MULTISPECIES: fructose-asparagine asparaginase [Klebsiella].

LOCUS       WP_004150784             347 aa            linear   BCT 13-JUL-2021
ACCESSION   WP_004150784
VERSION     WP_004150784.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
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="Klebsiella"
                     /db_xref="taxon:570"
     gene            1..347
                     /gene="fraE"
     Protein         1..347
                     /product="fructose-asparagine asparaginase"
                     /calculated_mol_wt=36669
     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 mnfrallaia lltmsslafs etrlphivil atggtiagsa asntqttgyk agaigvqtli
       61 navpemskia hvegeqvani gsenmtsdii lqlskrvnal larddvdgvv ithgtdtlde
      121 tpyflnltvk snkpvvftaa mrpataisad gpmnlleavt vaadpdargr gvmvvlndri
      181 gaarfvtktn atsldtfrap eegylgvvvg gkpqfetrvd kihtlrsvfd vrqlkvlpkv
      241 viiygyqddp eymydaaiah hadgiiyagt gagsvsvrsa agikkaqqag ivvvrasrtg
      301 sgvvppddsq pglvadslnp akarillmta ltqtkdpqli qqyfhty