SitesBLAST
Comparing WP_074201909.1 NCBI__GCF_900141795.1:WP_074201909.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
5d6rB Acetolactate synthase from klebsiella pneumoniae in complex with mechanism-based inhibitor
39% identity, 97% coverage: 3:536/548 of query aligns to 6:542/548 of 5d6rB
- active site: I26 (= I23), G28 (= G25), A29 (≠ E26), K30 (≠ E27), I31 (≠ N28), E51 (= E48), T74 (= T71), H113 (= H110), Q114 (= Q111), S115 (≠ V112), Q163 (≠ E160), L254 (= L252), E281 (≠ H279), M386 (≠ V380), Q412 (≠ A406), M414 (= M408), D439 (= D433), D466 (= D460), G468 (= G462), Y469 (= Y463), M471 (≠ L465), 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 (≠ V380), G387 (= G381), S388 (≠ A382), Q412 (≠ A406), M414 (= M408), D439 (= D433), G440 (≠ A434), G468 (= G462), Y469 (= Y463), N470 (≠ G464), M471 (≠ L465), Y535 (= Y529)
- binding magnesium ion: R63 (= R60), Q212 (≠ R210), D439 (= D433), D466 (= D460), G468 (= G462)
1ozfA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors (see paper)
39% identity, 97% coverage: 3:536/548 of query aligns to 6:541/545 of 1ozfA
- active site: I26 (= I23), G28 (= G25), A29 (≠ E26), K30 (≠ E27), I31 (≠ N28), E51 (= E48), T74 (= T71), H113 (= H110), Q114 (= Q111), S115 (≠ V112), Q163 (≠ E160), L253 (= L252), E280 (≠ H279), M385 (≠ V380), Q411 (≠ A406), M413 (= M408), D438 (= D433), D465 (= D460), G467 (= G462), Y468 (= Y463), M470 (≠ L465), V471 (≠ I466), Q474 (≠ K469), Y534 (= Y529)
- binding magnesium ion: D438 (= D433), D465 (= D460), G467 (= G462)
- binding phosphate ion: G249 (= G248), R250 (≠ T249), Q257 (= Q253), R343 (≠ L338), R394 (= R389), L396 (≠ F391), Y397 (≠ R392)
- binding thiamine diphosphate: G386 (= G381), S387 (≠ A382), F388 (≠ H383), Q411 (≠ A406), M413 (= M408), G437 (= G432), D438 (= D433), G439 (≠ A434), D465 (= D460), G467 (= G462), Y468 (= Y463), N469 (≠ G464), M470 (≠ L465), V471 (≠ I466), Y534 (= Y529)
4rjkF Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
37% identity, 97% coverage: 4:535/548 of query aligns to 3:539/552 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 (≠ A382), H387 (= H383), Q410 (≠ A406), L412 (≠ M408), G436 (= G432), D437 (= D433), G438 (≠ A434), G439 (= G435), T466 (≠ G462), Y467 (= Y463), D468 (≠ G464), M469 (≠ L465), V470 (≠ I466), Y533 (= Y529)
4rjiC Acetolactate synthase from bacillus subtilis bound to thdp - crystal form i (see paper)
37% identity, 97% coverage: 4:535/548 of query aligns to 4:540/555 of 4rjiC
- binding magnesium ion: D438 (= D433), D465 (= D460), T467 (≠ G462)
- binding thiamine diphosphate: P24 (= P24), E48 (= E48), P74 (= P74), S387 (≠ A382), H388 (= H383), Q411 (≠ A406), G437 (= G432), D438 (= D433), G439 (≠ A434), G440 (= G435), T467 (≠ G462), Y468 (= Y463), D469 (≠ G464), M470 (≠ L465), V471 (≠ I466), Y534 (= Y529)
4rjkG Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
37% identity, 97% coverage: 4:535/548 of query aligns to 3:539/553 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 (≠ V380), G385 (= G381), S386 (≠ A382), H387 (= H383), Q410 (≠ A406), L412 (≠ M408), G436 (= G432), D437 (= D433), G438 (≠ A434), G439 (= G435), T466 (≠ G462), Y467 (= Y463), D468 (≠ G464), M469 (≠ L465), V470 (≠ I466), Y533 (= Y529)
1ozgA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate (see paper)
39% identity, 97% coverage: 3:536/548 of query aligns to 7:545/549 of 1ozgA
- active site: I27 (= I23), G29 (= G25), A30 (≠ E26), K31 (≠ E27), I32 (≠ N28), E52 (= E48), T75 (= T71), H114 (= H110), Q115 (= Q111), S116 (≠ V112), Q164 (≠ E160), L257 (= L252), E284 (≠ H279), M389 (≠ V380), Q415 (≠ A406), M417 (= M408), D442 (= D433), D469 (= D460), G471 (= G462), Y472 (= Y463), M474 (≠ L465), V475 (≠ I466), Q478 (≠ K469), Y538 (= Y529)
- binding 2-hydroxyethyl dihydrothiachrome diphosphate: M389 (≠ V380), G390 (= G381), S391 (≠ A382), F392 (≠ H383), Q415 (≠ A406), M417 (= M408), G441 (= G432), D442 (= D433), G443 (≠ A434), D469 (= D460), G471 (= G462), Y472 (= Y463), N473 (≠ G464), M474 (≠ L465), V475 (≠ I466), Y538 (= Y529)
- binding magnesium ion: D442 (= D433), D469 (= D460), G471 (= G462)
- binding phosphate ion: G253 (= G248), R254 (≠ T249), Q261 (= Q253), R347 (≠ L338), R398 (= R389), Y401 (≠ R392)
5dx6B Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
39% identity, 97% coverage: 3:536/548 of query aligns to 18:548/557 of 5dx6B
- active site: I38 (= I23), G40 (= G25), A41 (≠ E26), K42 (≠ E27), I43 (≠ N28), E63 (= E48), T86 (= T71), H125 (= H110), Q126 (= Q111), S127 (≠ V112), Q175 (≠ E160), L268 (= L252), E295 (≠ H279), M392 (≠ V380), Q418 (≠ A406), M420 (= M408), D445 (= D433), D472 (= D460), G474 (= G462), Y475 (= Y463), M477 (≠ L465), V478 (≠ I466), Q481 (≠ K469), Y541 (= Y529)
- binding 3-fluoro-2-oxopropanoic acid: G264 (= G248), R265 (≠ T249), Q272 (= Q253), A400 (= A388), R401 (= R389), Y404 (≠ R392)
- binding magnesium ion: S135 (≠ N120), T138 (≠ S123), D445 (= D433), D472 (= D460), G474 (= G462)
- binding thiamine diphosphate: G393 (= G381), S394 (≠ A382), F395 (≠ H383), Q418 (≠ A406), M420 (= M408), G444 (= G432), D445 (= D433), G446 (≠ A434), D472 (= D460), G474 (= G462), Y475 (= Y463), N476 (≠ G464), M477 (≠ L465), V478 (≠ I466), Y541 (= Y529)
5dx6A Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
39% identity, 97% coverage: 3:536/548 of query aligns to 7:537/541 of 5dx6A
- active site: I27 (= I23), G29 (= G25), A30 (≠ E26), K31 (≠ E27), I32 (≠ N28), E52 (= E48), T75 (= T71), Q159 (≠ E160), L249 (= L252), E276 (≠ H279), M381 (≠ V380), Q407 (≠ A406), M409 (= M408), D434 (= D433), D461 (= D460), G463 (= G462), Y464 (= Y463), M466 (≠ L465), 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 (≠ V380), G382 (= G381), S383 (≠ A382), F384 (≠ H383), Q407 (≠ A406), M409 (= M408), G433 (= G432), D434 (= D433), G435 (≠ A434), D461 (= D460), G463 (= G462), Y464 (= Y463), N465 (≠ G464), Y530 (= Y529)
- binding magnesium ion: S119 (≠ N120), T122 (≠ S123), D434 (= D433), D461 (= D460), G463 (= G462)
5wdgA Acetolactate synthase from klebsiella pneumoniae in complex with a reaction intermediate
39% identity, 97% coverage: 3:536/548 of query aligns to 7:534/538 of 5wdgA
- active site: I27 (= I23), G29 (= G25), A30 (≠ E26), K31 (≠ E27), I32 (≠ N28), E52 (= E48), T75 (= T71), Q157 (≠ E160), L246 (= L252), E273 (≠ H279), M378 (≠ V380), Q404 (≠ A406), M406 (= M408), D431 (= D433), D458 (= D460), G460 (= G462), Y461 (= Y463), M463 (≠ L465), 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 (≠ V380), S380 (≠ A382), F381 (≠ H383), Q404 (≠ A406), M406 (= M408), G430 (= G432), D431 (= D433), G432 (≠ A434), G433 (= G435), D458 (= D460), G460 (= G462), Y461 (= Y463), N462 (≠ G464), M463 (≠ L465), V464 (≠ I466), Y527 (= Y529)
- binding magnesium ion: R64 (= R60), S117 (≠ N120), T120 (≠ S123), Q204 (≠ R210), D431 (= D433), D458 (= D460), G460 (= G462)
- binding pyruvic acid: G94 (≠ R90), R147 (≠ K150)
6lpiB Crystal structure of ahas holo-enzyme (see paper)
31% identity, 97% coverage: 3:532/548 of query aligns to 7:524/539 of 6lpiB
- active site: I27 (= I23), G29 (= G25), G30 (≠ E26), S31 (≠ E27), I32 (≠ N28), E53 (= E48), C76 (≠ T71), F115 (≠ H110), Q116 (= Q111), E117 (≠ V112), K165 (≠ E160), M256 (≠ L252), A283 (vs. gap), V375 (= V380), G401 (≠ A406), M403 (= M408), D428 (= D433), N455 (≠ D460), A457 (≠ G462), L458 (≠ Y463), L460 (= L465), V461 (≠ I466), Q464 (≠ K469)
- binding flavin-adenine dinucleotide: R155 (≠ K150), G212 (= G205), G213 (≠ N206), G214 (= G207), T236 (= T231), L237 (≠ F232), M238 (= M233), L254 (≠ A250), M256 (≠ L252), H257 (≠ Q253), G276 (= G272), A277 (vs. gap), R278 (vs. gap), D280 (= D274), R282 (vs. gap), A283 (vs. gap), D300 (= D295), I301 (≠ T296), D319 (≠ N314), V320 (≠ I315), M380 (= M385), G398 (≠ N403)
- binding magnesium ion: D428 (= D433), N455 (≠ D460)
- binding thiamine diphosphate: E53 (= E48), C76 (≠ T71), P79 (= P74), G376 (= G381), Q377 (≠ A382), H378 (= H383), G401 (≠ A406), M403 (= M408), G427 (= G432), D428 (= D433), G429 (≠ A434), S430 (≠ G435), M433 (= M438), N455 (≠ D460), A457 (≠ G462), L458 (≠ Y463), G459 (= G464), L460 (= L465), V461 (≠ I466)
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: 2:532/548 of query aligns to 94:643/667 of P09342
- C161 (= C68) modified: Disulfide link with 307
- P194 (≠ A101) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ V208) 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, 97% coverage: 2:532/548 of query aligns to 91:640/664 of P09114
- P191 (≠ A101) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
- W568 (= W468) mutation to L: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191.
2ihvA Carboxyethylarginine synthase from streptomyces clavuligerus: 5- guanidinovaleric acid complex (see paper)
32% identity, 89% coverage: 40:529/548 of query aligns to 39:551/563 of 2ihvA
- active site: E47 (= E48), T70 (= T71), H110 (= H110), Q111 (= Q111), C112 (≠ V112), V160 (≠ E160), I265 (≠ D256), L292 (≠ Y278), I400 (≠ V380), S426 (≠ A406), F428 (≠ M408), D453 (= D433), N480 (≠ D460), T482 (≠ G462), N483 (≠ Y463), L485 (= L465), I486 (= I466), Y489 (≠ K469), Y551 (= Y529)
- binding 5-{[amino(imino)methyl]amino}pentanoic acid: Y261 (≠ L252), D291 (vs. gap), H405 (≠ M385)
- binding magnesium ion: D453 (= D433), N480 (≠ D460), T482 (≠ G462)
- binding thiamine diphosphate: E47 (= E48), T70 (= T71), P73 (= P74), I400 (≠ V380), G401 (= G381), F402 (≠ A382), F403 (≠ H383), F428 (≠ M408), G452 (= G432), D453 (= D433), G454 (≠ A434), G455 (= G435), T482 (≠ G462), N483 (≠ Y463), G484 (= G464), L485 (= L465), Y551 (= Y529)
Sites not aligning to the query:
Q9LCV9 N(2)-(2-carboxyethyl)arginine synthase; CEA synthetase; CEAS; EC 2.5.1.66 from Streptomyces clavuligerus (see 2 papers)
32% identity, 89% coverage: 40:529/548 of query aligns to 49:561/573 of Q9LCV9
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 571 binding
2ihuA Carboxyethylarginine synthase from streptomyces clavuligerus: putative reaction intermediate complex (see paper)
32% identity, 89% coverage: 40:529/548 of query aligns to 39:551/562 of 2ihuA
- active site: E47 (= E48), T70 (= T71), H110 (= H110), Q111 (= Q111), C112 (≠ V112), V160 (≠ E160), I265 (≠ D256), L292 (≠ Y278), I400 (≠ V380), S426 (≠ A406), F428 (≠ M408), D453 (= D433), N480 (≠ D460), T482 (≠ G462), N483 (≠ Y463), L485 (= L465), I486 (= I466), Y489 (≠ K469), Y551 (= Y529)
- binding magnesium ion: D453 (= D433), N480 (≠ D460), T482 (≠ G462)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: E47 (= E48), T70 (= T71), P73 (= P74), G401 (= G381), F402 (≠ A382), F403 (≠ H383), F428 (≠ M408), G452 (= G432), D453 (= D433), G454 (≠ A434), G455 (= G435), T482 (≠ G462), N483 (≠ Y463), G484 (= G464), L485 (= L465), I486 (= I466), Y551 (= Y529)
Sites not aligning to the query:
2ihuC Carboxyethylarginine synthase from streptomyces clavuligerus: putative reaction intermediate complex (see paper)
32% identity, 89% coverage: 40:529/548 of query aligns to 39:551/551 of 2ihuC
- active site: E47 (= E48), T70 (= T71), H110 (= H110), Q111 (= Q111), C112 (≠ V112), V160 (≠ E160), I265 (≠ D256), L292 (≠ Y278), I400 (≠ V380), S426 (≠ A406), F428 (≠ M408), D453 (= D433), N480 (≠ D460), T482 (≠ G462), N483 (≠ Y463), L485 (= L465), I486 (= I466), Y489 (≠ K469), Y551 (= Y529)
- binding magnesium ion: D453 (= D433), N480 (≠ D460), T482 (≠ G462)
- binding 5-(2-{[hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-2-[(1z)-1-hydroxy-3-(phosphonooxy)prop-1-en-1-yl]-3-{[(4z)-4-imino-2-methyl-4,5-dihydropyrimidin-5-yl]methyl}-4-methyl-1,3-thiazol-3-ium: G401 (= G381), F402 (≠ A382), F403 (≠ H383), F428 (≠ M408), G452 (= G432), D453 (= D433), G454 (≠ A434), T482 (≠ G462), N483 (≠ Y463), G484 (= G464), L485 (= L465), I486 (= I466), Y489 (≠ K469), Y551 (= Y529)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: E47 (= E48), T70 (= T71), P73 (= P74)
Sites not aligning to the query:
1upaA Carboxyethylarginine synthase from streptomyces clavuligerus (semet structure) (see paper)
33% identity, 89% coverage: 40:529/548 of query aligns to 38:547/558 of 1upaA
- active site: E46 (= E48), T69 (= T71), H109 (= H110), Q110 (= Q111), C111 (≠ V112), V159 (vs. gap), I261 (≠ D256), L288 (≠ Y278), I396 (≠ V380), S422 (≠ A406), F424 (≠ M408), D449 (= D433), N476 (≠ D460), T478 (≠ G462), N479 (≠ Y463), L481 (= L465), I482 (= I466), Y485 (≠ K469), Y547 (= Y529)
- binding magnesium ion: D449 (= D433), N476 (≠ D460), T478 (≠ G462)
- binding sulfate ion: Y257 (≠ L252), R400 (≠ K384), H401 (≠ M385), N476 (≠ D460), N546 (≠ D528), Y547 (= Y529)
- binding thiamine diphosphate: E46 (= E48), T69 (= T71), I396 (≠ V380), G397 (= G381), F398 (≠ A382), F399 (≠ H383), F424 (≠ M408), G448 (= G432), D449 (= D433), G450 (≠ A434), T478 (≠ G462), N479 (≠ Y463), G480 (= G464), Y547 (= Y529)
Sites not aligning to the query:
6vz8D Arabidopsis thaliana acetohydroxyacid synthase complex with valine bound (see paper)
30% identity, 96% coverage: 2:526/548 of query aligns to 11:530/531 of 6vz8D
- active site: Y32 (≠ I23), G34 (= G25), G35 (≠ E26), A36 (≠ E27), S37 (≠ N28), E58 (= E48), T81 (= T71), F120 (≠ H110), Q121 (= Q111), E122 (≠ V112), K170 (≠ E160), M256 (≠ L252), V283 (≠ S288), V376 (= V380), G402 (≠ A406), M404 (= M408), D429 (= D433), N456 (≠ D460), H458 (≠ G462), L459 (≠ Y463), M461 (≠ L465), V462 (≠ I466), W465 (= W468)
- binding flavin-adenine dinucleotide: G214 (= G205), G215 (≠ N206), G216 (= G207), T236 (= T231), L237 (≠ F232), L254 (≠ A250), H257 (≠ Q253), R278 (vs. gap), R282 (≠ H287), V283 (≠ S288), I291 (≠ T296), G399 (≠ N403)
- binding magnesium ion: H458 (≠ G462), L459 (≠ Y463), G460 (= G464)
- binding thiamine diphosphate: E58 (= E48), P84 (= P74), V376 (= V380), G377 (= G381), Q378 (≠ A382), H379 (= H383), G402 (≠ A406), M404 (= M408), G428 (= G432), D429 (= D433), G430 (≠ A434), S431 (≠ G435), L459 (≠ Y463), G460 (= G464), M461 (≠ L465), V462 (≠ I466)
1t9aA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, tribenuron methyl (see paper)
31% identity, 96% coverage: 4:528/548 of query aligns to 11:556/597 of 1t9aA
- active site: Y30 (≠ I23), G32 (= G25), G33 (≠ E26), A34 (≠ E27), I35 (≠ N28), E56 (= E48), T79 (= T71), F118 (≠ H110), Q119 (= Q111), E120 (≠ V112), K168 (≠ E160), R228 (vs. gap), M264 (≠ L252), V291 (vs. gap), V407 (= V380), L432 (≠ F405), G433 (≠ A406), M435 (= M408), D460 (= D433), N487 (≠ D460), E489 (≠ G462), Q490 (≠ Y463), M492 (≠ L465), V493 (≠ I466), W496 (= W468), L518 (= L490), G523 (= G495), L524 (≠ A496)
- binding methyl 2-[4-methoxy-6-methyl-1,3,5-trazin-2-yl(methyl)carbamoylsulfamoyl]benzoate: G33 (≠ E26), V108 (≠ A100), P109 (≠ A101), F118 (≠ H110), K168 (≠ E160), M264 (≠ L252), D289 (vs. gap), R290 (vs. gap), M492 (≠ L465), V493 (≠ I466), W496 (= W468)
- binding flavin-adenine dinucleotide: R158 (≠ K150), G217 (= G205), A218 (≠ N206), G219 (= G207), N222 (≠ R210), T244 (= T231), L245 (≠ F232), Q246 (≠ M233), L262 (≠ A250), M264 (≠ L252), H265 (≠ Q253), G284 (= G272), A285 (vs. gap), R286 (vs. gap), D288 (= D274), R290 (vs. gap), V291 (vs. gap), E317 (≠ D295), V318 (≠ T296), N322 (≠ E300), G335 (= G313), D336 (≠ N314), A337 (≠ I315), Q411 (≠ K384), M412 (= M385), G430 (≠ N403), G431 (= G404)
- binding magnesium ion: D460 (= D433), N487 (≠ D460), E489 (≠ G462)
- binding propyl trihydrogen diphosphate: V407 (= V380), G408 (= G381), Q409 (≠ A382), H410 (= H383), M435 (= M408), G459 (= G432), D460 (= D433), A461 (= A434), S462 (≠ G435), N487 (≠ D460), E489 (≠ G462), Q490 (≠ Y463), G491 (= G464), M492 (≠ L465)
- 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:
1t9dA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
31% identity, 96% coverage: 4:528/548 of query aligns to 10:555/596 of 1t9dA
- active site: Y29 (≠ I23), G31 (= G25), G32 (≠ E26), A33 (≠ E27), I34 (≠ N28), E55 (= E48), T78 (= T71), F117 (≠ H110), Q118 (= Q111), E119 (≠ V112), K167 (≠ E160), R227 (vs. gap), M263 (≠ L252), V290 (vs. gap), V406 (= V380), L431 (≠ F405), G432 (≠ A406), M434 (= M408), D459 (= D433), N486 (≠ D460), E488 (≠ G462), Q489 (≠ Y463), M491 (≠ L465), V492 (≠ I466), W495 (= W468), L517 (= L490), 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 (≠ A100), P108 (≠ A101), F117 (≠ H110), K167 (≠ E160), M263 (≠ L252), D288 (vs. gap), R289 (vs. gap), W495 (= W468)
- binding flavin-adenine dinucleotide: R157 (≠ K150), G216 (= G205), A217 (≠ N206), G218 (= G207), N221 (≠ R210), T243 (= T231), L244 (≠ F232), Q245 (≠ M233), M260 (≠ T249), L261 (≠ A250), H264 (≠ Q253), G283 (= G272), A284 (vs. gap), R285 (vs. gap), D287 (= D274), R289 (vs. gap), V290 (vs. gap), E316 (≠ D295), V317 (≠ T296), N321 (≠ E300), G334 (= G313), D335 (≠ N314), A336 (≠ I315), Q410 (≠ K384), M411 (= M385), G429 (≠ N403), G430 (= G404)
- 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:
Query Sequence
>WP_074201909.1 NCBI__GCF_900141795.1:WP_074201909.1
MQNAAQLLVQCLEAEEVRFIFGIPGEENLDLIDALADSPIQFITTRHEQGAAFMADVYGR
LTGKAGVCISTLGPGATNLVTGVADANMDRAPIVALAGQAATTRMHKESHQVLDLVSLFN
PISKYAAQILEPETVPEVVRKAFKVAQSEKPGATFIDFPENIAKMPVPNTPLPVRRERLP
MAPESHLKKAAELIDAAENPLILAGNGVIRTHAHLELQAFAEALQIPVVNTFMAKGVVPF
FKNPLALGTAGLQAGDYENCGFRDADLVITVGFDMVEYHPYLWNPHHSHRIIHIDTTAAE
VDQDYLPDIELVGNIAKNLRRLTHLGIAPKHSRIGRQLRHSLIEEMNRCSHSTAWPLKPQ
KIIWDLRTVLPREGITVVDVGAHKMWMARMFRAEQPNTCIISNGFASMGIALPGAIAAAL
TYPERPVVAVSGDAGFMMNVQELETAVRLGVNMVVLIWNDGGYGLIEWKQQRQFGRSAYV
SFGNPDFVQLAQSFGAQGTRIDRAEALQPALKSALEAGGLHVIDCPVDYSENDRLIELLG
PVLSEAEE
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