MULTISPECIES: type III PLP-dependent enzyme [Pseudomonas].

LOCUS       WP_003094617             387 aa            linear   BCT 01-JAN-2025
ACCESSION   WP_003094617
VERSION     WP_003094617.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Eliot,A.C. and Kirsch,J.F.
  TITLE     Pyridoxal phosphate enzymes: mechanistic, structural, and
            evolutionary considerations
  JOURNAL   Annu Rev Biochem 73, 383-415 (2004)
   PUBMED   15189147
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Hayashi,H.
  TITLE     Pyridoxal enzymes: mechanistic diversity and uniformity
  JOURNAL   J Biochem 118 (3), 463-473 (1995)
   PUBMED   8690703
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 10089786
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..387
                     /product="type III PLP-dependent enzyme"
                     /EC_number="4.1.1.-"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /calculated_mol_wt=43429
     Region          25..387
                     /region_name="PLPDE_III_ODC"
                     /note="Type III Pyridoxal 5-phosphate (PLP)-Dependent
                     Enzyme Ornithine Decarboxylase; cd00622"
                     /db_xref="CDD:143482"
     Site            order(26,57,78..79,81..82,104,109,122,125,129,157..159,
                     281,283..284,294,296,298,301..302,310,312,332,334,336,339,
                     371,373,376..378,380)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143482"
     Site            order(55,57,76,142,186,189,226..227,264..267,311,335,367)
                     /site_type="active"
                     /db_xref="CDD:143482"
     Site            order(55,57,76,142,186,189,226..227,264..267,335,367)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate (PLP) binding site [chemical
                     binding]"
                     /db_xref="CDD:143482"
     Site            order(57,335)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143482"
     Site            order(310..311,335..336,367,376)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:143482"
ORIGIN      
        1 msikvedyfa petfqrmkaf adkqetpfvv idkqtiaday dqltdcfpfa riyyavkanp
       61 ateitellrd kgsnfdiasi yeldkvmktg vgperisygn tikkskdiry fyekgvrlfa
      121 tdseadlrni akaapgakvy vriltegstt adwplsrkfg cqtdmamdll ilarqlglep
      181 ygisfhvgsq qrdisvwdaa iakvkvifer lkeedgivlk minmgggfpa nyitktndle
      241 tyaeeiirfl kedfgddlpe iilepgrsli anagilvsev vlvarksrta verwvyadvg
      301 kfsglietmd esikfpiwte kqgemeevvi agptcdsadi myehykyglp lnlasgdrly
      361 wlstgaytts ysavefngfp plkafyl