MULTISPECIES: bifunctional acetylornithine/succinyldiaminopimelate

LOCUS       WP_000190023             405 aa            linear   BCT 20-JAN-2025
            transaminase [Salmonella].
ACCESSION   WP_000190023
VERSION     WP_000190023.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Ledwidge,R. and Blanchard,J.S.
  TITLE     The dual biosynthetic capability of N-acetylornithine
            aminotransferase in arginine and lysine biosynthesis
  JOURNAL   Biochemistry 38 (10), 3019-3024 (1999)
   PUBMED   10074354
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  :: BlastRule
            Evidence Accession :: NBR008112
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     gene            1..405
                     /gene="argD"
                     /gene_synonym="dapC"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
     Protein         1..405
                     /product="bifunctional
                     acetylornithine/succinyldiaminopimelate transaminase"
                     /EC_number="2.6.1.11"
                     /EC_number="2.6.1.17"
                     /calculated_mol_wt=43539
     Region          3..405
                     /region_name="argD"
                     /note="acetylornithine/succinyldiaminopimelate
                     transaminase; PRK05093"
                     /db_xref="CDD:179933"
     Site            order(107..109,141..142,144,193,226,228..229,255)
                     /site_type="active"
                     /note="inhibitor-cofactor binding pocket [active]"
                     /db_xref="CDD:99735"
     Site            order(108..109,141..142,193,226,229,255)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99735"
     Site            255
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99735"
ORIGIN      
        1 mateqtaitr atfdevilpv yapadfipvk gkgsrvwdqq gkeyidfagg iavtalghch
       61 palvealksq getlwhtsnv ftnepalrlg rklidatfae rvlfmnsgte anetafklar
      121 hyacvrhspf ktkiiafhna fhgrslftvs vggqpkysdg fgpkpadiih vpfndlhavk
      181 avmddhtcav vvepiqgegg vqaatpeflk glrdlcdehq allvfdevqc gmgrtgdlfa
      241 ymhygvtpdi ltsakalggg fpvsamlttq eiasafhvgs hgstyggnpl acavagaafd
      301 iintpevlqg ihtkrqqfvq hlqaideqfd ifsdirgmgl ligaelkpky kgrardflya
      361 gaeagvmvln agadvmrfap slvveeadih egmqrfaqav gkvva