SitesBLAST
Comparing 8499247 FitnessBrowser__Miya:8499247 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)
2q5qA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp and 5-phenyl-2-oxo-valeric acid (see paper)
57% identity, 99% coverage: 1:564/572 of query aligns to 3:533/533 of 2q5qA
- active site: I24 (= I22), G26 (= G24), D27 (= D25), F28 (= F26), A29 (= A27), E50 (= E48), T73 (= T71), H114 (= H112), H115 (= H113), G117 (≠ V115), R118 (≠ K116), T119 (= T117), L120 (≠ V118), R167 (= R165), V259 (= V256), N286 (= N283), M378 (≠ I410), A400 (= A432), M402 (= M434), D427 (= D458), N454 (= N485), S456 (= S487), W457 (= W488), M459 (= M490), L460 (= L491), F463 (= F494), R520 (≠ K551)
- binding 5-phenyl-2-keto-valeric acid: G26 (= G24), D27 (= D25), R62 (= R60), H114 (= H112), H115 (= H113), R216 (= R214), R217 (= R215), M240 (= M238), R242 (= R240), D284 (= D281), T285 (= T282), L373 (≠ P405), L393 (≠ M425), M394 (≠ V426), A395 (≠ G427), A400 (= A432), M459 (= M490), F530 (= F561)
- binding magnesium ion: D427 (= D458), N454 (= N485), S456 (= S487)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P25 (= P23), E50 (= E48), A76 (= A74), D380 (= D412), M402 (= M434), G426 (= G457), D427 (= D458), G428 (= G459), A429 (= A460), N454 (= N485), S456 (= S487), W457 (= W488), E458 (= E489), M459 (= M490), L460 (= L491)
2q5oA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp and phenylpyruvate (see paper)
57% identity, 99% coverage: 1:564/572 of query aligns to 2:528/529 of 2q5oA
- active site: I23 (= I22), G25 (= G24), D26 (= D25), F27 (= F26), A28 (= A27), E49 (= E48), T72 (= T71), H113 (= H112), H114 (= H113), G116 (≠ V115), R117 (≠ K116), T118 (= T117), L119 (≠ V118), R166 (= R165), V258 (= V256), N285 (= N283), M373 (≠ I410), A395 (= A432), M397 (= M434), D422 (= D458), N449 (= N485), S451 (= S487), W452 (= W488), M454 (= M490), L455 (= L491), F458 (= F494), R515 (≠ K551)
- binding magnesium ion: D422 (= D458), N449 (= N485), S451 (= S487)
- binding 3-phenylpyruvic acid: G25 (= G24), D26 (= D25), R61 (= R60), H113 (= H112), H114 (= H113), R215 (= R214), R216 (= R215), M239 (= M238), G242 (= G241), T284 (= T282), L388 (≠ M425), M389 (≠ V426), A390 (≠ G427), M454 (= M490), F525 (= F561)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P24 (= P23), E49 (= E48), A75 (= A74), D375 (= D412), M397 (= M434), G421 (= G457), D422 (= D458), G423 (= G459), A424 (= A460), N449 (= N485), S451 (= S487), W452 (= W488), E453 (= E489), M454 (= M490), L455 (= L491)
2q5lA X-ray structure of phenylpyruvate decarboxylase in complex with 2-(1- hydroxyethyl)-3-deaza-thdp (see paper)
56% identity, 99% coverage: 1:566/572 of query aligns to 7:538/538 of 2q5lA
- active site: I28 (= I22), G30 (= G24), D31 (= D25), F32 (= F26), A33 (= A27), E54 (= E48), T77 (= T71), T118 (= T117), L119 (≠ V118), R166 (= R165), V258 (= V256), N285 (= N283), M381 (≠ I410), A403 (= A432), M405 (= M434), D430 (= D458), N457 (= N485), S459 (= S487), W460 (= W488), M462 (= M490), L463 (= L491), F466 (= F494), R523 (≠ K551)
- binding magnesium ion: D430 (= D458), N457 (= N485), S459 (= S487)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: P29 (= P23), D31 (= D25), E54 (= E48), D383 (= D412), A403 (= A432), M405 (= M434), D430 (= D458), G431 (= G459), N457 (= N485), S459 (= S487), W460 (= W488), E461 (= E489), M462 (= M490), L463 (= L491)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1s)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: P29 (= P23), D31 (= D25), E54 (= E48), D383 (= D412), A403 (= A432), M405 (= M434), G429 (= G457), D430 (= D458), G431 (= G459), A432 (= A460), N457 (= N485), S459 (= S487), W460 (= W488), E461 (= E489), M462 (= M490), L463 (= L491)
2nxwA Crystal structure of phenylpyruvate decarboxylase of azospirillum brasilense (see paper)
56% identity, 99% coverage: 1:568/572 of query aligns to 8:537/537 of 2nxwA
- active site: I29 (= I22), G31 (= G24), D32 (= D25), F33 (= F26), A34 (= A27), E55 (= E48), T78 (= T71), R163 (= R165), V255 (= V256), N282 (= N283), M378 (≠ I410), A400 (= A432), M402 (= M434), D427 (= D458), N454 (= N485), S456 (= S487), W457 (= W488), M459 (= M490), L460 (= L491), F463 (= F494), R520 (≠ K551)
- binding magnesium ion: D427 (= D458), N454 (= N485), S456 (= S487)
- binding thiamine diphosphate: P30 (= P23), E55 (= E48), D380 (= D412), M402 (= M434), G426 (= G457), D427 (= D458), G428 (= G459), A429 (= A460), N454 (= N485), S456 (= S487), W457 (= W488), E458 (= E489), M459 (= M490), L460 (= L491)
2q5jA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp (see paper)
55% identity, 99% coverage: 1:567/572 of query aligns to 1:523/523 of 2q5jA
- active site: I22 (= I22), G24 (= G24), D25 (= D25), F26 (= F26), A27 (= A27), E48 (= E48), T71 (= T71), R150 (= R165), V242 (= V256), N269 (= N283), M365 (≠ I410), A387 (= A432), M389 (= M434), D414 (= D458), N441 (= N485), S443 (= S487), W444 (= W488), M446 (= M490), L447 (= L491), F450 (= F494), R507 (≠ K551)
- binding magnesium ion: D414 (= D458), N441 (= N485), S443 (= S487)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P23 (= P23), E48 (= E48), G366 (= G411), D367 (= D412), A387 (= A432), G388 (≠ S433), M389 (= M434), G413 (= G457), D414 (= D458), G415 (= G459), A416 (= A460), N441 (= N485), W444 (= W488), E445 (= E489), M446 (= M490), L447 (= L491)
5npuA Inferred ancestral pyruvate decarboxylase (see paper)
26% identity, 98% coverage: 11:569/572 of query aligns to 12:537/547 of 5npuA
- binding magnesium ion: D425 (= D458), N452 (= N485)
- binding thiamine diphosphate: D375 (= D412), G398 (≠ A432), H399 (≠ S433), I400 (≠ M434), G424 (= G457), D425 (= D458), S427 (≠ A460), N452 (= N485), G454 (≠ S487), Y455 (≠ W488), T456 (≠ M490), I457 (≠ L491), E458 (≠ R492)
2vbgA The complex structure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis with 2r-1-hydroxyethyl-deazathdp (see paper)
24% identity, 95% coverage: 7:551/572 of query aligns to 13:527/546 of 2vbgA
- active site: V28 (≠ I22), G30 (= G24), D31 (= D25), Y32 (≠ F26), N33 (≠ A27), N53 (≠ H47), E54 (= E48), T76 (= T71), F115 (≠ L110), V116 (≠ L111), H117 (= H112), H118 (= H113), L120 (≠ V115), A121 (≠ K116), V171 (≠ R165), K259 (≠ V256), S286 (≠ N283), E375 (≠ A388), Q376 (≠ E389), G401 (≠ A432), I403 (≠ M434), D428 (= D458), N455 (= N485), G457 (≠ S487), Y458 (≠ W488), V460 (≠ M490), E461 (≠ L491), K527 (= K551)
- binding magnesium ion: D428 (= D458), N455 (= N485), G457 (≠ S487)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: P29 (= P23), E54 (= E48), V79 (≠ A74), H118 (= H113), G377 (≠ P390), T378 (≠ D391), G401 (≠ A432), S402 (= S433), I403 (≠ M434), G427 (= G457), G429 (= G459), S430 (≠ A460), N455 (= N485), G457 (≠ S487), Y458 (≠ W488), T459 (≠ E489), V460 (≠ M490), E461 (≠ L491)
2vbfB The holostructure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis (see paper)
24% identity, 95% coverage: 7:551/572 of query aligns to 13:527/546 of 2vbfB
- active site: V28 (≠ I22), G30 (= G24), D31 (= D25), Y32 (≠ F26), N33 (≠ A27), N53 (≠ H47), E54 (= E48), T76 (= T71), F115 (≠ L110), V116 (≠ L111), H117 (= H112), H118 (= H113), L120 (≠ V115), A121 (≠ K116), V171 (≠ R165), K259 (≠ V256), S286 (≠ N283), E375 (≠ A388), Q376 (≠ E389), G401 (≠ A432), I403 (≠ M434), D428 (= D458), N455 (= N485), G457 (≠ S487), Y458 (≠ W488), V460 (≠ M490), E461 (≠ L491), K527 (= K551)
- binding magnesium ion: D428 (= D458), N455 (= N485), G457 (≠ S487)
- binding thiamine diphosphate: P29 (= P23), E54 (= E48), V79 (≠ A74), G377 (≠ P390), T378 (≠ D391), G401 (≠ A432), S402 (= S433), I403 (≠ M434), G427 (= G457), G429 (= G459), S430 (≠ A460), N455 (= N485), G457 (≠ S487), Y458 (≠ W488), T459 (≠ E489), V460 (≠ M490), E461 (≠ L491)
6vgsBBB Alpha-keto acid decarboxylase (see paper)
24% identity, 95% coverage: 7:551/572 of query aligns to 8:523/543 of 6vgsBBB
- active site: V23 (≠ I22), G25 (= G24), D26 (= D25), Y27 (≠ F26), N28 (≠ A27), E49 (= E48), T71 (= T71), H112 (= H112), H113 (= H113), L115 (≠ V115), A116 (≠ K116), V166 (≠ R165), S282 (≠ N283), Q372 (≠ E389), G397 (≠ A432), I399 (≠ M434), D424 (= D458), N451 (= N485), G453 (≠ S487), Y454 (≠ W488), V456 (≠ M490), E457 (≠ L491)
- binding magnesium ion: D424 (= D458), N451 (= N485), G453 (≠ S487)
- binding thiamine diphosphate: P24 (= P23), E49 (= E48), V74 (≠ A74), T374 (≠ D391), I399 (≠ M434), G423 (= G457), G425 (= G459), S426 (≠ A460), N451 (= N485), G453 (≠ S487), Y454 (≠ W488), T455 (≠ E489), V456 (≠ M490), E457 (≠ L491)
P23234 Indole-3-pyruvate decarboxylase; Indolepyruvate decarboxylase; EC 4.1.1.74 from Enterobacter cloacae (see paper)
27% identity, 97% coverage: 3:554/572 of query aligns to 7:535/552 of P23234
- E52 (= E48) binding
- D435 (= D458) binding
- N462 (= N485) binding
2vbiA Holostructure of pyruvate decarboxylase from acetobacter pasteurianus
25% identity, 97% coverage: 7:561/572 of query aligns to 8:542/554 of 2vbiA
- active site: G25 (= G24), D26 (= D25), Y27 (≠ F26), N28 (≠ A27), E49 (= E48), T71 (= T71), H112 (= H112), H113 (= H113), I115 (≠ V115), G116 (vs. gap), C167 (≠ R165), S290 (≠ T282), T383 (≠ I410), G408 (≠ A432), I410 (≠ M434), D435 (= D458), N462 (= N485), G464 (≠ S487), Y465 (≠ W488), I467 (≠ L491), E468 (≠ R492), R532 (≠ K551)
- binding magnesium ion: D435 (= D458), N462 (= N485), G464 (≠ S487)
- binding thiamine diphosphate: A24 (≠ P23), E49 (= E48), V74 (≠ A74), D385 (= D412), G408 (≠ A432), H409 (≠ S433), I410 (≠ M434), G434 (= G457), D435 (= D458), G436 (= G459), S437 (≠ A460), N462 (= N485), G464 (≠ S487), Y465 (≠ W488), V466 (≠ M490), I467 (≠ L491)
1ovmA Crystal structure of indolepyruvate decarboxylase from enterobacter cloacae (see paper)
26% identity, 97% coverage: 3:554/572 of query aligns to 5:519/535 of 1ovmA
- active site: G26 (= G24), D27 (= D25), Y28 (≠ F26), N29 (≠ A27), E50 (= E48), T72 (= T71), H113 (= H112), H114 (= H113), L116 (≠ V118), G117 (= G119), A167 (≠ R165), S262 (≠ V256), L289 (≠ N283), Q367 (≠ P384), G392 (≠ A432), I394 (≠ M434), D419 (= D458), N446 (= N485), G448 (≠ S487), V451 (≠ M490), E452 (≠ L491), I455 (≠ F494), K516 (= K551)
- binding magnesium ion: D419 (= D458), N446 (= N485), G448 (≠ S487)
- binding thiamine diphosphate: P25 (= P23), E50 (= E48), V75 (≠ A74), T369 (≠ V386), G392 (≠ A432), S393 (= S433), I394 (≠ M434), G418 (= G457), G420 (= G459), A421 (= A460), N446 (= N485), G448 (≠ S487), Y449 (≠ W488), T450 (≠ E489), V451 (≠ M490), E452 (≠ L491)
Q92345 Probable pyruvate decarboxylase C1F8.07c; EC 4.1.1.1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
24% identity, 99% coverage: 1:569/572 of query aligns to 9:561/569 of Q92345
- S233 (≠ D220) modified: Phosphoserine
- T521 (≠ A529) modified: Phosphothreonine
- S522 (≠ A530) modified: Phosphoserine
1qpbA Pyruvate decarboyxlase from yeast (form b) complexed with pyruvamide (see paper)
24% identity, 95% coverage: 7:549/572 of query aligns to 9:539/555 of 1qpbA
- active site: L24 (≠ I22), G26 (= G24), D27 (= D25), F28 (= F26), N29 (≠ A27), E50 (= E48), T72 (= T71), H113 (= H112), H114 (= H113), L116 (≠ V118), G117 (= G119), A168 (≠ R165), T265 (≠ V256), N292 (= N283), T387 (≠ P390), G412 (≠ A432), I414 (≠ M434), D443 (= D458), N470 (= N485), G472 (≠ S487), Y473 (≠ W488), I475 (≠ M490), E476 (≠ L491), I479 (≠ F494)
- binding magnesium ion: D443 (= D458), N470 (= N485), G472 (≠ S487)
- binding pyruvamide: Y156 (≠ L153), H224 (≠ Y216), D225 (≠ G217)
- binding thiamine diphosphate: P25 (= P23), E50 (= E48), V75 (≠ A74), T389 (≠ P392), I414 (≠ M434), G442 (= G457), G444 (= G459), S445 (≠ A460), N470 (= N485), G472 (≠ S487), Y473 (≠ W488), T474 (≠ E489), I475 (≠ M490), E476 (≠ L491)
Sites not aligning to the query:
P06169 Pyruvate decarboxylase isozyme 1; Thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase; 2ODC; EC 4.1.1.-; EC 4.1.1.43; EC 4.1.1.72; EC 4.1.1.74 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 5 papers)
24% identity, 95% coverage: 7:549/572 of query aligns to 10:540/563 of P06169
- R161 (= R157) modified: Omega-N-methylarginine
- D291 (= D281) mutation to N: In PDC1-8; reduces catalytic activity to 10% but retains autoregulatory activity.
- T390 (≠ P392) binding
- GSI 413:415 (≠ ASM 432:434) binding
- D444 (= D458) binding
- GS 445:446 (≠ GA 459:460) binding
- N471 (= N485) binding
- NDGYTI 471:476 (≠ NASWEM 485:490) binding
- G473 (≠ S487) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
2vjyA Pyruvate decarboxylase from kluyveromyces lactis in complex with the substrate analogue methyl acetylphosphonate (see paper)
24% identity, 95% coverage: 7:549/572 of query aligns to 9:539/562 of 2vjyA
- active site: L24 (≠ I22), G26 (= G24), D27 (= D25), F28 (= F26), N29 (≠ A27), E50 (= E48), T72 (= T71), H113 (= H112), H114 (= H113), L116 (≠ V118), G117 (= G119), A168 (≠ R165), T265 (≠ V256), N292 (= N283), T387 (≠ P384), G412 (≠ A432), I414 (≠ M434), D443 (= D458), N470 (= N485), G472 (≠ S487), Y473 (≠ W488), I475 (≠ M490), E476 (≠ L491), I479 (≠ F494)
- binding methoxy-[(1~{R})-1-oxidanylethyl]phosphinic acid: G26 (= G24), D27 (= D25), H91 (≠ K90), H113 (= H112), H114 (= H113), C220 (≠ E212), H224 (≠ Y216), G285 (= G276), A286 (≠ V277), F291 (≠ T282), H309 (≠ E300), S310 (≠ D301), E476 (≠ L491), I479 (≠ F494)
- binding methyl hydrogen (s)-acetylphosphonate: E17 (≠ G15), K64 (≠ R62), Y156 (≠ L153)
- binding magnesium ion: D443 (= D458), N470 (= N485), G472 (≠ S487)
- binding thiamine diphosphate: P25 (= P23), E50 (= E48), V75 (≠ A74), T389 (≠ V386), G412 (≠ A432), S413 (= S433), I414 (≠ M434), G442 (= G457), G444 (= G459), S445 (≠ A460), N470 (= N485), G472 (≠ S487), Y473 (≠ W488), T474 (≠ E489), I475 (≠ M490), E476 (≠ L491)
Sites not aligning to the query:
6efhA Pyruvate decarboxylase from kluyveromyces lactis soaked with pyruvamide
24% identity, 95% coverage: 7:549/572 of query aligns to 9:539/557 of 6efhA
- active site: L24 (≠ I22), G26 (= G24), D27 (= D25), F28 (= F26), N29 (≠ A27), E50 (= E48), T72 (= T71), H113 (= H112), H114 (= H113), L116 (≠ V118), G117 (= G119), A168 (≠ R165), T265 (≠ V256), N292 (= N283), T387 (≠ P384), G412 (≠ A432), I414 (≠ M434), D443 (= D458), N470 (= N485), G472 (≠ S487), Y473 (≠ W488), I475 (≠ M490), E476 (≠ L491), I479 (≠ F494)
- binding magnesium ion: D443 (= D458), N470 (= N485), G472 (≠ S487)
- binding (1S,2S)-1-amino-1,2-dihydroxypropan-1-olate: H91 (≠ K90), C220 (≠ E212), H224 (≠ Y216), G285 (= G276), A286 (≠ V277), H309 (≠ E300), S310 (≠ D301)
- binding thiamine diphosphate: P25 (= P23), E50 (= E48), V75 (≠ A74), G388 (≠ A385), T389 (≠ V386), G412 (≠ A432), I414 (≠ M434), G444 (= G459), S445 (≠ A460), N470 (= N485), G472 (≠ S487), Y473 (≠ W488), T474 (≠ E489), E476 (≠ L491)
Sites not aligning to the query:
2vk1A Crystal structure of the saccharomyces cerevisiae pyruvate decarboxylase variant d28a in complex with its substrate (see paper)
24% identity, 95% coverage: 7:549/572 of query aligns to 9:539/562 of 2vk1A
- active site: L24 (≠ I22), G26 (= G24), A27 (≠ D25), F28 (= F26), N29 (≠ A27), E50 (= E48), T72 (= T71), H113 (= H112), H114 (= H113), L116 (≠ V118), G117 (= G119), A168 (≠ R165), T265 (≠ V256), N292 (= N283), T387 (≠ P390), G412 (≠ A432), I414 (≠ M434), D443 (= D458), N470 (= N485), G472 (≠ S487), Y473 (≠ W488), I475 (≠ M490), E476 (≠ L491), I479 (≠ F494)
- binding magnesium ion: D443 (= D458), N470 (= N485), G472 (≠ S487)
- binding pyruvic acid: A27 (≠ D25), H114 (= H113), C220 (≠ E212), G285 (= G276), A286 (≠ V277), H309 (≠ E300), S310 (≠ D301)
- binding thiamine diphosphate: P25 (= P23), E50 (= E48), V75 (≠ A74), G388 (≠ D391), T389 (≠ P392), I414 (≠ M434), G442 (= G457), G444 (= G459), S445 (≠ A460), N470 (= N485), G472 (≠ S487), Y473 (≠ W488), T474 (≠ E489), I475 (≠ M490), E476 (≠ L491)
Sites not aligning to the query:
2w93A Crystal structure of the saccharomyces cerevisiae pyruvate decarboxylase variant e477q in complex with the surrogate pyruvamide
24% identity, 95% coverage: 7:549/572 of query aligns to 9:525/544 of 2w93A
- active site: L24 (≠ I22), G26 (= G24), D27 (= D25), F28 (= F26), N29 (≠ A27), E50 (= E48), T72 (= T71), H113 (= H112), H114 (= H113), L116 (≠ V118), G117 (= G119), A168 (≠ R165), T265 (≠ V256), T373 (≠ P390), G398 (≠ A432), I400 (≠ M434), D429 (= D458), N456 (= N485), G458 (≠ S487), Y459 (≠ W488), I461 (≠ M490), Q462 (≠ L491), I465 (≠ F494)
- binding magnesium ion: D429 (= D458), N456 (= N485), G458 (≠ S487)
- binding (1S,2S)-1-amino-1,2-dihydroxypropan-1-olate: D27 (= D25), H114 (= H113), C220 (≠ E212), H224 (≠ Y216), G285 (= G276), A286 (≠ V277), H295 (= H290), S296 (≠ I291)
- binding thiamine diphosphate: P25 (= P23), E50 (= E48), V75 (≠ A74), T375 (≠ P392), S399 (= S433), I400 (≠ M434), G428 (= G457), G430 (= G459), S431 (≠ A460), N456 (= N485), G458 (≠ S487), Y459 (≠ W488), T460 (≠ E489), I461 (≠ M490), Q462 (≠ L491)
Sites not aligning to the query:
5eujE Pyruvate decarboxylase (see paper)
25% identity, 99% coverage: 7:572/572 of query aligns to 8:550/556 of 5eujE
- active site: G25 (= G24), D26 (= D25), Y27 (≠ F26), N28 (≠ A27), E49 (= E48), T71 (= T71), H112 (= H112), H113 (= H113), I115 (≠ V115), G116 (≠ K116), C167 (≠ R165), E263 (≠ V256), A290 (≠ N283), E382 (= E389), T383 (≠ I410), G408 (≠ A432), D435 (= D458), N462 (= N485), G464 (≠ S487), I467 (≠ L491), E468 (≠ R492)
- binding 1,2-ethanediol: Y289 (≠ T282), E468 (≠ R492)
- binding magnesium ion: D435 (= D458), N462 (= N485), G464 (≠ S487)
- binding thiamine diphosphate: A24 (≠ P23), E49 (= E48), V74 (≠ A74), G384 (= G411), D385 (= D412), G408 (≠ A432), H409 (≠ S433), I410 (≠ M434), G434 (= G457), G436 (= G459), S437 (≠ A460), N462 (= N485), G464 (≠ S487), Y465 (≠ W488), V466 (≠ M490), I467 (≠ L491), E468 (≠ R492)
Query Sequence
>8499247 FitnessBrowser__Miya:8499247
MNITEALLHALKERGAREVWGIPGDFALPYFKIIEQTGILPLVTLTHEPGLGFAADAAAR
IRRGLSVAAVTYGAGAINMLNAVAQAFAEKSPLVVVSGAPGTAERARGLLLHHQVKTVGS
QFRMYQEVTCDQGILDDPATAPAIIERVLRNCLEHSRPVYLEIPRDMPAVACGPVAPHMP
TPCDAEAVAACAAEVLARLRAASRPVLMVGVEVRRYGLEDRVAELADRLGVPVVTSFMGR
GLLAGKACLQGTYMGVAGDAAITQAVEGSDGLLLLGVIMSDTNFGVSASHIDRRRLMHAE
DRQVRMGFHTYHDIPLESLVDALLAALPEGGQACAVPAGLDGDGGALGRNVVYRRGFVAD
DAPVTPDDIAVLLNDFYDGVLNGPAVSAEPDPFPWPFGGRPLPWPLACDIGDCLFTALSV
RPVPMVGPGYYASMGFGVPAGMGLQVTTGQRSLTLVGDGAFQMTGMELGNCARLGIDPVV
VVFNNASWEMLRVFQPETSYSAINTLDFAAFADALGGHGYRVTTRRELAAAFASATTERG
RFQLIDVRLEKGAISDTLANFVAGVKRVSGVK
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