SitesBLAST
Comparing WP_013836184.1 NCBI__GCF_000214825.1:WP_013836184.1 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)
4rjiC Acetolactate synthase from bacillus subtilis bound to thdp - crystal form i (see paper)
38% identity, 99% coverage: 3:542/547 of query aligns to 4:553/555 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, 99% coverage: 3:542/547 of query aligns to 3:552/553 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, 99% coverage: 3:542/547 of query aligns to 3:552/552 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)
5dx6B Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
37% identity, 97% coverage: 2:531/547 of query aligns to 18:544/557 of 5dx6B
- active site: I38 (= I22), G40 (= G24), A41 (≠ E25), K42 (≠ E26), I43 (≠ N27), E63 (= E47), T86 (= T70), H125 (= H109), Q126 (= Q110), S127 (≠ V111), Q175 (≠ E159), L268 (≠ T248), 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 (≠ T244), R265 (≠ A245), Q272 (= Q252), A400 (= A387), R401 (= R388), Y404 (≠ R391)
- binding magnesium ion: S135 (≠ K119), T138 (= T122), 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)
5d6rB Acetolactate synthase from klebsiella pneumoniae in complex with mechanism-based inhibitor
38% identity, 97% coverage: 2:531/547 of query aligns to 6:538/548 of 5d6rB
- active site: I26 (= I22), G28 (= G24), A29 (≠ E25), K30 (≠ E26), I31 (≠ N27), E51 (= E47), T74 (= T70), H113 (= H109), Q114 (= Q110), S115 (≠ V111), Q163 (≠ E159), L254 (≠ T248), 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)
1ozgA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate (see paper)
38% identity, 97% coverage: 2:531/547 of query aligns to 7:541/549 of 1ozgA
- active site: I27 (= I22), G29 (= G24), A30 (≠ E25), K31 (≠ E26), I32 (≠ N27), E52 (= E47), T75 (= T70), H114 (= H109), Q115 (= Q110), S116 (≠ V111), Q164 (≠ E159), L257 (≠ T248), 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 (≠ T244), R254 (≠ A245), Q261 (= Q252), R347 (vs. gap), R398 (= R388), Y401 (≠ R391)
1ozfA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors (see paper)
38% identity, 97% coverage: 2:531/547 of query aligns to 6:537/545 of 1ozfA
- active site: I26 (= I22), G28 (= G24), A29 (≠ E25), K30 (≠ E26), I31 (≠ N27), E51 (= E47), T74 (= T70), H113 (= H109), Q114 (= Q110), S115 (≠ V111), Q163 (≠ E159), L253 (≠ T248), 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 (≠ T244), R250 (≠ A245), Q257 (= Q252), R343 (vs. gap), 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)
5wdgA Acetolactate synthase from klebsiella pneumoniae in complex with a reaction intermediate
38% identity, 97% coverage: 2:531/547 of query aligns to 7:530/538 of 5wdgA
- active site: I27 (= I22), G29 (= G24), A30 (≠ E25), K31 (≠ E26), I32 (≠ N27), E52 (= E47), T75 (= T70), Q157 (≠ E159), L246 (≠ T248), 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 (= T122), Q204 (≠ R209), D431 (= D432), D458 (= D459), G460 (≠ Q461)
- binding pyruvic acid: G94 (≠ N89), R147 (≠ K149)
5dx6A Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
38% identity, 97% coverage: 2:531/547 of query aligns to 7:533/541 of 5dx6A
- active site: I27 (= I22), G29 (= G24), A30 (≠ E25), K31 (≠ E26), I32 (≠ N27), E52 (= E47), T75 (= T70), Q159 (≠ E159), L249 (≠ T248), 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 (= T122), D434 (= D432), D461 (= D459), G463 (≠ Q461)
6lpiB Crystal structure of ahas holo-enzyme (see paper)
32% identity, 92% coverage: 2:503/547 of query aligns to 7:501/539 of 6lpiB
- active site: I27 (= I22), G29 (= G24), G30 (≠ E25), S31 (≠ E26), I32 (≠ N27), E53 (= E47), C76 (≠ T70), F115 (≠ H109), Q116 (= Q110), E117 (≠ V111), K165 (≠ E159), M256 (≠ L251), A283 (vs. gap), V375 (= V379), G401 (≠ A405), M403 (= M407), D428 (= D432), N455 (≠ D459), A457 (≠ Q461), L458 (≠ Y462), L460 (= L464), V461 (≠ I465), Q464 (≠ K468)
- binding flavin-adenine dinucleotide: R155 (≠ K149), G212 (= G204), G213 (≠ N205), G214 (= G206), T236 (= T230), L237 (≠ F231), M238 (= M232), L254 (≠ A249), M256 (≠ L251), H257 (≠ Q252), G276 (= G271), A277 (vs. gap), R278 (vs. gap), D280 (= D273), R282 (vs. gap), A283 (vs. gap), D300 (= D294), I301 (≠ P295), D319 (= D313), V320 (≠ I314), M380 (= M384), G398 (≠ N402)
- binding magnesium ion: D428 (= D432), N455 (≠ D459)
- binding thiamine diphosphate: E53 (= E47), C76 (≠ T70), P79 (= P73), G376 (= G380), Q377 (≠ A381), H378 (= H382), G401 (≠ A405), M403 (= M407), G427 (= G431), D428 (= D432), G429 (≠ A433), S430 (≠ G434), M433 (= M437), N455 (≠ D459), A457 (≠ Q461), L458 (≠ Y462), G459 (= G463), L460 (= L464), V461 (≠ I465)
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)
29% 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 (≠ A207) 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: 2:531/547 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.
1t9bB Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron (see paper)
29% identity, 96% coverage: 1:527/547 of query aligns to 8:554/595 of 1t9bB
- active site: Y29 (≠ I22), G31 (= G24), G32 (≠ E25), A33 (≠ E26), I34 (≠ N27), E55 (= E47), T78 (= T70), F117 (≠ H109), Q118 (= Q110), E119 (≠ V111), K167 (≠ E159), R226 (≠ A214), M262 (≠ L251), V289 (vs. gap), V405 (= V379), L430 (≠ F404), G431 (≠ A405), M433 (= M407), D458 (= D432), N485 (≠ D459), E487 (≠ Q461), Q488 (≠ Y462), M490 (≠ L464), V491 (≠ I465), W494 (= W467), L516 (≠ Y489), G521 (= G494), L522 (≠ A495)
- binding 1-(2-chlorophenylsulfonyl)-3-(4-methoxy-6-methyl-l,3,5-triazin-2-yl)urea: V107 (≠ A99), P108 (≠ A100), D287 (vs. gap), R288 (vs. gap), M490 (≠ L464), W494 (= W467)
- binding flavin-adenine dinucleotide: R157 (≠ K149), G215 (= G204), A216 (≠ N205), G217 (= G206), N220 (vs. gap), T242 (= T230), L243 (≠ F231), Q244 (≠ M232), M259 (≠ T248), L260 (≠ A249), M262 (≠ L251), H263 (≠ Q252), G282 (= G271), A283 (vs. gap), R284 (vs. gap), D286 (= D273), R288 (vs. gap), V289 (vs. gap), E315 (≠ D294), V316 (≠ P295), N320 (≠ E299), G333 (= G312), D334 (= D313), A335 (≠ I314), Q409 (≠ K383), M410 (= M384), G428 (≠ N402), G429 (= G403)
- binding magnesium ion: D458 (= D432), N485 (≠ D459), E487 (≠ Q461)
Sites not aligning to the query:
1t9aA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, tribenuron methyl (see paper)
29% identity, 96% coverage: 1:527/547 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 (≠ H109), Q119 (= Q110), E120 (≠ V111), K168 (≠ E159), R228 (≠ A214), M264 (≠ L251), V291 (vs. gap), V407 (= V379), L432 (≠ F404), G433 (≠ A405), M435 (= M407), D460 (= D432), N487 (≠ D459), E489 (≠ Q461), Q490 (≠ Y462), M492 (≠ L464), 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 (≠ A99), P109 (≠ A100), F118 (≠ H109), K168 (≠ E159), M264 (≠ L251), D289 (vs. gap), R290 (vs. gap), M492 (≠ L464), V493 (≠ I465), W496 (= W467)
- binding flavin-adenine dinucleotide: R158 (≠ K149), G217 (= G204), A218 (≠ N205), G219 (= G206), N222 (vs. gap), T244 (= T230), L245 (≠ F231), Q246 (≠ M232), L262 (≠ A249), M264 (≠ L251), H265 (≠ Q252), G284 (= G271), A285 (vs. gap), R286 (vs. gap), D288 (= D273), R290 (vs. gap), V291 (vs. gap), E317 (≠ D294), V318 (≠ P295), N322 (≠ E299), G335 (= G312), D336 (= D313), A337 (≠ I314), Q411 (≠ K383), M412 (= M384), G430 (≠ N402), G431 (= G403)
- binding magnesium ion: D460 (= D432), N487 (≠ D459), E489 (≠ Q461)
- binding propyl trihydrogen diphosphate: V407 (= V379), G408 (= G380), Q409 (≠ A381), H410 (= H382), M435 (= M407), G459 (= G431), D460 (= D432), A461 (= A433), S462 (≠ G434), N487 (≠ D459), E489 (≠ Q461), Q490 (≠ Y462), G491 (= G463), M492 (≠ L464)
- 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:
1t9dA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
29% identity, 96% coverage: 1:527/547 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 (≠ H109), Q118 (= Q110), E119 (≠ V111), K167 (≠ E159), R227 (≠ A214), M263 (≠ L251), V290 (vs. gap), V406 (= V379), L431 (≠ F404), G432 (≠ A405), M434 (= M407), D459 (= D432), N486 (≠ D459), E488 (≠ Q461), Q489 (≠ Y462), M491 (≠ L464), 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 (≠ A99), P108 (≠ A100), F117 (≠ H109), K167 (≠ E159), M263 (≠ L251), D288 (vs. gap), R289 (vs. gap), W495 (= W467)
- binding flavin-adenine dinucleotide: R157 (≠ K149), G216 (= G204), A217 (≠ N205), G218 (= G206), N221 (vs. gap), T243 (= T230), L244 (≠ F231), Q245 (≠ M232), M260 (≠ T248), L261 (≠ A249), H264 (≠ Q252), G283 (= G271), A284 (vs. gap), R285 (vs. gap), D287 (= D273), R289 (vs. gap), V290 (vs. gap), E316 (≠ D294), V317 (≠ P295), N321 (≠ E299), G334 (= G312), D335 (= D313), A336 (≠ I314), Q410 (≠ K383), M411 (= M384), G429 (≠ N402), G430 (= G403)
- binding magnesium ion: D459 (= D432), N486 (≠ D459), E488 (≠ Q461)
- 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:
1n0hA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorimuron ethyl (see paper)
29% identity, 96% coverage: 1:527/547 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 (≠ H109), Q120 (= Q110), E121 (≠ V111), K169 (≠ E159), R230 (≠ A214), M266 (≠ L251), V293 (vs. gap), V409 (= V379), L434 (≠ F404), G435 (≠ A405), M437 (= M407), D462 (= D432), N489 (≠ D459), E491 (≠ Q461), Q492 (≠ Y462), M494 (≠ L464), 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 (= V379), G410 (= G380), Q411 (≠ A381), H412 (= H382), G435 (≠ A405), M437 (= M407), G461 (= G431), D462 (= D432), A463 (= A433), S464 (≠ G434), M467 (= M437), N489 (≠ D459), E491 (≠ Q461), Q492 (≠ Y462), 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 (≠ A99), P110 (≠ A100), F119 (≠ H109), K169 (≠ E159), M266 (≠ L251), D291 (vs. gap), R292 (vs. gap), V495 (≠ I465), W498 (= W467)
- binding flavin-adenine dinucleotide: R159 (≠ K149), G219 (= G204), A220 (≠ N205), G221 (= G206), N224 (vs. gap), T246 (= T230), L247 (≠ F231), Q248 (≠ M232), L264 (≠ A249), G265 (= G250), M266 (≠ L251), H267 (≠ Q252), G286 (= G271), A287 (vs. gap), R288 (vs. gap), D290 (= D273), R292 (vs. gap), V293 (vs. gap), E319 (≠ D294), V320 (≠ P295), N324 (≠ E299), G337 (= G312), D338 (= D313), A339 (≠ I314), M414 (= M384), G432 (≠ N402), G433 (= G403)
- binding magnesium ion: D462 (= D432), N489 (≠ D459), E491 (≠ Q461)
- binding thiamine diphosphate: Y31 (≠ I22), E57 (= E47), P83 (= P73)
Sites not aligning to the query:
1t9cA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, sulfometuron methyl (see paper)
29% identity, 96% coverage: 1:527/547 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 (≠ H109), Q118 (= Q110), E119 (≠ V111), K167 (≠ E159), R227 (≠ A214), M263 (≠ L251), V290 (vs. gap), V406 (= V379), L431 (≠ F404), G432 (≠ A405), M434 (= M407), D459 (= D432), N486 (≠ D459), E488 (≠ Q461), Q489 (≠ Y462), M491 (≠ L464), 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 (≠ A99), P108 (≠ A100), F117 (≠ H109), K167 (≠ E159), D288 (vs. gap), R289 (vs. gap), W495 (= W467)
- binding flavin-adenine dinucleotide: R157 (≠ K149), G216 (= G204), A217 (≠ N205), G218 (= G206), N221 (vs. gap), T243 (= T230), L244 (≠ F231), Q245 (≠ M232), L261 (≠ A249), M263 (≠ L251), H264 (≠ Q252), G283 (= G271), A284 (vs. gap), R285 (vs. gap), D287 (= D273), R289 (vs. gap), V290 (vs. gap), E316 (≠ D294), V317 (≠ P295), N321 (≠ E299), G334 (= G312), D335 (= D313), A336 (≠ I314), M411 (= M384), G429 (≠ N402), G430 (= G403)
- binding magnesium ion: D459 (= D432), N486 (≠ D459), E488 (≠ Q461)
Sites not aligning to the query:
6u9dB Saccharomyces cerevisiae acetohydroxyacid synthase (see paper)
29% identity, 96% coverage: 1:527/547 of query aligns to 12:566/607 of 6u9dB
- active site: Y33 (≠ I22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), I38 (≠ N27), E59 (= E47), T82 (= T70), F121 (≠ H109), Q122 (= Q110), E123 (≠ V111), K171 (≠ E159), M274 (≠ L251), V301 (vs. gap), V417 (= V379), G443 (≠ A405), M445 (= M407), D470 (= D432), N497 (≠ D459), E499 (≠ Q461), Q500 (≠ Y462), M502 (≠ L464), V503 (≠ I465), W506 (= W467)
- binding methyl 2-[(4,6-dimethoxypyrimidin-2-yl)carbamoylsulfamoylmethyl]benzoate: G36 (≠ E25), V111 (≠ A99), P112 (≠ A100), F121 (≠ H109), K171 (≠ E159), D299 (vs. gap), R300 (vs. gap), M502 (≠ L464), W506 (= W467)
- binding flavin-adenine dinucleotide: R161 (≠ K149), A228 (≠ N205), G229 (= G206), N232 (vs. gap), T254 (= T230), L255 (≠ F231), Q256 (≠ M232), L272 (≠ A249), M274 (≠ L251), G294 (= G271), R296 (vs. gap), D298 (= D273), R300 (vs. gap), V301 (vs. gap), E327 (≠ D294), V328 (≠ P295), N332 (≠ E299), D346 (= D313), A347 (≠ I314), M422 (= M384), G440 (≠ N402), G441 (= G403)
- binding magnesium ion: D470 (= D432), N497 (≠ D459)
- binding thiamine diphosphate: E59 (= E47), P85 (= P73), V417 (= V379), G418 (= G380), Q419 (≠ A381), H420 (= H382), G443 (≠ A405), M445 (= M407), A471 (= A433), S472 (≠ G434), N497 (≠ D459), E499 (≠ Q461), Q500 (≠ Y462), G501 (= G463), M502 (≠ L464), V503 (≠ I465)
P07342 Acetolactate synthase catalytic subunit, mitochondrial; Acetohydroxy-acid synthase catalytic subunit; AHAS; ALS; EC 2.2.1.6 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
29% identity, 96% coverage: 1:527/547 of query aligns to 92:646/687 of P07342
- R241 (≠ K149) binding FAD
- 355:376 (vs. 252:271, 27% identical) binding FAD
- 407:426 (vs. 294:313, 20% identical) binding FAD
5wkcA Saccharomyces cerevisiae acetohydroxyacid synthase in complex with the herbicide penoxsulam (see paper)
29% identity, 96% coverage: 1:527/547 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 (≠ H109), Q118 (= Q110), E119 (≠ V111), K167 (≠ E159), R222 (≠ A214), M258 (≠ L251), V285 (vs. gap), V401 (= V379), L426 (≠ F404), G427 (≠ A405), M429 (= M407), D454 (= D432), N481 (≠ D459), E483 (≠ Q461), Q484 (≠ Y462), M486 (≠ L464), 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 (= V379), G402 (= G380), Q403 (≠ A381), H404 (= H382), G427 (≠ A405), M429 (= M407), G453 (= G431), D454 (= D432), A455 (= A433), S456 (≠ G434), M459 (= M437), N481 (≠ D459), E483 (≠ Q461), Q484 (≠ Y462), G485 (= G463), M486 (≠ L464), V487 (≠ I465)
- binding ethaneperoxoic acid: G32 (≠ E25), Q118 (= Q110)
- binding flavin-adenine dinucleotide: R157 (≠ K149), G211 (= G204), A212 (≠ N205), G213 (= G206), N216 (vs. gap), T238 (= T230), L239 (≠ F231), Q240 (≠ M232), L256 (≠ A249), M258 (≠ L251), G278 (= G271), A279 (vs. gap), R280 (vs. gap), R284 (vs. gap), V285 (vs. gap), E311 (≠ D294), V312 (≠ P295), N316 (≠ E299), D330 (= D313), A331 (≠ I314), M406 (= M384), G424 (≠ N402)
- binding magnesium ion: D454 (= D432), N481 (≠ D459), E483 (≠ Q461)
- 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 (≠ A99), F117 (≠ H109), K167 (≠ E159), M258 (≠ L251), R284 (vs. gap), M486 (≠ L464), 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:
Query Sequence
>WP_013836184.1 NCBI__GCF_000214825.1:WP_013836184.1
MNAAQLFVKCLENEQVEFIFGIPGEENLDLVDALLDSEIRFITTRHEQGAAFMADVYGRL
TGKAGVCLSTLGPGATNLVTGVADANMDNAPLVAIAGQAATTRMHKESHQVVDLVSMFKP
ITKYATQILEPDTVPEVVRKAFKIAQTEKPGASFIDFPENIAEMATLSQPLPVKHSRPTT
ASEKLIKEAVLAIQSAESPLILVGNGAIRANASAQVYALAKQRNIPTVNTFMAKGVVPFF
KNATAMGTAGLQKGDYENGGFSKADLVICIGFDMVEYHPHLWNPRHQHRIIHIDPLPAEV
DASYLPEIELIGDIASNLLQLSAMLNTRANFPLDHPLRDATMAEMNRCKVSQDFPLLPQK
IIWDLRTAMKSNDIAICDVGAHKMWIARMFRAEKPNTCIISNGFAGMGIAVPGAIAAKLA
MPNRAVVAVTGDAGFMMNSQEIETALRCETPIVILIWNDSQYGLIEWKQTRKYGRAAYID
FKNPDFVQYAQSFGAKGYRINQADELLPTLEQALKDNTVSVIDCPVDYSQNDRLTQLLGS
VITEMHD
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