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MULTISPECIES: bifunctional acetylornithine/succinyldiaminopimelate


LOCUS       WP_002920226             406 aa            linear   BCT 20-JAN-2025
            transaminase [Klebsiella].
ACCESSION   WP_002920226
VERSION     WP_002920226.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
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="Klebsiella"
                     /db_xref="taxon:570"
     gene            1..406
                     /gene="argD"
                     /gene_synonym="dapC"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
     Protein         1..406
                     /product="bifunctional
                     acetylornithine/succinyldiaminopimelate transaminase"
                     /EC_number="2.6.1.11"
                     /EC_number="2.6.1.17"
                     /calculated_mol_wt=43423
     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 mateqpaitr atfdevilpi yapaefipvk gkgsrvwdqq gkeyidfagg iavtalghch
       61 palvaalhqq getlwhtsnv ftnepalrlg rklveatfae rvvfmnsgte anetafklar
      121 hyavtrhspy ktkiiafhna fhgrslftvs vggqpkysdg fgpkpadivh vpfndlqavk
      181 avmddhtcav vvepiqgegg vtaatpaflq glrelcdqhq allvfdevqc gmgrtgslfa
      241 ymhygvtpdi ltsakalggg fpvsamltth eiasafhags hgstyggnpl acavanaafd
      301 lintpavldg vsakrelfvk hlqrldaefd lfsdirgmgl ligaelkpqh kgrardflya
      361 aadagvmvln agpdvmrfvp sliideqdia egmarfaqav akving