SitesBLAST
Comparing WP_083768615.1 NCBI__GCF_000020385.1:WP_083768615.1 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)
5npuA Inferred ancestral pyruvate decarboxylase (see paper)
37% identity, 96% coverage: 19:557/563 of query aligns to 3:533/547 of 5npuA
- binding magnesium ion: D425 (= D449), N452 (= N476)
- binding thiamine diphosphate: D375 (= D399), G398 (≠ S422), H399 (≠ S423), I400 (= I424), G424 (= G448), D425 (= D449), S427 (≠ A451), N452 (= N476), G454 (= G478), Y455 (= Y479), T456 (≠ L480), I457 (≠ V481), E458 (= E482)
2vbgA The complex structure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis with 2r-1-hydroxyethyl-deazathdp (see paper)
36% identity, 96% coverage: 19:557/563 of query aligns to 8:538/546 of 2vbgA
- active site: V28 (= V39), G30 (= G41), D31 (= D42), Y32 (= Y43), N33 (≠ V44), N53 (= N63), E54 (= E64), T76 (= T86), F115 (≠ L125), V116 (= V126), H117 (= H127), H118 (= H128), L120 (≠ V130), A121 (= A131), V171 (≠ A180), K259 (≠ G275), S286 (≠ D302), E375 (= E396), Q376 (≠ P397), G401 (≠ S422), I403 (= I424), D428 (= D449), N455 (= N476), G457 (= G478), Y458 (= Y479), V460 (= V481), E461 (= E482), K527 (= K546)
- binding magnesium ion: D428 (= D449), N455 (= N476), G457 (= G478)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: P29 (= P40), E54 (= E64), V79 (= V89), H118 (= H128), G377 (= G398), T378 (≠ D399), G401 (≠ S422), S402 (= S423), I403 (= I424), G427 (= G448), G429 (= G450), S430 (≠ A451), N455 (= N476), G457 (= G478), Y458 (= Y479), T459 (≠ L480), V460 (= V481), E461 (= E482)
2vbfB The holostructure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis (see paper)
36% identity, 96% coverage: 19:557/563 of query aligns to 8:538/546 of 2vbfB
- active site: V28 (= V39), G30 (= G41), D31 (= D42), Y32 (= Y43), N33 (≠ V44), N53 (= N63), E54 (= E64), T76 (= T86), F115 (≠ L125), V116 (= V126), H117 (= H127), H118 (= H128), L120 (≠ V130), A121 (= A131), V171 (≠ A180), K259 (≠ G275), S286 (≠ D302), E375 (= E396), Q376 (≠ P397), G401 (≠ S422), I403 (= I424), D428 (= D449), N455 (= N476), G457 (= G478), Y458 (= Y479), V460 (= V481), E461 (= E482), K527 (= K546)
- binding magnesium ion: D428 (= D449), N455 (= N476), G457 (= G478)
- binding thiamine diphosphate: P29 (= P40), E54 (= E64), V79 (= V89), G377 (= G398), T378 (≠ D399), G401 (≠ S422), S402 (= S423), I403 (= I424), G427 (= G448), G429 (= G450), S430 (≠ A451), N455 (= N476), G457 (= G478), Y458 (= Y479), T459 (≠ L480), V460 (= V481), E461 (= E482)
6vgsBBB Alpha-keto acid decarboxylase (see paper)
36% identity, 96% coverage: 19:557/563 of query aligns to 3:534/543 of 6vgsBBB
- active site: V23 (= V39), G25 (= G41), D26 (= D42), Y27 (= Y43), N28 (≠ V44), E49 (= E64), T71 (= T86), H112 (= H127), H113 (= H128), L115 (≠ V130), A116 (= A131), V166 (≠ A180), S282 (≠ D302), Q372 (≠ P397), G397 (≠ S422), I399 (= I424), D424 (= D449), N451 (= N476), G453 (= G478), Y454 (= Y479), V456 (= V481), E457 (= E482)
- binding magnesium ion: D424 (= D449), N451 (= N476), G453 (= G478)
- binding thiamine diphosphate: P24 (= P40), E49 (= E64), V74 (= V89), T374 (≠ D399), I399 (= I424), G423 (= G448), G425 (= G450), S426 (≠ A451), N451 (= N476), G453 (= G478), Y454 (= Y479), T455 (≠ L480), V456 (= V481), E457 (= E482)
P23234 Indole-3-pyruvate decarboxylase; Indolepyruvate decarboxylase; EC 4.1.1.74 from Enterobacter cloacae (see paper)
38% identity, 95% coverage: 14:548/563 of query aligns to 1:534/552 of P23234
- E52 (= E64) binding thiamine diphosphate
- D435 (= D449) binding Mg(2+)
- N462 (= N476) binding Mg(2+)
1ovmA Crystal structure of indolepyruvate decarboxylase from enterobacter cloacae (see paper)
38% identity, 95% coverage: 16:548/563 of query aligns to 1:518/535 of 1ovmA
- active site: G26 (= G41), D27 (= D42), Y28 (= Y43), N29 (≠ V44), E50 (= E64), T72 (= T86), H113 (= H127), H114 (= H128), L116 (≠ V130), G117 (≠ A131), A167 (= A180), S262 (≠ G275), L289 (≠ D302), Q367 (≠ P397), G392 (≠ S422), I394 (= I424), D419 (= D449), N446 (= N476), G448 (= G478), V451 (= V481), E452 (= E482), I455 (≠ L485), K516 (= K546)
- binding magnesium ion: D419 (= D449), N446 (= N476), G448 (= G478)
- binding thiamine diphosphate: P25 (= P40), E50 (= E64), V75 (= V89), T369 (≠ D399), G392 (≠ S422), S393 (= S423), I394 (= I424), G418 (= G448), G420 (= G450), A421 (= A451), N446 (= N476), G448 (= G478), Y449 (= Y479), T450 (≠ L480), V451 (= V481), E452 (= E482)
2vbiA Holostructure of pyruvate decarboxylase from acetobacter pasteurianus
36% identity, 96% coverage: 19:557/563 of query aligns to 3:543/554 of 2vbiA
- active site: G25 (= G41), D26 (= D42), Y27 (= Y43), N28 (vs. gap), E49 (= E64), T71 (= T86), H112 (= H127), H113 (= H128), I115 (≠ V130), G116 (vs. gap), C167 (≠ A180), S290 (≠ D302), T383 (≠ P397), G408 (≠ S422), I410 (= I424), D435 (= D449), N462 (= N476), G464 (= G478), Y465 (= Y479), I467 (≠ V481), E468 (= E482), R532 (≠ K546)
- binding magnesium ion: D435 (= D449), N462 (= N476), G464 (= G478)
- binding thiamine diphosphate: A24 (≠ P40), E49 (= E64), V74 (= V89), D385 (= D399), G408 (≠ S422), H409 (≠ S423), I410 (= I424), G434 (= G448), D435 (= D449), G436 (= G450), S437 (≠ A451), N462 (= N476), G464 (= G478), Y465 (= Y479), V466 (≠ L480), I467 (≠ V481)
2wvgA Structural insights into the pre-reaction state of pyruvate decarboxylase from zymomonas mobilis (see paper)
35% identity, 96% coverage: 19:557/563 of query aligns to 3:551/565 of 2wvgA
- active site: D26 (= D42), Y27 (= Y43), E49 (= E64), Y72 (= Y87), H112 (= H127), H113 (= H128), L115 (≠ V130), G116 (≠ A131), C167 (≠ A180), Y289 (≠ L301), T387 (≠ P397), G412 (≠ S422), D439 (= D449), N466 (= N476), G468 (= G478), I471 (≠ V481), E472 (= E482)
- binding fluoride ion: G25 (= G41), D26 (= D42), T71 (= T86), H113 (= H128)
- binding magnesium ion: D439 (= D449), N466 (= N476), G468 (= G478)
- binding 2-{1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-methyl-1h-1,2,3-triazol-4-yl}ethyl trihydrogen diphosphate: A24 (≠ P40), E49 (= E64), V74 (= V89), D389 (= D399), G412 (≠ S422), H413 (≠ S423), I414 (= I424), G438 (= G448), D439 (= D449), G440 (= G450), S441 (≠ A451), N466 (= N476), G468 (= G478), Y469 (= Y479), T470 (≠ L480), I471 (≠ V481), E472 (= E482)
2wvaE Structural insights into the pre-reaction state of pyruvate decarboxylase from zymomonas mobilis (see paper)
35% identity, 96% coverage: 19:557/563 of query aligns to 3:551/565 of 2wvaE
- active site: D26 (= D42), Y27 (= Y43), E49 (= E64), Y72 (= Y87), H112 (= H127), H113 (= H128), L115 (≠ V130), G116 (≠ A131), C167 (≠ A180), Y289 (≠ L301), T387 (≠ P397), G412 (≠ S422), D439 (= D449), N466 (= N476), G468 (= G478), I471 (≠ V481), E472 (= E482)
- binding magnesium ion: D439 (= D449), N466 (= N476), G468 (= G478)
- binding pyruvic acid: D26 (= D42), H113 (= H128)
- binding 2-{1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-methyl-1h-1,2,3-triazol-4-yl}ethyl trihydrogen diphosphate: A24 (≠ P40), E49 (= E64), V74 (= V89), H113 (= H128), G388 (= G398), D389 (= D399), H413 (≠ S423), I414 (= I424), G438 (= G448), G440 (= G450), S441 (≠ A451), G468 (= G478), Y469 (= Y479), T470 (≠ L480), I471 (≠ V481), E472 (= E482)
2wvaA Structural insights into the pre-reaction state of pyruvate decarboxylase from zymomonas mobilis (see paper)
35% identity, 96% coverage: 19:557/563 of query aligns to 3:551/565 of 2wvaA
- active site: D26 (= D42), Y27 (= Y43), E49 (= E64), Y72 (= Y87), H112 (= H127), H113 (= H128), L115 (≠ V130), G116 (≠ A131), C167 (≠ A180), Y289 (≠ L301), T387 (≠ P397), G412 (≠ S422), D439 (= D449), N466 (= N476), G468 (= G478), I471 (≠ V481), E472 (= E482)
- binding magnesium ion: D439 (= D449), N466 (= N476), G468 (= G478)
- binding 2-{1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-methyl-1h-1,2,3-triazol-4-yl}ethyl trihydrogen diphosphate: A24 (≠ P40), E49 (= E64), V74 (= V89), H113 (= H128), D389 (= D399), G412 (≠ S422), H413 (≠ S423), I414 (= I424), G438 (= G448), D439 (= D449), G440 (= G450), S441 (≠ A451), N466 (= N476), G468 (= G478), Y469 (= Y479), T470 (≠ L480), I471 (≠ V481), E472 (= E482)
P06672 Pyruvate decarboxylase; PDC; EC 4.1.1.1 from Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) (see 2 papers)
35% identity, 96% coverage: 19:557/563 of query aligns to 4:552/568 of P06672
- E50 (= E64) mutation to Q: Almost complete loss of activity.
3oe1A Pyruvate decarboxylase variant glu473asp from z. Mobilis in complex with reaction intermediate 2-lactyl-thdp (see paper)
35% identity, 96% coverage: 19:557/563 of query aligns to 3:551/565 of 3oe1A
- active site: D26 (= D42), Y27 (= Y43), E49 (= E64), Y72 (= Y87), H112 (= H127), H113 (= H128), L115 (≠ V130), G116 (≠ A131), C167 (≠ A180), Y289 (≠ L301), T387 (≠ P397), G412 (≠ S422), D439 (= D449), N466 (= N476), G468 (= G478), I471 (≠ V481), D472 (≠ E482)
- binding magnesium ion: D439 (= D449), N466 (= N476), G468 (= G478)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-(1-carboxy-1-hydroxyethyl)-5-(2-{[hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: A24 (≠ P40), G25 (= G41), D26 (= D42), E49 (= E64), V74 (= V89), H113 (= H128), G388 (= G398), D389 (= D399), G412 (≠ S422), H413 (≠ S423), I414 (= I424), G440 (= G450), S441 (≠ A451), N466 (= N476), G468 (= G478), Y469 (= Y479), T470 (≠ L480), I471 (≠ V481), D472 (≠ E482)
1zpdA Pyruvate decarboxylase from zymomonas mobilis (see paper)
35% identity, 96% coverage: 19:557/563 of query aligns to 3:551/565 of 1zpdA
- active site: D26 (= D42), Y27 (= Y43), E49 (= E64), Y72 (= Y87), H112 (= H127), H113 (= H128), L115 (≠ V130), G116 (≠ A131), C167 (≠ A180), Y289 (≠ L301), T387 (≠ P397), G412 (≠ S422), I414 (= I424), D439 (= D449), N466 (= N476), G468 (= G478), I471 (≠ V481), E472 (= E482)
- binding mono-{4-[(4-amino-2-methyl-pyrimidin-5-ylmethyl)-amino]-2-hydroxy-3-mercapto-pent-3-enyl-phosphono} ester: A24 (≠ P40), E49 (= E64), V74 (= V89), D389 (= D399), G412 (≠ S422), H413 (≠ S423), I414 (= I424), G438 (= G448), G440 (= G450), S441 (≠ A451), N466 (= N476), G468 (= G478), Y469 (= Y479), T470 (≠ L480), I471 (≠ V481), E472 (= E482)
- binding magnesium ion: D439 (= D449), N466 (= N476), G468 (= G478)
Q92345 Probable pyruvate decarboxylase C1F8.07c; EC 4.1.1.1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
33% identity, 96% coverage: 19:561/563 of query aligns to 10:558/569 of Q92345
- S233 (≠ P238) modified: Phosphoserine
- T521 (≠ H524) modified: Phosphothreonine
- S522 (≠ A525) modified: Phosphoserine
4cokB Functional and structural characterization of pyruvate decarboxylase from gluconoacetobacter diazotrophicus (see paper)
37% identity, 96% coverage: 19:557/563 of query aligns to 4:537/549 of 4cokB
- active site: G26 (= G41), D27 (= D42), Y28 (= Y43), N29 (vs. gap), E50 (= E64), T72 (= T86), H113 (= H127), H114 (= H128), L116 (≠ V130), G117 (≠ A131), C168 (≠ A180), A284 (≠ D302), E376 (= E396), T377 (≠ P397), G402 (≠ S422), I404 (= I424), D429 (= D449), N456 (= N476), G458 (= G478), I461 (≠ V481), E462 (= E482), R526 (≠ K546)
- binding magnesium ion: D429 (= D449), N456 (= N476), G458 (= G478)
- binding thiamine diphosphate: A25 (≠ P40), E50 (= E64), V75 (= V89), D379 (= D399), G402 (≠ S422), H403 (≠ S423), I404 (= I424), G428 (= G448), G430 (= G450), S431 (≠ A451), N456 (= N476), G458 (= G478), Y459 (= Y479), T460 (≠ L480), I461 (≠ V481), E462 (= E482)
5tmaA Zymomonas mobilis pyruvate decarboxylase mutant pdc-2.3 (see paper)
34% identity, 96% coverage: 19:557/563 of query aligns to 4:552/567 of 5tmaA
- active site: D27 (= D42), Y28 (= Y43), E50 (= E64), Y73 (= Y87), H113 (= H127), H114 (= H128), L116 (≠ V130), G117 (vs. gap), C168 (≠ A180), Y290 (≠ L301), T388 (≠ P397), G413 (≠ S422), D440 (= D449), N467 (= N476), G469 (= G478), I472 (≠ V481), E473 (= E482)
- binding magnesium ion: D440 (= D449), N467 (= N476), G469 (= G478)
- binding thiamine diphosphate: D390 (= D399), G413 (≠ S422), H414 (≠ S423), I415 (= I424), G439 (= G448), G441 (= G450), S442 (≠ A451), N467 (= N476), G469 (= G478), Y470 (= Y479), T471 (≠ L480), I472 (≠ V481), E473 (= E482)
5eujE Pyruvate decarboxylase (see paper)
33% identity, 97% coverage: 19:562/563 of query aligns to 3:552/556 of 5eujE
- active site: G25 (= G41), D26 (= D42), Y27 (= Y43), N28 (vs. gap), E49 (= E64), T71 (= T86), H112 (= H127), H113 (= H128), I115 (≠ V130), G116 (≠ A131), C167 (≠ A180), E263 (≠ G275), A290 (≠ D302), E382 (= E396), T383 (≠ P397), G408 (≠ S422), D435 (= D449), N462 (= N476), G464 (= G478), I467 (≠ V481), E468 (= E482)
- binding 1,2-ethanediol: Y289 (≠ L301), E468 (= E482)
- binding magnesium ion: D435 (= D449), N462 (= N476), G464 (= G478)
- binding thiamine diphosphate: A24 (≠ P40), E49 (= E64), V74 (= V89), G384 (= G398), D385 (= D399), G408 (≠ S422), H409 (≠ S423), I410 (= I424), G434 (= G448), G436 (= G450), S437 (≠ A451), N462 (= N476), G464 (= G478), Y465 (= Y479), V466 (≠ L480), I467 (≠ V481), E468 (= E482)
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)
33% identity, 96% coverage: 16:553/563 of query aligns to 2:549/563 of P06169
- S2 (≠ T16) modified: N-acetylserine
- R161 (≠ L172) modified: Omega-N-methylarginine
- D291 (= D300) mutation to N: In PDC1-8; reduces catalytic activity to 10% but retains autoregulatory activity.
- T390 (≠ D399) binding thiamine diphosphate
- GSI 413:415 (≠ SSI 422:424) binding thiamine diphosphate
- D444 (= D449) binding Mg(2+)
- GS 445:446 (≠ GA 450:451) binding thiamine diphosphate
- N471 (= N476) binding Mg(2+)
- NDGYTI 471:476 (≠ NDGYLV 476:481) binding thiamine diphosphate
- G473 (= G478) binding Mg(2+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1qpbA Pyruvate decarboyxlase from yeast (form b) complexed with pyruvamide (see paper)
32% identity, 96% coverage: 16:553/563 of query aligns to 1:548/555 of 1qpbA
- active site: L24 (≠ V39), G26 (= G41), D27 (= D42), F28 (≠ Y43), N29 (≠ V44), E50 (= E64), T72 (= T86), H113 (= H127), H114 (= H128), L116 (≠ V130), G117 (≠ A131), A168 (= A180), T265 (≠ G275), N292 (≠ D302), T387 (≠ P397), G412 (≠ S422), I414 (= I424), D443 (= D449), N470 (= N476), G472 (= G478), Y473 (= Y479), I475 (≠ V481), E476 (= E482), I479 (≠ L485), V541 (≠ K546)
- binding magnesium ion: D443 (= D449), N470 (= N476), G472 (= G478)
- binding pyruvamide: Y156 (≠ I168), H224 (≠ F234), D225 (≠ G235)
- binding thiamine diphosphate: P25 (= P40), E50 (= E64), V75 (= V89), T389 (≠ D399), I414 (= I424), G442 (= G448), G444 (= G450), S445 (≠ A451), N470 (= N476), G472 (= G478), Y473 (= Y479), T474 (≠ L480), I475 (≠ V481), E476 (= E482)
2vjyA Pyruvate decarboxylase from kluyveromyces lactis in complex with the substrate analogue methyl acetylphosphonate (see paper)
32% identity, 96% coverage: 16:555/563 of query aligns to 1:550/562 of 2vjyA
- active site: L24 (≠ V39), G26 (= G41), D27 (= D42), F28 (≠ Y43), N29 (≠ V44), E50 (= E64), T72 (= T86), H113 (= H127), H114 (= H128), L116 (≠ V130), G117 (≠ A131), A168 (= A180), T265 (≠ G275), N292 (≠ D302), T387 (≠ P397), G412 (≠ S422), I414 (= I424), D443 (= D449), N470 (= N476), G472 (= G478), Y473 (= Y479), I475 (≠ V481), E476 (= E482), I479 (≠ L485), T541 (≠ K546)
- binding methoxy-[(1~{R})-1-oxidanylethyl]phosphinic acid: G26 (= G41), D27 (= D42), H91 (≠ M105), H113 (= H127), H114 (= H128), C220 (≠ E230), H224 (≠ F234), G285 (= G295), A286 (= A296), F291 (≠ L301), H309 (≠ G319), S310 (≠ R320), E476 (= E482), I479 (≠ L485)
- binding methyl hydrogen (s)-acetylphosphonate: E17 (≠ G32), K64 (≠ N78), Y156 (≠ I168)
- binding magnesium ion: D443 (= D449), N470 (= N476), G472 (= G478)
- binding thiamine diphosphate: P25 (= P40), E50 (= E64), V75 (= V89), T389 (≠ D399), G412 (≠ S422), S413 (= S423), I414 (= I424), G442 (= G448), G444 (= G450), S445 (≠ A451), N470 (= N476), G472 (= G478), Y473 (= Y479), T474 (≠ L480), I475 (≠ V481), E476 (= E482)
Query Sequence
>WP_083768615.1 NCBI__GCF_000020385.1:WP_083768615.1
MTIQISDGRGHQEMPTESTVSTYLLQRLKELGVNHLFGVPGDYVLDFLDQVIESPLAWVG
TCNELNAGYAADGYARLNGLGGAVVTYGVGGFSILNAVAGAFAEMVPLVLISGAPPTGRR
KAGALVHHLVADYNRQLEIFQKVTVDAALLDNPETAPALIDRLLATCISRKLPVYLELPA
DMARAACLPPSAPLLPAARSSAPDSLKACADAAAALLNRAVNPAILAGIEVSRFGLGPAL
LQLVEQAELPFATMLSSKSVLPELHPQFIGLYQGGWSRPAVQQQIESADCLLSLGAWMTD
LDTGIFSIHIDPQRVIEVGRDAVRIGDRQYPDILPGDLIRELVPRLRPRSYLELHPGEPR
AACGAFVPDTATALTAARMYEAIHGFLDDSMILLAEPGDAFCAAPEFTIEEAERFIVQSF
YSSIGYCTPAALGARLARPGRRPVVMTGDGAFQMTAQEVSTLVRLQIPAVVLVINNDGYL
VERMLHEDGPYNDIRMWRYAALPELFNAGSGGLGIRVTTEGELHAALQTAAAAPDKLVLI
EMCVQKLDCSAGLRRLGATMRKG
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