SitesBLAST
Comparing WP_020173663.1 NCBI__GCF_000385335.1:WP_020173663.1 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)
P07003 Pyruvate dehydrogenase [ubiquinone]; Pyruvate oxidase; POX; Pyruvate:ubiquinone-8 oxidoreductase; EC 1.2.5.1 from Escherichia coli (strain K12) (see 4 papers)
62% identity, 100% coverage: 2:576/576 of query aligns to 3:572/572 of P07003
- E50 (= E49) binding thiamine diphosphate
- 183:334 (vs. 184:336, 58% identical) FAD-binding domain
- S210 (= S211) binding FAD
- LR 234:235 (≠ LK 235:236) binding FAD
- TGLI 251:254 (= TGLI 252:255) binding FAD
- TQFPY 274:278 (≠ TDFPY 275:279) binding FAD
- D292 (= D294) binding FAD
- S297 (≠ Q299) binding FAD
- DI 311:312 (≠ EV 313:314) binding FAD
- 335:530 (vs. 337:534, 62% identical) PP-binding domain
- T382 (≠ L386) binding thiamine diphosphate
- FN 403:404 (≠ FW 407:408) binding FAD
- GSM 406:408 (= GSM 410:412) binding thiamine diphosphate
- D433 (= D437) binding Mg(2+)
- DGG 433:435 (= DGG 437:439) binding thiamine diphosphate
- N460 (= N464) binding Mg(2+)
- 460:466 (vs. 464:470, 71% identical) binding thiamine diphosphate
- V462 (≠ T466) binding Mg(2+)
- F465 (= F469) Moves into active site upon enzyme activation, plays a role in electron transfer
- 531:572 (vs. 535:576, 64% identical) Membrane-binding domain
- A533 (= A537) mutation to T: In poxB11; poor activity in vivo, no longer activated by lipids.
- YM 549:550 (≠ YT 553:554) In vitro cleavage to yield alpha-peptide
- 549:572 (vs. 553:576, 58% identical) mutation Missing: In poxB6. Inactive in vivo, does not complement inactive mutants. Active in vitro, no longer activated by nor binds to, detergents.
- A553 (= A557) mutation to V: In poxB14; poor activity in vivo, no longer activated by lipids.
- D560 (= D564) mutation to P: In poxB15; normal activity.
- E564 (= E568) mutation to P: In poxB16; loss of activity, weakly activated by cleavage.
- 564:572 (vs. 568:576, 67% identical) mutation Missing: In poxB7 Inactive in vivo, reduced activity in vitro.
- WLR 570:572 (≠ LWR 574:576) mutation Missing: In poxB8; reduced activity in vitro, not activated by lipids.
- R572 (= R576) mutation to G: In poxB10; reduced activity in vivo and in vitro; may interact less with membranes.
Sites not aligning to the query:
3ey9A Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from escherichia coli (see paper)
62% identity, 100% coverage: 2:576/576 of query aligns to 2:571/571 of 3ey9A
- active site: V23 (≠ I23), G25 (= G25), D26 (= D26), S27 (= S27), L28 (= L28), E49 (= E49), S72 (= S72), F111 (= F111), Q112 (= Q112), G160 (= G160), L252 (= L254), A279 (≠ Q281), V379 (= V384), G405 (= G410), M407 (= M412), D432 (= D437), N459 (= N464), V461 (≠ T466), L462 (= L467), F464 (= F469), V465 (= V470), E468 (= E473), K528 (≠ R533)
- binding flavin-adenine dinucleotide: G208 (= G210), S209 (= S211), G210 (= G212), A232 (= A234), L233 (= L235), R234 (≠ K236), T250 (= T252), G251 (= G253), I253 (= I255), G272 (= G274), T273 (= T275), Q274 (≠ D276), F275 (= F277), Y277 (= Y279), D291 (= D294), I292 (= I295), S296 (≠ Q299), G309 (= G312), D310 (≠ E313), I311 (≠ V314), T383 (= T388), F402 (= F407), N403 (≠ W408), Y548 (= Y553)
- binding magnesium ion: D432 (= D437), N459 (= N464)
- binding thiamine diphosphate: T24 (≠ V24), E49 (= E49), S72 (= S72), G76 (= G76), H79 (= H79), G380 (= G385), T381 (≠ L386), P382 (= P387), M407 (= M412), G431 (= G436), D432 (= D437), G433 (= G438), G434 (= G439), N459 (= N464), V461 (≠ T466), L462 (= L467), G463 (= G468)
9ev3A Corynebacterium glutamicum pyruvate:quinone oxidoreductase (pqo) purified from bacteria grown in acetate minimal medium (see paper)
47% identity, 99% coverage: 3:574/576 of query aligns to 3:572/577 of 9ev3A
- binding flavin-adenine dinucleotide: G208 (= G210), G210 (= G212), A232 (= A234), L233 (= L235), G234 (≠ K236), G251 (= G253), L253 (≠ I255), G272 (= G274), T273 (= T275), D274 (= D276), F275 (= F277), P276 (= P278), Y277 (= Y279), D290 (= D294), I291 (= I295), H295 (≠ Q299), D309 (≠ E313), V310 (= V314), N385 (≠ T388), F405 (= F407), R406 (≠ W408)
- binding magnesium ion: D435 (= D437), N462 (= N464), S464 (≠ T466)
- binding thiamine diphosphate: G382 (= G385), M383 (≠ L386), M410 (= M412), G434 (= G436), D435 (= D437), G436 (= G438), G437 (= G439), M440 (= M442), S464 (≠ T466), L465 (= L467), G466 (= G468), M467 (≠ F469), V468 (= V470)
9ev4A Pyruvate:quinone oxidoreductase (pqo) from corynebacterium glutamicum cs176 (see paper)
45% identity, 99% coverage: 2:574/576 of query aligns to 1:549/553 of 9ev4A
- binding flavin-adenine dinucleotide: G207 (= G210), A208 (≠ S211), G209 (= G212), A231 (= A234), L232 (= L235), G233 (≠ K236), G250 (= G253), L252 (≠ I255), G271 (= G274), T272 (= T275), D273 (= D276), F274 (= F277), Y276 (= Y279), D289 (= D294), I290 (= I295), H294 (≠ Q299), D308 (≠ E313), V309 (= V314), N384 (≠ T388), F404 (= F407), R405 (≠ W408)
1v5gA Crystal structure of the reaction intermediate between pyruvate oxidase containing fad and tpp, and substrate pyruvate (see paper)
31% identity, 95% coverage: 10:557/576 of query aligns to 11:561/589 of 1v5gA
- binding flavin-adenine dinucleotide: G212 (= G210), I213 (≠ S211), G214 (= G212), T236 (≠ A234), G237 (≠ L235), K238 (= K236), T254 (= T252), Y255 (≠ G253), R256 (≠ L254), V257 (≠ I255), G276 (= G274), S277 (≠ T275), N278 (≠ D276), F279 (= F277), F281 (≠ Y279), D298 (= D294), I299 (= I295), M303 (≠ Q299), D317 (≠ E313), A318 (≠ V314), P409 (≠ F407)
- binding 2-acetyl-thiamine diphosphate: V386 (= V384), N388 (≠ L386), M414 (= M412), G438 (= G436), G440 (= G438), A441 (≠ G439), N466 (= N464), E468 (≠ T466), Y469 (≠ L467), A470 (≠ G468), F471 (= F469), I472 (≠ V470)
- binding magnesium ion: D439 (= D437), N466 (= N464), E468 (≠ T466)
1v5fA Crystal structure of pyruvate oxidase complexed with fad and tpp, from aerococcus viridans (see paper)
31% identity, 95% coverage: 10:557/576 of query aligns to 11:561/589 of 1v5fA
- binding flavin-adenine dinucleotide: G212 (= G210), I213 (≠ S211), G214 (= G212), T236 (≠ A234), G237 (≠ L235), K238 (= K236), T254 (= T252), Y255 (≠ G253), R256 (≠ L254), V257 (≠ I255), G276 (= G274), S277 (≠ T275), N278 (≠ D276), F279 (= F277), P280 (= P278), F281 (≠ Y279), D298 (= D294), I299 (= I295), M303 (≠ Q299), D317 (≠ E313), A318 (≠ V314), P409 (≠ F407)
- binding magnesium ion: D439 (= D437), N466 (= N464)
- binding thiamine diphosphate: N388 (≠ L386), S389 (≠ P387), M414 (= M412), G438 (= G436), G440 (= G438), N466 (= N464), Y469 (≠ L467), A470 (≠ G468), F471 (= F469), I472 (≠ V470)
2djiA Crystal structure of pyruvate oxidase from aerococcus viridans containing fad (see paper)
31% identity, 95% coverage: 10:557/576 of query aligns to 12:562/590 of 2djiA
- active site: I25 (= I23), S27 (≠ G25), G28 (≠ D26), T29 (≠ S27), L30 (= L28), E52 (= E49), S75 (= S72), F114 (= F111), Q115 (= Q112), G163 (= G160), R257 (≠ L254), E284 (≠ Q281), V387 (= V384), A413 (≠ G410), M415 (= M412), D440 (= D437), N467 (= N464), E469 (≠ T466), Y470 (≠ L467), F472 (= F469), I473 (≠ V470), K476 (≠ E473), Q539 (= Q534)
- binding flavin-adenine dinucleotide: G213 (= G210), I214 (≠ S211), G215 (= G212), T237 (≠ A234), G238 (≠ L235), K239 (= K236), T255 (= T252), Y256 (≠ G253), R257 (≠ L254), V258 (≠ I255), G277 (= G274), S278 (≠ T275), N279 (≠ D276), F280 (= F277), P281 (= P278), F282 (≠ Y279), D299 (= D294), I300 (= I295), M304 (≠ Q299), D318 (≠ E313), A319 (≠ V314), P410 (≠ F407)
4feeA High-resolution structure of pyruvate oxidase in complex with reaction intermediate 2-hydroxyethyl-thiamin diphosphate carbanion-enamine, crystal b (see paper)
32% identity, 91% coverage: 10:531/576 of query aligns to 11:536/586 of 4feeA
- binding flavin-adenine dinucleotide: H93 (≠ R91), G212 (= G210), I213 (≠ S211), G214 (= G212), T236 (≠ A234), Y237 (≠ L235), P238 (≠ K236), A254 (≠ T252), N255 (≠ G253), V257 (≠ I255), G276 (= G274), N277 (≠ T275), N278 (≠ D276), P280 (= P278), F281 (≠ Y279), D298 (= D294), I299 (= I295), K303 (≠ Q299), D317 (≠ E313), A318 (≠ V314), N390 (≠ T388), N409 (≠ F407)
- binding magnesium ion: D439 (= D437), N466 (= N464), Q468 (≠ T466)
- binding pyruvic acid: N255 (≠ G253), R256 (≠ L254)
- 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 (= V384), D388 (≠ L386), A412 (≠ G410), M414 (= M412), G438 (= G436), G440 (= G438), N466 (= N464), Q468 (≠ T466), Y469 (≠ L467), G470 (= G468), F471 (= F469), I472 (≠ V470)
Sites not aligning to the query:
1powA The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from lactobacillus plantarum (see paper)
32% identity, 91% coverage: 10:531/576 of query aligns to 11:536/585 of 1powA
- active site: I24 (= I23), G26 (= G25), G27 (≠ D26), S28 (= S27), I29 (≠ L28), E51 (= E49), S74 (= S72), F113 (= F111), Q114 (= Q112), E115 (= E113), V162 (≠ G160), R256 (≠ L254), E283 (≠ Q281), V386 (= V384), A412 (≠ G410), M414 (= M412), D439 (= D437), N466 (= N464), Q468 (≠ T466), Y469 (≠ L467), F471 (= F469), I472 (≠ V470), E475 (= E473)
- binding flavin-adenine dinucleotide: H93 (≠ R91), G212 (= G210), I213 (≠ S211), G214 (= G212), T236 (≠ A234), Y237 (≠ L235), A254 (≠ T252), V257 (≠ I255), G276 (= G274), N277 (≠ T275), N278 (≠ D276), Y279 (≠ F277), P280 (= P278), F281 (≠ Y279), D298 (= D294), I299 (= I295), K303 (≠ Q299), D317 (≠ E313), A318 (≠ V314), N409 (≠ F407)
- binding magnesium ion: D439 (= D437), N466 (= N464), Q468 (≠ T466)
- binding thiamine diphosphate: D388 (≠ L386), M414 (= M412), G440 (= G438), N466 (= N464), Q468 (≠ T466), Y469 (≠ L467), G470 (= G468), F471 (= F469), I472 (≠ V470)
Sites not aligning to the query:
2ezuA Pyruvate oxidase variant f479w in complex with reaction intermediate 2-acetyl-thiamin diphosphate (see paper)
32% identity, 91% coverage: 10:531/576 of query aligns to 11:536/585 of 2ezuA
- active site: I24 (= I23), G26 (= G25), G27 (≠ D26), S28 (= S27), I29 (≠ L28), E51 (= E49), S74 (= S72), F113 (= F111), Q114 (= Q112), E115 (= E113), V162 (≠ G160), R256 (≠ L254), E283 (≠ Q281), V386 (= V384), A412 (≠ G410), M414 (= M412), D439 (= D437), N466 (= N464), Q468 (≠ T466), Y469 (≠ L467), W471 (≠ F469), I472 (≠ V470), E475 (= E473)
- binding flavin-adenine dinucleotide: H93 (≠ R91), G212 (= G210), I213 (≠ S211), G214 (= G212), T236 (≠ A234), Y237 (≠ L235), P238 (≠ K236), A254 (≠ T252), N255 (≠ G253), R256 (≠ L254), V257 (≠ I255), G276 (= G274), N277 (≠ T275), N278 (≠ D276), P280 (= P278), F281 (≠ Y279), D298 (= D294), I299 (= I295), K303 (≠ Q299), D317 (≠ E313), A318 (≠ V314), N409 (≠ F407)
- binding 2-acetyl-thiamine diphosphate: V386 (= V384), D388 (≠ L386), M414 (= M412), G438 (= G436), G440 (= G438), N466 (= N464), Q468 (≠ T466), Y469 (≠ L467), G470 (= G468), W471 (≠ F469), I472 (≠ V470)
- binding magnesium ion: D439 (= D437), N466 (= N464), Q468 (≠ T466)
Sites not aligning to the query:
2ez9A Pyruvate oxidase variant f479w in complex with reaction intermediate analogue 2-phosphonolactyl-thiamin diphosphate (see paper)
32% identity, 91% coverage: 10:531/576 of query aligns to 11:536/585 of 2ez9A
- active site: I24 (= I23), G26 (= G25), G27 (≠ D26), S28 (= S27), I29 (≠ L28), E51 (= E49), S74 (= S72), F113 (= F111), Q114 (= Q112), E115 (= E113), V162 (≠ G160), R256 (≠ L254), E283 (≠ Q281), V386 (= V384), A412 (≠ G410), M414 (= M412), D439 (= D437), N466 (= N464), Q468 (≠ T466), Y469 (≠ L467), W471 (≠ F469), I472 (≠ V470), E475 (= E473)
- binding flavin-adenine dinucleotide: H93 (≠ R91), G212 (= G210), I213 (≠ S211), G214 (= G212), T236 (≠ A234), Y237 (≠ L235), P238 (≠ K236), A254 (≠ T252), N255 (≠ G253), R256 (≠ L254), V257 (≠ I255), G276 (= G274), N277 (≠ T275), N278 (≠ D276), P280 (= P278), F281 (≠ Y279), D298 (= D294), I299 (= I295), K303 (≠ Q299), D317 (≠ E313), A318 (≠ V314), N409 (≠ F407)
- binding magnesium ion: D439 (= D437), N466 (= N464), Q468 (≠ T466)
- 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 (= V384), D388 (≠ L386), M414 (= M412), G438 (= G436), G440 (= G438), N466 (= N464), Q468 (≠ T466), Y469 (≠ L467), G470 (= G468), W471 (≠ F469), I472 (≠ V470), E475 (= E473)
Sites not aligning to the query:
2ez8A Pyruvate oxidase variant f479w in complex with reaction intermediate 2-lactyl-thiamin diphosphate (see paper)
32% identity, 91% coverage: 10:531/576 of query aligns to 11:536/585 of 2ez8A
- active site: I24 (= I23), G26 (= G25), G27 (≠ D26), S28 (= S27), I29 (≠ L28), E51 (= E49), S74 (= S72), F113 (= F111), Q114 (= Q112), E115 (= E113), V162 (≠ G160), R256 (≠ L254), E283 (≠ Q281), V386 (= V384), A412 (≠ G410), M414 (= M412), D439 (= D437), N466 (= N464), Q468 (≠ T466), Y469 (≠ L467), W471 (≠ F469), I472 (≠ V470), E475 (= E473)
- binding flavin-adenine dinucleotide: H93 (≠ R91), G212 (= G210), I213 (≠ S211), G214 (= G212), T236 (≠ A234), Y237 (≠ L235), P238 (≠ K236), A254 (≠ T252), N255 (≠ G253), R256 (≠ L254), V257 (≠ I255), G276 (= G274), N277 (≠ T275), N278 (≠ D276), P280 (= P278), F281 (≠ Y279), D298 (= D294), I299 (= I295), K303 (≠ Q299), D317 (≠ E313), A318 (≠ V314), N390 (≠ T388), N409 (≠ F407)
- binding magnesium ion: D439 (= D437), N466 (= N464), Q468 (≠ T466)
- 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 (≠ L386), M414 (= M412), G438 (= G436), G440 (= G438), N466 (= N464), Q468 (≠ T466), Y469 (≠ L467), G470 (= G468), W471 (≠ F469), I472 (≠ V470)
Sites not aligning to the query:
2ez4B Pyruvate oxidase variant f479w (see paper)
32% identity, 91% coverage: 10:531/576 of query aligns to 11:536/585 of 2ez4B
- active site: I24 (= I23), G26 (= G25), G27 (≠ D26), S28 (= S27), I29 (≠ L28), E51 (= E49), S74 (= S72), F113 (= F111), Q114 (= Q112), E115 (= E113), V162 (≠ G160), R256 (≠ L254), E283 (≠ Q281), V386 (= V384), A412 (≠ G410), M414 (= M412), D439 (= D437), N466 (= N464), Q468 (≠ T466), Y469 (≠ L467), W471 (≠ F469), I472 (≠ V470), E475 (= E473)
- binding flavin-adenine dinucleotide: H93 (≠ R91), G212 (= G210), I213 (≠ S211), G214 (= G212), T236 (≠ A234), Y237 (≠ L235), P238 (≠ K236), A254 (≠ T252), N255 (≠ G253), R256 (≠ L254), V257 (≠ I255), G276 (= G274), N277 (≠ T275), N278 (≠ D276), P280 (= P278), F281 (≠ Y279), D298 (= D294), I299 (= I295), K303 (≠ Q299), D317 (≠ E313), A318 (≠ V314), N409 (≠ F407)
- binding magnesium ion: D439 (= D437), N466 (= N464), Q468 (≠ T466)
- binding phosphate ion: W471 (≠ F469), E475 (= E473)
- binding thiamine diphosphate: D388 (≠ L386), A412 (≠ G410), M414 (= M412), G438 (= G436), D439 (= D437), G440 (= G438), G441 (= G439), N466 (= N464), Q468 (≠ T466), Y469 (≠ L467), G470 (= G468), W471 (≠ F469), I472 (≠ V470)
Sites not aligning to the query:
1y9dD Pyruvate oxidase variant v265a from lactobacillus plantarum (see paper)
32% identity, 91% coverage: 10:531/576 of query aligns to 11:511/560 of 1y9dD
- active site: I24 (= I23), G26 (= G25), G27 (≠ D26), S28 (= S27), I29 (≠ L28), E51 (= E49), S74 (= S72), E108 (= E113), V155 (≠ G160), R241 (≠ L254), V361 (= V384), A387 (≠ G410), M389 (= M412), D414 (= D437), N441 (= N464), Q443 (≠ T466), Y444 (≠ L467), F446 (= F469), I447 (≠ V470), E450 (= E473)
- binding flavin-adenine dinucleotide: I198 (≠ S211), G199 (= G212), T221 (≠ A234), P223 (≠ K236), G261 (= G274), N262 (≠ T275), N263 (≠ D276), D273 (= D294), I274 (= I295), K278 (≠ Q299), D292 (≠ E313), A293 (≠ V314)
- binding magnesium ion: D414 (= D437), N441 (= N464), Q443 (≠ T466)
- binding thiamine diphosphate: E51 (= E49), S74 (= S72), P77 (= P75), H81 (= H79), D363 (≠ L386), M389 (= M412), G413 (= G436), G415 (= G438), N441 (= N464), Q443 (≠ T466), Y444 (≠ L467), G445 (= G468), F446 (= F469), I447 (≠ V470)
Sites not aligning to the query:
6deqA Crystal structure of candida albicans acetohydroxyacid synthase in complex with the herbicide penoxsulam (see paper)
28% identity, 92% coverage: 8:539/576 of query aligns to 20:567/601 of 6deqA
- active site: Y35 (≠ I23), G37 (= G25), G38 (≠ D26), A39 (≠ S27), I40 (≠ L28), E61 (= E49), T84 (≠ S72), F123 (= F111), Q124 (= Q112), E125 (= E113), K173 (≠ G160), K232 (vs. gap), M268 (≠ L254), V295 (vs. gap), V411 (= V384), L436 (≠ H409), G437 (= G410), M439 (= M412), D464 (= D437), N491 (= N464), E493 (≠ T466), Q494 (≠ L467), M496 (≠ F469), V497 (= V470), W500 (≠ K475), L522 (≠ M494), N527 (≠ G499), V528 (≠ I500)
- binding flavin-adenine dinucleotide: R163 (≠ K150), G221 (= G210), A222 (≠ S211), G223 (= G212), N226 (≠ G215), T248 (≠ A234), L249 (= L235), Q250 (≠ K236), L266 (≠ T252), G288 (= G274), A289 (≠ T275), R290 (≠ D276), D292 (≠ P278), R294 (= R280), V295 (vs. gap), E321 (≠ D294), I322 (= I295), D340 (≠ E313), V341 (= V314), M416 (≠ V389), G434 (≠ F407)
- binding magnesium ion: D464 (= D437), N491 (= N464), E493 (≠ T466)
- binding 2-(2,2-difluoroethoxy)-N-(5,8-dimethoxy[1,2,4]triazolo[1,5-c]pyrimidin-2-yl)-6-(trifluoromethyl)benzenesulfonamide: M268 (≠ L254), R294 (= R280), M496 (≠ F469), V497 (= V470), W500 (≠ K475)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V411 (= V384), G412 (= G385), Q413 (≠ L386), H414 (≠ P387), M439 (= M412), G463 (= G436), D464 (= D437), A465 (≠ G438), S466 (≠ G439), N491 (= N464), E493 (≠ T466), Q494 (≠ L467), G495 (= G468), M496 (≠ F469), V497 (= V470)
Sites not aligning to the query:
6desA Crystal structure of candida albicans acetohydroxyacid synthase in complex with the herbicide propoxycarbazone (see paper)
28% identity, 92% coverage: 8:539/576 of query aligns to 18:564/598 of 6desA
- active site: Y33 (≠ I23), G35 (= G25), G36 (≠ D26), A37 (≠ S27), I38 (≠ L28), E59 (= E49), T82 (≠ S72), F121 (= F111), Q122 (= Q112), E123 (= E113), K171 (≠ G160), K229 (vs. gap), M265 (≠ L254), V292 (vs. gap), V408 (= V384), L433 (≠ H409), G434 (= G410), M436 (= M412), D461 (= D437), N488 (= N464), E490 (≠ T466), Q491 (≠ L467), M493 (≠ F469), V494 (= V470), W497 (≠ K475), L519 (≠ M494), N524 (≠ G499), V525 (≠ I500)
- binding methyl 2-[(4-methyl-5-oxidanylidene-3-propoxy-1,2,4-triazol-1-yl)carbonylsulfamoyl]benzoate: M265 (≠ L254), D290 (≠ Y279), R291 (= R280), W497 (≠ K475)
- binding flavin-adenine dinucleotide: R161 (≠ K150), G218 (= G210), A219 (≠ S211), G220 (= G212), N223 (≠ G215), T245 (≠ A234), L246 (= L235), Q247 (≠ K236), L263 (≠ T252), G285 (= G274), A286 (≠ T275), R287 (≠ D276), D289 (≠ P278), R291 (= R280), V292 (vs. gap), E318 (≠ D294), I319 (= I295), N323 (≠ Q299), D337 (≠ E313), V338 (= V314), Q412 (≠ T388), M413 (≠ V389), G431 (≠ F407)
- binding magnesium ion: D461 (= D437), N488 (= N464), E490 (≠ T466)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: V408 (= V384), G409 (= G385), Q410 (≠ L386), H411 (≠ P387), G434 (= G410), M436 (= M412), G460 (= G436), D461 (= D437), A462 (≠ G438), S463 (≠ G439), N488 (= N464), E490 (≠ T466), Q491 (≠ L467), G492 (= G468), M493 (≠ F469), V494 (= V470)
6depA Crystal structure of candida albicans acetohydroxyacid synthase in complex with the herbicide sulfometuron methyl (see paper)
28% identity, 92% coverage: 8:539/576 of query aligns to 18:564/598 of 6depA
- active site: Y33 (≠ I23), G35 (= G25), G36 (≠ D26), A37 (≠ S27), I38 (≠ L28), E59 (= E49), T82 (≠ S72), F121 (= F111), Q122 (= Q112), E123 (= E113), K171 (≠ G160), K229 (vs. gap), M265 (≠ L254), V292 (vs. gap), V408 (= V384), L433 (≠ H409), G434 (= G410), M436 (= M412), D461 (= D437), N488 (= N464), E490 (≠ T466), Q491 (≠ L467), M493 (≠ F469), V494 (= V470), W497 (≠ K475), L519 (≠ M494), N524 (≠ G499), V525 (≠ I500)
- binding methyl 2-[({[(4,6-dimethylpyrimidin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: D290 (≠ Y279), R291 (= R280), M493 (≠ F469), W497 (≠ K475)
- binding flavin-adenine dinucleotide: R161 (≠ K150), G218 (= G210), A219 (≠ S211), G220 (= G212), N223 (≠ G215), T245 (≠ A234), L246 (= L235), Q247 (≠ K236), L263 (≠ T252), G264 (= G253), G285 (= G274), A286 (≠ T275), R287 (≠ D276), D289 (≠ P278), R291 (= R280), V292 (vs. gap), E318 (≠ D294), I319 (= I295), N323 (≠ Q299), D337 (≠ E313), V338 (= V314), M413 (≠ V389), G431 (≠ F407)
- binding magnesium ion: D461 (= D437), N488 (= N464), E490 (≠ T466)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V408 (= V384), G409 (= G385), Q410 (≠ L386), H411 (≠ P387), G434 (= G410), M436 (= M412), G460 (= G436), D461 (= D437), A462 (≠ G438), S463 (≠ G439), M466 (= M442), N488 (= N464), E490 (≠ T466), Q491 (≠ L467), G492 (= G468), M493 (≠ F469), V494 (= V470)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: V408 (= V384), G409 (= G385), Q410 (≠ L386), H411 (≠ P387), G434 (= G410), M436 (= M412), G460 (= G436), D461 (= D437), A462 (≠ G438), S463 (≠ G439), M466 (= M442), N488 (= N464), E490 (≠ T466), Q491 (≠ L467), G492 (= G468), M493 (≠ F469), V494 (= V470)
6derA Crystal structure of candida albicans acetohydroxyacid synthase in complex with the herbicide metosulam (see paper)
28% identity, 92% coverage: 8:539/576 of query aligns to 20:566/600 of 6derA
- active site: Y35 (≠ I23), G37 (= G25), G38 (≠ D26), A39 (≠ S27), I40 (≠ L28), E61 (= E49), T84 (≠ S72), F123 (= F111), Q124 (= Q112), E125 (= E113), K173 (≠ G160), K231 (vs. gap), M267 (≠ L254), V294 (vs. gap), V410 (= V384), L435 (≠ H409), G436 (= G410), M438 (= M412), D463 (= D437), N490 (= N464), E492 (≠ T466), Q493 (≠ L467), M495 (≠ F469), V496 (= V470), W499 (≠ K475), L521 (≠ M494), N526 (≠ G499), V527 (≠ I500)
- binding flavin-adenine dinucleotide: R163 (≠ K150), G220 (= G210), A221 (≠ S211), G222 (= G212), N225 (≠ G215), T247 (≠ A234), L248 (= L235), Q249 (≠ K236), L265 (≠ T252), H268 (≠ I255), G287 (= G274), A288 (≠ T275), R289 (≠ D276), D291 (≠ P278), R293 (= R280), V294 (vs. gap), E320 (≠ D294), I321 (= I295), N325 (≠ Q299), G338 (= G312), D339 (≠ E313), V340 (= V314), Q414 (≠ T388), M415 (≠ V389), G433 (≠ F407)
- binding Metosulam: R293 (= R280), M495 (≠ F469), W499 (≠ K475)
- binding magnesium ion: D463 (= D437), N490 (= N464), E492 (≠ T466)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V410 (= V384), G411 (= G385), Q412 (≠ L386), H413 (≠ P387), G436 (= G410), M438 (= M412), G462 (= G436), D463 (= D437), A464 (≠ G438), S465 (≠ G439), N490 (= N464), E492 (≠ T466), Q493 (≠ L467), G494 (= G468), M495 (≠ F469), V496 (= V470)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: V410 (= V384), G411 (= G385), Q412 (≠ L386), H413 (≠ P387), G436 (= G410), M438 (= M412), G462 (= G436), D463 (= D437), A464 (≠ G438), S465 (≠ G439), M468 (= M442), N490 (= N464), E492 (≠ T466), Q493 (≠ L467), G494 (= G468), V496 (= V470)
Sites not aligning to the query:
6deoA Crystal structure of candida albicans acetohydroxyacid synthase in complex with the herbicide iodomuron methyl (see paper)
28% identity, 92% coverage: 8:539/576 of query aligns to 16:559/593 of 6deoA
- active site: Y31 (≠ I23), G33 (= G25), G34 (≠ D26), A35 (≠ S27), I36 (≠ L28), E57 (= E49), T80 (≠ S72), F119 (= F111), Q120 (= Q112), E121 (= E113), K169 (≠ G160), K224 (vs. gap), M260 (≠ L254), V287 (vs. gap), V403 (= V384), L428 (≠ H409), G429 (= G410), M431 (= M412), D456 (= D437), N483 (= N464), E485 (≠ T466), Q486 (≠ L467), M488 (≠ F469), V489 (= V470), W492 (≠ K475), L514 (≠ M494), N519 (≠ G499), V520 (≠ I500)
- binding flavin-adenine dinucleotide: R159 (≠ K150), G213 (= G210), A214 (≠ S211), G215 (= G212), N218 (≠ G215), T240 (≠ A234), L241 (= L235), Q242 (≠ K236), L258 (≠ T252), G280 (= G274), A281 (≠ T275), R282 (≠ D276), D284 (≠ P278), R286 (= R280), V287 (vs. gap), E313 (≠ D294), I314 (= I295), N318 (≠ Q299), D332 (≠ E313), V333 (= V314), M408 (≠ V389), G426 (≠ F407)
- binding methyl 2-{[(4-iodo-6-methoxypyrimidin-2-yl)carbamoyl]sulfamoyl}benzoate: M260 (≠ L254), D285 (≠ Y279), R286 (= R280), M488 (≠ F469), W492 (≠ K475)
- binding magnesium ion: D456 (= D437), N483 (= N464), E485 (≠ T466)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V403 (= V384), G404 (= G385), Q405 (≠ L386), H406 (≠ P387), G429 (= G410), M431 (= M412), G455 (= G436), D456 (= D437), A457 (≠ G438), S458 (≠ G439), M461 (= M442), N483 (= N464), E485 (≠ T466), Q486 (≠ L467), G487 (= G468), M488 (≠ F469), V489 (= V470)
6demA Crystal structure of candida albicans acetohydroxyacid synthase in complex with the herbicide bensulfuron methyl (see paper)
28% identity, 92% coverage: 8:539/576 of query aligns to 18:563/597 of 6demA
- active site: Y33 (≠ I23), G35 (= G25), G36 (≠ D26), A37 (≠ S27), I38 (≠ L28), E59 (= E49), T82 (≠ S72), F121 (= F111), Q122 (= Q112), E123 (= E113), K171 (≠ G160), K228 (vs. gap), M264 (≠ L254), V291 (vs. gap), V407 (= V384), L432 (≠ H409), G433 (= G410), M435 (= M412), D460 (= D437), N487 (= N464), E489 (≠ T466), Q490 (≠ L467), M492 (≠ F469), V493 (= V470), W496 (≠ K475), L518 (≠ M494), N523 (≠ G499), V524 (≠ I500)
- binding methyl 2-[(4,6-dimethoxypyrimidin-2-yl)carbamoylsulfamoylmethyl]benzoate: M264 (≠ L254), D289 (≠ Y279), R290 (= R280), M492 (≠ F469), W496 (≠ K475)
- binding flavin-adenine dinucleotide: R161 (≠ K150), G217 (= G210), A218 (≠ S211), G219 (= G212), N222 (≠ G215), T244 (≠ A234), L245 (= L235), Q246 (≠ K236), L262 (≠ T252), G284 (= G274), A285 (≠ T275), R286 (≠ D276), D288 (≠ P278), R290 (= R280), V291 (vs. gap), E317 (≠ D294), I318 (= I295), N322 (≠ Q299), D336 (≠ E313), V337 (= V314), M412 (≠ V389), G430 (≠ F407)
- binding magnesium ion: D460 (= D437), N487 (= N464), E489 (≠ T466)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: V407 (= V384), G408 (= G385), Q409 (≠ L386), H410 (≠ P387), M435 (= M412), G459 (= G436), D460 (= D437), A461 (≠ G438), S462 (≠ G439), M465 (= M442), N487 (= N464), E489 (≠ T466), Q490 (≠ L467), G491 (= G468), M492 (≠ F469), V493 (= V470)
Sites not aligning to the query:
Query Sequence
>WP_020173663.1 NCBI__GCF_000385335.1:WP_020173663.1
MKTVADQFAEVLAAAGVQRIYGIVGDSLNGFTDAIRRQGKIQWLHVRHEEVAAFAASAEA
HLTGSLAVCAGSCGPGNLHLINGLFDCHRSRVPVLAIAAHIPSAEIGSGYFQETHPENLF
KECSHYCELISSPSQMPRVVEIAIREAVGKRGAAVIVIPGDVALHEAVEAPVPTFASLIP
SEPVVVPKEADLKALANLLNGAGRVTLLCGSGCAGAHSQLLALGEKLKAPMVHALKGKEY
VEWDNPYDVGMTGLIGFSSGYFAMNDCDALLMLGTDFPYRQFYPQGTAKIAQIDIRPEQL
GKRAPIDLGLVGEVGATLDALLPLLTEKKERKHLDQAIGHYKKAREGLDELAKGVPGKRL
VHPQQVAKAISDFASVDAIFTCDVGLPTVWAARYLAMNGARRLIGSFWHGSMANAMAQAI
GAQATFPNRQVISLSGDGGFAMLMGDFLSLAQLGLPVKIVVFNNGTLGFVELEQKSTGFI
DFGTGFKNPNFAAMAEAAGIKGIRIEDAGEVEPGIKAALAHNGPVLVDAVVNRQELAIPP
KITAEMAKGFTLYTLKAVIGGKVDEVLELARTNLWR
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