SitesBLAST
Comparing BWI76_RS20520 FitnessBrowser__Koxy:BWI76_RS20520 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)
P23234 Indole-3-pyruvate decarboxylase; Indolepyruvate decarboxylase; EC 4.1.1.74 from Enterobacter cloacae (see paper)
63% identity, 100% coverage: 1:551/553 of query aligns to 1:551/552 of P23234
- E52 (= E52) binding
- D435 (= D435) binding
- N462 (= N462) binding
1ovmA Crystal structure of indolepyruvate decarboxylase from enterobacter cloacae (see paper)
64% identity, 99% coverage: 5:551/553 of query aligns to 3:535/535 of 1ovmA
- active site: G26 (= G28), D27 (= D29), Y28 (= Y30), N29 (= N31), E50 (= E52), T72 (= T74), H113 (= H115), H114 (= H116), L116 (= L118), G117 (= G119), A167 (= A169), S262 (≠ I264), L289 (≠ I291), Q367 (= Q383), G392 (= G408), I394 (= I410), D419 (= D435), N446 (= N462), G448 (= G464), V451 (= V467), E452 (= E468), I455 (= I471), K516 (= K532)
- binding magnesium ion: D419 (= D435), N446 (= N462), G448 (= G464)
- binding thiamine diphosphate: P25 (= P27), E50 (= E52), V75 (= V77), T369 (= T385), G392 (= G408), S393 (= S409), I394 (= I410), G418 (= G434), G420 (= G436), A421 (= A437), N446 (= N462), G448 (= G464), Y449 (= Y465), T450 (= T466), V451 (= V467), E452 (= E468)
2vbgA The complex structure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis with 2r-1-hydroxyethyl-deazathdp (see paper)
41% identity, 99% coverage: 5:550/553 of query aligns to 7:545/546 of 2vbgA
- active site: V28 (= V26), G30 (= G28), D31 (= D29), Y32 (= Y30), N33 (= N31), N53 (= N51), E54 (= E52), T76 (= T74), F115 (≠ L113), V116 (≠ L114), H117 (= H115), H118 (= H116), L120 (= L118), A121 (≠ G119), V171 (≠ A169), K259 (≠ I264), S286 (≠ I291), E375 (≠ D382), Q376 (= Q383), G401 (= G408), I403 (= I410), D428 (= D435), N455 (= N462), G457 (= G464), Y458 (= Y465), V460 (= V467), E461 (= E468), K527 (= K532)
- binding magnesium ion: D428 (= D435), N455 (= N462), G457 (= G464)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: P29 (= P27), E54 (= E52), V79 (= V77), H118 (= H116), G377 (= G384), T378 (= T385), G401 (= G408), S402 (= S409), I403 (= I410), G427 (= G434), G429 (= G436), S430 (≠ A437), N455 (= N462), G457 (= G464), Y458 (= Y465), T459 (= T466), V460 (= V467), E461 (= E468)
2vbfB The holostructure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis (see paper)
41% identity, 99% coverage: 5:550/553 of query aligns to 7:545/546 of 2vbfB
- active site: V28 (= V26), G30 (= G28), D31 (= D29), Y32 (= Y30), N33 (= N31), N53 (= N51), E54 (= E52), T76 (= T74), F115 (≠ L113), V116 (≠ L114), H117 (= H115), H118 (= H116), L120 (= L118), A121 (≠ G119), V171 (≠ A169), K259 (≠ I264), S286 (≠ I291), E375 (≠ D382), Q376 (= Q383), G401 (= G408), I403 (= I410), D428 (= D435), N455 (= N462), G457 (= G464), Y458 (= Y465), V460 (= V467), E461 (= E468), K527 (= K532)
- binding magnesium ion: D428 (= D435), N455 (= N462), G457 (= G464)
- binding thiamine diphosphate: P29 (= P27), E54 (= E52), V79 (= V77), G377 (= G384), T378 (= T385), G401 (= G408), S402 (= S409), I403 (= I410), G427 (= G434), G429 (= G436), S430 (≠ A437), N455 (= N462), G457 (= G464), Y458 (= Y465), T459 (= T466), V460 (= V467), E461 (= E468)
6vgsBBB Alpha-keto acid decarboxylase (see paper)
41% identity, 99% coverage: 5:550/553 of query aligns to 2:541/543 of 6vgsBBB
- active site: V23 (= V26), G25 (= G28), D26 (= D29), Y27 (= Y30), N28 (= N31), E49 (= E52), T71 (= T74), H112 (= H115), H113 (= H116), L115 (= L118), A116 (≠ G119), V166 (≠ A169), S282 (≠ I291), Q372 (= Q383), G397 (= G408), I399 (= I410), D424 (= D435), N451 (= N462), G453 (= G464), Y454 (= Y465), V456 (= V467), E457 (= E468)
- binding magnesium ion: D424 (= D435), N451 (= N462), G453 (= G464)
- binding thiamine diphosphate: P24 (= P27), E49 (= E52), V74 (= V77), T374 (= T385), I399 (= I410), G423 (= G434), G425 (= G436), S426 (≠ A437), N451 (= N462), G453 (= G464), Y454 (= Y465), T455 (= T466), V456 (= V467), E457 (= E468)
1qpbA Pyruvate decarboyxlase from yeast (form b) complexed with pyruvamide (see paper)
38% identity, 97% coverage: 6:539/553 of query aligns to 4:548/555 of 1qpbA
- active site: L24 (≠ V26), G26 (= G28), D27 (= D29), F28 (≠ Y30), N29 (= N31), E50 (= E52), T72 (= T74), H113 (= H115), H114 (= H116), L116 (= L118), G117 (= G119), A168 (= A169), T265 (≠ I264), N292 (≠ I291), T387 (≠ Q383), G412 (= G408), I414 (= I410), D443 (= D435), N470 (= N462), G472 (= G464), Y473 (= Y465), I475 (≠ V467), E476 (= E468), I479 (= I471), V541 (≠ K532)
- binding magnesium ion: D443 (= D435), N470 (= N462), G472 (= G464)
- binding pyruvamide: Y156 (≠ L157), H224 (≠ Y223), D225 (≠ G224)
- binding thiamine diphosphate: P25 (= P27), E50 (= E52), V75 (= V77), T389 (= T385), I414 (= I410), G442 (= G434), G444 (= G436), S445 (≠ A437), N470 (= N462), G472 (= G464), Y473 (= Y465), T474 (= T466), I475 (≠ V467), E476 (= E468)
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)
38% identity, 97% coverage: 6:539/553 of query aligns to 5:549/563 of P06169
- R161 (= R161) modified: Omega-N-methylarginine
- D291 (= D289) mutation to N: In PDC1-8; reduces catalytic activity to 10% but retains autoregulatory activity.
- T390 (= T385) binding
- GSI 413:415 (= GSI 408:410) binding
- D444 (= D435) binding
- GS 445:446 (≠ GA 436:437) binding
- N471 (= N462) binding
- NDGYTI 471:476 (≠ NEGYTV 462:467) binding
- G473 (= G464) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
2vk1A Crystal structure of the saccharomyces cerevisiae pyruvate decarboxylase variant d28a in complex with its substrate (see paper)
38% identity, 97% coverage: 6:539/553 of query aligns to 4:548/562 of 2vk1A
- active site: L24 (≠ V26), G26 (= G28), A27 (≠ D29), F28 (≠ Y30), N29 (= N31), E50 (= E52), T72 (= T74), H113 (= H115), H114 (= H116), L116 (= L118), G117 (= G119), A168 (= A169), T265 (≠ I264), N292 (≠ I291), T387 (≠ Q383), G412 (= G408), I414 (= I410), D443 (= D435), N470 (= N462), G472 (= G464), Y473 (= Y465), I475 (≠ V467), E476 (= E468), I479 (= I471), V541 (≠ K532)
- binding magnesium ion: D443 (= D435), N470 (= N462), G472 (= G464)
- binding pyruvic acid: A27 (≠ D29), H114 (= H116), C220 (≠ L219), G285 (= G284), A286 (≠ T285), H309 (≠ Q308), S310 (≠ P309)
- binding thiamine diphosphate: P25 (= P27), E50 (= E52), V75 (= V77), G388 (= G384), T389 (= T385), I414 (= I410), G442 (= G434), G444 (= G436), S445 (≠ A437), N470 (= N462), G472 (= G464), Y473 (= Y465), T474 (= T466), I475 (≠ V467), E476 (= E468)
2vjyA Pyruvate decarboxylase from kluyveromyces lactis in complex with the substrate analogue methyl acetylphosphonate (see paper)
38% identity, 99% coverage: 6:552/553 of query aligns to 4:561/562 of 2vjyA
- active site: L24 (≠ V26), G26 (= G28), D27 (= D29), F28 (≠ Y30), N29 (= N31), E50 (= E52), T72 (= T74), H113 (= H115), H114 (= H116), L116 (= L118), G117 (= G119), A168 (= A169), T265 (≠ I264), N292 (≠ I291), T387 (≠ Q383), G412 (= G408), I414 (= I410), D443 (= D435), N470 (= N462), G472 (= G464), Y473 (= Y465), I475 (≠ V467), E476 (= E468), I479 (= I471), T541 (≠ K532)
- binding methoxy-[(1~{R})-1-oxidanylethyl]phosphinic acid: G26 (= G28), D27 (= D29), H91 (= H93), H113 (= H115), H114 (= H116), C220 (≠ L219), H224 (≠ Y223), G285 (= G284), A286 (≠ T285), F291 (≠ T290), H309 (≠ Q308), S310 (≠ P309), E476 (= E468), I479 (= I471)
- binding methyl hydrogen (s)-acetylphosphonate: E17 (≠ G19), K64 (= K66), Y156 (≠ L157)
- binding magnesium ion: D443 (= D435), N470 (= N462), G472 (= G464)
- binding thiamine diphosphate: P25 (= P27), E50 (= E52), V75 (= V77), T389 (= T385), G412 (= G408), S413 (= S409), I414 (= I410), G442 (= G434), G444 (= G436), S445 (≠ A437), N470 (= N462), G472 (= G464), Y473 (= Y465), T474 (= T466), I475 (≠ V467), E476 (= E468)
6efhA Pyruvate decarboxylase from kluyveromyces lactis soaked with pyruvamide
38% identity, 97% coverage: 6:539/553 of query aligns to 4:548/557 of 6efhA
- active site: L24 (≠ V26), G26 (= G28), D27 (= D29), F28 (≠ Y30), N29 (= N31), E50 (= E52), T72 (= T74), H113 (= H115), H114 (= H116), L116 (= L118), G117 (= G119), A168 (= A169), T265 (≠ I264), N292 (≠ I291), T387 (≠ Q383), G412 (= G408), I414 (= I410), D443 (= D435), N470 (= N462), G472 (= G464), Y473 (= Y465), I475 (≠ V467), E476 (= E468), I479 (= I471), T541 (≠ K532)
- binding magnesium ion: D443 (= D435), N470 (= N462), G472 (= G464)
- binding (1S,2S)-1-amino-1,2-dihydroxypropan-1-olate: H91 (= H93), C220 (≠ L219), H224 (≠ Y223), G285 (= G284), A286 (≠ T285), H309 (≠ Q308), S310 (≠ P309)
- binding thiamine diphosphate: P25 (= P27), E50 (= E52), V75 (= V77), G388 (= G384), T389 (= T385), G412 (= G408), I414 (= I410), G444 (= G436), S445 (≠ A437), N470 (= N462), G472 (= G464), Y473 (= Y465), T474 (= T466), E476 (= E468)
2w93A Crystal structure of the saccharomyces cerevisiae pyruvate decarboxylase variant e477q in complex with the surrogate pyruvamide
38% identity, 97% coverage: 6:539/553 of query aligns to 4:534/544 of 2w93A
- active site: L24 (≠ V26), G26 (= G28), D27 (= D29), F28 (≠ Y30), N29 (= N31), E50 (= E52), T72 (= T74), H113 (= H115), H114 (= H116), L116 (= L118), G117 (= G119), A168 (= A169), T265 (≠ I264), T373 (≠ Q383), G398 (= G408), I400 (= I410), D429 (= D435), N456 (= N462), G458 (= G464), Y459 (= Y465), I461 (≠ V467), Q462 (≠ E468), I465 (= I471), V527 (≠ K532)
- binding magnesium ion: D429 (= D435), N456 (= N462), G458 (= G464)
- binding (1S,2S)-1-amino-1,2-dihydroxypropan-1-olate: D27 (= D29), H114 (= H116), C220 (≠ L219), H224 (≠ Y223), G285 (= G284), A286 (≠ T285), H295 (≠ F295), S296 (≠ T296)
- binding thiamine diphosphate: P25 (= P27), E50 (= E52), V75 (= V77), T375 (= T385), S399 (= S409), I400 (= I410), G428 (= G434), G430 (= G436), S431 (≠ A437), N456 (= N462), G458 (= G464), Y459 (= Y465), T460 (= T466), I461 (≠ V467), Q462 (≠ E468)
8hp4A Ctpdc complex
34% identity, 96% coverage: 6:536/553 of query aligns to 4:526/540 of 8hp4A
- binding magnesium ion: D423 (= D435), N451 (= N462), G453 (= G464)
- binding thiamine diphosphate: P25 (= P27), E50 (= E52), V77 (= V77), T369 (= T385), S393 (= S409), I394 (= I410), G422 (= G434), G424 (= G436), S425 (≠ A437), N451 (= N462), G453 (= G464), Y454 (= Y465), T455 (= T466), I456 (≠ V467)
5npuA Inferred ancestral pyruvate decarboxylase (see paper)
35% identity, 99% coverage: 4:552/553 of query aligns to 1:542/547 of 5npuA
- binding magnesium ion: D425 (= D435), N452 (= N462)
- binding thiamine diphosphate: D375 (≠ T385), G398 (= G408), H399 (≠ S409), I400 (= I410), G424 (= G434), D425 (= D435), S427 (≠ A437), N452 (= N462), G454 (= G464), Y455 (= Y465), T456 (= T466), I457 (≠ V467), E458 (= E468)
6efgD Pyruvate decarboxylase from kluyveromyces lactis
37% identity, 97% coverage: 6:539/553 of query aligns to 4:527/537 of 6efgD
- active site: L24 (≠ V26), G26 (= G28), D27 (= D29), F28 (≠ Y30), N29 (= N31), E50 (= E52), T72 (= T74), H104 (= H116), L106 (= L118), G107 (= G119), A158 (= A169), T255 (≠ I264), T366 (≠ Q383), G391 (= G408), I393 (= I410), D422 (= D435), N449 (= N462), G451 (= G464), Y452 (= Y465), I454 (≠ V467), E455 (= E468), I458 (= I471), T520 (≠ K532)
- binding magnesium ion: D422 (= D435), N449 (= N462), G451 (= G464)
- binding thiamine diphosphate: P25 (= P27), E50 (= E52), V75 (= V77), T368 (= T385), I393 (= I410), G421 (= G434), G423 (= G436), S424 (≠ A437), N449 (= N462), G451 (= G464), Y452 (= Y465), T453 (= T466), I454 (≠ V467), E455 (= E468)
Q06408 Transaminated amino acid decarboxylase; Thiamine diphosphate-dependent phenylpyruvate decarboxylase; PPDC; Thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase; 2ODC; Transaminated branched-chain amino acid decarboxylase; EC 4.1.1.-; EC 4.1.1.43; EC 4.1.1.72; EC 4.1.1.74; EC 4.1.1.80 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
32% identity, 99% coverage: 4:552/553 of query aligns to 24:635/635 of Q06408
- K588 (vs. gap) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Q92345 Probable pyruvate decarboxylase C1F8.07c; EC 4.1.1.1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
32% identity, 100% coverage: 2:552/553 of query aligns to 6:563/569 of Q92345
- S233 (≠ N227) modified: Phosphoserine
- T521 (≠ Q511) modified: Phosphothreonine
- S522 (≠ E512) modified: Phosphoserine
2vbiA Holostructure of pyruvate decarboxylase from acetobacter pasteurianus
32% identity, 99% coverage: 4:552/553 of query aligns to 1:552/554 of 2vbiA
- active site: G25 (= G28), D26 (= D29), Y27 (= Y30), N28 (= N31), E49 (= E52), T71 (= T74), H112 (= H115), H113 (= H116), I115 (≠ L118), G116 (= G119), C167 (≠ A169), S290 (≠ I291), T383 (≠ Q383), G408 (= G408), I410 (= I410), D435 (= D435), N462 (= N462), G464 (= G464), Y465 (= Y465), I467 (≠ V467), E468 (= E468), R532 (≠ K532)
- binding magnesium ion: D435 (= D435), N462 (= N462), G464 (= G464)
- binding thiamine diphosphate: A24 (≠ P27), E49 (= E52), V74 (= V77), D385 (≠ T385), G408 (= G408), H409 (≠ S409), I410 (= I410), G434 (= G434), D435 (= D435), G436 (= G436), S437 (≠ A437), N462 (= N462), G464 (= G464), Y465 (= Y465), V466 (≠ T466), I467 (≠ V467)
4cokB Functional and structural characterization of pyruvate decarboxylase from gluconoacetobacter diazotrophicus (see paper)
34% identity, 99% coverage: 4:552/553 of query aligns to 2:546/549 of 4cokB
- active site: G26 (= G28), D27 (= D29), Y28 (= Y30), N29 (= N31), E50 (= E52), T72 (= T74), H113 (= H115), H114 (= H116), L116 (= L118), G117 (= G119), C168 (≠ A169), A284 (≠ I291), E376 (≠ D382), T377 (≠ Q383), G402 (= G408), I404 (= I410), D429 (= D435), N456 (= N462), G458 (= G464), I461 (≠ V467), E462 (= E468), R526 (≠ K532)
- binding magnesium ion: D429 (= D435), N456 (= N462), G458 (= G464)
- binding thiamine diphosphate: A25 (≠ P27), E50 (= E52), V75 (= V77), D379 (≠ T385), G402 (= G408), H403 (≠ S409), I404 (= I410), G428 (= G434), G430 (= G436), S431 (≠ A437), N456 (= N462), G458 (= G464), Y459 (= Y465), T460 (= T466), I461 (≠ V467), E462 (= E468)
5eujE Pyruvate decarboxylase (see paper)
32% identity, 99% coverage: 5:552/553 of query aligns to 2:552/556 of 5eujE
- active site: G25 (= G28), D26 (= D29), Y27 (= Y30), N28 (= N31), E49 (= E52), T71 (= T74), H112 (= H115), H113 (= H116), I115 (≠ L118), G116 (= G119), C167 (≠ A169), E263 (≠ I264), A290 (≠ I291), E382 (≠ D382), T383 (≠ Q383), G408 (= G408), D435 (= D435), N462 (= N462), G464 (= G464), I467 (≠ V467), E468 (= E468)
- binding 1,2-ethanediol: Y289 (≠ T290), E468 (= E468)
- binding magnesium ion: D435 (= D435), N462 (= N462), G464 (= G464)
- binding thiamine diphosphate: A24 (≠ P27), E49 (= E52), V74 (= V77), G384 (= G384), D385 (≠ T385), G408 (= G408), H409 (≠ S409), I410 (= I410), G434 (= G434), G436 (= G436), S437 (≠ A437), N462 (= N462), G464 (= G464), Y465 (= Y465), V466 (≠ T466), I467 (≠ V467), E468 (= E468)
P06672 Pyruvate decarboxylase; PDC; EC 4.1.1.1 from Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) (see 2 papers)
33% identity, 99% coverage: 4:552/553 of query aligns to 2:561/568 of P06672
- E50 (= E52) mutation to Q: Almost complete loss of activity.
Query Sequence
>BWI76_RS20520 FitnessBrowser__Koxy:BWI76_RS20520
MQPTYTIGDYLLDRLVDCGIDRLFGVPGDYNLQFLDSVIAHRNLGWVGCANELNAAYAAD
GYARIKGAGALLTTYGVGELSALNGIAGSYAEHVPVLHIVGAPCTGAQQRGELLHHTLGD
GDFSHFSRMSEQITCSQAVLAAGNACHEIDRVLSEMLTHHRPGYLMLPADVAKAKTTPPA
HRLLIQGLPADENQLAGFREHAGRMLRSSRRVSLLADFLAQRYGLQNALREWVAKVPVAY
ATMLMGKGLFDEQQSGFVGTYSGIASAEETRDAIENADTIICIGTRFTDTITAGFTQHLP
LEKTIEIQPFAVRVADRWFSRIPMEKALAILIELSASLAAEWVSPNIQAPGVSGAPEGSL
TQKNFWNTVQKQLRPGDIILADQGTAAFGAAALKLPVDATLIVQPLWGSIGFTLPAAYGA
QIAAAERRVVLIVGDGAAQLTIQELGSMLRDKQRPLILLLNNEGYTVERAIHGPEQRYND
IALWDWNRLPDAFAPDVPSRCWRVTRTQELQEAMNSSVASDRLTLVEVMLPKMDIPDFLR
TVTQALEERNSRV
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