SitesBLAST
Comparing GFF3176 FitnessBrowser__Marino:GFF3176 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)
31% identity, 97% coverage: 11:549/556 of query aligns to 3:544/552 of 4rjkF
- binding magnesium ion: D437 (= D442), D464 (= D469), T466 (≠ A471)
- binding pyruvic acid: A25 (≠ E33), K26 (≠ E34)
- binding thiamine diphosphate: P23 (= P31), E47 (= E55), P73 (= P81), G385 (= G390), S386 (≠ M391), H387 (≠ Y392), Q410 (≠ A415), L412 (≠ M417), G436 (= G441), D437 (= D442), G438 (= G443), G439 (= G444), T466 (≠ A471), Y467 (= Y472), D468 (≠ G473), M469 (= M474), V470 (≠ I475), Y533 (= Y538)
4rjkG Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
31% identity, 97% coverage: 11:549/556 of query aligns to 3:544/553 of 4rjkG
- binding magnesium ion: D437 (= D442), D464 (= D469), T466 (≠ A471)
- 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 (= E55), Q110 (= Q118)
- binding thiamine diphosphate: I384 (≠ N389), G385 (= G390), S386 (≠ M391), H387 (≠ Y392), Q410 (≠ A415), L412 (≠ M417), G436 (= G441), D437 (= D442), G438 (= G443), G439 (= G444), T466 (≠ A471), Y467 (= Y472), D468 (≠ G473), M469 (= M474), V470 (≠ I475), Y533 (= Y538)
4rjiC Acetolactate synthase from bacillus subtilis bound to thdp - crystal form i (see paper)
31% identity, 97% coverage: 11:549/556 of query aligns to 4:545/555 of 4rjiC
- binding magnesium ion: D438 (= D442), D465 (= D469), T467 (≠ A471)
- binding thiamine diphosphate: P24 (= P31), E48 (= E55), P74 (= P81), S387 (≠ M391), H388 (≠ Y392), Q411 (≠ A415), G437 (= G441), D438 (= D442), G439 (= G443), G440 (= G444), T467 (≠ A471), Y468 (= Y472), D469 (≠ G473), M470 (= M474), V471 (≠ I475), Y534 (= Y538)
5dx6B Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
33% identity, 97% coverage: 3:541/556 of query aligns to 8:544/557 of 5dx6B
- active site: I38 (≠ V30), G40 (= G32), A41 (≠ E33), K42 (≠ E34), I43 (≠ N35), E63 (= E55), T86 (= T78), H125 (≠ F117), Q126 (= Q118), S127 (≠ I119), Q175 (≠ E167), L268 (= L260), E295 (≠ P287), M392 (≠ N389), Q418 (≠ A415), M420 (= M417), D445 (= D442), D472 (= D469), G474 (≠ A471), Y475 (= Y472), M477 (= M474), V478 (≠ I475), Q481 (≠ K478), Y541 (= Y538)
- binding 3-fluoro-2-oxopropanoic acid: G264 (= G256), R265 (≠ N257), Q272 (≠ S261), A400 (= A397), R401 (= R398), Y404 (≠ R401)
- binding magnesium ion: S135 (≠ R127), T138 (= T130), D445 (= D442), D472 (= D469), G474 (≠ A471)
- binding thiamine diphosphate: G393 (= G390), S394 (≠ M391), F395 (≠ Y392), Q418 (≠ A415), M420 (= M417), G444 (= G441), D445 (= D442), G446 (= G443), D472 (= D469), G474 (≠ A471), Y475 (= Y472), N476 (≠ G473), M477 (= M474), V478 (≠ I475), Y541 (= Y538)
5d6rB Acetolactate synthase from klebsiella pneumoniae in complex with mechanism-based inhibitor
32% identity, 96% coverage: 10:541/556 of query aligns to 6:538/548 of 5d6rB
- active site: I26 (≠ V30), G28 (= G32), A29 (≠ E33), K30 (≠ E34), I31 (≠ N35), E51 (= E55), T74 (= T78), H113 (≠ F117), Q114 (= Q118), S115 (≠ I119), Q163 (≠ E167), L254 (= L260), E281 (≠ P287), M386 (≠ N389), Q412 (≠ A415), M414 (= M417), D439 (= D442), D466 (= D469), G468 (≠ A471), Y469 (= Y472), M471 (= M474), V472 (≠ I475), Q475 (≠ K478), Y535 (= Y538)
- 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 (≠ N389), G387 (= G390), S388 (≠ M391), Q412 (≠ A415), M414 (= M417), D439 (= D442), G440 (= G443), G468 (≠ A471), Y469 (= Y472), N470 (≠ G473), M471 (= M474), Y535 (= Y538)
- binding magnesium ion: R63 (= R67), Q212 (≠ R219), D439 (= D442), D466 (= D469), G468 (≠ A471)
1ozgA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate (see paper)
32% identity, 96% coverage: 10:541/556 of query aligns to 7:541/549 of 1ozgA
- active site: I27 (≠ V30), G29 (= G32), A30 (≠ E33), K31 (≠ E34), I32 (≠ N35), E52 (= E55), T75 (= T78), H114 (≠ F117), Q115 (= Q118), S116 (≠ I119), Q164 (≠ E167), L257 (= L260), E284 (≠ P287), M389 (≠ N389), Q415 (≠ A415), M417 (= M417), D442 (= D442), D469 (= D469), G471 (≠ A471), Y472 (= Y472), M474 (= M474), V475 (≠ I475), Q478 (≠ K478), Y538 (= Y538)
- binding 2-hydroxyethyl dihydrothiachrome diphosphate: M389 (≠ N389), G390 (= G390), S391 (≠ M391), F392 (≠ Y392), Q415 (≠ A415), M417 (= M417), G441 (= G441), D442 (= D442), G443 (= G443), D469 (= D469), G471 (≠ A471), Y472 (= Y472), N473 (≠ G473), M474 (= M474), V475 (≠ I475), Y538 (= Y538)
- binding magnesium ion: D442 (= D442), D469 (= D469), G471 (≠ A471)
- binding phosphate ion: G253 (= G256), R254 (≠ N257), Q261 (≠ S261), R347 (≠ H354), R398 (= R398), Y401 (≠ R401)
1ozfA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors (see paper)
32% identity, 96% coverage: 10:541/556 of query aligns to 6:537/545 of 1ozfA
- active site: I26 (≠ V30), G28 (= G32), A29 (≠ E33), K30 (≠ E34), I31 (≠ N35), E51 (= E55), T74 (= T78), H113 (≠ F117), Q114 (= Q118), S115 (≠ I119), Q163 (≠ E167), L253 (= L260), E280 (≠ P287), M385 (≠ N389), Q411 (≠ A415), M413 (= M417), D438 (= D442), D465 (= D469), G467 (≠ A471), Y468 (= Y472), M470 (= M474), V471 (≠ I475), Q474 (≠ K478), Y534 (= Y538)
- binding magnesium ion: D438 (= D442), D465 (= D469), G467 (≠ A471)
- binding phosphate ion: G249 (= G256), R250 (≠ N257), Q257 (≠ S261), R343 (≠ H354), R394 (= R398), L396 (≠ Y400), Y397 (≠ R401)
- binding thiamine diphosphate: G386 (= G390), S387 (≠ M391), F388 (≠ Y392), Q411 (≠ A415), M413 (= M417), G437 (= G441), D438 (= D442), G439 (= G443), D465 (= D469), G467 (≠ A471), Y468 (= Y472), N469 (≠ G473), M470 (= M474), V471 (≠ I475), Y534 (= Y538)
5dx6A Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
32% identity, 96% coverage: 10:541/556 of query aligns to 7:533/541 of 5dx6A
- active site: I27 (≠ V30), G29 (= G32), A30 (≠ E33), K31 (≠ E34), I32 (≠ N35), E52 (= E55), T75 (= T78), Q159 (≠ E167), L249 (= L260), E276 (≠ P287), M381 (≠ N389), Q407 (≠ A415), M409 (= M417), D434 (= D442), D461 (= D469), G463 (≠ A471), Y464 (= Y472), M466 (= M474), V467 (≠ I475), Q470 (≠ K478), Y530 (= Y538)
- 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 (≠ N389), G382 (= G390), S383 (≠ M391), F384 (≠ Y392), Q407 (≠ A415), M409 (= M417), G433 (= G441), D434 (= D442), G435 (= G443), D461 (= D469), G463 (≠ A471), Y464 (= Y472), N465 (≠ G473), Y530 (= Y538)
- binding magnesium ion: S119 (≠ R127), T122 (= T130), D434 (= D442), D461 (= D469), G463 (≠ A471)
5wdgA Acetolactate synthase from klebsiella pneumoniae in complex with a reaction intermediate
32% identity, 96% coverage: 10:541/556 of query aligns to 7:530/538 of 5wdgA
- active site: I27 (≠ V30), G29 (= G32), A30 (≠ E33), K31 (≠ E34), I32 (≠ N35), E52 (= E55), T75 (= T78), Q157 (≠ E167), L246 (= L260), E273 (≠ P287), M378 (≠ N389), Q404 (≠ A415), M406 (= M417), D431 (= D442), D458 (= D469), G460 (≠ A471), Y461 (= Y472), M463 (= M474), V464 (≠ I475), Q467 (≠ K478), Y527 (= Y538)
- 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 (≠ N389), S380 (≠ M391), F381 (≠ Y392), Q404 (≠ A415), M406 (= M417), G430 (= G441), D431 (= D442), G432 (= G443), G433 (= G444), D458 (= D469), G460 (≠ A471), Y461 (= Y472), N462 (≠ G473), M463 (= M474), V464 (≠ I475), Y527 (= Y538)
- binding magnesium ion: R64 (= R67), S117 (≠ R127), T120 (= T130), Q204 (≠ R219), D431 (= D442), D458 (= D469), G460 (≠ A471)
- binding pyruvic acid: G94 (= G97), R147 (= R157)
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, 96% coverage: 9:541/556 of query aligns to 94:643/667 of P09342
- C161 (= C75) modified: Disulfide link with 307
- P194 (= P108) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ A217) 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, 96% coverage: 9:541/556 of query aligns to 91:640/664 of P09114
- P191 (= P108) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
- W568 (= W477) mutation to L: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191.
3ea4A Arabidopsis thaliana acetohydroxyacid synthase in complex with monosulfuron-ester (see paper)
30% identity, 96% coverage: 9:541/556 of query aligns to 11:560/582 of 3ea4A
- active site: Y32 (≠ V30), G34 (= G32), G35 (≠ E33), A36 (≠ E34), S37 (≠ N35), E58 (= E55), T81 (= T78), F120 (= F117), Q121 (= Q118), E122 (≠ I119), K170 (≠ E167), M265 (≠ L260), V292 (= V283), V399 (≠ N389), G425 (≠ A415), M427 (= M417), D452 (= D442), N479 (≠ D469), H481 (≠ A471), L482 (≠ Y472), M484 (= M474), V485 (≠ I475), W488 (= W477), H557 (≠ Y538)
- binding methyl 2-{[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl}benzoate: D290 (≠ H281), R291 (≠ D282), W488 (= W477)
- binding flavin-adenine dinucleotide-n5-isobutyl ketone: R160 (= R157), G221 (= G214), G222 (≠ A215), G223 (= G216), T245 (= T240), L246 (≠ Q241), M247 (= M242), L263 (= L255), G264 (= G256), M265 (≠ L260), H266 (≠ S261), G285 (= G280), R287 (vs. gap), D289 (vs. gap), R291 (≠ D282), D309 (≠ N302), I310 (≠ F303), G327 (= G320), D328 (= D321), V329 (≠ I322), M404 (≠ L394), G422 (≠ N412)
- binding magnesium ion: D452 (= D442), N479 (≠ D469), H481 (≠ A471)
- 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 (≠ N389), G400 (= G390), Q401 (≠ M391), H402 (≠ Y392), M427 (= M417), G451 (= G441), D452 (= D442), G453 (= G443), S454 (≠ G444), N479 (≠ D469), H481 (≠ A471), L482 (≠ Y472), G483 (= G473), M484 (= M474), V485 (≠ I475)
Sites not aligning to the query:
3e9yA Arabidopsis thaliana acetohydroxyacid synthase in complex with monosulfuron (see paper)
30% identity, 96% coverage: 9:541/556 of query aligns to 11:560/582 of 3e9yA
- active site: Y32 (≠ V30), G34 (= G32), G35 (≠ E33), A36 (≠ E34), S37 (≠ N35), E58 (= E55), T81 (= T78), F120 (= F117), Q121 (= Q118), E122 (≠ I119), K170 (≠ E167), M265 (≠ L260), V292 (= V283), V399 (≠ N389), G425 (≠ A415), M427 (= M417), D452 (= D442), N479 (≠ D469), H481 (≠ A471), L482 (≠ Y472), M484 (= M474), V485 (≠ I475), W488 (= W477), H557 (≠ Y538)
- binding N-[(4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide: D290 (≠ H281), R291 (≠ D282), W488 (= W477)
- binding flavin-adenine dinucleotide-n5-isobutyl ketone: R160 (= R157), G221 (= G214), G222 (≠ A215), G223 (= G216), T245 (= T240), L246 (≠ Q241), M247 (= M242), L263 (= L255), G285 (= G280), R287 (vs. gap), D289 (vs. gap), R291 (≠ D282), D309 (≠ N302), I310 (≠ F303), G327 (= G320), D328 (= D321), V329 (≠ I322), M404 (≠ L394), G422 (≠ N412)
- binding magnesium ion: D452 (= D442), N479 (≠ D469), H481 (≠ A471)
- 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 (≠ N389), G400 (= G390), Q401 (≠ M391), H402 (≠ Y392), M427 (= M417), G451 (= G441), G453 (= G443), S454 (≠ G444), N479 (≠ D469), H481 (≠ A471), L482 (≠ Y472), G483 (= G473), M484 (= M474), V485 (≠ I475)
Sites not aligning to the query:
5k3sA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a pyrimidinyl-benzoate herbicide, bispyribac-sodium (see paper)
30% identity, 96% coverage: 9:541/556 of query aligns to 12:561/583 of 5k3sA
- active site: Y33 (≠ V30), G35 (= G32), G36 (≠ E33), A37 (≠ E34), S38 (≠ N35), E59 (= E55), T82 (= T78), F121 (= F117), Q122 (= Q118), E123 (≠ I119), K171 (≠ E167), M266 (≠ L260), V293 (= V283), V400 (≠ N389), G426 (≠ A415), M428 (= M417), D453 (= D442), N480 (≠ D469), H482 (≠ A471), L483 (≠ Y472), M485 (= M474), V486 (≠ I475), W489 (= W477), H558 (≠ Y538)
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: R292 (≠ D282), M485 (= M474), W489 (= W477)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G214), G223 (≠ A215), G224 (= G216), T246 (= T240), L247 (≠ Q241), M248 (= M242), L264 (= L255), M266 (≠ L260), G286 (= G280), R288 (vs. gap), D290 (vs. gap), V293 (= V283), D310 (≠ N302), I311 (≠ F303), D329 (= D321), V330 (≠ I322), M405 (≠ L394), G423 (≠ N412)
- binding magnesium ion: D453 (= D442), N480 (≠ D469), H482 (≠ A471)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (≠ N389), G401 (= G390), Q402 (≠ M391), H403 (≠ Y392), G426 (≠ A415), M428 (= M417), D453 (= D442), G454 (= G443), S455 (≠ G444), N480 (≠ D469), H482 (≠ A471), L483 (≠ Y472), G484 (= G473), M485 (= M474), V486 (≠ I475)
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)
30% identity, 96% coverage: 9:541/556 of query aligns to 97:646/670 of P17597
- A122 (≠ E34) mutation to V: Reduced catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- M124 (≠ L36) 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 (= E55) binding
- S186 (≠ G97) binding
- P197 (= P108) mutation to S: In csr1-1/GH50; resistant to sulfonylurea but not to imidazolinone herbicides.
- R199 (≠ K110) mutation R->A,E: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- Q207 (= Q118) binding
- K220 (= K131) binding
- R246 (= R157) binding ; binding
- K256 (≠ E167) binding
- G308 (≠ A215) binding
- TL 331:332 (≠ TQ 240:241) binding
- C340 (vs. gap) modified: Cysteine sulfinic acid (-SO2H)
- LG---MH 349:352 (≠ LGNAALS 255:261) binding
- GVRFD 371:375 (≠ G---- 280) binding
- DR 376:377 (≠ HD 281:282) binding
- DI 395:396 (≠ NF 302:303) binding
- DV 414:415 (≠ DI 321:322) binding
- QH 487:488 (≠ MY 391:392) binding
- GG 508:509 (≠ NA 412:413) binding
- GAM 511:513 (≠ ASM 415:417) binding
- D538 (= D442) binding
- DGS 538:540 (≠ DGG 442:444) binding
- N565 (≠ D469) binding
- NQHLGM 565:570 (≠ DSAYGM 469:474) binding
- H567 (≠ A471) binding
- W574 (= W477) 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.
8et4A Crystal structure of wild-type arabidopsis thaliana acetohydroxyacid synthase in complex with amidosulfuron (see paper)
30% identity, 96% coverage: 9:541/556 of query aligns to 12:561/582 of 8et4A
- 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 (≠ N389), G401 (= G390), Q402 (≠ M391), H403 (≠ Y392), G426 (≠ A415), M428 (= M417), G452 (= G441), D453 (= D442), G454 (= G443), S455 (≠ G444), M458 (= M447), N480 (≠ D469), H482 (≠ A471), L483 (≠ Y472), G484 (= G473), M485 (= M474), V486 (≠ I475)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G214), G223 (≠ A215), G224 (= G216), T246 (= T240), L247 (≠ Q241), M248 (= M242), L264 (= L255), M266 (≠ L260), H267 (≠ S261), G286 (= G280), V287 (vs. gap), R288 (vs. gap), D290 (vs. gap), R292 (≠ D282), V293 (= V283), D310 (≠ N302), I311 (≠ F303), D329 (= D321), V330 (≠ I322), M405 (≠ L394), G423 (≠ N412)
- binding magnesium ion: F370 (≠ L355), D453 (= D442), M458 (= M447), Q461 (= Q450), N480 (≠ D469), H482 (≠ A471), K533 (≠ T513)
- binding N-{[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl}-N-methylmethanesulfonamide: M266 (≠ L260), R292 (≠ D282), M485 (= M474), W489 (= W477)
Sites not aligning to the query:
5wj1A Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a triazolopyrimidine herbicide, penoxsulam (see paper)
30% identity, 96% coverage: 9:541/556 of query aligns to 12:561/582 of 5wj1A
- active site: Y33 (≠ V30), G35 (= G32), G36 (≠ E33), A37 (≠ E34), S38 (≠ N35), E59 (= E55), T82 (= T78), F121 (= F117), Q122 (= Q118), E123 (≠ I119), K171 (≠ E167), M266 (≠ L260), V293 (= V283), V400 (≠ N389), G426 (≠ A415), M428 (= M417), D453 (= D442), N480 (≠ D469), H482 (≠ A471), L483 (≠ Y472), M485 (= M474), V486 (≠ I475), W489 (= W477), H558 (≠ Y538)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G214), G223 (≠ A215), G224 (= G216), T246 (= T240), L247 (≠ Q241), M248 (= M242), M263 (≠ Y254), L264 (= L255), G286 (= G280), R288 (vs. gap), V293 (= V283), D310 (≠ N302), I311 (≠ F303), D329 (= D321), V330 (≠ I322), M405 (≠ L394), G423 (≠ N412), G424 (≠ A413)
- binding magnesium ion: D453 (= D442), N480 (≠ D469), H482 (≠ A471)
- binding 2-(2,2-difluoroethoxy)-N-(5,8-dimethoxy[1,2,4]triazolo[1,5-c]pyrimidin-2-yl)-6-(trifluoromethyl)benzenesulfonamide: M266 (≠ L260), D291 (≠ H281), R292 (≠ D282), M485 (= M474), W489 (= W477)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (≠ N389), G401 (= G390), Q402 (≠ M391), H403 (≠ Y392), M428 (= M417), D453 (= D442), G454 (= G443), S455 (≠ G444), M458 (= M447), N480 (≠ D469), H482 (≠ A471), L483 (≠ Y472), G484 (= G473), M485 (= M474), V486 (≠ I475)
Sites not aligning to the query:
5k6tA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a sulfonylamino-carbonyl-triazolinone herbicide, propoxycarbazone-sodium (see paper)
30% identity, 96% coverage: 9:541/556 of query aligns to 12:561/582 of 5k6tA
- active site: Y33 (≠ V30), G35 (= G32), G36 (≠ E33), A37 (≠ E34), S38 (≠ N35), E59 (= E55), T82 (= T78), F121 (= F117), Q122 (= Q118), E123 (≠ I119), K171 (≠ E167), M266 (≠ L260), V293 (= V283), V400 (≠ N389), G426 (≠ A415), M428 (= M417), D453 (= D442), N480 (≠ D469), H482 (≠ A471), L483 (≠ Y472), M485 (= M474), V486 (≠ I475), W489 (= W477), H558 (≠ Y538)
- binding methyl 2-[(4-methyl-5-oxidanylidene-3-propoxy-1,2,4-triazol-1-yl)carbonylsulfamoyl]benzoate: H267 (≠ S261), R292 (≠ D282), M485 (= M474), W489 (= W477)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G214), G223 (≠ A215), G224 (= G216), T246 (= T240), L247 (≠ Q241), M248 (= M242), L264 (= L255), G286 (= G280), R288 (vs. gap), D290 (vs. gap), R292 (≠ D282), V293 (= V283), D310 (≠ N302), I311 (≠ F303), D329 (= D321), V330 (≠ I322), Q404 (≠ K393), M405 (≠ L394), G423 (≠ N412)
- binding magnesium ion: D453 (= D442), N480 (≠ D469), H482 (≠ A471)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: V400 (≠ N389), G401 (= G390), Q402 (≠ M391), H403 (≠ Y392), G426 (≠ A415), M428 (= M417), G452 (= G441), G454 (= G443), S455 (≠ G444), N480 (≠ D469), H482 (≠ A471), L483 (≠ Y472), G484 (= G473)
Sites not aligning to the query:
5k6rA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a sulfonylamino-carbonyl-triazolinone herbicide, thiencarbazone-methyl (see paper)
30% identity, 96% coverage: 9:541/556 of query aligns to 12:561/582 of 5k6rA
- active site: Y33 (≠ V30), G35 (= G32), G36 (≠ E33), A37 (≠ E34), S38 (≠ N35), E59 (= E55), T82 (= T78), F121 (= F117), Q122 (= Q118), E123 (≠ I119), K171 (≠ E167), M266 (≠ L260), V293 (= V283), V400 (≠ N389), G426 (≠ A415), M428 (= M417), D453 (= D442), N480 (≠ D469), H482 (≠ A471), L483 (≠ Y472), M485 (= M474), V486 (≠ I475), W489 (= W477), H558 (≠ Y538)
- binding methyl 4-[(3-methoxy-4-methyl-5-oxidanylidene-1,2,4-triazol-1-yl)carbonylsulfamoyl]-5-methyl-thiophene-3-carboxylate: R292 (≠ D282), W489 (= W477)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G214), G223 (≠ A215), G224 (= G216), T246 (= T240), L247 (≠ Q241), M248 (= M242), L264 (= L255), M266 (≠ L260), G286 (= G280), R288 (vs. gap), R292 (≠ D282), V293 (= V283), D310 (≠ N302), I311 (≠ F303), G328 (= G320), D329 (= D321), V330 (≠ I322), M405 (≠ L394), G423 (≠ N412)
- binding magnesium ion: D453 (= D442), N480 (≠ D469), H482 (≠ A471)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: V400 (≠ N389), G401 (= G390), Q402 (≠ M391), H403 (≠ Y392), G426 (≠ A415), M428 (= M417), D453 (= D442), G454 (= G443), S455 (≠ G444), M458 (= M447), N480 (≠ D469), H482 (≠ A471), L483 (≠ Y472), G484 (= G473), M485 (= M474), V486 (≠ I475)
Sites not aligning to the query:
1z8nA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with an imidazolinone herbicide, imazaquin (see paper)
30% identity, 96% coverage: 9:541/556 of query aligns to 12:561/582 of 1z8nA
- active site: Y33 (≠ V30), G35 (= G32), G36 (≠ E33), A37 (≠ E34), S38 (≠ N35), E59 (= E55), T82 (= T78), F121 (= F117), Q122 (= Q118), E123 (≠ I119), K171 (≠ E167), M266 (≠ L260), V293 (= V283), V400 (≠ N389), G426 (≠ A415), M428 (= M417), D453 (= D442), N480 (≠ D469), H482 (≠ A471), L483 (≠ Y472), M485 (= M474), V486 (≠ I475), W489 (= W477), H558 (≠ Y538)
- binding 2-(4-isopropyl-4-methyl-5-oxo-4,5-dihydro-1h-imidazol-2-yl)quinoline-3-carboxylic acid: K135 (= K131), R161 (= R157), Y191 (≠ D185), R194 (= R188), D291 (≠ H281), R292 (≠ D282), D312 (≠ S304), W489 (= W477)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G214), G224 (= G216), T246 (= T240), L247 (≠ Q241), M248 (= M242), L264 (= L255), G265 (= G256), M266 (≠ L260), H267 (≠ S261), G286 (= G280), V287 (vs. gap), R288 (vs. gap), D290 (vs. gap), R292 (≠ D282), V293 (= V283), D310 (≠ N302), I311 (≠ F303), D329 (= D321), V330 (≠ I322), M405 (≠ L394), G423 (≠ N412), G424 (≠ A413)
- binding magnesium ion: D453 (= D442), N480 (≠ D469)
- binding thiamine diphosphate: V400 (≠ N389), G401 (= G390), Q402 (≠ M391), H403 (≠ Y392), G426 (≠ A415), M428 (= M417), G452 (= G441), G454 (= G443), S455 (≠ G444), N480 (≠ D469), H482 (≠ A471), L483 (≠ Y472), G484 (= G473), M485 (= M474), V486 (≠ I475)
Sites not aligning to the query:
Query Sequence
>GFF3176 FitnessBrowser__Marino:GFF3176
MANEQTPARNGAELFIRALENEGVEYIFAVPGEENLAFLEALRTSSIQLVLNRHEQAAGF
MAATYGRLTGRVGVCLSTLGPGATNFVTAAAYAQLGGMPMMMISGQKPIKSSKQGLFQIL
DVVDLMRPLTKYTRQISNANTIPAKVREAFRLASEERPGAVHLELPEDIADEAPESDTHI
FKPSDARRPSASPKSLEMACEMLREARHPLIMIGAGANRKRVSQALLHLVNVTGIPFFTT
QMGKGVVDERHPRYLGNAALSAGDFVHCAIDRADLVINVGHDVVEKPPFFMTPGGKKVIH
VNFSAADVDPVYFPQHEVVGDIANSVEYMAENCGQCANHDFTRLMEVKEAVDAHLQERAE
DDRFPVIPQRIVHDVRQVMPDDGIITLDNGMYKLWFARNYRAYDNNTVLLDNALASMGAG
LPSGMMASMLYPDLKVMAICGDGGFMMNSQELETAVRLNLNLVVLIINDSAYGMIKWKQG
QEGYSDFGLDYRNPDFVTYAQSYGAKGHRLTRTEDLRPTLEGALAEGGVHVVDVPVDYSE
NRRVFDEELAELTCKL
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