O-succinylhomoserine (thiol)-lyase [Grimontia hollisae].

LOCUS       WP_005501411             388 aa            linear   BCT 13-OCT-2019
ACCESSION   WP_005501411
VERSION     WP_005501411.1
KEYWORDS    RefSeq.
SOURCE      Grimontia hollisae
  ORGANISM  Grimontia hollisae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Grimontia.
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 :: NF006463.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK08861
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Grimontia hollisae"
                     /db_xref="taxon:673"
     Protein         1..388
                     /product="O-succinylhomoserine (thiol)-lyase"
                     /calculated_mol_wt=41716
     Region          1..385
                     /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..33,35..36,47,49,75..76,78..79,101,106,109,197,
                     205,207,224,234,236..237,316)
                     /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 msdkksatia vrtgittdsq hhavvppiyl stnyefpefg tvptydyarg gnptrsllet
       61 alaelengag avvtncgmsa inlllsllsp ddliiaphdc yggtyrllds rarmgafkve
      121 fvdqtnpevl aaalaqqpkl vwletpsnpl lrvvdiaaic ekahdvgawv gvdntflspv
      181 lqqplnlgad fvvhsttkfi nghsdtvggv vvakdaglyd dlkwwgncig atgnafdsym
      241 tlrglrtlga rmrqheenst avldylkqep lvntiyhpal pthpgheiak kqqsgfggml
      301 sfelkggese lklflsslkl ftlaeslggv eslvthpgsm thramsddaq aeaglaatll
      361 rlsvgledka dlvadlkqaf dkvrenqq