4-aminobutyrate--2-oxoglutarate transaminase [Shigella flexneri].

LOCUS       WP_000935288             375 aa            linear   BCT 06-NOV-2024
ACCESSION   WP_000935288
VERSION     WP_000935288.1
KEYWORDS    RefSeq.
SOURCE      Shigella flexneri
  ORGANISM  Shigella flexneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
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 :: NF005985.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK08088
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Shigella flexneri"
                     /db_xref="taxon:623"
     gene            1..375
                     /gene="gabT"
     Protein         1..375
                     /product="4-aminobutyrate--2-oxoglutarate transaminase"
                     /EC_number="2.6.1.19"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0009448 - gamma-aminobutyric acid
                     metabolic process [Evidence IEA]"
                     /calculated_mol_wt=39923
     Region          1..374
                     /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(59..61,87..88,90,155,188,190..191,217)
                     /site_type="active"
                     /note="inhibitor-cofactor binding pocket [active]"
                     /db_xref="CDD:99735"
     Site            order(60..61,87..88,155,188,191,217)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99735"
     Site            217
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99735"
ORIGIN      
        1 mlntghlhpk vvaaveaqlk klshtcfqvl ayepylelce imnqkvpgdf akktllvttg
       61 seavenavki araatkrsgt iafsgeyhgr thytlaltgk vnpysagmgl mpghvyraly
      121 pcplhgised daiasihrif kndaapedia aimiepvqge ggfyaaspaf mqrlralcde
      181 hgimliadev qsgagrtgtl fameqmgvap dlttfaksia ggfplagvtg raevmdavap
      241 gglggtyagn piacvaalev lkvfeqenll qkandlgqkl kdgllaiaek hpeigdvrgl
      301 gsmiaielfe dgdhskpdak ltaeivarar dkglillscg pyynvlrilv pltiedaqir
      361 qgleiigqcf deakq