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tRNA-dihydrouridine synthase, partial [Klebsiella pneumoniae].


LOCUS       WP_014343074             232 aa            linear   BCT 02-MAR-2025
ACCESSION   WP_014343074
VERSION     WP_014343074.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group;
            Klebsiella; Klebsiella pneumoniae complex.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Xing,F., Martzen,M.R. and Phizicky,E.M.
  TITLE     A conserved family of Saccharomyces cerevisiae synthases effects
            dihydrouridine modification of tRNA
  JOURNAL   RNA 8 (3), 370-381 (2002)
   PUBMED   12003496
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 :: NF013380.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF01207.23
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: incomplete on both ends.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     Protein         <1..>232
                     /product="tRNA-dihydrouridine synthase"
                     /GO_function="GO:0017150 - tRNA dihydrouridine synthase
                     activity [Evidence IEA]"
                     /GO_function="GO:0050660 - flavin adenine dinucleotide
                     binding [Evidence IEA]"
                     /GO_process="GO:0008033 - tRNA processing [Evidence IEA]"
     Region          <1..204
                     /region_name="TIM-like beta/alpha barrel domains"
                     /note="A large family of domains similar to triose
                     phosphate isomerase (TIM) which, in general, share an
                     eight beta/alpha closed barrel structure; cl21457"
                     /db_xref="CDD:473867"
     Site            order(166..167,189..190)
                     /site_type="other"
                     /note="phosphate binding site [ion binding]"
                     /db_xref="CDD:240073"
ORIGIN      
        1 mafhdgdrap aelshadmar ikaafvasal raqrlgfeli elhaahgyll hqflsplsnq
       61 rrdeyggsle nrmryplevf kaireavgnt mavgvrlsat dwveggwdce qsikfsqqle
      121 tlgsdyihvs sgglspqqai avgpgyqlpf ardirqqvai pvigvglitd pqqaeaalen
      181 gdadlialar avlydphwpw haaaslgaqv rvpsqylrse phglkgtllp nr