MULTISPECIES: bifunctional threonine ammonia-lyase/L-serine

LOCUS       WP_002910762             329 aa            linear   BCT 20-NOV-2023
            ammonia-lyase TdcB [Klebsiella].
ACCESSION   WP_002910762
VERSION     WP_002910762.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
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 :: NF006389.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK08638
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     gene            1..329
                     /gene="tdcB"
     Protein         1..329
                     /product="bifunctional threonine ammonia-lyase/L-serine
                     ammonia-lyase TdcB"
                     /GO_function="GO:0004794 - L-threonine ammonia-lyase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0006567 - threonine catabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=34950
     Region          1..327
                     /region_name="PRK08638"
                     /note="bifunctional threonine ammonia-lyase/L-serine
                     ammonia-lyase TdcB"
                     /db_xref="CDD:236317"
     Site            order(11..12,15,18..19,50..51,197..198,267,270..271,274,
                     278..280,313..316)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:107205"
     Site            order(58,85,184..188,311)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:107205"
     Site            58
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:107205"
ORIGIN      
        1 mhitydlpvs iddileakqr lagkiyktgm prsnyfserc qgeiflkfen mqrtgsfkir
       61 gafnklcglt aaekrkgvva csagnhaqgv slscamlgid gkvvmpkgap kskvaatcdy
      121 saevvlhgdn fndtlakasd ivelegrifi ppyddpqvia gqgtigleil edlydvdnvi
      181 vpigggglia giaiaiksin ptiriigvqs envhgmaasw yageitshrh agtladgcdv
      241 arpgkltyei arqlvddivl vseddirqsm valiqrnkvi tegagalaca allsgkldsy
      301 iqnrktvsli sggnidlsrv sqitgfvda