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LOCUS WP_000848004 302 aa linear BCT 20-NOV-2023 ACCESSION WP_000848004 VERSION WP_000848004.1 KEYWORDS RefSeq. SOURCE Escherichia ORGANISM Escherichia Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 302) AUTHORS Zhang,X., Carter,M.S., Vetting,M.W., San Francisco,B., Zhao,S., Al-Obaidi,N.F., Solbiati,J.O., Thiaville,J.J., de Crecy-Lagard,V., Jacobson,M.P., Almo,S.C. and Gerlt,J.A. TITLE Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars JOURNAL Proc Natl Acad Sci U S A 113 (29), E4161-E4169 (2016) PUBMED 27402745 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 :: NF043037.1 Evidence Source :: NCBIFAM ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..302 /organism="Escherichia" /db_xref="taxon:561" gene 1..302 /gene="ltnD" /GO_function="GO:0050661 - NADP binding [Evidence IEA]" /GO_function="GO:0051287 - NAD binding [Evidence IEA]" Protein 1..302 /product="L-threonate dehydrogenase" /EC_number="1.1.1.411" /GO_function="GO:0016616 - oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [Evidence IEA]" /GO_process="GO:0005975 - carbohydrate metabolic process [Evidence IEA]" /calculated_mol_wt=30620 Region 8..292 /region_name="MmsB" /note="3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism]; COG2084" /db_xref="CDD:441687" ORIGIN 1 mktgsefhvg ivglgsmgmg aalsyvragl stwgadlnsn acatlkeaga cgvsdnaatf 61 aekldallvl vvnaaqvkqv lfgetgvaqh lkpgtavmvs stiasadaqe iatalagfdl 121 emldapvsgg avkaangemt vmasgsdiaf erlapvleav agkvyrigae pglgstvkii 181 hqllagvhia agaeamalaa ragipldvmy dvvtnaagns wmfenrmrhv vdgdytphsa 241 vdifvkdlgl vadtakalhf plplastaln mftsasnagy gkeddsavik ifsgitlpga 301 ks