phospho-sugar mutase [Listeria monocytogenes].

LOCUS       WP_010989599             557 aa            linear   BCT 26-MAR-2023
ACCESSION   WP_010989599
VERSION     WP_010989599.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 557)
  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..557
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..557
                     /product="phospho-sugar mutase"
                     /EC_number="5.4.2.-"
                     /GO_function="GO:0016868 - intramolecular transferase
                     activity, phosphotransferases [Evidence IEA]"
                     /calculated_mol_wt=61816
     Region          37..550
                     /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(40,42,45,139..141,149,294,296,298..299,345,366..368,
                     390,392,394,519,521..523,528)
                     /site_type="active"
                     /db_xref="CDD:100092"
     Site            order(42,139,299,345,366,368,390,392,394,519,521..523,528)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100092"
     Site            order(139,294,296,298)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:100092"
ORIGIN      
        1 mtwkhylsaw qnadlsnewr relqrveeeq erfdgyltfg tggmrgkmgi gtkrinlfti
       61 rrvakglgdy vvanegaemg vaiafdsrhh sgafaqetak vlaaqginvy lsdsirptpa
      121 lsfcvrekga fagvvitash npsiyngfkv ydkngcqitl gvaqeiagyl ekitdiftip
      181 vrelpnplvt plgkemdday lnaltavvsr pdlladygne lricytplhg agkelvmrgl
      241 lengfsetti iaeqsepdgd fptvispnpe eensfdlakk lakeiqadii latdpdadrl
      301 gvavlnkqat yqiltgnqlg alllnyilea ktpvtgadtm intivtgdlg gkiaydfgin
      361 hiqtltgfkf igekiaemeg teknflfgye esygyliapf vrdkdavqaa lltaemalfy
      421 kkegttllgk ltnlfekfgy hkeylhtitl ddsdgitkmi qvidalrkep ifmpeitvve
      481 dfltskrtnf vtmevtniel pkenvlkfyl mdsswfairp sgtepkckiy fqtsgeteei
      541 atkamnelrk rvlavwd