SitesBLAST
Comparing BPHYT_RS06145 FitnessBrowser__BFirm:BPHYT_RS06145 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
5d6rB Acetolactate synthase from klebsiella pneumoniae in complex with mechanism-based inhibitor
34% identity, 98% coverage: 4:541/550 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 (= H108), Q114 (= Q110), S115 (≠ I111), Q163 (≠ E159), L254 (= L250), E281 (≠ P277), M386 (≠ N383), Q412 (≠ A409), M414 (= M411), D439 (= D436), D466 (= D463), G468 (≠ A465), Y469 (≠ F466), M471 (= M468), V472 (≠ I469), Q475 (≠ K472), Y535 (= Y532)
- 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 (≠ N383), G387 (= G384), S388 (≠ M385), Q412 (≠ A409), M414 (= M411), D439 (= D436), G440 (= G437), G468 (≠ A465), Y469 (≠ F466), N470 (≠ G467), M471 (= M468), Y535 (= Y532)
- binding magnesium ion: R63 (= R59), Q212 (≠ R209), D439 (= D436), D466 (= D463), G468 (≠ A465)
1ozgA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate (see paper)
34% identity, 98% coverage: 4:541/550 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 (= H108), Q115 (= Q110), S116 (≠ I111), Q164 (≠ E159), L257 (= L250), E284 (≠ P277), M389 (≠ N383), Q415 (≠ A409), M417 (= M411), D442 (= D436), D469 (= D463), G471 (≠ A465), Y472 (≠ F466), M474 (= M468), V475 (≠ I469), Q478 (≠ K472), Y538 (= Y532)
- binding 2-hydroxyethyl dihydrothiachrome diphosphate: M389 (≠ N383), G390 (= G384), S391 (≠ M385), F392 (≠ Y386), Q415 (≠ A409), M417 (= M411), G441 (= G435), D442 (= D436), G443 (= G437), D469 (= D463), G471 (≠ A465), Y472 (≠ F466), N473 (≠ G467), M474 (= M468), V475 (≠ I469), Y538 (= Y532)
- binding magnesium ion: D442 (= D436), D469 (= D463), G471 (≠ A465)
- binding phosphate ion: G253 (= G246), R254 (≠ N247), Q261 (≠ D254), R347 (≠ K339), R398 (= R392), Y401 (≠ R395)
1ozfA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors (see paper)
34% identity, 98% coverage: 4:541/550 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 (= H108), Q114 (= Q110), S115 (≠ I111), Q163 (≠ E159), L253 (= L250), E280 (≠ P277), M385 (≠ N383), Q411 (≠ A409), M413 (= M411), D438 (= D436), D465 (= D463), G467 (≠ A465), Y468 (≠ F466), M470 (= M468), V471 (≠ I469), Q474 (≠ K472), Y534 (= Y532)
- binding magnesium ion: D438 (= D436), D465 (= D463), G467 (≠ A465)
- binding phosphate ion: G249 (= G246), R250 (≠ N247), Q257 (≠ D254), R343 (≠ K339), R394 (= R392), L396 (≠ Y394), Y397 (≠ R395)
- binding thiamine diphosphate: G386 (= G384), S387 (≠ M385), F388 (≠ Y386), Q411 (≠ A409), M413 (= M411), G437 (= G435), D438 (= D436), G439 (= G437), D465 (= D463), G467 (≠ A465), Y468 (≠ F466), N469 (≠ G467), M470 (= M468), V471 (≠ I469), Y534 (= Y532)
5dx6B Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
34% identity, 98% coverage: 4:541/550 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 (= H108), Q126 (= Q110), S127 (≠ I111), Q175 (≠ E159), L268 (= L250), E295 (≠ P277), M392 (≠ N383), Q418 (≠ A409), M420 (= M411), D445 (= D436), D472 (= D463), G474 (≠ A465), Y475 (≠ F466), M477 (= M468), V478 (≠ I469), Q481 (≠ K472), Y541 (= Y532)
- binding 3-fluoro-2-oxopropanoic acid: G264 (= G246), R265 (≠ N247), Q272 (≠ D254), A400 (= A391), R401 (= R392), Y404 (≠ R395)
- binding magnesium ion: S135 (≠ E119), T138 (= T122), D445 (= D436), D472 (= D463), G474 (≠ A465)
- binding thiamine diphosphate: G393 (= G384), S394 (≠ M385), F395 (≠ Y386), Q418 (≠ A409), M420 (= M411), G444 (= G435), D445 (= D436), G446 (= G437), D472 (= D463), G474 (≠ A465), Y475 (≠ F466), N476 (≠ G467), M477 (= M468), V478 (≠ I469), Y541 (= Y532)
5wdgA Acetolactate synthase from klebsiella pneumoniae in complex with a reaction intermediate
33% identity, 98% coverage: 4:541/550 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 (≠ N383), Q404 (≠ A409), M406 (= M411), D431 (= D436), D458 (= D463), G460 (≠ A465), Y461 (≠ F466), M463 (= M468), V464 (≠ I469), Q467 (≠ K472), Y527 (= Y532)
- 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 (≠ N383), S380 (≠ M385), F381 (≠ Y386), Q404 (≠ A409), M406 (= M411), G430 (= G435), D431 (= D436), G432 (= G437), G433 (= G438), D458 (= D463), G460 (≠ A465), Y461 (≠ F466), N462 (≠ G467), M463 (= M468), V464 (≠ I469), Y527 (= Y532)
- binding magnesium ion: R64 (= R59), S117 (≠ E119), T120 (= T122), Q204 (≠ R209), D431 (= D436), D458 (= D463), G460 (≠ A465)
- binding pyruvic acid: G94 (= G89), R147 (= R149)
5dx6A Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
33% identity, 98% coverage: 4:541/550 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 (≠ N383), Q407 (≠ A409), M409 (= M411), D434 (= D436), D461 (= D463), G463 (≠ A465), Y464 (≠ F466), M466 (= M468), V467 (≠ I469), Q470 (≠ K472), Y530 (= Y532)
- 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 (≠ N383), G382 (= G384), S383 (≠ M385), F384 (≠ Y386), Q407 (≠ A409), M409 (= M411), G433 (= G435), D434 (= D436), G435 (= G437), D461 (= D463), G463 (≠ A465), Y464 (≠ F466), N465 (≠ G467), Y530 (= Y532)
- binding magnesium ion: S119 (≠ E119), T122 (= T122), D434 (= D436), D461 (= D463), G463 (≠ A465)
4rjkF Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
32% identity, 97% coverage: 2:535/550 of query aligns to 2:536/552 of 4rjkF
- binding magnesium ion: D437 (= D436), D464 (= D463), T466 (≠ A465)
- binding pyruvic acid: A25 (≠ E25), K26 (≠ E26)
- binding thiamine diphosphate: P23 (= P23), E47 (= E47), P73 (= P73), G385 (= G384), S386 (≠ M385), H387 (≠ Y386), Q410 (≠ A409), L412 (≠ M411), G436 (= G435), D437 (= D436), G438 (= G437), G439 (= G438), T466 (≠ A465), Y467 (≠ F466), D468 (≠ G467), M469 (= M468), V470 (≠ I469), Y533 (= Y532)
4rjiC Acetolactate synthase from bacillus subtilis bound to thdp - crystal form i (see paper)
32% identity, 97% coverage: 2:535/550 of query aligns to 3:537/555 of 4rjiC
- binding magnesium ion: D438 (= D436), D465 (= D463), T467 (≠ A465)
- binding thiamine diphosphate: P24 (= P23), E48 (= E47), P74 (= P73), S387 (≠ M385), H388 (≠ Y386), Q411 (≠ A409), G437 (= G435), D438 (= D436), G439 (= G437), G440 (= G438), T467 (≠ A465), Y468 (≠ F466), D469 (≠ G467), M470 (= M468), V471 (≠ I469), Y534 (= Y532)
4rjkG Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
32% identity, 97% coverage: 2:535/550 of query aligns to 2:536/553 of 4rjkG
- binding magnesium ion: D437 (= D436), D464 (= D463), T466 (≠ A465)
- 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 (≠ N383), G385 (= G384), S386 (≠ M385), H387 (≠ Y386), Q410 (≠ A409), L412 (≠ M411), G436 (= G435), D437 (= D436), G438 (= G437), G439 (= G438), T466 (≠ A465), Y467 (≠ F466), D468 (≠ G467), M469 (= M468), V470 (≠ I469), Y533 (= Y532)
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)
30% identity, 97% coverage: 2:535/550 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 (≠ G207) modified: Disulfide link with 161
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, 97% coverage: 2:535/550 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 (= W471) 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)
30% identity, 96% coverage: 4:531/550 of query aligns to 9:520/539 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 (≠ V273), V375 (≠ N383), G401 (≠ A409), M403 (= M411), D428 (= D436), N455 (≠ D463), A457 (= A465), L458 (≠ F466), L460 (≠ M468), V461 (≠ I469), Q464 (= Q473)
- binding flavin-adenine dinucleotide: R155 (= R149), G212 (= G206), G213 (= G207), G214 (≠ N208), T236 (= T230), L237 (≠ Q231), M238 (= M232), L254 (≠ A248), M256 (≠ L250), H257 (≠ S251), G276 (= G270), A277 (vs. gap), R278 (vs. gap), D280 (vs. gap), R282 (≠ D272), A283 (≠ V273), D300 (≠ N295), I301 (≠ F296), D319 (= D314), V320 (≠ I315), M380 (≠ I388), G398 (≠ N406)
- binding magnesium ion: D428 (= D436), N455 (≠ D463)
- binding thiamine diphosphate: E53 (= E47), C76 (≠ T70), P79 (= P73), G376 (= G384), Q377 (≠ M385), H378 (≠ Y386), G401 (≠ A409), M403 (= M411), G427 (= G435), D428 (= D436), G429 (= G437), S430 (≠ G438), M433 (= M441), N455 (≠ D463), A457 (= A465), L458 (≠ F466), G459 (= G467), L460 (≠ M468), V461 (≠ I469)
3ea4A Arabidopsis thaliana acetohydroxyacid synthase in complex with monosulfuron-ester (see paper)
28% identity, 96% coverage: 2:528/550 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 (≠ P277), V399 (≠ N383), G425 (≠ A409), M427 (= M411), D452 (= D436), N479 (≠ D463), H481 (≠ A465), L482 (≠ F466), M484 (= M468), V485 (≠ I469), W488 (≠ K472)
- binding methyl 2-{[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl}benzoate: D290 (≠ E275), R291 (≠ K276), W488 (≠ K472)
- binding flavin-adenine dinucleotide-n5-isobutyl ketone: R160 (= R149), G221 (= G204), G222 (= G206), G223 (= G207), T245 (= T230), L246 (≠ Q231), M247 (= M232), L263 (≠ A248), G264 (≠ T249), M265 (≠ L250), H266 (≠ S251), G285 (= G270), R287 (≠ D272), D289 (≠ I274), R291 (≠ K276), D309 (≠ N295), I310 (≠ F296), G327 (= G313), D328 (= D314), V329 (≠ I315), M404 (≠ I388), G422 (≠ N406)
- binding magnesium ion: D452 (= D436), N479 (≠ D463), H481 (≠ A465)
- 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 (≠ N383), G400 (= G384), Q401 (≠ M385), H402 (≠ Y386), M427 (= M411), G451 (= G435), D452 (= D436), G453 (= G437), S454 (≠ G438), N479 (≠ D463), H481 (≠ A465), L482 (≠ F466), G483 (= G467), M484 (= M468), V485 (≠ I469)
Sites not aligning to the query:
3e9yA Arabidopsis thaliana acetohydroxyacid synthase in complex with monosulfuron (see paper)
28% identity, 96% coverage: 2:528/550 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 (≠ P277), V399 (≠ N383), G425 (≠ A409), M427 (= M411), D452 (= D436), N479 (≠ D463), H481 (≠ A465), L482 (≠ F466), M484 (= M468), V485 (≠ I469), W488 (≠ K472)
- binding N-[(4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide: D290 (≠ E275), R291 (≠ K276), W488 (≠ K472)
- binding flavin-adenine dinucleotide-n5-isobutyl ketone: R160 (= R149), G221 (= G204), G222 (= G206), G223 (= G207), T245 (= T230), L246 (≠ Q231), M247 (= M232), L263 (≠ A248), G285 (= G270), R287 (≠ D272), D289 (≠ I274), R291 (≠ K276), D309 (≠ N295), I310 (≠ F296), G327 (= G313), D328 (= D314), V329 (≠ I315), M404 (≠ I388), G422 (≠ N406)
- binding magnesium ion: D452 (= D436), N479 (≠ D463), H481 (≠ A465)
- 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 (≠ N383), G400 (= G384), Q401 (≠ M385), H402 (≠ Y386), M427 (= M411), G451 (= G435), G453 (= G437), S454 (≠ G438), N479 (≠ D463), H481 (≠ A465), L482 (≠ F466), G483 (= G467), M484 (= M468), V485 (≠ I469)
Sites not aligning to the query:
5wkcA Saccharomyces cerevisiae acetohydroxyacid synthase in complex with the herbicide penoxsulam (see paper)
30% identity, 97% coverage: 1:531/550 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 (vs. gap), V401 (≠ N383), L426 (= L408), G427 (≠ A409), M429 (= M411), D454 (= D436), N481 (≠ D463), E483 (≠ A465), Q484 (≠ F466), M486 (= M468), V487 (≠ I469), W490 (≠ K472), L512 (≠ Y493), G517 (= G498), L518 (≠ A499)
- 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 (≠ N383), G402 (= G384), Q403 (≠ M385), H404 (≠ Y386), G427 (≠ A409), M429 (= M411), G453 (= G435), D454 (= D436), A455 (≠ G437), S456 (≠ G438), M459 (= M441), N481 (≠ D463), E483 (≠ A465), Q484 (≠ F466), G485 (= G467), M486 (= M468), V487 (≠ I469)
- binding ethaneperoxoic acid: G32 (≠ E25), Q118 (= Q110)
- binding flavin-adenine dinucleotide: R157 (= R149), G211 (= G204), A212 (= A205), G213 (= G206), N216 (= N208), T238 (= T230), L239 (≠ Q231), Q240 (≠ M232), L256 (≠ A248), M258 (≠ L250), G278 (= G270), A279 (≠ H271), R280 (vs. gap), R284 (vs. gap), V285 (vs. gap), E311 (≠ N295), V312 (≠ F296), N316 (≠ E300), D330 (= D314), A331 (≠ I315), M406 (≠ I388), G424 (≠ N406)
- binding magnesium ion: D454 (= D436), N481 (≠ D463), E483 (≠ A465)
- 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 (vs. gap), M486 (= M468), W490 (≠ K472)
- 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:
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)
28% identity, 96% coverage: 2:528/550 of query aligns to 98:639/670 of P17597
- A122 (≠ E26) mutation to V: Reduced catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- M124 (≠ L28) 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 (= E47) binding
- S186 (≠ G89) binding
- P197 (= P100) mutation to S: In csr1-1/GH50; resistant to sulfonylurea but not to imidazolinone herbicides.
- R199 (≠ K102) mutation R->A,E: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- Q207 (= Q110) binding
- K220 (= K123) binding
- R246 (= R149) binding ; binding
- K256 (≠ E159) binding
- G308 (= G206) binding
- TL 331:332 (≠ TQ 230:231) binding
- C340 (≠ E239) modified: Cysteine sulfinic acid (-SO2H)
- LGMH 349:352 (≠ ATLS 248:251) binding
- GVRFD 371:375 (≠ GHDVI 270:274) binding
- DR 376:377 (≠ EK 275:276) binding
- DI 395:396 (≠ NF 295:296) binding
- DV 414:415 (≠ DI 314:315) binding
- QH 487:488 (≠ MY 385:386) binding
- GG 508:509 (≠ NA 406:407) binding
- GAM 511:513 (≠ ASM 409:411) binding
- D538 (= D436) binding
- DGS 538:540 (≠ DGG 436:438) binding
- N565 (≠ D463) binding
- NQHLGM 565:570 (≠ DDAFGM 463:468) binding
- H567 (≠ A465) binding
- W574 (≠ K472) binding ; 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.
Sites not aligning to the query:
- 653 binding ; S→A: No effect on catalytic activity or sensitivity to herbicides.; S→F: No effect on catalytic activity. Resistant to imidazolinone herbicides and also slightly sulfonylurea-resistant.; S→N: In csr1-2/GH90; no effect on catalytic activity. Resistant to imidazolinone but not to sulfonylurea herbicides.; S→T: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
5k2oA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a pyrimidinyl-benzoate herbicide, pyrithiobac (see paper)
28% identity, 96% coverage: 2:528/550 of query aligns to 13:554/585 of 5k2oA
- active site: Y33 (≠ I22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), S38 (≠ N27), E59 (= E47), T82 (= T70), F121 (= F109), Q122 (= Q110), E123 (≠ I111), K171 (≠ E159), M266 (≠ L250), V293 (≠ P277), V400 (≠ N383), G426 (≠ A409), M428 (= M411), D453 (= D436), N480 (≠ D463), H482 (≠ A465), L483 (≠ F466), M485 (= M468), V486 (≠ I469), W489 (≠ K472)
- binding 2-chloranyl-6-(4,6-dimethoxypyrimidin-2-yl)sulfanyl-benzoic acid: M266 (≠ L250), R292 (≠ K276), W489 (≠ K472)
- binding flavin-adenine dinucleotide: R161 (= R149), G222 (= G204), G223 (= G206), G224 (= G207), T246 (= T230), L247 (≠ Q231), M248 (= M232), L264 (≠ A248), G286 (= G270), R288 (≠ D272), D290 (≠ I274), V293 (≠ P277), D310 (≠ N295), I311 (≠ F296), D329 (= D314), V330 (≠ I315), Q404 (≠ K387), M405 (≠ I388), G423 (≠ N406)
- binding magnesium ion: D453 (= D436), N480 (≠ D463), H482 (≠ A465)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (≠ N383), G401 (= G384), Q402 (≠ M385), H403 (≠ Y386), M428 (= M411), D453 (= D436), G454 (= G437), S455 (≠ G438), N480 (≠ D463), H482 (≠ A465), L483 (≠ F466), G484 (= G467), M485 (= M468), V486 (≠ I469)
Sites not aligning to the query:
5k3sA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a pyrimidinyl-benzoate herbicide, bispyribac-sodium (see paper)
28% identity, 96% coverage: 2:528/550 of query aligns to 13:554/583 of 5k3sA
- active site: Y33 (≠ I22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), S38 (≠ N27), E59 (= E47), T82 (= T70), F121 (= F109), Q122 (= Q110), E123 (≠ I111), K171 (≠ E159), M266 (≠ L250), V293 (≠ P277), V400 (≠ N383), G426 (≠ A409), M428 (= M411), D453 (= D436), N480 (≠ D463), H482 (≠ A465), L483 (≠ F466), M485 (= M468), V486 (≠ I469), W489 (≠ K472)
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: R292 (≠ K276), M485 (= M468), W489 (≠ K472)
- binding flavin-adenine dinucleotide: R161 (= R149), G222 (= G204), G223 (= G206), G224 (= G207), T246 (= T230), L247 (≠ Q231), M248 (= M232), L264 (≠ A248), M266 (≠ L250), G286 (= G270), R288 (≠ D272), D290 (≠ I274), V293 (≠ P277), D310 (≠ N295), I311 (≠ F296), D329 (= D314), V330 (≠ I315), M405 (≠ I388), G423 (≠ N406)
- binding magnesium ion: D453 (= D436), N480 (≠ D463), H482 (≠ A465)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (≠ N383), G401 (= G384), Q402 (≠ M385), H403 (≠ Y386), G426 (≠ A409), M428 (= M411), D453 (= D436), G454 (= G437), S455 (≠ G438), N480 (≠ D463), H482 (≠ A465), L483 (≠ F466), G484 (= G467), M485 (= M468), V486 (≠ I469)
Sites not aligning to the query:
8et4A Crystal structure of wild-type arabidopsis thaliana acetohydroxyacid synthase in complex with amidosulfuron (see paper)
28% identity, 96% coverage: 2:528/550 of query aligns to 13:554/582 of 8et4A
- binding 2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-2-[(1~{S})-1-(dioxidanyl)-1-oxidanyl-ethyl]-4-methyl-1,3-thiazol-5-yl]ethyl phosphono hydrogen phosphate: V400 (≠ N383), G401 (= G384), Q402 (≠ M385), H403 (≠ Y386), G426 (≠ A409), M428 (= M411), G452 (= G435), D453 (= D436), G454 (= G437), S455 (≠ G438), M458 (= M441), N480 (≠ D463), H482 (≠ A465), L483 (≠ F466), G484 (= G467), M485 (= M468), V486 (≠ I469)
- binding flavin-adenine dinucleotide: R161 (= R149), G222 (= G204), G223 (= G206), G224 (= G207), T246 (= T230), L247 (≠ Q231), M248 (= M232), L264 (≠ A248), M266 (≠ L250), H267 (≠ S251), G286 (= G270), V287 (≠ H271), R288 (≠ D272), D290 (≠ I274), R292 (≠ K276), V293 (≠ P277), D310 (≠ N295), I311 (≠ F296), D329 (= D314), V330 (≠ I315), M405 (≠ I388), G423 (≠ N406)
- binding magnesium ion: F370 (= F358), D453 (= D436), M458 (= M441), Q461 (= Q444), N480 (≠ D463), H482 (≠ A465), K533 (≠ A507)
- binding N-{[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl}-N-methylmethanesulfonamide: M266 (≠ L250), R292 (≠ K276), M485 (= M468), W489 (≠ K472)
Sites not aligning to the query:
5wj1A Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a triazolopyrimidine herbicide, penoxsulam (see paper)
28% identity, 96% coverage: 2:528/550 of query aligns to 13:554/582 of 5wj1A
- active site: Y33 (≠ I22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), S38 (≠ N27), E59 (= E47), T82 (= T70), F121 (= F109), Q122 (= Q110), E123 (≠ I111), K171 (≠ E159), M266 (≠ L250), V293 (≠ P277), V400 (≠ N383), G426 (≠ A409), M428 (= M411), D453 (= D436), N480 (≠ D463), H482 (≠ A465), L483 (≠ F466), M485 (= M468), V486 (≠ I469), W489 (≠ K472)
- binding flavin-adenine dinucleotide: R161 (= R149), G222 (= G204), G223 (= G206), G224 (= G207), T246 (= T230), L247 (≠ Q231), M248 (= M232), M263 (≠ N247), L264 (≠ A248), G286 (= G270), R288 (≠ D272), V293 (≠ P277), D310 (≠ N295), I311 (≠ F296), D329 (= D314), V330 (≠ I315), M405 (≠ I388), G423 (≠ N406), G424 (≠ A407)
- binding magnesium ion: D453 (= D436), N480 (≠ D463), H482 (≠ A465)
- binding 2-(2,2-difluoroethoxy)-N-(5,8-dimethoxy[1,2,4]triazolo[1,5-c]pyrimidin-2-yl)-6-(trifluoromethyl)benzenesulfonamide: M266 (≠ L250), D291 (≠ E275), R292 (≠ K276), M485 (= M468), W489 (≠ K472)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (≠ N383), G401 (= G384), Q402 (≠ M385), H403 (≠ Y386), M428 (= M411), D453 (= D436), G454 (= G437), S455 (≠ G438), M458 (= M441), N480 (≠ D463), H482 (≠ A465), L483 (≠ F466), G484 (= G467), M485 (= M468), V486 (≠ I469)
Sites not aligning to the query:
Query Sequence
>BPHYT_RS06145 FitnessBrowser__BFirm:BPHYT_RS06145
MKASDLFVKSLEAEGVEYVFGIPGEENLDLLESLRRSKIRLILTRHEQAAGFMAATYGRL
TGRTGVCLATLGPGATNFVTAAAYAQLGGMPMLMVTGQKPIKSSKQGHFQIVDVVRMMEP
LTKYTRQIVSIANIPAMVREAVRQAEEERPGATHLELPEDVAHEEGDGKPIPKSFSRRPV
AEEKAVARAVEAITGAKHPLLMIGAGGNRKTTTKMLREFVDQIGIPFFTTQMGKGVIDES
HPMWLGNATLSDGDFVHRAIDHADCIINVGHDVIEKPPFFMRSGDAGEKTVIHVNFLGAE
VDTVYFPQIEVVGDIANAVWQLKESLKERQEHWDFTRFKEIKEHFEAHLAKGQHDDRFPM
YPVRVVNDVYETTPVDGIVCLDNGMYKIWFARYYRAHEPNSLLLDNALASMGAGLPSAIA
TKIVHPDRKVMAVCGDGGFMMNSQELETAVRLKLDLVILIVRDDAFGMIRWKQENMNFPD
YGMTLSNPDFVAYAESYGAKGHRIETAAEFAPLLRECFATPGVHVIDLPIDYSDNERVLN
REIKRLSAQL
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