biosynthetic arginine decarboxylase [Klebsiella pneumoniae].

LOCUS       WP_004219805             632 aa            linear   BCT 29-MAR-2020
ACCESSION   WP_004219805
VERSION     WP_004219805.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group;
            Klebsiella; Klebsiella pneumoniae complex.
REFERENCE   1  (residues 1 to 632)
  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 632)
  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..632
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     gene            1..632
                     /gene="speA"
     Protein         1..632
                     /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=70974
     Region          1..632
                     /region_name="PRK05354"
                     /note="biosynthetic arginine decarboxylase"
                     /db_xref="CDD:235427"
     Site            order(60,101,124..125,127..128,151,171,175,179,215..218,
                     351..353,453,458,460,462,465,499,501..503,505,545..547,
                     550..552)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143503"
     Site            order(99,101,122,146,196,246,249,285..286,334..337,
                     502..503,542,546,550)
                     /site_type="active"
                     /db_xref="CDD:143503"
     Site            order(99,101,122,146,196,246,249,285..286,334..337,502,
                     542)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate (PLP) binding site [chemical
                     binding]"
                     /db_xref="CDD:143503"
     Site            order(101,502)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143503"
     Site            order(249,337,502..503,542,546,550)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:143503"
ORIGIN      
        1 mssqeaskml rtyniawwgn nyydvnelgh isvcpdpdvp earvdlaelv kareaqgqrl
       61 palfcfpqil qhrlrsinaa fkraresygy ngdyflvypi kvnqhrrvie slihsgeplg
      121 leagskaelm avlahagmtr svivcngykd reyirlalvg ekmghkvylv iekmseiaiv
      181 leeaerlnvv prlgvrarla sqgsgkwqss ggekskfgla atqvlqlvei lreaghlesl
      241 qllhfhlgsq manirdiatg vresvrfyve lhklgvniqc fdvggglgvd yegtrsqsdc
      301 svnyglneya nniiwaigda ceenglphpt vitesgravt ahhtvlvsni igverneyte
      361 atppaedaar plqsmwetwl emhetgnrrs lrewlhdsqm dlhdihigys sgtfnlqera
      421 waeqlylnmc hevqkqldps nrahrpiide lqermadkiy vnfslfqsmp dawgidqlfp
      481 vmpleglnks perravlldi tcdsdgaidh yvdgdgiatt mpmpeydpen ppmlgffmvg
      541 ayqeilgnmh nlfgdteavd vfvfpdgsve velsdegdtv admlqyvqld pntlltqfrd
      601 qvkntgldda lqqqfleefe aglygytyle de