bifunctional acetylornithine/succinyldiaminopimelate transaminase

LOCUS       WP_000963819             406 aa            linear   BCT 21-JAN-2025
            [Escherichia coli].
ACCESSION   WP_000963819
VERSION     WP_000963819.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 406)
  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..406
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..406
                     /gene="argD"
                     /gene_synonym="dapC"
     Protein         1..406
                     /product="bifunctional
                     acetylornithine/succinyldiaminopimelate transaminase"
                     /EC_number="2.6.1.11"
                     /EC_number="2.6.1.17"
                     /calculated_mol_wt=43624
     Region          4..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 maieqtaitr atfdevilpi yapaefipvk gqgsriwdqq gkeyvdfagg iavtalghch
       61 palvnalktq getlwhisnv ftnepalrlg rklieatfae rvvfmnsgte anetafklar
      121 hyacvrhspf ktkiiafhna fhgrslftvs vggqpkysdg fgpkpsdiih vpfndlhavk
      181 avmddhtcav vvepiqgegg vtaatpeflq glrelcdqhq allvfdevqc gmgrtgdlfa
      241 ymhygvtpdi ltsakalggg fpisamltta eiasafhpgs hgstyggnpl acavagaafd
      301 iintpevleg iqakrqrfvd hlqkidqqyd vfsdirgmgl ligaelkpqy kgqardflya
      361 gaeagvmvln agpdvmrfap slvvedadid egmqrfahav akvvga