SitesBLAST
Comparing WP_011383235.1 NCBI__GCF_000009985.1:WP_011383235.1 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)
8rpjA Janthe from janthinobacterium sp. Hh01
34% identity, 96% coverage: 1:590/613 of query aligns to 4:595/605 of 8rpjA
- binding flavin-adenine dinucleotide: R159 (= R156), G219 (= G217), N220 (≠ G218), G221 (= G219), A225 (= A223), S245 (≠ T243), W246 (= W244), A247 (≠ N245), A263 (≠ I261), G264 (= G262), Y266 (= Y264), G285 (= G283), T286 (≠ S284), R287 (= R285), P291 (≠ R289), Q292 (≠ I290), D310 (= D308), I311 (≠ V309), D330 (= D330), A331 (= A331), T427 (≠ N428)
- binding magnesium ion: D457 (= D458), N484 (= N485), G486 (≠ I487)
- binding thiamine diphosphate: I26 (≠ Y23), E51 (= E48), G405 (= G406), T406 (≠ G407), M432 (= M433), C456 (≠ G457), G458 (= G459), G459 (= G460), N484 (= N485), G486 (≠ I487), Y487 (= Y488), L488 (≠ G489), M489 (≠ I490), I490 (≠ T491)
8rpiA Janthe from janthinobacterium sp. Hh01, lactyl-thdp
34% identity, 96% coverage: 1:590/613 of query aligns to 4:595/605 of 8rpiA
- binding flavin-adenine dinucleotide: R159 (= R156), G219 (= G217), N220 (≠ G218), G221 (= G219), A225 (= A223), S245 (≠ T243), W246 (= W244), A247 (≠ N245), A263 (≠ I261), G264 (= G262), Y266 (= Y264), G285 (= G283), T286 (≠ S284), R287 (= R285), P291 (≠ R289), Q292 (≠ I290), D310 (= D308), I311 (≠ V309), D330 (= D330), A331 (= A331), T427 (≠ N428)
- binding magnesium ion: D457 (= D458), N484 (= N485), G486 (≠ I487)
- 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: A28 (= A25), E51 (= E48), G405 (= G406), T406 (≠ G407), M432 (= M433), C456 (≠ G457), G458 (= G459), G459 (= G460), N484 (= N485), G486 (≠ I487), Y487 (= Y488), L488 (≠ G489), M489 (≠ I490), I490 (≠ T491)
8rphD Thiamine pyrophosphate-binding protein
34% identity, 96% coverage: 1:590/613 of query aligns to 4:598/608 of 8rphD
- binding (2~{S})-2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-4-methyl-5-[2-[oxidanyl(phosphonooxy)phosphoryl]oxyethyl]-1,3-thiazol-2-yl]-2-oxidanyl-butanoic acid: I26 (≠ Y23), E51 (= E48), G405 (= G406), T406 (≠ G407), G430 (≠ S431), M432 (= M433), C456 (≠ G457), G458 (= G459), G459 (= G460), N484 (= N485), G486 (≠ I487), Y487 (= Y488), L488 (≠ G489), M489 (≠ I490), I490 (≠ T491)
- binding flavin-adenine dinucleotide: R159 (= R156), G219 (= G217), N220 (≠ G218), G221 (= G219), S245 (≠ T243), W246 (= W244), A247 (≠ N245), A263 (≠ I261), G264 (= G262), Y266 (= Y264), G285 (= G283), T286 (≠ S284), R287 (= R285), P291 (≠ R289), Q292 (≠ I290), D310 (= D308), I311 (≠ V309), D330 (= D330), A331 (= A331), T427 (≠ N428)
- binding magnesium ion: D457 (= D458), N484 (= N485), G486 (≠ I487)
5ahkA Crystal structure of acetohydroxy acid synthase pf5 from pseudomonas protegens
33% identity, 92% coverage: 1:566/613 of query aligns to 1:543/555 of 5ahkA
- active site: L22 (≠ V22), G24 (= G24), G25 (≠ A25), M26 (≠ A26), I27 (≠ N27), E48 (= E48), T73 (= T71), K110 (≠ D108), R111 (≠ P109), F118 (= F116), Q119 (= Q117), M168 (≠ L166), A253 (≠ T263), Q280 (≠ I290), V384 (≠ C405), G410 (≠ S431), M412 (= M433), D436 (= D458), N463 (= N485), S465 (≠ I487), L466 (≠ Y488), M468 (≠ I490), V469 (≠ T491), F472 (≠ Y494), D535 (≠ E558)
- binding flavin-adenine dinucleotide: R158 (= R156), G208 (= G217), G209 (= G218), G210 (= G219), S234 (≠ T243), L235 (≠ W244), M250 (≠ R260), L251 (≠ I261), Y254 (= Y264), G273 (= G283), S274 (= S284), R275 (= R285), D277 (≠ S287), R279 (= R289), Q280 (≠ I290), D298 (≠ H317), L299 (= L318), Q303 (≠ P322), E317 (≠ F334), L318 (= L335), M389 (≠ V410), G407 (≠ N428)
- binding magnesium ion: D436 (= D458), N463 (= N485), S465 (≠ I487)
- binding thiamine diphosphate: I23 (≠ Y23), E48 (= E48), P76 (= P74), V384 (≠ C405), G385 (= G406), N386 (≠ G407), N387 (= N408), G410 (≠ S431), M412 (= M433), D436 (= D458), G437 (= G459), G438 (= G460), N463 (= N485), S465 (≠ I487), L466 (≠ Y488), G467 (= G489), M468 (≠ I490), V469 (≠ T491)
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, 91% coverage: 2:560/613 of query aligns to 95:643/667 of P09342
- C161 (≠ T68) modified: Disulfide link with 307
- P194 (≠ N101) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ V220) 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)
30% identity, 91% coverage: 2:560/613 of query aligns to 92:640/664 of P09114
- P191 (≠ N101) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
- W568 (≠ Y494) mutation to L: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191.
1n0hA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorimuron ethyl (see paper)
30% identity, 91% coverage: 11:568/613 of query aligns to 20:569/599 of 1n0hA
- active site: Y31 (≠ V22), G33 (= G24), G34 (≠ A25), A35 (= A26), I36 (≠ N27), E57 (= E48), T80 (= T71), F119 (= F116), Q120 (= Q117), E121 (= E118), K169 (≠ L166), R230 (≠ D227), M266 (≠ T263), V293 (≠ I290), V409 (vs. gap), L434 (≠ N430), G435 (≠ S431), M437 (= M433), D462 (= D458), N489 (= N485), E491 (≠ I487), Q492 (≠ Y488), M494 (≠ I490), V495 (≠ T491), W498 (≠ Y494), L520 (≠ I519), G525 (= G524), L526 (≠ V525), K559 (≠ E558)
- binding 4-{[(4'-amino-2'-methylpyrimidin-5'-yl)methyl]amino}pent-3-enyl diphosphate: V409 (vs. gap), G410 (vs. gap), Q411 (vs. gap), H412 (vs. gap), G435 (≠ S431), M437 (= M433), G461 (= G457), D462 (= D458), A463 (≠ G459), S464 (≠ G460), M467 (= M463), N489 (= N485), E491 (≠ I487), Q492 (≠ Y488), G493 (= G489), V495 (≠ T491)
- binding 2-[[[[(4-chloro-6-methoxy-2-pyrimidinyl)amino]carbonyl]amino]sulfonyl]benzoic acid ethyl ester: G34 (≠ A25), A35 (= A26), V109 (≠ I100), P110 (= P107), F119 (= F116), K169 (≠ L166), M266 (≠ T263), D291 (≠ G288), R292 (= R289), V495 (≠ T491), W498 (≠ Y494)
- binding flavin-adenine dinucleotide: R159 (= R156), G219 (= G217), A220 (≠ G218), G221 (= G219), N224 (≠ R221), T246 (= T243), L247 (≠ W244), Q248 (≠ N245), L264 (≠ I261), G265 (= G262), M266 (≠ T263), H267 (≠ Y264), G286 (= G283), A287 (≠ S284), R288 (= R285), D290 (≠ S287), R292 (= R289), V293 (≠ I290), E319 (≠ Q319), V320 (≠ Q320), N324 (≠ D324), G337 (≠ C329), D338 (= D330), A339 (= A331), M414 (vs. gap), G432 (≠ N428), G433 (= G429)
- binding magnesium ion: D462 (= D458), N489 (= N485), E491 (≠ I487)
- binding thiamine diphosphate: Y31 (≠ V22), E57 (= E48), P83 (= P74)
1t9dA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
30% identity, 91% coverage: 11:568/613 of query aligns to 18:566/596 of 1t9dA
- active site: Y29 (≠ V22), G31 (= G24), G32 (≠ A25), A33 (= A26), I34 (≠ N27), E55 (= E48), T78 (= T71), F117 (= F116), Q118 (= Q117), E119 (= E118), K167 (≠ L166), R227 (≠ D227), M263 (≠ T263), V290 (≠ I290), V406 (vs. gap), L431 (≠ N430), G432 (≠ S431), M434 (= M433), D459 (= D458), N486 (= N485), E488 (≠ I487), Q489 (≠ Y488), M491 (≠ I490), V492 (≠ T491), W495 (≠ Y494), L517 (≠ I519), G522 (= G524), L523 (≠ V525), K556 (≠ E558)
- binding methyl 2-[({[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (≠ A25), A33 (= A26), V107 (≠ I100), P108 (= P107), F117 (= F116), K167 (≠ L166), M263 (≠ T263), D288 (≠ G288), R289 (= R289), W495 (≠ Y494)
- binding flavin-adenine dinucleotide: R157 (= R156), G216 (= G217), A217 (≠ G218), G218 (= G219), N221 (≠ R221), T243 (= T243), L244 (≠ W244), Q245 (≠ N245), M260 (≠ R260), L261 (≠ I261), H264 (≠ Y264), G283 (= G283), A284 (≠ S284), R285 (= R285), D287 (≠ S287), R289 (= R289), V290 (≠ I290), E316 (≠ Q319), V317 (≠ Q320), N321 (≠ D324), G334 (≠ C329), D335 (= D330), A336 (= A331), Q410 (vs. gap), M411 (vs. gap), G429 (≠ N428), G430 (= G429)
- binding magnesium ion: D459 (= D458), N486 (= N485), E488 (≠ I487)
- binding 2,5-dimethyl-pyrimidin-4-ylamine: E55 (= E48), P81 (= P74), Q118 (= Q117), G432 (≠ S431), M434 (= M433), M464 (= M463)
1t9aA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, tribenuron methyl (see paper)
30% identity, 91% coverage: 11:568/613 of query aligns to 19:567/597 of 1t9aA
- active site: Y30 (≠ V22), G32 (= G24), G33 (≠ A25), A34 (= A26), I35 (≠ N27), E56 (= E48), T79 (= T71), F118 (= F116), Q119 (= Q117), E120 (= E118), K168 (≠ L166), R228 (≠ D227), M264 (≠ T263), V291 (≠ I290), V407 (vs. gap), L432 (≠ N430), G433 (≠ S431), M435 (= M433), D460 (= D458), N487 (= N485), E489 (≠ I487), Q490 (≠ Y488), M492 (≠ I490), V493 (≠ T491), W496 (≠ Y494), L518 (≠ I519), G523 (= G524), L524 (≠ V525), K557 (≠ E558)
- binding methyl 2-[4-methoxy-6-methyl-1,3,5-trazin-2-yl(methyl)carbamoylsulfamoyl]benzoate: G33 (≠ A25), V108 (≠ I100), P109 (= P107), F118 (= F116), K168 (≠ L166), M264 (≠ T263), D289 (≠ G288), R290 (= R289), M492 (≠ I490), V493 (≠ T491), W496 (≠ Y494)
- binding flavin-adenine dinucleotide: R158 (= R156), G217 (= G217), A218 (≠ G218), G219 (= G219), N222 (≠ R221), T244 (= T243), L245 (≠ W244), Q246 (≠ N245), L262 (≠ I261), M264 (≠ T263), H265 (≠ Y264), G284 (= G283), A285 (≠ S284), R286 (= R285), D288 (≠ S287), R290 (= R289), V291 (≠ I290), E317 (≠ Q319), V318 (≠ Q320), N322 (≠ D324), G335 (≠ C329), D336 (= D330), A337 (= A331), Q411 (vs. gap), M412 (vs. gap), G430 (≠ N428), G431 (= G429)
- binding magnesium ion: D460 (= D458), N487 (= N485), E489 (≠ I487)
- binding propyl trihydrogen diphosphate: V407 (vs. gap), G408 (vs. gap), Q409 (vs. gap), H410 (vs. gap), M435 (= M433), G459 (= G457), D460 (= D458), A461 (≠ G459), S462 (≠ G460), N487 (= N485), E489 (≠ I487), Q490 (≠ Y488), G491 (= G489), M492 (≠ I490)
- binding 5-{[ethyl(methyl)amino]methyl}-2-methyl-5,6-dihydropyrimidin-4-amine: G433 (≠ S431), M435 (= M433), M465 (= M463)
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, 91% coverage: 11:568/613 of query aligns to 102:657/687 of P07342
- R241 (= R156) binding
- 355:376 (vs. 264:285, 50% identical) binding
- 407:426 (vs. 319:330, 20% identical) binding
6u9dB Saccharomyces cerevisiae acetohydroxyacid synthase (see paper)
29% identity, 91% coverage: 11:568/613 of query aligns to 22:577/607 of 6u9dB
- active site: Y33 (≠ V22), G35 (= G24), G36 (≠ A25), A37 (= A26), I38 (≠ N27), E59 (= E48), T82 (= T71), F121 (= F116), Q122 (= Q117), E123 (= E118), K171 (≠ L166), M274 (≠ T263), V301 (≠ I290), V417 (vs. gap), G443 (≠ S431), M445 (= M433), D470 (= D458), N497 (= N485), E499 (≠ I487), Q500 (≠ Y488), M502 (≠ I490), V503 (≠ T491), W506 (≠ Y494)
- binding methyl 2-[(4,6-dimethoxypyrimidin-2-yl)carbamoylsulfamoylmethyl]benzoate: G36 (≠ A25), V111 (≠ I100), P112 (= P107), F121 (= F116), K171 (≠ L166), D299 (≠ G288), R300 (= R289), M502 (≠ I490), W506 (≠ Y494)
- binding flavin-adenine dinucleotide: R161 (= R156), A228 (≠ G218), G229 (= G219), N232 (≠ R221), T254 (= T243), L255 (≠ W244), Q256 (≠ N245), L272 (≠ I261), M274 (≠ T263), G294 (= G283), R296 (= R285), D298 (≠ S287), R300 (= R289), V301 (≠ I290), E327 (≠ Q319), V328 (≠ Q320), N332 (≠ D324), D346 (= D330), A347 (= A331), M422 (vs. gap), G440 (≠ N428), G441 (= G429)
- binding magnesium ion: D470 (= D458), N497 (= N485)
- binding thiamine diphosphate: E59 (= E48), P85 (= P74), V417 (vs. gap), G418 (vs. gap), Q419 (vs. gap), H420 (vs. gap), G443 (≠ S431), M445 (= M433), A471 (≠ G459), S472 (≠ G460), N497 (= N485), E499 (≠ I487), Q500 (≠ Y488), G501 (= G489), M502 (≠ I490), V503 (≠ T491)
1t9cA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, sulfometuron methyl (see paper)
29% identity, 91% coverage: 11:568/613 of query aligns to 18:566/596 of 1t9cA
- active site: Y29 (≠ V22), G31 (= G24), G32 (≠ A25), A33 (= A26), I34 (≠ N27), E55 (= E48), T78 (= T71), F117 (= F116), Q118 (= Q117), E119 (= E118), K167 (≠ L166), R227 (≠ D227), M263 (≠ T263), V290 (≠ I290), V406 (vs. gap), L431 (≠ N430), G432 (≠ S431), M434 (= M433), D459 (= D458), N486 (= N485), E488 (≠ I487), Q489 (≠ Y488), M491 (≠ I490), V492 (≠ T491), W495 (≠ Y494), L517 (≠ I519), G522 (= G524), L523 (≠ V525), K556 (≠ E558)
- binding methyl 2-[({[(4,6-dimethylpyrimidin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (≠ A25), V107 (≠ I100), P108 (= P107), F117 (= F116), K167 (≠ L166), D288 (≠ G288), R289 (= R289), W495 (≠ Y494)
- binding flavin-adenine dinucleotide: R157 (= R156), G216 (= G217), A217 (≠ G218), G218 (= G219), N221 (≠ R221), T243 (= T243), L244 (≠ W244), Q245 (≠ N245), L261 (≠ I261), M263 (≠ T263), H264 (≠ Y264), G283 (= G283), A284 (≠ S284), R285 (= R285), D287 (≠ S287), R289 (= R289), V290 (≠ I290), E316 (≠ Q319), V317 (≠ Q320), N321 (≠ D324), G334 (≠ C329), D335 (= D330), A336 (= A331), M411 (vs. gap), G429 (≠ N428), G430 (= G429)
- binding magnesium ion: D459 (= D458), N486 (= N485), E488 (≠ I487)
5wkcA Saccharomyces cerevisiae acetohydroxyacid synthase in complex with the herbicide penoxsulam (see paper)
29% identity, 91% coverage: 11:568/613 of query aligns to 18:561/591 of 5wkcA
- active site: Y29 (≠ V22), G31 (= G24), G32 (≠ A25), A33 (= A26), I34 (≠ N27), E55 (= E48), T78 (= T71), F117 (= F116), Q118 (= Q117), E119 (= E118), K167 (≠ L166), R222 (≠ D227), M258 (≠ T263), V285 (≠ I290), V401 (vs. gap), L426 (≠ N430), G427 (≠ S431), M429 (= M433), D454 (= D458), N481 (= N485), E483 (≠ I487), Q484 (≠ Y488), M486 (≠ I490), V487 (≠ T491), W490 (≠ Y494), L512 (≠ I519), G517 (= G524), L518 (≠ V525), K551 (≠ E558)
- 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 (vs. gap), G402 (vs. gap), Q403 (vs. gap), H404 (vs. gap), G427 (≠ S431), M429 (= M433), G453 (= G457), D454 (= D458), A455 (≠ G459), S456 (≠ G460), M459 (= M463), N481 (= N485), E483 (≠ I487), Q484 (≠ Y488), G485 (= G489), M486 (≠ I490), V487 (≠ T491)
- binding ethaneperoxoic acid: G32 (≠ A25), Q118 (= Q117)
- binding flavin-adenine dinucleotide: R157 (= R156), G211 (= G217), A212 (≠ G218), G213 (= G219), N216 (≠ R221), T238 (= T243), L239 (≠ W244), Q240 (≠ N245), L256 (≠ I261), M258 (≠ T263), G278 (= G283), A279 (≠ S284), R280 (= R285), R284 (= R289), V285 (≠ I290), E311 (≠ Q319), V312 (≠ Q320), N316 (≠ D324), D330 (= D330), A331 (= A331), M406 (vs. gap), G424 (≠ N428)
- binding magnesium ion: D454 (= D458), N481 (= N485), E483 (≠ I487)
- binding 2-(2,2-difluoroethoxy)-N-(5,8-dimethoxy[1,2,4]triazolo[1,5-c]pyrimidin-2-yl)-6-(trifluoromethyl)benzenesulfonamide: G32 (≠ A25), A33 (= A26), V107 (≠ I100), F117 (= F116), K167 (≠ L166), M258 (≠ T263), R284 (= R289), M486 (≠ I490), W490 (≠ Y494)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: P30 (≠ Y23), E55 (= E48)
1t9bB Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron (see paper)
29% identity, 91% coverage: 11:568/613 of query aligns to 18:565/595 of 1t9bB
- active site: Y29 (≠ V22), G31 (= G24), G32 (≠ A25), A33 (= A26), I34 (≠ N27), E55 (= E48), T78 (= T71), F117 (= F116), Q118 (= Q117), E119 (= E118), K167 (≠ L166), R226 (≠ D227), M262 (≠ T263), V289 (≠ I290), V405 (vs. gap), L430 (≠ N430), G431 (≠ S431), M433 (= M433), D458 (= D458), N485 (= N485), E487 (≠ I487), Q488 (≠ Y488), M490 (≠ I490), V491 (≠ T491), W494 (≠ Y494), L516 (≠ I519), G521 (= G524), L522 (≠ V525), K555 (≠ E558)
- binding 1-(2-chlorophenylsulfonyl)-3-(4-methoxy-6-methyl-l,3,5-triazin-2-yl)urea: V107 (≠ I100), P108 (= P107), D287 (≠ G288), R288 (= R289), M490 (≠ I490), W494 (≠ Y494)
- binding flavin-adenine dinucleotide: R157 (= R156), G215 (= G217), A216 (≠ G218), G217 (= G219), N220 (≠ R221), T242 (= T243), L243 (≠ W244), Q244 (≠ N245), M259 (≠ R260), L260 (≠ I261), M262 (≠ T263), H263 (≠ Y264), G282 (= G283), A283 (≠ S284), R284 (= R285), D286 (≠ S287), R288 (= R289), V289 (≠ I290), E315 (≠ Q319), V316 (≠ Q320), N320 (≠ D324), G333 (≠ C329), D334 (= D330), A335 (= A331), Q409 (vs. gap), M410 (vs. gap), G428 (≠ N428), G429 (= G429)
- binding magnesium ion: D458 (= D458), N485 (= N485), E487 (≠ I487)
7tzzA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase p197t mutant in complex with bispyribac-sodium (see paper)
29% identity, 91% coverage: 2:560/613 of query aligns to 13:561/582 of 7tzzA
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: M266 (≠ T263), R292 (= R289), W489 (≠ Y494)
- 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 (≠ C405), G401 (= G406), Q402 (≠ G407), H403 (≠ N408), G426 (≠ S431), M428 (= M433), G452 (= G457), D453 (= D458), G454 (= G459), S455 (≠ G460), L483 (≠ Y488), G484 (= G489), M485 (≠ I490), V486 (≠ T491)
- binding flavin-adenine dinucleotide: R161 (= R156), G222 (= G217), G223 (= G218), G224 (= G219), T246 (= T243), L247 (≠ W244), M248 (≠ N245), M263 (≠ R260), L264 (≠ I261), M266 (≠ T263), H267 (≠ Y264), G286 (= G283), R288 (= R285), V293 (≠ I290), D310 (= D308), I311 (≠ V309), D329 (= D330), V330 (≠ A331), M405 (≠ V410), G423 (≠ N428)
- binding magnesium ion: A37 (= A26), T82 (= T71), S83 (= S72), Q122 (= Q117), Y381 (≠ A386), D453 (= D458), M458 (= M463), Q461 (= Q466), N480 (= N485), H482 (≠ I487), K533 (≠ Q533)
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)
29% identity, 91% coverage: 2:561/613 of query aligns to 98:647/670 of P17597
- A122 (= A26) mutation to V: Reduced catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- M124 (≠ G28) 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 (= E48) binding
- S186 (= S90) binding
- P197 (≠ N101) mutation to S: In csr1-1/GH50; resistant to sulfonylurea but not to imidazolinone herbicides.
- R199 (≠ Q103) mutation R->A,E: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- Q207 (= Q117) binding
- K220 (= K130) binding
- R246 (= R156) binding ; binding
- K256 (≠ L166) binding
- G308 (= G218) binding
- TL 331:332 (≠ TW 243:244) binding
- C340 (≠ S252) modified: Cysteine sulfinic acid (-SO2H)
- LGMH 349:352 (≠ IGTY 261:264) binding
- GVRFD 371:375 (≠ GSRIS 283:287) binding
- DR 376:377 (≠ GR 288:289) binding
- DI 395:396 (≠ DV 308:309) binding
- DV 414:415 (≠ DA 330:331) binding
- QH 487:488 (≠ GN 407:408) binding
- GG 508:509 (≠ NG 428:429) binding
- GAM 511:513 (≠ SPM 431:433) binding
- D538 (= D458) binding
- DGS 538:540 (≠ DGG 458:460) binding
- N565 (= N485) binding
- NQHLGM 565:570 (≠ NHIYGI 485:490) binding
- H567 (≠ I487) binding
- W574 (≠ Y494) 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)
29% identity, 91% coverage: 2:561/613 of query aligns to 13:562/585 of 5k2oA
- active site: Y33 (≠ V22), G35 (= G24), G36 (≠ A25), A37 (= A26), S38 (≠ N27), E59 (= E48), T82 (= T71), F121 (= F116), Q122 (= Q117), E123 (= E118), K171 (≠ L166), M266 (≠ T263), V293 (≠ I290), V400 (≠ C405), G426 (≠ S431), M428 (= M433), D453 (= D458), N480 (= N485), H482 (≠ I487), L483 (≠ Y488), M485 (≠ I490), V486 (≠ T491), W489 (≠ Y494), H558 (= H557)
- binding 2-chloranyl-6-(4,6-dimethoxypyrimidin-2-yl)sulfanyl-benzoic acid: M266 (≠ T263), R292 (= R289), W489 (≠ Y494)
- binding flavin-adenine dinucleotide: R161 (= R156), G222 (= G217), G223 (= G218), G224 (= G219), T246 (= T243), L247 (≠ W244), M248 (≠ N245), L264 (≠ I261), G286 (= G283), R288 (= R285), D290 (≠ S287), V293 (≠ I290), D310 (= D308), I311 (≠ V309), D329 (= D330), V330 (≠ A331), Q404 (≠ I409), M405 (≠ V410), G423 (≠ N428)
- binding magnesium ion: D453 (= D458), N480 (= N485), H482 (≠ I487)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (≠ C405), G401 (= G406), Q402 (≠ G407), H403 (≠ N408), M428 (= M433), D453 (= D458), G454 (= G459), S455 (≠ G460), N480 (= N485), H482 (≠ I487), L483 (≠ Y488), G484 (= G489), M485 (≠ I490), V486 (≠ T491)
Sites not aligning to the query:
6desA Crystal structure of candida albicans acetohydroxyacid synthase in complex with the herbicide propoxycarbazone (see paper)
28% identity, 90% coverage: 4:554/613 of query aligns to 15:554/598 of 6desA
- active site: Y33 (≠ V22), G35 (= G24), G36 (≠ A25), A37 (= A26), I38 (≠ N27), E59 (= E48), T82 (= T71), F121 (= F116), Q122 (= Q117), E123 (= E118), K171 (≠ L166), K229 (≠ D228), M265 (≠ T263), V292 (≠ I290), V408 (≠ C405), L433 (≠ N430), G434 (≠ S431), M436 (= M433), D461 (= D458), N488 (= N485), E490 (≠ I487), Q491 (≠ Y488), M493 (≠ I490), V494 (≠ T491), W497 (≠ Y494), L519 (≠ I519), N524 (≠ G524), V525 (= V525)
- binding methyl 2-[(4-methyl-5-oxidanylidene-3-propoxy-1,2,4-triazol-1-yl)carbonylsulfamoyl]benzoate: M265 (≠ T263), D290 (≠ G288), R291 (= R289), W497 (≠ Y494)
- binding flavin-adenine dinucleotide: R161 (= R156), G218 (= G217), A219 (≠ G218), G220 (= G219), N223 (≠ L222), T245 (= T243), L246 (≠ W244), Q247 (≠ N245), L263 (≠ I261), G285 (= G283), A286 (≠ S284), R287 (= R285), D289 (≠ S287), R291 (= R289), V292 (≠ I290), E318 (≠ Q319), I319 (≠ Q320), N323 (≠ D324), D337 (≠ R337), V338 (≠ L338), Q412 (≠ I409), M413 (≠ V410), G431 (≠ N428)
- binding magnesium ion: D461 (= D458), N488 (= N485), E490 (≠ I487)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: V408 (≠ C405), G409 (= G406), Q410 (≠ G407), H411 (≠ N408), G434 (≠ S431), M436 (= M433), G460 (= G457), D461 (= D458), A462 (≠ G459), S463 (≠ G460), N488 (= N485), E490 (≠ I487), Q491 (≠ Y488), G492 (= G489), M493 (≠ I490), V494 (≠ T491)
6depA Crystal structure of candida albicans acetohydroxyacid synthase in complex with the herbicide sulfometuron methyl (see paper)
28% identity, 90% coverage: 4:554/613 of query aligns to 15:554/598 of 6depA
- active site: Y33 (≠ V22), G35 (= G24), G36 (≠ A25), A37 (= A26), I38 (≠ N27), E59 (= E48), T82 (= T71), F121 (= F116), Q122 (= Q117), E123 (= E118), K171 (≠ L166), K229 (≠ D228), M265 (≠ T263), V292 (≠ I290), V408 (≠ C405), L433 (≠ N430), G434 (≠ S431), M436 (= M433), D461 (= D458), N488 (= N485), E490 (≠ I487), Q491 (≠ Y488), M493 (≠ I490), V494 (≠ T491), W497 (≠ Y494), L519 (≠ I519), N524 (≠ G524), V525 (= V525)
- binding methyl 2-[({[(4,6-dimethylpyrimidin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: D290 (≠ G288), R291 (= R289), M493 (≠ I490), W497 (≠ Y494)
- binding flavin-adenine dinucleotide: R161 (= R156), G218 (= G217), A219 (≠ G218), G220 (= G219), N223 (≠ L222), T245 (= T243), L246 (≠ W244), Q247 (≠ N245), L263 (≠ I261), G264 (= G262), G285 (= G283), A286 (≠ S284), R287 (= R285), D289 (≠ S287), R291 (= R289), V292 (≠ I290), E318 (≠ Q319), I319 (≠ Q320), N323 (≠ D324), D337 (≠ R337), V338 (≠ L338), M413 (≠ V410), G431 (≠ N428)
- binding magnesium ion: D461 (= D458), N488 (= N485), E490 (≠ I487)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V408 (≠ C405), G409 (= G406), Q410 (≠ G407), H411 (≠ N408), G434 (≠ S431), M436 (= M433), G460 (= G457), D461 (= D458), A462 (≠ G459), S463 (≠ G460), M466 (= M463), N488 (= N485), E490 (≠ I487), Q491 (≠ Y488), G492 (= G489), M493 (≠ I490), V494 (≠ T491)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: V408 (≠ C405), G409 (= G406), Q410 (≠ G407), H411 (≠ N408), G434 (≠ S431), M436 (= M433), G460 (= G457), D461 (= D458), A462 (≠ G459), S463 (≠ G460), M466 (= M463), N488 (= N485), E490 (≠ I487), Q491 (≠ Y488), G492 (= G489), M493 (≠ I490), V494 (≠ T491)
3ea4A Arabidopsis thaliana acetohydroxyacid synthase in complex with monosulfuron-ester (see paper)
29% identity, 91% coverage: 2:561/613 of query aligns to 12:561/582 of 3ea4A
- active site: Y32 (≠ V22), G34 (= G24), G35 (≠ A25), A36 (= A26), S37 (≠ N27), E58 (= E48), T81 (= T71), F120 (= F116), Q121 (= Q117), E122 (= E118), K170 (≠ L166), M265 (≠ T263), V292 (≠ I290), V399 (≠ C405), G425 (≠ S431), M427 (= M433), D452 (= D458), N479 (= N485), H481 (≠ I487), L482 (≠ Y488), M484 (≠ I490), V485 (≠ T491), W488 (≠ Y494), H557 (= H557)
- binding methyl 2-{[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl}benzoate: D290 (≠ G288), R291 (= R289), W488 (≠ Y494)
- binding flavin-adenine dinucleotide-n5-isobutyl ketone: R160 (= R156), G221 (= G217), G222 (= G218), G223 (= G219), T245 (= T243), L246 (≠ W244), M247 (≠ N245), L263 (≠ I261), G264 (= G262), M265 (≠ T263), H266 (≠ Y264), G285 (= G283), R287 (= R285), D289 (≠ S287), R291 (= R289), D309 (= D308), I310 (≠ V309), G327 (≠ C329), D328 (= D330), V329 (≠ A331), M404 (≠ V410), G422 (≠ N428)
- binding magnesium ion: D452 (= D458), N479 (= N485), H481 (≠ I487)
- 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 (≠ C405), G400 (= G406), Q401 (≠ G407), H402 (≠ N408), M427 (= M433), G451 (= G457), D452 (= D458), G453 (= G459), S454 (≠ G460), N479 (= N485), H481 (≠ I487), L482 (≠ Y488), G483 (= G489), M484 (≠ I490), V485 (≠ T491)
Sites not aligning to the query:
Query Sequence
>WP_011383235.1 NCBI__GCF_000009985.1:WP_011383235.1
MKVGDYVINRLAEEGIDKIFVVYGAANGDLIDAFTRTNKTEYVATMHEQGGGFAAEAYAK
IKGIPGATIATSGPGGQNLLTSMGNCFYDSIPCVFMTGQINSQFLRPDPSIRQVGFQETD
IVGMAKPVTKYAKMITSAAEIRYEVEKALFIAKEGRPGPVLLDIPLNIQKQDIDPDKLFG
FDTVAAQRSWNLDAVDAAIDTYLADLAKSKRPTIMVGGGVRLANAVDDLVELGEVLGVPM
FPTWNALDVVTSDLPQYGGRIGTYGGAGRNFGIQNSDLLLAVGSRISGRITGGNIHSFAR
EAKKYVVDVDETLLQKHLQQVPLDVNVLCDAGIFLRRLVARAKALRANGGLGDHKAWLSK
VLDWRDRYDPVLPEFFEQKGTVHPYAFVRKLSEMMKGGDIVVGDCGGNIVVTSHAFETKR
GQRLLTNNGNSPMGFSFAGAMGAWFAAPNNQVVCIIGDGGMNMNIQELQTFVNYGVKVKT
FILNNHIYGITKAYQETNFNGRAEACGPKGYAPPDFVKIAQAYGVKTVTIETQQEMEAKI
AEVLAADCAVVCDVNMHEYHTYEPRIFGWKTPIEDMYPYLPRDEFRANMLIEPLDDWQNP
AYPDVVQKKTLDP
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