SitesBLAST
Comparing WP_013835722.1 NCBI__GCF_000214825.1:WP_013835722.1 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)
4rjiC Acetolactate synthase from bacillus subtilis bound to thdp - crystal form i (see paper)
39% identity, 99% coverage: 3:540/543 of query aligns to 4:553/555 of 4rjiC
- binding magnesium ion: D438 (= D430), D465 (= D457), T467 (≠ G459)
- binding thiamine diphosphate: P24 (= P23), E48 (= E47), P74 (= P73), S387 (≠ A379), H388 (= H380), Q411 (≠ A403), G437 (= G429), D438 (= D430), G439 (≠ A431), G440 (= G432), T467 (≠ G459), Y468 (= Y460), D469 (≠ G461), M470 (≠ L462), V471 (≠ I463), Y534 (= Y526)
4rjkG Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
39% identity, 99% coverage: 3:540/543 of query aligns to 3:552/553 of 4rjkG
- binding magnesium ion: D437 (= D430), D464 (= D457), T466 (≠ G459)
- 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 (= E47), Q110 (= Q110)
- binding thiamine diphosphate: I384 (≠ V377), G385 (= G378), S386 (≠ A379), H387 (= H380), Q410 (≠ A403), L412 (≠ M405), G436 (= G429), D437 (= D430), G438 (≠ A431), G439 (= G432), T466 (≠ G459), Y467 (= Y460), D468 (≠ G461), M469 (≠ L462), V470 (≠ I463), Y533 (= Y526)
4rjkF Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
39% identity, 99% coverage: 3:540/543 of query aligns to 3:552/552 of 4rjkF
- binding magnesium ion: D437 (= D430), D464 (= D457), T466 (≠ G459)
- binding pyruvic acid: A25 (≠ E25), K26 (≠ E26)
- binding thiamine diphosphate: P23 (= P23), E47 (= E47), P73 (= P73), G385 (= G378), S386 (≠ A379), H387 (= H380), Q410 (≠ A403), L412 (≠ M405), G436 (= G429), D437 (= D430), G438 (≠ A431), G439 (= G432), T466 (≠ G459), Y467 (= Y460), D468 (≠ G461), M469 (≠ L462), V470 (≠ I463), Y533 (= Y526)
5d6rB Acetolactate synthase from klebsiella pneumoniae in complex with mechanism-based inhibitor
36% identity, 99% coverage: 2:536/543 of query aligns to 6:545/548 of 5d6rB
- active site: I26 (= I22), G28 (= G24), A29 (≠ E25), K30 (≠ E26), I31 (≠ N27), E51 (= E47), T74 (= T70), H113 (= H109), Q114 (= Q110), S115 (≠ V111), Q163 (≠ E159), L254 (≠ T247), E281 (≠ H277), M386 (≠ V377), Q412 (≠ A403), M414 (= M405), D439 (= D430), D466 (= D457), G468 (= G459), Y469 (= Y460), M471 (≠ L462), V472 (≠ I463), Q475 (≠ K466), Y535 (= Y526)
- 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 (≠ V377), G387 (= G378), S388 (≠ A379), Q412 (≠ A403), M414 (= M405), D439 (= D430), G440 (≠ A431), G468 (= G459), Y469 (= Y460), N470 (≠ G461), M471 (≠ L462), Y535 (= Y526)
- binding magnesium ion: R63 (= R59), Q212 (≠ R209), D439 (= D430), D466 (= D457), G468 (= G459)
1ozfA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors (see paper)
36% identity, 99% coverage: 2:536/543 of query aligns to 6:544/545 of 1ozfA
- active site: I26 (= I22), G28 (= G24), A29 (≠ E25), K30 (≠ E26), I31 (≠ N27), E51 (= E47), T74 (= T70), H113 (= H109), Q114 (= Q110), S115 (≠ V111), Q163 (≠ E159), L253 (≠ T247), E280 (≠ H277), M385 (≠ V377), Q411 (≠ A403), M413 (= M405), D438 (= D430), D465 (= D457), G467 (= G459), Y468 (= Y460), M470 (≠ L462), V471 (≠ I463), Q474 (≠ K466), Y534 (= Y526)
- binding magnesium ion: D438 (= D430), D465 (= D457), G467 (= G459)
- binding phosphate ion: G249 (≠ L243), R250 (≠ A244), Q257 (= Q251), R343 (≠ N328), R394 (= R386), L396 (= L387), Y397 (= Y388)
- binding thiamine diphosphate: G386 (= G378), S387 (≠ A379), F388 (≠ H380), Q411 (≠ A403), M413 (= M405), G437 (= G429), D438 (= D430), G439 (≠ A431), D465 (= D457), G467 (= G459), Y468 (= Y460), N469 (≠ G461), M470 (≠ L462), V471 (≠ I463), Y534 (= Y526)
5dx6B Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
36% identity, 99% coverage: 2:536/543 of query aligns to 18:551/557 of 5dx6B
- active site: I38 (= I22), G40 (= G24), A41 (≠ E25), K42 (≠ E26), I43 (≠ N27), E63 (= E47), T86 (= T70), H125 (= H109), Q126 (= Q110), S127 (≠ V111), Q175 (≠ E159), L268 (≠ T247), E295 (≠ H277), M392 (≠ V377), Q418 (≠ A403), M420 (= M405), D445 (= D430), D472 (= D457), G474 (= G459), Y475 (= Y460), M477 (≠ L462), V478 (≠ I463), Q481 (≠ K466), Y541 (= Y526)
- binding 3-fluoro-2-oxopropanoic acid: G264 (≠ L243), R265 (≠ A244), Q272 (= Q251), A400 (= A385), R401 (= R386), Y404 (≠ P389)
- binding magnesium ion: S135 (≠ Q119), T138 (= T122), D445 (= D430), D472 (= D457), G474 (= G459)
- binding thiamine diphosphate: G393 (= G378), S394 (≠ A379), F395 (≠ H380), Q418 (≠ A403), M420 (= M405), G444 (= G429), D445 (= D430), G446 (≠ A431), D472 (= D457), G474 (= G459), Y475 (= Y460), N476 (≠ G461), M477 (≠ L462), V478 (≠ I463), Y541 (= Y526)
1ozgA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate (see paper)
36% identity, 99% coverage: 2:536/543 of query aligns to 7:548/549 of 1ozgA
- active site: I27 (= I22), G29 (= G24), A30 (≠ E25), K31 (≠ E26), I32 (≠ N27), E52 (= E47), T75 (= T70), H114 (= H109), Q115 (= Q110), S116 (≠ V111), Q164 (≠ E159), L257 (≠ T247), E284 (≠ H277), M389 (≠ V377), Q415 (≠ A403), M417 (= M405), D442 (= D430), D469 (= D457), G471 (= G459), Y472 (= Y460), M474 (≠ L462), V475 (≠ I463), Q478 (≠ K466), Y538 (= Y526)
- binding 2-hydroxyethyl dihydrothiachrome diphosphate: M389 (≠ V377), G390 (= G378), S391 (≠ A379), F392 (≠ H380), Q415 (≠ A403), M417 (= M405), G441 (= G429), D442 (= D430), G443 (≠ A431), D469 (= D457), G471 (= G459), Y472 (= Y460), N473 (≠ G461), M474 (≠ L462), V475 (≠ I463), Y538 (= Y526)
- binding magnesium ion: D442 (= D430), D469 (= D457), G471 (= G459)
- binding phosphate ion: G253 (≠ L243), R254 (≠ A244), Q261 (= Q251), R347 (≠ N328), R398 (= R386), Y401 (= Y388)
5wdgA Acetolactate synthase from klebsiella pneumoniae in complex with a reaction intermediate
36% identity, 99% coverage: 2:536/543 of query aligns to 7:537/538 of 5wdgA
- active site: I27 (= I22), G29 (= G24), A30 (≠ E25), K31 (≠ E26), I32 (≠ N27), E52 (= E47), T75 (= T70), Q157 (≠ E159), L246 (≠ T247), E273 (≠ H277), M378 (≠ V377), Q404 (≠ A403), M406 (= M405), D431 (= D430), D458 (= D457), G460 (= G459), Y461 (= Y460), M463 (≠ L462), V464 (≠ I463), Q467 (≠ K466), Y527 (= Y526)
- 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 (≠ V377), S380 (≠ A379), F381 (≠ H380), Q404 (≠ A403), M406 (= M405), G430 (= G429), D431 (= D430), G432 (≠ A431), G433 (= G432), D458 (= D457), G460 (= G459), Y461 (= Y460), N462 (≠ G461), M463 (≠ L462), V464 (≠ I463), Y527 (= Y526)
- binding magnesium ion: R64 (= R59), S117 (≠ Q119), T120 (= T122), Q204 (≠ R209), D431 (= D430), D458 (= D457), G460 (= G459)
- binding pyruvic acid: G94 (≠ H89), R147 (≠ K149)
5dx6A Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
36% identity, 99% coverage: 2:536/543 of query aligns to 7:540/541 of 5dx6A
- active site: I27 (= I22), G29 (= G24), A30 (≠ E25), K31 (≠ E26), I32 (≠ N27), E52 (= E47), T75 (= T70), Q159 (≠ E159), L249 (≠ T247), E276 (≠ H277), M381 (≠ V377), Q407 (≠ A403), M409 (= M405), D434 (= D430), D461 (= D457), G463 (= G459), Y464 (= Y460), M466 (≠ L462), V467 (≠ I463), Q470 (≠ K466), Y530 (= Y526)
- 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 (≠ V377), G382 (= G378), S383 (≠ A379), F384 (≠ H380), Q407 (≠ A403), M409 (= M405), G433 (= G429), D434 (= D430), G435 (≠ A431), D461 (= D457), G463 (= G459), Y464 (= Y460), N465 (≠ G461), Y530 (= Y526)
- binding magnesium ion: S119 (≠ Q119), T122 (= T122), D434 (= D430), D461 (= D457), G463 (= G459)
6lpiB Crystal structure of ahas holo-enzyme (see paper)
33% identity, 98% coverage: 1:530/543 of query aligns to 6:525/539 of 6lpiB
- active site: I27 (= I22), G29 (= G24), G30 (≠ E25), S31 (≠ E26), I32 (≠ N27), E53 (= E47), C76 (≠ T70), F115 (≠ H109), Q116 (= Q110), E117 (≠ V111), K165 (≠ E159), M256 (≠ L250), A283 (≠ H277), V375 (= V377), G401 (≠ A403), M403 (= M405), D428 (= D430), N455 (≠ D457), A457 (≠ G459), L458 (≠ Y460), L460 (= L462), V461 (≠ I463), Q464 (≠ K466)
- binding flavin-adenine dinucleotide: R155 (≠ K149), G212 (= G204), G213 (≠ N205), G214 (= G206), T236 (= T230), L237 (≠ F231), M238 (= M232), L254 (≠ I248), M256 (≠ L250), H257 (≠ Q251), G276 (= G270), A277 (≠ Y271), R278 (≠ D272), D280 (≠ V274), R282 (≠ Y276), A283 (≠ H277), D300 (= D293), I301 (≠ S294), D319 (= D312), V320 (≠ L313), M380 (= M382), G398 (≠ N400)
- binding magnesium ion: D428 (= D430), N455 (≠ D457)
- binding thiamine diphosphate: E53 (= E47), C76 (≠ T70), P79 (= P73), G376 (= G378), Q377 (≠ A379), H378 (= H380), G401 (≠ A403), M403 (= M405), G427 (= G429), D428 (= D430), G429 (≠ A431), S430 (≠ G432), M433 (= M435), N455 (≠ D457), A457 (≠ G459), L458 (≠ Y460), G459 (= G461), L460 (= L462), V461 (≠ I463)
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)
31% identity, 97% coverage: 2:530/543 of query aligns to 92:641/664 of P09114
- P191 (≠ S100) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
- W568 (= W465) mutation to L: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191.
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)
31% identity, 97% coverage: 2:530/543 of query aligns to 95:644/667 of P09342
- C161 (= C67) modified: Disulfide link with 307
- P194 (≠ S100) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ I207) modified: Disulfide link with 161
7tzzA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase p197t mutant in complex with bispyribac-sodium (see paper)
31% identity, 96% coverage: 2:523/543 of query aligns to 13:557/582 of 7tzzA
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: M266 (≠ L250), R292 (≠ Y276), W489 (= W465)
- 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 (= V377), G401 (= G378), Q402 (≠ A379), H403 (= H380), G426 (≠ A403), M428 (= M405), G452 (= G429), D453 (= D430), G454 (≠ A431), S455 (≠ G432), L483 (≠ Y460), G484 (= G461), M485 (≠ L462), V486 (≠ I463)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G222 (= G204), G223 (≠ N205), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), M263 (≠ T247), L264 (≠ I248), M266 (≠ L250), H267 (≠ Q251), G286 (= G270), R288 (≠ D272), V293 (vs. gap), D310 (= D293), I311 (≠ S294), D329 (= D312), V330 (≠ L313), M405 (= M382), G423 (≠ N400)
- binding magnesium ion: A37 (≠ E26), T82 (= T70), S83 (≠ L71), Q122 (= Q110), Y381 (≠ K358), D453 (= D430), M458 (= M435), Q461 (= Q438), N480 (≠ D457), H482 (≠ G459), K533 (≠ D501)
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)
31% identity, 96% coverage: 2:523/543 of query aligns to 13:557/583 of 5k3sA
- active site: Y33 (≠ I22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), S38 (≠ N27), E59 (= E47), T82 (= T70), F121 (≠ H109), Q122 (= Q110), E123 (≠ V111), K171 (≠ E159), M266 (≠ L250), V293 (vs. gap), V400 (= V377), G426 (≠ A403), M428 (= M405), D453 (= D430), N480 (≠ D457), H482 (≠ G459), L483 (≠ Y460), M485 (≠ L462), V486 (≠ I463), W489 (= W465)
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: R292 (≠ Y276), M485 (≠ L462), W489 (= W465)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G222 (= G204), G223 (≠ N205), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), L264 (≠ I248), M266 (≠ L250), G286 (= G270), R288 (≠ D272), D290 (≠ V274), V293 (vs. gap), D310 (= D293), I311 (≠ S294), D329 (= D312), V330 (≠ L313), M405 (= M382), G423 (≠ N400)
- binding magnesium ion: D453 (= D430), N480 (≠ D457), H482 (≠ G459)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (= V377), G401 (= G378), Q402 (≠ A379), H403 (= H380), G426 (≠ A403), M428 (= M405), D453 (= D430), G454 (≠ A431), S455 (≠ G432), N480 (≠ D457), H482 (≠ G459), L483 (≠ Y460), G484 (= G461), M485 (≠ L462), V486 (≠ I463)
Sites not aligning to the query:
5k2oA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a pyrimidinyl-benzoate herbicide, pyrithiobac (see paper)
31% identity, 96% coverage: 2:523/543 of query aligns to 13:557/585 of 5k2oA
- active site: Y33 (≠ I22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), S38 (≠ N27), E59 (= E47), T82 (= T70), F121 (≠ H109), Q122 (= Q110), E123 (≠ V111), K171 (≠ E159), M266 (≠ L250), V293 (vs. gap), V400 (= V377), G426 (≠ A403), M428 (= M405), D453 (= D430), N480 (≠ D457), H482 (≠ G459), L483 (≠ Y460), M485 (≠ L462), V486 (≠ I463), W489 (= W465)
- binding 2-chloranyl-6-(4,6-dimethoxypyrimidin-2-yl)sulfanyl-benzoic acid: M266 (≠ L250), R292 (≠ Y276), W489 (= W465)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G222 (= G204), G223 (≠ N205), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), L264 (≠ I248), G286 (= G270), R288 (≠ D272), D290 (≠ V274), V293 (vs. gap), D310 (= D293), I311 (≠ S294), D329 (= D312), V330 (≠ L313), Q404 (≠ K381), M405 (= M382), G423 (≠ N400)
- binding magnesium ion: D453 (= D430), N480 (≠ D457), H482 (≠ G459)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (= V377), G401 (= G378), Q402 (≠ A379), H403 (= H380), M428 (= M405), D453 (= D430), G454 (≠ A431), S455 (≠ G432), N480 (≠ D457), H482 (≠ G459), L483 (≠ Y460), G484 (= G461), M485 (≠ L462), V486 (≠ I463)
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)
31% identity, 96% coverage: 2:523/543 of query aligns to 98:642/670 of P17597
- A122 (≠ E26) mutation to V: Reduced catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- M124 (≠ L28) 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 (= E47) binding thiamine diphosphate
- S186 (≠ H89) binding FAD
- P197 (≠ S100) mutation to S: In csr1-1/GH50; resistant to sulfonylurea but not to imidazolinone herbicides.
- R199 (≠ N102) mutation R->A,E: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- Q207 (= Q110) binding thiamine diphosphate
- K220 (= K123) binding (R)-imazaquin
- R246 (≠ K149) binding (R)-imazaquin; binding FAD
- K256 (≠ E159) binding chlorimuron-ethyl
- G308 (≠ N205) binding FAD
- TL 331:332 (≠ TF 230:231) binding FAD
- C340 (= C239) modified: Cysteine sulfinic acid (-SO2H)
- LGMH 349:352 (≠ IGLQ 248:251) binding FAD
- GVRFD 371:375 (≠ GYDIV 270:274) binding FAD
- DR 376:377 (≠ EY 275:276) binding chlorimuron-ethyl
- DI 395:396 (≠ DS 293:294) binding FAD
- DV 414:415 (≠ DL 312:313) binding FAD
- QH 487:488 (≠ AH 379:380) binding thiamine diphosphate
- GG 508:509 (≠ NG 400:401) binding FAD
- GAM 511:513 (≠ AAM 403:405) binding thiamine diphosphate
- D538 (= D430) binding Mg(2+)
- DGS 538:540 (≠ DAG 430:432) binding thiamine diphosphate
- N565 (≠ D457) binding Mg(2+)
- NQHLGM 565:570 (≠ DSGYGL 457:462) binding thiamine diphosphate
- H567 (≠ G459) binding Mg(2+)
- W574 (= W465) binding chlorimuron-ethyl; 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 chlorimuron-ethyl; 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)
31% identity, 96% coverage: 2:523/543 of query aligns to 13:557/582 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 (= V377), G401 (= G378), Q402 (≠ A379), H403 (= H380), G426 (≠ A403), M428 (= M405), G452 (= G429), D453 (= D430), G454 (≠ A431), S455 (≠ G432), M458 (= M435), N480 (≠ D457), H482 (≠ G459), L483 (≠ Y460), G484 (= G461), M485 (≠ L462), V486 (≠ I463)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G222 (= G204), G223 (≠ N205), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), L264 (≠ I248), M266 (≠ L250), H267 (≠ Q251), G286 (= G270), V287 (≠ Y271), R288 (≠ D272), D290 (≠ V274), R292 (≠ Y276), V293 (vs. gap), D310 (= D293), I311 (≠ S294), D329 (= D312), V330 (≠ L313), M405 (= M382), G423 (≠ N400)
- binding magnesium ion: F370 (vs. gap), D453 (= D430), M458 (= M435), Q461 (= Q438), N480 (≠ D457), H482 (≠ G459), K533 (≠ D501)
- binding N-{[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl}-N-methylmethanesulfonamide: M266 (≠ L250), R292 (≠ Y276), M485 (≠ L462), W489 (= W465)
Sites not aligning to the query:
5wj1A Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a triazolopyrimidine herbicide, penoxsulam (see paper)
31% identity, 96% coverage: 2:523/543 of query aligns to 13:557/582 of 5wj1A
- active site: Y33 (≠ I22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), S38 (≠ N27), E59 (= E47), T82 (= T70), F121 (≠ H109), Q122 (= Q110), E123 (≠ V111), K171 (≠ E159), M266 (≠ L250), V293 (vs. gap), V400 (= V377), G426 (≠ A403), M428 (= M405), D453 (= D430), N480 (≠ D457), H482 (≠ G459), L483 (≠ Y460), M485 (≠ L462), V486 (≠ I463), W489 (= W465)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G222 (= G204), G223 (≠ N205), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), M263 (≠ T247), L264 (≠ I248), G286 (= G270), R288 (≠ D272), V293 (vs. gap), D310 (= D293), I311 (≠ S294), D329 (= D312), V330 (≠ L313), M405 (= M382), G423 (≠ N400), G424 (= G401)
- binding magnesium ion: D453 (= D430), N480 (≠ D457), H482 (≠ G459)
- binding 2-(2,2-difluoroethoxy)-N-(5,8-dimethoxy[1,2,4]triazolo[1,5-c]pyrimidin-2-yl)-6-(trifluoromethyl)benzenesulfonamide: M266 (≠ L250), D291 (≠ E275), R292 (≠ Y276), M485 (≠ L462), W489 (= W465)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (= V377), G401 (= G378), Q402 (≠ A379), H403 (= H380), M428 (= M405), D453 (= D430), G454 (≠ A431), S455 (≠ G432), M458 (= M435), N480 (≠ D457), H482 (≠ G459), L483 (≠ Y460), G484 (= G461), M485 (≠ L462), V486 (≠ I463)
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)
31% identity, 96% coverage: 2:523/543 of query aligns to 13:557/582 of 5k6tA
- active site: Y33 (≠ I22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), S38 (≠ N27), E59 (= E47), T82 (= T70), F121 (≠ H109), Q122 (= Q110), E123 (≠ V111), K171 (≠ E159), M266 (≠ L250), V293 (vs. gap), V400 (= V377), G426 (≠ A403), M428 (= M405), D453 (= D430), N480 (≠ D457), H482 (≠ G459), L483 (≠ Y460), M485 (≠ L462), V486 (≠ I463), W489 (= W465)
- binding methyl 2-[(4-methyl-5-oxidanylidene-3-propoxy-1,2,4-triazol-1-yl)carbonylsulfamoyl]benzoate: H267 (≠ Q251), R292 (≠ Y276), M485 (≠ L462), W489 (= W465)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G222 (= G204), G223 (≠ N205), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), L264 (≠ I248), G286 (= G270), R288 (≠ D272), D290 (≠ V274), R292 (≠ Y276), V293 (vs. gap), D310 (= D293), I311 (≠ S294), D329 (= D312), V330 (≠ L313), Q404 (≠ K381), M405 (= M382), G423 (≠ N400)
- binding magnesium ion: D453 (= D430), N480 (≠ D457), H482 (≠ G459)
- 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 (= V377), G401 (= G378), Q402 (≠ A379), H403 (= H380), G426 (≠ A403), M428 (= M405), G452 (= G429), G454 (≠ A431), S455 (≠ G432), N480 (≠ D457), H482 (≠ G459), L483 (≠ Y460), G484 (= G461)
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)
31% identity, 96% coverage: 2:523/543 of query aligns to 13:557/582 of 5k6rA
- active site: Y33 (≠ I22), G35 (= G24), G36 (≠ E25), A37 (≠ E26), S38 (≠ N27), E59 (= E47), T82 (= T70), F121 (≠ H109), Q122 (= Q110), E123 (≠ V111), K171 (≠ E159), M266 (≠ L250), V293 (vs. gap), V400 (= V377), G426 (≠ A403), M428 (= M405), D453 (= D430), N480 (≠ D457), H482 (≠ G459), L483 (≠ Y460), M485 (≠ L462), V486 (≠ I463), W489 (= W465)
- binding methyl 4-[(3-methoxy-4-methyl-5-oxidanylidene-1,2,4-triazol-1-yl)carbonylsulfamoyl]-5-methyl-thiophene-3-carboxylate: R292 (≠ Y276), W489 (= W465)
- binding flavin-adenine dinucleotide: R161 (≠ K149), G222 (= G204), G223 (≠ N205), G224 (= G206), T246 (= T230), L247 (≠ F231), M248 (= M232), L264 (≠ I248), M266 (≠ L250), G286 (= G270), R288 (≠ D272), R292 (≠ Y276), V293 (vs. gap), D310 (= D293), I311 (≠ S294), G328 (≠ A311), D329 (= D312), V330 (≠ L313), M405 (= M382), G423 (≠ N400)
- binding magnesium ion: D453 (= D430), N480 (≠ D457), H482 (≠ G459)
- 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 (= V377), G401 (= G378), Q402 (≠ A379), H403 (= H380), G426 (≠ A403), M428 (= M405), D453 (= D430), G454 (≠ A431), S455 (≠ G432), M458 (= M435), N480 (≠ D457), H482 (≠ G459), L483 (≠ Y460), G484 (= G461), M485 (≠ L462), V486 (≠ I463)
Sites not aligning to the query:
Query Sequence
>WP_013835722.1 NCBI__GCF_000214825.1:WP_013835722.1
MNAAELLVKCLENEGVEYIFGIPGEENLDIMDALLDSPIEFILTRHEQGGAFMADVYGRL
TGKAGVCLSTLGPGATNLVTGVADANMDHAPVVAIAGQASTNRLHKESHQVLDLVNLFQP
ITKYSTQILSPDIVPEVVRKAFKVAQMEKPGCCFIDFPENIAPMTVNKQPLKPQAPKAPF
PHPDKVALAAEIISKARYPIILAGNGIVRNNANTALATFAESHQIPVANTFMAKGVLPCR
HPLALGTIGLQARDYIACGIDRADVIICVGYDIVEYHPHLWNHCPDCHIIHLDSQPAEVD
EFYSLAVGIVADLNESLNQLSKQVVRQNQTDVSPIKRLIDNELSQFAADNHFPVKPQKAI
YDLRQALADEDIVICDVGAHKMWMARLYPAQAPNTCIISNGFAAMGIALPGAMAAKLAHP
DRKVVALTGDAGFLMNVQEIETAVRLKLNIVVLIWNDSGYGLIKWKQLNEFGRESHIAFN
NPDFVKLADAFGATGLRVTADFSLEQALTKAIATDGVVIIDCPVDYSENLKLTERLGQMV
CPT
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