SitesBLAST
Comparing BPHYT_RS31615 FitnessBrowser__BFirm:BPHYT_RS31615 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)
P07003 Pyruvate dehydrogenase [ubiquinone]; Pyruvate oxidase; POX; Pyruvate:ubiquinone-8 oxidoreductase; EC 1.2.5.1 from Escherichia coli (strain K12) (see 4 papers)
34% identity, 98% coverage: 1:597/610 of query aligns to 1:567/572 of P07003
- 1:182 (vs. 1:202, 36% identical) Pyr domain
- E50 (= E63) binding
- 183:334 (vs. 203:355, 35% identical) FAD-binding domain
- S210 (≠ A229) binding
- LR 234:235 (≠ LL 253:254) binding
- TGLI 251:254 (≠ IGLL 270:273) binding
- TQFPY 274:278 (≠ SGFPY 293:297) binding
- D292 (= D313) binding
- S297 (≠ M318) binding
- DI 311:312 (≠ DS 332:333) binding
- 335:530 (vs. 356:561, 30% identical) PP-binding domain
- T382 (≠ S404) binding
- FN 403:404 (≠ LS 423:424) binding
- G--SM 406:408 (≠ GLASM 426:430) binding
- D433 (= D455) binding
- DGG 433:435 (≠ DGA 455:457) binding
- N460 (= N488) binding
- 460:466 (vs. 488:494, 57% identical) binding
- V462 (≠ D490) binding
- F465 (≠ Q493) Moves into active site upon enzyme activation, plays a role in electron transfer
- A533 (≠ P564) mutation to T: In poxB11; poor activity in vivo, no longer activated by lipids.
- YM 549:550 (≠ TL 580:581) In vitro cleavage to yield alpha-peptide
- A553 (≠ G584) mutation to V: In poxB14; poor activity in vivo, no longer activated by lipids.
- D560 (≠ N590) mutation to P: In poxB15; normal activity.
- E564 (= E594) mutation to P: In poxB16; loss of activity, weakly activated by cleavage.
Sites not aligning to the query:
- 531:572 Membrane-binding domain
- 549:572 mutation Missing: In poxB6. Inactive in vivo, does not complement inactive mutants. Active in vitro, no longer activated by nor binds to, detergents.
- 564:572 mutation Missing: In poxB7 Inactive in vivo, reduced activity in vitro.
- 570:572 mutation Missing: In poxB8; reduced activity in vitro, not activated by lipids.
- 572 R→G: In poxB10; reduced activity in vivo and in vitro; may interact less with membranes.
3ey9A Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from escherichia coli (see paper)
34% identity, 98% coverage: 3:597/610 of query aligns to 2:566/571 of 3ey9A
- active site: V23 (≠ Y24), G25 (= G26), D26 (= D27), S27 (≠ G28), L28 (≠ I29), E49 (= E63), S72 (≠ T86), F111 (≠ Q125), Q112 (= Q126), G160 (≠ N175), L252 (= L272), A279 (≠ E299), V379 (≠ S402), G405 (= G426), M407 (= M430), D432 (= D455), N459 (= N488), V461 (≠ D490), L462 (= L491), F464 (≠ Q493), V465 (= V494), E468 (= E497), K528 (≠ P560)
- binding flavin-adenine dinucleotide: G208 (= G228), S209 (≠ A229), G210 (= G230), A232 (= A252), L233 (= L253), R234 (≠ L254), T250 (≠ I270), G251 (= G271), I253 (≠ L273), G272 (= G292), T273 (≠ S293), Q274 (≠ G294), F275 (= F295), Y277 (= Y297), D291 (= D313), I292 (≠ L314), S296 (≠ M318), G309 (= G331), D310 (= D332), I311 (≠ S333), T383 (≠ A406), F402 (≠ L423), N403 (≠ S424), Y548 (≠ T580)
- binding magnesium ion: D432 (= D455), N459 (= N488)
- binding thiamine diphosphate: T24 (≠ P25), E49 (= E63), S72 (≠ T86), G76 (= G90), H79 (= H93), G380 (= G403), T381 (≠ S404), P382 (≠ C405), M407 (= M430), G431 (= G454), D432 (= D455), G433 (= G456), G434 (≠ A457), N459 (= N488), V461 (≠ D490), L462 (= L491), G463 (≠ N492)
1v5gA Crystal structure of the reaction intermediate between pyruvate oxidase containing fad and tpp, and substrate pyruvate (see paper)
30% identity, 95% coverage: 4:583/610 of query aligns to 4:560/589 of 1v5gA
- binding flavin-adenine dinucleotide: G212 (= G228), I213 (≠ A229), G214 (= G230), T236 (≠ A252), G237 (≠ L253), K238 (≠ L254), T254 (≠ I270), Y255 (≠ G271), R256 (≠ L272), V257 (≠ L273), G276 (= G292), S277 (= S293), N278 (≠ G294), F279 (= F295), F281 (≠ Y297), D298 (= D313), I299 (≠ L314), M303 (= M318), D317 (= D332), A318 (≠ S333), P409 (≠ D425)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ S402), N388 (≠ S404), M414 (= M430), G438 (= G454), G440 (= G456), A441 (= A457), N466 (= N488), E468 (≠ Q493), Y469 (≠ V494), A470 (≠ T495), F471 (≠ W496), I472 (≠ E497)
- binding magnesium ion: D439 (= D455), N466 (= N488), E468 (≠ Q493)
1v5fA Crystal structure of pyruvate oxidase complexed with fad and tpp, from aerococcus viridans (see paper)
30% identity, 95% coverage: 4:583/610 of query aligns to 4:560/589 of 1v5fA
- binding flavin-adenine dinucleotide: G212 (= G228), I213 (≠ A229), G214 (= G230), T236 (≠ A252), G237 (≠ L253), K238 (≠ L254), T254 (≠ I270), Y255 (≠ G271), R256 (≠ L272), V257 (≠ L273), G276 (= G292), S277 (= S293), N278 (≠ G294), F279 (= F295), P280 (= P296), F281 (≠ Y297), D298 (= D313), I299 (≠ L314), M303 (= M318), D317 (= D332), A318 (≠ S333), P409 (≠ D425)
- binding magnesium ion: D439 (= D455), N466 (= N488)
- binding thiamine diphosphate: N388 (≠ S404), S389 (≠ C405), M414 (= M430), G438 (= G454), G440 (= G456), N466 (= N488), Y469 (≠ V494), A470 (≠ T495), F471 (≠ W496), I472 (≠ E497)
2djiA Crystal structure of pyruvate oxidase from aerococcus viridans containing fad (see paper)
30% identity, 95% coverage: 4:583/610 of query aligns to 5:561/590 of 2djiA
- active site: I25 (≠ Y24), S27 (≠ N30), G28 (= G31), T29 (≠ V32), L30 (≠ F33), E52 (= E63), S75 (≠ T86), F114 (≠ Q125), Q115 (= Q126), G163 (≠ N175), R257 (≠ L272), E284 (= E299), V387 (≠ S402), A413 (= A428), M415 (= M430), D440 (= D455), N467 (= N488), E469 (≠ Q493), Y470 (≠ V494), F472 (≠ W496), I473 (≠ E497), K476 (≠ A500), Q539 (≠ P560)
- binding flavin-adenine dinucleotide: G213 (= G228), I214 (≠ A229), G215 (= G230), T237 (≠ A252), G238 (≠ L253), K239 (≠ L254), T255 (≠ I270), Y256 (≠ G271), R257 (≠ L272), V258 (≠ L273), G277 (= G292), S278 (= S293), N279 (≠ G294), F280 (= F295), P281 (= P296), F282 (≠ Y297), D299 (= D313), I300 (≠ L314), M304 (= M318), D318 (= D332), A319 (≠ S333), P410 (≠ D425)
1powA The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from lactobacillus plantarum (see paper)
28% identity, 90% coverage: 6:555/610 of query aligns to 6:533/585 of 1powA
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E63), S74 (≠ T86), F113 (≠ Q125), Q114 (= Q126), E115 (= E127), V162 (≠ N175), R256 (≠ L272), E283 (= E299), V386 (≠ S402), A412 (= A428), M414 (= M430), D439 (= D455), N466 (= N488), Q468 (≠ D490), Y469 (≠ L491), F471 (≠ Q493), I472 (≠ V494), E475 (= E497)
- binding flavin-adenine dinucleotide: H93 (= H105), G212 (= G228), I213 (≠ A229), G214 (= G230), T236 (≠ A252), Y237 (≠ L253), A254 (≠ I270), V257 (≠ L273), G276 (= G292), N277 (≠ S293), N278 (≠ G294), Y279 (≠ F295), P280 (= P296), F281 (≠ Y297), D298 (= D313), I299 (≠ L314), K303 (≠ M318), D317 (= D332), A318 (≠ S333), N409 (≠ D425)
- binding magnesium ion: D439 (= D455), N466 (= N488), Q468 (≠ D490)
- binding thiamine diphosphate: D388 (≠ S404), M414 (= M430), G440 (= G456), N466 (= N488), Q468 (≠ D490), Y469 (≠ L491), G470 (≠ N492), F471 (≠ Q493), I472 (≠ V494)
Sites not aligning to the query:
4feeA High-resolution structure of pyruvate oxidase in complex with reaction intermediate 2-hydroxyethyl-thiamin diphosphate carbanion-enamine, crystal b (see paper)
28% identity, 90% coverage: 6:555/610 of query aligns to 6:533/586 of 4feeA
- binding flavin-adenine dinucleotide: H93 (= H105), G212 (= G228), I213 (≠ A229), G214 (= G230), T236 (≠ A252), Y237 (≠ L253), P238 (≠ L254), A254 (≠ I270), N255 (≠ G271), V257 (≠ L273), G276 (= G292), N277 (≠ S293), N278 (≠ G294), P280 (= P296), F281 (≠ Y297), D298 (= D313), I299 (≠ L314), K303 (≠ M318), D317 (= D332), A318 (≠ S333), N390 (≠ A406), N409 (≠ D425)
- binding magnesium ion: D439 (= D455), N466 (= N488), Q468 (≠ D490)
- binding pyruvic acid: N255 (≠ G271), R256 (≠ L272)
- 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: V386 (≠ S402), D388 (≠ S404), A412 (= A428), M414 (= M430), G438 (= G454), G440 (= G456), N466 (= N488), Q468 (≠ D490), Y469 (≠ L491), G470 (≠ N492), F471 (≠ Q493), I472 (≠ V494)
Sites not aligning to the query:
2ezuA Pyruvate oxidase variant f479w in complex with reaction intermediate 2-acetyl-thiamin diphosphate (see paper)
28% identity, 90% coverage: 6:555/610 of query aligns to 6:533/585 of 2ezuA
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E63), S74 (≠ T86), F113 (≠ Q125), Q114 (= Q126), E115 (= E127), V162 (≠ N175), R256 (≠ L272), E283 (= E299), V386 (≠ S402), A412 (= A428), M414 (= M430), D439 (= D455), N466 (= N488), Q468 (≠ D490), Y469 (≠ L491), W471 (≠ Q493), I472 (≠ V494), E475 (= E497)
- binding flavin-adenine dinucleotide: H93 (= H105), G212 (= G228), I213 (≠ A229), G214 (= G230), T236 (≠ A252), Y237 (≠ L253), P238 (≠ L254), A254 (≠ I270), N255 (≠ G271), R256 (≠ L272), V257 (≠ L273), G276 (= G292), N277 (≠ S293), N278 (≠ G294), P280 (= P296), F281 (≠ Y297), D298 (= D313), I299 (≠ L314), K303 (≠ M318), D317 (= D332), A318 (≠ S333), N409 (≠ D425)
- binding 2-acetyl-thiamine diphosphate: V386 (≠ S402), D388 (≠ S404), M414 (= M430), G438 (= G454), G440 (= G456), N466 (= N488), Q468 (≠ D490), Y469 (≠ L491), G470 (≠ N492), W471 (≠ Q493), I472 (≠ V494)
- binding magnesium ion: D439 (= D455), N466 (= N488), Q468 (≠ D490)
Sites not aligning to the query:
2ez9A Pyruvate oxidase variant f479w in complex with reaction intermediate analogue 2-phosphonolactyl-thiamin diphosphate (see paper)
28% identity, 90% coverage: 6:555/610 of query aligns to 6:533/585 of 2ez9A
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E63), S74 (≠ T86), F113 (≠ Q125), Q114 (= Q126), E115 (= E127), V162 (≠ N175), R256 (≠ L272), E283 (= E299), V386 (≠ S402), A412 (= A428), M414 (= M430), D439 (= D455), N466 (= N488), Q468 (≠ D490), Y469 (≠ L491), W471 (≠ Q493), I472 (≠ V494), E475 (= E497)
- binding flavin-adenine dinucleotide: H93 (= H105), G212 (= G228), I213 (≠ A229), G214 (= G230), T236 (≠ A252), Y237 (≠ L253), P238 (≠ L254), A254 (≠ I270), N255 (≠ G271), R256 (≠ L272), V257 (≠ L273), G276 (= G292), N277 (≠ S293), N278 (≠ G294), P280 (= P296), F281 (≠ Y297), D298 (= D313), I299 (≠ L314), K303 (≠ M318), D317 (= D332), A318 (≠ S333), N409 (≠ D425)
- binding magnesium ion: D439 (= D455), N466 (= N488), Q468 (≠ D490)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(1s)-1-hydroxy-1-[(r)-hydroxy(methoxy)phosphoryl]ethyl}-5-(2-{[(s)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: V386 (≠ S402), D388 (≠ S404), M414 (= M430), G438 (= G454), G440 (= G456), N466 (= N488), Q468 (≠ D490), Y469 (≠ L491), G470 (≠ N492), W471 (≠ Q493), I472 (≠ V494), E475 (= E497)
Sites not aligning to the query:
2ez8A Pyruvate oxidase variant f479w in complex with reaction intermediate 2-lactyl-thiamin diphosphate (see paper)
28% identity, 90% coverage: 6:555/610 of query aligns to 6:533/585 of 2ez8A
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E63), S74 (≠ T86), F113 (≠ Q125), Q114 (= Q126), E115 (= E127), V162 (≠ N175), R256 (≠ L272), E283 (= E299), V386 (≠ S402), A412 (= A428), M414 (= M430), D439 (= D455), N466 (= N488), Q468 (≠ D490), Y469 (≠ L491), W471 (≠ Q493), I472 (≠ V494), E475 (= E497)
- binding flavin-adenine dinucleotide: H93 (= H105), G212 (= G228), I213 (≠ A229), G214 (= G230), T236 (≠ A252), Y237 (≠ L253), P238 (≠ L254), A254 (≠ I270), N255 (≠ G271), R256 (≠ L272), V257 (≠ L273), G276 (= G292), N277 (≠ S293), N278 (≠ G294), P280 (= P296), F281 (≠ Y297), D298 (= D313), I299 (≠ L314), K303 (≠ M318), D317 (= D332), A318 (≠ S333), N390 (≠ A406), N409 (≠ D425)
- binding magnesium ion: D439 (= D455), N466 (= N488), Q468 (≠ D490)
- 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: D388 (≠ S404), M414 (= M430), G438 (= G454), G440 (= G456), N466 (= N488), Q468 (≠ D490), Y469 (≠ L491), G470 (≠ N492), W471 (≠ Q493), I472 (≠ V494)
Sites not aligning to the query:
2ez4B Pyruvate oxidase variant f479w (see paper)
28% identity, 90% coverage: 6:555/610 of query aligns to 6:533/585 of 2ez4B
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E63), S74 (≠ T86), F113 (≠ Q125), Q114 (= Q126), E115 (= E127), V162 (≠ N175), R256 (≠ L272), E283 (= E299), V386 (≠ S402), A412 (= A428), M414 (= M430), D439 (= D455), N466 (= N488), Q468 (≠ D490), Y469 (≠ L491), W471 (≠ Q493), I472 (≠ V494), E475 (= E497)
- binding flavin-adenine dinucleotide: H93 (= H105), G212 (= G228), I213 (≠ A229), G214 (= G230), T236 (≠ A252), Y237 (≠ L253), P238 (≠ L254), A254 (≠ I270), N255 (≠ G271), R256 (≠ L272), V257 (≠ L273), G276 (= G292), N277 (≠ S293), N278 (≠ G294), P280 (= P296), F281 (≠ Y297), D298 (= D313), I299 (≠ L314), K303 (≠ M318), D317 (= D332), A318 (≠ S333), N409 (≠ D425)
- binding magnesium ion: D439 (= D455), N466 (= N488), Q468 (≠ D490)
- binding phosphate ion: W471 (≠ Q493), E475 (= E497)
- binding thiamine diphosphate: D388 (≠ S404), A412 (= A428), M414 (= M430), G438 (= G454), D439 (= D455), G440 (= G456), G441 (≠ A457), N466 (= N488), Q468 (≠ D490), Y469 (≠ L491), G470 (≠ N492), W471 (≠ Q493), I472 (≠ V494)
Sites not aligning to the query:
1y9dD Pyruvate oxidase variant v265a from lactobacillus plantarum (see paper)
27% identity, 90% coverage: 6:555/610 of query aligns to 6:508/560 of 1y9dD
- active site: I24 (≠ Y24), G26 (= G26), G27 (≠ D27), S28 (≠ G28), I29 (= I29), E51 (= E63), S74 (≠ T86), E108 (= E127), V155 (≠ N175), R241 (≠ L272), V361 (≠ S402), A387 (= A428), M389 (= M430), D414 (= D455), N441 (= N488), Q443 (≠ D490), Y444 (≠ L491), F446 (≠ Q493), I447 (≠ V494), E450 (= E497)
- binding flavin-adenine dinucleotide: I198 (≠ A229), G199 (= G230), T221 (≠ A252), P223 (≠ L254), G261 (= G292), N262 (≠ S293), N263 (≠ G294), D273 (= D313), I274 (≠ L314), K278 (≠ M318), D292 (= D332), A293 (≠ S333)
- binding magnesium ion: D414 (= D455), N441 (= N488), Q443 (≠ D490)
- binding thiamine diphosphate: E51 (= E63), S74 (≠ T86), P77 (= P89), H81 (= H93), D363 (≠ S404), M389 (= M430), G413 (= G454), G415 (= G456), N441 (= N488), Q443 (≠ D490), Y444 (≠ L491), G445 (≠ N492), F446 (≠ Q493), I447 (≠ V494)
Sites not aligning to the query:
1ozfA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors (see paper)
28% identity, 92% coverage: 7:565/610 of query aligns to 9:539/545 of 1ozfA
- active site: I26 (≠ Y24), G28 (= G26), A29 (≠ D27), K30 (≠ G28), I31 (= I29), E51 (= E63), T74 (= T86), H113 (≠ Q125), Q114 (= Q126), S115 (≠ E127), Q163 (≠ N175), L253 (= L272), E280 (≠ S298), M385 (≠ S402), Q411 (≠ A428), M413 (= M430), D438 (= D455), D465 (≠ N488), G467 (≠ D490), Y468 (≠ L491), M470 (≠ Q493), V471 (= V494), Q474 (≠ E502), Y534 (≠ P560)
- binding magnesium ion: D438 (= D455), D465 (≠ N488), G467 (≠ D490)
- binding phosphate ion: G249 (= G268), R250 (≠ A269), Q257 (≠ K276), R343 (≠ T360), R394 (= R411), L396 (= L413), Y397 (≠ K414)
- binding thiamine diphosphate: G386 (= G403), S387 (= S404), F388 (≠ C405), Q411 (≠ A428), M413 (= M430), G437 (= G454), D438 (= D455), G439 (= G456), D465 (≠ N488), G467 (≠ D490), Y468 (≠ L491), N469 (= N492), M470 (≠ Q493), V471 (= V494), Y534 (≠ P560)
1ozgA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate (see paper)
28% identity, 92% coverage: 7:565/610 of query aligns to 10:543/549 of 1ozgA
- active site: I27 (≠ Y24), G29 (= G26), A30 (≠ D27), K31 (≠ G28), I32 (= I29), E52 (= E63), T75 (= T86), H114 (≠ Q125), Q115 (= Q126), S116 (≠ E127), Q164 (≠ N175), L257 (= L272), E284 (≠ S298), M389 (≠ S402), Q415 (≠ A428), M417 (= M430), D442 (= D455), D469 (≠ N488), G471 (≠ D490), Y472 (≠ L491), M474 (≠ Q493), V475 (= V494), Q478 (≠ E502), Y538 (≠ P560)
- binding 2-hydroxyethyl dihydrothiachrome diphosphate: M389 (≠ S402), G390 (= G403), S391 (= S404), F392 (≠ C405), Q415 (≠ A428), M417 (= M430), G441 (= G454), D442 (= D455), G443 (= G456), D469 (≠ N488), G471 (≠ D490), Y472 (≠ L491), N473 (= N492), M474 (≠ Q493), V475 (= V494), Y538 (≠ P560)
- binding magnesium ion: D442 (= D455), D469 (≠ N488), G471 (≠ D490)
- binding phosphate ion: G253 (= G268), R254 (≠ A269), Q261 (≠ K276), R347 (≠ T360), R398 (= R411), Y401 (≠ K414)
5d6rB Acetolactate synthase from klebsiella pneumoniae in complex with mechanism-based inhibitor
28% identity, 92% coverage: 7:565/610 of query aligns to 9:540/548 of 5d6rB
- active site: I26 (≠ Y24), G28 (= G26), A29 (≠ D27), K30 (≠ G28), I31 (= I29), E51 (= E63), T74 (= T86), H113 (≠ Q125), Q114 (= Q126), S115 (≠ E127), Q163 (≠ N175), L254 (= L272), E281 (≠ S298), M386 (≠ S402), Q412 (≠ A428), M414 (= M430), D439 (= D455), D466 (≠ N488), G468 (≠ D490), Y469 (≠ L491), M471 (≠ Q493), V472 (= V494), Q475 (≠ E502), Y535 (≠ P560)
- 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 (≠ S402), G387 (= G403), S388 (= S404), Q412 (≠ A428), M414 (= M430), D439 (= D455), G440 (= G456), G468 (≠ D490), Y469 (≠ L491), N470 (= N492), M471 (≠ Q493), Y535 (≠ P560)
- binding magnesium ion: R63 (≠ K75), Q212 (≠ A231), D439 (= D455), D466 (≠ N488), G468 (≠ D490)
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)
28% identity, 95% coverage: 7:585/610 of query aligns to 95:659/664 of P09114
- P191 (≠ A116) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
- W568 (= W496) 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)
28% identity, 95% coverage: 7:585/610 of query aligns to 98:662/667 of P09342
- C161 (= C83) modified: Disulfide link with 307
- P194 (≠ A116) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ A231) modified: Disulfide link with 161
5dx6B Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
28% identity, 92% coverage: 7:565/610 of query aligns to 21:546/557 of 5dx6B
- active site: I38 (≠ Y24), G40 (= G26), A41 (≠ D27), K42 (≠ G28), I43 (= I29), E63 (= E63), T86 (= T86), H125 (≠ Q125), Q126 (= Q126), S127 (≠ E127), Q175 (≠ N175), L268 (= L272), E295 (≠ S298), M392 (≠ S402), Q418 (≠ A428), M420 (= M430), D445 (= D455), D472 (≠ N488), G474 (≠ D490), Y475 (≠ L491), M477 (≠ Q493), V478 (= V494), Q481 (≠ E502), Y541 (≠ P560)
- binding 3-fluoro-2-oxopropanoic acid: G264 (= G268), R265 (≠ A269), Q272 (≠ K276), A400 (= A410), R401 (= R411), Y404 (≠ K414)
- binding magnesium ion: S135 (≠ K135), T138 (≠ A138), D445 (= D455), D472 (≠ N488), G474 (≠ D490)
- binding thiamine diphosphate: G393 (= G403), S394 (= S404), F395 (≠ C405), Q418 (≠ A428), M420 (= M430), G444 (= G454), D445 (= D455), G446 (= G456), D472 (≠ N488), G474 (≠ D490), Y475 (≠ L491), N476 (= N492), M477 (≠ Q493), V478 (= V494), Y541 (≠ P560)
5dx6A Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
28% identity, 92% coverage: 7:565/610 of query aligns to 10:535/541 of 5dx6A
- active site: I27 (≠ Y24), G29 (= G26), A30 (≠ D27), K31 (≠ G28), I32 (= I29), E52 (= E63), T75 (= T86), Q159 (≠ N175), L249 (= L272), E276 (≠ S298), M381 (≠ S402), Q407 (≠ A428), M409 (= M430), D434 (= D455), D461 (≠ N488), G463 (≠ D490), Y464 (≠ L491), M466 (≠ Q493), V467 (= V494), Q470 (≠ E502), Y530 (≠ P560)
- 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 (≠ S402), G382 (= G403), S383 (= S404), F384 (≠ C405), Q407 (≠ A428), M409 (= M430), G433 (= G454), D434 (= D455), G435 (= G456), D461 (≠ N488), G463 (≠ D490), Y464 (≠ L491), N465 (= N492), Y530 (≠ P560)
- binding magnesium ion: S119 (≠ K135), T122 (≠ A138), D434 (= D455), D461 (≠ N488), G463 (≠ D490)
6lpiB Crystal structure of ahas holo-enzyme (see paper)
26% identity, 81% coverage: 4:498/610 of query aligns to 7:465/539 of 6lpiB
- active site: I27 (≠ Y24), G29 (= G26), G30 (≠ D27), S31 (≠ G28), I32 (= I29), E53 (= E63), C76 (≠ T86), F115 (≠ Q125), Q116 (= Q126), E117 (= E127), K165 (≠ N175), M256 (≠ L272), A283 (vs. gap), V375 (≠ S402), G401 (≠ A428), M403 (= M430), D428 (= D455), N455 (= N488), A457 (≠ D490), L458 (= L491), L460 (≠ Q493), V461 (= V494), Q464 (≠ E497)
- binding flavin-adenine dinucleotide: R155 (= R166), G212 (= G228), G213 (≠ A229), G214 (= G230), T236 (≠ A252), L237 (= L253), M238 (≠ L254), L254 (≠ I270), M256 (≠ L272), H257 (≠ L273), G276 (= G292), A277 (≠ S293), R278 (≠ G294), D280 (vs. gap), R282 (vs. gap), A283 (vs. gap), D300 (= D313), I301 (≠ L314), D319 (= D332), V320 (≠ S333), M380 (≠ N407), G398 (≠ D425)
- binding magnesium ion: D428 (= D455), N455 (= N488)
- binding thiamine diphosphate: E53 (= E63), C76 (≠ T86), P79 (= P89), G376 (= G403), Q377 (≠ S404), H378 (≠ C405), G401 (≠ A428), M403 (= M430), G427 (= G454), D428 (= D455), G429 (= G456), S430 (≠ A457), M433 (= M460), N455 (= N488), A457 (≠ D490), L458 (= L491), G459 (≠ N492), L460 (≠ Q493), V461 (= V494)
Query Sequence
>BPHYT_RS31615 FitnessBrowser__BFirm:BPHYT_RS31615
MAQTVGDFIIGRLHAWGVRRIYGYPGDGINGVFGALNRAQSEARNSKSGNPTQPIEFVQV
RHEEMAAFMASAHAKFTGELGVCIATSGPGASHLITGLYDARMDHMPVLAIAGQQARAAL
GGHYQQELDLASMFKDVAGAFVEQASVPAQVRHLVDRAVRTALAERKVTALILPNDLQDL
RYEAPDRKHGTLHSGVGYRAPRLVPYPDDLQQAAEVLNAGKKVAILVGAGALHATDEVIA
IAEKLGAGVAKALLGKAALPDDLPWVTGAIGLLGTKPSYDLMMECDTLLMIGSGFPYSEF
LPKEGAARGVQIDLKADMLSLRYPMEVNLVGDSVETLRALLPLLEDKKDRAWRGKIEGWT
KDWWKTLDKRAHEAGKDAVNPQRTVWELSKRIPADSIVTSDSGSCANWYARDLKVQRGMM
CSLSDGLASMGAAVPYAIAAKFAFPERPVIALVGDGAMQMNNMAELITVSKYWKDWANPR
WICMVLNNSDLNQVTWEQRAVEGDPKFEASQDIPSVPYHKFAELIGLKGIYVDNDEQMGA
AWDEALAADRPVVIEVKSDPNIAPLPPHITLAQAKAFASTLMKGDPNEGNVIVETAKQVL
GAVLPGHHDK
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