MULTISPECIES: fructose-asparagine asparaginase [Salmonella].

LOCUS       WP_000702755             347 aa            linear   BCT 13-JUL-2021
ACCESSION   WP_000702755
VERSION     WP_000702755.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Sabag-Daigle,A., Sengupta,A., Blunk,H.M., Biswas,P.K., Cron,M.C.,
            Bogard,A.J., Behrman,E.J., Gopalan,V. and Ahmer,B.M.M.
  TITLE     Salmonella FraE, an Asparaginase Homolog, Contributes to
            Fructose-Asparagine but Not Asparagine Utilization
  JOURNAL   J Bacteriol 199 (22), e00330-17 (2017)
   PUBMED   28847920
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Ali,M.M., Newsom,D.L., Gonzalez,J.F., Sabag-Daigle,A., Stahl,C.,
            Steidley,B., Dubena,J., Dyszel,J.L., Smith,J.N., Dieye,Y.,
            Arsenescu,R., Boyaka,P.N., Krakowka,S., Romeo,T., Behrman,E.J.,
            White,P. and Ahmer,B.M.
  TITLE     Fructose-asparagine is a primary nutrient during growth of
            Salmonella in the inflamed intestine
  JOURNAL   PLoS Pathog 10 (6), e1004209 (2014)
   PUBMED   24967579
  REMARK    Publication Status: Online-Only
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 :: NBR014532
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     gene            1..347
                     /gene="fraE"
     Protein         1..347
                     /product="fructose-asparagine asparaginase"
                     /calculated_mol_wt=36803
     Region          1..347
                     /region_name="L-asparaginase_like"
                     /note="Bacterial L-asparaginases and related enzymes;
                     cl00216"
                     /db_xref="CDD:469665"
     Site            order(34..35,81..83,114..116,140,188,274)
                     /site_type="active"
                     /db_xref="CDD:199208"
     Site            order(35,83..87,90,116,120,142,147..149,152..153,177..178,
                     182,184,188..191,193,203..205,207,209,214,216..218,
                     220..221,242,244,246,250,252,260,262,270..272,274,276,
                     297..298,305..306)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:199208"
     Site            order(83..87,90,116..117,119..121,188..192,240..242,244,
                     246,250,252..253,256..257,260,262,270..272,274..276,
                     297..299,302..303,320..321,324)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:199208"
ORIGIN      
        1 mkirvfmatv lllishcvfs ttslphivil atggtiagta anntqtagyk sgelgvqtli
       61 navpemnnia rvdgeqvani gsenmtsdii lklsqkvnal larddvdgvv ithgtdtlde
      121 tayflnltvk sdkpvvftaa mrpasaisad gamnlleavt vaadpnakgr gvmvvlndri
      181 gsarfvtktn attldtfkap eegylgvivn gqpqfetrve kihtlrsvfd vrnikklpnv
      241 viiygyqddp eymydaaiah hadgiiyagt gagsvsvrsd agikkaekag iivvrasrtg
      301 ngvvpldkgq pglvsdslnp akarvllmta ltqtrnpeli qsyfsty