biosynthetic arginine decarboxylase [Shigella flexneri].

LOCUS       WP_011069502             668 aa            linear   BCT 29-MAR-2020
ACCESSION   WP_011069502
VERSION     WP_011069502.1
KEYWORDS    RefSeq.
SOURCE      Shigella flexneri
  ORGANISM  Shigella flexneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Patel,C.N., Adcock,R.S., Sell,K.G. and Oliveira,M.A.
  TITLE     Crystallization, X-ray diffraction and oligomeric characterization
            of arginine decarboxylase from Yersinia pestis, a key polyamine
            biosynthetic enzyme
  JOURNAL   Acta Crystallogr. D Biol. Crystallogr. 60 (Pt 12 Pt 2), 2396-2398
            (2004)
   PUBMED   15583399
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Nakada,Y. and Itoh,Y.
  TITLE     Identification of the putrescine biosynthetic genes in Pseudomonas
            aeruginosa and characterization of agmatine deiminase and
            N-carbamoylputrescine amidohydrolase of the arginine decarboxylase
            pathway
  JOURNAL   Microbiology (Reading, Engl.) 149 (Pt 3), 707-714 (2003)
   PUBMED   12634339
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 :: NF003763.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK05354
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Shigella flexneri"
                     /db_xref="taxon:623"
     gene            1..668
                     /gene="speA"
     Protein         1..668
                     /product="biosynthetic 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]"
                     /calculated_mol_wt=74871
     Region          26..662
                     /region_name="PRK05354"
                     /note="biosynthetic arginine decarboxylase"
                     /db_xref="CDD:235427"
     Site            order(90,131,154..155,157..158,181,201,205,209,245..248,
                     381..383,483,488,490,492,495,529,531..533,535,575..577,
                     580..582)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143503"
     Site            order(129,131,152,176,226,276,279,315..316,364..367,
                     532..533,572,576,580)
                     /site_type="active"
                     /db_xref="CDD:143503"
     Site            order(129,131,152,176,226,276,279,315..316,364..367,532,
                     572)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate (PLP) binding site [chemical
                     binding]"
                     /db_xref="CDD:143503"
     Site            order(131,532)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143503"
     Site            order(279,367,532..533,572,576,580)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:143503"
ORIGIN      
        1 mrfamsddms mglpssageh gvlrsmqeva mssqeaskml rtyniawwgn nyydvnelgh
       61 isvcpdpdvp earvdlaqlv ktreaqgqrl palfcfpqil qhrlrsinaa fkraresygy
      121 ngdyflvypi kvnqhrrvie slihsgeplg leagskaelm avlahagmtr svivcngykd
      181 reyirlalig ekmghkvylv iekmseiaiv ldeaerlnvv prlgvrarla sqgsgkwqss
      241 ggekskfgla atqvlqlvet lreagrldsl qllhfhlgsq manirdiatg vresarfyve
      301 lhklgvniqc fdvggglgvd yegtrsqsdc svnyglneya nniiwaigda ceenglphpt
      361 vitesgravt ahhtvlvsni igverneytv ptapvedapr alqsmwetwq emhepgtrrs
      421 lrewlhdsqm dlhdihigys sgtfslqera waeqlylsmc hevqkqldpq nrahrpiide
      481 lqermadkmy vnfslfqsmp dawgidqlfp vlplegldqv perravlldi tcdsdgaidh
      541 yidgdgiatt mpmpeydpen ppmlgffmvg ayqeilgnmh nlfgdteavd vfvfpdgsve
      601 velsdegdtv admlqyvqld pktlltqfrd qvkktdldae lqqqfleefe aglygytyle
      661 ddaanlli