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LOCUS WP_003113831 469 aa linear BCT 20-NOV-2023 ACCESSION WP_003113831 VERSION WP_003113831.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 469) AUTHORS Parsot,C. TITLE Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase JOURNAL EMBO J 5 (11), 3013-3019 (1986) PUBMED 3098560 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: TIGR00260.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..469 /organism="Pseudomonas" /db_xref="taxon:286" gene 1..469 /gene="thrC" Protein 1..469 /product="threonine synthase" /EC_number="4.2.3.1" /GO_function="GO:0004795 - threonine synthase activity [Evidence IEA]" /GO_process="GO:0009088 - threonine biosynthetic process [Evidence IEA]" /calculated_mol_wt=51664 Region 2..458 /region_name="Thr-synth_2" /note="Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria; cd01560" /db_xref="CDD:107203" Site order(112,255..256,410) /site_type="other" /note="pyridoxal 5'-phosphate binding site [chemical binding]" /db_xref="CDD:107203" Site 112 /site_type="active" /note="catalytic residue [active]" /db_xref="CDD:107203" ORIGIN 1 mryistrgqa palnfedvll aglasdggly vpenlprftl eeiaswvglp yhelafrvmr 61 pfvagsiada dfkkileety gvfahdavap lrqlngnewv lelfhgptla fkdfalqllg 121 rlldhvlakr gervvimgat sgdtgsaaie gcrrcdnvdi fimhphnrvs evqrrqmtti 181 lgdnihniai egnfddcqem vkasfadqgf lkgtrlvavn sinwarimaq ivyyfhaalq 241 lgaphrsvaf svptgnfgdi fagylarnmg lpvsqlivat nrndilhrfm sgnrydkdtl 301 hpslspsmdi mvssnferll fdlhgrngka vaelldafka sgklsvedqr wtearklfds 361 lavsdeqtce tiaevyrssg elldphtaig vraarecrrs lsvpmvtlgt ahpvkfpeav 421 ekagigqapa lpahladlfe reerctvlpn elakvqafvs qhgnrgkpl