LOCUS       WP_122970296             257 aa            linear   BCT 08-NOV-2018
DEFINITION  dihydroorotate dehydrogenase electron transfer subunit
            [Lysinibacillus halotolerans].
ACCESSION   WP_122970296
VERSION     WP_122970296.1
KEYWORDS    RefSeq.
SOURCE      Lysinibacillus halotolerans
  ORGANISM  Lysinibacillus halotolerans
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
            Lysinibacillus.
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..257
                     /organism="Lysinibacillus halotolerans"
                     /db_xref="taxon:1368476"
     Protein         1..257
                     /product="dihydroorotate dehydrogenase electron transfer
                     subunit"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=28189
     Region          9..251
                     /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(50,52..55,69..71,77..79,117,216..217)
                     /site_type="other"
                     /note="FAD binding pocket [chemical binding]"
                     /db_xref="CDD:99814"
     Site            order(52,54..55)
                     /site_type="other"
                     /note="FAD binding motif [chemical binding]"
                     /db_xref="CDD:99814"
     Site            order(76,79,82,86,94,96)
                     /site_type="other"
                     /note="phosphate binding motif [ion binding]"
                     /db_xref="CDD:99814"
     Site            order(112,116..119,121)
                     /site_type="other"
                     /note="beta-alpha-beta structure motif"
                     /db_xref="CDD:99814"
     Site            order(117..118,141..143,193..194)
                     /site_type="other"
                     /note="NAD binding pocket [chemical binding]"
                     /db_xref="CDD:99814"
     Site            order(220,225,228,244)
                     /site_type="other"
                     /note="Iron coordination center [ion binding]"
                     /db_xref="CDD:99814"
ORIGIN      
        1 miqqermivv rqseiahhif eltiqgqivq dmnpgqfvhi rvsetfepll rrpisianid
       61 ketgevtliy raegrgtnll sqrqvgdevd vlgplgngfs vetapeggta llvgggigvp
      121 plyelskqln argirtihvf gfateevtfy eeqfstlgdt hfvtvdgtkg tkgfvtdlle
      181 elkpefdvfy acgpmpmlra leqfypdkqg ylsfeermgc gigacfacvc kttdsadkdy
      241 vkvcsdgpvf pkgvvql
//