Searching in Acidimicrobium ferrooxidans DSM 10331 (GCF_000023265.1)
Found 8 curated entries in PaperBLAST's database that match '2.5.1.65' as complete word(s).
These curated entries have 5 distinct sequences.
Running ublast with E ≤ 0.01
Found 3 relevant proteins in Acidimicrobium ferrooxidans DSM 10331, or try another query
| cysK AFER_RS06875 Afer_1336 WP_015798746.1: cysteine synthase A is similar to: | PaperBLAST |
CS1 / A2EI82: O-phosphoserine sulfhydrylase monomer (EC 2.5.1.47; EC 2.5.1.65) from Trichomonas vaginalis | 44% id, 99% cov |
P9WP53: [CysO sulfur-carrier protein]-thiocarboxylate-dependent cysteine synthase (EC 2.5.1.113); O-phosphoserine sulfhydrylase (EC 2.5.1.65) from Mycobacterium tuberculosis | 39% id, 96% cov |
cysK / Q5JIZ7: O-phosphoserine sulfhydrylase monomer (EC 2.5.1.65) from Thermococcus kodakarensis | 34% id, 97% cov |
| AFER_RS01390 Afer_0269 WP_015797743.1: cysteine synthase family protein is similar to: | PaperBLAST |
CS1 / A2EI82: O-phosphoserine sulfhydrylase monomer (EC 2.5.1.47; EC 2.5.1.65) from Trichomonas vaginalis | 40% id, 97% cov |
P9WP53: [CysO sulfur-carrier protein]-thiocarboxylate-dependent cysteine synthase (EC 2.5.1.113); O-phosphoserine sulfhydrylase (EC 2.5.1.65) from Mycobacterium tuberculosis | 37% id, 99% cov |
cysK / Q5JIZ7: O-phosphoserine sulfhydrylase monomer (EC 2.5.1.65) from Thermococcus kodakarensis | 29% id, 96% cov |
| thrC AFER_RS09355 Afer_1812 WP_015799203.1: threonine synthase is similar to: | PaperBLAST |
CS1 / A2EI82: O-phosphoserine sulfhydrylase monomer (EC 2.5.1.47; EC 2.5.1.65) from Trichomonas vaginalis | 26% id, 97% cov |
P9WP53: [CysO sulfur-carrier protein]-thiocarboxylate-dependent cysteine synthase (EC 2.5.1.113); O-phosphoserine sulfhydrylase (EC 2.5.1.65) from Mycobacterium tuberculosis | 28% id, 76% 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