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MULTISPECIES: xanthosine phosphorylase [Enterobacteriaceae].


LOCUS       WP_000084573             277 aa            linear   BCT 03-JUN-2024
ACCESSION   WP_000084573
VERSION     WP_000084573.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Seeger,C., Poulsen,C. and Dandanell,G.
  TITLE     Identification and characterization of genes (xapA, xapB, and xapR)
            involved in xanthosine catabolism in Escherichia coli
  JOURNAL   J Bacteriol 177 (19), 5506-5516 (1995)
   PUBMED   7559336
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 :: TIGR01699.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..277
                     /gene="xapA"
     Protein         1..277
                     /product="xanthosine phosphorylase"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004731 - purine-nucleoside phosphorylase
                     activity [Evidence IEA]"
                     /GO_process="GO:0055086 - nucleobase-containing small
                     molecule metabolic process [Evidence IEA]"
                     /calculated_mol_wt=29704
     Region          13..276
                     /region_name="PRK08202"
                     /note="purine nucleoside phosphorylase; Provisional"
                     /db_xref="CDD:236183"
     Site            order(33..34,85,87,89,115..119,191,196..197,202,213..216,
                     238..241,249,251,254)
                     /site_type="active"
                     /db_xref="CDD:350160"
     Site            order(33..34,65,85,87,116..117,216)
                     /site_type="other"
                     /note="phosphate binding site [ion binding]"
                     /db_xref="CDD:350160"
     Site            order(34,87,89,117..119,196..197,213..215,238..239,251,
                     254)
                     /site_type="other"
                     /note="purine nucleoside binding site [chemical binding]"
                     /db_xref="CDD:350160"
     Site            order(88..92,134..140,142..143,145..146,157..163,166,169,
                     173,187,190..201,203..204,206..208,215,222,242,247..249,
                     251)
                     /site_type="other"
                     /note="homotrimer interface [polypeptide binding]"
                     /db_xref="CDD:350160"
ORIGIN      
        1 msqvqfshnp lfcidiikty kpdftprvaf ilgsglgala dqienavais yeklpgfpvs
       61 tvhghagelv lghlqgvpvv cmkgrghfye grgmtimtda irtfkllgce llfctnaags
      121 lrpevgagsl valkdhintm pgtpmvglnd drfgerffsl anaydaeyra llqkvakeeg
      181 fpltegvfvs ypgpnfetaa eirmmqiigg dvvgmsvvpe visarhcdlk vvavsaitnm
      241 aeglsdvkls haqtlaaael skqnfinlic gflrkia