MULTISPECIES: catabolic alanine racemase DadX [Klebsiella].

LOCUS       WP_002910887             356 aa            linear   BCT 20-NOV-2023
ACCESSION   WP_002910887
VERSION     WP_002910887.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
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="Klebsiella"
                     /db_xref="taxon:570"
     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=38601
     Region          2..356
                     /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 mtrpvvasid llalrqnlqi vrraapgsrl wavvkanayg hgvarvwsal saadgfalln
       61 leeaillreq gwkgpillle gffhadelav ldqyrlttsv hsnwqikalq qaklrapldi
      121 ylkvnsgmnr lgfmpervht vwqqlraisn vgemtlmshf aeaenpqgiv epmrrieqaa
      181 egldcprsla nsaatlwhpe ahfdwvrpgi vlygaspsgq wqdiantglk pvmtlrseii
      241 gvqnlrpgea igygglyrtt qeqrigivac gyadgyprva psgtpvlvdg vrtttvgrvs
      301 mdmlavdltp cpqagigapv elwgkeikid dvaassgtvg yelmcalapr vpvvtl