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MULTISPECIES: UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate


LOCUS       WP_003113425             359 aa            linear   BCT 10-AUG-2020
            aminotransferase [Pseudomonas].
ACCESSION   WP_003113425
VERSION     WP_003113425.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Dow,G.T., Gilbert,M., Thoden,J.B. and Holden,H.M.
  TITLE     Structural investigation on WlaRG from Campylobacter jejuni: A
            sugar aminotransferase
  JOURNAL   Protein Sci. 26 (3), 586-599 (2017)
   PUBMED   28028852
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Larkin,A., Olivier,N.B. and Imperiali,B.
  TITLE     Structural analysis of WbpE from Pseudomonas aeruginosa PAO1: a
            nucleotide sugar aminotransferase involved in O-antigen assembly
  JOURNAL   Biochemistry 49 (33), 7227-7237 (2010)
   PUBMED   20604544
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Larkin,A. and Imperiali,B.
  TITLE     Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes
            in the Wbp pathway responsible for O-antigen assembly in
            Pseudomonas aeruginosa PAO1
  JOURNAL   Biochemistry 48 (23), 5446-5455 (2009)
   PUBMED   19348502
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Westman,E.L., McNally,D.J., Charchoglyan,A., Brewer,D., Field,R.A.
            and Lam,J.S.
  TITLE     Characterization of WbpB, WbpE, and WbpD and reconstitution of a
            pathway for the biosynthesis of
            UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas
            aeruginosa
  JOURNAL   J. Biol. Chem. 284 (18), 11854-11862 (2009)
   PUBMED   19282284
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Westman,E.L., Preston,A., Field,R.A. and Lam,J.S.
  TITLE     Biosynthesis of a rare di-N-acetylated sugar in the
            lipopolysaccharides of both Pseudomonas aeruginosa and Bordetella
            pertussis occurs via an identical scheme despite different gene
            clusters
  JOURNAL   J. Bacteriol. 190 (18), 6060-6069 (2008)
   PUBMED   18621892
REFERENCE   6  (residues 1 to 359)
  AUTHORS   Burrows,L.L., Charter,D.F. and Lam,J.S.
  TITLE     Molecular characterization of the Pseudomonas aeruginosa serotype
            O5 (PAO1) B-band lipopolysaccharide gene cluster
  JOURNAL   Mol. Microbiol. 22 (3), 481-495 (1996)
   PUBMED   8939432
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  :: BlastRule
            Evidence Accession :: NBR012676
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..359
                     /gene="wbpE"
     Protein         1..359
                     /product="UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate
                     aminotransferase"
                     /EC_number="2.6.1.98"
                     /calculated_mol_wt=38794
     Region          4..357
                     /region_name="WecE"
                     /note="dTDP-4-amino-4,6-dideoxygalactose transaminase
                     [Cell wall/membrane/envelope biogenesis]; COG0399"
                     /db_xref="CDD:440168"
ORIGIN      
        1 miefidlknq qarikdkida giqrvlrhgq yilgpevtel edrladfvga kyciscangt
       61 dalqivqmal gvgpgdevit pgftyvatae tvallgakpv yvdidprtyn ldpqlleaai
      121 tprtkaiipv slygqcadfd ainaiaskyg ipviedaaqs fgasykgkrs cnlstvacts
      181 ffpskplgcy gdggaiftnd delatairqi arhgqdrryh hirvgvnsrl dtlqaaillp
      241 kleifeeeia lrqkvaaeyd lslkqvgigt pfievnnisv yaqytvrmdn resvqaslka
      301 agvptavhyp iplnkqpava dekaklpvgd kaatqvmslp mhpyldtasi kiicaaltn