MULTISPECIES: D-allulose 6-phosphate 3-epimerase

FASTA View on NCBI
LOCUS       WP_004151641             229 aa            linear   BCT 24-FEB-2024
            [Enterobacterales].
ACCESSION   WP_004151641
VERSION     WP_004151641.1
KEYWORDS    RefSeq.
SOURCE      Enterobacterales
  ORGANISM  Enterobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Chan,K.K., Fedorov,A.A., Fedorov,E.V., Almo,S.C. and Gerlt,J.A.
  TITLE     Structural basis for substrate specificity in phosphate binding
            (beta/alpha)8-barrels: D-allulose 6-phosphate 3-epimerase from
            Escherichia coli K-12
  JOURNAL   Biochemistry 47 (36), 9608-9617 (2008)
   PUBMED   18700786
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Kim,C., Song,S. and Park,C.
  TITLE     The D-allose operon of Escherichia coli K-12
  JOURNAL   J Bacteriol 179 (24), 7631-7637 (1997)
   PUBMED   9401019
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 :: NF007266.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK09722
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Enterobacterales"
                     /db_xref="taxon:91347"
     gene            1..229
                     /gene="alsE"
     Protein         1..229
                     /product="D-allulose 6-phosphate 3-epimerase"
                     /calculated_mol_wt=25330
     Region          1..229
                     /region_name="PRK09722"
                     /note="allulose-6-phosphate 3-epimerase; Provisional"
                     /db_xref="CDD:236616"
     Site            order(8,10,34,67,141..142,144..145,175,177,197,199)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238244"
     Site            order(15,18,37,39..40,42,44..47,70,74,96,98..99,117,120,
                     122,126,140,149,151,155)
                     /site_type="other"
                     /note="hexamer interface [polypeptide binding]"
                     /db_xref="CDD:238244"
     Site            order(32,34,65,175)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:238244"
ORIGIN      
        1 mryylspslm cmdmmklteq lrflnskadr lhvdimdghy vknlalsasf vaqirpytsl
       61 pidvhlmvea pasfipalld agadafslhp eticreafrv inmlrqagke vgmvlnpatp
      121 vesiqhylhl ldkvtvmtvd pgyagqpfip emlakitqlh qlketgslrf llevdgscnr
      181 ntyrallgag aqilvmgssg lfradmplel awetmsrels aalhspelv