SitesBLAST
Comparing BPHYT_RS19345 FitnessBrowser__BFirm:BPHYT_RS19345 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)
4rjiC Acetolactate synthase from bacillus subtilis bound to thdp - crystal form i (see paper)
29% identity, 97% coverage: 15:570/572 of query aligns to 1:554/555 of 4rjiC
- binding magnesium ion: D438 (= D453), D465 (≠ N480), T467 (≠ H482)
- binding thiamine diphosphate: P24 (= P38), E48 (= E64), P74 (= P90), S387 (≠ N403), H388 (≠ Y404), Q411 (≠ G426), G437 (= G452), D438 (= D453), G439 (= G454), G440 (≠ C455), T467 (≠ H482), Y468 (≠ F483), D469 (≠ G484), M470 (≠ T485), V471 (≠ I486), Y534 (≠ Q550)
4rjkG Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
30% identity, 97% coverage: 18:570/572 of query aligns to 3:553/553 of 4rjkG
- binding magnesium ion: D437 (= D453), D464 (≠ N480), T466 (≠ H482)
- 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 (= E64), Q110 (= Q127)
- binding thiamine diphosphate: I384 (≠ A401), G385 (= G402), S386 (≠ N403), H387 (≠ Y404), Q410 (≠ G426), L412 (≠ M428), G436 (= G452), D437 (= D453), G438 (= G454), G439 (≠ C455), T466 (≠ H482), Y467 (≠ F483), D468 (≠ G484), M469 (≠ T485), V470 (≠ I486), Y533 (≠ Q550)
4rjkF Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
30% identity, 92% coverage: 18:546/572 of query aligns to 3:529/552 of 4rjkF
- binding magnesium ion: D437 (= D453), D464 (≠ N480), T466 (≠ H482)
- binding pyruvic acid: A25 (≠ E40), K26 (≠ S41)
- binding thiamine diphosphate: P23 (= P38), E47 (= E64), P73 (= P90), G385 (= G402), S386 (≠ N403), H387 (≠ Y404), Q410 (≠ G426), L412 (≠ M428), G436 (= G452), D437 (= D453), G438 (= G454), G439 (≠ C455), T466 (≠ H482), Y467 (≠ F483), D468 (≠ G484), M469 (≠ T485), V470 (≠ I486)
Sites not aligning to the query:
6wo1A Hybrid acetohydroxyacid synthase complex structure with cryptococcus neoformans ahas catalytic subunit and saccharomyces cerevisiae ahas regulatory subunit (see paper)
28% identity, 94% coverage: 17:555/572 of query aligns to 10:533/551 of 6wo1A
- active site: Y30 (≠ V37), G32 (= G39), G33 (≠ E40), A34 (≠ S41), I35 (≠ F42), E56 (= E64), T79 (= T87), F118 (= F126), Q119 (= Q127), E120 (= E128), K168 (≠ E176), M255 (≠ L268), V282 (≠ T295), V398 (≠ A401), G424 (= G426), M426 (= M428), D451 (= D453), N478 (= N480)
- binding 2-methylpyrimidin-4-amine: G424 (= G426), T425 (≠ A427), M426 (= M428)
- binding diphosphate: V398 (≠ A401), G399 (= G402), Q400 (≠ N403), H401 (≠ Y404), G450 (= G452), D451 (= D453), A452 (≠ G454), S453 (≠ C455)
- binding flavin-adenine dinucleotide: D97 (= D105), R158 (= R166), G208 (= G222), G210 (= G223), S213 (≠ W226), T235 (≠ A248), L236 (≠ F249), Q237 (≠ R250), I253 (≠ V266), G254 (= G267), M255 (≠ L268), G275 (= G288), V276 (≠ P289), R277 (= R290), D279 (≠ G292), R281 (≠ A294), V282 (≠ T295), E308 (≠ H315), I309 (≠ Q316), D327 (≠ E337), V328 (≠ L338), Q402 (≠ A405), G421 (≠ T424), G422 (≠ S425)
- binding magnesium ion: D451 (= D453), N478 (= N480)
1n0hA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorimuron ethyl (see paper)
26% identity, 95% coverage: 7:551/572 of query aligns to 1:560/599 of 1n0hA
- active site: Y31 (≠ V37), G33 (= G39), G34 (≠ E40), A35 (≠ S41), I36 (≠ F42), E57 (= E64), T80 (= T87), F119 (= F126), Q120 (= Q127), E121 (= E128), K169 (≠ E176), R230 (≠ D233), M266 (≠ L268), V293 (≠ T295), V409 (≠ A401), L434 (vs. gap), G435 (= G426), M437 (= M428), D462 (= D453), N489 (= N480), E491 (≠ H482), Q492 (≠ F483), M494 (≠ T485), V495 (≠ I486), W498 (≠ H489), L520 (≠ F511), G525 (= G516), L526 (≠ A517), K559 (≠ Q550)
- binding 4-{[(4'-amino-2'-methylpyrimidin-5'-yl)methyl]amino}pent-3-enyl diphosphate: V409 (≠ A401), G410 (= G402), Q411 (≠ N403), H412 (≠ Y404), G435 (= G426), M437 (= M428), G461 (= G452), D462 (= D453), A463 (≠ G454), S464 (≠ C455), M467 (= M458), N489 (= N480), E491 (≠ H482), Q492 (≠ F483), G493 (= G484), V495 (≠ I486)
- binding 2-[[[[(4-chloro-6-methoxy-2-pyrimidinyl)amino]carbonyl]amino]sulfonyl]benzoic acid ethyl ester: G34 (≠ E40), A35 (≠ S41), V109 (≠ C116), P110 (≠ A117), F119 (= F126), K169 (≠ E176), M266 (≠ L268), D291 (≠ E293), R292 (≠ A294), V495 (≠ I486), W498 (≠ H489)
- binding flavin-adenine dinucleotide: R159 (= R166), G219 (= G222), A220 (≠ G223), G221 (≠ S224), N224 (≠ T227), T246 (≠ A248), L247 (≠ F249), Q248 (≠ R250), L264 (≠ V266), G265 (= G267), M266 (≠ L268), H267 (≠ G269), G286 (= G288), A287 (≠ P289), R288 (= R290), D290 (≠ G292), R292 (≠ A294), V293 (≠ T295), E319 (≠ H315), V320 (≠ Q316), N324 (≠ E320), G337 (vs. gap), D338 (≠ S333), A339 (≠ G334), M414 (≠ T406), G432 (≠ T424), G433 (≠ S425)
- binding magnesium ion: D462 (= D453), N489 (= N480), E491 (≠ H482)
- binding thiamine diphosphate: Y31 (≠ V37), E57 (= E64), P83 (= P90)
1t9dA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
26% identity, 94% coverage: 17:551/572 of query aligns to 9:557/596 of 1t9dA
- active site: Y29 (≠ V37), G31 (= G39), G32 (≠ E40), A33 (≠ S41), I34 (≠ F42), E55 (= E64), T78 (= T87), F117 (= F126), Q118 (= Q127), E119 (= E128), K167 (≠ E176), R227 (≠ D233), M263 (≠ L268), V290 (≠ T295), V406 (≠ A401), L431 (vs. gap), G432 (= G426), M434 (= M428), D459 (= D453), N486 (= N480), E488 (≠ H482), Q489 (≠ F483), M491 (≠ T485), V492 (≠ I486), W495 (≠ H489), L517 (≠ F511), G522 (= G516), L523 (≠ A517), K556 (≠ Q550)
- binding methyl 2-[({[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (≠ E40), A33 (≠ S41), V107 (≠ C116), P108 (≠ A117), F117 (= F126), K167 (≠ E176), M263 (≠ L268), D288 (≠ E293), R289 (≠ A294), W495 (≠ H489)
- binding flavin-adenine dinucleotide: R157 (= R166), G216 (= G222), A217 (≠ G223), G218 (≠ S224), N221 (≠ T227), T243 (≠ A248), L244 (≠ F249), Q245 (≠ R250), M260 (≠ D265), L261 (≠ V266), H264 (≠ G269), G283 (= G288), A284 (≠ P289), R285 (= R290), D287 (≠ G292), R289 (≠ A294), V290 (≠ T295), E316 (≠ H315), V317 (≠ Q316), N321 (≠ E320), G334 (vs. gap), D335 (≠ S333), A336 (≠ G334), Q410 (≠ A405), M411 (≠ T406), G429 (≠ T424), G430 (≠ S425)
- binding magnesium ion: D459 (= D453), N486 (= N480), E488 (≠ H482)
- binding 2,5-dimethyl-pyrimidin-4-ylamine: E55 (= E64), P81 (= P90), Q118 (= Q127), G432 (= G426), M434 (= M428), M464 (= M458)
1t9cA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, sulfometuron methyl (see paper)
26% identity, 94% coverage: 17:551/572 of query aligns to 9:557/596 of 1t9cA
- active site: Y29 (≠ V37), G31 (= G39), G32 (≠ E40), A33 (≠ S41), I34 (≠ F42), E55 (= E64), T78 (= T87), F117 (= F126), Q118 (= Q127), E119 (= E128), K167 (≠ E176), R227 (≠ D233), M263 (≠ L268), V290 (≠ T295), V406 (≠ A401), L431 (vs. gap), G432 (= G426), M434 (= M428), D459 (= D453), N486 (= N480), E488 (≠ H482), Q489 (≠ F483), M491 (≠ T485), V492 (≠ I486), W495 (≠ H489), L517 (≠ F511), G522 (= G516), L523 (≠ A517), K556 (≠ Q550)
- binding methyl 2-[({[(4,6-dimethylpyrimidin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (≠ E40), V107 (≠ C116), P108 (≠ A117), F117 (= F126), K167 (≠ E176), D288 (≠ E293), R289 (≠ A294), W495 (≠ H489)
- binding flavin-adenine dinucleotide: R157 (= R166), G216 (= G222), A217 (≠ G223), G218 (≠ S224), N221 (≠ T227), T243 (≠ A248), L244 (≠ F249), Q245 (≠ R250), L261 (≠ V266), M263 (≠ L268), H264 (≠ G269), G283 (= G288), A284 (≠ P289), R285 (= R290), D287 (≠ G292), R289 (≠ A294), V290 (≠ T295), E316 (≠ H315), V317 (≠ Q316), N321 (≠ E320), G334 (vs. gap), D335 (≠ S333), A336 (≠ G334), M411 (≠ T406), G429 (≠ T424), G430 (≠ S425)
- binding magnesium ion: D459 (= D453), N486 (= N480), E488 (≠ H482)
1t9aA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, tribenuron methyl (see paper)
26% identity, 94% coverage: 17:551/572 of query aligns to 10:558/597 of 1t9aA
- active site: Y30 (≠ V37), G32 (= G39), G33 (≠ E40), A34 (≠ S41), I35 (≠ F42), E56 (= E64), T79 (= T87), F118 (= F126), Q119 (= Q127), E120 (= E128), K168 (≠ E176), R228 (≠ D233), M264 (≠ L268), V291 (≠ T295), V407 (≠ A401), L432 (vs. gap), G433 (= G426), M435 (= M428), D460 (= D453), N487 (= N480), E489 (≠ H482), Q490 (≠ F483), M492 (≠ T485), V493 (≠ I486), W496 (≠ H489), L518 (≠ F511), G523 (= G516), L524 (≠ A517), K557 (≠ Q550)
- binding methyl 2-[4-methoxy-6-methyl-1,3,5-trazin-2-yl(methyl)carbamoylsulfamoyl]benzoate: G33 (≠ E40), V108 (≠ C116), P109 (≠ A117), F118 (= F126), K168 (≠ E176), M264 (≠ L268), D289 (≠ E293), R290 (≠ A294), M492 (≠ T485), V493 (≠ I486), W496 (≠ H489)
- binding flavin-adenine dinucleotide: R158 (= R166), G217 (= G222), A218 (≠ G223), G219 (≠ S224), N222 (≠ T227), T244 (≠ A248), L245 (≠ F249), Q246 (≠ R250), L262 (≠ V266), M264 (≠ L268), H265 (≠ G269), G284 (= G288), A285 (≠ P289), R286 (= R290), D288 (≠ G292), R290 (≠ A294), V291 (≠ T295), E317 (≠ H315), V318 (≠ Q316), N322 (≠ E320), G335 (vs. gap), D336 (≠ S333), A337 (≠ G334), Q411 (≠ A405), M412 (≠ T406), G430 (≠ T424), G431 (≠ S425)
- binding magnesium ion: D460 (= D453), N487 (= N480), E489 (≠ H482)
- binding propyl trihydrogen diphosphate: V407 (≠ A401), G408 (= G402), Q409 (≠ N403), H410 (≠ Y404), M435 (= M428), G459 (= G452), D460 (= D453), A461 (≠ G454), S462 (≠ C455), N487 (= N480), E489 (≠ H482), Q490 (≠ F483), G491 (= G484), M492 (≠ T485)
- binding 5-{[ethyl(methyl)amino]methyl}-2-methyl-5,6-dihydropyrimidin-4-amine: G433 (= G426), M435 (= M428), M465 (= M458)
1t9bB Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron (see paper)
27% identity, 94% coverage: 17:551/572 of query aligns to 9:556/595 of 1t9bB
- active site: Y29 (≠ V37), G31 (= G39), G32 (≠ E40), A33 (≠ S41), I34 (≠ F42), E55 (= E64), T78 (= T87), F117 (= F126), Q118 (= Q127), E119 (= E128), K167 (≠ E176), R226 (≠ D233), M262 (≠ L268), V289 (≠ T295), V405 (≠ A401), L430 (vs. gap), G431 (= G426), M433 (= M428), D458 (= D453), N485 (= N480), E487 (≠ H482), Q488 (≠ F483), M490 (≠ T485), V491 (≠ I486), W494 (≠ H489), L516 (≠ F511), G521 (= G516), L522 (≠ A517), K555 (≠ Q550)
- binding 1-(2-chlorophenylsulfonyl)-3-(4-methoxy-6-methyl-l,3,5-triazin-2-yl)urea: V107 (≠ C116), P108 (≠ A117), D287 (≠ E293), R288 (≠ A294), M490 (≠ T485), W494 (≠ H489)
- binding flavin-adenine dinucleotide: R157 (= R166), G215 (= G222), A216 (≠ G223), G217 (≠ S224), N220 (≠ T227), T242 (≠ A248), L243 (≠ F249), Q244 (≠ R250), M259 (≠ D265), L260 (≠ V266), M262 (≠ L268), H263 (≠ G269), G282 (= G288), A283 (≠ P289), R284 (= R290), D286 (≠ G292), R288 (≠ A294), V289 (≠ T295), E315 (≠ H315), V316 (≠ Q316), N320 (≠ E320), G333 (vs. gap), D334 (≠ S333), A335 (≠ G334), Q409 (≠ A405), M410 (≠ T406), G428 (≠ T424), G429 (≠ S425)
- binding magnesium ion: D458 (= D453), N485 (= N480), E487 (≠ H482)
5wkcA Saccharomyces cerevisiae acetohydroxyacid synthase in complex with the herbicide penoxsulam (see paper)
26% identity, 94% coverage: 17:551/572 of query aligns to 9:552/591 of 5wkcA
- active site: Y29 (≠ V37), G31 (= G39), G32 (≠ E40), A33 (≠ S41), I34 (≠ F42), E55 (= E64), T78 (= T87), F117 (= F126), Q118 (= Q127), E119 (= E128), K167 (≠ E176), R222 (≠ D233), M258 (≠ L268), V285 (≠ T295), V401 (≠ A401), L426 (vs. gap), G427 (= G426), M429 (= M428), D454 (= D453), N481 (= N480), E483 (≠ H482), Q484 (≠ F483), M486 (≠ T485), V487 (≠ I486), W490 (≠ H489), L512 (≠ F511), G517 (= G516), L518 (≠ A517), K551 (≠ Q550)
- binding 2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-2-[(1~{S})-1-(dioxidanyl)-1-oxidanyl-ethyl]-4-methyl-1,3-thiazol-5-yl]ethyl phosphono hydrogen phosphate: V401 (≠ A401), G402 (= G402), Q403 (≠ N403), H404 (≠ Y404), G427 (= G426), M429 (= M428), G453 (= G452), D454 (= D453), A455 (≠ G454), S456 (≠ C455), M459 (= M458), N481 (= N480), E483 (≠ H482), Q484 (≠ F483), G485 (= G484), M486 (≠ T485), V487 (≠ I486)
- binding ethaneperoxoic acid: G32 (≠ E40), Q118 (= Q127)
- binding flavin-adenine dinucleotide: R157 (= R166), G211 (= G222), A212 (≠ G223), G213 (≠ S224), N216 (≠ T227), T238 (≠ A248), L239 (≠ F249), Q240 (≠ R250), L256 (≠ V266), M258 (≠ L268), G278 (= G288), A279 (≠ P289), R280 (= R290), R284 (≠ A294), V285 (≠ T295), E311 (≠ H315), V312 (≠ Q316), N316 (≠ E320), D330 (≠ S333), A331 (≠ G334), M406 (≠ T406), G424 (≠ T424)
- binding magnesium ion: D454 (= D453), N481 (= N480), E483 (≠ H482)
- binding 2-(2,2-difluoroethoxy)-N-(5,8-dimethoxy[1,2,4]triazolo[1,5-c]pyrimidin-2-yl)-6-(trifluoromethyl)benzenesulfonamide: G32 (≠ E40), A33 (≠ S41), V107 (≠ C116), F117 (= F126), K167 (≠ E176), M258 (≠ L268), R284 (≠ A294), M486 (≠ T485), W490 (≠ H489)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: P30 (= P38), E55 (= E64)
5d6rB Acetolactate synthase from klebsiella pneumoniae in complex with mechanism-based inhibitor
31% identity, 92% coverage: 18:546/572 of query aligns to 7:531/548 of 5d6rB
- active site: I26 (≠ V37), G28 (= G39), A29 (≠ E40), K30 (≠ S41), I31 (≠ F42), E51 (= E64), T74 (= T87), H113 (≠ F126), Q114 (= Q127), S115 (≠ E128), Q163 (≠ E176), L254 (= L268), E281 (≠ T295), M386 (≠ A401), Q412 (≠ G426), M414 (= M428), D439 (= D453), D466 (≠ N479), G468 (= G481), Y469 (≠ F483), M471 (≠ T485), V472 (≠ I486), Q475 (≠ H489)
- 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 (≠ A401), G387 (= G402), S388 (≠ N403), Q412 (≠ G426), M414 (= M428), D439 (= D453), G440 (= G454), G468 (= G481), Y469 (≠ F483), N470 (≠ G484), M471 (≠ T485)
- binding magnesium ion: R63 (≠ K76), Q212 (≠ T227), D439 (= D453), D466 (≠ N479), G468 (= G481)
Sites not aligning to the query:
1t9bA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron (see paper)
27% identity, 94% coverage: 17:551/572 of query aligns to 9:544/583 of 1t9bA
- active site: Y29 (≠ V37), G31 (= G39), G32 (≠ E40), A33 (≠ S41), I34 (≠ F42), E55 (= E64), T78 (= T87), F117 (= F126), Q118 (= Q127), E119 (= E128), K167 (≠ E176), R214 (≠ D233), M250 (≠ L268), V277 (≠ T295), V393 (≠ A401), L418 (vs. gap), G419 (= G426), M421 (= M428), D446 (= D453), N473 (= N480), E475 (≠ H482), Q476 (≠ F483), M478 (≠ T485), V479 (≠ I486), W482 (≠ H489), L504 (≠ F511), G509 (= G516), L510 (≠ A517), K543 (≠ Q550)
- binding 1-(2-chlorophenylsulfonyl)-3-(4-methoxy-6-methyl-l,3,5-triazin-2-yl)urea: V107 (≠ C116), P108 (≠ A117), F117 (= F126), D275 (≠ E293), R276 (≠ A294), M478 (≠ T485), W482 (≠ H489)
- binding flavin-adenine dinucleotide: R157 (= R166), G203 (= G222), A204 (≠ G223), G205 (≠ S224), N208 (≠ T227), T230 (≠ A248), L231 (≠ F249), Q232 (≠ R250), M247 (≠ D265), L248 (≠ V266), M250 (≠ L268), H251 (≠ G269), G270 (= G288), A271 (≠ P289), R272 (= R290), D274 (≠ G292), R276 (≠ A294), V277 (≠ T295), E303 (≠ H315), V304 (≠ Q316), N308 (≠ E320), D322 (≠ S333), A323 (≠ G334), Q397 (≠ A405), M398 (≠ T406), G416 (≠ T424), G417 (≠ S425)
- binding magnesium ion: D446 (= D453), N473 (= N480), E475 (≠ H482)
1t9dB Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
27% identity, 94% coverage: 17:551/572 of query aligns to 8:543/582 of 1t9dB
- active site: Y28 (≠ V37), G30 (= G39), G31 (≠ E40), A32 (≠ S41), I33 (≠ F42), E54 (= E64), T77 (= T87), F116 (= F126), Q117 (= Q127), E118 (= E128), K166 (≠ E176), R213 (≠ D233), M249 (≠ L268), V276 (≠ T295), V392 (≠ A401), L417 (vs. gap), G418 (= G426), M420 (= M428), D445 (= D453), N472 (= N480), E474 (≠ H482), Q475 (≠ F483), M477 (≠ T485), V478 (≠ I486), W481 (≠ H489), L503 (≠ F511), G508 (= G516), L509 (≠ A517), K542 (≠ Q550)
- binding methyl 2-[({[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G31 (≠ E40), A32 (≠ S41), V106 (≠ C116), P107 (≠ A117), F116 (= F126), K166 (≠ E176), M249 (≠ L268), D274 (≠ E293), R275 (≠ A294), W481 (≠ H489)
- binding flavin-adenine dinucleotide: R156 (= R166), G202 (= G222), A203 (≠ G223), G204 (≠ S224), N207 (≠ T227), T229 (≠ A248), L230 (≠ F249), Q231 (≠ R250), L247 (≠ V266), M249 (≠ L268), H250 (≠ G269), G269 (= G288), A270 (≠ P289), R271 (= R290), D273 (≠ G292), R275 (≠ A294), V276 (≠ T295), E302 (≠ H315), V303 (≠ Q316), N307 (≠ E320), G320 (vs. gap), D321 (≠ S333), A322 (≠ G334), Q396 (≠ A405), M397 (≠ T406), G415 (≠ T424), G416 (≠ S425)
- binding magnesium ion: D445 (= D453), N472 (= N480), E474 (≠ H482)
- binding 2,5-dimethyl-pyrimidin-4-ylamine: E54 (= E64), P80 (= P90), G418 (= G426), M420 (= M428), M450 (= M458)
5dx6B Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
31% identity, 92% coverage: 18:546/572 of query aligns to 19:537/557 of 5dx6B
- active site: I38 (≠ V37), G40 (= G39), A41 (≠ E40), K42 (≠ S41), I43 (≠ F42), E63 (= E64), T86 (= T87), H125 (≠ F126), Q126 (= Q127), S127 (≠ E128), Q175 (≠ E176), L268 (= L268), E295 (≠ T295), M392 (≠ A401), Q418 (≠ G426), M420 (= M428), D445 (= D453), D472 (≠ N479), G474 (= G481), Y475 (≠ F483), M477 (≠ T485), V478 (≠ I486), Q481 (≠ H489)
- binding 3-fluoro-2-oxopropanoic acid: G264 (= G264), R265 (≠ D265), Q272 (≠ P272), A400 (≠ H409), R401 (= R410), Y404 (≠ F412)
- binding magnesium ion: S135 (≠ G136), T138 (≠ A139), D445 (= D453), D472 (≠ N479), G474 (= G481)
- binding thiamine diphosphate: G393 (= G402), S394 (≠ N403), F395 (≠ Y404), Q418 (≠ G426), M420 (= M428), G444 (= G452), D445 (= D453), G446 (= G454), D472 (≠ N479), G474 (= G481), Y475 (≠ F483), N476 (≠ G484), M477 (≠ T485), V478 (≠ I486)
Sites not aligning to the query:
P07342 Acetolactate synthase catalytic subunit, mitochondrial; Acetohydroxy-acid synthase catalytic subunit; AHAS; ALS; EC 2.2.1.6 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 95% coverage: 7:551/572 of query aligns to 83:648/687 of P07342
- R241 (= R166) binding
- 355:376 (vs. 269:290, 23% identical) binding
- 407:426 (vs. 315:333, 5% identical) binding
6u9dB Saccharomyces cerevisiae acetohydroxyacid synthase (see paper)
26% identity, 95% coverage: 7:551/572 of query aligns to 3:568/607 of 6u9dB
- active site: Y33 (≠ V37), G35 (= G39), G36 (≠ E40), A37 (≠ S41), I38 (≠ F42), E59 (= E64), T82 (= T87), F121 (= F126), Q122 (= Q127), E123 (= E128), K171 (≠ E176), M274 (≠ L268), V301 (≠ T295), V417 (≠ A401), G443 (= G426), M445 (= M428), D470 (= D453), N497 (= N480), E499 (≠ H482), Q500 (≠ F483), M502 (≠ T485), V503 (≠ I486), W506 (≠ H489)
- binding methyl 2-[(4,6-dimethoxypyrimidin-2-yl)carbamoylsulfamoylmethyl]benzoate: G36 (≠ E40), V111 (≠ C116), P112 (≠ A117), F121 (= F126), K171 (≠ E176), D299 (≠ E293), R300 (≠ A294), M502 (≠ T485), W506 (≠ H489)
- binding flavin-adenine dinucleotide: R161 (= R166), A228 (≠ G223), G229 (≠ S224), N232 (≠ T227), T254 (≠ A248), L255 (≠ F249), Q256 (≠ R250), L272 (≠ V266), M274 (≠ L268), G294 (= G288), R296 (= R290), D298 (≠ G292), R300 (≠ A294), V301 (≠ T295), E327 (≠ H315), V328 (≠ Q316), N332 (≠ E320), D346 (≠ S333), A347 (≠ G334), M422 (≠ T406), G440 (≠ T424), G441 (≠ S425)
- binding magnesium ion: D470 (= D453), N497 (= N480)
- binding thiamine diphosphate: E59 (= E64), P85 (= P90), V417 (≠ A401), G418 (= G402), Q419 (≠ N403), H420 (≠ Y404), G443 (= G426), M445 (= M428), A471 (≠ G454), S472 (≠ C455), N497 (= N480), E499 (≠ H482), Q500 (≠ F483), G501 (= G484), M502 (≠ T485), V503 (≠ I486)
1ozgA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate (see paper)
31% identity, 92% coverage: 18:546/572 of query aligns to 8:534/549 of 1ozgA
- active site: I27 (≠ V37), G29 (= G39), A30 (≠ E40), K31 (≠ S41), I32 (≠ F42), E52 (= E64), T75 (= T87), H114 (≠ F126), Q115 (= Q127), S116 (≠ E128), Q164 (≠ E176), L257 (= L268), E284 (≠ T295), M389 (≠ A401), Q415 (≠ G426), M417 (= M428), D442 (= D453), D469 (≠ N479), G471 (= G481), Y472 (≠ F483), M474 (≠ T485), V475 (≠ I486), Q478 (≠ H489)
- binding 2-hydroxyethyl dihydrothiachrome diphosphate: M389 (≠ A401), G390 (= G402), S391 (≠ N403), F392 (≠ Y404), Q415 (≠ G426), M417 (= M428), G441 (= G452), D442 (= D453), G443 (= G454), D469 (≠ N479), G471 (= G481), Y472 (≠ F483), N473 (≠ G484), M474 (≠ T485), V475 (≠ I486)
- binding magnesium ion: D442 (= D453), D469 (≠ N479), G471 (= G481)
- binding phosphate ion: G253 (= G264), R254 (≠ D265), Q261 (≠ P272), R347 (vs. gap), R398 (= R410), Y401 (≠ F412)
Sites not aligning to the query:
1ozfA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors (see paper)
31% identity, 92% coverage: 18:546/572 of query aligns to 7:530/545 of 1ozfA
- active site: I26 (≠ V37), G28 (= G39), A29 (≠ E40), K30 (≠ S41), I31 (≠ F42), E51 (= E64), T74 (= T87), H113 (≠ F126), Q114 (= Q127), S115 (≠ E128), Q163 (≠ E176), L253 (= L268), E280 (≠ T295), M385 (≠ A401), Q411 (≠ G426), M413 (= M428), D438 (= D453), D465 (≠ N479), G467 (= G481), Y468 (≠ F483), M470 (≠ T485), V471 (≠ I486), Q474 (≠ H489)
- binding magnesium ion: D438 (= D453), D465 (≠ N479), G467 (= G481)
- binding phosphate ion: G249 (= G264), R250 (≠ D265), Q257 (≠ P272), R343 (vs. gap), R394 (= R410), L396 (vs. gap), Y397 (≠ F412)
- binding thiamine diphosphate: G386 (= G402), S387 (≠ N403), F388 (≠ Y404), Q411 (≠ G426), M413 (= M428), G437 (= G452), D438 (= D453), G439 (= G454), D465 (≠ N479), G467 (= G481), Y468 (≠ F483), N469 (≠ G484), M470 (≠ T485), V471 (≠ I486)
Sites not aligning to the query:
7egvA Acetolactate synthase from trichoderma harzianum with inhibitor harzianic acid (see paper)
28% identity, 93% coverage: 17:546/572 of query aligns to 8:546/590 of 7egvA
- active site: Y28 (≠ V37), G30 (= G39), G31 (≠ E40), A32 (≠ S41), I33 (≠ F42), E54 (= E64), T77 (= T87), F116 (= F126), Q117 (= Q127), K166 (≠ E176), E220 (≠ A232), M256 (≠ D265), V283 (≠ T295), V400 (≠ A401), L425 (vs. gap), G426 (= G426), M428 (= M428), Q483 (≠ F483), M485 (≠ T485), V486 (≠ I486), W489 (≠ H489), L511 (≠ F511), G516 (= G516), I517 (≠ A517)
- binding flavin-adenine dinucleotide: R156 (= R166), G209 (= G222), Q210 (vs. gap), G211 (= G223), T236 (vs. gap), L237 (vs. gap), H238 (vs. gap), G276 (= G288), S277 (≠ P289), R278 (= R290), D280 (≠ G292), R282 (≠ A294), V283 (≠ T295), E309 (≠ H315), I310 (≠ Q316), D328 (vs. gap), V329 (= V332), M405 (≠ T406), G423 (≠ T424), G424 (≠ S425)
- binding (2S)-3-methyl-2-[[(2S,4R)-1-methyl-4-[(2E,4E)-octa-2,4-dienoyl]-3,5-bis(oxidanylidene)pyrrolidin-2-yl]methyl]-2-oxidanyl-butanoic acid: F493 (≠ H493), Y494 (= Y494)
- binding magnesium ion: D453 (= D453), N480 (= N480), E482 (≠ H482)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: P29 (= P38), E54 (= E64), Q117 (= Q127), V400 (≠ A401), G401 (= G402), Q402 (≠ N403), H403 (≠ Y404), G426 (= G426), M428 (= M428), D453 (= D453), A454 (≠ G454), S455 (≠ C455), E482 (≠ H482), Q483 (≠ F483), G484 (= G484), M485 (≠ T485), V486 (≠ I486)
6bd9A Saccharomyces cerevisiae acetohydroxyacid synthase
26% identity, 95% coverage: 7:551/572 of query aligns to 1:542/542 of 6bd9A
- active site: Y31 (≠ V37), G33 (= G39), G34 (≠ E40), A35 (≠ S41), I36 (≠ F42), E57 (= E64), T80 (= T87), F119 (= F126), Q120 (= Q127), E121 (= E128), K169 (≠ E176), R228 (≠ D233), M264 (≠ L268), V291 (≠ T295), V407 (≠ A401), L432 (vs. gap), G433 (= G426), M435 (= M428), D460 (= D453), N487 (= N480), E489 (= E491), L502 (≠ F511), G507 (= G516), L508 (≠ A517), K541 (≠ Q550)
- binding flavin-adenine dinucleotide: R159 (= R166), G217 (= G222), A218 (≠ G223), G219 (≠ S224), N222 (≠ T227), T244 (≠ A248), L245 (≠ F249), L262 (≠ V266), G263 (= G267), H265 (≠ G269), G284 (= G288), A285 (≠ P289), R286 (= R290), D288 (≠ G292), R290 (≠ A294), V291 (≠ T295), E317 (≠ H315), V318 (≠ Q316), N322 (≠ E320), G335 (vs. gap), D336 (≠ S333), A337 (≠ G334)
- binding magnesium ion: D460 (= D453), N487 (= N480)
- binding oxygen molecule: G34 (≠ E40), T80 (= T87), Q120 (= Q127), A461 (≠ G454), Q494 (≠ L503)
- binding pyruvic acid: G33 (= G39), G34 (≠ E40), G34 (≠ E40), A35 (≠ S41), Q120 (= Q127)
- binding thiamine diphosphate: P32 (= P38), E57 (= E64), V407 (≠ A401), G408 (= G402), Q409 (≠ N403), H410 (≠ Y404), G433 (= G426), M435 (= M428), G459 (= G452), D460 (= D453), A461 (≠ G454), S462 (≠ C455), M465 (= M458), N487 (= N480)
Query Sequence
>BPHYT_RS19345 FitnessBrowser__BFirm:BPHYT_RS19345
MSQPNAPVSESAAAQTTGARLVVDALLTHGVERVFCVPGESFLAVLDSLHDETERIQTIV
CRHEAAAANMAEAVGKLTGRPGVALVTRGPGATHASIGVHTAYQDSTPMILLIGQCAREH
LDREAFQEIDYRRMFGQMAKWVAQIDDPKRIPEYLSHAFHTATSGRPGPVVLSLPEDVLS
DACAAVAGAPAYQRVAASPSAAQIEKLRVLLEGAQRPMVIAGGSGWTPAACADFRRFVEN
WQLPVGLAFRFQDTLDNEHPNYAGDVGLGINPALAQRIRDADVLLAIGPRLGEATTNGYT
LLDIPKTKQTLIHVHQGAEELGRVYAADLPIVSGMPELAAMLAELEPLSEQLAWSGAASE
AHQAYLDWRKPRQIPGDVQMGEVIQQLRAHLPDDAILTNGAGNYATWLHRHFSYRHYRSQ
LAPTSGAMGYGVPAAIAAKSMYPHRAVVALAGDGCFMMAAQELATAMQYDLHVLFIVVNN
GHFGTIRMHQERHYPGRVHGTGLTNPDFAAFARSFGAHGETVERTEDFLPALKRSIEAKR
AAVIEIRMPQEASTPGATLEQIREQGRKMRGE
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