5-methyltetrahydropteroyltriglutamate--homocysteine

LOCUS       WP_009930625             367 aa            linear   BCT 11-APR-2024
            S-methyltransferase [Listeria monocytogenes].
ACCESSION   WP_009930625
VERSION     WP_009930625.1
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  :: HMM
            Evidence Accession :: NF005085.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK06520
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..367
                     /product="5-methyltetrahydropteroyltriglutamate--
                     homocysteine S-methyltransferase"
                     /EC_number="2.1.1.14"
                     /GO_function="GO:0003871 -
                     5-methyltetrahydropteroyltriglutamate-homocysteine
                     S-methyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_process="GO:0009086 - methionine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=41675
     Region          1..365
                     /region_name="URO-D_CIMS_like"
                     /note="The URO-D_CIMS_like protein superfamily includes
                     bacterial and eukaryotic uroporphyrinogen decarboxylases
                     (URO-D), coenzyme M methyltransferases and other putative
                     bacterial methyltransferases, as well as cobalamine (B12)
                     independent methionine synthases; cl00464"
                     /db_xref="CDD:469779"
     Site            order(12..14,65,71,185,187,237,239,334..335)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:239427"
     Site            order(237,239,272,334)
                     /site_type="other"
                     /note="zinc-binding site [ion binding]"
                     /db_xref="CDD:239427"
ORIGIN      
        1 mnqvapfyad hvgsilrtkg ikdarekfqs geitalelrk ienteikyiv ekqkevglks
       61 itdgefrraw whfdflenld gvegydaagg iqfskvqtks hsvkitgpid ftthpfiedf
      121 iflkeavgdn hvakqtipsp amlhyrgdie yqpylddaek fandlatayq kaiqafydag
      181 crylqlddts wsylcsdeqr evvrqrgfdp etlqetyknl ineaikhkpa dmvitmhicr
      241 gnfrstwiae ggygpvaetl fgklnidgff leydnersgd faplkyvtrp dlkivlglit
      301 sktgeledea aikarieeas eivplsqlrl spqcgfaste egnilteeeq wdklryvvrl
      361 andiwge