SitesBLAST
Comparing Pf1N1B4_4279 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4279 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)
6lpiB Crystal structure of ahas holo-enzyme (see paper)
25% identity, 89% coverage: 2:571/643 of query aligns to 2:495/539 of 6lpiB
- active site: I27 (= I34), G29 (≠ H40), G30 (= G41), S31 (≠ N42), I32 (≠ V43), E53 (= E65), C76 (≠ S90), F115 (≠ L129), Q116 (= Q130), E117 (≠ Q131), K165 (≠ Q188), M256 (≠ E283), A283 (≠ T310), V375 (≠ A439), G401 (≠ S465), M403 (= M467), D428 (= D492), N455 (= N519), A457 (≠ T521), L458 (≠ F522), L460 (≠ C524), V461 (≠ I525), Q464 (≠ L528)
- binding flavin-adenine dinucleotide: R155 (≠ E178), G212 (= G237), G213 (= G238), G214 (= G239), T236 (= T263), L237 (≠ Q264), M238 (≠ A265), L254 (≠ I281), M256 (≠ E283), H257 (≠ T284), G276 (= G303), A277 (≠ T304), R278 (= R305), D280 (≠ S307), R282 (≠ F309), A283 (≠ T310), D300 (≠ N328), I301 (= I329), D319 (= D345), V320 (≠ A346), M380 (vs. gap), G398 (= G454)
- binding magnesium ion: D428 (= D492), N455 (= N519)
- binding thiamine diphosphate: E53 (= E65), C76 (≠ S90), P79 (= P93), G376 (= G440), Q377 (vs. gap), H378 (vs. gap), G401 (≠ S465), M403 (= M467), G427 (= G491), D428 (= D492), G429 (= G493), S430 (= S494), M433 (= M497), N455 (= N519), A457 (≠ T521), L458 (≠ F522), G459 (= G523), L460 (≠ C524), V461 (≠ I525)
1t9bA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron (see paper)
24% identity, 88% coverage: 36:600/643 of query aligns to 25:541/583 of 1t9bA
- active site: Y29 (≠ H40), G31 (vs. gap), G32 (= G41), A33 (≠ N42), I34 (≠ V43), E55 (= E65), T78 (≠ S88), F117 (≠ L129), Q118 (= Q130), E119 (≠ Q131), K167 (≠ Q188), R214 (≠ A247), M250 (≠ E283), V277 (≠ T310), V393 (≠ A439), L418 (≠ Y464), G419 (≠ S465), M421 (= M467), D446 (= D492), N473 (= N519), E475 (≠ T521), Q476 (≠ F522), M478 (≠ C524), V479 (≠ I525), W482 (≠ L528), L504 (≠ S563), G509 (= G568), L510 (≠ C569)
- binding 1-(2-chlorophenylsulfonyl)-3-(4-methoxy-6-methyl-l,3,5-triazin-2-yl)urea: V107 (= V119), P108 (≠ Y120), F117 (≠ L129), D275 (= D308), R276 (≠ F309), M478 (≠ C524), W482 (≠ L528)
- binding flavin-adenine dinucleotide: R157 (≠ E178), G203 (= G237), A204 (≠ G238), G205 (= G239), N208 (≠ K241), T230 (= T263), L231 (≠ Q264), Q232 (≠ A265), M247 (≠ G280), L248 (≠ I281), M250 (≠ E283), H251 (≠ T284), G270 (= G303), A271 (≠ T304), R272 (= R305), D274 (≠ S307), R276 (≠ F309), V277 (≠ T310), E303 (≠ N328), V304 (≠ I329), N308 (≠ D333), D322 (= D359), A323 (= A371), Q397 (≠ P443), M398 (≠ G444), G416 (≠ Y462), G417 (= G463)
- binding magnesium ion: D446 (= D492), N473 (= N519), E475 (≠ T521)
Sites not aligning to the query:
1t9dB Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
24% identity, 88% coverage: 36:600/643 of query aligns to 24:540/582 of 1t9dB
- active site: Y28 (≠ H40), G30 (vs. gap), G31 (= G41), A32 (≠ N42), I33 (≠ V43), E54 (= E65), T77 (≠ S88), F116 (≠ L129), Q117 (= Q130), E118 (≠ Q131), K166 (≠ Q188), R213 (≠ A247), M249 (≠ E283), V276 (≠ T310), V392 (≠ A439), L417 (≠ Y464), G418 (≠ S465), M420 (= M467), D445 (= D492), N472 (= N519), E474 (≠ T521), Q475 (≠ F522), M477 (≠ C524), V478 (≠ I525), W481 (≠ L528), L503 (≠ S563), G508 (= G568), L509 (≠ C569)
- binding methyl 2-[({[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G31 (= G41), A32 (≠ N42), V106 (= V119), P107 (≠ Y120), F116 (≠ L129), K166 (≠ Q188), M249 (≠ E283), D274 (= D308), R275 (≠ F309), W481 (≠ L528)
- binding flavin-adenine dinucleotide: R156 (≠ E178), G202 (= G237), A203 (≠ G238), G204 (= G239), N207 (≠ K241), T229 (= T263), L230 (≠ Q264), Q231 (≠ A265), L247 (≠ I281), M249 (≠ E283), H250 (≠ T284), G269 (= G303), A270 (≠ T304), R271 (= R305), D273 (≠ S307), R275 (≠ F309), V276 (≠ T310), E302 (≠ N328), V303 (≠ I329), N307 (≠ D333), G320 (= G358), D321 (= D359), A322 (= A371), Q396 (≠ P443), M397 (≠ G444), G415 (≠ Y462), G416 (= G463)
- binding magnesium ion: D445 (= D492), N472 (= N519), E474 (≠ T521)
- binding 2,5-dimethyl-pyrimidin-4-ylamine: E54 (= E65), P80 (= P93), G418 (≠ S465), M420 (= M467), M450 (= M497)
Sites not aligning to the query:
8beoB Crystal structure of e. Coli glyoxylate carboligase mutant i393a with map
26% identity, 82% coverage: 63:588/643 of query aligns to 48:538/592 of 8beoB
- binding methyl hydrogen (s)-acetylphosphonate: C490 (≠ G538), Q492 (≠ E540)
- binding flavin-adenine dinucleotide: R153 (≠ E178), P154 (≠ T179), G210 (= G237), G211 (= G238), G212 (= G239), N215 (≠ Y242), T236 (= T263), L237 (≠ Q264), M238 (≠ A265), V254 (≠ I281), G255 (= G282), Q257 (≠ E283), T258 (= T284), G277 (= G303), N278 (≠ T304), R279 (= R305), A281 (≠ S307), R283 (≠ F309), H284 (≠ T310), D301 (≠ N328), I302 (= I329), Q306 (≠ D333), D320 (= D345), A321 (= A346), G415 (= G454)
- binding magnesium ion: D445 (= D492), F450 (≠ M497), L451 (= L498), E453 (≠ S500), N472 (= N519), Y474 (≠ T521)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(1s)-1-hydroxy-1-[(r)-hydroxy(methoxy)phosphoryl]ethyl}-5-(2-{[(s)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: R283 (≠ F309), G393 (≠ C415), L394 (= L416), S395 (≠ T417), L420 (≠ M467), G444 (= G491), D445 (= D492), F446 (≠ G493), D447 (≠ S494), N472 (= N519), Y474 (≠ T521), L475 (≠ F522), G476 (= G523), L477 (≠ C524), I478 (= I525)
- binding 2,3-dimethoxy-5-methyl-1,4-benzoquinone: Q352 (≠ E378), R356 (≠ I382)
Sites not aligning to the query:
8beoA Crystal structure of e. Coli glyoxylate carboligase mutant i393a with map
26% identity, 82% coverage: 63:588/643 of query aligns to 48:538/592 of 8beoA
- binding flavin-adenine dinucleotide: R153 (≠ E178), P154 (≠ T179), G210 (= G237), G211 (= G238), G212 (= G239), N215 (≠ Y242), T236 (= T263), L237 (≠ Q264), M238 (≠ A265), V254 (≠ I281), G255 (= G282), Q257 (≠ E283), T258 (= T284), G277 (= G303), N278 (≠ T304), R279 (= R305), A281 (≠ S307), R283 (≠ F309), H284 (≠ T310), D301 (≠ N328), I302 (= I329), Q306 (≠ D333), D320 (= D345), A321 (= A346), I397 (≠ V436), G415 (= G454)
- binding magnesium ion: R384 (= R406), V405 (≠ G444), F406 (≠ D445), H410 (≠ S449), D445 (= D492), F450 (≠ M497), L451 (= L498), E453 (≠ S500), N472 (= N519), Y474 (≠ T521)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(1s)-1-hydroxy-1-[(r)-hydroxy(methoxy)phosphoryl]ethyl}-5-(2-{[(s)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: R283 (≠ F309), G393 (≠ C415), L394 (= L416), S395 (≠ T417), L420 (≠ M467), G444 (= G491), D445 (= D492), F446 (≠ G493), D447 (≠ S494), N472 (= N519), Y474 (≠ T521), L475 (≠ F522), G476 (= G523), L477 (≠ C524), I478 (= I525)
- binding 2,3-dimethoxy-5-methyl-1,4-benzoquinone: E248 (≠ P275), Q352 (≠ E378)
Sites not aligning to the query:
5wkcA Saccharomyces cerevisiae acetohydroxyacid synthase in complex with the herbicide penoxsulam (see paper)
24% identity, 88% coverage: 36:600/643 of query aligns to 25:549/591 of 5wkcA
- active site: Y29 (≠ H40), G31 (vs. gap), G32 (= G41), A33 (≠ N42), I34 (≠ V43), E55 (= E65), T78 (≠ S88), F117 (≠ L129), Q118 (= Q130), E119 (≠ Q131), K167 (≠ Q188), R222 (≠ A247), M258 (≠ E283), V285 (≠ T310), V401 (≠ A439), L426 (≠ Y464), G427 (≠ S465), M429 (= M467), D454 (= D492), N481 (= N519), E483 (≠ T521), Q484 (≠ F522), M486 (≠ C524), V487 (≠ I525), W490 (≠ L528), L512 (≠ S563), G517 (= G568), L518 (≠ C569)
- 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 (≠ A439), G402 (= G440), Q403 (≠ S441), H404 (≠ L442), G427 (≠ S465), M429 (= M467), G453 (= G491), D454 (= D492), A455 (≠ G493), S456 (= S494), M459 (= M497), N481 (= N519), E483 (≠ T521), Q484 (≠ F522), G485 (= G523), M486 (≠ C524), V487 (≠ I525)
- binding ethaneperoxoic acid: G32 (= G41), Q118 (= Q130)
- binding flavin-adenine dinucleotide: R157 (≠ E178), G211 (= G237), A212 (≠ G238), G213 (= G239), N216 (≠ K241), T238 (= T263), L239 (≠ Q264), Q240 (≠ A265), L256 (≠ I281), M258 (≠ E283), G278 (= G303), A279 (≠ T304), R280 (= R305), R284 (≠ F309), V285 (≠ T310), E311 (≠ N328), V312 (≠ I329), N316 (≠ D333), D330 (= D359), A331 (= A371), M406 (≠ G444), G424 (≠ Y462)
- binding magnesium ion: D454 (= D492), N481 (= N519), E483 (≠ T521)
- binding 2-(2,2-difluoroethoxy)-N-(5,8-dimethoxy[1,2,4]triazolo[1,5-c]pyrimidin-2-yl)-6-(trifluoromethyl)benzenesulfonamide: G32 (= G41), A33 (≠ N42), V107 (= V119), F117 (≠ L129), K167 (≠ Q188), M258 (≠ E283), R284 (≠ F309), M486 (≠ C524), W490 (≠ L528)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: P30 (vs. gap), E55 (= E65)
Sites not aligning to the query:
1t9bB Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron (see paper)
24% identity, 88% coverage: 36:600/643 of query aligns to 25:553/595 of 1t9bB
- active site: Y29 (≠ H40), G31 (vs. gap), G32 (= G41), A33 (≠ N42), I34 (≠ V43), E55 (= E65), T78 (≠ S88), F117 (≠ L129), Q118 (= Q130), E119 (≠ Q131), K167 (≠ Q188), R226 (≠ A247), M262 (≠ E283), V289 (≠ T310), V405 (≠ A439), L430 (≠ Y464), G431 (≠ S465), M433 (= M467), D458 (= D492), N485 (= N519), E487 (≠ T521), Q488 (≠ F522), M490 (≠ C524), V491 (≠ I525), W494 (≠ L528), L516 (≠ S563), G521 (= G568), L522 (≠ C569)
- binding 1-(2-chlorophenylsulfonyl)-3-(4-methoxy-6-methyl-l,3,5-triazin-2-yl)urea: V107 (= V119), P108 (≠ Y120), D287 (= D308), R288 (≠ F309), M490 (≠ C524), W494 (≠ L528)
- binding flavin-adenine dinucleotide: R157 (≠ E178), G215 (= G237), A216 (≠ G238), G217 (= G239), N220 (≠ K241), T242 (= T263), L243 (≠ Q264), Q244 (≠ A265), M259 (≠ G280), L260 (≠ I281), M262 (≠ E283), H263 (≠ T284), G282 (= G303), A283 (≠ T304), R284 (= R305), D286 (≠ S307), R288 (≠ F309), V289 (≠ T310), E315 (≠ N328), V316 (≠ I329), N320 (≠ D333), G333 (= G358), D334 (= D359), A335 (= A371), Q409 (≠ P443), M410 (≠ G444), G428 (≠ Y462), G429 (= G463)
- binding magnesium ion: D458 (= D492), N485 (= N519), E487 (≠ T521)
Sites not aligning to the query:
1t9cA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, sulfometuron methyl (see paper)
24% identity, 88% coverage: 36:600/643 of query aligns to 25:554/596 of 1t9cA
- active site: Y29 (≠ H40), G31 (vs. gap), G32 (= G41), A33 (≠ N42), I34 (≠ V43), E55 (= E65), T78 (≠ S88), F117 (≠ L129), Q118 (= Q130), E119 (≠ Q131), K167 (≠ Q188), R227 (≠ A247), M263 (≠ E283), V290 (≠ T310), V406 (≠ A439), L431 (≠ Y464), G432 (≠ S465), M434 (= M467), D459 (= D492), N486 (= N519), E488 (≠ T521), Q489 (≠ F522), M491 (≠ C524), V492 (≠ I525), W495 (≠ L528), L517 (≠ S563), G522 (= G568), L523 (≠ C569)
- binding methyl 2-[({[(4,6-dimethylpyrimidin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (= G41), V107 (= V119), P108 (≠ Y120), F117 (≠ L129), K167 (≠ Q188), D288 (= D308), R289 (≠ F309), W495 (≠ L528)
- binding flavin-adenine dinucleotide: R157 (≠ E178), G216 (= G237), A217 (≠ G238), G218 (= G239), N221 (≠ K241), T243 (= T263), L244 (≠ Q264), Q245 (≠ A265), L261 (≠ I281), M263 (≠ E283), H264 (≠ T284), G283 (= G303), A284 (≠ T304), R285 (= R305), D287 (≠ S307), R289 (≠ F309), V290 (≠ T310), E316 (≠ N328), V317 (≠ I329), N321 (≠ D333), G334 (= G358), D335 (= D359), A336 (= A371), M411 (≠ G444), G429 (≠ Y462), G430 (= G463)
- binding magnesium ion: D459 (= D492), N486 (= N519), E488 (≠ T521)
Sites not aligning to the query:
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)
24% identity, 88% coverage: 36:600/643 of query aligns to 109:645/687 of P07342
- R241 (≠ E178) binding
- 355:376 (vs. 284:305, 59% identical) binding
- 407:426 (vs. 328:359, 22% identical) binding
1t9aA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, tribenuron methyl (see paper)
24% identity, 88% coverage: 36:600/643 of query aligns to 26:555/597 of 1t9aA
- active site: Y30 (≠ H40), G32 (vs. gap), G33 (= G41), A34 (≠ N42), I35 (≠ V43), E56 (= E65), T79 (≠ S88), F118 (≠ L129), Q119 (= Q130), E120 (≠ Q131), K168 (≠ Q188), R228 (≠ A247), M264 (≠ E283), V291 (≠ T310), V407 (≠ A439), L432 (≠ Y464), G433 (≠ S465), M435 (= M467), D460 (= D492), N487 (= N519), E489 (≠ T521), Q490 (≠ F522), M492 (≠ C524), V493 (≠ I525), W496 (≠ L528), L518 (≠ S563), G523 (= G568), L524 (≠ C569)
- binding methyl 2-[4-methoxy-6-methyl-1,3,5-trazin-2-yl(methyl)carbamoylsulfamoyl]benzoate: G33 (= G41), V108 (= V119), P109 (≠ Y120), F118 (≠ L129), K168 (≠ Q188), M264 (≠ E283), D289 (= D308), R290 (≠ F309), M492 (≠ C524), V493 (≠ I525), W496 (≠ L528)
- binding flavin-adenine dinucleotide: R158 (≠ E178), G217 (= G237), A218 (≠ G238), G219 (= G239), N222 (≠ K241), T244 (= T263), L245 (≠ Q264), Q246 (≠ A265), L262 (≠ I281), M264 (≠ E283), H265 (≠ T284), G284 (= G303), A285 (≠ T304), R286 (= R305), D288 (≠ S307), R290 (≠ F309), V291 (≠ T310), E317 (≠ N328), V318 (≠ I329), N322 (≠ D333), G335 (= G358), D336 (= D359), A337 (= A371), Q411 (≠ P443), M412 (≠ G444), G430 (≠ Y462), G431 (= G463)
- binding magnesium ion: D460 (= D492), N487 (= N519), E489 (≠ T521)
- binding propyl trihydrogen diphosphate: V407 (≠ A439), G408 (= G440), Q409 (≠ S441), H410 (≠ L442), M435 (= M467), G459 (= G491), D460 (= D492), A461 (≠ G493), S462 (= S494), N487 (= N519), E489 (≠ T521), Q490 (≠ F522), G491 (= G523), M492 (≠ C524)
- binding 5-{[ethyl(methyl)amino]methyl}-2-methyl-5,6-dihydropyrimidin-4-amine: G433 (≠ S465), M435 (= M467), M465 (= M497)
Sites not aligning to the query:
1t9dA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
24% identity, 88% coverage: 36:600/643 of query aligns to 25:554/596 of 1t9dA
- active site: Y29 (≠ H40), G31 (vs. gap), G32 (= G41), A33 (≠ N42), I34 (≠ V43), E55 (= E65), T78 (≠ S88), F117 (≠ L129), Q118 (= Q130), E119 (≠ Q131), K167 (≠ Q188), R227 (≠ A247), M263 (≠ E283), V290 (≠ T310), V406 (≠ A439), L431 (≠ Y464), G432 (≠ S465), M434 (= M467), D459 (= D492), N486 (= N519), E488 (≠ T521), Q489 (≠ F522), M491 (≠ C524), V492 (≠ I525), W495 (≠ L528), L517 (≠ S563), G522 (= G568), L523 (≠ C569)
- binding methyl 2-[({[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (= G41), A33 (≠ N42), V107 (= V119), P108 (≠ Y120), F117 (≠ L129), K167 (≠ Q188), M263 (≠ E283), D288 (= D308), R289 (≠ F309), W495 (≠ L528)
- binding flavin-adenine dinucleotide: R157 (≠ E178), G216 (= G237), A217 (≠ G238), G218 (= G239), N221 (≠ K241), T243 (= T263), L244 (≠ Q264), Q245 (≠ A265), M260 (≠ G280), L261 (≠ I281), H264 (≠ T284), G283 (= G303), A284 (≠ T304), R285 (= R305), D287 (≠ S307), R289 (≠ F309), V290 (≠ T310), E316 (≠ N328), V317 (≠ I329), N321 (≠ D333), G334 (= G358), D335 (= D359), A336 (= A371), Q410 (≠ P443), M411 (≠ G444), G429 (≠ Y462), G430 (= G463)
- binding magnesium ion: D459 (= D492), N486 (= N519), E488 (≠ T521)
- binding 2,5-dimethyl-pyrimidin-4-ylamine: E55 (= E65), P81 (= P93), Q118 (= Q130), G432 (≠ S465), M434 (= M467), M464 (= M497)
Sites not aligning to the query:
6u9dB Saccharomyces cerevisiae acetohydroxyacid synthase (see paper)
24% identity, 88% coverage: 36:600/643 of query aligns to 29:565/607 of 6u9dB
- active site: Y33 (≠ H40), G35 (vs. gap), G36 (= G41), A37 (≠ N42), I38 (≠ V43), E59 (= E65), T82 (≠ S88), F121 (≠ L129), Q122 (= Q130), E123 (≠ Q131), K171 (≠ Q188), M274 (≠ E283), V301 (≠ T310), V417 (≠ A439), G443 (≠ S465), M445 (= M467), D470 (= D492), N497 (= N519), E499 (≠ T521), Q500 (≠ F522), M502 (≠ C524), V503 (≠ I525), W506 (≠ L528)
- binding methyl 2-[(4,6-dimethoxypyrimidin-2-yl)carbamoylsulfamoylmethyl]benzoate: G36 (= G41), V111 (= V119), P112 (≠ Y120), F121 (≠ L129), K171 (≠ Q188), D299 (= D308), R300 (≠ F309), M502 (≠ C524), W506 (≠ L528)
- binding flavin-adenine dinucleotide: R161 (≠ E178), A228 (≠ G238), G229 (= G239), N232 (≠ K241), T254 (= T263), L255 (≠ Q264), Q256 (≠ A265), L272 (≠ I281), M274 (≠ E283), G294 (= G303), R296 (= R305), D298 (≠ S307), R300 (≠ F309), V301 (≠ T310), E327 (≠ N328), V328 (≠ I329), N332 (≠ D333), D346 (= D359), A347 (= A371), M422 (≠ G444), G440 (≠ Y462), G441 (= G463)
- binding magnesium ion: D470 (= D492), N497 (= N519)
- binding thiamine diphosphate: E59 (= E65), P85 (= P93), V417 (≠ A439), G418 (= G440), Q419 (≠ S441), H420 (≠ L442), G443 (≠ S465), M445 (= M467), A471 (≠ G493), S472 (= S494), N497 (= N519), E499 (≠ T521), Q500 (≠ F522), G501 (= G523), M502 (≠ C524), V503 (≠ I525)
1n0hA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorimuron ethyl (see paper)
24% identity, 88% coverage: 36:600/643 of query aligns to 27:557/599 of 1n0hA
- active site: Y31 (≠ H40), G33 (vs. gap), G34 (= G41), A35 (≠ N42), I36 (≠ V43), E57 (= E65), T80 (≠ S88), F119 (≠ L129), Q120 (= Q130), E121 (≠ Q131), K169 (≠ Q188), R230 (≠ A247), M266 (≠ E283), V293 (≠ T310), V409 (≠ A439), L434 (≠ Y464), G435 (≠ S465), M437 (= M467), D462 (= D492), N489 (= N519), E491 (≠ T521), Q492 (≠ F522), M494 (≠ C524), V495 (≠ I525), W498 (≠ L528), L520 (≠ S563), G525 (= G568), L526 (≠ C569)
- binding 4-{[(4'-amino-2'-methylpyrimidin-5'-yl)methyl]amino}pent-3-enyl diphosphate: V409 (≠ A439), G410 (= G440), Q411 (≠ S441), H412 (≠ L442), G435 (≠ S465), M437 (= M467), G461 (= G491), D462 (= D492), A463 (≠ G493), S464 (= S494), M467 (= M497), N489 (= N519), E491 (≠ T521), Q492 (≠ F522), G493 (= G523), V495 (≠ I525)
- binding 2-[[[[(4-chloro-6-methoxy-2-pyrimidinyl)amino]carbonyl]amino]sulfonyl]benzoic acid ethyl ester: G34 (= G41), A35 (≠ N42), V109 (= V119), P110 (≠ Y120), F119 (≠ L129), K169 (≠ Q188), M266 (≠ E283), D291 (= D308), R292 (≠ F309), V495 (≠ I525), W498 (≠ L528)
- binding flavin-adenine dinucleotide: R159 (≠ E178), G219 (= G237), A220 (≠ G238), G221 (= G239), N224 (≠ K241), T246 (= T263), L247 (≠ Q264), Q248 (≠ A265), L264 (≠ I281), G265 (= G282), M266 (≠ E283), H267 (≠ T284), G286 (= G303), A287 (≠ T304), R288 (= R305), D290 (≠ S307), R292 (≠ F309), V293 (≠ T310), E319 (≠ N328), V320 (≠ I329), N324 (≠ D333), G337 (= G358), D338 (= D359), A339 (= A371), M414 (≠ G444), G432 (≠ Y462), G433 (= G463)
- binding magnesium ion: D462 (= D492), N489 (= N519), E491 (≠ T521)
- binding thiamine diphosphate: Y31 (≠ H40), E57 (= E65), P83 (= P93)
Sites not aligning to the query:
6bd3A Saccharomyces cerevisiae acetohydroxyacid synthase
24% identity, 75% coverage: 36:519/643 of query aligns to 27:484/538 of 6bd3A
- active site: Y31 (≠ H40), G33 (vs. gap), G34 (= G41), A35 (≠ N42), I36 (≠ V43), E57 (= E65), T80 (≠ S88), F119 (≠ L129), Q120 (= Q130), E121 (≠ Q131), K169 (≠ Q188), R225 (≠ A247), M261 (≠ E283), V288 (≠ T310), V404 (≠ A439), L429 (≠ Y464), G430 (≠ S465), M432 (= M467), D457 (= D492), N484 (= N519)
- binding flavin-adenine dinucleotide: R159 (≠ E178), G214 (= G237), A215 (≠ G238), G216 (= G239), N219 (≠ K241), T241 (= T263), L242 (≠ Q264), Q243 (≠ A265), L259 (≠ I281), G260 (= G282), H262 (≠ T284), G281 (= G303), A282 (≠ T304), R283 (= R305), D285 (≠ S307), R287 (≠ F309), V288 (≠ T310), E314 (≠ N328), V315 (≠ I329), D333 (= D359), A334 (= A371)
- binding 2-acetyl-thiamine diphosphate: P32 (vs. gap), E57 (= E65), P83 (= P93)
- binding magnesium ion: D457 (= D492), N484 (= N519)
- binding oxygen molecule: A35 (≠ N42), T80 (≠ S88), S81 (= S89), Q120 (= Q130)
- binding thiamine diphosphate: V404 (≠ A439), G405 (= G440), Q406 (≠ S441), H407 (≠ L442), G430 (≠ S465), M432 (= M467), D457 (= D492), A458 (≠ G493), S459 (= S494), M462 (= M497), N484 (= N519)
Sites not aligning to the query:
5imsA Saccharomyces cerevisiae acetohydroxyacid synthase
24% identity, 75% coverage: 36:519/643 of query aligns to 27:488/541 of 5imsA
- active site: Y31 (≠ H40), G33 (vs. gap), G34 (= G41), A35 (≠ N42), I36 (≠ V43), E57 (= E65), T80 (≠ S88), F119 (≠ L129), Q120 (= Q130), E121 (≠ Q131), K169 (≠ Q188), R229 (≠ A247), M265 (≠ E283), V292 (≠ T310), V408 (≠ A439), L433 (≠ Y464), G434 (≠ S465), M436 (= M467), D461 (= D492), N488 (= N519)
- binding flavin-adenine dinucleotide: R159 (≠ E178), G218 (= G237), A219 (≠ G238), G220 (= G239), N223 (≠ K241), T245 (= T263), L246 (≠ Q264), L263 (≠ I281), G264 (= G282), H266 (≠ T284), G285 (= G303), A286 (≠ T304), R287 (= R305), D289 (≠ S307), R291 (≠ F309), V292 (≠ T310), E318 (≠ N328), V319 (≠ I329), N323 (≠ D333), D337 (= D359), A338 (= A371)
- binding magnesium ion: D461 (= D492), N488 (= N519)
- binding oxygen molecule: G34 (= G41), T80 (≠ S88), Q120 (= Q130)
- binding thiamine diphosphate: P32 (vs. gap), E57 (= E65), V408 (≠ A439), G409 (= G440), Q410 (≠ S441), H411 (≠ L442), G434 (≠ S465), M436 (= M467), G460 (= G491), D461 (= D492), A462 (≠ G493), S463 (= S494), M466 (= M497), N488 (= N519)
Sites not aligning to the query:
1jscA Crystal structure of the catalytic subunit of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors (see paper)
24% identity, 75% coverage: 36:519/643 of query aligns to 27:486/541 of 1jscA
- active site: Y31 (≠ H40), G33 (vs. gap), G34 (= G41), A35 (≠ N42), I36 (≠ V43), E57 (= E65), T80 (≠ S88), F119 (≠ L129), Q120 (= Q130), E121 (≠ Q131), K169 (≠ A177), M263 (≠ E283), V290 (≠ T310), V406 (≠ A439), G432 (≠ S465), M434 (= M467), D459 (= D492), N486 (= N519)
- binding dihydrogenphosphate ion: G33 (vs. gap), G34 (= G41), Q120 (= Q130)
- binding flavin-adenine dinucleotide: R159 (≠ I167), G216 (= G237), A217 (≠ G238), G218 (= G239), N221 (≠ K241), T243 (= T263), L244 (≠ Q264), L261 (≠ I281), G262 (= G282), H264 (≠ T284), G283 (= G303), A284 (≠ T304), R285 (= R305), D287 (≠ S307), R289 (≠ F309), V290 (≠ T310), E316 (≠ N328), V317 (≠ I329), N321 (≠ D333), G334 (= G358), D335 (= D359), A336 (= A371)
- binding magnesium ion: D459 (= D492), N486 (= N519)
- binding thiamine diphosphate: Y31 (≠ H40), P32 (vs. gap), E57 (= E65), P83 (= P93), V406 (≠ A439), G407 (= G440), Q408 (≠ S441), H409 (≠ L442), M434 (= M467), D459 (= D492), A460 (≠ G493), S461 (= S494), N486 (= N519)
Sites not aligning to the query:
6bd9A Saccharomyces cerevisiae acetohydroxyacid synthase
24% identity, 75% coverage: 36:519/643 of query aligns to 27:487/542 of 6bd9A
- active site: Y31 (≠ H40), G33 (vs. gap), G34 (= G41), A35 (≠ N42), I36 (≠ V43), E57 (= E65), T80 (≠ S88), F119 (≠ L129), Q120 (= Q130), E121 (≠ Q131), K169 (≠ Q188), R228 (≠ A247), M264 (≠ E283), V291 (≠ T310), V407 (≠ A439), L432 (≠ Y464), G433 (≠ S465), M435 (= M467), D460 (= D492), N487 (= N519)
- binding flavin-adenine dinucleotide: R159 (≠ E178), G217 (= G237), A218 (≠ G238), G219 (= G239), N222 (≠ K241), T244 (= T263), L245 (≠ Q264), L262 (≠ I281), G263 (= G282), H265 (≠ T284), G284 (= G303), A285 (≠ T304), R286 (= R305), D288 (≠ S307), R290 (≠ F309), V291 (≠ T310), E317 (≠ N328), V318 (≠ I329), N322 (≠ D333), G335 (= G358), D336 (= D359), A337 (= A371)
- binding magnesium ion: D460 (= D492), N487 (= N519)
- binding oxygen molecule: G34 (= G41), T80 (≠ S88), Q120 (= Q130), A461 (≠ G493)
- binding pyruvic acid: G33 (vs. gap), G34 (= G41), G34 (= G41), A35 (≠ N42), Q120 (= Q130)
- binding thiamine diphosphate: P32 (vs. gap), E57 (= E65), V407 (≠ A439), G408 (= G440), Q409 (≠ S441), H410 (≠ L442), G433 (≠ S465), M435 (= M467), G459 (= G491), D460 (= D492), A461 (≠ G493), S462 (= S494), M465 (= M497), N487 (= N519)
Sites not aligning to the query:
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)
24% identity, 78% coverage: 23:525/643 of query aligns to 101:568/667 of P09342
- C161 (= C87) modified: Disulfide link with 307
- P194 (vs. gap) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ V240) 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)
24% identity, 78% coverage: 23:525/643 of query aligns to 98:565/664 of P09114
- P191 (vs. gap) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
Sites not aligning to the query:
- 568 W→L: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191.
7tzzA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase p197t mutant in complex with bispyribac-sodium (see paper)
25% identity, 77% coverage: 33:525/643 of query aligns to 26:486/582 of 7tzzA
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: M266 (≠ E283), R292 (≠ F309)
- 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 (≠ A439), G401 (= G440), Q402 (≠ S441), H403 (≠ L442), G426 (≠ S465), M428 (= M467), G452 (= G491), D453 (= D492), G454 (= G493), S455 (= S494), L483 (≠ F522), G484 (= G523), M485 (≠ C524), V486 (≠ I525)
- binding flavin-adenine dinucleotide: R161 (≠ E178), G222 (= G237), G223 (= G238), G224 (= G239), T246 (= T263), L247 (≠ Q264), M248 (≠ A265), M263 (≠ G280), L264 (≠ I281), M266 (≠ E283), H267 (≠ T284), G286 (= G303), R288 (= R305), V293 (≠ T310), D310 (≠ N326), I311 (≠ L327), D329 (= D345), V330 (≠ A346), M405 (≠ G444), G423 (≠ Y462)
- binding magnesium ion: A37 (≠ N42), T82 (≠ S90), S83 (≠ V91), Q122 (≠ H136), Y381 (≠ R420), D453 (= D492), M458 (= M497), Q461 (≠ S500), N480 (= N519), H482 (≠ T521)
Sites not aligning to the query:
Query Sequence
>Pf1N1B4_4279 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4279
MTTTRLTMAQALVKFLDNQYIEVDGVQSKFVAGIFTIFGHGNVLGLGQALEQDSGDLIVH
QGRNEQGMAHAAIGFAKQHLRRKIYACSSSVGPGAANMLTAAATATANRIPLLLLPGDVY
ACRQPDPVLQQIEQFHDLSISTNDAFKAVSKYWDRINRPEQLMTAAIHAMRVLTDPAETG
AVTLALPQDVQAEAYDYPDYFLQKRVHRIERRPATEAMLGDAVALFKGKHKPLIICGGGV
KYSGANAALQAFAERFDIPFAETQAGKSAVVSSHPLNVGGIGETGCLAANLLAKDADLII
GVGTRYSDFTTASKSLFKHPDVQFLNLNISPCDALKLDGVQLLADAKTGLQALAEVLGDY
RSSWGDQPRQAKTQLDEEVDRIYQVEYQAKDFVPEINDHLDPAVLREFIELTGSCLTQSR
VLGVLNETLADDAVIVAAAGSLPGDLQRSWRSKGVNTYHVEYGYSCMGYEVNAALGVKLA
EPEREVYALVGDGSYMMLHSELATSIQERRKINVVLLDNMTFGCINNLQMEHGMDSFGTE
FRFRNPETGKLDGGFVPVDFAMSAAAYGCKTYKVNTVEQLQDALADARLQTVSTLIDIKV
LPKTMIHKYLSWWRVGVAQVSTSARTDAVAKTLNERLAKARQY
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