SitesBLAST
Comparing WP_012706784.1 NCBI__GCF_000018545.1:WP_012706784.1 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)
6lpiB Crystal structure of ahas holo-enzyme (see paper)
32% identity, 97% coverage: 7:527/537 of query aligns to 7:517/539 of 6lpiB
- active site: I27 (= I27), G29 (= G29), G30 (≠ V30), S31 (≠ H31), I32 (≠ T32), E53 (= E52), C76 (≠ I75), F115 (≠ L116), Q116 (≠ H117), E117 (= E118), K165 (≠ T167), M256 (≠ S253), A283 (≠ D282), V375 (≠ T382), G401 (= G408), M403 (≠ L410), D428 (= D435), N455 (= N462), A457 (≠ G464), L458 (≠ Y465), L460 (vs. gap), V461 (vs. gap), Q464 (≠ I468)
- binding flavin-adenine dinucleotide: R155 (= R157), G212 (= G212), G213 (= G213), G214 (= G214), T236 (= T236), L237 (≠ V237), M238 (≠ N238), L254 (≠ P251), M256 (≠ S253), H257 (≠ P254), G276 (= G273), A277 (≠ T274), R278 (≠ E275), D280 (≠ T279), R282 (≠ Y281), A283 (≠ D282), D300 (= D299), I301 (= I300), D319 (≠ G318), V320 (≠ A319), M380 (≠ V385), G398 (≠ A404)
- binding magnesium ion: D428 (= D435), N455 (= N462)
- binding thiamine diphosphate: E53 (= E52), C76 (≠ I75), P79 (= P78), G376 (vs. gap), Q377 (vs. gap), H378 (≠ Q383), G401 (= G408), M403 (≠ L410), G427 (= G434), D428 (= D435), G429 (= G436), S430 (≠ G437), M433 (≠ F440), N455 (= N462), A457 (≠ G464), L458 (≠ Y465), G459 (vs. gap), L460 (vs. gap), V461 (vs. gap)
3ea4A Arabidopsis thaliana acetohydroxyacid synthase in complex with monosulfuron-ester (see paper)
29% identity, 97% coverage: 10:530/537 of query aligns to 15:559/582 of 3ea4A
- active site: Y32 (≠ I27), G34 (= G29), G35 (≠ V30), A36 (≠ H31), S37 (≠ T32), E58 (= E52), T81 (≠ I75), F120 (≠ L116), Q121 (≠ H117), E122 (= E118), K170 (≠ T167), M265 (≠ V259), V292 (≠ A285), V399 (≠ D380), G425 (= G408), M427 (≠ L410), D452 (= D435), N479 (vs. gap), H481 (vs. gap), L482 (vs. gap), M484 (vs. gap), V485 (vs. gap), W488 (= W460), H557 (= H528)
- binding methyl 2-{[(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl}benzoate: D290 (≠ L283), R291 (≠ Y284), W488 (= W460)
- binding flavin-adenine dinucleotide-n5-isobutyl ketone: R160 (= R157), G221 (= G212), G222 (= G213), G223 (= G214), T245 (= T236), L246 (≠ V237), M247 (≠ N238), L263 (≠ K257), G264 (≠ A258), M265 (≠ V259), H266 (≠ R260), G285 (= G273), R287 (≠ E275), D289 (= D282), R291 (≠ Y284), D309 (= D299), I310 (= I300), G327 (≠ S317), D328 (≠ G318), V329 (≠ A319), M404 (≠ V385), G422 (≠ A404)
- binding magnesium ion: D452 (= D435), N479 (vs. gap), H481 (vs. gap)
- 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 (≠ D380), G400 (≠ S381), Q401 (≠ T382), H402 (≠ Q383), M427 (≠ L410), G451 (= G434), D452 (= D435), G453 (= G436), S454 (≠ G437), N479 (vs. gap), H481 (vs. gap), L482 (vs. gap), G483 (vs. gap), M484 (vs. gap), V485 (vs. gap)
Sites not aligning to the query:
3e9yA Arabidopsis thaliana acetohydroxyacid synthase in complex with monosulfuron (see paper)
29% identity, 97% coverage: 10:530/537 of query aligns to 15:559/582 of 3e9yA
- active site: Y32 (≠ I27), G34 (= G29), G35 (≠ V30), A36 (≠ H31), S37 (≠ T32), E58 (= E52), T81 (≠ I75), F120 (≠ L116), Q121 (≠ H117), E122 (= E118), K170 (≠ T167), M265 (≠ V259), V292 (≠ A285), V399 (≠ D380), G425 (= G408), M427 (≠ L410), D452 (= D435), N479 (vs. gap), H481 (vs. gap), L482 (vs. gap), M484 (vs. gap), V485 (vs. gap), W488 (= W460), H557 (= H528)
- binding N-[(4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide: D290 (≠ L283), R291 (≠ Y284), W488 (= W460)
- binding flavin-adenine dinucleotide-n5-isobutyl ketone: R160 (= R157), G221 (= G212), G222 (= G213), G223 (= G214), T245 (= T236), L246 (≠ V237), M247 (≠ N238), L263 (≠ K257), G285 (= G273), R287 (≠ E275), D289 (= D282), R291 (≠ Y284), D309 (= D299), I310 (= I300), G327 (≠ S317), D328 (≠ G318), V329 (≠ A319), M404 (≠ V385), G422 (≠ A404)
- binding magnesium ion: D452 (= D435), N479 (vs. gap), H481 (vs. gap)
- 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 (≠ D380), G400 (≠ S381), Q401 (≠ T382), H402 (≠ Q383), M427 (≠ L410), G451 (= G434), G453 (= G436), S454 (≠ G437), N479 (vs. gap), H481 (vs. gap), L482 (vs. gap), G483 (vs. gap), M484 (vs. gap), V485 (vs. gap)
Sites not aligning to the query:
7tzzA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase p197t mutant in complex with bispyribac-sodium (see paper)
28% identity, 97% coverage: 10:530/537 of query aligns to 16:560/582 of 7tzzA
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: M266 (≠ V259), R292 (≠ Y284), W489 (= W460)
- 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 (≠ D380), G401 (≠ S381), Q402 (≠ T382), H403 (≠ Q383), G426 (= G408), M428 (≠ L410), G452 (= G434), D453 (= D435), G454 (= G436), S455 (≠ G437), L483 (vs. gap), G484 (vs. gap), M485 (vs. gap), V486 (vs. gap)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G212), G223 (= G213), G224 (= G214), T246 (= T236), L247 (≠ V237), M248 (≠ N238), M263 (≠ L256), L264 (≠ K257), M266 (≠ V259), H267 (≠ R260), G286 (= G273), R288 (≠ E275), V293 (≠ A285), D310 (= D299), I311 (= I300), D329 (≠ G318), V330 (≠ A319), M405 (≠ V385), G423 (≠ A404)
- binding magnesium ion: A37 (≠ H31), T82 (≠ I75), S83 (≠ T76), Q122 (≠ H117), Y381 (≠ L367), D453 (= D435), M458 (≠ F440), Q461 (≠ A443), N480 (vs. gap), H482 (vs. gap), K533 (≠ I506)
Sites not aligning to the query:
5k2oA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a pyrimidinyl-benzoate herbicide, pyrithiobac (see paper)
28% identity, 97% coverage: 10:530/537 of query aligns to 16:560/585 of 5k2oA
- active site: Y33 (≠ I27), G35 (= G29), G36 (≠ V30), A37 (≠ H31), S38 (≠ T32), E59 (= E52), T82 (≠ I75), F121 (≠ L116), Q122 (≠ H117), E123 (= E118), K171 (≠ T167), M266 (≠ V259), V293 (≠ A285), V400 (≠ D380), G426 (= G408), M428 (≠ L410), D453 (= D435), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), M485 (vs. gap), V486 (vs. gap), W489 (= W460), H558 (= H528)
- binding 2-chloranyl-6-(4,6-dimethoxypyrimidin-2-yl)sulfanyl-benzoic acid: M266 (≠ V259), R292 (≠ Y284), W489 (= W460)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G212), G223 (= G213), G224 (= G214), T246 (= T236), L247 (≠ V237), M248 (≠ N238), L264 (≠ K257), G286 (= G273), R288 (≠ E275), D290 (= D282), V293 (≠ A285), D310 (= D299), I311 (= I300), D329 (≠ G318), V330 (≠ A319), Q404 (≠ A384), M405 (≠ V385), G423 (≠ A404)
- binding magnesium ion: D453 (= D435), N480 (vs. gap), H482 (vs. gap)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (≠ D380), G401 (≠ S381), Q402 (≠ T382), H403 (≠ Q383), M428 (≠ L410), D453 (= D435), G454 (= G436), S455 (≠ G437), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), G484 (vs. gap), M485 (vs. gap), V486 (vs. gap)
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)
28% identity, 97% coverage: 10:530/537 of query aligns to 101:645/670 of P17597
- A122 (≠ H31) mutation to V: Reduced catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- M124 (≠ V33) 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 (= E52) binding thiamine diphosphate
- S186 (= S94) binding FAD
- P197 (≠ R105) mutation to S: In csr1-1/GH50; resistant to sulfonylurea but not to imidazolinone herbicides.
- R199 (≠ D107) mutation R->A,E: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- Q207 (≠ H117) binding thiamine diphosphate
- K220 (≠ L131) binding (R)-imazaquin
- R246 (= R157) binding (R)-imazaquin; binding FAD
- K256 (≠ T167) binding chlorimuron-ethyl
- G308 (= G213) binding FAD
- TL 331:332 (≠ TV 236:237) binding FAD
- C340 (≠ L248) modified: Cysteine sulfinic acid (-SO2H)
- LGMH 349:352 (≠ KAVR 257:260) binding FAD
- GVR-----FD 371:375 (≠ GTEMGQTDYD 273:282) binding FAD
- DR 376:377 (≠ LY 283:284) binding chlorimuron-ethyl
- DI 395:396 (= DI 299:300) binding FAD
- DV 414:415 (≠ GA 318:319) binding FAD
- QH 487:488 (≠ TQ 382:383) binding thiamine diphosphate
- G-G 508:509 (≠ ATG 404:406) binding FAD
- GAM 511:513 (≠ GSL 408:410) binding thiamine diphosphate
- D538 (= D435) binding Mg(2+)
- DGS 538:540 (≠ DGG 435:437) binding thiamine diphosphate
- N565 (vs. gap) binding Mg(2+)
- NQHLGM 565:570 (vs. gap) binding thiamine diphosphate
- H567 (vs. gap) binding Mg(2+)
- W574 (= W460) 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.
5k3sA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a pyrimidinyl-benzoate herbicide, bispyribac-sodium (see paper)
28% identity, 97% coverage: 10:530/537 of query aligns to 16:560/583 of 5k3sA
- active site: Y33 (≠ I27), G35 (= G29), G36 (≠ V30), A37 (≠ H31), S38 (≠ T32), E59 (= E52), T82 (≠ I75), F121 (≠ L116), Q122 (≠ H117), E123 (= E118), K171 (≠ T167), M266 (≠ V259), V293 (≠ A285), V400 (≠ D380), G426 (= G408), M428 (≠ L410), D453 (= D435), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), M485 (vs. gap), V486 (vs. gap), W489 (= W460), H558 (= H528)
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: R292 (≠ Y284), M485 (vs. gap), W489 (= W460)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G212), G223 (= G213), G224 (= G214), T246 (= T236), L247 (≠ V237), M248 (≠ N238), L264 (≠ K257), M266 (≠ V259), G286 (= G273), R288 (≠ E275), D290 (= D282), V293 (≠ A285), D310 (= D299), I311 (= I300), D329 (≠ G318), V330 (≠ A319), M405 (≠ V385), G423 (≠ A404)
- binding magnesium ion: D453 (= D435), N480 (vs. gap), H482 (vs. gap)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (≠ D380), G401 (≠ S381), Q402 (≠ T382), H403 (≠ Q383), G426 (= G408), M428 (≠ L410), D453 (= D435), G454 (= G436), S455 (≠ G437), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), G484 (vs. gap), M485 (vs. gap), V486 (vs. gap)
Sites not aligning to the query:
8et4A Crystal structure of wild-type arabidopsis thaliana acetohydroxyacid synthase in complex with amidosulfuron (see paper)
28% identity, 97% coverage: 10:530/537 of query aligns to 16:560/582 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 (≠ D380), G401 (≠ S381), Q402 (≠ T382), H403 (≠ Q383), G426 (= G408), M428 (≠ L410), G452 (= G434), D453 (= D435), G454 (= G436), S455 (≠ G437), M458 (≠ F440), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), G484 (vs. gap), M485 (vs. gap), V486 (vs. gap)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G212), G223 (= G213), G224 (= G214), T246 (= T236), L247 (≠ V237), M248 (≠ N238), L264 (≠ K257), M266 (≠ V259), H267 (≠ R260), G286 (= G273), V287 (≠ T274), R288 (≠ E275), D290 (= D282), R292 (≠ Y284), V293 (≠ A285), D310 (= D299), I311 (= I300), D329 (≠ G318), V330 (≠ A319), M405 (≠ V385), G423 (≠ A404)
- binding magnesium ion: F370 (≠ P356), D453 (= D435), M458 (≠ F440), Q461 (≠ A443), N480 (vs. gap), H482 (vs. gap), K533 (≠ I506)
- binding N-{[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl}-N-methylmethanesulfonamide: M266 (≠ V259), R292 (≠ Y284), M485 (vs. gap), W489 (= W460)
Sites not aligning to the query:
5wj1A Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a triazolopyrimidine herbicide, penoxsulam (see paper)
28% identity, 97% coverage: 10:530/537 of query aligns to 16:560/582 of 5wj1A
- active site: Y33 (≠ I27), G35 (= G29), G36 (≠ V30), A37 (≠ H31), S38 (≠ T32), E59 (= E52), T82 (≠ I75), F121 (≠ L116), Q122 (≠ H117), E123 (= E118), K171 (≠ T167), M266 (≠ V259), V293 (≠ A285), V400 (≠ D380), G426 (= G408), M428 (≠ L410), D453 (= D435), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), M485 (vs. gap), V486 (vs. gap), W489 (= W460), H558 (= H528)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G212), G223 (= G213), G224 (= G214), T246 (= T236), L247 (≠ V237), M248 (≠ N238), M263 (≠ L256), L264 (≠ K257), G286 (= G273), R288 (≠ E275), V293 (≠ A285), D310 (= D299), I311 (= I300), D329 (≠ G318), V330 (≠ A319), M405 (≠ V385), G423 (≠ A404), G424 (= G406)
- binding magnesium ion: D453 (= D435), N480 (vs. gap), H482 (vs. gap)
- binding 2-(2,2-difluoroethoxy)-N-(5,8-dimethoxy[1,2,4]triazolo[1,5-c]pyrimidin-2-yl)-6-(trifluoromethyl)benzenesulfonamide: M266 (≠ V259), D291 (≠ L283), R292 (≠ Y284), M485 (vs. gap), W489 (= W460)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V400 (≠ D380), G401 (≠ S381), Q402 (≠ T382), H403 (≠ Q383), M428 (≠ L410), D453 (= D435), G454 (= G436), S455 (≠ G437), M458 (≠ F440), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), G484 (vs. gap), M485 (vs. gap), V486 (vs. gap)
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)
28% identity, 97% coverage: 10:530/537 of query aligns to 16:560/582 of 5k6tA
- active site: Y33 (≠ I27), G35 (= G29), G36 (≠ V30), A37 (≠ H31), S38 (≠ T32), E59 (= E52), T82 (≠ I75), F121 (≠ L116), Q122 (≠ H117), E123 (= E118), K171 (≠ T167), M266 (≠ V259), V293 (≠ A285), V400 (≠ D380), G426 (= G408), M428 (≠ L410), D453 (= D435), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), M485 (vs. gap), V486 (vs. gap), W489 (= W460), H558 (= H528)
- binding methyl 2-[(4-methyl-5-oxidanylidene-3-propoxy-1,2,4-triazol-1-yl)carbonylsulfamoyl]benzoate: H267 (≠ R260), R292 (≠ Y284), M485 (vs. gap), W489 (= W460)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G212), G223 (= G213), G224 (= G214), T246 (= T236), L247 (≠ V237), M248 (≠ N238), L264 (≠ K257), G286 (= G273), R288 (≠ E275), D290 (= D282), R292 (≠ Y284), V293 (≠ A285), D310 (= D299), I311 (= I300), D329 (≠ G318), V330 (≠ A319), Q404 (≠ A384), M405 (≠ V385), G423 (≠ A404)
- binding magnesium ion: D453 (= D435), N480 (vs. gap), H482 (vs. gap)
- 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 (≠ D380), G401 (≠ S381), Q402 (≠ T382), H403 (≠ Q383), G426 (= G408), M428 (≠ L410), G452 (= G434), G454 (= G436), S455 (≠ G437), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), G484 (vs. gap)
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)
28% identity, 97% coverage: 10:530/537 of query aligns to 16:560/582 of 5k6rA
- active site: Y33 (≠ I27), G35 (= G29), G36 (≠ V30), A37 (≠ H31), S38 (≠ T32), E59 (= E52), T82 (≠ I75), F121 (≠ L116), Q122 (≠ H117), E123 (= E118), K171 (≠ T167), M266 (≠ V259), V293 (≠ A285), V400 (≠ D380), G426 (= G408), M428 (≠ L410), D453 (= D435), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), M485 (vs. gap), V486 (vs. gap), W489 (= W460), H558 (= H528)
- binding methyl 4-[(3-methoxy-4-methyl-5-oxidanylidene-1,2,4-triazol-1-yl)carbonylsulfamoyl]-5-methyl-thiophene-3-carboxylate: R292 (≠ Y284), W489 (= W460)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G212), G223 (= G213), G224 (= G214), T246 (= T236), L247 (≠ V237), M248 (≠ N238), L264 (≠ K257), M266 (≠ V259), G286 (= G273), R288 (≠ E275), R292 (≠ Y284), V293 (≠ A285), D310 (= D299), I311 (= I300), G328 (≠ S317), D329 (≠ G318), V330 (≠ A319), M405 (≠ V385), G423 (≠ A404)
- binding magnesium ion: D453 (= D435), N480 (vs. gap), H482 (vs. gap)
- 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 (≠ D380), G401 (≠ S381), Q402 (≠ T382), H403 (≠ Q383), G426 (= G408), M428 (≠ L410), D453 (= D435), G454 (= G436), S455 (≠ G437), M458 (≠ F440), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), G484 (vs. gap), M485 (vs. gap), V486 (vs. gap)
Sites not aligning to the query:
1z8nA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with an imidazolinone herbicide, imazaquin (see paper)
28% identity, 97% coverage: 10:530/537 of query aligns to 16:560/582 of 1z8nA
- active site: Y33 (≠ I27), G35 (= G29), G36 (≠ V30), A37 (≠ H31), S38 (≠ T32), E59 (= E52), T82 (≠ I75), F121 (≠ L116), Q122 (≠ H117), E123 (= E118), K171 (≠ T167), M266 (≠ V259), V293 (≠ A285), V400 (≠ D380), G426 (= G408), M428 (≠ L410), D453 (= D435), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), M485 (vs. gap), V486 (vs. gap), W489 (= W460), H558 (= H528)
- binding 2-(4-isopropyl-4-methyl-5-oxo-4,5-dihydro-1h-imidazol-2-yl)quinoline-3-carboxylic acid: K135 (≠ L131), R161 (= R157), Y191 (≠ A183), R194 (= R186), D291 (≠ L283), R292 (≠ Y284), D312 (= D301), W489 (= W460)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G212), G224 (= G214), T246 (= T236), L247 (≠ V237), M248 (≠ N238), L264 (≠ K257), G265 (≠ A258), M266 (≠ V259), H267 (≠ R260), G286 (= G273), V287 (≠ T274), R288 (≠ E275), D290 (= D282), R292 (≠ Y284), V293 (≠ A285), D310 (= D299), I311 (= I300), D329 (≠ G318), V330 (≠ A319), M405 (≠ V385), G423 (≠ A404), G424 (= G406)
- binding magnesium ion: D453 (= D435), N480 (vs. gap)
- binding thiamine diphosphate: V400 (≠ D380), G401 (≠ S381), Q402 (≠ T382), H403 (≠ Q383), G426 (= G408), M428 (≠ L410), G452 (= G434), G454 (= G436), S455 (≠ G437), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), G484 (vs. gap), M485 (vs. gap), V486 (vs. gap)
Sites not aligning to the query:
1yi1A Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a sulfonylurea herbicide, tribenuron methyl (see paper)
28% identity, 97% coverage: 10:530/537 of query aligns to 16:560/582 of 1yi1A
- active site: Y33 (≠ I27), G35 (= G29), G36 (≠ V30), A37 (≠ H31), S38 (≠ T32), E59 (= E52), T82 (≠ I75), F121 (≠ L116), Q122 (≠ H117), E123 (= E118), K171 (≠ T167), M266 (≠ V259), V293 (≠ A285), V400 (≠ D380), G426 (= G408), M428 (≠ L410), D453 (= D435), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), M485 (vs. gap), V486 (vs. gap), W489 (= W460), H558 (= H528)
- binding methyl 2-[4-methoxy-6-methyl-1,3,5-trazin-2-yl(methyl)carbamoylsulfamoyl]benzoate: D291 (≠ L283), R292 (≠ Y284), W489 (= W460)
- binding flavin-adenine dinucleotide: R161 (= R157), G223 (= G213), G224 (= G214), T246 (= T236), L247 (≠ V237), M248 (≠ N238), M263 (≠ L256), L264 (≠ K257), G265 (≠ A258), M266 (≠ V259), H267 (≠ R260), G286 (= G273), V287 (≠ T274), R288 (≠ E275), D290 (= D282), V293 (≠ A285), D310 (= D299), I311 (= I300), D329 (≠ G318), V330 (≠ A319), M405 (≠ V385), G423 (≠ A404), G424 (= G406)
- binding magnesium ion: D453 (= D435), N480 (vs. gap), H482 (vs. gap)
Sites not aligning to the query:
1yi0A Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a sulfonylurea herbicide, sulfometuron methyl (see paper)
28% identity, 97% coverage: 10:530/537 of query aligns to 16:560/582 of 1yi0A
- active site: Y33 (≠ I27), G35 (= G29), G36 (≠ V30), A37 (≠ H31), S38 (≠ T32), E59 (= E52), T82 (≠ I75), F121 (≠ L116), Q122 (≠ H117), E123 (= E118), K171 (≠ T167), M266 (≠ V259), V293 (≠ A285), V400 (≠ D380), G426 (= G408), M428 (≠ L410), D453 (= D435), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), M485 (vs. gap), V486 (vs. gap), W489 (= W460), H558 (= H528)
- binding methyl 2-[({[(4,6-dimethylpyrimidin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: D291 (≠ L283), R292 (≠ Y284), W489 (= W460)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G212), G223 (= G213), G224 (= G214), T246 (= T236), L247 (≠ V237), M248 (≠ N238), L264 (≠ K257), G265 (≠ A258), M266 (≠ V259), H267 (≠ R260), G286 (= G273), V287 (≠ T274), R288 (≠ E275), D290 (= D282), R292 (≠ Y284), V293 (≠ A285), D310 (= D299), I311 (= I300), G328 (≠ S317), D329 (≠ G318), V330 (≠ A319), M405 (≠ V385), G423 (≠ A404), G424 (= G406)
- binding magnesium ion: D453 (= D435), N480 (vs. gap), H482 (vs. gap)
Sites not aligning to the query:
1yhzA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron (see paper)
28% identity, 97% coverage: 10:530/537 of query aligns to 16:560/582 of 1yhzA
- active site: Y33 (≠ I27), G35 (= G29), G36 (≠ V30), A37 (≠ H31), S38 (≠ T32), E59 (= E52), T82 (≠ I75), F121 (≠ L116), Q122 (≠ H117), E123 (= E118), K171 (≠ T167), M266 (≠ V259), V293 (≠ A285), V400 (≠ D380), G426 (= G408), M428 (≠ L410), D453 (= D435), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), M485 (vs. gap), V486 (vs. gap), W489 (= W460), H558 (= H528)
- binding 1-(2-chlorophenylsulfonyl)-3-(4-methoxy-6-methyl-l,3,5-triazin-2-yl)urea: D291 (≠ L283), R292 (≠ Y284), M485 (vs. gap), W489 (= W460)
- binding flavin-adenine dinucleotide: R161 (= R157), G223 (= G213), G224 (= G214), T246 (= T236), L247 (≠ V237), M248 (≠ N238), L264 (≠ K257), M266 (≠ V259), H267 (≠ R260), G286 (= G273), V287 (≠ T274), R288 (≠ E275), D290 (= D282), V293 (≠ A285), D310 (= D299), I311 (= I300), D329 (≠ G318), V330 (≠ A319), Q404 (≠ A384), M405 (≠ V385), G423 (≠ A404), G424 (= G406)
- binding magnesium ion: D453 (= D435), N480 (vs. gap), H482 (vs. gap)
Sites not aligning to the query:
1yhyA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
28% identity, 97% coverage: 10:530/537 of query aligns to 16:560/582 of 1yhyA
- active site: Y33 (≠ I27), G35 (= G29), G36 (≠ V30), A37 (≠ H31), S38 (≠ T32), E59 (= E52), T82 (≠ I75), F121 (≠ L116), Q122 (≠ H117), E123 (= E118), K171 (≠ T167), M266 (≠ V259), V293 (≠ A285), V400 (≠ D380), G426 (= G408), M428 (≠ L410), D453 (= D435), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), M485 (vs. gap), V486 (vs. gap), W489 (= W460), H558 (= H528)
- binding methyl 2-[({[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: D291 (≠ L283), R292 (≠ Y284), V486 (vs. gap), W489 (= W460)
- binding flavin-adenine dinucleotide: R161 (= R157), G222 (= G212), G223 (= G213), G224 (= G214), T246 (= T236), L247 (≠ V237), M248 (≠ N238), L264 (≠ K257), G265 (≠ A258), M266 (≠ V259), H267 (≠ R260), G286 (= G273), V287 (≠ T274), R288 (≠ E275), D290 (= D282), V293 (≠ A285), D310 (= D299), I311 (= I300), D329 (≠ G318), V330 (≠ A319), Q404 (≠ A384), M405 (≠ V385), G423 (≠ A404), G424 (= G406)
- binding magnesium ion: D453 (= D435), N480 (vs. gap), H482 (vs. gap)
Sites not aligning to the query:
1ybhA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a sulfonylurea herbicide chlorimuron ethyl (see paper)
28% identity, 97% coverage: 10:530/537 of query aligns to 16:560/582 of 1ybhA
- active site: Y33 (≠ I27), G35 (= G29), G36 (≠ V30), A37 (≠ H31), S38 (≠ T32), E59 (= E52), T82 (≠ I75), F121 (≠ L116), Q122 (≠ H117), E123 (= E118), K171 (≠ T167), M266 (≠ V259), V293 (≠ A285), V400 (≠ D380), G426 (= G408), M428 (≠ L410), D453 (= D435), N480 (vs. gap), H482 (vs. gap), L483 (vs. gap), M485 (vs. gap), V486 (vs. gap), W489 (= W460), H558 (= H528)
- binding 2-[[[[(4-chloro-6-methoxy-2-pyrimidinyl)amino]carbonyl]amino]sulfonyl]benzoic acid ethyl ester: M266 (≠ V259), D291 (≠ L283), R292 (≠ Y284), M485 (vs. gap), W489 (= W460)
- binding flavin-adenine dinucleotide: R161 (= R157), G223 (= G213), G224 (= G214), T246 (= T236), L247 (≠ V237), M248 (≠ N238), L264 (≠ K257), M266 (≠ V259), H267 (≠ R260), G286 (= G273), V287 (≠ T274), R288 (≠ E275), D290 (= D282), V293 (≠ A285), D310 (= D299), I311 (= I300), D329 (≠ G318), V330 (≠ A319), Q404 (≠ A384), M405 (≠ V385), G423 (≠ A404), G424 (= G406)
- binding magnesium ion: D453 (= D435), N480 (vs. gap), H482 (vs. gap)
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)
28% identity, 98% coverage: 4:530/537 of query aligns to 92:642/667 of P09342
- C161 (≠ A72) modified: Disulfide link with 307
- P194 (≠ R105) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ A215) 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)
29% identity, 98% coverage: 4:530/537 of query aligns to 89:639/664 of P09114
- P191 (≠ R105) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
- W568 (= W460) mutation to L: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191.
P40149 Oxalyl-CoA decarboxylase; EC 4.1.1.8 from Oxalobacter formigenes (see 2 papers)
27% identity, 99% coverage: 2:535/537 of query aligns to 6:551/568 of P40149
- E56 (= E52) mutation to A: Loss of the decarboxylase activity. The mutant forms a dimer and not a tetramer.
- Y120 (≠ L116) mutation to A: 3-fold reduction in the affinity binding and strong reduction in the catalytic efficiency for oxalyl-CoA.; mutation to F: 2 and 12-fold reduction in the affinity binding and in the catalytic efficiency for oxalyl-CoA, respectively.
- E121 (≠ H117) mutation to A: 2-fold reduction in the affinity binding and strong reduction in the catalytic efficiency for oxalyl-CoA.; mutation to Q: Slight increase of the affinity binding and strong reduction in the catalytic efficiency for oxalyl-CoA.
- R160 (= R157) binding ADP
- K222 (≠ G213) binding ADP
- R282 (≠ E275) binding ADP
- D306 (= D299) binding ADP
- I326 (≠ A319) binding ADP
- Y377 (vs. gap) binding thiamine diphosphate
- D452 (= D435) binding Mg(2+)
- N479 (= N462) binding Mg(2+)
- G481 (= G464) binding Mg(2+)
- Y483 (= Y465) binding thiamine diphosphate; mutation to A: Does not affect oxalyl-CoA binding, but it strongly reduces the catalytic efficiency for oxalyl-CoA.; mutation to F: 2-fold reduction in the affinity binding and strong reduction in the catalytic efficiency for oxalyl-CoA.
Sites not aligning to the query:
- 553 S→A: Does not affect oxalyl-CoA binding, but it reduces 7-fold the catalytic efficiency for oxalyl-CoA.
- 555 R→A: 3-fold reduction in the affinity binding for oxalyl-CoA, but it does not affect the catalytic efficiency.
Query Sequence
>WP_012706784.1 NCBI__GCF_000018545.1:WP_012706784.1
MSVETKTVGEVLVDLLEANGVEVVFGIPGVHTVELYRGLAASKIRHVTPRHEQGAGFMAD
GYARVSGKPGVALVITGPGLTNTITAMAQARQDSIPMLVISGVNRRDSLGHGRGLLHELP
DQQGMMKTLALYSHTLINPADLPLVVDRAFAVLLSGRPGPVHIEIPTDVMAERIESRGTK
PAAATRPRSDGETLQRAAILCAEASRPVILCGGGALTAEAEVRGLAEQIGAPVVTTVNAR
GMLAGHPLRVPASPSLKAVRALLRDADLVLALGTEMGQTDYDLYADGGFPMLRNLIRTDI
DAAQLARGPQAALSVLSGARAATAGILGFLPGHTAARDGASRADATRKAALKELTPKMRA
EVGIIDLIYKALPDCTIVGDSTQAVYAGNLYCDAPRQRAWFNSATGYGSLGYAPPAAVGA
AVADRARPVVCLVGDGGFQFSLAEIGSAVDAGARVIFLVWNNDGYREIESHMVEAGVTPE
GVKPSAPDFLLTAGAYGVPAERLAKIGDLPRALADAASRSGPSLIEIHQEKTAGVGG
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