LOCUS       WP_002261877             397 aa            linear   BCT 18-JUN-2019
DEFINITION  bifunctional ornithine acetyltransferase/N-acetylglutamate synthase
            [Streptococcus mutans].
ACCESSION   WP_002261877
VERSION     WP_002261877.1
KEYWORDS    RefSeq.
SOURCE      Streptococcus mutans
  ORGANISM  Streptococcus mutans
            Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
            Streptococcus.
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 :: TIGR00120.1
            Evidence Source    :: JCVI
            Source Identifier  :: TIGR00120
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Streptococcus mutans"
                     /db_xref="taxon:1309"
     gene            1..397
                     /gene="argJ"
     Protein         1..397
                     /product="bifunctional ornithine
                     acetyltransferase/N-acetylglutamate synthase"
                     /EC_number="2.3.1.1"
                     /EC_number="2.3.1.35"
                     /calculated_mol_wt=42288
     Region          11..397
                     /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..117,177,181,218..221,299..301,
                     304..305,307..308,310,312..315,317..318,321..324,342,
                     384..386)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:239065"
     Site            order(113..114,147..148,173,176,184,392,396..397)
                     /site_type="active"
                     /note="active site pocket [active]"
                     /db_xref="CDD:239065"
     Site            183..184
                     /site_type="cleavage"
                     /db_xref="CDD:239065"
ORIGIN      
        1 mkiidgnias plgfsadglh agfkkrkkdf gwivsevpas vagvyttnkv iaaplivtre
       61 svkkaqkmqa lvvnsgvans ctglqgmeda ytmqkwtatk lkiapelvgv astgvigdlm
      121 pmdtlqkgls klvvngnsdd faqailttdt kvktvavteq fgrdevtmag vakgsgmihp
      181 nmatmlafit cdavissetl qlalsqnvet tfnqitvdgd tstndmvlvl sngctlnkei
      241 lpdtpefdkf samlhfvmqe lakkiakdge gatklievev inapnsldac mmaksvvgss
      301 lvktaifged pnwgrilaav gyagvdvpvd nidiyladip vmlasspvdf deedmqdvmr
      361 adtikiivdl hagdsvgkaw gcdlsydyvk inalyrt
//