SitesBLAST
Comparing AZOBR_RS04230 FitnessBrowser__azobra:AZOBR_RS04230 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)
99% identity, 98% coverage: 1:535/545 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 (= G115), R118 (= R116), T119 (= T117), L120 (= L118), R167 (= R165), V259 (= V257), N286 (= N284), M378 (= M380), A400 (= A402), M402 (= M404), D427 (= D429), N454 (= N456), S456 (= S458), W457 (= W459), M459 (= M461), L460 (= L462), F463 (= F465), R520 (= R522)
- 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 (= D282), T285 (= T283), L373 (= L375), L393 (= L395), M394 (= M396), A395 (= A397), A400 (= A402), M459 (= M461), F530 (= F532)
- binding magnesium ion: D427 (= D429), N454 (= N456), S456 (= S458)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P25 (= P23), E50 (= E48), A76 (= A74), D380 (= D382), M402 (= M404), G426 (= G428), D427 (= D429), G428 (= G430), A429 (= A431), N454 (= N456), S456 (= S458), W457 (= W459), E458 (= E460), M459 (= M461), L460 (= L462)
2q5lA X-ray structure of phenylpyruvate decarboxylase in complex with 2-(1- hydroxyethyl)-3-deaza-thdp (see paper)
99% identity, 99% coverage: 1:537/545 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 (= L118), R166 (= R165), V258 (= V257), N285 (= N284), M381 (= M380), A403 (= A402), M405 (= M404), D430 (= D429), N457 (= N456), S459 (= S458), W460 (= W459), M462 (= M461), L463 (= L462), F466 (= F465), R523 (= R522)
- binding magnesium ion: D430 (= D429), N457 (= N456), S459 (= S458)
- 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 (= D382), A403 (= A402), M405 (= M404), D430 (= D429), G431 (= G430), N457 (= N456), S459 (= S458), W460 (= W459), E461 (= E460), M462 (= M461), L463 (= L462)
- 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 (= D382), A403 (= A402), M405 (= M404), G429 (= G428), D430 (= D429), G431 (= G430), A432 (= A431), N457 (= N456), S459 (= S458), W460 (= W459), E461 (= E460), M462 (= M461), L463 (= L462)
2q5oA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp and phenylpyruvate (see paper)
98% identity, 98% coverage: 1:536/545 of query aligns to 2:529/529 of 2q5oA
- active site: I23 (= I22), G25 (= G24), D26 (= D25), F27 (= F26), A28 (= A27), E49 (= E48), T72 (= T71), H113 (= H112), H114 (= H113), G116 (= G115), R117 (= R116), T118 (= T117), L119 (= L118), R166 (= R165), V258 (= V257), N285 (= N284), M373 (= M380), A395 (= A402), M397 (= M404), D422 (= D429), N449 (= N456), S451 (= S458), W452 (= W459), M454 (= M461), L455 (= L462), F458 (= F465), R515 (= R522)
- binding magnesium ion: D422 (= D429), N449 (= N456), S451 (= S458)
- binding 3-phenylpyruvic acid: G25 (= G24), D26 (= D25), R61 (= R60), H113 (= H112), H114 (= H113), R215 (= R214), R216 (= R215), M239 (= M238), G242 (= G241), T284 (= T283), L388 (= L395), M389 (= M396), A390 (= A397), M454 (= M461), F525 (= F532)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P24 (= P23), E49 (= E48), A75 (= A74), D375 (= D382), M397 (= M404), G421 (= G428), D422 (= D429), G423 (= G430), A424 (= A431), N449 (= N456), S451 (= S458), W452 (= W459), E453 (= E460), M454 (= M461), L455 (= L462)
2nxwA Crystal structure of phenylpyruvate decarboxylase of azospirillum brasilense (see paper)
98% identity, 99% coverage: 1:539/545 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 (= V257), N282 (= N284), M378 (= M380), A400 (= A402), M402 (= M404), D427 (= D429), N454 (= N456), S456 (= S458), W457 (= W459), M459 (= M461), L460 (= L462), F463 (= F465), R520 (= R522)
- binding magnesium ion: D427 (= D429), N454 (= N456), S456 (= S458)
- binding thiamine diphosphate: P30 (= P23), E55 (= E48), D380 (= D382), M402 (= M404), G426 (= G428), D427 (= D429), G428 (= G430), A429 (= A431), N454 (= N456), S456 (= S458), W457 (= W459), E458 (= E460), M459 (= M461), L460 (= L462)
2q5jA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp (see paper)
97% identity, 99% coverage: 1:538/545 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 (= V257), N269 (= N284), M365 (= M380), A387 (= A402), M389 (= M404), D414 (= D429), N441 (= N456), S443 (= S458), W444 (= W459), M446 (= M461), L447 (= L462), F450 (= F465), R507 (= R522)
- binding magnesium ion: D414 (= D429), N441 (= N456), S443 (= S458)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P23 (= P23), E48 (= E48), G366 (= G381), D367 (= D382), A387 (= A402), G388 (= G403), M389 (= M404), G413 (= G428), D414 (= D429), G415 (= G430), A416 (= A431), N441 (= N456), W444 (= W459), E445 (= E460), M446 (= M461), L447 (= L462)
5npuA Inferred ancestral pyruvate decarboxylase (see paper)
28% identity, 94% coverage: 11:522/545 of query aligns to 12:522/547 of 5npuA
- binding magnesium ion: D425 (= D429), N452 (= N456)
- binding thiamine diphosphate: D375 (= D382), G398 (≠ A402), H399 (≠ G403), I400 (≠ M404), G424 (= G428), D425 (= D429), S427 (≠ A431), N452 (= N456), G454 (≠ S458), Y455 (≠ W459), T456 (≠ E460), I457 (≠ M461), E458 (≠ L462)
P23234 Indole-3-pyruvate decarboxylase; Indolepyruvate decarboxylase; EC 4.1.1.74 from Enterobacter cloacae (see paper)
29% identity, 95% coverage: 3:522/545 of query aligns to 7:532/552 of P23234
- E52 (= E48) binding
- D435 (= D429) binding
- N462 (= N456) binding
1ovmA Crystal structure of indolepyruvate decarboxylase from enterobacter cloacae (see paper)
29% identity, 95% coverage: 3:522/545 of query aligns to 5:516/535 of 1ovmA
- active site: G26 (= G24), D27 (= D25), Y28 (≠ F26), N29 (≠ A27), E50 (= E48), T72 (= T71), H113 (= H112), H114 (= H113), L116 (= L118), G117 (vs. gap), A167 (≠ R165), S262 (≠ V257), L289 (≠ N284), Q367 (≠ M380), G392 (≠ A402), I394 (≠ M404), D419 (= D429), N446 (= N456), G448 (≠ S458), V451 (≠ M461), E452 (≠ L462), I455 (≠ F465), K516 (≠ R522)
- binding magnesium ion: D419 (= D429), N446 (= N456), G448 (≠ S458)
- binding thiamine diphosphate: P25 (= P23), E50 (= E48), V75 (≠ A74), T369 (≠ D382), G392 (≠ A402), S393 (≠ G403), I394 (≠ M404), G418 (= G428), G420 (= G430), A421 (= A431), N446 (= N456), G448 (≠ S458), Y449 (≠ W459), T450 (≠ E460), V451 (≠ M461), E452 (≠ L462)
2vbgA The complex structure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis with 2r-1-hydroxyethyl-deazathdp (see paper)
25% identity, 95% coverage: 3:522/545 of query aligns to 9:527/546 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 (≠ G115), A121 (≠ R116), V171 (≠ R165), K259 (≠ V257), S286 (≠ N284), E375 (≠ D379), Q376 (≠ M380), G401 (≠ A402), I403 (≠ M404), D428 (= D429), N455 (= N456), G457 (≠ S458), Y458 (≠ W459), V460 (≠ M461), E461 (≠ L462), K527 (≠ R522)
- binding magnesium ion: D428 (= D429), N455 (= N456), G457 (≠ S458)
- 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 (= G381), T378 (≠ D382), G401 (≠ A402), S402 (≠ G403), I403 (≠ M404), G427 (= G428), G429 (= G430), S430 (≠ A431), N455 (= N456), G457 (≠ S458), Y458 (≠ W459), T459 (≠ E460), V460 (≠ M461), E461 (≠ L462)
2vbfB The holostructure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis (see paper)
25% identity, 95% coverage: 3:522/545 of query aligns to 9:527/546 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 (≠ G115), A121 (≠ R116), V171 (≠ R165), K259 (≠ V257), S286 (≠ N284), E375 (≠ D379), Q376 (≠ M380), G401 (≠ A402), I403 (≠ M404), D428 (= D429), N455 (= N456), G457 (≠ S458), Y458 (≠ W459), V460 (≠ M461), E461 (≠ L462), K527 (≠ R522)
- binding magnesium ion: D428 (= D429), N455 (= N456), G457 (≠ S458)
- binding thiamine diphosphate: P29 (= P23), E54 (= E48), V79 (≠ A74), G377 (= G381), T378 (≠ D382), G401 (≠ A402), S402 (≠ G403), I403 (≠ M404), G427 (= G428), G429 (= G430), S430 (≠ A431), N455 (= N456), G457 (≠ S458), Y458 (≠ W459), T459 (≠ E460), V460 (≠ M461), E461 (≠ L462)
6vgsBBB Alpha-keto acid decarboxylase (see paper)
25% identity, 95% coverage: 3:522/545 of query aligns to 4:523/543 of 6vgsBBB
- active site: V23 (≠ I22), G25 (= G24), D26 (= D25), Y27 (≠ F26), N28 (≠ A27), E49 (= E48), T71 (= T71), H112 (= H112), H113 (= H113), L115 (≠ G115), A116 (≠ R116), V166 (≠ R165), S282 (≠ N284), Q372 (≠ M380), G397 (≠ A402), I399 (≠ M404), D424 (= D429), N451 (= N456), G453 (≠ S458), Y454 (≠ W459), V456 (≠ M461), E457 (≠ L462)
- binding magnesium ion: D424 (= D429), N451 (= N456), G453 (≠ S458)
- binding thiamine diphosphate: P24 (= P23), E49 (= E48), V74 (≠ A74), T374 (≠ D382), I399 (≠ M404), G423 (= G428), G425 (= G430), S426 (≠ A431), N451 (= N456), G453 (≠ S458), Y454 (≠ W459), T455 (≠ E460), V456 (≠ M461), E457 (≠ L462)
Q92345 Probable pyruvate decarboxylase C1F8.07c; EC 4.1.1.1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
25% identity, 100% coverage: 1:543/545 of query aligns to 9:564/569 of Q92345
- S233 (≠ A220) modified: Phosphoserine
- T521 (≠ K500) modified: Phosphothreonine
- S522 (≠ A501) modified: Phosphoserine
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)
26% identity, 96% coverage: 1:521/545 of query aligns to 4:541/563 of P06169
- R161 (= R157) modified: Omega-N-methylarginine
- D291 (= D282) mutation to N: In PDC1-8; reduces catalytic activity to 10% but retains autoregulatory activity.
- T390 (≠ D382) binding
- GSI 413:415 (≠ AGM 402:404) binding
- D444 (= D429) binding
- GS 445:446 (≠ GA 430:431) binding
- N471 (= N456) binding
- NDGYTI 471:476 (≠ NASWEM 456:461) binding
- G473 (≠ S458) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
2vbiA Holostructure of pyruvate decarboxylase from acetobacter pasteurianus
27% identity, 98% coverage: 1:532/545 of query aligns to 6:542/554 of 2vbiA
- active site: G25 (= G24), D26 (= D25), Y27 (≠ F26), N28 (≠ A27), E49 (= E48), T71 (= T71), H112 (= H112), H113 (= H113), I115 (vs. gap), G116 (= G115), C167 (≠ R165), S290 (≠ N284), T383 (≠ M380), G408 (≠ A402), I410 (≠ M404), D435 (= D429), N462 (= N456), G464 (≠ S458), Y465 (≠ W459), I467 (≠ L462), E468 (≠ R463), R532 (= R522)
- binding magnesium ion: D435 (= D429), N462 (= N456), G464 (≠ S458)
- binding thiamine diphosphate: A24 (≠ P23), E49 (= E48), V74 (≠ A74), D385 (= D382), G408 (≠ A402), H409 (≠ G403), I410 (≠ M404), G434 (= G428), D435 (= D429), G436 (= G430), S437 (≠ A431), N462 (= N456), G464 (≠ S458), Y465 (≠ W459), V466 (≠ M461), I467 (≠ L462)
1qpbA Pyruvate decarboyxlase from yeast (form b) complexed with pyruvamide (see paper)
26% identity, 96% coverage: 1:521/545 of query aligns to 3:540/555 of 1qpbA
- active site: L24 (≠ I22), G26 (= G24), D27 (= D25), F28 (= F26), N29 (≠ A27), E50 (= E48), T72 (= T71), H113 (= H112), H114 (= H113), L116 (≠ G115), G117 (≠ R116), A168 (≠ R165), T265 (≠ V257), N292 (= N284), T387 (≠ M380), G412 (≠ A402), I414 (≠ M404), D443 (= D429), N470 (= N456), G472 (≠ S458), Y473 (≠ W459), I475 (≠ M461), E476 (≠ L462), I479 (≠ F465)
- binding magnesium ion: D443 (= D429), N470 (= N456), G472 (≠ S458)
- binding pyruvamide: Y156 (≠ R153), H224 (≠ Y216), D225 (≠ G217)
- binding thiamine diphosphate: P25 (= P23), E50 (= E48), V75 (≠ A74), T389 (≠ D382), I414 (≠ M404), G442 (= G428), G444 (= G430), S445 (≠ A431), N470 (= N456), G472 (≠ S458), Y473 (≠ W459), T474 (≠ E460), I475 (≠ M461), E476 (≠ L462)
Sites not aligning to the query:
6efhA Pyruvate decarboxylase from kluyveromyces lactis soaked with pyruvamide
26% identity, 96% coverage: 1:521/545 of query aligns to 3:540/557 of 6efhA
- active site: L24 (≠ I22), G26 (= G24), D27 (= D25), F28 (= F26), N29 (≠ A27), E50 (= E48), T72 (= T71), H113 (= H112), H114 (= H113), L116 (≠ G115), G117 (≠ R116), A168 (≠ R165), T265 (≠ V257), N292 (= N284), T387 (≠ M380), G412 (≠ A402), I414 (≠ M404), D443 (= D429), N470 (= N456), G472 (≠ S458), Y473 (≠ W459), I475 (≠ M461), E476 (≠ L462), I479 (≠ F465)
- binding magnesium ion: D443 (= D429), N470 (= N456), G472 (≠ S458)
- binding (1S,2S)-1-amino-1,2-dihydroxypropan-1-olate: H91 (≠ K90), C220 (≠ E212), H224 (≠ Y216), G285 (= G277), A286 (= A278), H309 (≠ F301), S310 (≠ D302)
- binding thiamine diphosphate: P25 (= P23), E50 (= E48), V75 (≠ A74), G388 (= G381), T389 (≠ D382), G412 (≠ A402), I414 (≠ M404), G444 (= G430), S445 (≠ A431), N470 (= N456), G472 (≠ S458), Y473 (≠ W459), T474 (≠ E460), E476 (≠ L462)
Sites not aligning to the query:
2vjyA Pyruvate decarboxylase from kluyveromyces lactis in complex with the substrate analogue methyl acetylphosphonate (see paper)
26% identity, 96% coverage: 1:521/545 of query aligns to 3:540/562 of 2vjyA
- active site: L24 (≠ I22), G26 (= G24), D27 (= D25), F28 (= F26), N29 (≠ A27), E50 (= E48), T72 (= T71), H113 (= H112), H114 (= H113), L116 (≠ G115), G117 (≠ R116), A168 (≠ R165), T265 (≠ V257), N292 (= N284), T387 (≠ M380), G412 (≠ A402), I414 (≠ M404), D443 (= D429), N470 (= N456), G472 (≠ S458), Y473 (≠ W459), I475 (≠ M461), E476 (≠ L462), I479 (≠ F465)
- binding methoxy-[(1~{R})-1-oxidanylethyl]phosphinic acid: G26 (= G24), D27 (= D25), H91 (≠ K90), H113 (= H112), H114 (= H113), C220 (≠ E212), H224 (≠ Y216), G285 (= G277), A286 (= A278), F291 (≠ T283), H309 (≠ F301), S310 (≠ D302), E476 (≠ L462), I479 (≠ F465)
- binding methyl hydrogen (s)-acetylphosphonate: E17 (≠ G15), K64 (≠ S62), Y156 (≠ R153)
- binding magnesium ion: D443 (= D429), N470 (= N456), G472 (≠ S458)
- binding thiamine diphosphate: P25 (= P23), E50 (= E48), V75 (≠ A74), T389 (≠ D382), G412 (≠ A402), S413 (≠ G403), I414 (≠ M404), G442 (= G428), G444 (= G430), S445 (≠ A431), N470 (= N456), G472 (≠ S458), Y473 (≠ W459), T474 (≠ E460), I475 (≠ M461), E476 (≠ L462)
Sites not aligning to the query:
5eujE Pyruvate decarboxylase (see paper)
28% identity, 97% coverage: 1:529/545 of query aligns to 6:539/556 of 5eujE
- active site: G25 (= G24), D26 (= D25), Y27 (≠ F26), N28 (≠ A27), E49 (= E48), T71 (= T71), H112 (= H112), H113 (= H113), I115 (≠ G115), G116 (≠ R116), C167 (≠ R165), E263 (≠ V257), A290 (vs. gap), E382 (≠ D379), T383 (≠ M380), G408 (≠ A402), D435 (= D429), N462 (= N456), G464 (≠ S458), I467 (≠ L462), E468 (≠ R463)
- binding 1,2-ethanediol: Y289 (vs. gap), E468 (≠ R463)
- binding magnesium ion: D435 (= D429), N462 (= N456), G464 (≠ S458)
- binding thiamine diphosphate: A24 (≠ P23), E49 (= E48), V74 (≠ A74), G384 (= G381), D385 (= D382), G408 (≠ A402), H409 (≠ G403), I410 (≠ M404), G434 (= G428), G436 (= G430), S437 (≠ A431), N462 (= N456), G464 (≠ S458), Y465 (≠ W459), V466 (≠ M461), I467 (≠ L462), E468 (≠ R463)
2vk1A Crystal structure of the saccharomyces cerevisiae pyruvate decarboxylase variant d28a in complex with its substrate (see paper)
25% identity, 96% coverage: 1:521/545 of query aligns to 3:540/562 of 2vk1A
- active site: L24 (≠ I22), G26 (= G24), A27 (≠ D25), F28 (= F26), N29 (≠ A27), E50 (= E48), T72 (= T71), H113 (= H112), H114 (= H113), L116 (≠ G115), G117 (≠ R116), A168 (≠ R165), T265 (≠ V257), N292 (= N284), T387 (≠ M380), G412 (≠ A402), I414 (≠ M404), D443 (= D429), N470 (= N456), G472 (≠ S458), Y473 (≠ W459), I475 (≠ M461), E476 (≠ L462), I479 (≠ F465)
- binding magnesium ion: D443 (= D429), N470 (= N456), G472 (≠ S458)
- binding pyruvic acid: A27 (≠ D25), H114 (= H113), C220 (≠ E212), G285 (= G277), A286 (= A278), H309 (≠ F301), S310 (≠ D302)
- binding thiamine diphosphate: P25 (= P23), E50 (= E48), V75 (≠ A74), G388 (= G381), T389 (≠ D382), I414 (≠ M404), G442 (= G428), G444 (= G430), S445 (≠ A431), N470 (= N456), G472 (≠ S458), Y473 (≠ W459), T474 (≠ E460), I475 (≠ M461), E476 (≠ L462)
Sites not aligning to the query:
2w93A Crystal structure of the saccharomyces cerevisiae pyruvate decarboxylase variant e477q in complex with the surrogate pyruvamide
26% identity, 96% coverage: 1:521/545 of query aligns to 3:526/544 of 2w93A
- active site: L24 (≠ I22), G26 (= G24), D27 (= D25), F28 (= F26), N29 (≠ A27), E50 (= E48), T72 (= T71), H113 (= H112), H114 (= H113), L116 (≠ G115), G117 (≠ R116), A168 (≠ R165), T265 (≠ V257), T373 (≠ M380), G398 (≠ A402), I400 (≠ M404), D429 (= D429), N456 (= N456), G458 (≠ S458), Y459 (≠ W459), I461 (≠ M461), Q462 (≠ L462), I465 (≠ F465)
- binding magnesium ion: D429 (= D429), N456 (= N456), G458 (≠ S458)
- binding (1S,2S)-1-amino-1,2-dihydroxypropan-1-olate: D27 (= D25), H114 (= H113), C220 (≠ E212), H224 (≠ Y216), G285 (= G277), A286 (= A278), H295 (≠ K291), S296 (≠ I292)
- binding thiamine diphosphate: P25 (= P23), E50 (= E48), V75 (≠ A74), T375 (≠ D382), S399 (≠ G403), I400 (≠ M404), G428 (= G428), G430 (= G430), S431 (≠ A431), N456 (= N456), G458 (≠ S458), Y459 (≠ W459), T460 (≠ E460), I461 (≠ M461), Q462 (≠ L462)
Sites not aligning to the query:
Query Sequence
>AZOBR_RS04230 FitnessBrowser__azobra:AZOBR_RS04230
MKLAEALLRALKDRGAQAMFGIPGDFALPFFKVAEETQILPLHTLSHEPAVGFAADAAAR
YSSTLGVAAVTYGAGAFNMVNAVAGAYAEKSPVVVISGAPGTTEGNAGLLLHHQGRTLDT
QFQVFKEITVAQARLDDPAKAPAEIARVLGAARALSRPVYLEIPRNMVNAEVEPVGDDPA
WPVDRDALAACADEVLAAMRSATSPVLMVCVEVRRYGLEAKVAELAQRLGVPVVTTFMGR
GLLADAPTPPLGTYIGVAGDAEITRLVEESDGLFLLGAILSDTNFAVSQRKIDLRKTIHA
FDRAVTLGYHTYADIPLAGLVDALLERLPPSDRTTRGKEPHAYPTGLQADGEPIAPMDIA
RAVNDRVRAGQEPLLIAADMGDCLFTAMDMIDAGLMAPGYYAGMGFGVPAGIGAQCVSGG
KRILTVVGDGAFQMTGWELGNCRRLGIDPIVILFNNASWEMLRTFQPESAFNDLDDWRFA
DMAAGMGGDGVRVRTRAELKAALDKAFATRGRFQLIEAMIPRGVLSDTLARFVQGQKRLH
AAPRE
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