ribulose-phosphate 3-epimerase [Listeria monocytogenes].

LOCUS       WP_003722018             224 aa            linear   BCT 26-JUL-2024
ACCESSION   WP_003722018
VERSION     WP_003722018.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10087218
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..224
                     /product="ribulose-phosphate 3-epimerase"
                     /EC_number="5.1.3.1"
                     /GO_function="GO:0004750 - D-ribulose-phosphate
                     3-epimerase activity [Evidence IEA]"
                     /GO_function="GO:0046872 - metal ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=25119
     Region          3..213
                     /region_name="RPE"
                     /note="Ribulose-5-phosphate 3-epimerase (RPE). This enzyme
                     catalyses the interconversion of D-ribulose 5-phosphate
                     (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin
                     cycle (reductive pentose phosphate pathway) in
                     chloroplasts and in the oxidative pentose...; cd00429"
                     /db_xref="CDD:238244"
     Site            order(7,9,34,67,140..141,143..144,174,176,196,198)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238244"
     Site            order(14,17,37,39..40,42,44..47,70,74,95,97..98,116,119,
                     121,125,139,148,150,154)
                     /site_type="other"
                     /note="hexamer interface [polypeptide binding]"
                     /db_xref="CDD:238244"
     Site            order(32,34,65,174)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:238244"
ORIGIN      
        1 mrkiaasimc adqlhlgdel qrlesagvel lhcdvmdgvy vnnlalgpey leivrnntei
       61 pldihlatit plkyidmfgp vkpeyisfhv evaedvseii rkirsynvkp siainpetpi
      121 eaiypylddv emvlmmtvnp gfagqkfqtd vlqklhdlka klagkihapl ievdgninke
      181 tvglmrdclp diyvlgtsal fhdrdktsya erlvhiwsnv ekhv