Searching in Stenotrophomonas chelatiphaga DSM 21508 (GCF_001431535.1)
Found 15 curated entries in PaperBLAST's database that match '4.1.1.43' as complete word(s).
These curated entries have 9 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Stenotrophomonas chelatiphaga DSM 21508, or try another query
ABB28_RS13320 ABB28_13360 WP_057509083.1: alpha-ketoacid dehydrogenase subunit beta is similar to: | PaperBLAST |
ppdcβ / G1UHX5: phenylpyruvate decarboxylase β subunit (EC 4.1.1.43) from Streptomyces virginiae | 47% id, 97% cov |
pdhA ABB28_RS13325 ABB28_13365 WP_057509084.1: pyruvate dehydrogenase (acetyl-transferring) E1 component subunit alpha is similar to: | PaperBLAST |
ppdcα / A0A222AKA3: phenylpyruvate decarboxylase α subunit (EC 4.1.1.43) from Streptomyces virginiae | 36% id, 87% cov |
ilvG ABB28_RS14475 ABB28_14515 WP_057509298.1: acetolactate synthase 2 catalytic subunit is similar to: | PaperBLAST |
ipdC / P51852: phenylpyruvate decarboxylase (EC 4.1.1.43) from Azospirillum brasilense | 26% id, 93% cov |
ARO10_YEAST / 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 | 26% id, 25% cov |
ABB28_RS02940 ABB28_02955 WP_057507191.1: acetolactate synthase large subunit is similar to: | PaperBLAST |
Q2UKV4: phenylpyruvate decarboxylase (EC 4.1.1.43) from Aspergillus oryzae | 25% id, 89% cov |
PDC6_YEAST / P26263: Pyruvate decarboxylase isozyme 3; 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 | 30% id, 16% cov |
The hits are sorted by %identity * %coverage (highest first)
Running ublast against the 6-frame translation. All reading frames of at least 30 codons are included.
Found hits to 4 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory