MULTISPECIES: catabolic alanine racemase DadX [Salmonella].

LOCUS       WP_000197903             356 aa            linear   BCT 11-DEC-2019
ACCESSION   WP_000197903
VERSION     WP_000197903.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Walsh,C.T.
  TITLE     Enzymes in the D-alanine branch of bacterial cell wall
            peptidoglycan assembly
  JOURNAL   J. Biol. Chem. 264 (5), 2393-2396 (1989)
   PUBMED   2644260
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 :: NF002970.2
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK03646
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     gene            1..356
                     /gene="dadX"
     Protein         1..356
                     /product="catabolic alanine racemase DadX"
                     /EC_number="5.1.1.1"
                     /GO_function="GO:0008784 - alanine racemase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006522 - alanine metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=38673
     Region          2..355
                     /region_name="dadX"
                     /note="catabolic alanine racemase; PRK03646"
                     /db_xref="CDD:179622"
     Site            order(33,35,39,79,123,130,157,159,191..193,207..210,341)
                     /site_type="active"
                     /db_xref="CDD:143500"
     Site            order(33,35,39,79,159,191..192,207,209..210,341)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate (PLP) binding site [chemical
                     binding]"
                     /db_xref="CDD:143500"
     Site            order(35,39,130,159,341)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:143500"
     Site            order(35,253)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143500"
     Site            order(240,243,249..250,252..254,267,272,278,300,302,339,
                     341..342,347,350)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143500"
ORIGIN      
        1 mtrpiqasld lqvmkqnlai vrraapearv wsvvkanayg hgiervwsal gatdgfamln
       61 leeaitlrer gwkgpilmle gffhaqdlea ydtyrlttci hsnwqlkalq narlnapldi
      121 yvkvnsgmnr lgfqperaqt vwqqlramrn vgemtlmshf aqadhpegig eamrrialat
      181 eglqcaysls nsaatlwhpq ahydwvrpgi ilygaspsgq wrdiadtglk pvmtlsseii
      241 gvqtlsager vgygggysvt qeqrigivaa gyadgyprha ptgtpvlvdg irtrtvgtvs
      301 mdmlavdltp cpqagigtpv elwgkeikvd dvasaagtlg yellcavapr vpfvtt