SitesBLAST
Comparing 14996 FitnessBrowser__Keio:14996 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)
P07003 Pyruvate dehydrogenase [ubiquinone]; Pyruvate oxidase; POX; Pyruvate:ubiquinone-8 oxidoreductase; EC 1.2.5.1 from Escherichia coli (strain K12) (see 4 papers)
100% identity, 100% coverage: 1:572/572 of query aligns to 1:572/572 of P07003
- 1:182 (vs. 1:182, 100% identical) Pyr domain
- E50 (= E50) binding thiamine diphosphate
- 183:334 (vs. 183:334, 100% identical) FAD-binding domain
- S210 (= S210) binding FAD
- LR 234:235 (= LR 234:235) binding FAD
- TGLI 251:254 (= TGLI 251:254) binding FAD
- TQFPY 274:278 (= TQFPY 274:278) binding FAD
- D292 (= D292) binding FAD
- S297 (= S297) binding FAD
- DI 311:312 (= DI 311:312) binding FAD
- 335:530 (vs. 335:530, 100% identical) PP-binding domain
- T382 (= T382) binding thiamine diphosphate
- FN 403:404 (= FN 403:404) binding FAD
- GSM 406:408 (= GSM 406:408) binding thiamine diphosphate
- D433 (= D433) binding Mg(2+)
- DGG 433:435 (= DGG 433:435) binding thiamine diphosphate
- N460 (= N460) binding Mg(2+)
- 460:466 (vs. 460:466, 100% identical) binding thiamine diphosphate
- V462 (= V462) binding Mg(2+)
- F465 (= F465) Moves into active site upon enzyme activation, plays a role in electron transfer
- 531:572 (vs. 531:572, 100% identical) Membrane-binding domain
- A533 (= A533) mutation to T: In poxB11; poor activity in vivo, no longer activated by lipids.
- YM 549:550 (= YM 549:550) In vitro cleavage to yield alpha-peptide
- 549:572 (vs. 549:572, 100% 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 (= A553) mutation to V: In poxB14; poor activity in vivo, no longer activated by lipids.
- D560 (= D560) mutation to P: In poxB15; normal activity.
- E564 (= E564) mutation to P: In poxB16; loss of activity, weakly activated by cleavage.
- 564:572 (vs. 564:572, 100% identical) mutation Missing: In poxB7 Inactive in vivo, reduced activity in vitro.
- WLR 570:572 (= WLR 570:572) mutation Missing: In poxB8; reduced activity in vitro, not activated by lipids.
- R572 (= R572) mutation to 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)
100% identity, 100% coverage: 2:572/572 of query aligns to 1:571/571 of 3ey9A
- active site: V23 (= V24), G25 (= G26), D26 (= D27), S27 (= S28), L28 (= L29), E49 (= E50), S72 (= S73), F111 (= F112), Q112 (= Q113), G160 (= G161), L252 (= L253), A279 (= A280), V379 (= V380), G405 (= G406), M407 (= M408), D432 (= D433), N459 (= N460), V461 (= V462), L462 (= L463), F464 (= F465), V465 (= V466), E468 (= E469), K528 (= K529)
- binding flavin-adenine dinucleotide: G208 (= G209), S209 (= S210), G210 (= G211), A232 (= A233), L233 (= L234), R234 (= R235), T250 (= T251), G251 (= G252), I253 (= I254), G272 (= G273), T273 (= T274), Q274 (= Q275), F275 (= F276), Y277 (= Y278), D291 (= D292), I292 (= I293), S296 (= S297), G309 (= G310), D310 (= D311), I311 (= I312), T383 (= T384), F402 (= F403), N403 (= N404), Y548 (= Y549)
- binding magnesium ion: D432 (= D433), N459 (= N460)
- binding thiamine diphosphate: T24 (= T25), E49 (= E50), S72 (= S73), G76 (= G77), H79 (= H80), G380 (= G381), T381 (= T382), P382 (= P383), M407 (= M408), G431 (= G432), D432 (= D433), G433 (= G434), G434 (= G435), N459 (= N460), V461 (= V462), L462 (= L463), G463 (= G464)
1powA The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from lactobacillus plantarum (see paper)
31% identity, 94% coverage: 7:543/572 of query aligns to 7:552/585 of 1powA
- active site: I24 (≠ V24), G26 (= G26), G27 (≠ D27), S28 (= S28), I29 (≠ L29), E51 (= E50), S74 (= S73), F113 (= F112), Q114 (= Q113), E115 (= E114), V162 (≠ G161), R256 (≠ L253), E283 (vs. gap), V386 (= V380), A412 (≠ G406), M414 (= M408), D439 (= D433), N466 (= N460), Q468 (≠ V462), Y469 (≠ L463), F471 (= F465), I472 (≠ V466), E475 (= E469), G538 (≠ K529)
- binding flavin-adenine dinucleotide: H93 (= H92), G212 (= G209), I213 (≠ S210), G214 (= G211), T236 (≠ A233), Y237 (≠ L234), A254 (≠ T251), V257 (≠ I254), G276 (= G273), N277 (≠ T274), N278 (≠ Q275), Y279 (≠ F276), P280 (= P277), F281 (≠ Y278), D298 (= D292), I299 (= I293), K303 (≠ S297), D317 (= D311), A318 (≠ I312), N409 (≠ F403)
- binding magnesium ion: D439 (= D433), N466 (= N460), Q468 (≠ V462)
- binding thiamine diphosphate: D388 (≠ T382), M414 (= M408), G440 (= G434), N466 (= N460), Q468 (≠ V462), Y469 (≠ L463), G470 (= G464), F471 (= F465), I472 (≠ V466)
4feeA High-resolution structure of pyruvate oxidase in complex with reaction intermediate 2-hydroxyethyl-thiamin diphosphate carbanion-enamine, crystal b (see paper)
31% identity, 94% coverage: 7:543/572 of query aligns to 7:552/586 of 4feeA
- binding flavin-adenine dinucleotide: H93 (= H92), G212 (= G209), I213 (≠ S210), G214 (= G211), T236 (≠ A233), Y237 (≠ L234), P238 (≠ R235), A254 (≠ T251), N255 (≠ G252), V257 (≠ I254), G276 (= G273), N277 (≠ T274), N278 (≠ Q275), P280 (= P277), F281 (≠ Y278), D298 (= D292), I299 (= I293), K303 (≠ S297), D317 (= D311), A318 (≠ I312), N390 (≠ T384), N409 (≠ F403)
- binding magnesium ion: D439 (= D433), N466 (= N460), Q468 (≠ V462)
- binding pyruvic acid: N255 (≠ G252), R256 (≠ L253), L547 (≠ I538), L549 (= L540), D550 (≠ E541)
- 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 (= V380), D388 (≠ T382), A412 (≠ G406), M414 (= M408), G438 (= G432), G440 (= G434), N466 (= N460), Q468 (≠ V462), Y469 (≠ L463), G470 (= G464), F471 (= F465), I472 (≠ V466)
Sites not aligning to the query:
1v5gA Crystal structure of the reaction intermediate between pyruvate oxidase containing fad and tpp, and substrate pyruvate (see paper)
31% identity, 90% coverage: 2:514/572 of query aligns to 2:520/589 of 1v5gA
- binding flavin-adenine dinucleotide: G212 (= G209), I213 (≠ S210), G214 (= G211), T236 (≠ A233), G237 (≠ L234), K238 (≠ R235), T254 (= T251), Y255 (≠ G252), R256 (≠ L253), V257 (≠ I254), G276 (= G273), S277 (≠ T274), N278 (≠ Q275), F279 (= F276), F281 (≠ Y278), D298 (= D292), I299 (= I293), M303 (≠ S297), D317 (= D311), A318 (≠ I312), P409 (≠ F403)
- binding 2-acetyl-thiamine diphosphate: V386 (= V380), N388 (≠ T382), M414 (= M408), G438 (= G432), G440 (= G434), A441 (≠ G435), N466 (= N460), E468 (≠ V462), Y469 (≠ L463), A470 (≠ G464), F471 (= F465), I472 (≠ V466)
- binding magnesium ion: D439 (= D433), N466 (= N460), E468 (≠ V462)
1v5fA Crystal structure of pyruvate oxidase complexed with fad and tpp, from aerococcus viridans (see paper)
31% identity, 90% coverage: 2:514/572 of query aligns to 2:520/589 of 1v5fA
- binding flavin-adenine dinucleotide: G212 (= G209), I213 (≠ S210), G214 (= G211), T236 (≠ A233), G237 (≠ L234), K238 (≠ R235), T254 (= T251), Y255 (≠ G252), R256 (≠ L253), V257 (≠ I254), G276 (= G273), S277 (≠ T274), N278 (≠ Q275), F279 (= F276), P280 (= P277), F281 (≠ Y278), D298 (= D292), I299 (= I293), M303 (≠ S297), D317 (= D311), A318 (≠ I312), P409 (≠ F403)
- binding magnesium ion: D439 (= D433), N466 (= N460)
- binding thiamine diphosphate: N388 (≠ T382), S389 (≠ P383), M414 (= M408), G438 (= G432), G440 (= G434), N466 (= N460), Y469 (≠ L463), A470 (≠ G464), F471 (= F465), I472 (≠ V466)
2djiA Crystal structure of pyruvate oxidase from aerococcus viridans containing fad (see paper)
31% identity, 90% coverage: 2:514/572 of query aligns to 3:521/590 of 2djiA