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1:  YP_001258348Reports  dihydroorotate de...[gi:148560177] BLink, Conserved Domains, Links
LOCUS       YP_001258348             364 aa            linear   BCT 30-JUL-2008
DEFINITION  dihydroorotate dehydrogenase 2 [Brucella ovis ATCC 25840].
ACCESSION   YP_001258348
VERSION     YP_001258348.1  GI:148560177
DBSOURCE    REFSEQ: accession NC_009505.1
KEYWORDS    .
SOURCE      Brucella ovis ATCC 25840
  ORGANISM  Brucella ovis ATCC 25840
            Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
            Brucellaceae; Brucella.
REFERENCE   1  (residues 1 to 364)
  CONSRTM   NCBI Genome Project
  TITLE     Direct Submission
  JOURNAL   Submitted (04-JUN-2007) National Center for Biotechnology
            Information, NIH, Bethesda, MD 20894, USA
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Paulsen,I.
  TITLE     Direct Submission
  JOURNAL   Submitted (22-MAY-2007) The Institute for Genomic Research, 9712
            Medical Center Dr, Rockville, MD 20850, USA
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from ABQ61413.
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Brucella ovis ATCC 25840"
                     /strain="ATCC 25840"
                     /db_xref="ATCC:25840"
                     /db_xref="taxon:444178"
                     /chromosome="I"
     Protein         1..364
                     /product="dihydroorotate dehydrogenase 2"
                     /EC_number="1.3.3.1"
                     /calculated_mol_wt=39141
     CDS             1..364
                     /gene="pyrD"
                     /locus_tag="BOV_0325"
                     /coded_by="complement(NC_009505.1:343837..344931)"
                     /note="catalyzes the conversion of dihydroorotate to
                     orotate in the pyrimidine biosynthesis pathway; uses a
                     flavin nucleotide as an essential cofactor; class 2
                     enzymes are monomeric and compared to the class 1 class 2
                     possess an extended N terminus, which plays a role in the
                     membrane association of the enzyme and provides the
                     binding site for the respiratory quinones that serve as
                     physiological electron acceptors"
                     /transl_table=11
                     /db_xref="GeneID:5201581"
ORIGIN      
        1 msglfetlgr ralftfdaeq ahglsitglk tgivtcrtpe dpalsvkvag lkfpnplgma
       61 agydknaevp dallklgfgf aevgtltprp qsgnprprif rlvddkavin rlgfnneghe
      121 aafkrlsrra gksgivgvni gankdaedri adyvagirrf yqlaryftvn isspntpglr
      181 nlqarealhe llsrvleard eegnmctlkr pvflkiapdl tdeelddiaa eadaqkldgi
      241 ivsnttlsrs glknpensne tgglsgaplf erstvvlarm rervgpdmpl igvggidsae
      301 talakikaga dlvqlytgli yrgpglpgei lrglstaikh egvssiaelr drdtkewaar
      361 klis
//

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Last update: Wed, 05 Nov 2008 Rev. 145015