SitesBLAST
Comparing WP_011735476.1 NCBI__GCF_000015045.1:WP_011735476.1 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)
2q5oA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp and phenylpyruvate (see paper)
37% identity, 95% coverage: 8:524/545 of query aligns to 4:513/529 of 2q5oA
- active site: I23 (= I27), G25 (= G29), D26 (= D30), F27 (≠ Y31), A28 (≠ V32), E49 (= E52), T72 (= T74), H113 (= H115), H114 (= H116), G116 (≠ V118), R117 (≠ K119), T118 (≠ E120), L119 (≠ F121), R166 (= R168), V258 (≠ G261), N285 (≠ D288), M373 (≠ T381), A395 (= A406), M397 (≠ L408), D422 (= D433), N449 (= N460), S451 (≠ G462), W452 (≠ Y463), M454 (≠ T465), L455 (≠ E466), F458 (≠ M469)
- binding magnesium ion: D422 (= D433), N449 (= N460), S451 (≠ G462)
- binding 3-phenylpyruvic acid: G25 (= G29), D26 (= D30), R61 (= R64), H113 (= H115), H114 (= H116), R215 (≠ L218), R216 (= R219), M239 (≠ L242), G242 (≠ S245), T284 (≠ L287), L388 (≠ F399), M389 (= M400), A390 (≠ S401), M454 (≠ T465)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P24 (= P28), E49 (= E52), A75 (≠ V77), D375 (= D383), M397 (≠ L408), G421 (= G432), D422 (= D433), G423 (= G434), A424 (= A435), N449 (= N460), S451 (≠ G462), W452 (≠ Y463), E453 (≠ G464), M454 (≠ T465), L455 (≠ E466)
Sites not aligning to the query:
2q5qA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp and 5-phenyl-2-oxo-valeric acid (see paper)
37% identity, 95% coverage: 8:524/545 of query aligns to 5:518/533 of 2q5qA
- active site: I24 (= I27), G26 (= G29), D27 (= D30), F28 (≠ Y31), A29 (≠ V32), E50 (= E52), T73 (= T74), H114 (= H115), H115 (= H116), G117 (≠ V118), R118 (≠ K119), T119 (≠ E120), L120 (≠ F121), R167 (= R168), V259 (≠ G261), N286 (≠ D288), M378 (≠ T381), A400 (= A406), M402 (≠ L408), D427 (= D433), N454 (= N460), S456 (≠ G462), W457 (≠ Y463), M459 (≠ T465), L460 (≠ E466), F463 (≠ M469)
- binding 5-phenyl-2-keto-valeric acid: G26 (= G29), D27 (= D30), R62 (= R64), H114 (= H115), H115 (= H116), R216 (≠ L218), R217 (= R219), M240 (≠ L242), R242 (≠ K244), D284 (= D286), T285 (≠ L287), L373 (≠ F376), L393 (≠ F399), M394 (= M400), A395 (≠ S401), A400 (= A406), M459 (≠ T465)
- binding magnesium ion: D427 (= D433), N454 (= N460), S456 (≠ G462)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P25 (= P28), E50 (= E52), A76 (≠ V77), D380 (= D383), M402 (≠ L408), G426 (= G432), D427 (= D433), G428 (= G434), A429 (= A435), N454 (= N460), S456 (≠ G462), W457 (≠ Y463), E458 (≠ G464), M459 (≠ T465), L460 (≠ E466)
Sites not aligning to the query:
2q5lA X-ray structure of phenylpyruvate decarboxylase in complex with 2-(1- hydroxyethyl)-3-deaza-thdp (see paper)
37% identity, 98% coverage: 8:543/545 of query aligns to 9:538/538 of 2q5lA
- active site: I28 (= I27), G30 (= G29), D31 (= D30), F32 (≠ Y31), A33 (≠ V32), E54 (= E52), T77 (= T74), T118 (≠ E120), L119 (≠ F121), R166 (= R168), V258 (≠ G261), N285 (≠ D288), M381 (≠ T381), A403 (= A406), M405 (≠ L408), D430 (= D433), N457 (= N460), S459 (≠ G462), W460 (≠ Y463), M462 (≠ T465), L463 (≠ E466), F466 (≠ M469), R523 (≠ P526)
- binding magnesium ion: D430 (= D433), N457 (= N460), S459 (≠ G462)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: P29 (= P28), D31 (= D30), E54 (= E52), D383 (= D383), A403 (= A406), M405 (≠ L408), D430 (= D433), G431 (= G434), N457 (= N460), S459 (≠ G462), W460 (≠ Y463), E461 (≠ G464), M462 (≠ T465), L463 (≠ E466)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1s)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: P29 (= P28), D31 (= D30), E54 (= E52), D383 (= D383), A403 (= A406), M405 (≠ L408), G429 (= G432), D430 (= D433), G431 (= G434), A432 (= A435), N457 (= N460), S459 (≠ G462), W460 (≠ Y463), E461 (≠ G464), M462 (≠ T465), L463 (≠ E466)
2nxwA Crystal structure of phenylpyruvate decarboxylase of azospirillum brasilense (see paper)
37% identity, 98% coverage: 8:543/545 of query aligns to 10:535/537 of 2nxwA
- active site: I29 (= I27), G31 (= G29), D32 (= D30), F33 (≠ Y31), A34 (≠ V32), E55 (= E52), T78 (= T74), R163 (= R168), V255 (≠ G261), N282 (≠ D288), M378 (≠ T381), A400 (= A406), M402 (≠ L408), D427 (= D433), N454 (= N460), S456 (≠ G462), W457 (≠ Y463), M459 (≠ T465), L460 (≠ E466), F463 (≠ M469), R520 (≠ P526)
- binding magnesium ion: D427 (= D433), N454 (= N460), S456 (≠ G462)
- binding thiamine diphosphate: P30 (= P28), E55 (= E52), D380 (= D383), M402 (≠ L408), G426 (= G432), D427 (= D433), G428 (= G434), A429 (= A435), N454 (= N460), S456 (≠ G462), W457 (≠ Y463), E458 (≠ G464), M459 (≠ T465), L460 (≠ E466)
2q5jA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp (see paper)
36% identity, 98% coverage: 8:543/545 of query aligns to 3:522/523 of 2q5jA
- active site: I22 (= I27), G24 (= G29), D25 (= D30), F26 (≠ Y31), A27 (≠ V32), E48 (= E52), T71 (= T74), R150 (= R168), V242 (≠ G261), N269 (≠ D288), M365 (≠ T381), A387 (= A406), M389 (≠ L408), D414 (= D433), N441 (= N460), S443 (≠ G462), W444 (≠ Y463), M446 (≠ T465), L447 (≠ E466), F450 (≠ M469), R507 (≠ P526)
- binding magnesium ion: D414 (= D433), N441 (= N460), S443 (≠ G462)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P23 (= P28), E48 (= E52), G366 (= G382), D367 (= D383), A387 (= A406), G388 (≠ S407), M389 (≠ L408), G413 (= G432), D414 (= D433), G415 (= G434), A416 (= A435), N441 (= N460), W444 (≠ Y463), E445 (≠ G464), M446 (≠ T465), L447 (≠ E466)
6vgsBBB Alpha-keto acid decarboxylase (see paper)
30% identity, 99% coverage: 7:545/545 of query aligns to 3:542/543 of 6vgsBBB
- active site: V23 (≠ I27), G25 (= G29), D26 (= D30), Y27 (= Y31), N28 (≠ V32), E49 (= E52), T71 (= T74), H112 (= H115), H113 (= H116), L115 (≠ V118), A116 (≠ K119), V166 (≠ R168), S282 (≠ D288), Q372 (≠ T381), G397 (≠ A406), I399 (≠ L408), D424 (= D433), N451 (= N460), G453 (= G462), Y454 (= Y463), V456 (≠ T465), E457 (= E466)
- binding magnesium ion: D424 (= D433), N451 (= N460), G453 (= G462)
- binding thiamine diphosphate: P24 (= P28), E49 (= E52), V74 (= V77), T374 (≠ D383), I399 (≠ L408), G423 (= G432), G425 (= G434), S426 (≠ A435), N451 (= N460), G453 (= G462), Y454 (= Y463), T455 (≠ G464), V456 (≠ T465), E457 (= E466)
2vbgA The complex structure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis with 2r-1-hydroxyethyl-deazathdp (see paper)
31% identity, 99% coverage: 7:545/545 of query aligns to 8:546/546 of 2vbgA
- active site: V28 (≠ I27), G30 (= G29), D31 (= D30), Y32 (= Y31), N33 (≠ V32), N53 (≠ D51), E54 (= E52), T76 (= T74), F115 (≠ L113), V116 (≠ L114), H117 (= H115), H118 (= H116), L120 (≠ V118), A121 (≠ K119), V171 (≠ R168), K259 (≠ G261), S286 (≠ D288), E375 (≠ D380), Q376 (≠ T381), G401 (≠ A406), I403 (≠ L408), D428 (= D433), N455 (= N460), G457 (= G462), Y458 (= Y463), V460 (≠ T465), E461 (= E466), K527 (≠ P526)
- binding magnesium ion: D428 (= D433), N455 (= N460), G457 (= G462)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: P29 (= P28), E54 (= E52), V79 (= V77), H118 (= H116), G377 (= G382), T378 (≠ D383), G401 (≠ A406), S402 (= S407), I403 (≠ L408), G427 (= G432), G429 (= G434), S430 (≠ A435), N455 (= N460), G457 (= G462), Y458 (= Y463), T459 (≠ G464), V460 (≠ T465), E461 (= E466)
2vbfB The holostructure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis (see paper)
31% identity, 99% coverage: 7:545/545 of query aligns to 8:546/546 of 2vbfB
- active site: V28 (≠ I27), G30 (= G29), D31 (= D30), Y32 (= Y31), N33 (≠ V32), N53 (≠ D51), E54 (= E52), T76 (= T74), F115 (≠ L113), V116 (≠ L114), H117 (= H115), H118 (= H116), L120 (≠ V118), A121 (≠ K119), V171 (≠ R168), K259 (≠ G261), S286 (≠ D288), E375 (≠ D380), Q376 (≠ T381), G401 (≠ A406), I403 (≠ L408), D428 (= D433), N455 (= N460), G457 (= G462), Y458 (= Y463), V460 (≠ T465), E461 (= E466), K527 (≠ P526)
- binding magnesium ion: D428 (= D433), N455 (= N460), G457 (= G462)
- binding thiamine diphosphate: P29 (= P28), E54 (= E52), V79 (= V77), G377 (= G382), T378 (≠ D383), G401 (≠ A406), S402 (= S407), I403 (≠ L408), G427 (= G432), G429 (= G434), S430 (≠ A435), N455 (= N460), G457 (= G462), Y458 (= Y463), T459 (≠ G464), V460 (≠ T465), E461 (= E466)
5npuA Inferred ancestral pyruvate decarboxylase (see paper)
30% identity, 99% coverage: 7:544/545 of query aligns to 3:536/547 of 5npuA
- binding magnesium ion: D425 (= D433), N452 (= N460)
- binding thiamine diphosphate: D375 (= D383), G398 (≠ A406), H399 (≠ S407), I400 (≠ L408), G424 (= G432), D425 (= D433), S427 (≠ A435), N452 (= N460), G454 (= G462), Y455 (= Y463), T456 (≠ G464), I457 (≠ T465), E458 (= E466)
P23234 Indole-3-pyruvate decarboxylase; Indolepyruvate decarboxylase; EC 4.1.1.74 from Enterobacter cloacae (see paper)
31% identity, 98% coverage: 8:540/545 of query aligns to 7:546/552 of P23234
- E52 (= E52) binding thiamine diphosphate
- D435 (= D433) binding Mg(2+)
- N462 (= N460) binding Mg(2+)
1ovmA Crystal structure of indolepyruvate decarboxylase from enterobacter cloacae (see paper)
31% identity, 98% coverage: 8:540/545 of query aligns to 5:530/535 of 1ovmA
- active site: G26 (= G29), D27 (= D30), Y28 (= Y31), N29 (≠ V32), E50 (= E52), T72 (= T74), H113 (= H115), H114 (= H116), L116 (≠ V118), G117 (≠ K119), A167 (≠ R168), S262 (≠ G261), L289 (≠ D288), Q367 (≠ T381), G392 (≠ A406), I394 (≠ L408), D419 (= D433), N446 (= N460), G448 (= G462), V451 (≠ T465), E452 (= E466), I455 (≠ M469), K516 (≠ P526)
- binding magnesium ion: D419 (= D433), N446 (= N460), G448 (= G462)
- binding thiamine diphosphate: P25 (= P28), E50 (= E52), V75 (= V77), T369 (≠ D383), G392 (≠ A406), S393 (= S407), I394 (≠ L408), G418 (= G432), G420 (= G434), A421 (= A435), N446 (= N460), G448 (= G462), Y449 (= Y463), T450 (≠ G464), V451 (≠ T465), E452 (= E466)
1qpbA Pyruvate decarboyxlase from yeast (form b) complexed with pyruvamide (see paper)
32% identity, 90% coverage: 4:491/545 of query aligns to 1:503/555 of 1qpbA
- active site: L24 (≠ I27), G26 (= G29), D27 (= D30), F28 (≠ Y31), N29 (≠ V32), E50 (= E52), T72 (= T74), H113 (= H115), H114 (= H116), L116 (≠ V118), G117 (≠ K119), A168 (≠ R168), T265 (≠ G261), N292 (≠ D288), T387 (= T381), G412 (≠ A406), I414 (≠ L408), D443 (= D433), N470 (= N460), G472 (= G462), Y473 (= Y463), I475 (≠ T465), E476 (= E466), I479 (≠ L470)
- binding magnesium ion: D443 (= D433), N470 (= N460), G472 (= G462)
- binding pyruvamide: Y156 (≠ L156), H224 (≠ Y220), D225 (≠ G221)
- binding thiamine diphosphate: P25 (= P28), E50 (= E52), V75 (= V77), T389 (≠ D383), I414 (≠ L408), G442 (= G432), G444 (= G434), S445 (≠ A435), N470 (= N460), G472 (= G462), Y473 (= Y463), T474 (≠ G464), I475 (≠ T465), E476 (= E466)
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)
32% identity, 90% coverage: 4:491/545 of query aligns to 2:504/563 of P06169
- S2 (≠ A4) modified: N-acetylserine
- R161 (= R160) modified: Omega-N-methylarginine
- D291 (= D286) mutation to N: In PDC1-8; reduces catalytic activity to 10% but retains autoregulatory activity.
- T390 (≠ D383) binding thiamine diphosphate
- GSI 413:415 (≠ ASL 406:408) binding thiamine diphosphate
- D444 (= D433) binding Mg(2+)
- GS 445:446 (≠ GA 434:435) binding thiamine diphosphate
- N471 (= N460) binding Mg(2+)
- NDGYTI 471:476 (≠ NSGYGT 460:465) binding thiamine diphosphate
- G473 (= G462) binding Mg(2+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Q92345 Probable pyruvate decarboxylase C1F8.07c; EC 4.1.1.1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 97% coverage: 7:533/545 of query aligns to 10:550/569 of Q92345
- S233 (≠ H224) modified: Phosphoserine
- T521 (≠ E504) modified: Phosphothreonine
- S522 (≠ V505) modified: Phosphoserine
2vk1A Crystal structure of the saccharomyces cerevisiae pyruvate decarboxylase variant d28a in complex with its substrate (see paper)
32% identity, 90% coverage: 4:491/545 of query aligns to 1:503/562 of 2vk1A
- active site: L24 (≠ I27), G26 (= G29), A27 (≠ D30), F28 (≠ Y31), N29 (≠ V32), E50 (= E52), T72 (= T74), H113 (= H115), H114 (= H116), L116 (≠ V118), G117 (≠ K119), A168 (≠ R168), T265 (≠ G261), N292 (≠ D288), T387 (= T381), G412 (≠ A406), I414 (≠ L408), D443 (= D433), N470 (= N460), G472 (= G462), Y473 (= Y463), I475 (≠ T465), E476 (= E466), I479 (≠ L470)
- binding magnesium ion: D443 (= D433), N470 (= N460), G472 (= G462)
- binding pyruvic acid: A27 (≠ D30), H114 (= H116), C220 (≠ E216), G285 (= G281), A286 (≠ V282), H309 (≠ T305), S310 (= S306)
- binding thiamine diphosphate: P25 (= P28), E50 (= E52), V75 (= V77), G388 (= G382), T389 (≠ D383), I414 (≠ L408), G442 (= G432), G444 (= G434), S445 (≠ A435), N470 (= N460), G472 (= G462), Y473 (= Y463), T474 (≠ G464), I475 (≠ T465), E476 (= E466)
Sites not aligning to the query:
2vbiA Holostructure of pyruvate decarboxylase from acetobacter pasteurianus
28% identity, 99% coverage: 7:543/545 of query aligns to 3:553/554 of 2vbiA
- active site: G25 (= G29), D26 (= D30), Y27 (= Y31), N28 (≠ V32), E49 (= E52), T71 (= T74), H112 (= H115), H113 (= H116), I115 (≠ V118), G116 (vs. gap), C167 (≠ R168), S290 (≠ D288), T383 (= T381), G408 (≠ A406), I410 (≠ L408), D435 (= D433), N462 (= N460), G464 (= G462), Y465 (= Y463), I467 (≠ T465), E468 (= E466), R532 (≠ P526)
- binding magnesium ion: D435 (= D433), N462 (= N460), G464 (= G462)
- binding thiamine diphosphate: A24 (≠ P28), E49 (= E52), V74 (= V77), D385 (= D383), G408 (≠ A406), H409 (≠ S407), I410 (≠ L408), G434 (= G432), D435 (= D433), G436 (= G434), S437 (≠ A435), N462 (= N460), G464 (= G462), Y465 (= Y463), V466 (≠ G464), I467 (≠ T465)
8hp4A Ctpdc complex
30% identity, 90% coverage: 4:493/545 of query aligns to 1:486/540 of 8hp4A
- binding magnesium ion: D423 (= D433), N451 (= N460), G453 (= G462)
- binding thiamine diphosphate: P25 (= P28), E50 (= E52), V77 (= V77), T369 (≠ D383), S393 (= S407), I394 (≠ L408), G422 (= G432), G424 (= G434), S425 (≠ A435), N451 (= N460), G453 (= G462), Y454 (= Y463), T455 (≠ G464), I456 (≠ T465)
6efhA Pyruvate decarboxylase from kluyveromyces lactis soaked with pyruvamide
31% identity, 90% coverage: 4:491/545 of query aligns to 1:503/557 of 6efhA
- active site: L24 (≠ I27), G26 (= G29), D27 (= D30), F28 (≠ Y31), N29 (≠ V32), E50 (= E52), T72 (= T74), H113 (= H115), H114 (= H116), L116 (≠ V118), G117 (≠ K119), A168 (≠ R168), T265 (≠ G261), N292 (≠ D288), T387 (= T381), G412 (≠ A406), I414 (≠ L408), D443 (= D433), N470 (= N460), G472 (= G462), Y473 (= Y463), I475 (≠ T465), E476 (= E466), I479 (≠ L470)
- binding magnesium ion: D443 (= D433), N470 (= N460), G472 (= G462)
- binding (1S,2S)-1-amino-1,2-dihydroxypropan-1-olate: H91 (≠ E93), C220 (≠ E216), H224 (≠ Y220), G285 (= G281), A286 (≠ V282), H309 (≠ T305), S310 (= S306)
- binding thiamine diphosphate: P25 (= P28), E50 (= E52), V75 (= V77), G388 (= G382), T389 (≠ D383), G412 (≠ A406), I414 (≠ L408), G444 (= G434), S445 (≠ A435), N470 (= N460), G472 (= G462), Y473 (= Y463), T474 (≠ G464), E476 (= E466)
Sites not aligning to the query:
2vjyA Pyruvate decarboxylase from kluyveromyces lactis in complex with the substrate analogue methyl acetylphosphonate (see paper)
31% identity, 90% coverage: 4:491/545 of query aligns to 1:503/562 of 2vjyA
- active site: L24 (≠ I27), G26 (= G29), D27 (= D30), F28 (≠ Y31), N29 (≠ V32), E50 (= E52), T72 (= T74), H113 (= H115), H114 (= H116), L116 (≠ V118), G117 (≠ K119), A168 (≠ R168), T265 (≠ G261), N292 (≠ D288), T387 (= T381), G412 (≠ A406), I414 (≠ L408), D443 (= D433), N470 (= N460), G472 (= G462), Y473 (= Y463), I475 (≠ T465), E476 (= E466), I479 (≠ L470)
- binding methoxy-[(1~{R})-1-oxidanylethyl]phosphinic acid: G26 (= G29), D27 (= D30), H91 (≠ E93), H113 (= H115), H114 (= H116), C220 (≠ E216), H224 (≠ Y220), G285 (= G281), A286 (≠ V282), F291 (≠ L287), H309 (≠ T305), S310 (= S306), E476 (= E466), I479 (≠ L470)
- binding methyl hydrogen (s)-acetylphosphonate: E17 (≠ R20), K64 (≠ R66), Y156 (≠ L156)
- binding magnesium ion: D443 (= D433), N470 (= N460), G472 (= G462)
- binding thiamine diphosphate: P25 (= P28), E50 (= E52), V75 (= V77), T389 (≠ D383), G412 (≠ A406), S413 (= S407), I414 (≠ L408), G442 (= G432), G444 (= G434), S445 (≠ A435), N470 (= N460), G472 (= G462), Y473 (= Y463), T474 (≠ G464), I475 (≠ T465), E476 (= E466)
Sites not aligning to the query:
2w93A Crystal structure of the saccharomyces cerevisiae pyruvate decarboxylase variant e477q in complex with the surrogate pyruvamide
31% identity, 90% coverage: 4:491/545 of query aligns to 1:489/544 of 2w93A
- active site: L24 (≠ I27), G26 (= G29), D27 (= D30), F28 (≠ Y31), N29 (≠ V32), E50 (= E52), T72 (= T74), H113 (= H115), H114 (= H116), L116 (≠ V118), G117 (≠ K119), A168 (≠ R168), T265 (≠ G261), T373 (= T381), G398 (≠ A406), I400 (≠ L408), D429 (= D433), N456 (= N460), G458 (= G462), Y459 (= Y463), I461 (≠ T465), Q462 (≠ E466), I465 (≠ L470)
- binding magnesium ion: D429 (= D433), N456 (= N460), G458 (= G462)
- binding (1S,2S)-1-amino-1,2-dihydroxypropan-1-olate: D27 (= D30), H114 (= H116), C220 (≠ E216), H224 (≠ Y220), G285 (= G281), A286 (≠ V282), H295 (≠ T305), S296 (= S306)
- binding thiamine diphosphate: P25 (= P28), E50 (= E52), V75 (= V77), T375 (≠ D383), S399 (= S407), I400 (≠ L408), G428 (= G432), G430 (= G434), S431 (≠ A435), N456 (= N460), G458 (= G462), Y459 (= Y463), T460 (≠ G464), I461 (≠ T465), Q462 (≠ E466)
Sites not aligning to the query:
Query Sequence
>WP_011735476.1 NCBI__GCF_000015045.1:WP_011735476.1
MEPAETTIGEYLIHRLYQLRVQHAFGIPGDYVLGFYKQLDESRIKIINTCDEQGAGFAAT
AYARVRGLGAVCVTYGVGGLKVVNTTAQAYAEETAVVVISGAPGVREQAGNPLLHHKVKE
FDTQLKVFQQLTVAQTVLDNPATACREINRVLGAALCYRRPVYIELPRDMVTVKIVPQEE
PLQPPDVDREPFREASREAVDMINAATQPVIVAGVELLRYGMHHHLQELVEKTNIPVTST
LLGKSAMGERHPGYIGLYEGGLSREDIRQYVESSDCIVLLGVLLTDLDLGIFTAHLDQGK
SIHATSEKTSIRHHTYPGVYLNGFLLGLLQADIRRRETCETPHAPAPTPFHPAPDTRITV
ERLFQRLETFFDDSTFVIADTGDALFAAADISIPRAAEFMSSAYYASLGFAVPASLGVQL
ALPTLRPLVLVGDGAFQMTGMEVATAARYHLNPIIIVLNNSGYGTERPMLDGSFNDVYPW
RYARLPELLGAGRGFDVQTEEQLEVALEAARGYRDGFCILDVRLDPYDFSPALRRMTSVL
GKKVK
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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