MULTISPECIES: aminotransferase class I/II-fold pyridoxal

LOCUS       WP_000847144             361 aa            linear   BCT 02-MAR-2025
            phosphate-dependent enzyme [Enterobacteriaceae].
ACCESSION   WP_000847144
VERSION     WP_000847144.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Ko,T.P., Wu,S.P., Yang,W.Z., Tsai,H. and Yuan,H.S.
  TITLE     Crystallization and preliminary crystallographic analysis of the
            Escherichia coli tyrosine aminotransferase
  JOURNAL   Acta Crystallogr D Biol Crystallogr 55 (Pt 8), 1474-1477 (1999)
   PUBMED   10417420
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Nakai,T., Okada,K., Akutsu,S., Miyahara,I., Kawaguchi,S., Kato,R.,
            Kuramitsu,S. and Hirotsu,K.
  TITLE     Structure of Thermus thermophilus HB8 aspartate aminotransferase
            and its complex with maleate
  JOURNAL   Biochemistry 38 (8), 2413-2424 (1999)
   PUBMED   10029535
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 :: NF012382.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF00155.27
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     Protein         1..361
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009058 - biosynthetic process [Evidence
                     IEA]"
                     /calculated_mol_wt=38468
     Region          75..>239
                     /region_name="AAT_I"
                     /note="Aspartate aminotransferase (AAT) superfamily (fold
                     type I) of pyridoxal phosphate (PLP)-dependent enzymes.
                     PLP combines with an alpha-amino acid to form a compound
                     called a Schiff base or aldimine intermediate, which
                     depending on the reaction, is the...; cl18945"
                     /db_xref="CDD:450240"
     Site            order(75..76,79,141,170,173,193,196)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:99738"
     Site            196
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99738"
ORIGIN      
        1 mktfplqslt iieaqqkqfa lvdsicrhfp gsefltggdl gltpglnqpr vtqrveqvla
       61 dafhaqaaal vqgagtgair aglaallkpg qrllvhdapv ypttrviieq mgltlitvdf
      121 ndlsalkqvv deqqpdaalv qhtrqqpqds yvladvlatl raagvpaltd dnyavmkvar
      181 igcecganvs tfscfklfgp egvgavvgda dvinriratl ysggsqiqga qalevlrglv
      241 fapvmhavqa gvserllall nggavpevks avianaqskv livefhqpia arvleeaqkr
      301 galpypvgae skyeipplfy rlsgtfrqan pqsehcairi npnrsgeetv lrilresias
      361 i