SitesBLAST
Comparing Ac3H11_3309 FitnessBrowser__acidovorax_3H11:Ac3H11_3309 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)
2q5oA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp and phenylpyruvate (see paper)
58% identity, 97% coverage: 8:536/548 of query aligns to 8:528/529 of 2q5oA
- active site: I23 (= I23), G25 (= G25), D26 (= D26), F27 (= F27), A28 (≠ I28), E49 (= E49), T72 (= T72), H113 (= H113), H114 (= H114), G116 (≠ V116), R117 (= R117), T118 (≠ H118), L119 (≠ V119), R166 (= R166), V258 (= V258), N285 (= N285), M373 (≠ I382), A395 (= A404), M397 (= M406), D422 (= D430), N449 (= N457), S451 (≠ T459), W452 (= W460), M454 (= M462), L455 (≠ I463), F458 (= F466), R515 (≠ P523)
- binding magnesium ion: D422 (= D430), N449 (= N457), S451 (≠ T459)
- binding 3-phenylpyruvic acid: G25 (= G25), D26 (= D26), R61 (= R61), H113 (= H113), H114 (= H114), R215 (= R215), R216 (= R216), M239 (= M239), G242 (= G242), T284 (≠ S284), L388 (= L397), M389 (≠ V398), A390 (= A399), M454 (= M462), F525 (= F533)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P24 (= P24), E49 (= E49), A75 (= A75), D375 (= D384), M397 (= M406), G421 (= G429), D422 (= D430), G423 (= G431), A424 (= A432), N449 (= N457), S451 (≠ T459), W452 (= W460), E453 (= E461), M454 (= M462), L455 (≠ I463)
2q5qA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp and 5-phenyl-2-oxo-valeric acid (see paper)
57% identity, 97% coverage: 8:536/548 of query aligns to 9:533/533 of 2q5qA
- active site: I24 (= I23), G26 (= G25), D27 (= D26), F28 (= F27), A29 (≠ I28), E50 (= E49), T73 (= T72), H114 (= H113), H115 (= H114), G117 (≠ V116), R118 (= R117), T119 (≠ H118), L120 (≠ V119), R167 (= R166), V259 (= V258), N286 (= N285), M378 (≠ I382), A400 (= A404), M402 (= M406), D427 (= D430), N454 (= N457), S456 (≠ T459), W457 (= W460), M459 (= M462), L460 (≠ I463), F463 (= F466), R520 (≠ P523)
- binding 5-phenyl-2-keto-valeric acid: G26 (= G25), D27 (= D26), R62 (= R61), H114 (= H113), H115 (= H114), R216 (= R215), R217 (= R216), M240 (= M239), R242 (= R241), D284 (= D283), T285 (≠ S284), L373 (≠ N377), L393 (= L397), M394 (≠ V398), A395 (= A399), A400 (= A404), M459 (= M462), F530 (= F533)
- binding magnesium ion: D427 (= D430), N454 (= N457), S456 (≠ T459)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P25 (= P24), E50 (= E49), A76 (= A75), D380 (= D384), M402 (= M406), G426 (= G429), D427 (= D430), G428 (= G431), A429 (= A432), N454 (= N457), S456 (≠ T459), W457 (= W460), E458 (= E461), M459 (= M462), L460 (≠ I463)
2q5lA X-ray structure of phenylpyruvate decarboxylase in complex with 2-(1- hydroxyethyl)-3-deaza-thdp (see paper)
57% identity, 97% coverage: 8:538/548 of query aligns to 13:538/538 of 2q5lA
- active site: I28 (= I23), G30 (= G25), D31 (= D26), F32 (= F27), A33 (≠ I28), E54 (= E49), T77 (= T72), T118 (≠ H113), L119 (≠ V119), R166 (= R166), V258 (= V258), N285 (= N285), M381 (≠ I382), A403 (= A404), M405 (= M406), D430 (= D430), N457 (= N457), S459 (≠ T459), W460 (= W460), M462 (= M462), L463 (≠ I463), F466 (= F466), R523 (≠ P523)
- binding magnesium ion: D430 (= D430), N457 (= N457), S459 (≠ T459)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: P29 (= P24), D31 (= D26), E54 (= E49), D383 (= D384), A403 (= A404), M405 (= M406), D430 (= D430), G431 (= G431), N457 (= N457), S459 (≠ T459), W460 (= W460), E461 (= E461), M462 (= M462), L463 (≠ I463)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1s)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: P29 (= P24), D31 (= D26), E54 (= E49), D383 (= D384), A403 (= A404), M405 (= M406), G429 (= G429), D430 (= D430), G431 (= G431), A432 (= A432), N457 (= N457), S459 (≠ T459), W460 (= W460), E461 (= E461), M462 (= M462), L463 (≠ I463)
2nxwA Crystal structure of phenylpyruvate decarboxylase of azospirillum brasilense (see paper)
57% identity, 97% coverage: 8:540/548 of query aligns to 14:537/537 of 2nxwA
- active site: I29 (= I23), G31 (= G25), D32 (= D26), F33 (= F27), A34 (≠ I28), E55 (= E49), T78 (= T72), R163 (= R166), V255 (= V258), N282 (= N285), M378 (≠ I382), A400 (= A404), M402 (= M406), D427 (= D430), N454 (= N457), S456 (≠ T459), W457 (= W460), M459 (= M462), L460 (≠ I463), F463 (= F466), R520 (≠ P523)
- binding magnesium ion: D427 (= D430), N454 (= N457), S456 (≠ T459)
- binding thiamine diphosphate: P30 (= P24), E55 (= E49), D380 (= D384), M402 (= M406), G426 (= G429), D427 (= D430), G428 (= G431), A429 (= A432), N454 (= N457), S456 (≠ T459), W457 (= W460), E458 (= E461), M459 (= M462), L460 (≠ I463)
2q5jA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp (see paper)
56% identity, 97% coverage: 8:538/548 of query aligns to 7:522/523 of 2q5jA
- active site: I22 (= I23), G24 (= G25), D25 (= D26), F26 (= F27), A27 (≠ I28), E48 (= E49), T71 (= T72), R150 (= R166), V242 (= V258), N269 (= N285), M365 (≠ I382), A387 (= A404), M389 (= M406), D414 (= D430), N441 (= N457), S443 (≠ T459), W444 (= W460), M446 (= M462), L447 (≠ I463), F450 (= F466), R507 (≠ P523)
- binding magnesium ion: D414 (= D430), N441 (= N457), S443 (≠ T459)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P23 (= P24), E48 (= E49), G366 (= G383), D367 (= D384), A387 (= A404), G388 (≠ S405), M389 (= M406), G413 (= G429), D414 (= D430), G415 (= G431), A416 (= A432), N441 (= N457), W444 (= W460), E445 (= E461), M446 (= M462), L447 (≠ I463)
2vjyA Pyruvate decarboxylase from kluyveromyces lactis in complex with the substrate analogue methyl acetylphosphonate (see paper)
26% identity, 99% coverage: 4:543/548 of query aligns to 5:561/562 of 2vjyA
- active site: L24 (≠ I23), G26 (= G25), D27 (= D26), F28 (= F27), N29 (≠ I28), E50 (= E49), T72 (= T72), H113 (= H113), H114 (= H114), L116 (≠ V116), G117 (≠ R117), A168 (≠ R166), T265 (≠ V258), N292 (= N285), T387 (≠ I382), G412 (≠ A404), I414 (≠ M406), D443 (= D430), N470 (= N457), G472 (≠ T459), Y473 (≠ W460), I475 (≠ M462), E476 (≠ I463), I479 (≠ F466), T541 (≠ P523)
- binding methoxy-[(1~{R})-1-oxidanylethyl]phosphinic acid: G26 (= G25), D27 (= D26), H91 (≠ R91), H113 (= H113), H114 (= H114), C220 (≠ E213), H224 (≠ F217), G285 (= G278), A286 (= A279), F291 (≠ S284), H309 (≠ A302), S310 (≠ H303), E476 (≠ I463), I479 (≠ F466)
- binding methyl hydrogen (s)-acetylphosphonate: E17 (≠ G16), K64 (≠ H63), Y156 (≠ R154)
- binding magnesium ion: D443 (= D430), N470 (= N457), G472 (≠ T459)
- binding thiamine diphosphate: P25 (= P24), E50 (= E49), V75 (≠ A75), T389 (≠ D384), G412 (≠ A404), S413 (= S405), I414 (≠ M406), G442 (= G429), G444 (= G431), S445 (≠ A432), N470 (= N457), G472 (≠ T459), Y473 (≠ W460), T474 (≠ E461), I475 (≠ M462), E476 (≠ I463)
6efhA Pyruvate decarboxylase from kluyveromyces lactis soaked with pyruvamide
26% identity, 97% coverage: 4:532/548 of query aligns to 5:550/557 of 6efhA
- active site: L24 (≠ I23), G26 (= G25), D27 (= D26), F28 (= F27), N29 (≠ I28), E50 (= E49), T72 (= T72), H113 (= H113), H114 (= H114), L116 (≠ V116), G117 (≠ R117), A168 (≠ R166), T265 (≠ V258), N292 (= N285), T387 (≠ I382), G412 (≠ A404), I414 (≠ M406), D443 (= D430), N470 (= N457), G472 (≠ T459), Y473 (≠ W460), I475 (≠ M462), E476 (≠ I463), I479 (≠ F466), T541 (≠ P523)
- binding magnesium ion: D443 (= D430), N470 (= N457), G472 (≠ T459)
- binding (1S,2S)-1-amino-1,2-dihydroxypropan-1-olate: H91 (≠ R91), C220 (≠ E213), H224 (≠ F217), G285 (= G278), A286 (= A279), H309 (≠ A302), S310 (≠ H303)
- binding thiamine diphosphate: P25 (= P24), E50 (= E49), V75 (≠ A75), G388 (= G383), T389 (≠ D384), G412 (≠ A404), I414 (≠ M406), G444 (= G431), S445 (≠ A432), N470 (= N457), G472 (≠ T459), Y473 (≠ W460), T474 (≠ E461), E476 (≠ I463)
2vbgA The complex structure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis with 2r-1-hydroxyethyl-deazathdp (see paper)
26% identity, 97% coverage: 1:532/548 of query aligns to 6:536/546 of 2vbgA
- active site: V28 (≠ I23), G30 (= G25), D31 (= D26), Y32 (≠ F27), N33 (≠ I28), N53 (≠ H48), E54 (= E49), T76 (= T72), F115 (≠ V111), V116 (≠ L112), H117 (= H113), H118 (= H114), L120 (≠ V116), A121 (≠ R117), V171 (≠ R166), K259 (≠ V258), S286 (≠ N285), E375 (≠ D381), Q376 (≠ I382), G401 (≠ A404), I403 (≠ M406), D428 (= D430), N455 (= N457), G457 (≠ T459), Y458 (≠ W460), V460 (≠ M462), E461 (≠ I463), K527 (≠ P523)
- binding magnesium ion: D428 (= D430), N455 (= N457), G457 (≠ T459)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: P29 (= P24), E54 (= E49), V79 (≠ A75), H118 (= H114), G377 (= G383), T378 (≠ D384), G401 (≠ A404), S402 (= S405), I403 (≠ M406), G427 (= G429), G429 (= G431), S430 (≠ A432), N455 (= N457), G457 (≠ T459), Y458 (≠ W460), T459 (≠ E461), V460 (≠ M462), E461 (≠ I463)
2vbfB The holostructure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis (see paper)
26% identity, 97% coverage: 1:532/548 of query aligns to 6:536/546 of 2vbfB
- active site: V28 (≠ I23), G30 (= G25), D31 (= D26), Y32 (≠ F27), N33 (≠ I28), N53 (≠ H48), E54 (= E49), T76 (= T72), F115 (≠ V111), V116 (≠ L112), H117 (= H113), H118 (= H114), L120 (≠ V116), A121 (≠ R117), V171 (≠ R166), K259 (≠ V258), S286 (≠ N285), E375 (≠ D381), Q376 (≠ I382), G401 (≠ A404), I403 (≠ M406), D428 (= D430), N455 (= N457), G457 (≠ T459), Y458 (≠ W460), V460 (≠ M462), E461 (≠ I463), K527 (≠ P523)
- binding magnesium ion: D428 (= D430), N455 (= N457), G457 (≠ T459)
- binding thiamine diphosphate: P29 (= P24), E54 (= E49), V79 (≠ A75), G377 (= G383), T378 (≠ D384), G401 (≠ A404), S402 (= S405), I403 (≠ M406), G427 (= G429), G429 (= G431), S430 (≠ A432), N455 (= N457), G457 (≠ T459), Y458 (≠ W460), T459 (≠ E461), V460 (≠ M462), E461 (≠ I463)
5npuA Inferred ancestral pyruvate decarboxylase (see paper)
28% identity, 99% coverage: 4:543/548 of query aligns to 4:542/547 of 5npuA
- binding magnesium ion: D425 (= D430), N452 (≠ Q458)
- binding thiamine diphosphate: D375 (= D384), G398 (≠ A404), H399 (≠ S405), I400 (≠ M406), G424 (= G429), D425 (= D430), S427 (≠ A432), N452 (≠ Q458), G454 (≠ W460), Y455 (≠ E461), T456 (≠ M462), I457 (= I463), E458 (≠ R464)
6vgsBBB Alpha-keto acid decarboxylase (see paper)
25% identity, 97% coverage: 1:532/548 of query aligns to 1:532/543 of 6vgsBBB
- active site: V23 (≠ I23), G25 (= G25), D26 (= D26), Y27 (≠ F27), N28 (≠ I28), E49 (= E49), T71 (= T72), H112 (= H113), H113 (= H114), L115 (≠ V116), A116 (≠ R117), V166 (≠ R166), S282 (≠ N285), Q372 (≠ I382), G397 (≠ A404), I399 (≠ M406), D424 (= D430), N451 (= N457), G453 (≠ T459), Y454 (≠ W460), V456 (≠ M462), E457 (≠ I463)
- binding magnesium ion: D424 (= D430), N451 (= N457), G453 (≠ T459)
- binding thiamine diphosphate: P24 (= P24), E49 (= E49), V74 (≠ A75), T374 (≠ D384), I399 (≠ M406), G423 (= G429), G425 (= G431), S426 (≠ A432), N451 (= N457), G453 (≠ T459), Y454 (≠ W460), T455 (≠ E461), V456 (≠ M462), E457 (≠ I463)
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)
25% identity, 96% coverage: 4:530/548 of query aligns to 6:549/563 of P06169
- R161 (≠ Q158) modified: Omega-N-methylarginine
- D291 (= D283) mutation to N: In PDC1-8; reduces catalytic activity to 10% but retains autoregulatory activity.
- T390 (≠ D384) binding
- GSI 413:415 (≠ ASM 404:406) binding
- D444 (= D430) binding
- GS 445:446 (≠ GA 431:432) binding
- N471 (= N457) binding
- NDGYTI 471:476 (≠ NQTWEM 457:462) binding
- G473 (≠ T459) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
1qpbA Pyruvate decarboyxlase from yeast (form b) complexed with pyruvamide (see paper)
25% identity, 96% coverage: 4:530/548 of query aligns to 5:548/555 of 1qpbA
- active site: L24 (≠ I23), G26 (= G25), D27 (= D26), F28 (= F27), N29 (≠ I28), E50 (= E49), T72 (= T72), H113 (= H113), H114 (= H114), L116 (≠ V116), G117 (≠ R117), A168 (≠ R166), T265 (≠ V258), N292 (= N285), T387 (≠ I382), G412 (≠ A404), I414 (≠ M406), D443 (= D430), N470 (= N457), G472 (≠ T459), Y473 (≠ W460), I475 (≠ M462), E476 (≠ I463), I479 (≠ F466), V541 (≠ P523)
- binding magnesium ion: D443 (= D430), N470 (= N457), G472 (≠ T459)
- binding pyruvamide: Y156 (≠ R154), H224 (≠ F217), D225 (≠ G218)
- binding thiamine diphosphate: P25 (= P24), E50 (= E49), V75 (≠ A75), T389 (≠ D384), I414 (≠ M406), G442 (= G429), G444 (= G431), S445 (≠ A432), N470 (= N457), G472 (≠ T459), Y473 (≠ W460), T474 (≠ E461), I475 (≠ M462), E476 (≠ I463)
1ovmA Crystal structure of indolepyruvate decarboxylase from enterobacter cloacae (see paper)
27% identity, 97% coverage: 8:539/548 of query aligns to 9:532/535 of 1ovmA
- active site: G26 (= G25), D27 (= D26), Y28 (≠ F27), N29 (≠ I28), E50 (= E49), T72 (= T72), H113 (= H113), H114 (= H114), L116 (≠ V116), G117 (≠ R117), A167 (≠ R166), S262 (≠ V258), L289 (≠ N285), Q367 (≠ I382), G392 (≠ A404), I394 (≠ M406), D419 (= D430), N446 (= N457), G448 (≠ T459), V451 (≠ M462), E452 (≠ I463), I455 (≠ F466), K516 (≠ P523)
- binding magnesium ion: D419 (= D430), N446 (= N457), G448 (≠ T459)
- binding thiamine diphosphate: P25 (= P24), E50 (= E49), V75 (≠ A75), T369 (≠ D384), G392 (≠ A404), S393 (= S405), I394 (≠ M406), G418 (= G429), G420 (= G431), A421 (= A432), N446 (= N457), G448 (≠ T459), Y449 (≠ W460), T450 (≠ E461), V451 (≠ M462), E452 (≠ I463)
8hp4A Ctpdc complex
26% identity, 96% coverage: 6:530/548 of query aligns to 10:529/540 of 8hp4A
- binding magnesium ion: D423 (= D430), N451 (= N457), G453 (≠ T459)
- binding thiamine diphosphate: P25 (= P24), E50 (= E49), V77 (≠ A75), T369 (≠ D384), S393 (= S405), I394 (≠ M406), G422 (= G429), G424 (= G431), S425 (≠ A432), N451 (= N457), G453 (≠ T459), Y454 (≠ W460), T455 (≠ E461), I456 (≠ M462)
2vk1A Crystal structure of the saccharomyces cerevisiae pyruvate decarboxylase variant d28a in complex with its substrate (see paper)
24% identity, 96% coverage: 4:530/548 of query aligns to 5:548/562 of 2vk1A
- active site: L24 (≠ I23), G26 (= G25), A27 (≠ D26), F28 (= F27), N29 (≠ I28), E50 (= E49), T72 (= T72), H113 (= H113), H114 (= H114), L116 (≠ V116), G117 (≠ R117), A168 (≠ R166), T265 (≠ V258), N292 (= N285), T387 (≠ I382), G412 (≠ A404), I414 (≠ M406), D443 (= D430), N470 (= N457), G472 (≠ T459), Y473 (≠ W460), I475 (≠ M462), E476 (≠ I463), I479 (≠ F466), V541 (≠ P523)
- binding magnesium ion: D443 (= D430), N470 (= N457), G472 (≠ T459)
- binding pyruvic acid: A27 (≠ D26), H114 (= H114), C220 (≠ E213), G285 (= G278), A286 (= A279), H309 (≠ A302), S310 (≠ H303)
- binding thiamine diphosphate: P25 (= P24), E50 (= E49), V75 (≠ A75), G388 (= G383), T389 (≠ D384), I414 (≠ M406), G442 (= G429), G444 (= G431), S445 (≠ A432), N470 (= N457), G472 (≠ T459), Y473 (≠ W460), T474 (≠ E461), I475 (≠ M462), E476 (≠ I463)
P23234 Indole-3-pyruvate decarboxylase; Indolepyruvate decarboxylase; EC 4.1.1.74 from Enterobacter cloacae (see paper)
27% identity, 97% coverage: 8:539/548 of query aligns to 11:548/552 of P23234
- E52 (= E49) binding
- D435 (= D430) binding
- N462 (= N457) binding
2w93A Crystal structure of the saccharomyces cerevisiae pyruvate decarboxylase variant e477q in complex with the surrogate pyruvamide
25% identity, 96% coverage: 4:530/548 of query aligns to 5:534/544 of 2w93A
- active site: L24 (≠ I23), G26 (= G25), D27 (= D26), F28 (= F27), N29 (≠ I28), E50 (= E49), T72 (= T72), H113 (= H113), H114 (= H114), L116 (≠ V116), G117 (≠ R117), A168 (≠ R166), T265 (≠ V258), T373 (≠ I382), G398 (≠ A404), I400 (≠ M406), D429 (= D430), N456 (= N457), G458 (≠ T459), Y459 (≠ W460), I461 (≠ M462), Q462 (≠ I463), I465 (≠ F466), V527 (≠ P523)
- binding magnesium ion: D429 (= D430), N456 (= N457), G458 (≠ T459)
- binding (1S,2S)-1-amino-1,2-dihydroxypropan-1-olate: D27 (= D26), H114 (= H114), C220 (≠ E213), H224 (≠ F217), G285 (= G278), A286 (= A279), H295 (≠ S289), S296 (≠ A290)
- binding thiamine diphosphate: P25 (= P24), E50 (= E49), V75 (≠ A75), T375 (≠ D384), S399 (= S405), I400 (≠ M406), G428 (= G429), G430 (= G431), S431 (≠ A432), N456 (= N457), G458 (≠ T459), Y459 (≠ W460), T460 (≠ E461), I461 (≠ M462), Q462 (≠ I463)
Q92345 Probable pyruvate decarboxylase C1F8.07c; EC 4.1.1.1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 99% coverage: 4:547/548 of query aligns to 11:567/569 of Q92345
- S233 (≠ G221) modified: Phosphoserine
- T521 (≠ K501) modified: Phosphothreonine
- S522 (≠ A502) modified: Phosphoserine
2vbiA Holostructure of pyruvate decarboxylase from acetobacter pasteurianus
25% identity, 99% coverage: 4:543/548 of query aligns to 4:552/554 of 2vbiA
- active site: G25 (= G25), D26 (= D26), Y27 (≠ F27), N28 (≠ I28), E49 (= E49), T71 (= T72), H112 (= H113), H113 (= H114), I115 (≠ V116), G116 (≠ R117), C167 (≠ R166), S290 (= S284), T383 (≠ I382), G408 (≠ A404), I410 (≠ M406), D435 (= D430), N462 (≠ Q458), G464 (≠ W460), Y465 (≠ E461), I467 (= I463), E468 (≠ R464), R532 (≠ P523)
- binding magnesium ion: D435 (= D430), N462 (≠ Q458), G464 (≠ W460)
- binding thiamine diphosphate: A24 (≠ P24), E49 (= E49), V74 (≠ A75), D385 (= D384), G408 (≠ A404), H409 (≠ S405), I410 (≠ M406), G434 (= G429), D435 (= D430), G436 (= G431), S437 (≠ A432), N462 (≠ Q458), G464 (≠ W460), Y465 (≠ E461), V466 (≠ M462), I467 (= I463)
Query Sequence
>Ac3H11_3309 FitnessBrowser__acidovorax_3H11:Ac3H11_3309
MNPLGLQLLHALKTHGAREIFGIPGDFILPLFKQIEESGILPLVTLSHEPSLGFAADAAA
RMHCGLGVVAVTYGAGALNVVNAVAGAYAERSPLVVLAGCPGEVEAHSGLVLHHQVRHVD
SQWRIFREITCDQVRLSDPATAPADLARVLRSCREYSQPVLIEVPRDMTLHPMAEVPLLP
PSPFNEAAVAECADEWMARIDAAQRPVLVVDVEVRRFGLEGRVAELARRLQLPVLTTFMG
RGLLAEEGVPFHGTYLGVAGAPETSALLDDSDLPMMLGAILSDSNFGVSAQRMDFRRALI
AAHREARVGHHLYPNIPLAALVEALLARAPAVGQQATRTLPPAPVCPEGLVADDTPVCAA
DLSRALNDHIRAQGPMNIVADIGDCLFAAMELLPTPLVAPGYYASMGFGVPAGIGAQVAS
GQRSLVLVGDGAFQMTGWELGNCPRLGLDPVVIVLNNQTWEMIRAFQTESRCAALGDWHL
AQAADALGGRGHRVHTRAQFKAALDAAFAERGRFQLIELMVPPGDSTPTLRRFSEGIRAL
RARAASAA
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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