MULTISPECIES: biosynthetic arginine decarboxylase [Salmonella].

LOCUS       WP_001278580             658 aa            linear   BCT 29-MAR-2020
ACCESSION   WP_001278580
VERSION     WP_001278580.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 658)
  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 658)
  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..658
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     gene            1..658
                     /gene="speA"
     Protein         1..658
                     /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=73702
     Region          22..658
                     /region_name="PRK05354"
                     /note="biosynthetic arginine decarboxylase"
                     /db_xref="CDD:235427"
     Site            order(86,127,150..151,153..154,177,197,201,205,241..244,
                     377..379,479,484,486,488,491,525,527..529,531,571..573,
                     576..578)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143503"
     Site            order(125,127,148,172,222,272,275,311..312,360..363,
                     528..529,568,572,576)
                     /site_type="active"
                     /db_xref="CDD:143503"
     Site            order(125,127,148,172,222,272,275,311..312,360..363,528,
                     568)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate (PLP) binding site [chemical
                     binding]"
                     /db_xref="CDD:143503"
     Site            order(127,528)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143503"
     Site            order(275,363,528..529,568,572,576)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:143503"
ORIGIN      
        1 msddmsmgsp ssageqgvlr smqevamssq easkmlrtyn iawwgnnyyd vnelghisvc
       61 pdpdvpearv dlaklvkare aqgqrlpalf cfpqilqhrl rsinaafkra resygyngdy
      121 flvypikvnq hrrvieslih sgeplgleag skaelmavla hagmtrsviv cngykdreyi
      181 rlaligekmg hkvylviekm seiaivleea erlnvvprlg vrarlasqgs gkwqssggek
      241 skfglaatqv lqlvetlrda grldslqllh fhlgsqmani rdiatgvres arfyvelhkl
      301 gvniqcfdvg gglgvdyegt rsqsdcsvny glneyannii waigdaceeh glphptvite
      361 sgravtahht vlvsniigve rneytdptap aedapralqn lwetwqemhk pgtrrslrew
      421 lhdsqmdlhd ihigyssgaf slqerawaeq lylsmchevq kqldpqnrah rpiidelqer
      481 madkmyvnfs lfqsmpdawg idqlfpvlpl egldqvperr avllditcds dgaidhyidg
      541 dgiattmpmp eydpenppml gffmvgayqe ilgnmhnlfg dteavdvfvf pdgsvevels
      601 degdtvadml qyvqldpktl lthfrdqvkq tdlddalqqq fleefeagly gytylede