bifunctional glutamate N-acetyltransferase/amino-acid

LOCUS       WP_010989754             398 aa            linear   BCT 02-JUN-2019
            acetyltransferase ArgJ [Listeria monocytogenes].
ACCESSION   WP_010989754
VERSION     WP_010989754.1
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 :: NF003802.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK05388
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     gene            1..398
                     /gene="argJ"
     Protein         1..398
                     /product="bifunctional glutamate
                     N-acetyltransferase/amino-acid acetyltransferase ArgJ"
                     /EC_number="2.3.1.1"
                     /EC_number="2.3.1.35"
                     /GO_function="GO:0004358 - glutamate N-acetyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006526 - arginine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=42606
     Region          11..398
                     /region_name="OAT"
                     /note="Ornithine acetyltransferase (OAT) family; also
                     referred to as ArgJ. OAT catalyzes the first and fifth
                     steps in arginine biosynthesis, coupling acetylation of
                     glutamate with deacetylation of N-acetylornithine, which
                     allows recycling of the acetyl group in...; cd02152"
                     /db_xref="CDD:239065"
     Site            order(47..51,81,116..117,178,182,219..222,300..302,
                     305..306,308..309,311,313..316,318..319,322..325,343,
                     385..387)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:239065"
     Site            order(113..114,148..149,174,177,185,393,397..398)
                     /site_type="active"
                     /note="active site pocket [active]"
                     /db_xref="CDD:239065"
     Site            184..185
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:239065"
ORIGIN      
        1 melikgnias pkgfyadgkh aglkrkrndi gwiysevpan aaavytmnqm qaapifvtkd
       61 sfqsnaklqa iivnsgnana ctgnqgmlda lamraqtaek leipldsvav astgiigdml
      121 pmdkinagie mlekqtgnaa dfeeailttd tfqkqisfqt eiggrkvtms gvakgsgmih
      181 pnmatmlafi ttdaaipael lqkllkikvd ktfnqitvdg dtstndmvvv mangcaenpm
      241 lqegtadfak fadmfqavte hlaksiardg egatklievq vngatkteda rmiakkivss
      301 slvktaafgg dgnwgriica igysggrfap dnitikiggi eilnhssqti ynqqaldayl
      361 eeehiiievd lhiglesgta wgcdlsyeyv kinacyrt