SitesBLAST
Comparing WP_019895085.1 NCBI__GCF_000384235.1:WP_019895085.1 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)
4rjiC Acetolactate synthase from bacillus subtilis bound to thdp - crystal form i (see paper)
38% identity, 97% coverage: 2:534/547 of query aligns to 3:540/555 of 4rjiC
- binding magnesium ion: D438 (= D432), D465 (= D459), T467 (≠ Q461)
- binding thiamine diphosphate: P24 (= P23), E48 (= E47), P74 (= P73), S387 (≠ A381), H388 (= H382), Q411 (≠ A405), G437 (= G431), D438 (= D432), G439 (≠ A433), G440 (= G434), T467 (≠ Q461), Y468 (= Y462), D469 (≠ G463), M470 (≠ L464), V471 (≠ I465), Y534 (= Y528)
4rjkG Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
38% identity, 97% coverage: 2:534/547 of query aligns to 2:539/553 of 4rjkG
- binding magnesium ion: D437 (= D432), D464 (= D459), T466 (≠ Q461)
- 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 (≠ V379), G385 (= G380), S386 (≠ A381), H387 (= H382), Q410 (≠ A405), L412 (≠ M407), G436 (= G431), D437 (= D432), G438 (≠ A433), G439 (= G434), T466 (≠ Q461), Y467 (= Y462), D468 (≠ G463), M469 (≠ L464), V470 (≠ I465), Y533 (= Y528)
4rjkF Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
38% identity, 97% coverage: 2:534/547 of query aligns to 2:539/552 of 4rjkF
- binding magnesium ion: D437 (= D432), D464 (= D459), T466 (≠ Q461)
- binding pyruvic acid: A25 (≠ E25), K26 (≠ E26)
- binding thiamine diphosphate: P23 (= P23), E47 (= E47), P73 (= P73), G385 (= G380), S386 (≠ A381), H387 (= H382), Q410 (≠ A405), L412 (≠ M407), G436 (= G431), D437 (= D432), G438 (≠ A433), G439 (= G434), T466 (≠ Q461), Y467 (= Y462), D468 (≠ G463), M469 (≠ L464), V470 (≠ I465), Y533 (= Y528)
5d6rB Acetolactate synthase from klebsiella pneumoniae in complex with mechanism-based inhibitor
36% identity, 97% coverage: 3:531/547 of query aligns to 7:538/548 of 5d6rB
- active site: I26 (≠ V22), G28 (= G24), A29 (≠ E25), K30 (≠ E26), I31 (≠ N27), E51 (= E47), T74 (= T70), H113 (= H109), Q114 (= Q110), S115 (≠ V111), Q163 (≠ E159), L254 (= L251), E281 (≠ H278), M386 (≠ V379), Q412 (≠ A405), M414 (= M407), D439 (= D432), D466 (= D459), G468 (≠ Q461), Y469 (= Y462), M471 (≠ L464), 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 (≠ V379), G387 (= G380), S388 (≠ A381), Q412 (≠ A405), M414 (= M407), D439 (= D432), G440 (≠ A433), G468 (≠ Q461), Y469 (= Y462), N470 (≠ G463), M471 (≠ L464), Y535 (= Y528)
- binding magnesium ion: R63 (= R59), Q212 (≠ R209), D439 (= D432), D466 (= D459), G468 (≠ Q461)
5dx6B Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
37% identity, 98% coverage: 3:538/547 of query aligns to 19:551/557 of 5dx6B
- active site: I38 (≠ V22), G40 (= G24), A41 (≠ E25), K42 (≠ E26), I43 (≠ N27), E63 (= E47), T86 (= T70), H125 (= H109), Q126 (= Q110), S127 (≠ V111), Q175 (≠ E159), L268 (= L251), E295 (≠ H278), M392 (≠ V379), Q418 (≠ A405), M420 (= M407), D445 (= D432), D472 (= D459), G474 (≠ Q461), Y475 (= Y462), M477 (≠ L464), V478 (≠ I465), Q481 (≠ K468), Y541 (= Y528)
- binding 3-fluoro-2-oxopropanoic acid: G264 (= G247), R265 (≠ T248), Q272 (≠ D255), A400 (= A387), R401 (= R388), Y404 (≠ R391)
- binding magnesium ion: S135 (≠ K119), T138 (≠ S122), D445 (= D432), D472 (= D459), G474 (≠ Q461)
- binding thiamine diphosphate: G393 (= G380), S394 (≠ A381), F395 (≠ H382), Q418 (≠ A405), M420 (= M407), G444 (= G431), D445 (= D432), G446 (≠ A433), D472 (= D459), G474 (≠ Q461), Y475 (= Y462), N476 (≠ G463), M477 (≠ L464), V478 (≠ I465), Y541 (= Y528)
1ozfA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors (see paper)
36% identity, 97% coverage: 3:531/547 of query aligns to 7:537/545 of 1ozfA
- active site: I26 (≠ V22), G28 (= G24), A29 (≠ E25), K30 (≠ E26), I31 (≠ N27), E51 (= E47), T74 (= T70), H113 (= H109), Q114 (= Q110), S115 (≠ V111), Q163 (≠ E159), L253 (= L251), E280 (≠ H278), M385 (≠ V379), Q411 (≠ A405), M413 (= M407), D438 (= D432), D465 (= D459), G467 (≠ Q461), Y468 (= Y462), M470 (≠ L464), V471 (≠ I465), Q474 (≠ K468), Y534 (= Y528)
- binding magnesium ion: D438 (= D432), D465 (= D459), G467 (≠ Q461)
- binding phosphate ion: G249 (= G247), R250 (≠ T248), Q257 (≠ D255), R343 (≠ M341), R394 (= R388), L396 (≠ F390), Y397 (≠ R391)
- binding thiamine diphosphate: G386 (= G380), S387 (≠ A381), F388 (≠ H382), Q411 (≠ A405), M413 (= M407), G437 (= G431), D438 (= D432), G439 (≠ A433), D465 (= D459), G467 (≠ Q461), Y468 (= Y462), N469 (≠ G463), M470 (≠ L464), V471 (≠ I465), Y534 (= Y528)
1ozgA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate (see paper)
36% identity, 98% coverage: 3:538/547 of query aligns to 8:548/549 of 1ozgA
- active site: I27 (≠ V22), G29 (= G24), A30 (≠ E25), K31 (≠ E26), I32 (≠ N27), E52 (= E47), T75 (= T70), H114 (= H109), Q115 (= Q110), S116 (≠ V111), Q164 (≠ E159), L257 (= L251), E284 (≠ H278), M389 (≠ V379), Q415 (≠ A405), M417 (= M407), D442 (= D432), D469 (= D459), G471 (≠ Q461), Y472 (= Y462), M474 (≠ L464), V475 (≠ I465), Q478 (≠ K468), Y538 (= Y528)
- binding 2-hydroxyethyl dihydrothiachrome diphosphate: M389 (≠ V379), G390 (= G380), S391 (≠ A381), F392 (≠ H382), Q415 (≠ A405), M417 (= M407), G441 (= G431), D442 (= D432), G443 (≠ A433), D469 (= D459), G471 (≠ Q461), Y472 (= Y462), N473 (≠ G463), M474 (≠ L464), V475 (≠ I465), Y538 (= Y528)
- binding magnesium ion: D442 (= D432), D469 (= D459), G471 (≠ Q461)
- binding phosphate ion: G253 (= G247), R254 (≠ T248), Q261 (≠ D255), R347 (≠ M341), R398 (= R388), Y401 (≠ R391)
5wdgA Acetolactate synthase from klebsiella pneumoniae in complex with a reaction intermediate
36% identity, 97% coverage: 3:531/547 of query aligns to 8:530/538 of 5wdgA
- active site: I27 (≠ V22), G29 (= G24), A30 (≠ E25), K31 (≠ E26), I32 (≠ N27), E52 (= E47), T75 (= T70), Q157 (= Q162), L246 (= L251), E273 (≠ H278), M378 (≠ V379), Q404 (≠ A405), M406 (= M407), D431 (= D432), D458 (= D459), G460 (≠ Q461), Y461 (= Y462), M463 (≠ L464), 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 (≠ V379), S380 (≠ A381), F381 (≠ H382), Q404 (≠ A405), M406 (= M407), G430 (= G431), D431 (= D432), G432 (≠ A433), G433 (= G434), D458 (= D459), G460 (≠ Q461), Y461 (= Y462), N462 (≠ G463), M463 (≠ L464), V464 (≠ I465), Y527 (= Y528)
- binding magnesium ion: R64 (= R59), S117 (≠ K119), T120 (≠ S122), Q204 (≠ R209), D431 (= D432), D458 (= D459), G460 (≠ Q461)
- binding pyruvic acid: G94 (≠ R89), R147 (≠ K149)
5dx6A Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
36% identity, 98% coverage: 3:538/547 of query aligns to 8:540/541 of 5dx6A
- active site: I27 (≠ V22), G29 (= G24), A30 (≠ E25), K31 (≠ E26), I32 (≠ N27), E52 (= E47), T75 (= T70), Q159 (≠ E159), L249 (= L251), E276 (≠ H278), M381 (≠ V379), Q407 (≠ A405), M409 (= M407), D434 (= D432), D461 (= D459), G463 (≠ Q461), Y464 (= Y462), M466 (≠ L464), 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 (≠ V379), G382 (= G380), S383 (≠ A381), F384 (≠ H382), Q407 (≠ A405), M409 (= M407), G433 (= G431), D434 (= D432), G435 (≠ A433), D461 (= D459), G463 (≠ Q461), Y464 (= Y462), N465 (≠ G463), Y530 (= Y528)
- binding magnesium ion: S119 (≠ K119), T122 (≠ S122), D434 (= D432), D461 (= D459), G463 (≠ Q461)
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)
33% identity, 97% coverage: 2:531/547 of query aligns to 92:640/664 of P09114
- P191 (≠ A100) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
- W568 (= W467) 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)
33% identity, 97% coverage: 2:531/547 of query aligns to 95:643/667 of P09342
- C161 (= C67) modified: Disulfide link with 307
- P194 (≠ A100) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ V207) modified: Disulfide link with 161
7tzzA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase p197t mutant in complex with bispyribac-sodium (see paper)
32% identity, 96% coverage: 2:525/547 of query aligns to 13:557/582 of 7tzzA
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: M266 (≠ L251), R292 (≠ E276), W489 (= W467)
- 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 (= V379), G401 (= G380), Q402 (≠ A381), H403 (= H382), G426 (≠ A405), M428 (= M407), G452 (= G431), D453 (= D432), G454 (≠ A433), S455 (≠ G434), L483 (≠ Y462), G484 (= G463), M485 (≠ L464), V486 (≠ I465)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G222 (= G204), G223 (≠ N205), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), M263 (≠ T248), L264 (≠ T249), M266 (≠ L251), H267 (≠ Q252), G286 (= G271), R288 (vs. gap), V293 (≠ Y277), D310 (= D294), I311 (≠ T295), D329 (≠ N313), V330 (≠ I314), M405 (= M384), G423 (≠ N402)
- binding magnesium ion: A37 (≠ E26), T82 (= T70), S83 (≠ L71), Q122 (= Q110), Y381 (≠ K360), D453 (= D432), M458 (= M437), Q461 (= Q440), N480 (≠ D459), H482 (≠ Q461), K533 (≠ A503)
Sites not aligning to the query:
5k2oA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a pyrimidinyl-benzoate herbicide, pyrithiobac (see paper)
32% identity, 96% coverage: 2:525/547 of query aligns to 13:557/585 of 5k2oA
- active site: Y33 (≠ V22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), S38 (≠ N27), E59 (= E47), T82 (= T70), F121 (≠ H109), Q122 (= Q110), E123 (≠ V111), K171 (≠ E159), M266 (≠ L251), V293 (≠ Y277), V400 (= V379), G426 (≠ A405), M428 (= M407), D453 (= D432), N480 (≠ D459), H482 (≠ Q461), L483 (≠ Y462), M485 (≠ L464), V486 (≠ I465), W489 (= W467)
- binding 2-chloranyl-6-(4,6-dimethoxypyrimidin-2-yl)sulfanyl-benzoic acid: M266 (≠ L251), R292 (≠ E276), W489 (= W467)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G222 (= G204), G223 (≠ N205), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), L264 (≠ T249), G286 (= G271), R288 (vs. gap), D290 (= D273), V293 (≠ Y277), D310 (= D294), I311 (≠ T295), D329 (≠ N313), V330 (≠ I314), Q404 (≠ K383), M405 (= M384), G423 (≠ N402)
- binding magnesium ion: D453 (= D432), N480 (≠ D459), H482 (≠ Q461)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (= V379), G401 (= G380), Q402 (≠ A381), H403 (= H382), M428 (= M407), D453 (= D432), G454 (≠ A433), S455 (≠ G434), N480 (≠ D459), H482 (≠ Q461), L483 (≠ Y462), G484 (= G463), M485 (≠ L464), V486 (≠ I465)
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)
32% identity, 96% coverage: 2:525/547 of query aligns to 13:557/583 of 5k3sA
- active site: Y33 (≠ V22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), S38 (≠ N27), E59 (= E47), T82 (= T70), F121 (≠ H109), Q122 (= Q110), E123 (≠ V111), K171 (≠ E159), M266 (≠ L251), V293 (≠ Y277), V400 (= V379), G426 (≠ A405), M428 (= M407), D453 (= D432), N480 (≠ D459), H482 (≠ Q461), L483 (≠ Y462), M485 (≠ L464), V486 (≠ I465), W489 (= W467)
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: R292 (≠ E276), M485 (≠ L464), W489 (= W467)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G222 (= G204), G223 (≠ N205), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), L264 (≠ T249), M266 (≠ L251), G286 (= G271), R288 (vs. gap), D290 (= D273), V293 (≠ Y277), D310 (= D294), I311 (≠ T295), D329 (≠ N313), V330 (≠ I314), M405 (= M384), G423 (≠ N402)
- binding magnesium ion: D453 (= D432), N480 (≠ D459), H482 (≠ Q461)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (= V379), G401 (= G380), Q402 (≠ A381), H403 (= H382), G426 (≠ A405), M428 (= M407), D453 (= D432), G454 (≠ A433), S455 (≠ G434), N480 (≠ D459), H482 (≠ Q461), L483 (≠ Y462), G484 (= G463), M485 (≠ L464), V486 (≠ I465)
Sites not aligning to the query:
8et4A Crystal structure of wild-type arabidopsis thaliana acetohydroxyacid synthase in complex with amidosulfuron (see paper)
32% identity, 96% coverage: 2:525/547 of query aligns to 13:557/582 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 (= V379), G401 (= G380), Q402 (≠ A381), H403 (= H382), G426 (≠ A405), M428 (= M407), G452 (= G431), D453 (= D432), G454 (≠ A433), S455 (≠ G434), M458 (= M437), N480 (≠ D459), H482 (≠ Q461), L483 (≠ Y462), G484 (= G463), M485 (≠ L464), V486 (≠ I465)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G222 (= G204), G223 (≠ N205), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), L264 (≠ T249), M266 (≠ L251), H267 (≠ Q252), G286 (= G271), V287 (vs. gap), R288 (vs. gap), D290 (= D273), R292 (≠ E276), V293 (≠ Y277), D310 (= D294), I311 (≠ T295), D329 (≠ N313), V330 (≠ I314), M405 (= M384), G423 (≠ N402)
- binding magnesium ion: F370 (≠ Q339), D453 (= D432), M458 (= M437), Q461 (= Q440), N480 (≠ D459), H482 (≠ Q461), K533 (≠ A503)
- binding N-{[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl}-N-methylmethanesulfonamide: M266 (≠ L251), R292 (≠ E276), M485 (≠ L464), W489 (= W467)
Sites not aligning to the query:
5wj1A Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a triazolopyrimidine herbicide, penoxsulam (see paper)
32% identity, 96% coverage: 2:525/547 of query aligns to 13:557/582 of 5wj1A
- active site: Y33 (≠ V22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), S38 (≠ N27), E59 (= E47), T82 (= T70), F121 (≠ H109), Q122 (= Q110), E123 (≠ V111), K171 (≠ E159), M266 (≠ L251), V293 (≠ Y277), V400 (= V379), G426 (≠ A405), M428 (= M407), D453 (= D432), N480 (≠ D459), H482 (≠ Q461), L483 (≠ Y462), M485 (≠ L464), V486 (≠ I465), W489 (= W467)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G222 (= G204), G223 (≠ N205), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), M263 (≠ T248), L264 (≠ T249), G286 (= G271), R288 (vs. gap), V293 (≠ Y277), D310 (= D294), I311 (≠ T295), D329 (≠ N313), V330 (≠ I314), M405 (= M384), G423 (≠ N402), G424 (= G403)
- binding magnesium ion: D453 (= D432), N480 (≠ D459), H482 (≠ Q461)
- binding 2-(2,2-difluoroethoxy)-N-(5,8-dimethoxy[1,2,4]triazolo[1,5-c]pyrimidin-2-yl)-6-(trifluoromethyl)benzenesulfonamide: M266 (≠ L251), D291 (≠ M274), R292 (≠ E276), M485 (≠ L464), W489 (= W467)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (= V379), G401 (= G380), Q402 (≠ A381), H403 (= H382), M428 (= M407), D453 (= D432), G454 (≠ A433), S455 (≠ G434), M458 (= M437), N480 (≠ D459), H482 (≠ Q461), L483 (≠ Y462), G484 (= G463), M485 (≠ L464), V486 (≠ I465)
Sites not aligning to the query:
5k6tA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a sulfonylamino-carbonyl-triazolinone herbicide, propoxycarbazone-sodium (see paper)
32% identity, 96% coverage: 2:525/547 of query aligns to 13:557/582 of 5k6tA
- active site: Y33 (≠ V22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), S38 (≠ N27), E59 (= E47), T82 (= T70), F121 (≠ H109), Q122 (= Q110), E123 (≠ V111), K171 (≠ E159), M266 (≠ L251), V293 (≠ Y277), V400 (= V379), G426 (≠ A405), M428 (= M407), D453 (= D432), N480 (≠ D459), H482 (≠ Q461), L483 (≠ Y462), M485 (≠ L464), V486 (≠ I465), W489 (= W467)
- binding methyl 2-[(4-methyl-5-oxidanylidene-3-propoxy-1,2,4-triazol-1-yl)carbonylsulfamoyl]benzoate: H267 (≠ Q252), R292 (≠ E276), M485 (≠ L464), W489 (= W467)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G222 (= G204), G223 (≠ N205), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), L264 (≠ T249), G286 (= G271), R288 (vs. gap), D290 (= D273), R292 (≠ E276), V293 (≠ Y277), D310 (= D294), I311 (≠ T295), D329 (≠ N313), V330 (≠ I314), Q404 (≠ K383), M405 (= M384), G423 (≠ N402)
- binding magnesium ion: D453 (= D432), N480 (≠ D459), H482 (≠ Q461)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: V400 (= V379), G401 (= G380), Q402 (≠ A381), H403 (= H382), G426 (≠ A405), M428 (= M407), G452 (= G431), G454 (≠ A433), S455 (≠ G434), N480 (≠ D459), H482 (≠ Q461), L483 (≠ Y462), G484 (= G463)
Sites not aligning to the query:
5k6rA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a sulfonylamino-carbonyl-triazolinone herbicide, thiencarbazone-methyl (see paper)
32% identity, 96% coverage: 2:525/547 of query aligns to 13:557/582 of 5k6rA
- active site: Y33 (≠ V22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), S38 (≠ N27), E59 (= E47), T82 (= T70), F121 (≠ H109), Q122 (= Q110), E123 (≠ V111), K171 (≠ E159), M266 (≠ L251), V293 (≠ Y277), V400 (= V379), G426 (≠ A405), M428 (= M407), D453 (= D432), N480 (≠ D459), H482 (≠ Q461), L483 (≠ Y462), M485 (≠ L464), V486 (≠ I465), W489 (= W467)
- binding methyl 4-[(3-methoxy-4-methyl-5-oxidanylidene-1,2,4-triazol-1-yl)carbonylsulfamoyl]-5-methyl-thiophene-3-carboxylate: R292 (≠ E276), W489 (= W467)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G222 (= G204), G223 (≠ N205), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), L264 (≠ T249), M266 (≠ L251), G286 (= G271), R288 (vs. gap), R292 (≠ E276), V293 (≠ Y277), D310 (= D294), I311 (≠ T295), G328 (= G312), D329 (≠ N313), V330 (≠ I314), M405 (= M384), G423 (≠ N402)
- binding magnesium ion: D453 (= D432), N480 (≠ D459), H482 (≠ Q461)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: V400 (= V379), G401 (= G380), Q402 (≠ A381), H403 (= H382), G426 (≠ A405), M428 (= M407), D453 (= D432), G454 (≠ A433), S455 (≠ G434), M458 (= M437), N480 (≠ D459), H482 (≠ Q461), L483 (≠ Y462), G484 (= G463), M485 (≠ L464), V486 (≠ I465)
Sites not aligning to the query:
1z8nA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with an imidazolinone herbicide, imazaquin (see paper)
32% identity, 96% coverage: 2:525/547 of query aligns to 13:557/582 of 1z8nA
- active site: Y33 (≠ V22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), S38 (≠ N27), E59 (= E47), T82 (= T70), F121 (≠ H109), Q122 (= Q110), E123 (≠ V111), K171 (≠ E159), M266 (≠ L251), V293 (≠ Y277), V400 (= V379), G426 (≠ A405), M428 (= M407), D453 (= D432), N480 (≠ D459), H482 (≠ Q461), L483 (≠ Y462), M485 (≠ L464), V486 (≠ I465), W489 (= W467)
- binding 2-(4-isopropyl-4-methyl-5-oxo-4,5-dihydro-1h-imidazol-2-yl)quinoline-3-carboxylic acid: K135 (= K123), R161 (≠ K149), Y191 (≠ V174), R194 (= R177), D291 (≠ M274), R292 (≠ E276), D312 (≠ C296), W489 (= W467)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G222 (= G204), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), L264 (≠ T249), G265 (= G250), M266 (≠ L251), H267 (≠ Q252), G286 (= G271), V287 (vs. gap), R288 (vs. gap), D290 (= D273), R292 (≠ E276), V293 (≠ Y277), D310 (= D294), I311 (≠ T295), D329 (≠ N313), V330 (≠ I314), M405 (= M384), G423 (≠ N402), G424 (= G403)
- binding magnesium ion: D453 (= D432), N480 (≠ D459)
- binding thiamine diphosphate: V400 (= V379), G401 (= G380), Q402 (≠ A381), H403 (= H382), G426 (≠ A405), M428 (= M407), G452 (= G431), G454 (≠ A433), S455 (≠ G434), N480 (≠ D459), H482 (≠ Q461), L483 (≠ Y462), G484 (= G463), M485 (≠ L464), V486 (≠ I465)
Sites not aligning to the query:
1yi1A Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a sulfonylurea herbicide, tribenuron methyl (see paper)
32% identity, 96% coverage: 2:525/547 of query aligns to 13:557/582 of 1yi1A
- active site: Y33 (≠ V22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), S38 (≠ N27), E59 (= E47), T82 (= T70), F121 (≠ H109), Q122 (= Q110), E123 (≠ V111), K171 (≠ E159), M266 (≠ L251), V293 (≠ Y277), V400 (= V379), G426 (≠ A405), M428 (= M407), D453 (= D432), N480 (≠ D459), H482 (≠ Q461), L483 (≠ Y462), M485 (≠ L464), V486 (≠ I465), W489 (= W467)
- binding methyl 2-[4-methoxy-6-methyl-1,3,5-trazin-2-yl(methyl)carbamoylsulfamoyl]benzoate: D291 (≠ M274), R292 (≠ E276), W489 (= W467)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G223 (≠ N205), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), M263 (≠ T248), L264 (≠ T249), G265 (= G250), M266 (≠ L251), H267 (≠ Q252), G286 (= G271), V287 (vs. gap), R288 (vs. gap), D290 (= D273), V293 (≠ Y277), D310 (= D294), I311 (≠ T295), D329 (≠ N313), V330 (≠ I314), M405 (= M384), G423 (≠ N402), G424 (= G403)
- binding magnesium ion: D453 (= D432), N480 (≠ D459), H482 (≠ Q461)
Sites not aligning to the query:
Query Sequence
>WP_019895085.1 NCBI__GCF_000384235.1:WP_019895085.1
MKAAKRFVQCLENEGVEFVFGVPGEENMDILDALLDSDIRFITCRHEQGAAFMADVYGRI
TGRAGVCLSTLGPGATNLVTGVADANMDRSPIVAIAGQAATTRLHKESHQVVDLVSLFKP
ISKYATQVLEPETLPEVVRKAFKLAQAEKPGASFIDFPENIQEMLTPETPLPVVPTRLSL
ADHKLLKQAAQIIDQAKRPMILVGNGVARANASKQVQAFAEHRQIPLVNTFMAKGSVPHY
KNPLSMGTTGLQKGDYENGGFANSDVVICVGFDMVEYHPHLWNPNREHTIVHIDTCAAEV
DYSYMPDVELVGNIGRNLKALSEHLPANDTPPQPFPLRQAMIAEMDQFENDQAWPLKPQK
IIWDLRTAMDKDAIAICDVGAHKMWMARFFRAEQPNTCIISNGFASMGIALPGAVGAKLA
HPDKAVVAVTGDAGLMMNVQELETALREQTPIVILIWNDSQYGLIEWKQKRRFQRSAYID
FKNPDFVTFAQSFGATGVRIESADQLLPALKTAIATPTVTLIDCPVDYSENDRLTDLLGN
VISEMTN
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