catabolic alanine racemase DadX [Escherichia coli].

LOCUS       WP_000197859             356 aa            linear   BCT 11-DEC-2019
ACCESSION   WP_000197859
VERSION     WP_000197859.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia coli"
                     /db_xref="taxon:562"
     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=38728
     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 mtrpiqasld lqalkqnlsi vrqaapharv wsvvkanayg hgieriwsal gatdgfalln
       61 leeaitlrer gwkgpilmle gffhaqdlem ydqhrlttcv hsnwqlkalq narlkapldi
      121 ylkvnsgmnr lgfqpdrvlt vwqqlraman vgemtlmshf aeaehpdgis gamarieqaa
      181 eglecrrsls nsaatlwhpe ahfdwvrpgi ilygaspsgq wrdiantglr pvmtlsseii
      241 gvqtlkager vgyggrytar deqrigivaa gyadgyprha ptgtpvlvdg vrtmtvgtvs
      301 mdmlavdltp cpqagigtpv elwgkeikid dvaaaagtvg yelmcalalr vpvvtv