aminotransferase class I/II-fold pyridoxal phosphate-dependent

LOCUS       WP_010895553             515 aa            linear   BCT 23-JUL-2024
            enzyme [Pseudomonas aeruginosa].
ACCESSION   WP_010895553
VERSION     WP_010895553.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Koper,K., Han,S.W., Pastor,D.C., Yoshikuni,Y. and Maeda,H.A.
  TITLE     Evolutionary origin and functional diversification of
            aminotransferases
  JOURNAL   J Biol Chem 298 (8), 102122 (2022)
   PUBMED   35697072
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Phillips,R.S.
  TITLE     Chemistry and diversity of pyridoxal-5'-phosphate dependent enzymes
  JOURNAL   Biochim Biophys Acta 1854 (9), 1167-1174 (2015)
   PUBMED   25615531
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11449461
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..515
                     /product="aminotransferase class I/II-fold pyridoxal
                     phosphate-dependent enzyme"
                     /GO_function="GO:0016831 - carboxy-lyase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=56120
     Region          25..131
                     /region_name="REC"
                     /note="phosphoacceptor receiver (REC) domain of response
                     regulators (RRs) and pseudo response regulators (PRRs);
                     cl19078"
                     /db_xref="CDD:473134"
     Region          <214..497
                     /region_name="PRK15029"
                     /note="arginine decarboxylase; Provisional"
                     /db_xref="CDD:184989"
ORIGIN      
        1 msrnnpsrhs ilvtsninaa ndanrlselc rqleirgyrl fqapsrkval dflgnaahpa
       61 gilllvaept geneaaqlaa ldelrqvaps iplfllfrql rieqlssqll deaqgcfnla
      121 agparfiaer idsdlrewra pagprrlrdy appvprtpvs aryngrarld lapakqwrig
      181 sgstaerlat plndlstayr ktsagapaah agdiaeafrr alweaaarla redgdtwffe
      241 ilrgnpgpgi eagretpakr whglaetlds sprldplrva lsapgldsrg rpasfgvpaa
      301 vvcrylrrhg iaplrtgdyr flllfpqgar aehaqplvdr lcefkrrhdd daplkqvlpe
      361 lldssplyry iglrelcami heaslrlhlt aladaaaraa ghaalapatv yghlvrdete
      421 avaidrlggr vvaslvgvhp aatplllpge rvaeespali dyllalqafg ehfpgfapel
      481 qgieidergr yrvrcvrpaa largsglrla trrpd