dihydroorotate dehydrogenase electron transfer subunit [Listeria

LOCUS       WP_010989827             254 aa            linear   BCT 04-OCT-2019
            monocytogenes].
ACCESSION   WP_010989827
VERSION     WP_010989827.1
KEYWORDS    RefSeq.
SOURCE      Listeria monocytogenes
  ORGANISM  Listeria monocytogenes
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae;
            Listeria.
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 :: NF000799.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK00054
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Listeria monocytogenes"
                     /db_xref="taxon:1639"
     Protein         1..254
                     /product="dihydroorotate dehydrogenase electron transfer
                     subunit"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=27489
     Region          8..248
                     /region_name="DHOD_e_trans"
                     /note="FAD/NAD binding domain in the electron transfer
                     subunit of dihydroorotate dehydrogenase. Dihydroorotate
                     dehydrogenases (DHODs) catalyze the only redox reaction in
                     pyrimidine de novo biosynthesis. They catalyze the
                     oxidation of (S)-dihydroorotate to...; cd06218"
                     /db_xref="CDD:99814"
     Site            order(48,50..53,67..69,75..77,115,214..215)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99814"
     Site            order(50,52..53)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99814"
     Site            order(74,77,80,84,92,94)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99814"
     Site            order(110,114..117,119)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99814"
     Site            order(115..116,139..141,191..192)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99814"
     Site            order(218,223,226,241)
                     /site_type="other"
                     /note="Iron coordination center [ion binding]"
                     /db_xref="CDD:99814"
ORIGIN      
        1 mlqtemkviq qteiadkvye liltgecvag mspgqflmlk psrsdllmrr pisicsydkt
       61 aktcillyrv egdgtrdfsk lsegdtidvl gplgkgfdid ttpapktall igggigvppm
      121 yqlgkelaek gvqvmfvngf qsakdsfyaq emaeygtvhi atvdgslgtq gfvtditknf
      181 peepdviysc gpkamlqavk asfpetktyl sleermacgi gacyacvcpk addtnkqfkv
      241 cedgpvfrad evkl