glucosamine-6-phosphate deaminase [Listeria monocytogenes].

LOCUS       WP_009932532             234 aa            linear   BCT 03-JUN-2024
ACCESSION   WP_009932532
VERSION     WP_009932532.1
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 :: TIGR00502.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     gene            1..234
                     /gene="nagB"
     Protein         1..234
                     /product="glucosamine-6-phosphate deaminase"
                     /EC_number="3.5.99.6"
                     /GO_function="GO:0004342 - glucosamine-6-phosphate
                     deaminase activity [Evidence IEA]"
                     /GO_process="GO:0006044 - N-acetylglucosamine metabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=25380
     Region          11..234
                     /region_name="GlcN6P_deaminase"
                     /note="Glucosamine-6-phosphate (GlcN6P) deaminase
                     subfamily; GlcN6P deaminase catalyzes the reversible
                     conversion of GlcN6P to D-fructose-6-phosphate (Fru6P) and
                     ammonium. The reaction is an aldo-keto isomerization
                     coupled with an amination or deamination. It...; cd01399"
                     /db_xref="CDD:238693"
     Site            order(36..39,62..63,125..126,131,133,160,195)
                     /site_type="active"
                     /db_xref="CDD:238693"
     Site            order(138,140..141,149,203..209,217..219)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:238693"
     Site            order(139..140,146..149)
                     /site_type="active"
                     /note="allosteric site [active]"
                     /db_xref="CDD:238693"
     Site            order(151,154..164,167..169)
                     /site_type="active"
                     /note="active site lid [active]"
                     /db_xref="CDD:238693"
     Site            order(156,193,197,228,231..234)
                     /site_type="other"
                     /note="hexamer (dimer of trimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:238693"
ORIGIN      
        1 mqlittenkl agskkaleii ekgitsgevn tlglatgstp etlyaelvks dvdtknvttt
       61 nldeyvglaa sdpnsyhyym ndllfskkaf kesflpngea tdaeaecary eeilsehpid
      121 iqvlgigtng higfnepgts fdsithkvvl tdstreankr ffereedvpt haysmgiksi
      181 mnakkiilla fgenkaqaik etikgpvdvn cpasvlqnhp dvtvildnea asll