aminotransferase class I/II-fold pyridoxal phosphate-dependent

LOCUS       WP_003733294             374 aa            linear   BCT 02-MAR-2025
            enzyme [Listeria monocytogenes].
ACCESSION   WP_003733294
VERSION     WP_003733294.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
REFERENCE   1  (residues 1 to 374)
  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 374)
  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..374
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..374
                     /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=41121
     Region          7..366
                     /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(30..33,47,49,75..76,78..79,101,106,109,197,205,207,
                     224,234,236..237,299)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99738"
     Site            order(76..78,101,144,173,195,197..198,207)
                     /site_type="active"
                     /note="substrate-cofactor binding pocket [active]"
                     /db_xref="CDD:99738"
     Site            order(76..78,101,173,176,195,197..198)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99738"
     Site            198
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99738"
ORIGIN      
        1 maklkqetia aqignrkcer tgavnmpvyf stayqhadlg vstgydytrt gnptrdalqe
       61 alaelength afatssgmsa iqlvfqlfkt gehiissqdl yggtfryfeq fgaqyqigfs
      121 ywdgaeiadl eklirpetka ifietptnpl mqetdiatva kwahahdllv ivdntfytpv
      181 lqqplslgad ivihsatkyl gghndvlaga vivkeeklgk fffdqlnatg tvlspfdswl
      241 lirglktlvl rvrqhqanaq kiaafleehk lveevrypgr ggmisffird aalvspllke
      301 lelftfaesl ggveslityp ttqthadipv elrnsygltd kllrisvgie asedliadls
      361 kaldavleev sarg