phospho-sugar mutase [Listeria monocytogenes].

LOCUS       WP_010990002             576 aa            linear   BCT 26-MAR-2023
ACCESSION   WP_010990002
VERSION     WP_010990002.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Shackelford,G.S., Regni,C.A. and Beamer,L.J.
  TITLE     Evolutionary trace analysis of the alpha-D-phosphohexomutase
            superfamily
  JOURNAL   Protein Sci 13 (8), 2130-2138 (2004)
   PUBMED   15238632
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 10146591
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..576
                     /product="phospho-sugar mutase"
                     /EC_number="5.4.2.-"
                     /GO_function="GO:0016868 - intramolecular transferase
                     activity, phosphotransferases [Evidence IEA]"
                     /calculated_mol_wt=63983
     Region          41..568
                     /region_name="PGM2"
                     /note="This CD includes PGM2 (phosphoglucomutase 2) and
                     PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2
                     is thought to be a phosphopentomutase that catalyzes the
                     conversion of the nucleoside breakdown products,
                     ribose-1-phosphate and...; cd05799"
                     /db_xref="CDD:100092"
     Site            order(45,47,50,146..148,156,305,307,309..310,359,380..382,
                     405,407,409,537,539..541,546)
                     /site_type="active"
                     /db_xref="CDD:100092"
     Site            order(47,146,310,359,380,382,405,407,409,537,539..541,546)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100092"
     Site            order(146,305,307,309)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:100092"
ORIGIN      
        1 mnwqeeyqkw vandkldstl rkqltnmetn ekeledsfyr nmefgtagmr gvlgagtnrm
       61 niytirkasl glaqfvaeng eeakkrgivi aydprhmsre fafesaavlg hhgvksyvfd
      121 alrptpelsf avrhlnafgg ivitashnpp eyngykiyge dggqmpptga savieyinav
      181 edifsvevan qelliengll evisekvdrp yleklkeviv nkelvqerge dlkivftplh
      241 gtggilgvpa lesvgftniv kvdeqfvndp dfgtvkspnp enreafllai eygkkfggdi
      301 lvgtdpdadr lgvavrnadg eyevlsgnqi gaiilhyllk qkkaqselpa naavlksivt
      361 snlgteiakh ygaemievlt gfkfiaeqik hfeetgkhtf efgyeesngy mvkpftrdkd
      421 aiqavlaiae valvskvagr tlledldqiy defgyynedl vsltlsgkdg serikeitss
      481 freqlptsmg gfvveraedy lrsettwiat gkteaihlpt advikcyfed gswfclrpsg
      541 tepkikfyfs irgeskeest aklekvkadl mqhiea