MULTISPECIES: arginine decarboxylase [Pseudomonas].

LOCUS       WP_003095365             636 aa            linear   BCT 04-JUN-2024
ACCESSION   WP_003095365
VERSION     WP_003095365.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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 :: TIGR01273.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..636
                     /gene="speA"
     Protein         1..636
                     /product="arginine decarboxylase"
                     /EC_number="4.1.1.19"
                     /GO_function="GO:0008792 - arginine decarboxylase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006527 - arginine catabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0008295 - spermidine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=70537
     Region          6..636
                     /region_name="PRK05354"
                     /note="biosynthetic arginine decarboxylase"
                     /db_xref="CDD:235427"
     Site            order(69,110,134..135,137..138,160,180,184,188,224..227,
                     360..363,464,466,468,471,505,507..509,511,551..553,
                     556..558)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143503"
     Site            order(108,110,132,155,205,255,258,294..295,343..346,
                     508..509,548,552,556)
                     /site_type="active"
                     /db_xref="CDD:143503"
     Site            order(108,110,132,155,205,255,258,294..295,343..346,508,
                     548)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate (PLP) binding site [chemical
                     binding]"
                     /db_xref="CDD:143503"
     Site            order(110,508)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143503"
     Site            order(258,346,508..509,548,552,556)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:143503"
ORIGIN      
        1 maarrtrkdd gsnwtvadsr gvygirhwga gyfaindggn vevrpqgads tpidlyelvg
       61 qlreaglslp llvrfpdilq drvrkltgaf danierleyq srytalypik vnqqeavven
      121 iiatenvsig leagskpelm avlalapkgg tivcngykdr efiklalmgq klghnvfivi
      181 ekesevqlvi eeaanvgvqp qvglrvrlss lasskwadtg gekakfglsa aqllsvverf
      241 rqagldqgvr llhfhmgsqi anladyqhgf keairyygel ralglpvdhi dvggglgvdy
      301 dgthsrnass inydiddyag vvvgmlkefc daqglphphi fsesgralta hhavlitqvt
      361 dverhnddvp kivdldeqpe ivrwlaellg ptdaemvtet ywrathyigd aaaqyadgki
      421 slaqkalaeq cyfaicrrlh nqlkarqrsh rqvldelndk ladkyicnfs vfqslpdtwa
      481 igqvlpilpl hrlgeepdrr avlqdltcds dgkitqyvde qsietslpvh evkegedyli
      541 gvflvgayqe ilgdmhnlfg dtdsvnvyqr adggiyhagi ethdtiedml ryvhlspeel
      601 mtlyrdkvag akltarernq yldalrlglt rsayls