SitesBLAST
Comparing PP_3365 FitnessBrowser__Putida:PP_3365 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)
4rjkF Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
34% identity, 98% coverage: 3:540/547 of query aligns to 2:544/552 of 4rjkF
- binding magnesium ion: D437 (= D433), D464 (= D460), T466 (≠ G462)
- binding pyruvic acid: A25 (≠ E26), K26 (≠ E27)
- binding thiamine diphosphate: P23 (= P24), E47 (= E48), P73 (= P74), G385 (= G381), S386 (≠ I382), H387 (≠ Y383), Q410 (≠ A406), L412 (≠ M408), G436 (= G432), D437 (= D433), G438 (= G434), G439 (= G435), T466 (≠ G462), Y467 (= Y463), D468 (≠ G464), M469 (= M465), V470 (≠ I466), Y533 (= Y529)
4rjiC Acetolactate synthase from bacillus subtilis bound to thdp - crystal form i (see paper)
34% identity, 98% coverage: 3:540/547 of query aligns to 3:545/555 of 4rjiC
- binding magnesium ion: D438 (= D433), D465 (= D460), T467 (≠ G462)
- binding thiamine diphosphate: P24 (= P24), E48 (= E48), P74 (= P74), S387 (≠ I382), H388 (≠ Y383), Q411 (≠ A406), G437 (= G432), D438 (= D433), G439 (= G434), G440 (= G435), T467 (≠ G462), Y468 (= Y463), D469 (≠ G464), M470 (= M465), V471 (≠ I466), Y534 (= Y529)
4rjkG Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
34% identity, 98% coverage: 3:540/547 of query aligns to 2:544/553 of 4rjkG
- binding magnesium ion: D437 (= D433), D464 (= D460), T466 (≠ G462)
- 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 (= E48), Q110 (= Q111)
- binding thiamine diphosphate: I384 (≠ N380), G385 (= G381), S386 (≠ I382), H387 (≠ Y383), Q410 (≠ A406), L412 (≠ M408), G436 (= G432), D437 (= D433), G438 (= G434), G439 (= G435), T466 (≠ G462), Y467 (= Y463), D468 (≠ G464), M469 (= M465), V470 (≠ I466), Y533 (= Y529)
5d6rB Acetolactate synthase from klebsiella pneumoniae in complex with mechanism-based inhibitor
35% identity, 97% coverage: 2:532/547 of query aligns to 5:538/548 of 5d6rB
- active site: I26 (= I23), G28 (= G25), A29 (≠ E26), K30 (≠ E27), I31 (≠ N28), E51 (= E48), T74 (= T71), H113 (≠ F110), Q114 (= Q111), S115 (≠ I112), Q163 (≠ E160), L254 (= L251), E281 (≠ P278), M386 (≠ N380), Q412 (≠ A406), M414 (= M408), D439 (= D433), D466 (= D460), G468 (= G462), Y469 (= Y463), M471 (= M465), V472 (≠ I466), Q475 (≠ K469), Y535 (= Y529)
- 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 (≠ N380), G387 (= G381), S388 (≠ I382), Q412 (≠ A406), M414 (= M408), D439 (= D433), G440 (= G434), G468 (= G462), Y469 (= Y463), N470 (≠ G464), M471 (= M465), Y535 (= Y529)
- binding magnesium ion: R63 (= R60), Q212 (≠ R210), D439 (= D433), D466 (= D460), G468 (= G462)
1ozgA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate (see paper)
35% identity, 97% coverage: 2:532/547 of query aligns to 6:541/549 of 1ozgA
- active site: I27 (= I23), G29 (= G25), A30 (≠ E26), K31 (≠ E27), I32 (≠ N28), E52 (= E48), T75 (= T71), H114 (≠ F110), Q115 (= Q111), S116 (≠ I112), Q164 (≠ E160), L257 (= L251), E284 (≠ P278), M389 (≠ N380), Q415 (≠ A406), M417 (= M408), D442 (= D433), D469 (= D460), G471 (= G462), Y472 (= Y463), M474 (= M465), V475 (≠ I466), Q478 (≠ K469), Y538 (= Y529)
- binding 2-hydroxyethyl dihydrothiachrome diphosphate: M389 (≠ N380), G390 (= G381), S391 (≠ I382), F392 (≠ Y383), Q415 (≠ A406), M417 (= M408), G441 (= G432), D442 (= D433), G443 (= G434), D469 (= D460), G471 (= G462), Y472 (= Y463), N473 (≠ G464), M474 (= M465), V475 (≠ I466), Y538 (= Y529)
- binding magnesium ion: D442 (= D433), D469 (= D460), G471 (= G462)
- binding phosphate ion: G253 (= G247), R254 (≠ N248), Q261 (≠ D255), R347 (vs. gap), R398 (= R389), Y401 (≠ K392)
1ozfA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors (see paper)
35% identity, 97% coverage: 2:532/547 of query aligns to 5:537/545 of 1ozfA
- active site: I26 (= I23), G28 (= G25), A29 (≠ E26), K30 (≠ E27), I31 (≠ N28), E51 (= E48), T74 (= T71), H113 (≠ F110), Q114 (= Q111), S115 (≠ I112), Q163 (≠ E160), L253 (= L251), E280 (≠ P278), M385 (≠ N380), Q411 (≠ A406), M413 (= M408), D438 (= D433), D465 (= D460), G467 (= G462), Y468 (= Y463), M470 (= M465), V471 (≠ I466), Q474 (≠ K469), Y534 (= Y529)
- binding magnesium ion: D438 (= D433), D465 (= D460), G467 (= G462)
- binding phosphate ion: G249 (= G247), R250 (≠ N248), Q257 (≠ D255), R343 (vs. gap), R394 (= R389), L396 (≠ Y391), Y397 (≠ K392)
- binding thiamine diphosphate: G386 (= G381), S387 (≠ I382), F388 (≠ Y383), Q411 (≠ A406), M413 (= M408), G437 (= G432), D438 (= D433), G439 (= G434), D465 (= D460), G467 (= G462), Y468 (= Y463), N469 (≠ G464), M470 (= M465), V471 (≠ I466), Y534 (= Y529)
5wdgA Acetolactate synthase from klebsiella pneumoniae in complex with a reaction intermediate
34% identity, 97% coverage: 2:532/547 of query aligns to 6:530/538 of 5wdgA
- active site: I27 (= I23), G29 (= G25), A30 (≠ E26), K31 (≠ E27), I32 (≠ N28), E52 (= E48), T75 (= T71), Q157 (≠ E160), L246 (= L251), E273 (≠ P278), M378 (≠ N380), Q404 (≠ A406), M406 (= M408), D431 (= D433), D458 (= D460), G460 (= G462), Y461 (= Y463), M463 (= M465), V464 (≠ I466), Q467 (≠ K469), Y527 (= Y529)
- 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 (≠ N380), S380 (≠ I382), F381 (≠ Y383), Q404 (≠ A406), M406 (= M408), G430 (= G432), D431 (= D433), G432 (= G434), G433 (= G435), D458 (= D460), G460 (= G462), Y461 (= Y463), N462 (≠ G464), M463 (= M465), V464 (≠ I466), Y527 (= Y529)
- binding magnesium ion: R64 (= R60), S117 (≠ D120), T120 (= T123), Q204 (≠ R210), D431 (= D433), D458 (= D460), G460 (= G462)
- binding pyruvic acid: G94 (= G90), R147 (≠ K150)
5dx6B Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
35% identity, 97% coverage: 2:532/547 of query aligns to 17:544/557 of 5dx6B
- active site: I38 (= I23), G40 (= G25), A41 (≠ E26), K42 (≠ E27), I43 (≠ N28), E63 (= E48), T86 (= T71), H125 (≠ F110), Q126 (= Q111), S127 (≠ I112), Q175 (≠ E160), L268 (= L251), E295 (≠ P278), M392 (≠ N380), Q418 (≠ A406), M420 (= M408), D445 (= D433), D472 (= D460), G474 (= G462), Y475 (= Y463), M477 (= M465), V478 (≠ I466), Q481 (≠ K469), Y541 (= Y529)
- binding 3-fluoro-2-oxopropanoic acid: G264 (= G247), R265 (≠ N248), Q272 (≠ D255), A400 (= A388), R401 (= R389), Y404 (≠ K392)
- binding magnesium ion: S135 (≠ D120), T138 (= T123), D445 (= D433), D472 (= D460), G474 (= G462)
- binding thiamine diphosphate: G393 (= G381), S394 (≠ I382), F395 (≠ Y383), Q418 (≠ A406), M420 (= M408), G444 (= G432), D445 (= D433), G446 (= G434), D472 (= D460), G474 (= G462), Y475 (= Y463), N476 (≠ G464), M477 (= M465), V478 (≠ I466), Y541 (= Y529)
5dx6A Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
34% identity, 97% coverage: 2:532/547 of query aligns to 6:533/541 of 5dx6A
- active site: I27 (= I23), G29 (= G25), A30 (≠ E26), K31 (≠ E27), I32 (≠ N28), E52 (= E48), T75 (= T71), Q159 (≠ E160), L249 (= L251), E276 (≠ P278), M381 (≠ N380), Q407 (≠ A406), M409 (= M408), D434 (= D433), D461 (= D460), G463 (= G462), Y464 (= Y463), M466 (= M465), V467 (≠ I466), Q470 (≠ K469), Y530 (= Y529)
- 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 (≠ N380), G382 (= G381), S383 (≠ I382), F384 (≠ Y383), Q407 (≠ A406), M409 (= M408), G433 (= G432), D434 (= D433), G435 (= G434), D461 (= D460), G463 (= G462), Y464 (= Y463), N465 (≠ G464), Y530 (= Y529)
- binding magnesium ion: S119 (≠ D120), T122 (= T123), D434 (= D433), D461 (= D460), G463 (= G462)
1t9bB Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron (see paper)
31% identity, 95% coverage: 10:528/547 of query aligns to 16:554/595 of 1t9bB
- active site: Y29 (≠ I23), G31 (= G25), G32 (≠ E26), A33 (≠ E27), I34 (≠ N28), E55 (= E48), T78 (= T71), F117 (= F110), Q118 (= Q111), E119 (≠ I112), K167 (≠ E160), R226 (≠ K215), M262 (≠ L251), V289 (vs. gap), V405 (≠ N380), L430 (= L405), G431 (≠ A406), M433 (= M408), D458 (= D433), N485 (≠ D460), E487 (≠ G462), Q488 (≠ Y463), M490 (= M465), V491 (≠ I466), W494 (= W468), L516 (≠ Y490), G521 (= G495), L522 (≠ A496)
- binding 1-(2-chlorophenylsulfonyl)-3-(4-methoxy-6-methyl-l,3,5-triazin-2-yl)urea: V107 (≠ K100), P108 (= P101), D287 (≠ E276), R288 (≠ K277), M490 (= M465), W494 (= W468)
- binding flavin-adenine dinucleotide: R157 (≠ K150), G215 (= G205), A216 (= A206), G217 (= G207), N220 (= N209), T242 (= T231), L243 (≠ Q232), Q244 (≠ M233), M259 (≠ N248), L260 (≠ A249), M262 (≠ L251), H263 (≠ S252), G282 (= G271), A283 (≠ H272), R284 (≠ D273), D286 (≠ I275), R288 (≠ K277), V289 (vs. gap), E315 (≠ N293), V316 (≠ F294), N320 (≠ E298), G333 (= G311), D334 (= D312), A335 (≠ I313), Q409 (≠ K384), M410 (≠ I385), G428 (≠ N403), G429 (≠ A404)
- binding magnesium ion: D458 (= D433), N485 (≠ D460), E487 (≠ G462)
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)
30% identity, 97% coverage: 3:532/547 of query aligns to 95:643/667 of P09342
- C161 (≠ S68) modified: Disulfide link with 307
- P194 (= P101) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ A208) modified: Disulfide link with 161
5wkcA Saccharomyces cerevisiae acetohydroxyacid synthase in complex with the herbicide penoxsulam (see paper)
31% identity, 95% coverage: 10:528/547 of query aligns to 16:550/591 of 5wkcA
- active site: Y29 (≠ I23), G31 (= G25), G32 (≠ E26), A33 (≠ E27), I34 (≠ N28), E55 (= E48), T78 (= T71), F117 (= F110), Q118 (= Q111), E119 (≠ I112), K167 (≠ E160), R222 (≠ K215), M258 (≠ L251), V285 (vs. gap), V401 (≠ N380), L426 (= L405), G427 (≠ A406), M429 (= M408), D454 (= D433), N481 (≠ D460), E483 (≠ G462), Q484 (≠ Y463), M486 (= M465), V487 (≠ I466), W490 (= W468), L512 (≠ Y490), G517 (= G495), L518 (≠ A496)
- 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 (≠ N380), G402 (= G381), Q403 (≠ I382), H404 (≠ Y383), G427 (≠ A406), M429 (= M408), G453 (= G432), D454 (= D433), A455 (≠ G434), S456 (≠ G435), M459 (= M438), N481 (≠ D460), E483 (≠ G462), Q484 (≠ Y463), G485 (= G464), M486 (= M465), V487 (≠ I466)
- binding ethaneperoxoic acid: G32 (≠ E26), Q118 (= Q111)
- binding flavin-adenine dinucleotide: R157 (≠ K150), G211 (= G205), A212 (= A206), G213 (= G207), N216 (= N209), T238 (= T231), L239 (≠ Q232), Q240 (≠ M233), L256 (≠ A249), M258 (≠ L251), G278 (= G271), A279 (≠ H272), R280 (≠ D273), R284 (≠ K277), V285 (vs. gap), E311 (≠ N293), V312 (≠ F294), N316 (≠ E298), D330 (= D312), A331 (≠ I313), M406 (≠ I385), G424 (≠ N403)
- binding magnesium ion: D454 (= D433), N481 (≠ D460), E483 (≠ G462)
- binding 2-(2,2-difluoroethoxy)-N-(5,8-dimethoxy[1,2,4]triazolo[1,5-c]pyrimidin-2-yl)-6-(trifluoromethyl)benzenesulfonamide: G32 (≠ E26), A33 (≠ E27), V107 (≠ K100), F117 (= F110), K167 (≠ E160), M258 (≠ L251), R284 (≠ K277), M486 (= M465), W490 (= W468)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: P30 (= P24), E55 (= E48)
Sites not aligning to the query:
1t9cA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, sulfometuron methyl (see paper)
31% identity, 95% coverage: 10:528/547 of query aligns to 16:555/596 of 1t9cA
- active site: Y29 (≠ I23), G31 (= G25), G32 (≠ E26), A33 (≠ E27), I34 (≠ N28), E55 (= E48), T78 (= T71), F117 (= F110), Q118 (= Q111), E119 (≠ I112), K167 (≠ E160), R227 (≠ K215), M263 (≠ L251), V290 (vs. gap), V406 (≠ N380), L431 (= L405), G432 (≠ A406), M434 (= M408), D459 (= D433), N486 (≠ D460), E488 (≠ G462), Q489 (≠ Y463), M491 (= M465), V492 (≠ I466), W495 (= W468), L517 (≠ Y490), G522 (= G495), L523 (≠ A496)
- binding methyl 2-[({[(4,6-dimethylpyrimidin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (≠ E26), V107 (≠ K100), P108 (= P101), F117 (= F110), K167 (≠ E160), D288 (≠ E276), R289 (≠ K277), W495 (= W468)
- binding flavin-adenine dinucleotide: R157 (≠ K150), G216 (= G205), A217 (= A206), G218 (= G207), N221 (= N209), T243 (= T231), L244 (≠ Q232), Q245 (≠ M233), L261 (≠ A249), M263 (≠ L251), H264 (≠ S252), G283 (= G271), A284 (≠ H272), R285 (≠ D273), D287 (≠ I275), R289 (≠ K277), V290 (vs. gap), E316 (≠ N293), V317 (≠ F294), N321 (≠ E298), G334 (= G311), D335 (= D312), A336 (≠ I313), M411 (≠ I385), G429 (≠ N403), G430 (≠ A404)
- binding magnesium ion: D459 (= D433), N486 (≠ D460), E488 (≠ G462)
Sites not aligning to the query:
1t9aA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, tribenuron methyl (see paper)
31% identity, 95% coverage: 10:528/547 of query aligns to 17:556/597 of 1t9aA
- active site: Y30 (≠ I23), G32 (= G25), G33 (≠ E26), A34 (≠ E27), I35 (≠ N28), E56 (= E48), T79 (= T71), F118 (= F110), Q119 (= Q111), E120 (≠ I112), K168 (≠ E160), R228 (≠ K215), M264 (≠ L251), V291 (vs. gap), V407 (≠ N380), L432 (= L405), G433 (≠ A406), M435 (= M408), D460 (= D433), N487 (≠ D460), E489 (≠ G462), Q490 (≠ Y463), M492 (= M465), V493 (≠ I466), W496 (= W468), L518 (≠ Y490), G523 (= G495), L524 (≠ A496)
- binding methyl 2-[4-methoxy-6-methyl-1,3,5-trazin-2-yl(methyl)carbamoylsulfamoyl]benzoate: G33 (≠ E26), V108 (≠ K100), P109 (= P101), F118 (= F110), K168 (≠ E160), M264 (≠ L251), D289 (≠ E276), R290 (≠ K277), M492 (= M465), V493 (≠ I466), W496 (= W468)
- binding flavin-adenine dinucleotide: R158 (≠ K150), G217 (= G205), A218 (= A206), G219 (= G207), N222 (= N209), T244 (= T231), L245 (≠ Q232), Q246 (≠ M233), L262 (≠ A249), M264 (≠ L251), H265 (≠ S252), G284 (= G271), A285 (≠ H272), R286 (≠ D273), D288 (≠ I275), R290 (≠ K277), V291 (vs. gap), E317 (≠ N293), V318 (≠ F294), N322 (≠ E298), G335 (= G311), D336 (= D312), A337 (≠ I313), Q411 (≠ K384), M412 (≠ I385), G430 (≠ N403), G431 (≠ A404)
- binding magnesium ion: D460 (= D433), N487 (≠ D460), E489 (≠ G462)
- binding propyl trihydrogen diphosphate: V407 (≠ N380), G408 (= G381), Q409 (≠ I382), H410 (≠ Y383), M435 (= M408), G459 (= G432), D460 (= D433), A461 (≠ G434), S462 (≠ G435), N487 (≠ D460), E489 (≠ G462), Q490 (≠ Y463), G491 (= G464), M492 (= M465)
- binding 5-{[ethyl(methyl)amino]methyl}-2-methyl-5,6-dihydropyrimidin-4-amine: G433 (≠ A406), M435 (= M408), M465 (= M438)
Sites not aligning to the query:
1n0hA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorimuron ethyl (see paper)
31% identity, 95% coverage: 10:528/547 of query aligns to 18:558/599 of 1n0hA
- active site: Y31 (≠ I23), G33 (= G25), G34 (≠ E26), A35 (≠ E27), I36 (≠ N28), E57 (= E48), T80 (= T71), F119 (= F110), Q120 (= Q111), E121 (≠ I112), K169 (≠ E160), R230 (≠ K215), M266 (≠ L251), V293 (vs. gap), V409 (≠ N380), L434 (= L405), G435 (≠ A406), M437 (= M408), D462 (= D433), N489 (≠ D460), E491 (≠ G462), Q492 (≠ Y463), M494 (= M465), V495 (≠ I466), W498 (= W468), L520 (≠ Y490), G525 (= G495), L526 (≠ A496)
- binding 4-{[(4'-amino-2'-methylpyrimidin-5'-yl)methyl]amino}pent-3-enyl diphosphate: V409 (≠ N380), G410 (= G381), Q411 (≠ I382), H412 (≠ Y383), G435 (≠ A406), M437 (= M408), G461 (= G432), D462 (= D433), A463 (≠ G434), S464 (≠ G435), M467 (= M438), N489 (≠ D460), E491 (≠ G462), Q492 (≠ Y463), G493 (= G464), V495 (≠ I466)
- binding 2-[[[[(4-chloro-6-methoxy-2-pyrimidinyl)amino]carbonyl]amino]sulfonyl]benzoic acid ethyl ester: G34 (≠ E26), A35 (≠ E27), V109 (≠ K100), P110 (= P101), F119 (= F110), K169 (≠ E160), M266 (≠ L251), D291 (≠ E276), R292 (≠ K277), V495 (≠ I466), W498 (= W468)
- binding flavin-adenine dinucleotide: R159 (≠ K150), G219 (= G205), A220 (= A206), G221 (= G207), N224 (= N209), T246 (= T231), L247 (≠ Q232), Q248 (≠ M233), L264 (≠ A249), G265 (≠ A250), M266 (≠ L251), H267 (≠ S252), G286 (= G271), A287 (≠ H272), R288 (≠ D273), D290 (≠ I275), R292 (≠ K277), V293 (vs. gap), E319 (≠ N293), V320 (≠ F294), N324 (≠ E298), G337 (= G311), D338 (= D312), A339 (≠ I313), M414 (≠ I385), G432 (≠ N403), G433 (≠ A404)
- binding magnesium ion: D462 (= D433), N489 (≠ D460), E491 (≠ G462)
- binding thiamine diphosphate: Y31 (≠ I23), E57 (= E48), P83 (= P74)
Sites not aligning to the query:
1t9dA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
31% identity, 95% coverage: 10:528/547 of query aligns to 16:555/596 of 1t9dA
- active site: Y29 (≠ I23), G31 (= G25), G32 (≠ E26), A33 (≠ E27), I34 (≠ N28), E55 (= E48), T78 (= T71), F117 (= F110), Q118 (= Q111), E119 (≠ I112), K167 (≠ E160), R227 (≠ K215), M263 (≠ L251), V290 (vs. gap), V406 (≠ N380), L431 (= L405), G432 (≠ A406), M434 (= M408), D459 (= D433), N486 (≠ D460), E488 (≠ G462), Q489 (≠ Y463), M491 (= M465), V492 (≠ I466), W495 (= W468), L517 (≠ Y490), G522 (= G495), L523 (≠ A496)
- binding methyl 2-[({[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (≠ E26), A33 (≠ E27), V107 (≠ K100), P108 (= P101), F117 (= F110), K167 (≠ E160), M263 (≠ L251), D288 (≠ E276), R289 (≠ K277), W495 (= W468)
- binding flavin-adenine dinucleotide: R157 (≠ K150), G216 (= G205), A217 (= A206), G218 (= G207), N221 (= N209), T243 (= T231), L244 (≠ Q232), Q245 (≠ M233), M260 (≠ N248), L261 (≠ A249), H264 (≠ S252), G283 (= G271), A284 (≠ H272), R285 (≠ D273), D287 (≠ I275), R289 (≠ K277), V290 (vs. gap), E316 (≠ N293), V317 (≠ F294), N321 (≠ E298), G334 (= G311), D335 (= D312), A336 (≠ I313), Q410 (≠ K384), M411 (≠ I385), G429 (≠ N403), G430 (≠ A404)
- binding magnesium ion: D459 (= D433), N486 (≠ D460), E488 (≠ G462)
- binding 2,5-dimethyl-pyrimidin-4-ylamine: E55 (= E48), P81 (= P74), Q118 (= Q111), G432 (≠ A406), M434 (= M408), M464 (= M438)
Sites not aligning to the query:
1t9bA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron (see paper)
31% identity, 95% coverage: 10:528/547 of query aligns to 16:542/583 of 1t9bA
- active site: Y29 (≠ I23), G31 (= G25), G32 (≠ E26), A33 (≠ E27), I34 (≠ N28), E55 (= E48), T78 (= T71), F117 (= F110), Q118 (= Q111), E119 (≠ I112), K167 (≠ E160), R214 (≠ K215), M250 (≠ L251), V277 (vs. gap), V393 (≠ N380), L418 (= L405), G419 (≠ A406), M421 (= M408), D446 (= D433), N473 (≠ D460), E475 (≠ G462), Q476 (≠ Y463), M478 (= M465), V479 (≠ I466), W482 (= W468), L504 (≠ Y490), G509 (= G495), L510 (≠ A496)
- binding 1-(2-chlorophenylsulfonyl)-3-(4-methoxy-6-methyl-l,3,5-triazin-2-yl)urea: V107 (≠ K100), P108 (= P101), F117 (= F110), D275 (≠ E276), R276 (≠ K277), M478 (= M465), W482 (= W468)
- binding flavin-adenine dinucleotide: R157 (≠ K150), G203 (= G205), A204 (= A206), G205 (= G207), N208 (= N209), T230 (= T231), L231 (≠ Q232), Q232 (≠ M233), M247 (≠ N248), L248 (≠ A249), M250 (≠ L251), H251 (≠ S252), G270 (= G271), A271 (≠ H272), R272 (≠ D273), D274 (≠ I275), R276 (≠ K277), V277 (vs. gap), E303 (≠ N293), V304 (≠ F294), N308 (≠ E298), D322 (= D312), A323 (≠ I313), Q397 (≠ K384), M398 (≠ I385), G416 (≠ N403), G417 (≠ A404)
- binding magnesium ion: D446 (= D433), N473 (≠ D460), E475 (≠ G462)
Sites not aligning to the query:
1t9dB Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
31% identity, 95% coverage: 10:528/547 of query aligns to 15:541/582 of 1t9dB
- active site: Y28 (≠ I23), G30 (= G25), G31 (≠ E26), A32 (≠ E27), I33 (≠ N28), E54 (= E48), T77 (= T71), F116 (= F110), Q117 (= Q111), E118 (≠ I112), K166 (≠ E160), R213 (≠ K215), M249 (≠ L251), V276 (vs. gap), V392 (≠ N380), L417 (= L405), G418 (≠ A406), M420 (= M408), D445 (= D433), N472 (≠ D460), E474 (≠ G462), Q475 (≠ Y463), M477 (= M465), V478 (≠ I466), W481 (= W468), L503 (≠ Y490), G508 (= G495), L509 (≠ A496)
- binding methyl 2-[({[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G31 (≠ E26), A32 (≠ E27), V106 (≠ K100), P107 (= P101), F116 (= F110), K166 (≠ E160), M249 (≠ L251), D274 (≠ E276), R275 (≠ K277), W481 (= W468)
- binding flavin-adenine dinucleotide: R156 (≠ K150), G202 (= G205), A203 (= A206), G204 (= G207), N207 (= N209), T229 (= T231), L230 (≠ Q232), Q231 (≠ M233), L247 (≠ A249), M249 (≠ L251), H250 (≠ S252), G269 (= G271), A270 (≠ H272), R271 (≠ D273), D273 (≠ I275), R275 (≠ K277), V276 (vs. gap), E302 (≠ N293), V303 (≠ F294), N307 (≠ E298), G320 (= G311), D321 (= D312), A322 (≠ I313), Q396 (≠ K384), M397 (≠ I385), G415 (≠ N403), G416 (≠ A404)
- binding magnesium ion: D445 (= D433), N472 (≠ D460), E474 (≠ G462)
- binding 2,5-dimethyl-pyrimidin-4-ylamine: E54 (= E48), P80 (= P74), G418 (≠ A406), M420 (= M408), M450 (= M438)
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)
31% identity, 95% coverage: 10:528/547 of query aligns to 100:646/687 of P07342
- R241 (≠ K150) binding
- 355:376 (vs. 252:273, 36% identical) binding
- 407:426 (vs. 293:312, 25% identical) binding
6u9dB Saccharomyces cerevisiae acetohydroxyacid synthase (see paper)
31% identity, 95% coverage: 10:528/547 of query aligns to 20:566/607 of 6u9dB
- active site: Y33 (≠ I23), G35 (= G25), G36 (≠ E26), A37 (≠ E27), I38 (≠ N28), E59 (= E48), T82 (= T71), F121 (= F110), Q122 (= Q111), E123 (≠ I112), K171 (≠ E160), M274 (≠ L251), V301 (vs. gap), V417 (≠ N380), G443 (≠ A406), M445 (= M408), D470 (= D433), N497 (≠ D460), E499 (≠ G462), Q500 (≠ Y463), M502 (= M465), V503 (≠ I466), W506 (= W468)
- binding methyl 2-[(4,6-dimethoxypyrimidin-2-yl)carbamoylsulfamoylmethyl]benzoate: G36 (≠ E26), V111 (≠ K100), P112 (= P101), F121 (= F110), K171 (≠ E160), D299 (≠ E276), R300 (≠ K277), M502 (= M465), W506 (= W468)
- binding flavin-adenine dinucleotide: R161 (≠ K150), A228 (= A206), G229 (= G207), N232 (= N209), T254 (= T231), L255 (≠ Q232), Q256 (≠ M233), L272 (≠ A249), M274 (≠ L251), G294 (= G271), R296 (≠ D273), D298 (≠ I275), R300 (≠ K277), V301 (vs. gap), E327 (≠ N293), V328 (≠ F294), N332 (≠ E298), D346 (= D312), A347 (≠ I313), M422 (≠ I385), G440 (≠ N403), G441 (≠ A404)
- binding magnesium ion: D470 (= D433), N497 (≠ D460)
- binding thiamine diphosphate: E59 (= E48), P85 (= P74), V417 (≠ N380), G418 (= G381), Q419 (≠ I382), H420 (≠ Y383), G443 (≠ A406), M445 (= M408), A471 (≠ G434), S472 (≠ G435), N497 (≠ D460), E499 (≠ G462), Q500 (≠ Y463), G501 (= G464), M502 (= M465), V503 (≠ I466)
Query Sequence
>PP_3365 FitnessBrowser__Putida:PP_3365
MAKAADVVVQCLENEGVEYVFGIPGEENLDLLESLRKSKIKLVLTRHEQSAGFMAATYGR
LTGKTGVSLSTLGPGATNLVTASAYAYLGGMPMMMITGQKPIKKSKQGRFQIIDVCGMMD
PITKYTHQFASADNIPARMREAFRLAEEEKPGAVHLELPEDIAAEQTDALPIPRSLHRRP
LAEHVAIEAAVEKLQNARNPILVIGAGANRKMTAKVLKQLIDKTGIPFITTQMGKGVVDE
RHPRFLGNAALSSGDFVHRAVEAADLIINIGHDVIEKPPFFMVRGGTEVIHINFRSAEVD
AVYFPQVEVIGDIANAVWQISEALNDTSHWDFTRLMAIREANEAQIAEGADDDRFPVYPQ
RMVADIRRVLPSEGIVALDNGIYKIWFARNYKAHKPNTVLLDNALATMGAGLPSAMAAHL
VHPDRPVISVCGDGGFMMNSQELETAVRLGMHITVVILRDDGYGMIRWKQANMGFTDFGL
DYGNPDFVKYAEAYGANGHRVESAEGLLPLLEHCIKTPGVHVIDCPVDYSENDRILNSEL
RERALAV
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