Y527 (= Y528)
- binding (2S,3S)-2,3-dihydroxy-3-[(7S,8R,9aS)-8-(2-{[(R)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-2,7-dimethyl-5,7,8,10-tetrahydro-9aH-pyrimido[4,5-d][1,3]thiazolo[3,2-a]pyrimidin-9a-yl]-2-methylbutanoic acid: M378 (≠ N379), S380 (≠ V381), F381 (≠ Y382), Q404 (≠ A405), M406 (= M407), G430 (= G431), D431 (= D432), G432 (= G433), G433 (= G434), D458 (= D459), G460 (≠ A461), Y461 (≠ F462), N462 (≠ G463), M463 (= M464), V464 (≠ I465), Y527 (= Y528)
- binding magnesium ion: R64 (= R59), S117 (≠ H119), T120 (= T122), Q204 (≠ R209), D431 (= D432), D458 (= D459), G460 (≠ A461)
- binding pyruvic acid: G94 (≠ A89), R147 (= R149)
4rjkF Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
33% identity, 95% coverage: 2:531/560 of query aligns to 2:536/552 of 4rjkF
- binding magnesium ion: D437 (= D432), D464 (= D459), T466 (≠ A461)
- binding pyruvic acid: A25 (≠ E25), K26 (≠ E26)
- binding thiamine diphosphate: P23 (= P23), E47 (= E47), P73 (= P73), G385 (= G380), S386 (≠ V381), H387 (≠ Y382), Q410 (≠ A405), L412 (≠ M407), G436 (= G431), D437 (= D432), G438 (= G433), G439 (= G434), T466 (≠ A461), Y467 (≠ F462), D468 (≠ G463), M469 (= M464), V470 (≠ I465), Y533 (= Y528)
4rjkG Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
33% identity, 95% coverage: 2:531/560 of query aligns to 2:536/553 of 4rjkG
- binding magnesium ion: D437 (= D432), D464 (= D459), T466 (≠ A461)
- 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: E47 (= E47), Q110 (= Q110)
- binding thiamine diphosphate: I384 (≠ N379), G385 (= G380), S386 (≠ V381), H387 (≠ Y382), Q410 (≠ A405), L412 (≠ M407), G436 (= G431), D437 (= D432), G438 (= G433), G439 (= G434), T466 (≠ A461), Y467 (≠ F462), D468 (≠ G463), M469 (= M464), V470 (≠ I465), Y533 (= Y528)
4rjiC Acetolactate synthase from bacillus subtilis bound to thdp - crystal form i (see paper)
33% identity, 95% coverage: 2:531/560 of query aligns to 3:537/555 of 4rjiC
- binding magnesium ion: D438 (= D432), D465 (= D459), T467 (≠ A461)
- binding thiamine diphosphate: P24 (= P23), E48 (= E47), P74 (= P73), S387 (≠ V381), H388 (≠ Y382), Q411 (≠ A405), G437 (= G431), D438 (= D432), G439 (= G433), G440 (= G434), T467 (≠ A461), Y468 (≠ F462), D469 (≠ G463), M470 (= M464), V471 (≠ I465), Y534 (= Y528)
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, 95% coverage: 2:531/560 of query aligns to 92:640/664 of P09114
- P191 (= P100) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
- W568 (vs. gap) mutation to L: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191.
6lpiB Crystal structure of ahas holo-enzyme (see paper)
28% identity, 94% coverage: 4:531/560 of query aligns to 9:524/539 of 6lpiB
- active site: I27 (= I22), G29 (= G24), G30 (≠ E25), S31 (≠ E26), I32 (≠ N27), E53 (= E47), C76 (≠ T70), F115 (= F109), Q116 (= Q110), E117 (≠ I111), K165 (≠ E159), M256 (≠ L250), A283 (≠ F279), V375 (≠ N379), G401 (≠ A405), M403 (= M407), D428 (= D432), N455 (≠ D459), A457 (= A461), L458 (≠ F462), L460 (≠ M464), V461 (≠ I465), Q464 (= Q469)
- binding flavin-adenine dinucleotide: R155 (= R149), G212 (= G204), G213 (≠ A205), G214 (≠ A206), T236 (= T230), L237 (≠ Q231), M238 (= M232), L254 (≠ A248), M256 (≠ L250), H257 (≠ S251), G276 (= G270), A277 (≠ H271), R278 (≠ D272), D280 (≠ V274), R282 (≠ K276), A283 (≠ F279), D300 (≠ N292), I301 (≠ F293), D319 (= D311), V320 (≠ I312), M380 (≠ I384), G398 (≠ N402)
- binding magnesium ion: D428 (= D432), N455 (≠ D459)
- binding thiamine diphosphate: E53 (= E47), C76 (≠ T70), P79 (= P73), G376 (= G380), Q377 (≠ V381), H378 (≠ Y382), G401 (≠ A405), M403 (= M407), G427 (= G431), D428 (= D432), G429 (= G433), S430 (≠ G434), M433 (= M437), N455 (≠ D459), A457 (= A461), L458 (≠ F462), G459 (= G463), L460 (≠ M464), V461 (≠ I465)
1t9cA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, sulfometuron methyl (see paper)
28% identity, 94% coverage: 1:527/560 of query aligns to 8:555/596 of 1t9cA
- active site: Y29 (≠ I22), G31 (= G24), G32 (≠ E25), A33 (≠ E26), I34 (≠ N27), E55 (= E47), T78 (= T70), F117 (= F109), Q118 (= Q110), E119 (≠ I111), K167 (≠ E159), R227 (≠ K214), M263 (≠ L250), V290 (≠ P277), V406 (≠ N379), L431 (= L404), G432 (≠ A405), M434 (= M407), D459 (= D432), N486 (≠ D459), E488 (≠ A461), Q489 (≠ F462), M491 (= M464), V492 (≠ I465), W495 (= W467), L517 (≠ Y489), G522 (= G494), L523 (≠ A495)
- binding methyl 2-[({[(4,6-dimethylpyrimidin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (≠ E25), V107 (≠ K99), P108 (= P100), F117 (= F109), K167 (≠ E159), D288 (≠ E275), R289 (≠ K276), W495 (= W467)
- binding flavin-adenine dinucleotide: R157 (= R149), G216 (= G204), A217 (= A205), G218 (≠ A206), N221 (= N208), T243 (= T230), L244 (≠ Q231), Q245 (≠ M232), L261 (≠ A248), M263 (≠ L250), H264 (≠ S251), G283 (= G270), A284 (≠ H271), R285 (≠ D272), D287 (≠ V274), R289 (≠ K276), V290 (≠ P277), E316 (≠ N292), V317 (≠ F293), N321 (≠ S297), G334 (= G310), D335 (= D311), A336 (≠ I312), M411 (≠ I384), G429 (≠ N402), G430 (≠ A403)
- binding magnesium ion: D459 (= D432), N486 (≠ D459), E488 (≠ A461)
Sites not aligning to the query:
1t9dA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
28% identity, 94% coverage: 1:527/560 of query aligns to 8:555/596 of 1t9dA
- active site: Y29 (≠ I22), G31 (= G24), G32 (≠ E25), A33 (≠ E26), I34 (≠ N27), E55 (= E47), T78 (= T70), F117 (= F109), Q118 (= Q110), E119 (≠ I111), K167 (≠ E159), R227 (≠ K214), M263 (≠ L250), V290 (≠ P277), V406 (≠ N379), L431 (= L404), G432 (≠ A405), M434 (= M407), D459 (= D432), N486 (≠ D459), E488 (≠ A461), Q489 (≠ F462), M491 (= M464), V492 (≠ I465), W495 (= W467), L517 (≠ Y489), G522 (= G494), L523 (≠ A495)
- binding methyl 2-[({[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (≠ E25), A33 (≠ E26), V107 (≠ K99), P108 (= P100), F117 (= F109), K167 (≠ E159), M263 (≠ L250), D288 (≠ E275), R289 (≠ K276), W495 (= W467)
- binding flavin-adenine dinucleotide: R157 (= R149), G216 (= G204), A217 (= A205), G218 (≠ A206), N221 (= N208), T243 (= T230), L244 (≠ Q231), Q245 (≠ M232), M260 (≠ C247), L261 (≠ A248), H264 (≠ S251), G283 (= G270), A284 (≠ H271), R285 (≠ D272), D287 (≠ V274), R289 (≠ K276), V290 (≠ P277), E316 (≠ N292), V317 (≠ F293), N321 (≠ S297), G334 (= G310), D335 (= D311), A336 (≠ I312), Q410 (≠ K383), M411 (≠ I384), G429 (≠ N402), G430 (≠ A403)
- binding magnesium ion: D459 (= D432), N486 (≠ D459), E488 (≠ A461)
- binding 2,5-dimethyl-pyrimidin-4-ylamine: E55 (= E47), P81 (= P73), Q118 (= Q110), G432 (≠ A405), M434 (= M407), M464 (= M437)
Sites not aligning to the query:
1t9aA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, tribenuron methyl (see paper)
28% identity, 94% coverage: 1:527/560 of query aligns to 9:556/597 of 1t9aA
- active site: Y30 (≠ I22), G32 (= G24), G33 (≠ E25), A34 (≠ E26), I35 (≠ N27), E56 (= E47), T79 (= T70), F118 (= F109), Q119 (= Q110), E120 (≠ I111), K168 (≠ E159), R228 (≠ K214), M264 (≠ L250), V291 (vs. gap), V407 (≠ N379), L432 (= L404), G433 (≠ A405), M435 (= M407), D460 (= D432), N487 (≠ D459), E489 (≠ A461), Q490 (≠ F462), M492 (= M464), V493 (≠ I465), W496 (= W467), L518 (≠ Y489), G523 (= G494), L524 (≠ A495)
- binding methyl 2-[4-methoxy-6-methyl-1,3,5-trazin-2-yl(methyl)carbamoylsulfamoyl]benzoate: G33 (≠ E25), V108 (≠ K99), P109 (= P100), F118 (= F109), K168 (≠ E159), M264 (≠ L250), D289 (≠ E275), R290 (≠ K276), M492 (= M464), V493 (≠ I465), W496 (= W467)
- binding flavin-adenine dinucleotide: R158 (= R149), G217 (= G204), A218 (= A205), G219 (≠ A206), N222 (= N208), T244 (= T230), L245 (≠ Q231), Q246 (≠ M232), L262 (≠ A248), M264 (≠ L250), H265 (≠ S251), G284 (= G270), A285 (≠ H271), R286 (≠ D272), D288 (≠ V274), R290 (≠ K276), V291 (vs. gap), E317 (≠ N292), V318 (≠ F293), N322 (≠ S297), G335 (= G310), D336 (= D311), A337 (≠ I312), Q411 (≠ K383), M412 (≠ I384), G430 (≠ N402), G431 (≠ A403)
- binding magnesium ion: D460 (= D432), N487 (≠ D459), E489 (≠ A461)
- binding propyl trihydrogen diphosphate: V407 (≠ N379), G408 (= G380), Q409 (≠ V381), H410 (≠ Y382), M435 (= M407), G459 (= G431), D460 (= D432), A461 (≠ G433), S462 (≠ G434), N487 (≠ D459), E489 (≠ A461), Q490 (≠ F462), G491 (= G463), M492 (= M464)
- binding 5-{[ethyl(methyl)amino]methyl}-2-methyl-5,6-dihydropyrimidin-4-amine: G433 (≠ A405), M435 (= M407), M465 (= M437)
Sites not aligning to the query:
5wkcA Saccharomyces cerevisiae acetohydroxyacid synthase in complex with the herbicide penoxsulam (see paper)
28% identity, 94% coverage: 1:527/560 of query aligns to 8:550/591 of 5wkcA
- active site: Y29 (≠ I22), G31 (= G24), G32 (≠ E25), A33 (≠ E26), I34 (≠ N27), E55 (= E47), T78 (= T70), F117 (= F109), Q118 (= Q110), E119 (≠ I111), K167 (≠ E159), R222 (≠ K214), M258 (≠ L250), V285 (≠ P277), V401 (≠ N379), L426 (= L404), G427 (≠ A405), M429 (= M407), D454 (= D432), N481 (≠ D459), E483 (≠ A461), Q484 (≠ F462), M486 (= M464), V487 (≠ I465), W490 (= W467), L512 (≠ Y489), G517 (= G494), L518 (≠ A495)
- 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: V401 (≠ N379), G402 (= G380), Q403 (≠ V381), H404 (≠ Y382), G427 (≠ A405), M429 (= M407), G453 (= G431), D454 (= D432), A455 (≠ G433), S456 (≠ G434), M459 (= M437), N481 (≠ D459), E483 (≠ A461), Q484 (≠ F462), G485 (= G463), M486 (= M464), V487 (≠ I465)
- binding ethaneperoxoic acid: G32 (≠ E25), Q118 (= Q110)
- binding flavin-adenine dinucleotide: R157 (= R149), G211 (= G204), A212 (= A205), G213 (≠ A206), N216 (= N208), T238 (= T230), L239 (≠ Q231), Q240 (≠ M232), L256 (≠ A248), M258 (≠ L250), G278 (= G270), A279 (≠ H271), R280 (≠ D272), R284 (≠ K276), V285 (≠ P277), E311 (≠ N292), V312 (≠ F293), N316 (≠ S297), D330 (= D311), A331 (≠ I312), M406 (≠ I384), G424 (≠ N402)
- binding magnesium ion: D454 (= D432), N481 (≠ D459), E483 (≠ A461)
- binding 2-(2,2-difluoroethoxy)-N-(5,8-dimethoxy[1,2,4]triazolo[1,5-c]pyrimidin-2-yl)-6-(trifluoromethyl)benzenesulfonamide: G32 (≠ E25), A33 (≠ E26), V107 (≠ K99), F117 (= F109), K167 (≠ E159), M258 (≠ L250), R284 (≠ K276), M486 (= M464), W490 (= W467)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: P30 (= P23), E55 (= E47)
Sites not aligning to the query:
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, 95% coverage: 2:531/560 of query aligns to 95:643/667 of P09342
- C161 (= C67) modified: Disulfide link with 307
- P194 (= P100) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ A207) modified: Disulfide link with 161
7egvA Acetolactate synthase from trichoderma harzianum with inhibitor harzianic acid (see paper)
29% identity, 94% coverage: 3:527/560 of query aligns to 9:549/590 of 7egvA
- active site: Y28 (≠ I22), G30 (= G24), G31 (≠ E25), A32 (≠ E26), I33 (≠ N27), E54 (= E47), T77 (= T70), F116 (= F109), Q117 (= Q110), K166 (≠ E159), E220 (≠ K214), M256 (≠ L250), V283 (vs. gap), V400 (≠ N379), L425 (= L404), G426 (≠ A405), M428 (= M407), Q483 (≠ F462), M485 (= M464), V486 (≠ I465), W489 (= W467), L511 (≠ Y489), G516 (= G494), I517 (≠ A495)
- binding flavin-adenine dinucleotide: R156 (= R149), G209 (= G204), Q210 (≠ A205), G211 (≠ A206), T236 (= T230), L237 (≠ Q231), H238 (≠ M232), G276 (= G270), S277 (≠ H271), R278 (vs. gap), D280 (vs. gap), R282 (vs. gap), V283 (vs. gap), E309 (≠ N292), I310 (≠ F293), D328 (= D311), V329 (≠ I312), M405 (≠ I384), G423 (≠ N402), G424 (≠ A403)
- binding (2S)-3-methyl-2-[[(2S,4R)-1-methyl-4-[(2E,4E)-octa-2,4-dienoyl]-3,5-bis(oxidanylidene)pyrrolidin-2-yl]methyl]-2-oxidanyl-butanoic acid: F493 (≠ G473), Y494 (≠ F474)
- binding magnesium ion: D453 (= D432), N480 (≠ D459), E482 (≠ A461)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: P29 (= P23), E54 (= E47), Q117 (= Q110), V400 (≠ N379), G401 (= G380), Q402 (≠ V381), H403 (≠ Y382), G426 (≠ A405), M428 (= M407), D453 (= D432), A454 (≠ G433), S455 (≠ G434), E482 (≠ A461), Q483 (≠ F462), G484 (= G463), M485 (= M464), V486 (≠ I465)
3ea4A Arabidopsis thaliana acetohydroxyacid synthase in complex with monosulfuron-ester (see paper)
29% identity, 93% coverage: 2:524/560 of query aligns to 12:553/582 of 3ea4A
- active site: Y32 (≠ I22), G34 (= G24), G35 (≠ E25), A36 (≠ E26), S37 (≠ N27), E58 (= E47), T81 (= T70), F120 (= F109), Q121 (= Q110), E122 (≠ I111), K170 (≠ E159), M265 (≠ L250), V292 (= V273), V399 (≠ N379), G425 (≠ A405), M427 (= M407), D452 (= D432), N479 (≠ D459), H481 (≠ A461), L482 (≠ F462), M484 (= M464), V485 (≠ I465), W488 (vs. gap)
- binding methyl 2-{[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl}benzoate: D290 (≠ H271), R291 (≠ D272), W488 (vs. gap)
- binding flavin-adenine dinucleotide-n5-isobutyl ketone: R160 (= R149), G221 (= G204), G222 (≠ A205), G223 (≠ A206), T245 (= T230), L246 (≠ Q231), M247 (= M232), L263 (≠ A248), G264 (≠ A249), M265 (≠ L250), H266 (≠ S251), G285 (= G270), R287 (vs. gap), D289 (vs. gap), R291 (≠ D272), D309 (≠ N292), I310 (≠ F293), G327 (= G310), D328 (= D311), V329 (≠ I312), M404 (≠ I384), G422 (≠ N402)
- binding magnesium ion: D452 (= D432), N479 (≠ D459), H481 (≠ A461)
- 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: V399 (≠ N379), G400 (= G380), Q401 (≠ V381), H402 (≠ Y382), M427 (= M407), G451 (= G431), D452 (= D432), G453 (= G433), S454 (≠ G434), N479 (≠ D459), H481 (≠ A461), L482 (≠ F462), G483 (= G463), M484 (= M464), V485 (≠ I465)
Sites not aligning to the query:
3e9yA Arabidopsis thaliana acetohydroxyacid synthase in complex with monosulfuron (see paper)
29% identity, 93% coverage: 2:524/560 of query aligns to 12:553/582 of 3e9yA
- active site: Y32 (≠ I22), G34 (= G24), G35 (≠ E25), A36 (≠ E26), S37 (≠ N27), E58 (= E47), T81 (= T70), F120 (= F109), Q121 (= Q110), E122 (≠ I111), K170 (≠ E159), M265 (≠ L250), V292 (= V273), V399 (≠ N379), G425 (≠ A405), M427 (= M407), D452 (= D432), N479 (≠ D459), H481 (≠ A461), L482 (≠ F462), M484 (= M464), V485 (≠ I465), W488 (vs. gap)
- binding N-[(4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide: D290 (≠ H271), R291 (≠ D272), W488 (vs. gap)
- binding flavin-adenine dinucleotide-n5-isobutyl ketone: R160 (= R149), G221 (= G204), G222 (≠ A205), G223 (≠ A206), T245 (= T230), L246 (≠ Q231), M247 (= M232), L263 (≠ A248), G285 (= G270), R287 (vs. gap), D289 (vs. gap), R291 (≠ D272), D309 (≠ N292), I310 (≠ F293), G327 (= G310), D328 (= D311), V329 (≠ I312), M404 (≠ I384), G422 (≠ N402)
- binding magnesium ion: D452 (= D432), N479 (≠ D459), H481 (≠ A461)
- 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: V399 (≠ N379), G400 (= G380), Q401 (≠ V381), H402 (≠ Y382), M427 (= M407), G451 (= G431), G453 (= G433), S454 (≠ G434), N479 (≠ D459), H481 (≠ A461), L482 (≠ F462), G483 (= G463), M484 (= M464), V485 (≠ I465)
Sites not aligning to the query:
1n0hA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorimuron ethyl (see paper)
28% identity, 94% coverage: 1:527/560 of query aligns to 10:558/599 of 1n0hA
- active site: Y31 (≠ I22), G33 (= G24), G34 (≠ E25), A35 (≠ E26), I36 (≠ N27), E57 (= E47), T80 (= T70), F119 (= F109), Q120 (= Q110), E121 (≠ I111), K169 (≠ E159), R230 (≠ K214), M266 (≠ L250), V293 (≠ P277), V409 (≠ N379), L434 (= L404), G435 (≠ A405), M437 (= M407), D462 (= D432), N489 (≠ D459), E491 (≠ A461), Q492 (≠ F462), M494 (= M464), V495 (≠ I465), W498 (= W467), L520 (≠ Y489), G525 (= G494), L526 (≠ A495)
- binding 4-{[(4'-amino-2'-methylpyrimidin-5'-yl)methyl]amino}pent-3-enyl diphosphate: V409 (≠ N379), G410 (= G380), Q411 (≠ V381), H412 (≠ Y382), G435 (≠ A405), M437 (= M407), G461 (= G431), D462 (= D432), A463 (≠ G433), S464 (≠ G434), M467 (= M437), N489 (≠ D459), E491 (≠ A461), Q492 (≠ F462), G493 (= G463), V495 (≠ I465)
- binding 2-[[[[(4-chloro-6-methoxy-2-pyrimidinyl)amino]carbonyl]amino]sulfonyl]benzoic acid ethyl ester: G34 (≠ E25), A35 (≠ E26), V109 (≠ K99), P110 (= P100), F119 (= F109), K169 (≠ E159), M266 (≠ L250), D291 (≠ E275), R292 (≠ K276), V495 (≠ I465), W498 (= W467)
- binding flavin-adenine dinucleotide: R159 (= R149), G219 (= G204), A220 (= A205), G221 (≠ A206), N224 (= N208), T246 (= T230), L247 (≠ Q231), Q248 (≠ M232), L264 (≠ A248), G265 (≠ A249), M266 (≠ L250), H267 (≠ S251), G286 (= G270), A287 (≠ H271), R288 (≠ D272), D290 (≠ V274), R292 (≠ K276), V293 (≠ P277), E319 (≠ N292), V320 (≠ F293), N324 (≠ S297), G337 (= G310), D338 (= D311), A339 (≠ I312), M414 (≠ I384), G432 (≠ N402), G433 (≠ A403)
- binding magnesium ion: D462 (= D432), N489 (≠ D459), E491 (≠ A461)
- binding thiamine diphosphate: Y31 (≠ I22), E57 (= E47), P83 (= P73)
Sites not aligning to the query:
Query Sequence
>WP_019557431.1 NCBI__GCF_000381085.1:WP_019557431.1
MKASDLFVKALEAEGVEYIFGIPGEENLDLLNSLKDSHIKLIVTRHEQAAGFMAATYGRL
TGHAGVCLSTLGPGATNLVTAAAYANLGAMPMVMITGQKPIKSSKQGQFQIIDVVDMMHP
ITKYACQITSGHNIPARIREAFRIAKTERPGAVHLELPEDIADEETNSQVIEQSAHRRPL
AEDKGVATAVKMIEDAKHPLILIGAAANRKTAGKMIRQLIDQTGIPFFTTQMGKGVVDER
HHLYLGCAALSDHDFVNAALKRADLIVNIGHDVVEKPPFFMKQDGFKVIHVNFTNASVDP
VYFPQADVVGDIANSVYQIKTKLQNQSHWKFGCFMEVKVHIDRNLAEGTQDNRFPVYPQR
LVSDIRKVVPETGVIALDNGVYKIWFARNFLAYHHNTVLLDNALATMGAGLPSAIAAKLV
TPEAKVMAICGDGGFMMNSQELETAVRLKLDLVVLILNDNAFGMIRWKQANMGFEDFGLK
LNNPDFVLYAQSYGAYGHRVSSADDVIPTVEKCYAQGGVHVIEVPIDYSDNDRILNHEIR
EQSDALNEILSKAEERSIHA
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