SitesBLAST
Comparing WP_066917916.1 NCBI__GCF_001579945.1:WP_066917916.1 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)
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)
43% identity, 94% coverage: 18:590/611 of query aligns to 93:656/664 of P09114
- P191 (= P125) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
- W568 (= W507) mutation to L: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191.
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)
43% identity, 96% coverage: 16:603/611 of query aligns to 92:679/687 of P07342
- R241 (= R174) binding FAD
- 355:376 (vs. 286:307, 55% identical) binding FAD
- 407:426 (vs. 330:352, 26% identical) binding FAD
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)
43% identity, 94% coverage: 18:590/611 of query aligns to 96:659/667 of P09342
- C161 (= C92) modified: Disulfide link with 307
- P194 (= P125) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ V242) modified: Disulfide link with 161
6u9dB Saccharomyces cerevisiae acetohydroxyacid synthase (see paper)
43% identity, 96% coverage: 16:603/611 of query aligns to 12:599/607 of 6u9dB
- active site: Y33 (= Y37), G35 (= G39), G36 (= G40), A37 (= A41), I38 (= I42), E59 (= E72), T82 (= T95), F121 (= F134), Q122 (= Q135), E123 (= E136), K171 (= K184), M274 (= M285), V301 (= V312), V417 (= V418), G443 (= G444), M445 (= M446), D470 (= D471), N497 (= N498), E499 (≠ G500), Q500 (≠ D501), M502 (= M503), V503 (= V504), W506 (= W507)
- binding methyl 2-[(4,6-dimethoxypyrimidin-2-yl)carbamoylsulfamoylmethyl]benzoate: G36 (= G40), V111 (= V124), P112 (= P125), F121 (= F134), K171 (= K184), D299 (= D310), R300 (= R311), M502 (= M503), W506 (= W507)
- binding flavin-adenine dinucleotide: R161 (= R174), A228 (≠ G240), G229 (= G241), N232 (vs. gap), T254 (= T265), L255 (= L266), Q256 (≠ M267), L272 (= L283), M274 (= M285), G294 (= G305), R296 (= R307), D298 (= D309), R300 (= R311), V301 (= V312), E327 (≠ D330), V328 (≠ I331), N332 (≠ E335), D346 (≠ E352), A347 (= A353), M422 (= M423), G440 (= G441), G441 (≠ S442)
- binding magnesium ion: D470 (= D471), N497 (= N498)
- binding thiamine diphosphate: E59 (= E72), P85 (= P98), V417 (= V418), G418 (= G419), Q419 (= Q420), H420 (= H421), G443 (= G444), M445 (= M446), A471 (≠ S472), S472 (= S473), N497 (= N498), E499 (≠ G500), Q500 (≠ D501), G501 (= G502), M502 (= M503), V503 (= V504)
1t9cA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, sulfometuron methyl (see paper)
43% identity, 96% coverage: 16:603/611 of query aligns to 8:588/596 of 1t9cA
- active site: Y29 (= Y37), G31 (= G39), G32 (= G40), A33 (= A41), I34 (= I42), E55 (= E72), T78 (= T95), F117 (= F134), Q118 (= Q135), E119 (= E136), K167 (= K184), R227 (≠ Q249), M263 (= M285), V290 (= V312), V406 (= V418), L431 (≠ M443), G432 (= G444), M434 (= M446), D459 (= D471), N486 (= N498), E488 (≠ G500), Q489 (≠ D501), M491 (= M503), V492 (= V504), W495 (= W507), L517 (≠ A531), G522 (= G536), L523 (≠ F537), K556 (≠ P571)
- binding methyl 2-[({[(4,6-dimethylpyrimidin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (= G40), V107 (= V124), P108 (= P125), F117 (= F134), K167 (= K184), D288 (= D310), R289 (= R311), W495 (= W507)
- binding flavin-adenine dinucleotide: R157 (= R174), G216 (= G239), A217 (≠ G240), G218 (= G241), N221 (vs. gap), T243 (= T265), L244 (= L266), Q245 (≠ M267), L261 (= L283), M263 (= M285), H264 (= H286), G283 (= G305), A284 (= A306), R285 (= R307), D287 (= D309), R289 (= R311), V290 (= V312), E316 (≠ D330), V317 (≠ I331), N321 (≠ E335), G334 (≠ P351), D335 (≠ E352), A336 (= A353), M411 (= M423), G429 (= G441), G430 (≠ S442)
- binding magnesium ion: D459 (= D471), N486 (= N498), E488 (≠ G500)
1t9dA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
43% identity, 96% coverage: 16:603/611 of query aligns to 8:588/596 of 1t9dA
- active site: Y29 (= Y37), G31 (= G39), G32 (= G40), A33 (= A41), I34 (= I42), E55 (= E72), T78 (= T95), F117 (= F134), Q118 (= Q135), E119 (= E136), K167 (= K184), R227 (≠ Q249), M263 (= M285), V290 (= V312), V406 (= V418), L431 (≠ M443), G432 (= G444), M434 (= M446), D459 (= D471), N486 (= N498), E488 (≠ G500), Q489 (≠ D501), M491 (= M503), V492 (= V504), W495 (= W507), L517 (≠ A531), G522 (= G536), L523 (≠ F537), K556 (≠ P571)
- binding methyl 2-[({[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (= G40), A33 (= A41), V107 (= V124), P108 (= P125), F117 (= F134), K167 (= K184), M263 (= M285), D288 (= D310), R289 (= R311), W495 (= W507)
- binding flavin-adenine dinucleotide: R157 (= R174), G216 (= G239), A217 (≠ G240), G218 (= G241), N221 (vs. gap), T243 (= T265), L244 (= L266), Q245 (≠ M267), M260 (= M282), L261 (= L283), H264 (= H286), G283 (= G305), A284 (= A306), R285 (= R307), D287 (= D309), R289 (= R311), V290 (= V312), E316 (≠ D330), V317 (≠ I331), N321 (≠ E335), G334 (≠ P351), D335 (≠ E352), A336 (= A353), Q410 (= Q422), M411 (= M423), G429 (= G441), G430 (≠ S442)
- binding magnesium ion: D459 (= D471), N486 (= N498), E488 (≠ G500)
- binding 2,5-dimethyl-pyrimidin-4-ylamine: E55 (= E72), P81 (= P98), Q118 (= Q135), G432 (= G444), M434 (= M446), M464 (= M476)
1t9aA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, tribenuron methyl (see paper)
43% identity, 96% coverage: 16:603/611 of query aligns to 9:589/597 of 1t9aA
- active site: Y30 (= Y37), G32 (= G39), G33 (= G40), A34 (= A41), I35 (= I42), E56 (= E72), T79 (= T95), F118 (= F134), Q119 (= Q135), E120 (= E136), K168 (= K184), R228 (≠ Q249),