Searching in Paramagnetospirillum magneticum AMB-1 (GCF_000009985.1)
Found 50 curated entries in PaperBLAST's database that match '4.3.1.17'.
These curated entries have 35 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Paramagnetospirillum magneticum AMB-1, or try another query
| AMB_RS09340 amb1847 WP_011384252.1: cystathionine beta-synthase is similar to: | PaperBLAST |
TSAL_THEMA / Q9WYJ1: L-threonine ammonia-lyase; L-serine ammonia-lyase; Threonine dehydratase; EC 4.3.1.19; EC 4.3.1.17 from Thermotoga maritima | 27% id, 83% cov |
B1N2N4: L-serine ammonia-lyase (EC 4.3.1.17) from Entamoeba histolytica | 24% id, 86% cov |
| cysK AMB_RS01005 amb0199 WP_011382646.1: cysteine synthase A is similar to: | PaperBLAST |
SRR_ORYSJ / Q7XSN8: Serine racemase; D-serine dehydratase; D-serine ammonia-lyase; L-serine dehydratase; L-serine ammonia-lyase; EC 5.1.1.18; EC 4.3.1.18; EC 4.3.1.17 from Oryza sativa | 23% id, 81% cov |
SDSL_MOUSE / Q8R238: Serine dehydratase-like; L-serine deaminase; L-serine dehydratase/L-threonine deaminase; L-threonine dehydratase; TDH; SDH; EC 4.3.1.17; EC 4.3.1.19 from Mus musculus | 24% id, 73% cov |
SDSL_HUMAN / Q96GA7: Serine dehydratase-like; L-serine deaminase; L-serine dehydratase/L-threonine deaminase; L-threonine dehydratase; TDH; Serine dehydratase 2; SDH 2; EC 4.3.1.19; EC 4.3.1.17 from Homo sapiens | 28% id, 56% cov |
| AMB_RS06615 amb1300 WP_043743637.1: cysteine synthase A is similar to: | PaperBLAST |
O57809: L-serine ammonia-lyase (EC 4.3.1.17); D-Serine ammonia-lyase (EC 4.3.1.18) from Pyrococcus horikoshii | 26% id, 60% cov |
| trpB AMB_RS20295 amb4010 WP_011386363.1: tryptophan synthase subunit beta is similar to: | PaperBLAST |
B1N2N4: L-serine ammonia-lyase (EC 4.3.1.17) from Entamoeba histolytica | 34% id, 15% 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 3 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory